Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Abz-PR-acetyl-K-QLATKAARKSAK-Dnp + H2O
?
-
-
-
?
Abz-PRKQLAT-acetyl-K-AARKSAK-Dnp + H2O
?
-
-
-
?
Abz-PRKQLATKAAR-dimethyl-K-SAK-Dnp + H2O
?
-
-
-
?
Abz-PRKQLATKAARKSAK-Dnp + H2O
?
-
-
-
?
alpha-casein + H2O
?
-
-
-
?
benzyloxycarbonyl-L-Arg-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Arg-L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
CV-(L-Phe-Arg)2 + H2O
?
-
-
-
?
dynamin + H2O
?
CatL is highly reactive toward recombinant dynamin at pH 5.0 and 6.0
-
-
?
histone H3 + H2O
?
-
-
-
?
L-Leu-L-Arg-7-amido-4-methylcoumarin + H2O
L-Leu-L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
N-benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
N-benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
procathepsin L + H2O
cathepsin L + ?
autoactivation
-
-
?
soluble type I collagen + H2O
?
kinetics of collagen binding to cathepsin L, overview. The enzyme cleaves after residue Gln24, the recognition sequence is Gly-Phe-Gln-/-Gly-Pro-Pro (corresponding to positions P3 to P3')
-
-
?
Z-Phe-Arg-7-amido-4-methylcoumarin + H2O
Z-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
Z-Val-Val-Arg-AMC + H2O
Z-Val-Val-Arg + 7-amino-4-methylcoumarin
a cathepsin L-specific substrate
-
-
?
(benzyloxycarbonyl-Phe-Arg)2-R110 + H2O
?
-
rhodamine-labeled substrate
-
-
?
2-aminobenzoic acid-Lys-Leu-Ala-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Ala + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Ala-Leu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Ala-Leu-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Arg-Leu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Arg-Leu-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Asn-Leu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Asn-Leu-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Gln-Leu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Gln-Leu-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Glu-Glu-epsilon-amino-caproic acid-Glu-Leu-Lys-Leu-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Glu-Glu-epsilon-amino-caproic acid-Glu-Leu-Lys + Leu-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Glu-Leu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Glu-Leu-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Glu-Leu-Lys-Leu-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Glu-Leu-Lys + Leu-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Gly-Leu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Gly-Leu-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-His-Leu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-His-Leu-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Ile-Leu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Ile-Leu-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Leu-Leu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Leu-Leu-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Arg-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Arg-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Asn-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Asn-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Asp-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Asp-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Gln-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Gln-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Glu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Glu-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Gly-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Gly-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-His-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-His-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Ile-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Ile-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Ala-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
?
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Arg-Arg-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Arg-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Arg-Asn-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Asn-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Arg-Gln-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Gln-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Arg-Glu-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Glu-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Arg-Gly-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Gly-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Arg-His-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + His-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Arg-Ile-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Ile-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Arg-Leu-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Leu-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Arg-Phe-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Phe-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Arg-Pro-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Pro-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Arg-Ser-Ala-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Ser-Ala-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Arg-Ser-Arg-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Ser-Arg-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Arg-Ser-Asn-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Ser-Asn-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Arg-Ser-Gln-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Ser-Gln-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Arg-Ser-Glu-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Ser-Glu-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Arg-Ser-Gly-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Ser-Gly-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Arg-Ser-His-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Ser-His-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Arg-Ser-Ile-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Ser-Ile-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Arg-Ser-Leu-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Ser-Leu-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Arg-Ser-Phe-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Ser-Phe-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Arg-Ser-Pro-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Ser-Pro-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Arg-Ser-Val-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Ser-Val-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Arg-Val-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Val-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Asn-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Asn + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Asp-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Asp + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Gln-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Gln + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Glu-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Glu + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Gly-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Gly + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-His-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-His + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Ile-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Ile + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Lys-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Lys + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Met-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Met + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Phe-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Phe + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Pro-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Pro + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Ser-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Ser + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Thr-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Thr + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Val-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Val + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Lys-epsilon-amino-caproic acid-Glu-Leu-Lys-Leu-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Lys-epsilon-amino-caproic acid-Glu-Leu-Lys + Leu-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Met-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Met-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Phe-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Phe-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Pro-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Pro-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Ser-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Ser-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Thr-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Thr-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Trp-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Trp-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Tyr-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Tyr-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Lys-Val-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Val-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Met-Ile-Ser-Leu-Met-Lys-Arg-Pro-Pro-Gly-Trp-Ser-Pro-Phe-Arg-Ser-Ser-Arg-Ile-Trp-NH2 + H2O
2-aminobenzoyl-Met-Ile-Ser-Leu-Met-Lys + Arg-Pro-Pro-Gly-Trp-Ser-Pro-Phe-Arg + 2-aminobenzoyl-Met-Ile-Ser-Leu-Met + Lys-Arg-Pro-Pro-Gly-Trp-Ser-Pro-Phe-Arg + Ser-Ser-Arg-Ile-Trp-NH2
-
-
-
-
?
2-aminobenzoyl-Phe-Leu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Phe-Leu-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-Val-Leu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Val-Leu-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
48 kDa intermediate of cathepsin D + H2O
34 kDa mature cathepsin D + ?
-
-
-
-
?
Abz-3-biphenyl-L-Ala-Arg-Ala-Ala-Tyr(3-NO2)-NH2 + H2O
Abz-3-biphenyl-L-Ala-Arg + L-Ala-Ala-3-nitrotyrosineamide
-
-
-
-
?
Abz-3-biphenyl-L-Ala-Arg-Ala-Gln-Tyr(3-NO2)-NH2 + H2O
Abz-3-biphenyl-L-Ala-Arg + L-Ala-Gln-3-nitrotyrosineamide
-
-
-
-
?
Abz-3-biphenyl-L-Ala-Arg-Ala-Ser-Tyr(3-NO2)-NH2 + H2O
Abz-3-biphenyl-L-Ala-Arg + L-Ala-Ser-3-nitrotyrosineamide
-
-
-
-
?
Arg-4-methylcoumarin 7-amide + H2O
Arg + 7-amino-4-methylcoumarin
-
no activity
-
-
?
benzyloxycarbonyl-Arg-Arg-4-methylcoumarin 7-amide + H2O
?
benzyloxycarbonyl-Gly-Pro-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Gly-Pro-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-L-citrulline-4-methylcoumarin 7-amide + H2O
benzyloxycarbonyl-L-citrulline 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-L-Phe-L-Arg-4-nitroanilide + H2O
benzyloxycarbonyl-L-Phe-L-Arg + 4-nitroaniline
-
-
-
-
?
benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Leu-Arg-4-methylcoumarin 7-amide + H2O
benzyloxycarbonyl-Leu-Arg + 7-amino-4-methyl-coumarin
-
-
-
-
?
benzyloxycarbonyl-Leu-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Leu-Arg + 7-amino-4-methylcoumarin
benzyloxycarbonyl-Phe-Ala-Arg-4-methylcoumarin 7-amide + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin 7-amide + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin 7-amide + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-nitroanilide + H2O
?
-
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
cathepsin D + H2O
?
-
-
-
-
?
Cbz-Phe-Arg-7-amido-4-methylcoumarin + H2O
Cbz-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
CCAAT-displacement protein/cut homeobox protein + H2O
p90 isoform of CCAAT-displacement protein/cut homeobox protein + p110 isoform of CCAAT-displacement protein/cut homeobox protein + ?
-
-
-
-
?
CCALNNGGGALVPRGSGTAK-(5-carboxyfluorescein)-NH2 + H2O
?
-
-
-
-
?
chromogranin A + H2O
catestatin fragments + ?
-
-
-
-
?
Collagen + H2O
?
-
substrate for cathepsin L mutant A205L
-
-
?
collagen XVIII + H2O
endostatin + ?
-
-
-
-
?
CUX1 transcription factor + H2O
?
-
-
-
-
?
D-Val-Leu-Lys-7-amido-4-methylcoumarin + H2O
D-Val-Leu-Lys + 7-amino-4-methylcoumarin
-
-
-
-
?
E-cadherin + H2O
?
-
-
-
-
?
endorepellin + H2O
anti-apoptotic C-terminal fragment of endorepellin + ?
Fibronectin + H2O
?
-
-
-
-
?
GABARAP-II protein + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
-
-
-
?
H2N-Abz-DLVGDVRLAGV-3-nitroYA-CONH2 + H2O
?
-
-
-
-
?
histone H1 + H2O
?
-
-
-
-
?
insulin receptor + H2O
?
-
-
-
-
?
insulin-like growth factor-1 receptor + H2O
?
-
-
-
-
?
interleukin-8 precursor + H2O
?
-
enzyme plays an important role in IL-8 processing in inflammatory sites
-
?
kininogen + H2O
kinin + ?
LC3-II protein + H2O
?
-
-
-
-
?
N-benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
N-benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
N-benzyloxycarbonyl-Phe-Arg-2-(4-methoxynaphthylamide) + H2O
N-benzyloxycarbonyl-Phe-Arg + 4-methoxy-2-naphthylamine
-
-
-
-
?
Nipah virus fusion protein + H2O
?
-
proteolytically processed within endosomes by cathepsin L
-
-
?
perforin + H2O
?
-
CatL preferentially cleaves a site on full-length recombinant perforin close to its C terminus
-
-
?
precursor form 77IL-8 of interleukin-8 + H2O
precursor form 72IL-8 of interleukin-8 + ?
-
cleavage between Arg5 and Ser6
-
?
pro-dipeptidyl peptidase I
?
proheparanase + H2O
active form of heparanase + ?
-
removal of the linker peptide and conversion of proheparanase into its active 850-kDa form is brought about predominantly by cathepsin L. Excision of a 10-amino acid peptide located at the C terminus of the linker segment between two functional cathepsin L cleavage sites at Y156Q and Y146Q is critical for activation of proheparanase. The entire linker segment of proheparanase is susceptible to multiple endocleavages by cathepsin L, generating small peptides. Processing and activation of proheparanase can be brought about solely by cathepsin L
-
-
?
secretory leukocyte protease inhibitor + H2O
?
-
incubation of recombinant secretory leukocyte protease inhibitor with cathepsin L leads to complete loss of activity while encapsulation of recombinant secretory leukocyte protease inhibitor in 1,2-dioleoyl-sn-glycero-3-[phospho-L-serine]-cholesterol liposomes retains 92.6% of its activity after challenge with cathepsin L
-
-
?
thyroglobulin type-1 domain + H2O
?
-
the thyroglobulin type-1 domain is a protein module that occurs in a variety of secreted and membrane proteins and is recognised as a potent inhibitor of cysteine proteases. Nevertheless, at high enzyme and inhibitor concentrations in the mircomolar range cathepsin L degrades thyroglobulin type-1 domain
-
-
?
topoisomerase-IIalpha + H2O
?
-
-
-
-
?
trypsinogen + H2O
trypsin + ?
-
cathepsin L inactivates human trypsinogen, CTSL-induced cleavage of trypsinogen occurs 3 amino acids toward the C-terminus from the cathepsin B activation site and results in a truncated, inactive form of trypsin and an elongated propeptide (trypsinogen activation peptide)
-
-
?
Type I collagen + H2O
?
-
-
-
-
?
Z-Phe-Arg-7-amido-4-methyl-coumarin + H2O
?
-
5 microM, pH 6.5, 28°C
-
-
?
Z-Phe-Arg-7-amido-4-methylcoumarin + H2O
Z-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Zaire Ebola virus glycoprotein + H2O
?
-
-
three cleavage fragments with masses of 23000, 19000, and 4000 Da. Cleavage removes a glycosylated glycan cap and mucin-like domain (MUC domain) and exposes the conserved core residues implicated in receptor binding
-
?
additional information
?
-
benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Arg-Arg-4-methylcoumarin 7-amide + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Arg-Arg-4-methylcoumarin 7-amide + H2O
?
-
no activity
-
-
?
benzyloxycarbonyl-Leu-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Leu-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Leu-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Leu-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
substrate for both cathepsin L and cathepsin B
-
-
?
Elastin + H2O
?
-
tritiated elastin
-
-
?
Elastin + H2O
?
-
the enzyme shows distinctive preferences in degrading elastins from bovine neck ligament, aorta, and lung
-
-
?
endorepellin + H2O
anti-apoptotic C-terminal fragment of endorepellin + ?
-
recombinant endorepellin is an in vitro substrate. Inhibition of cathepsin L activity in endothelial cells exposed to pro-apoptotic stimuli prevents release of anti-apoptotic C-terminal fragment of endorepellin without modulating the development of apoptosis. Inhibition of caspase-3 activation in endothelial cells concomitantly prevents cathepsin L release, production of anti-apoptotic C-terminal fragment of endorepellin, and the development of paracrine anti-apoptotic activity
-
-
?
endorepellin + H2O
anti-apoptotic C-terminal fragment of endorepellin + ?
-
recombinant endorepellin is an in vitro substrate
-
-
?
kininogen + H2O
kinin + ?
-
-
-
-
?
kininogen + H2O
kinin + ?
-
high and low molecular weight kininogen
-
?
pro-dipeptidyl peptidase I
?
-
cleavage at K133
-
?
pro-dipeptidyl peptidase I
?
-
cathepsin L could be an important activator of dipeptidyl peptidase I in vivo
-
?
additional information
?
-
catL is essential for epidermal homeostasis and regular hair follicle morphogenesis and cycling
-
-
?
additional information
?
-
human cathepsin L shows no proline specificity, but collagenolytic activity. Cathepsin L also is a strong gelatinase. Comparison with cathepsin K, overview
-
-
?
additional information
?
-
-
human cathepsin L shows no proline specificity, but collagenolytic activity. Cathepsin L also is a strong gelatinase. Comparison with cathepsin K, overview
-
-
?
additional information
?
-
the enzyme binds to concanavalin A, but not to Lens culinaris agglutinin, Ricinus communis agglutinin 120 (RCA120), and wheat germ agglutinin
-
-
?
additional information
?
-
-
the enzyme binds to concanavalin A, but not to Lens culinaris agglutinin, Ricinus communis agglutinin 120 (RCA120), and wheat germ agglutinin
-
-
?
additional information
?
-
the enzyme performs autocatalytic cleavage
-
-
?
additional information
?
-
-
no activity with benzyloxycarbonyl-Phe-Ala-4-methylcoumarin 7-amide and with benzyloxycarbonyl-Phe-Met-4-methylcoumarin 7-amide
-
-
?
additional information
?
-
-
the enzyme is involved in tissue destruction in arthritis
-
-
?
additional information
?
-
-
the enzyme plays a crucial role in the degradation of the invariant chain during maturation of major histocompatibility complex class II molecules and antigen processing
-
-
?
additional information
?
-
-
differentiation of human macrophages within the lung is accompanied by synthesis and expression of cathepsin L
-
-
?
additional information
?
-
-
CAT L plays a significant role in numerous important physiological and pathological processes, such as bone resorption, cancer progression and atherosclerosis
-
-
?
additional information
?
-
-
cathepsin L has a pro-survival function within the cell which may be due, at least in part, to its ability to deplete the cells from the proapoptotic molecule caspase-3. The existence of a proteolytic hierarchy between pro-survival and pro-death proteases suggests that changes in cellular proteolytic profiles are likely to have significant consequences not only on its survival but also on the type of death it may undergo in response to a specific stress
-
-
?
additional information
?
-
-
contributions of cathepsin L and cathepsin B to autophagic protein degradation of cytoplasmic proteins in HeLa and Huh-7 cells are nearly equal. Cathepsin L does not play a general role in the degradation of proteins in the lumen of autophagosomes, but rather is involved specifically in the degradation of autophagosomal membrane markers
-
-
?
additional information
?
-
-
pituitary gland may utilize the cathepsin L and prohormone convertase pathways for producing propiomelanocortin-derived peptide hormones
-
-
?
additional information
?
-
-
the enzyme does not hydrolyze ortho-aminobenzoic acid-VLFEKKVYLQ-N-[2,4-dinitrophenyl]ethylenediamine, ortho-aminobenzoic acid-KPVSTEQLAQ-N-[2,4-dinitrophenyl]ethylenediamine , Ortho-aminobenzoic acid-KPPVVLLPDQ-N-[2,4-dinitrophenyl]ethylenediamine, ortho-aminobenzoic acid-LFEKQ-N-[2,4-dinitrophenyl]ethylenediamine, ortho-aminobenzoic acid-VLFEKQ-N-[2,4-dinitrophenyl]ethylenediamine, and ortho-aminobenzoic acid-VLFEKKQ-N-[2,4-dinitrophenyl]ethylenediamine
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(2-fluorobenzophenone) thiosemicarbazone
-
(2E)-2-(6-bromo-1,1-dioxido-2,3-dihydro-4H-thiochromen-4-ylidene)hydrazinecarbothioamide
-
(2E)-2-(6-bromo-2,3-dihydro-4H-thiochromen-4-ylidene)hydrazinecarbothioamide
-
(2E)-2-(6-bromo-2,3-dihydroquinolin-4(1H)-ylidene)hydrazinecarbothioamide
-
(2E)-2-(6-nitro-2,3-dihydro-4H-thiochromen-4-ylidene)hydrazinecarbothioamide
-
(2E)-2-[6-(propan-2-yloxy)-2,3-dihydro-4H-thiochromen-4-ylidene]hydrazinecarbothioamide
-
(2Z)-1-[(12R)-22-amino-12-[(1S)-2-(4-benzoylphenyl)-1-[[(benzyloxy)carbonyl]amino]ethyl]-6,13,22-trioxo-17,20-dioxa-7,14-diazadocos-1-yl]-2-[(2E)-3-(1-ethyl-3,3-dimethyl-5-sulfo-2,3-dihydro-1H-indol-2-yl)prop-2-en-1-ylidene]-3,3-dimethyl-2,3-dihydro-1H-indole-5-sulfonic acid
-
(3-bromo-2'-fluoro-3'-hydroxybenzophenone) thiosemicarbazone
-
(3-bromo-3'-hydroxybenzophenone) thiosemicarbazone
a slowly reversible inhibitor of cathepsin L
(3-hydroxybenzophenone) thiosemicarbazone
-
(4-bromo-2'-fluoro-3'-hydroxybenzophenone) thiosemicarbazone
-
(N-[4-(5-benzoyl-1H-benzimidazol-2-yl)phenyl]-2-chlorobenzamide)
-
(R)-S-2-(2-ethylphenylamino)-2-oxoethyl 2-(2-(tert-butoxycarbonylamino)-3-(1H-indol-3-yl)propanoyl)hydrazinecarbothioate
R-enantiomer, thiol ester containing a diacyl hydrazine functionality and one stereogenic center
(S)-2-(3,4-dihydroquinolin-1(2H)-yl)-2-oxoethyl 2-(2-(tert-butoxycarbonylamino)-3-(1H-indol-3-yl)propanoyl)hydrazinecarboxylate
-
(S)-S-2-(2-ethylphenylamino)-2-oxoethyl 2-(2-(tert-butoxycarbonylamino)-3-(1H-indol-3-yl)propanoyl)hydrazinecarbothioate
S-enantiomer, thiol ester containing a diacyl hydrazine functionality and one stereogenic center
1,3,5-trisbenzoylbenzene thiosemicarbazone
-
1,3-bis(2-fluorobenzoyl)-5-bromobenzene thiosemicarbazone
molecular docking in the active site
1,3-bis(3-bromobenzoyl)-5-bromobenzene thiosemicarbazone
-
1,3-bis(3-bromobenzoyl)-5-hydroxybenzene thiosemicarbazone
-
1,3-bis(3-hydroxybenzoyl)-5-bromobenzene thiosemicarbazone
-
1,3-bis(3-methylbenzoyl)benzene thisosemicarbazone
-
1,3-bis(4-bromobenzoyl)benzene bis-thiosemicarbazone
-
1,3-bis(4-bromobenzoyl)benzene thiosemicarbazone
-
1,3-bis(4-fluorobenzoyl)benzene thiosemicarbazone
-
1,3-bis(4-hydroxybenzoyl)benzene thiosemicarbazone
-
1,3-bis(4-isopropoxybenzoyl)benzene thiosemicarbazone
-
1,3-bis(4-methoxybenzoyl)benzene thiosemicarbazone
-
2,6-dimethoxy-4-[4-(4-phenoxyphenyl)-5-phenyl-1H-imidazol-2-yl]phenol
-
2,6-dimethoxy-4-[5-phenyl-4-[4-(phenylsulfanyl)phenyl]-1H-imidazol-2-yl]phenol
-
2-(1,3-benzodioxol-5-yl)-5-phenyl-4-[4-(phenylsulfanyl)phenyl]-1H-imidazole
-
2-(3,4-dimethoxyphenyl)-5-phenyl-4-[4-(phenylsulfanyl)phenyl]-1H-imidazole
-
2-(4-methoxyphenyl)-4-[8-[2-(4-methoxyphenyl)-4-phenyl-1H-imidazol-5-yl]dibenzo[b,d]furan-2-yl]-5-phenyl-1H-imidazole
-
2-(4-methoxyphenyl)-5-phenyl-4-[4-(phenylsulfanyl)phenyl]-1H-imidazole
-
2-(acetylamino)-N-[4-(6-[[2-(acetylamino)benzoyl]amino]-1H-benzimidazol-2-yl)phenyl]benzamide
-
2-(furan-2-yl)-4-[8-[2-(furan-2-yl)-4-phenyl-1H-imidazol-5-yl]dibenzo[b,d]furan-2-yl]-5-phenyl-1H-imidazole
-
2-cyano-4-(2-hydroxyethoxy)-N-methyl-6-[(spiro[3.5]non-7-ylmethyl)amino]pyrimidine-5-carboxamide
-
2-cyano-4-(cyclohexylamino)-N-(2-phenylethyl)pyrimidine-5-carboxamide
-
2-cyano-4-(cyclohexylmethoxy)-N-(2-phenylethyl)pyrimidine-5-carboxamide
-
2-cyano-4-[(1,4-dioxaspiro[4.5]dec-8-ylmethyl)amino]-N-methyl-6-[(1-methylpiperidin-4-yl)methoxy]pyrimidine-5-carboxamide
-
2-cyano-4-[(2-cyclopentylethyl)amino]-N-methyl-6-[(1-methylpiperidin-4-yl)methoxy]pyrimidine-5-carboxamide
-
2-cyano-4-[(6,8-dioxaspiro[3.5]non-7-ylmethyl)amino]-N-methyl-6-[(1-methylpiperidin-4-yl)methoxy]pyrimidine-5-carboxamide
-
2-cyano-4-[(cyclohexylmethyl)(methyl)amino]-N-(2-phenylethyl)pyrimidine-5-carboxamide
-
2-cyano-4-[(cyclohexylmethyl)amino]-N-(2-phenylethyl)pyrimidine-5-carboxamide
-
2-cyano-4-[2-(1-methylpiperidin-4-yl)ethoxy]-N-(2-phenylethyl)-6-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
-
2-cyano-4-[[(4,4-difluorocyclohexyl)methyl]amino]-N-(2-phenylethyl)pyrimidine-5-carboxamide
-
2-cyano-4-[[(4,4-dimethylcyclohexyl)methyl]amino]-N-(2-phenylethyl)pyrimidine-5-carboxamide
-
2-cyano-4-[[1-(2-hydroxyethyl)piperidin-4-yl]methoxy]-N-methyl-6-[(spiro[3.5]non-7-ylmethyl)amino]pyrimidine-5-carboxamide
-
2-cyano-N-(1-methyl-4-phenylpiperidin-4-yl)-4-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
-
2-cyano-N-(2-phenylethyl)-4-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
-
2-cyano-N-(4,5-dimethoxybiphenyl-2-yl)-4-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
-
2-cyano-N-methyl-4-(piperidin-4-ylmethoxy)-6-[(spiro[3.5]non-7-ylmethyl)amino]pyrimidine-5-carboxamide
-
2-cyano-N-methyl-4-[(1-methylpiperidin-4-yl)methoxy]-6-[(spiro[3.5]non-7-ylmethyl)amino]pyrimidine-5-carboxamide
-
2-cyano-N-methyl-4-[(1-methylpiperidin-4-yl)methoxy]-6-[(spiro[4.5]dec-8-ylmethyl)amino]pyrimidine-5-carboxamide
-
2-cyano-N-methyl-4-[(spiro[3.5]non-7-ylmethyl)amino]-6-[(2,2,6,6-tetramethylpiperidin-4-yl)oxy]pyrimidine-5-carboxamide
-
2-cyano-N-methyl-4-[2-(1-methylpiperidin-4-yl)ethoxy]-6-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
-
2-cyano-N-methyl-4-[2-(1-methylpiperidin-4-yl)ethoxy]-6-[(spiro[3.5]non-7-ylmethyl)amino]pyrimidine-5-carboxamide
-
2-cyano-N-methyl-4-[[1-(1-methylethyl)piperidin-4-yl]methoxy]-6-[(spiro[3.5]non-7-ylmethyl)amino]pyrimidine-5-carboxamide
-
2-cyano-N-[(1-methyl-4-phenylpiperidin-4-yl)methyl]-4-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
-
2-cyano-N-[(1R)-2-pyridin-2-yl-1-(pyrrolidin-1-ylmethyl)ethyl]-4-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
-
2-cyano-N-[5-[(1-methylpiperidin-4-yl)oxy]biphenyl-2-yl]-4-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
-
3-benzoylbenzhydrol thiosemicarbazone
-
3-[(E)-(4-[[4-([2-[([[3-cyclohexyl-N-(morpholin-4-ylcarbonyl)-L-alanyl]amino][(6-[(2Z)-2-[(2E,4E,6Z)-7-(1-ethyl-3,3-dimethyl-5-sulfo-2,3-dihydro-1H-indol-2-yl)hepta-2,4,6-trien-1-ylidene]-3,3-dimethyl-5-sulfo-2,3-dihydro-1H-indol-1-yl]hexanoyl)amino]acetyl)amino]ethyl]amino)-4-oxobutyl](methyl)amino]phenyl)diazenyl]-7-(diethylamino)-5-phenylphenazin-5-ium
-
4,4'-[methanediylbis(1H-benzimidazole-5,2-diyl)]dianiline
-
4-(4-[8-[2-(4-carboxyphenyl)-4-phenyl-1H-imidazol-5-yl]dibenzo[b,d]furan-2-yl]-5-phenyl-1H-imidazol-2-yl)benzoic acid
-
4-(4-[8-[2-(4-hydroxyphenyl)-4-phenyl-1H-imidazol-5-yl]dibenzo[b,d]furan-2-yl]-5-phenyl-1H-imidazol-2-yl)phenol
-
4-amino-N-(4-[6-[(4-aminobenzoyl)amino]-1H-benzimidazol-2-yl]phenyl)benzamide
-
4-bromophenyl (1E,3S)-3-([N-[(benzyloxy)carbonyl]-L-phenylalanyl]amino)-5-methylhex-1-ene-1-sulfonate
i.e. KD-1
4-bromophenyl (S,E)-3-((S)-2-((((4-ethynylbenzyl)oxy)carbonyl)amino)-3-phenylpropanamido)-5-methylhex-1-ene-1-sulfonate
i.e. KDP-1, in vivo inhibition of cathepsin L. Inhibition of cathepsin L compared to other cathepsins, overview
4-[(1-acetylpiperidin-4-yl)methoxy]-2-cyano-N-methyl-6-[(spiro[3.5]non-7-ylmethyl)amino]pyrimidine-5-carboxamide
-
4-[(E)-benzylideneamino]-N-[4-[6-([4-[(E)-benzylideneamino]benzoyl]amino)-1H-benzimidazol-2-yl]phenyl]benzamide
-
4-[2-(1-methylpiperidin-4-yl)ethoxy]-6-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-2-carbonitrile
-
4-[4-(5,5-dioxidodibenzo[b,d]thiophen-2-yl)-5-phenyl-1H-imidazol-2-yl]-2,6-dimethoxyphenol
-
4-[5-(4-[[2-(4-aminophenyl)-1H-benzimidazol-6-yl]oxy]phenoxy)-1H-benzimidazol-2-yl]aniline
-
4-[5-phenyl-4-[4-(phenylsulfanyl)phenyl]-1H-imidazol-2-yl]phenol
-
4-[8-(2,4-diphenyl-1H-imidazol-5-yl)dibenzo[b,d]furan-2-yl]-2,5-diphenyl-1H-imidazole)
-
5-bromo-4-[2-(1-methylpiperidin-4-yl)ethoxy]-6-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-2-carbonitrile
-
5-phenyl-4-[4-(phenylsulfanyl)phenyl]-2-(2,4,5-trimethoxyphenyl)-1H-imidazole
-
5-phenyl-4-[4-(phenylsulfanyl)phenyl]-2-(3,4,5-trimethoxyphenyl)-1H-imidazole
-
benzophenone thiosemicarbazone
-
benzoylbenzophenone thiosemicarbazone
molecular docking in the active site
benzyloxycarbonyl-Phe-Phe-fluoromethyl ketone
-
biphenyl-4-yl-acetylasparagine-D-Arg-Phe-Phe-NH2
-
biphenyl-4-yl-acetylcysteine-D-Arg-Abu-N-(2-phenylethyl)amide
-
biphenyl-4-yl-acetylcysteine-D-Arg-Arg-N-(2-phenylethyl)amide
-
biphenyl-4-yl-acetylcysteine-D-Arg-N-(2-phenylethyl)amide
-
biphenyl-4-yl-acetylcysteine-D-Arg-Phe-N-(2-phenylethyl)amide
-
biphenyl-4-yl-acetylcysteine-D-Arg-Phe-Phe-NH2
-
biphenyl-4-yl-acetylcysteine-D-Arg-Trp-N-(2-phenylethyl)amide
-
biphenyl-4-yl-acetylcysteine-D-Arg-Tyr-N-(2-phenylethyl)amide
-
biphenyl-4-yl-acetylmethylcysteine-D-Arg-Leu-N-(2-phenylethyl)amide
-
biphenyl-4-yl-acetylmethylcysteine-D-Arg-Met-N-(2-phenylethyl)amide
-
biphenyl-4-yl-acetylmethylcysteine-D-Arg-Phe-N-(2-phenylethyl)amide
the inhibitor shows a 310fold and 210fold selectivity for cathepsin L over cathepsin K and B, respectively
biphenyl-4-yl-acetylmethylcysteine-D-Arg-Phe-N-(3-phenylpropyl)amide
-
biphenyl-4-yl-acetylmethylcysteine-D-Arg-Phe-N-(benzyl)amide
-
biphenyl-4-yl-acetylmethylcysteine-D-Arg-Phe-Phe-NH2
-
biphenyl-4-yl-acetylmethylcysteine-D-Orn-Phe-N-(2-phenylethyl)amide
-
biphenyl-4-yl-acetylmethylcysteine-Gly-Phe-Phe-NH2
-
biphenyl-4-yl-acetylnorvaline-D-Arg-Phe-N-(2-phenylethyl)amide
-
biphenyl-4-yl-acetylserine-D-Arg-Phe-Phe-NH2
-
biphenylacetyl-(N6-biphenylacetyl)-Lys-D-Arg-Tyr-N-phenylethyl
-
biphenylacetyl-(N6-biphenylacetyl)Lys-D-Arg-Phe-N-phenylethyl
-
biphenylacetyl-MCys-D-Arg-Phe-N-phenylethyl
-
bis[2-(4-aminophenyl)-1H-benzimidazol-5-yl]methanone
-
cathepsin L inhibitor 1
-
CLIK-181
cathepsin L-specific inhibitor
E64
inhibition of gelatinolytic activity
KAPR-acetyl-K-QLATKAARKSAPA
-
KAPRKQLAT-acetyl-K-AARKSAPA
-
KAPRKQLATKAAR-dimethyl-K-SAPA
-
L-trans-epoxysuccinyl-leucylamido-(4-guanidino)butane
E-64
L-trans-epoxysuccinylleucylamido-(4-guanidino)butane
i.e. E-64, complete inhibition at 0.26 mM
leupeptin
inhibition of gelatinolytic activity and of autolcleavage of cathepsin L
N-(4-benzyl-1-methylpiperidin-4-yl)-2-cyano-4-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
-
N-acetyl-Leu-Leumethional
inhibition of gelatinolytic activity
N-benzyl-2-cyano-4-[(1-methylpiperidin-4-yl)methoxy]-6-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
-
N-benzyl-2-cyano-4-[(1-methylpiperidin-4-yl)oxy]-6-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
-
N-benzyl-2-cyano-4-[2-(1-methylpiperidin-4-yl)ethoxy]-6-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
-
N-benzyloxycarbonyl-phenylalanyl-phenylalanine-fluoromethyl ketone
an irreversible cathepsin inhibitor
N-[(1R)-1-benzyl-2-pyrrolidin-1-ylethyl]-2-cyano-4-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
-
N-[(1R)-1-benzyl-2-pyrrolidin-1-ylpropyl]-2-cyano-4-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
-
N-[(1S)-1-benzyl-2-pyrrolidin-1-ylethyl]-2-cyano-4-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
-
N-[4-(1H-benzimidazol-2-yl)phenyl]-2,2-diphenylacetamide
-
N-[4-(5-benzoyl-1H-benzimidazol-2-yl)phenyl]-2-chlorobenzamide
-
N-[6-[(6-[3,3-dimethyl-2-[(1E,3E,5E)-5-(1,3,3-trimethyl-1,3-dihydro-2H-indol-2-ylidene)penta-1,3-dien-1-yl]-3H-indolium-1-yl]hexanoyl)amino]hexanoyl]-L-histidyl-L-threonyl-N-[(2R)-1-(benzylsulfanyl)-4-[(2,6-dimethylbenzoyl)oxy]-3-oxobutan-2-yl]-2,3,4,5,6-pentafluoro-L-phenylalaninamide
-
N2-[(benzyloxy)carbonyl]-L-lysyl-N-[4-([[(5-methyl-7-oxo-7,8-dihydronaphthalen-2-yl)carbamoyl]oxy]methyl)phenyl]-L-lysinamide
-
Nalpha-[(benzyloxy)carbonyl]-N-[(3S)-7-[(6-[(2Z)-3,3-dimethyl-5-sulfo-2-[(2E,4E)-5-(1,3,3-trimethyl-5-sulfo-2,3-dihydro-1H-indol-2-yl)penta-2,4-dien-1-ylidene]-2,3-dihydro-1H-indol-1-yl]hexanoyl)amino]-2-oxo-1-(2,3,5,6-tetrafluoro-4-[[2-([[1-(2-[(3E)-3-(5-sulfo-2,3-dihydro-1H-indolium-1-ylidene)-6-(5-sulfo-2,3-dihydro-1H-indol-1-yl)-3H-xanthen-9-yl]benzene-1-sulfonyl)piperidin-4-yl]carbonyl]amino)ethyl]carbamoyl]phenoxy)heptan-3-yl]-L-phenylalaninamide
-
p41-fragment-human
64 residues present in the p41 form of the human major histocompatibility complex II (MHCII)-associated invariant chain
-
Phe-Tyr-(OBut)-COCHO
potent, reversible, synthetic peptidyl inhibitor of cathepsin L
Phe-Tyr-(tert-Bu)-diazomethylketone
irreversible inhibitor that can inactivate cathepsin L at micromolar concentrations
soluble type I collagen
inhibitory against cathepsin L, Ki is 0.36 mg/ml, collagen is also a substrate for the enzyme
-
Stefin B
a potent cathepsin L inhibitor, colorectal carcinoma cells reveal only very faint amounts of immunolabeled stefin B within their nuclei, while it is prominently present within the cytoplasm of Caco-2 and SW-620 cells, and mostly associated with the cytoplasmic face of vesicles in HCT-116 cells
-
(((2S,3S)-epoxysuccinyl-(S)-leucyl)amino)-4-guanidinobutane
-
-
(13alpha,17alpha,20S,24Z)-3-hydroxylanosta-7,24-dien-26-oic acid
-
competitive inhibition
(13alpha,17alpha,20S,24Z)-3-oxolanosta-7,24-dien-26-oic acid
-
competitive inhibition
(2E)-2-(7-bromo-3,4-dihydronaphthalen-1(2H)-ylidene)hydrazinecarbothioamide
-
-
(2E)-2-[(2-fluorophenyl)(4-fluorophenyl)methylidene]hydrazinecarbothioamide
-
-
(2E)-2-[(3-bromophenyl)(3,4,5-trifluorophenyl)methylidene]hydrazinecarbothioamide
-
-
(2E)-2-[(3-bromophenyl)(3,5-dichlorophenyl)methylidene]hydrazinecarbothioamide
-
-
(2E)-2-[(3-bromophenyl)(3,5-difluorophenyl)methylidene]hydrazinecarbothioamide
-
-
(2E)-2-[(3-bromophenyl)(3-chlorophenyl)methylidene]hydrazinecarbothioamide
-
-
(2E)-2-[(3-bromophenyl)(3-fluorophenyl)methylidene]hydrazinecarbothioamide
-
-
(2E)-2-[(3-bromophenyl)(3-methylphenyl)methylidene]hydrazinecarbothioamide
-
-
(2E)-2-[(3-bromophenyl)(4-bromophenyl)methylidene]hydrazinecarbothioamide
-
-
(2E)-2-[(3-bromophenyl)(4-chlorophenyl)methylidene]hydrazinecarbothioamide
-
-
(2E)-2-[(3-bromophenyl)(4-fluorophenyl)methylidene]hydrazinecarbothioamide
-
-
(2E)-2-[(3-bromophenyl)(4-methylphenyl)methylidene]hydrazinecarbothioamide
-
-
(2E)-2-[(3-bromophenyl)[3-(trifluoromethyl)phenyl]methylidene]hydrazinecarbothioamide
-
-
(2E)-2-[(3-bromophenyl)[4-(trifluoromethyl)phenyl]methylidene]hydrazinecarbothioamide
-
-
(2E)-2-[(4-bromophenyl)(4-chlorophenyl)methylidene]hydrazinecarbothioamide
-
-
(2E)-2-[(4-bromophenyl)(4-fluorophenyl)methylidene]hydrazinecarbothioamide
-
-
(2E)-2-[(4-bromophenyl)(4-methylphenyl)methylidene]hydrazinecarbothioamide
-
-
(2E)-2-[(4-bromophenyl)[4-(trifluoromethyl)phenyl]methylidene]hydrazinecarbothioamide
-
-
(2E)-2-[[3,5-bis(trifluoromethyl)phenyl](3-bromophenyl)methylidene]hydrazinecarbothioamide
-
-
(2E)-[(3E)-28-methoxy-28-oxours-12-en-3-ylidene]acetic acid
-
competitive inhibition
(2R,3R)-dibenzyl-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(S)-prolyl]-aziridine-2,3-dicarboxylate
-
-
(2R,3R)-diethyl-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(R)-azetidine-2-carbonyl]aziridine-2,3-dicarboxylate
-
-
(2R,3R)-diethyl-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(R)-nipecotyl]aziridine-2,3-dicarboxylate
-
-
(2R,3R)-diethyl-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(S)-azetidine-2-carbonyl]aziridine-2,3-dicarboxylate
-
-
(2R,3R)-diethyl-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(S)-nipecotyl]aziridine-2,3-dicarboxylate
-
-
(2R,3R)-diethyl-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-isonipecotyl]-aziridine-2,3-dicarboxylate
-
-
(2S,3S)-1-[N-(tert-butoxycarbonyl)-(R)-leucyl-(S)-nipecotyl]aziridine-2,3-dicarboxylic acid
-
-
(2S,3S)-1-[N-(tert-butoxycarbonyl)-(R)-phenylalanyl-(R)-alanyl]aziridine-2,3-dicarboxylic acid
-
-
(2S,3S)-1-[N-(tert-butoxycarbonyl)-(R)-phenylalanyl-(S)-alanyl]aziridine-2,3-dicarboxylic acid
-
-
(2S,3S)-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(R)-nipecotyl]aziridine-2,3-dicarboxylic acid
-
-
(2S,3S)-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(S)-nipecotyl]aziridine-2,3-dicarboxylic acid
-
-
(2S,3S)-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(S)-prolyl]aziridine-2,3-dicarboxylic acid
-
-
(2S,3S)-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-isonipecotyl]aziridine-2,3-dicarboxylic acid
-
-
(2S,3S)-1-[N-(tert-butoxycarbonyl)-(S)-phenylalanyl-(R)-alanyl]aziridine-2,3-dicarboxylic acid
-
-
(2S,3S)-1-[N-(tert-butoxycarbonyl)-(S)-phenylalanyl-(S)-alanyl]aziridine-2,3-dicarboxylic acid
-
-
(2S,3S)-1-[N-(tert-butoxycarbonyl)-glycyl-(R)-nipecotyl]aziridine-2,3-dicarboxylic acid
-
-
(2S,3S)-1-[N-(tert-butoxycarbonyl)-glycyl-(R)-prolyl]aziridine-2,3-dicarboxylic acid
-
-
(2S,3S)-1-[N-(tert-butoxycarbonyl)-glycyl-(S)-nipecotyl]aziridine-2,3-dicarboxylic acid
-
-
(2S,3S)-1-[N-(tert-butoxycarbonyl)-glycyl-(S)-prolyl]aziridine-2,3-dicarboxylic acid
-
-
(2S,3S)-3-([(2S)-1-[(8-carbamimidamidooctyl)amino]-4-methyl-1-oxopentan-2-yl]carbamoyl)oxirane-2-carboxylic acid
-
-
(2S,3S)-dibenzyl-1-[1-[N-(tert-butoxycarbonyl)-(R)-leucyl]-(S)-aziridine-2-carbonyl]aziridine-2,3-dicarboxylate
-
-
(2S,3S)-dibenzyl-1-[1-[N-(tert-butoxycarbonyl)-(S)-leucyl]-(S)-aziridine-2-carbonyl]aziridine-2,3-dicarboxylate
-
-
(2S,3S)-dibenzyl-1-[biotinyl-6-aminohexanoyl]-aziridine-2,3-dicarboxylate
-
-
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-(R)-leucyl-(R)-nipecotyl]aziridine-2,3-dicarboxylate
-
-
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-(R)-leucyl-(R)-prolyl]-aziridine-2,3-dicarboxylate
-
-
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-(R)-leucyl-(S)-nipecotyl]aziridine-2,3-dicarboxylate
-
-
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-(R)-leucyl-(S)-prolyl]-aziridine-2,3-dicarboxylate
-
-
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-(R)-phenylalanyl-(R)-alanyl]aziridine-2,3-dicarboxylate
-
-
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-(R)-phenylalanyl-(S)-alanyl]aziridine-2,3-dicarboxylate
-
-
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(R)-azetidine-2-carbonyl]aziridine-2,3-dicarboxylate
-
-
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(R)-nipecotyl]aziridine-2,3-dicarboxylate
-
-
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(R)-prolyl]-aziridine-2,3-dicarboxylate
-
-
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(S)-azetidine-2-carbonyl]aziridine-2,3-dicarboxylate
-
-
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(S)-nipecotyl]aziridine-2,3-dicarboxylate
-
-
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-(S)-phenylalanyl-(R)-alanyl]aziridine-2,3-dicarboxylate
-
-
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-(S)-phenylalanyl-(S)-alanyl]aziridine-2,3-dicarboxylate
-
-
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-glycyl-(R)-nipecotyl]aziridine-2,3-dicarboxylate
-
-
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-glycyl-(R)-prolyl]aziridine-2,3-dicarboxylate
-
-
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-glycyl-(R+S)-nipecotyl]aziridine-2,3-dicarboxylate
-
-
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-glycyl-(S)-pipecolyl]-aziridine-2,3-dicarboxylate
-
-
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-glycyl-(S)-prolyl]aziridine-2,3-dicarboxylate
-
-
(2S,3S)-diethyl-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(R)-nipecotyl]aziridine-2,3-dicarboxylate
-
-
(2S,3S)-diethyl-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(S)-nipecotyl]aziridine-2,3-dicarboxylate
-
-
(2S,3S)-diethyl-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(S)-prolyl]aziridine-2,3-dicarboxylate
-
-
(2S,3S)-diethyl-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-isonipecotyl]-aziridine-2,3-dicarboxylate
-
-
(2S,3S)-oxirane-2,3-dicarboxylic acid 2-[((S)-1-benzylcarbamoyl-2-phenyl-ethyl)-amide] 3-[[2-(4-hydroxy-phenyl)-ethyl]-amide]
-
i.e. CAA0225. Significantly inhibits degradation of long-lived proteins in HeLa and Huh-7 cells cultured under nutrient-deprived conditions. CAA0225 effectively inhibits degradation of microtubule-associated protein IA/IB light chain 3-II and gamma-aminobutyric acid (A) receptor-associated protein
(2S,3S+2R,3R)-dibenzyl-1-[desthiobiotinyl-6-aminohexanoyl]-aziridine-2,3-dicarboxylate
-
-
(2Z)-2-[(2-bromophenyl)(3-bromophenyl)methylidene]hydrazinecarbothioamide
-
-
(2Z)-2-[(2-bromophenyl)(4-bromophenyl)methylidene]hydrazinecarbothioamide
-
-
(2Z)-2-[(2-fluorophenyl)(phenyl)methylidene]hydrazinecarbothioamide
-
-
(2Z)-2-[(3-bromo-2-fluorophenyl)(3-bromophenyl)methylidene]hydrazinecarbothioamide
-
-
(2Z)-2-[(3-bromo-4-fluorophenyl)(3-bromophenyl)methylidene]hydrazinecarbothioamide
-
-
(2Z)-2-[(3-bromophenyl)(2,3,4,5-tetrafluorophenyl)methylidene]hydrazinecarbothioamide
-
-
(2Z)-2-[(3-bromophenyl)(2,3-difluorophenyl)methylidene]hydrazinecarbothioamide
-
-
(2Z)-2-[(3-bromophenyl)(2,6-difluorophenyl)methylidene]hydrazinecarbothioamide
-
-
(2Z)-2-[(3-bromophenyl)(2-chlorophenyl)methylidene]hydrazinecarbothioamide
-
-
(2Z)-2-[(3-bromophenyl)(2-fluorophenyl)methylidene]hydrazinecarbothioamide
-
-
(2Z)-2-[(3-bromophenyl)(2-methylphenyl)methylidene]hydrazinecarbothioamide
-
-
(2Z)-2-[(4-bromophenyl)(2-fluorophenyl)methylidene]hydrazinecarbothioamide
-
-
(2Z)-2-[[3,5-bis(trifluoromethyl)phenyl](4-methylphenyl)methylidene]hydrazinecarbothioamide
-
-
(3-[[2-cyano-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidin-6-yl]methoxy]phenyl)acetic acid
-
pyrrolopyrimidine inhibitor by modification of the P3 moieties
(3E)-3-(carboxymethylidene)olean-12-en-28-oic acid
-
competitive inhibition
(3E)-3-(carboxymethylidene)urs-12-en-28-oic acid
-
competitive inhibition
(E)N-[(S)1-[(S)2-cyano-1-pyrrolidinecarbonyl]-3-methylbutyl]-2,3-diphenylacrylamide
-
selective towards cathepsin L over cathepsin B
1,3-dihydro-pyrrolo[3,4-b]quinoline-2-carbonitrile
-
IC50: 0.00045 mM
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([2-methyl-4-[(methylsulfonyl)amino]phenyl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([3-methyl-4-[(methylsulfonyl)amino]phenyl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([3-methyl-4-[(phenylsulfonyl)amino]phenyl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([3-[(methylsulfonyl)amino]phenyl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([4-[(methylsulfonyl)amino]phenyl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([4-[(phenylsulfonyl)amino]phenyl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([4-[(pyridin-2-ylsulfonyl)amino]phenyl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([4-[(pyridin-3-ylsulfonyl)amino]phenyl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([4-[(pyridin-4-ylsulfonyl)amino]phenyl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([4-[(thiophen-2-ylsulfonyl)amino]phenyl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([4-[methyl(methylsulfonyl)amino]phenyl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([6-[(methylsulfonyl)amino]pyridin-3-yl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([6-[(phenylsulfonyl)amino]pyridin-3-yl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-2-([[4-([[(dimethylamino)methyl]sulfonyl]amino)phenyl]carbonyl]amino)-3-(1-methylcyclopentyl)propanoyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-2-[([2-methoxy-4-[(methylsulfonyl)amino]phenyl]carbonyl)amino]-3-(1-methylcyclopentyl)propanoyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-2-[([3-fluoro-4-[(methylsulfonyl)amino]phenyl]carbonyl)amino]-3-(1-methylcyclopentyl)propanoyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-2-[([3-methoxy-4-[(methylsulfonyl)amino]phenyl]carbonyl)amino]-3-(1-methylcyclopentyl)propanoyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-2-[([4-[(ethylsulfonyl)amino]phenyl]carbonyl)amino]-3-(1-methylcyclopentyl)propanoyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-2-[[(4-[[(2,4-dimethyl-1,3-thiazol-5-yl)sulfonyl]amino]phenyl)carbonyl]amino]-3-(1-methylcyclopentyl)propanoyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-2-[[(4-[[(2-fluorophenyl)sulfonyl]amino]phenyl)carbonyl]amino]-3-(1-methylcyclopentyl)propanoyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-2-[[(4-[[(3-fluorophenyl)sulfonyl]amino]phenyl)carbonyl]amino]-3-(1-methylcyclopentyl)propanoyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-2-[[(4-[[(3-methoxyphenyl)sulfonyl]amino]phenyl)carbonyl]amino]-3-(1-methylcyclopentyl)propanoyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-2-[[(4-[[(4-fluorophenyl)sulfonyl]amino]phenyl)carbonyl]amino]-3-(1-methylcyclopentyl)propanoyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-2-[[(4-[[(4-methoxyphenyl)sulfonyl]amino]phenyl)carbonyl]amino]-3-(1-methylcyclopentyl)propanoyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-3-(1-methylcyclopentyl)-2-([[4-(methylsulfamoyl)phenyl]carbonyl]amino)propanoyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-3-(1-methylcyclopentyl)-2-([[4-([[4-(1-methylethyl)-1,3-thiazol-2-yl]sulfonyl]amino)phenyl]carbonyl]amino)propanoyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-3-(1-methylcyclopentyl)-2-[[(4-sulfamoylphenyl)carbonyl]amino]propanoyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-3-(1-methylcyclopentyl)-2-[[(4-[[(1-methyl-1H-imidazol-2-yl)sulfonyl]amino]phenyl)carbonyl]amino]propanoyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-3-(1-methylcyclopentyl)-2-[[(4-[[(1-methylethyl)sulfonyl]amino]phenyl)carbonyl]amino]propanoyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-3-(1-methylcyclopentyl)-2-[[(4-[[(2,2,2-trifluoroethyl)sulfonyl]amino]phenyl)carbonyl]amino]propanoyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-3-(1-methylcyclopentyl)-2-[[(4-[[(2-methylphenyl)sulfonyl]amino]phenyl)carbonyl]amino]propanoyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-3-(1-methylcyclopentyl)-2-[[(4-[[(4-methyl-1,3-thiazol-2-yl)sulfonyl]amino]phenyl)carbonyl]amino]propanoyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-3-(1-methylcyclopentyl)-2-[[(4-[[(4-methylpyridin-3-yl)sulfonyl]amino]phenyl)carbonyl]amino]propanoyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-3-(1-methylcyclopentyl)-2-[[(4-[[(5-methyl-1,3-thiazol-2-yl)sulfonyl]amino]phenyl)carbonyl]amino]propanoyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[4-methyl-N-(thiophen-3-ylcarbonyl)-L-leucyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3-[[(2S)-2-[([3-chloro-4-[(methylsulfonyl)amino]phenyl]carbonyl)amino]-3-(1-methylcyclopentyl)propanoyl]amino]-3,5,6-trideoxy-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3-[[(2S)-2-[([3-chloro-4-[(phenylsulfonyl)amino]phenyl]carbonyl)amino]-3-(1-methylcyclopentyl)propanoyl]amino]-3,5,6-trideoxy-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3-[[(2S)-2-[([4-[(benzylsulfonyl)amino]phenyl]carbonyl)amino]-3-(1-methylcyclopentyl)propanoyl]amino]-3,5,6-trideoxy-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3-[[(2S)-2-[([4-[(butylsulfonyl)amino]phenyl]carbonyl)amino]-3-(1-methylcyclopentyl)propanoyl]amino]-3,5,6-trideoxy-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3-[[(2S)-2-[([4-[(cyclopropylsulfonyl)amino]phenyl]carbonyl)amino]-3-(1-methylcyclopentyl)propanoyl]amino]-3,5,6-trideoxy-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3-[[(2S)-2-[[(4-[[(2-chloropyridin-3-yl)sulfonyl]amino]phenyl)carbonyl]amino]-3-(1-methylcyclopentyl)propanoyl]amino]-3,5,6-trideoxy-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3-[[(2S)-2-[[(4-[[(2-cyanophenyl)sulfonyl]amino]phenyl)carbonyl]amino]-3-(1-methylcyclopentyl)propanoyl]amino]-3,5,6-trideoxy-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3-[[(2S)-2-[[(4-[[(3-cyanophenyl)sulfonyl]amino]phenyl)carbonyl]amino]-3-(1-methylcyclopentyl)propanoyl]amino]-3,5,6-trideoxy-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3-[[(2S)-2-[[(4-[[(4-cyanophenyl)sulfonyl]amino]phenyl)carbonyl]amino]-3-(1-methylcyclopentyl)propanoyl]amino]-3,5,6-trideoxy-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3-[[(2S)-2-[[(4-[[(cyclohexylmethyl)sulfonyl]amino]phenyl)carbonyl]amino]-3-(1-methylcyclopentyl)propanoyl]amino]-3,5,6-trideoxy-L-glycero-hex-2-ulose
-
-
1-cyano-3-azetidinyl cyclohexylmethyl ether
-
IC50: 0.00001 mM
1-cyanoazetidine
-
IC50: 0.00043 mM
1-cyanopyrrolidine
-
IC50: 0.004 mM
1-naphthalenesulfonyl-Ile-Trp-aldehyde
1-nathalenesulfonyl-Ile-Trp-CHO
-
treatment of cells results in suppression of cellular proliferation and the induction of a cell death with no detecable caspase-3 activation or DNA fragmentation. Cell death is associated with increased accumulation of cathepsin D, cellular vacuolization, expression of the mannose 6-phosphate recepto, and the autophagy marker LC-II
2-(3,4-dihydroquinolin-1(2H)-yl)-2-oxoethyl 2-[(2S)-2-[(tert-butoxycarbonyl)amino]-3-(1H-indol-3-yl)propanoyl]hydrazinecarboxylate
-
unreactive to transesterification by cysteine and dithiothreitol nucleophiles. Inhibitor remains intact for greater than 24 h when incubated with cathepsin L under stoichiometric conditions, and in the presence of assay buffer
2-[bis(3-bromophenyl)methylidene]-N-ethylhydrazinecarbothioamide
-
-
2-[bis(3-bromophenyl)methylidene]-N-phenylhydrazinecarbothioamide
-
-
2-[bis(3-fluorophenyl)methylidene]hydrazinecarbothioamide
-
-
2-[bis(4-bromophenyl)methylidene]hydrazinecarbothioamide
-
-
2-[bis(4-fluorophenyl)methylidene]hydrazinecarbothioamide
-
-
2-[cyclohexyl(methyl)amino]-4H-3,1-benzothiazin-4-one
-
selective towards cathepsin L over cathepsin G, chymotrypsin, trypsin, human angiotensin-converting enzyme, human leukocyte elastase, acetylcholinesterase
2RS,3RS)-2-benzyl-3-ethyl-1-[N-(benzyloxycarbonyl)-glycyl-(S)-prolyl]aziridine-2,3-dicarboxylate
-
-
3-(benzyloxy)-1-cyanoazetidine
-
IC50: 0.00001 mM
3-(hydroxyimino)masticadienoic acid
-
competitive inhibition
3-(hydroxyimino)oleanolic acid
-
competitive inhibition
3-chloro-N-[(2S)-3-(3-chlorophenyl)-1-[(cyanomethyl)amino]-1-oxopropan-2-yl]benzamide
-
pH and temperature not specified in the publication
3-epiursolic acid
-
competitive inhibition
3-hydroxyolean-12-en-28-oic acid
-
competitive inhibition
3-hydroxyurs-12-en-28-oic acid
-
competitive inhibition
3-oxoolean-12-en-28-oic acid
-
competitive inhibition
3-oxours-12-en-28-oic acid
-
competitive inhibition
3-[(benzyloxy)methyl]-1-cyanopyrrolidine
-
IC50: 0.00015 mM
3-[[(2S)-2-[([3-acetyl-4-[(methylsulfonyl)amino]phenyl]carbonyl)amino]-3-(1-methylcyclopentyl)propanoyl]amino]-1,4-anhydro-3,5,6-trideoxy-L-glycero-hex-2-ulose
-
-
3-[[(2S)-2-[[(4-[[(4-aminophenyl)sulfonyl]amino]phenyl)carbonyl]amino]-3-(1-methylcyclopentyl)propanoyl]amino]-1,4-anhydro-3,5,6-trideoxy-L-glycero-hex-2-ulose
-
-
3-[[2-cyano-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidin-6-yl]methoxy]benzamide
-
pyrrolopyrimidine inhibitor by modification of the P3 moieties
4-[[2-cyano-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidin-6-yl]methoxy]benzamide
-
pyrrolopyrimidine inhibitor by modification of the P3 moieties
4-[[2-cyano-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidin-6-yl]methoxy]benzoic acid
-
pyrrolopyrimidine inhibitor by modification of the P3 moieties
6-(4-chlorobenzyl)-7-(2,2-dimethylpropyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P2 moieties
6-(4-chlorobenzyl)-7-(2-cycloheptylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P2 moieties
6-(4-chlorobenzyl)-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P2 moieties
6-(4-chlorobenzyl)-7-(2-cyclooctylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P2 moieties
6-(4-chlorobenzyl)-7-(2-cyclopentylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P2 moieties
6-(4-chlorobenzyl)-7-(2-phenylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P2 moieties
6-(4-chlorobenzyl)-7-(2-piperidin-1-ylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P2 moieties
6-(4-chlorobenzyl)-7-(3,3-dimethylbutyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P2 moieties
6-(4-chlorobenzyl)-7-(3-cyclohexylpropyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P2 moieties
6-(4-chlorobenzyl)-7-(4,4-dimethylpentyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P2 moieties
6-(4-chlorobenzyl)-7-(cyclohexylmethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P2 moieties
6-(4-chlorobenzyl)-7-[2-(3-chlorophenyl)ethyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P2 moieties
6-(4-chlorobenzyl)-7-[2-(4-chlorophenyl)ethyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P2 moieties
6-[[4-(1-acetyl-1,2,3,6-tetrahydropyridin-4-yl)phenoxy]methyl]-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P3 moieties
6-[[4-(1-acetylpiperidin-4-yl)phenoxy]methyl]-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P3 moieties
6-[[4-(4-acetyl-1,4-diazepan-1-yl)phenoxy]methyl]-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
-
6-[[4-(4-acetylpiperazin-1-yl)-2-fluorophenoxy]methyl]-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
-
6-[[4-(4-acetylpiperazin-1-yl)-3-fluorophenoxy]methyl]-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
-
6-[[4-(4-acetylpiperazin-1-yl)phenoxy]methyl]-7-(2-cycloheptylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
-
6-[[4-(4-acetylpiperazin-1-yl)phenoxy]methyl]-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
6-[[4-(4-acetylpiperazin-1-yl)phenoxy]methyl]-7-(2-cyclopentylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
-
6-[[4-(4-acetylpiperazin-1-yl)phenoxy]methyl]-7-[2-(4,4-difluorocyclohexyl)ethyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
-
6-[[4-(4-acetylpiperazin-1-yl)phenoxy]methyl]-7-[2-(4-chlorophenyl)ethyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
-
7-(2-cyclohexylethyl)-6-(4-methoxybenzyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P3 moieties
7-(2-cyclohexylethyl)-6-(cyclohexylmethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P3 moieties
7-(2-cyclohexylethyl)-6-(phenoxymethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P3 moieties
7-(2-cyclohexylethyl)-6-[(phenylamino)methyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P3 moieties
7-(2-cyclohexylethyl)-6-[(pyridin-2-yloxy)methyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P3 moieties
7-(2-cyclohexylethyl)-6-[(pyridin-2-ylsulfanyl)methyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P3 moieties
7-(2-cyclohexylethyl)-6-[[methyl(phenyl)amino]methyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P3 moieties
acetyl-Leu-Leu-Tyr-CHN2
-
-
alpha2 cysteine-proteinase inhibitor
-
-
-
benzofuran-2-carboxylic acid ((S)-1-[3-oxo-1-(pyridine-2-sulfonyl)azepan-4-ylcarbamoyl]-2-naphthylen-2-yl)amide
-
-
benzofuran-2-carboxylic acid ((S)-1-[3-oxo-1-(pyridine-2-sulfonyl)azepan-4-ylcarbamoyl]-2-phenyl-ethyl)amide
-
-
benzyl 1-cyano-3-pyrrolidinylcarbamate
-
IC50: 0.000054 mM
benzyl [(2S)-1-[[(2S)-1,6-diamino-1-oxohexan-2-yl]amino]-1-oxo-3-(1,1':4',1''-terphenyl-4-yl)propan-2-yl]carbamate
-
-
benzyl [(2S)-1-[[(2S)-1,6-diamino-1-oxohexan-2-yl]amino]-3-(2'-methylbiphenyl-4-yl)-1-oxopropan-2-yl]carbamate
-
-
benzyl [(2S)-1-[[(2S)-1,6-diamino-1-oxohexan-2-yl]amino]-3-(3'-methylbiphenyl-4-yl)-1-oxopropan-2-yl]carbamate
-
-
benzyl [(2S)-1-[[(2S)-1,6-diamino-1-oxohexan-2-yl]amino]-3-(4'-methylbiphenyl-4-yl)-1-oxopropan-2-yl]carbamate
-
-
benzyl [(2S)-3-(3'-aminobiphenyl-4-yl)-1-[[(2S)-1,6-diamino-1-oxohexan-2-yl]amino]-1-oxopropan-2-yl]carbamate
-
-
benzyl [(2S)-3-(3'-chlorobiphenyl-4-yl)-1-[[(2S)-1,6-diamino-1-oxohexan-2-yl]amino]-1-oxopropan-2-yl]carbamate
-
-
benzyl [(2S)-3-(biphenyl-4-yl)-1-[[(2S)-1,6-diamino-1-oxohexan-2-yl]amino]-1-oxopropan-2-yl]carbamate
-
-
benzyloxycarbonyl-iodophenylalanine-Ala-CHN2
-
-
benzyloxycarbonyl-iodotyrosine-Ala-CHN2
-
-
benzyloxycarbonyl-L-Phe-L-Phe-fluoromethylketone
benzyloxycarbonyl-Leu-homophenylalanine-CHN2
-
-
benzyloxycarbonyl-Leu-Leu-Phe-CHN2
-
-
benzyloxycarbonyl-Leu-Leu-Tyr-CHN2
-
-
benzyloxycarbonyl-Leu-Met-CHN2
-
-
benzyloxycarbonyl-Leu-Trp-CHN2
-
-
benzyloxycarbonyl-Leu-Tyr-CHN2
-
-
Benzyloxycarbonyl-Phe-Ala-CHN2
-
-
benzyloxycarbonyl-Phe-Ala-CNH2
-
-
benzyloxycarbonyl-Phe-Phe fluoromethylketone
-
cell-permeable irreversible cathepsin inhibitor
Benzyloxycarbonyl-Phe-Phe-CHN2
-
-
benzyloxycarbonyl-Phe-Tyr-(tert-butyl)-diazomethylketone
benzyloxycarbonyl-Phe-Tyr-CHO
-
-
benzyloxycarbonyl-Tyr-Ala-CHN2
-
-
CAA0225
-
i.e. (2S,3S)-oxirane-2,3-dicarboxylic acid 2-[((S)-1-benzylcarbamoyl-2-phenyl-ethyl)-amide]3-[[2-(4-hydroxy-phenyl)-ethyl]-amide], a cathepsin L-specific inhibitor
cathepsin K propeptide
-
-
-
cathepsin L propeptide
-
-
-
cathepsin S propeptide
-
-
-
chagasin mutant delta T31-T32
-
-
-
chagasin mutant P30A
-
-
-
chagasin mutant T31A
-
-
-
chagasin mutant T31A/T32A
-
-
-
chagasin mutant T31S
-
-
-
chagasin mutant T31V
-
-
-
chagasin mutant T31Y
-
-
-
chagasin mutant T32A
-
-
-
chagasin mutant T32S
-
-
-
chagasin mutant T32V
-
-
-
chagasin mutant T32Y
-
-
-
chagasin mutant W93A
-
-
-
Chloroquine
-
chloroquine inhibits the infection with live Nipah virus and Hendra virus at a concentration of 1 microM in vitro. The mechanism for the antiviral action likely is the inhibition of cathepsin L, which is essential for the processing of the viral fusion glycoprotein and the maturation of newly budding virions
CID 16725315
-
2% inhibition at 0.025 mM
CID 23631927
-
38% inhibition at 0.025 mM, sub-nanomolar slow-binding, reversible inhibitor of human cathepsin L with cathepsin L/B selectivity of above 700fold that blocks SARS-CoV and Ebola pseudotype virus entry in human cells
CLIK195
-
complete inhibition at 0.01 mM
cystatin
-
from chicken, activity with benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
-
diethyl-cyanamide
-
IC50 is above 0.1 mM
endopin 2
-
enodgenous inhibitor, present in pituitary gland
-
endopin 2C
-
endopin 2C inactivaties cathepsin L by binding to the enzyme, after dissociation from cathepsin L its activity is recovered within 60 min
-
fragment p41 of major histocompatibility complex class II-associated invariant chain
inhibitory to human cathepsin V, cathepsin L, cathepsin K, cathepsin F with Ki values in the low nanomolar range. Ki values are sufficiently low to ensure complex formation at physiological concentrations. Regulation of the proteolytic activity of most of the cysteine cathepsins by the p41 fragment is an important and widespread control mechanism of antigen presentation
-
glucose
-
high concentrations
JPM-565
-
cathepsin L irreversible binding
JPM-OEt
-
cathepsin L irreversible binding
LFLRL
-
0.05 mM, 78% inhibition
LFLTR-NH2
-
IC50: 0.0008 mM
LKFTR
-
0.05 mM, 78% inhibition
LKLFF
-
0.05 mM, 42% inhibition
LKLFW
-
0.05 mM, 22% inhibition
LKLLW
-
0.05 mM, 75% inhibition
LLFLW
-
0.05 mM, 52% inhibition
LLFRW
-
0.05 mM, 52% inhibition
LLLLR
-
0.05 mM, 62% inhibition
LLLLW
-
0.05 mM, 37% inhibition
LLLRW
-
0.05 mM, 83% inhibition
LLLTB
-
0.05 mM, 58% inhibition
LLLTL
-
0.05 mM, 67% inhibition
LLLTR-NH2
-
IC50: 0.0005 mM
LLLTW
-
0.05 mM, 62% inhibition
LLYLW
-
0.05 mM, 47% inhibition
LLYTB
-
0.05 mM, 25% inhibition
LLYTR
-
0.05 mM, 62% inhibition
LLYTW
-
0.05 mM, 30% inhibition
low-MW cysteine proteinase inhibitor
-
-
-
LRFTF
-
0.05 mM, 25% inhibition
LRLLW
-
0.05 mM, 73% inhibition
LWFFW
-
0.05 mM, 61% inhibition
LWFRQ
-
0.05 mM, 20% inhibition
LWFRW
-
0.05 mM, 20% inhibition
LWLFL
-
0.05 mM, 73% inhibition
LWLFW
-
0.05 mM, 31% inhibition
LWLLW
-
0.05 mM, 52% inhibition
methyl (13alpha,17alpha,20S,24Z)-3-hydroxylanosta-7,24-dien-26-oate
-
competitive inhibition
methyl (3Z,13alpha,17alpha,20S,24Z)-3-(hydroxyimino)lanosta-7,24-dien-26-oate
-
competitive inhibition
methyl 5-acetyloxy-dinaphtho[1,2-2'3']furan-7,12-dione-6-carboxylate
-
furanquinone from Paulownia tomentosa stem, inhibitory to both cathepsin L and cathepsin K
methyl 5-hydroxy-dinaphtho[1,2-2'3']furan-7,12-dione-6-carboxylate
-
furanquinone from Paulownia tomentosa stem, inhibitory to both cathepsin L and cathepsin K
N-(1-cyano-3-pyrrolidinyl)benzamide
-
IC50: 0.00175 mM
N-(1-cyano-3-pyrrolidinyl)benzenesulfonamide
-
IC50: 0.00008 mM
N-(1-cyano-3-pyrrolidinyl)[1,1'-biphenyl]-4-carboxamide
-
IC50: 0.00085 mM
N-(1-cyanopyrrolidin-3-yl)benzenesulfonamide
-
-
N-(2,6-dimethylbenzoyl)-L-phenylalanyl-L-lysinamide
-
-
N-(2-chloro-5-nitrobenzoyl)-L-phenylalanyl-L-lysinamide
-
-
N-(3-phenylpropanoyl)-L-phenylalanyl-L-lysinamide
-
-
N-(4-biphenylacetyl)-S-methylcysteine-(D)-Arg-Phe-beta-phenethylamide
-
also called Cat L inhibitor 7, specific inhibitor
N-(4-bromobenzoyl)-L-phenylalanyl-L-lysinamide
-
-
N-(4-[[2-cyano-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidin-6-yl]methoxy]phenyl)acetamide
-
pyrrolopyrimidine inhibitor by modification of the P3 moieties
N-(4-[[2-cyano-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidin-6-yl]methoxy]phenyl)propanamide
-
pyrrolopyrimidine inhibitor by modification of the P3 moieties
N-(biphenyl-4-ylcarbonyl)-L-phenylalanyl-L-lysinamide
-
-
N-(cyclopent-1-en-1-ylcarbonyl)-L-phenylalanyl-L-lysinamide
-
-
N-(naphthalen-2-ylcarbonyl)-L-phenylalanyl-L-lysinamide
-
-
N-(pentafluorobenzoyl)-L-phenylalanyl-L-lysinamide
-
-
N-(piperidin-2-ylcarbonyl)-L-phenylalanyl-L-lysinamide
-
-
N-(pyridin-2-ylcarbonyl)-L-phenylalanyl-L-lysinamide
-
-
N-benzyl-2-[bis(3-bromophenyl)methylidene]hydrazinecarbothioamide
-
-
N-benzyloxycarbonyl-Phe-Phe-fluoromethylketone
-
-
N-[(1-cyano-2-pyrrolidinyl)methyl]benzamide
-
IC50: 0.023 mM
N-[(1-cyano-2-pyrrolidinyl)methyl]benzenesulfonamide
-
IC50: 0.0115 mM
N-[(1-cyano-3-azetidinyl)methyl]benzamide
-
IC50: 0.00065 mM
N-[(1-cyano-3-azetidinyl)methyl]benzenesulfonamide
-
IC50: 0.00005 mM
N-[(1-cyano-3-azetidinyl)methyl]cyclohexanecarboxamide
-
IC50: 0.000006 mM
N-[(1-cyano-3-pyrrolidinyl)methyl]benzenesulfonamide
-
IC50: 0.00035 mM
N-[(2R)-2-[(2-amino-2-oxoethyl)amino]-2-[[(benzyloxy)carbonyl]amino]acetyl]-L-phenylalanyl-L-lysinamide
-
-
N-[(2R)-2-[(3-aminopropyl)amino]-2-[[(benzyloxy)carbonyl]amino]acetyl]-L-phenylalanyl-L-lysinamide
-
-
N-[(2R)-2-[[(benzyloxy)carbonyl]amino]-2-(3a,7a-dihydro-1H-indol-3-ylamino)acetyl]-L-phenylalanyl-L-lysinamide
-
-
N-[(2R)-2-[[(benzyloxy)carbonyl]amino]-2-(propan-2-ylamino)acetyl]-L-phenylalanyl-L-lysinamide
-
-
N-[(2R)-2-[[(benzyloxy)carbonyl]amino]-2-[(2-carbamimidamidoethyl)amino]acetyl]-L-phenylalanyl-L-lysinamide
-
-
N-[(2S)-1-(1H-indol-3-yl)-3-oxopropan-2-yl]-N2-(naphthalen-1-ylsulfonyl)-L-isoleucinamide
-
-
N-[(2S)-1-(3-chlorophenyl)-3-[(cyanomethyl)amino]but-3-en-2-yl]benzamide
-
-
N-[(2S)-3-(3-chlorophenyl)-1-[(cyanomethyl)amino]-1-oxopropan-2-yl]-1,3-dimethyl-1H-pyrazole-4-carboxamide
-
pH and temperature not specified in the publication
N-[(2S)-3-(3-chlorophenyl)-1-[(cyanomethyl)amino]-1-oxopropan-2-yl]-1,3-dimethyl-1H-pyrazole-5-carboxamide
-
pH and temperature not specified in the publication
N-[(2S)-3-(3-chlorophenyl)-1-[(cyanomethyl)amino]-1-oxopropan-2-yl]-1-methyl-3-(propan-2-yl)-1H-pyrazole-5-carboxamide
-
pH and temperature not specified in the publication
N-[(2S)-3-(3-chlorophenyl)-1-[(cyanomethyl)amino]-1-oxopropan-2-yl]-2,3-dimethylbenzamide
-
pH and temperature not specified in the publication
N-[(2S)-3-(3-chlorophenyl)-1-[(cyanomethyl)amino]-1-oxopropan-2-yl]-2,4-dimethyl-1,3-thiazole-5-carboxamide
-
pH and temperature not specified in the publication
N-[(2S)-3-(3-chlorophenyl)-1-[(cyanomethyl)amino]-1-oxopropan-2-yl]-2,5-dimethyl-1,3-oxazole-4-carboxamide
-
pH and temperature not specified in the publication
N-[(2S)-3-(3-chlorophenyl)-1-[(cyanomethyl)amino]-1-oxopropan-2-yl]-2,5-dimethylbenzamide
-
pH and temperature not specified in the publication
N-[(2S)-3-(3-chlorophenyl)-1-[(cyanomethyl)amino]-1-oxopropan-2-yl]-2,5-dimethylthiophene-3-carboxamide
-
pH and temperature not specified in the publication
N-[(2S)-3-(3-chlorophenyl)-1-[(cyanomethyl)amino]-1-oxopropan-2-yl]-2-methylbenzamide
-
pH and temperature not specified in the publication
N-[(2S)-3-(3-chlorophenyl)-1-[(cyanomethyl)amino]-1-oxopropan-2-yl]-3,5-dimethylbenzamide
-
pH and temperature not specified in the publication
N-[(2S)-3-(3-chlorophenyl)-1-[(cyanomethyl)amino]-1-oxopropan-2-yl]-3,7-dimethylnaphthalene-1-carboxamide
-
pH and temperature not specified in the publication
N-[(2S)-3-(3-chlorophenyl)-1-[(cyanomethyl)amino]-1-oxopropan-2-yl]-3-ethyl-1-methyl-1H-pyrazole-5-carboxamide
-
pH and temperature not specified in the publication
N-[(2S)-3-(3-chlorophenyl)-1-[(cyanomethyl)amino]-1-oxopropan-2-yl]-3-methylbenzamide
-
pH and temperature not specified in the publication
N-[(2S)-3-(3-chlorophenyl)-1-[(cyanomethyl)amino]-1-oxopropan-2-yl]-4-methylbenzamide
-
pH and temperature not specified in the publication
N-[(2S)-3-(3-chlorophenyl)-1-[(cyanomethyl)amino]-1-oxopropan-2-yl]-5,6,7,8-tetrahydronaphthalene-1-carboxamide
-
pH and temperature not specified in the publication
N-[(2S)-3-(3-chlorophenyl)-1-[(cyanomethyl)amino]-1-oxopropan-2-yl]benzamide
-
pH and temperature not specified in the publication
N-[(2S)-3-(3-chlorophenyl)-1-[(cyanomethyl)amino]-1-oxopropan-2-yl]cycloheptanecarboxamide
-
pH and temperature not specified in the publication
N-[(2S)-3-(3-chlorophenyl)-1-[(cyanomethyl)amino]-1-oxopropan-2-yl]cyclohex-1-ene-1-carboxamide
-
pH and temperature not specified in the publication
N-[(2S)-3-(3-chlorophenyl)-1-[(cyanomethyl)amino]-1-oxopropan-2-yl]cyclohexanecarboxamide
-
pH and temperature not specified in the publication
N-[(2S)-3-(3-chlorophenyl)-1-[(cyanomethyl)amino]-1-oxopropan-2-yl]naphthalene-1-carboxamide
-
pH and temperature not specified in the publication
N-[(2S)-3-(3-chlorophenyl)-1-[(cyanomethyl)amino]-1-oxopropan-2-yl]quinoline-4-carboxamide
-
pH and temperature not specified in the publication
N-[(2S)-4-methyl-1-oxo-1-[[(4S)-3-oxo-1-(pyridin-2-ylsulfonyl)azepan-4-yl]amino]pentan-2-yl]-1-benzofuran-2-carboxamide
-
-
N-[(4'-carboxy-2,2'-bipyridin-4-yl)carbonyl]-L-phenylalanyl-L-lysinamide
-
-
N-[(6-aminopyridin-3-yl)carbonyl]-L-phenylalanyl-L-lysinamide
-
-
N-[(benzyloxy)carbonyl]-3-(1H-indazol-1-yl)-L-alanyl-L-lysinamide
-
-
N-[(benzyloxy)carbonyl]-3-(1H-indol-1-yl)-L-alanyl-L-lysinamide
-
-
N-[(benzyloxy)carbonyl]-4-(thiophen-2-yl)-L-phenylalanyl-L-lysinamide
-
-
N-[(benzyloxy)carbonyl]-L-leucyl-N-[(3S)-7-amino-1-[(2,6-dimethylbenzoyl)oxy]-2-oxoheptan-3-yl]-L-phenylalaninamide
-
irreversible inhibitor
N-[(benzyloxy)carbonyl]-L-phenylalanyl-3-(1H-imidazol-1-yl)-L-alaninamide
-
-
N-[(benzyloxy)carbonyl]-L-phenylalanyl-4-amino-L-phenylalaninamide
-
-
N-[(benzyloxy)carbonyl]-L-phenylalanyl-6-hydroxy-L-lysinamide
-
-
N-[(benzyloxy)carbonyl]-L-phenylalanyl-L-alaninamide
-
-
N-[(benzyloxy)carbonyl]-L-phenylalanyl-L-argininamide
-
-
N-[(benzyloxy)carbonyl]-L-phenylalanyl-L-leucinamide
-
-
N-[(benzyloxy)carbonyl]-L-phenylalanyl-L-lysinamide
-
-
N-[(benzyloxy)carbonyl]-L-phenylalanyl-L-methioninamide
-
-
N-[(benzyloxy)carbonyl]-L-phenylalanyl-L-ornithinamide
-
-
N-[(benzyloxy)carbonyl]-L-phenylalanyl-L-valinamide
-
-
N-[(benzyloxy)carbonyl]-L-phenylalanyl-N6-methyl-L-lysinamide
-
-
N-[(benzyloxy)carbonyl]-L-tryptophyl-N-[(3S)-7-amino-1-[(2,6-dimethylbenzoyl)oxy]-2-oxoheptan-3-yl]-L-phenylalaninamide
-
irreversible inhibitor
N-[(benzyloxy)carbonyl]-L-tyrosyl-L-lysinamide
-
-
N-[3-(4-hydroxyphenyl)propanoyl]-L-phenylalanyl-L-lysinamide
-
-
N-[3-(acetyloxy)benzoyl]-L-phenylalanyl-L-lysinamide
-
-
N-[4-(acetyloxy)benzoyl]-L-phenylalanyl-L-lysinamide
-
-
N-[4-(dimethylamino)benzoyl]-L-phenylalanyl-L-lysinamide
-
-
N-[4-(trifluoromethyl)benzoyl]-L-phenylalanyl-L-lysinamide
-
-
N2-acetyl-L-arginyl-L-lysyl-L-leucyl-L-leucyl-L-tryptophanamide
-
potent inhibitor
N2-[(benzyloxy)carbonyl]-L-arginyl-N-[(3S)-7-amino-1-[(2,6-dimethylbenzoyl)oxy]-2-oxoheptan-3-yl]-L-phenylalaninamide
-
irreversible inhibitor
N2-[(benzyloxy)carbonyl]-L-ornithyl-N-[(3S)-7-amino-1-[(2,6-dimethylbenzoyl)oxy]-2-oxoheptan-3-yl]-L-phenylalaninamide
-
irreversible inhibitor
N2-[(benzyloxy)carbonyl]-N-[(3S)-1-cyanopyrrolidin-3-yl]-L-leucinamide
-
-
Nalpha-[(3-tert-butyl-1-methyl-1H-pyrazol-5-yl)carbonyl]-3-chloro-N-(cyanomethyl)-L-phenylalaninamide
-
pH and temperature not specified in the publication
Nalpha-[(3-tert-butyl-1-methyl-1H-pyrazol-5-yl)carbonyl]-N-(cyanomethyl)-3-methyl-L-phenylalaninamide
-
pH and temperature not specified in the publication
Nalpha-[(benzyloxy)carbonyl]-N-[(1R)-1,2-diamino-2-oxoethyl]-L-phenylalaninamide
-
-
naphthalene-2-carboxylic acid ((S)-2-naphthalen-2-yl-1-[(S)-3-oxo-1-(pyridine-2-sulfonyl)azepan-4-ylcarbamoyl]ethyl)amide
-
-
naphthoic-1-carboxylic acid ((S)-1-[3-oxo-1-(pyridine-2-sulfonyl)azepan-4-ylcarbamoyl]-3-methyl-butyl)amide
-
-
ortho-aminobenzoic acid-LFEKQ-N-[2,4-dinitrophenyl]ethylenediamine
-
-
ortho-aminobenzoic acid-VLFEKKQ-N-[2,4-dinitrophenyl]ethylenediamine
-
-
ortho-aminobenzoic acid-VLFEKKVYLQ-N-[2,4-dinitrophenyl]ethylenediamine
-
efficient cathepsin L inhibitor
ortho-aminobenzoic acid-VLFEKQ-N-[2,4-dinitrophenyl]ethylenediamine
-
-
P41icf
-
synthesis and NMR structure of the potent inhibitor
-
phenylmethanesulfonyl fluoride
-
-
Protein C inhibitor
-
inhibits cathepsin L with an inhibition rate (k2) of 30000 0 M-1 s-1
-
quinoline-2-carboxylic acid ((S)-1-[3-oxo-1-(pyridine-2-sulfonyl)azepan-4-ylcarbamoyl]-3-methyl-butyl)amide
-
-
quinoline-8-carboxylic acid ((S)-1-[3-oxo-1-(pyridine-2-sulfonyl)azepan-4-ylcarbamoyl]-3-methyl-butyl)amide
-
-
RFLRW
-
0.05 mM, 21% inhibition
RFLYR
-
0.05 mM, 64% inhibition
RKLFL
-
0.05 mM, 79% inhibition
RKLLW-NH2
-
IC50: 0.0006 mM
RKLWD-NH2
-
IC50: 0.014 mM
RKLWF
-
0.05 mM, 52% inhibition
RKLWL-NH2
-
IC50: 0.0008 mM
RKLWV
-
0.05 mM, 41% inhibition
RLLLW
-
0.05 mM, 75% inhibition
RLLYW
-
0.05 mM, 29% inhibition
RRFYV
-
0.05 mM, 24% inhibition
RRLTW
-
0.05 mM, 38% inhibition
RRYLB
-
0.05 mM, 33% inhibition
RWLTL
-
0.05 mM, 61% inhibition
RWLYL
-
0.05 mM, 65% inhibition
S-(2-oxo-1-phenylpyrrolidin-3-yl) 2-[(2S)-2-[(tert-butoxycarbonyl)amino]-3-(1H-indol-3-yl)propanoyl]hydrazinecarbothioate
-
-
S-[2-(3,4-dihydroquinolin-1(2H)-yl)-2-oxoethyl] 2-[(2S)-2-[(tert-butoxycarbonyl)amino]-3-(1H-indol-3-yl)propanoyl]hydrazinecarbothioate
-
-
S-[2-[(2-ethylphenyl)amino]-2-oxoethyl] 2-[(2S)-2-[(tert-butoxycarbonyl)amino]-3-(1H-indol-3-yl)propanoyl]hydrazinecarbothioate
S-[2-[(2-ethylphenyl)amino]-2-oxoethyl] 2-[(2S)-2-[(tert-butoxycarbonyl)amino]-3-phenylpropanoyl]hydrazinecarbothioate
-
-
serpin B3
-
about 35% inhibition at 7.5 nM, the presence of heparin accelerates inhibition of cathepsin L by serpin B3 (4.1fold increase in rate of inhibition)
-
serpin B4
-
about 70% inhibition at 100 nM, the presence of 50 nM heparin accelerates inhibition of cathepsin L by serpin B4 (4.1fold increase in rate of inhibition)
-
tert-butyloxycarbonyl-Lys(epsilon-9-fluorenylmethoxycarbonyl)-Leu-Tyr-CHN2
-
-
tert-butyloxycarbonyl-Lys-Leu-Tyr-CHN2
-
-
tert-butyloxycarbonyl-Val-Lys(epsilon-benzyloxycarbonyl)-Leu-Tyr-CHN2
-
-
testican-1
-
strong competitive inhibitor, inhibition is independent of its chondroitin sulfate chains and is effective at both pH 5.5 and pH 7.2, does not inhibit the structurally related lysosomal cysteine protease cathepsin B
-
Tg1 domain of testican-1
-
-
-
thyroglobulin type-1 domain
-
-
-
trans-epoxysuccinyl-L-leucylamido-(4-guanidino)butane
YFLLR
-
0.05 mM, 30% inhibition
YFLTF
-
0.05 mM, 29% inhibition
YKLLR
-
0.05 mM, 72% inhibition
YLLFW
-
0.05 mM, 37% inhibition
YLYLF
-
0.05 mM, 40% inhibition
YWFTF
-
0.05 mM, 43% inhibition
YWLLR
-
0.05 mM, 73% inhibition
YWYYL
-
0.05 mM, 20% inhibition
YYLLR
-
0.05 mM, 56% inhibition
CLIK-148
-
CLIK-148
cathepsin L-specific inhibitor
E-64
-
E-64
a broad-spectrum cysteine peptidase inhibitor
E-64
a pan cysteine cathepsin inhibitor
1-naphthalenesulfonyl-Ile-Trp-aldehyde
-
cathepsin L inhibitor
1-naphthalenesulfonyl-Ile-Trp-aldehyde
-
selective intra- and extracellular cathepsin L inhibitor
6-[[4-(4-acetylpiperazin-1-yl)phenoxy]methyl]-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
-
6-[[4-(4-acetylpiperazin-1-yl)phenoxy]methyl]-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P3 moieties
benzyloxycarbonyl-L-Phe-L-Phe-fluoromethylketone
-
-
benzyloxycarbonyl-L-Phe-L-Phe-fluoromethylketone
-
irreversible and selective inhibitor of cathepsin L
benzyloxycarbonyl-Phe-Tyr-(tert-butyl)-diazomethylketone
-
-
benzyloxycarbonyl-Phe-Tyr-(tert-butyl)-diazomethylketone
-
irreversible cathepsin L inhibitor
CLIK148
-
complete inhibition at 0.01 mM
CLIK148
-
cathepsin L-specific inhibitor
cystatin B
-
-
-
cystatin B
-
cystatin B (stefin B) plays an important role in regulating the proteolytic activity of cathepsin L in the nucleus by protecting the CUX1 transcription factor and probably other substrates from proteolytic cleavage by cathepsin L
-
E-64
-
-
E-64
-
irreversible inhibitor
E-64
-
activity with benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
E-64
-
broad-spectrum cathepsin inhibitor, cathepsin L irreversible binding
E-64
-
i.e. 1-[N-[(L-3-trans-carboxyoxirane-2-carbonyl)-L-leucyl]amino]-4-guanidinobutane
Ep-475
-
-
Ep-475
-
cathepsin L irreversible binding
LKFTF
-
0.05 mM, 32% inhibition
LKFTF
-
0.05 mM, 24% inhibition
S-[2-[(2-ethylphenyl)amino]-2-oxoethyl] 2-[(2S)-2-[(tert-butoxycarbonyl)amino]-3-(1H-indol-3-yl)propanoyl]hydrazinecarbothioate
-
-
S-[2-[(2-ethylphenyl)amino]-2-oxoethyl] 2-[(2S)-2-[(tert-butoxycarbonyl)amino]-3-(1H-indol-3-yl)propanoyl]hydrazinecarbothioate
-
slow binding and slowly reversible inhibitor. 7- to 151fold greater selectivity towards cathepsin L then papain and cathepsins B, K, V, and S with no activity against cathepsin G. Inhibitor lacks toxicitiy in human aortic endothelial cells and inhibits in vitro propagation of Plasmodium falciparum with an IC50 value of 15.4 microM and of Leishmania major with an IC50 value of 12.5 microM
S-[2-[(2-ethylphenyl)amino]-2-oxoethyl] 2-[(2S)-2-[(tert-butoxycarbonyl)amino]-3-(1H-indol-3-yl)propanoyl]hydrazinecarbothioate
-
CID16725315, slowly reversible inhibition
trans-epoxysuccinyl-L-leucylamido-(4-guanidino)butane
-
-
trans-epoxysuccinyl-L-leucylamido-(4-guanidino)butane
-
i.e. E-64, irreversible
additional information
development and synthesis of a clickable and tagless activity-based probes of cathepsin L, method, overview. The probe KDP-1 is highly efficient, active-site directed and activity-dependent, selective, cell penetrable, and non-toxic to human cells. Using a zebrafish model, it is schown that the probe can inhibit cathepsin L function in vivo during the hatching process. KDP-1 exhibits a strong time dependent inactivation of cathepsin L activity, although with about 10fold lower rate than KD-1
-
additional information
-
development and synthesis of a clickable and tagless activity-based probes of cathepsin L, method, overview. The probe KDP-1 is highly efficient, active-site directed and activity-dependent, selective, cell penetrable, and non-toxic to human cells. Using a zebrafish model, it is schown that the probe can inhibit cathepsin L function in vivo during the hatching process. KDP-1 exhibits a strong time dependent inactivation of cathepsin L activity, although with about 10fold lower rate than KD-1
-
additional information
endogenous cysteine peptidase inhibitors like stefin B act in safe-guarding mammalian cells by their presence in the cyto- or nucleoplasm, and thus protect from activities of proteolytic enzymes leaking into the cytoplasm upon, for instance, non-intended rupture of endolysosomes in pathological situations
-
additional information
no inhibition by EDTA, PMSF, and pepstatin A
-
additional information
-
no inhibition by EDTA, PMSF, and pepstatin A
-
additional information
screening and identification of inhibitors of Trypanosoma brucei cathepsin L with antitrypanosomal activity, overview
-
additional information
-
screening and identification of inhibitors of Trypanosoma brucei cathepsin L with antitrypanosomal activity, overview
-
additional information
synthesis and biochemical evaluation of benzoylbenzophenone thiosemicarbazone analogues as potent and selective inhibitors of cathepsin L, molecular modeling, overview
-
additional information
-
synthesis and biochemical evaluation of benzoylbenzophenone thiosemicarbazone analogues as potent and selective inhibitors of cathepsin L, molecular modeling, overview
-
additional information
-
MHC class II-associated invariant chain fragment from human kidney that has inhibitory effect on the enzyme
-
additional information
-
no inhibition with 0.14 mM (2R,3R)-diethyl-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(S)-prolyl]aziridine-2,3-dicarboxylate, (2R,3R)-diethyl-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(R)-nipecotyl]aziridine-2,3-dicarboxylate, (2R,3R)-diethyl-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(S)-nipecotyl]aziridine-2,3-dicarboxylate, (2R,3R)-diethyl-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(R)-azetidine-2-carbonyl]aziridine-2,3-dicarboxylate, or (2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(S)-prolyl]-aziridine-2,3-dicarboxylate
-
additional information
-
heparin cofactor II and plasminogen activator inhibitor 1 do not inhibit cathepsin L
-
additional information
-
histones do not inhibit cathepsin L activity even at a 100fold molar excess (0.00215 mM histone concentration)
-
additional information
-
native cathepsin L was completely inhibited by 0.001, 0.004, or 0.01 mM cathepsin L propeptide (10 min, pH 6.5, room temperature)
-
additional information
-
not inhibited by N-(L-3-trans-(propylcarbamoyl)oxilane-2-carbonyl)-L-isoluecyl-L-proline (CA-074)
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Abortion, Spontaneous
[Expression of cathepsins B and L in early gestational decidua and chorionic villi]
Acute Coronary Syndrome
Plasma cathepsin L and its related pro/antiangiogenic factors play useful roles in predicting rich coronary collaterals in patients with coronary heart disease.
Acute Coronary Syndrome
Serum and saliva levels of cathepsin L in patients with acute coronary syndrome.
Acute Coronary Syndrome
Usefulness of serum cathepsin L as an independent biomarker in patients with coronary heart disease.
Adenocarcinoma
Assessment of cathepsin L activity by use of the inhibitor CA-074 compared to cathepsin B activity in human lung tumor tissue.
Adenocarcinoma
Cloning, genomic organization, and chromosomal localization of human cathepsin L.
Adenocarcinoma
Expression of cathepsin L in normal endometrium and endometrial cancer.
Adenocarcinoma
Expression, proliferation activity and clinical significance of cathepsin B and cathepsin L in operated lung cancer.
Adenocarcinoma
Prognostic impact of cysteine proteases cathepsin B and cathepsin L in pancreatic adenocarcinoma.
Adenocarcinoma
ras mutation and expression of the ras-regulated genes osteopontin and cathepsin L in human esophageal cancer.
Adenocarcinoma of Lung
Alterations in cathepsin L expression in lung cancers.
Adenocarcinoma of Lung
Cysteine proteases and cysteine protease inhibitors in non-small cell lung cancer.
Albuminuria
Urinary cathepsin L is predictive of changes in albuminuria and correlates with glucosepane in patients with type 2 diabetes in a closed-cohort study.
Alopecia
The human cysteine protease cathepsin V can compensate for murine cathepsin L in mouse epidermis and hair follicles.
Alzheimer Disease
Abeta-mediated activation of the apoptotic cascade in cultured cortical neurones: a role for cathepsin-L.
Alzheimer Disease
Cysteine Cathepsins in the secretory vesicle produce active peptides: Cathepsin L generates peptide neurotransmitters and cathepsin B produces beta-amyloid of Alzheimer's disease.
Alzheimer Disease
PLA2G4A/cPLA2-mediated lysosomal membrane damage leads to inhibition of autophagy and neurodegeneration after brain trauma.
Alzheimer Disease
Restoration of CTSD (cathepsin D) and lysosomal function in stroke is neuroprotective.
Amyloidosis
Cathepsin protease activity modulates amyloid load in extracerebral amyloidosis.
Amyloidosis
Proteolysis of serum amyloid A and AA amyloid proteins by cysteine proteases: cathepsin B generates AA amyloid proteins and cathepsin L may prevent their formation.
Amyotrophic Lateral Sclerosis
Restoration of CTSD (cathepsin D) and lysosomal function in stroke is neuroprotective.
Aneurysm
Activity of enzymes with different subcellular localization in the blood plasma of patients with aortic aneurysm.
Aneurysm
Cathepsin D and cathepsin L activities in aortic aneurysm wall and parietal thrombus.
Aneurysm
Differential expression of genes in elastase-induced saccular aneurysms with high and low aspect ratios.
Angina, Stable
Usefulness of serum cathepsin L as an independent biomarker in patients with coronary heart disease.
Angina, Unstable
Usefulness of serum cathepsin L as an independent biomarker in patients with coronary heart disease.
Aortic Aneurysm
Cathepsin D and cathepsin L activities in aortic aneurysm wall and parietal thrombus.
Aortic Aneurysm
Expression levels of cathepsin L and cystatin C in a hyperglycemic environment were associated with aortic aneurysm development in a mouse model.
Aortic Aneurysm, Abdominal
Cathepsin L Activity Is Essential to Elastase Perfusion-Induced Abdominal Aortic Aneurysms in Mice.
Aortic Aneurysm, Abdominal
Cathepsin L expression and regulation in human abdominal aortic aneurysm, atherosclerosis, and vascular cells.
Arteriosclerosis
Effects of intermittent exercise on biomarkers of cardiovascular risk in night shift workers.
Arthritis
Caught in the act: the crystal structure of cleaved cathepsin L bound to the active site of Cathepsin L.
Arthritis
Collagenase, cathepsin B and cathepsin L gene expression in the synovial membrane of patients with early inflammatory arthritis.
Arthritis
Contribution of cathepsin L to secretome composition and cleavage pattern of mouse embryonic fibroblasts.
Arthritis
Elevation of cathepsin L levels in the synovial lining of rabbits with antigen-induced arthritis.
Arthritis
Mode of activation of the precursor to cathepsin L: implication for matrix degradation in arthritis.
Arthritis, Experimental
Purification and characterization of collagenolytic property of renal cathepsin L from arthritic rat.
Arthritis, Rheumatoid
Cathepsin S and cathepsin L in serum and synovial fluid in rheumatoid arthritis with and without autoantibodies.
Arthritis, Rheumatoid
Cathepsins B and L in synovial fluids from patients with rheumatoid arthritis and the effect of cathepsin B on the activation of pro-urokinase.
Arthritis, Rheumatoid
Comparative analysis of cathepsin L, cathepsin D, and collagenase messenger RNA expression in synovial tissues of patients with rheumatoid arthritis and osteoarthritis, by in situ hybridization.
Arthritis, Rheumatoid
Cysteine and serine proteases of synovial tissue in rheumatoid arthritis and osteoarthritis.
Arthritis, Rheumatoid
Decreased arthritis severity in cathepsin L-deficient mice is attributed to an impaired T helper cell compartment.
Arthritis, Rheumatoid
Expression of the collagenolytic and Ras-induced cysteine proteinase cathepsin L and proliferation-associated oncogenes in synovial cells of MRL/I mice and patients with rheumatoid arthritis.
Arthritis, Rheumatoid
Macrophage cathepsin L, a factor in the erosion of subchondral bone in rheumatoid arthritis.
Arthritis, Rheumatoid
Measurement of elastase and cysteine proteinases in synovial fluid of patients with rheumatoid arthritis, sero-negative spondylarthropathies, and osteoarthritis.
Arthritis, Rheumatoid
Structural basis for reversible and irreversible inhibition of human cathepsin L by their respective dipeptidyl glyoxal and diazomethylketone inhibitors.
Arthritis, Rheumatoid
Targeting cathepsin L (CL) by specific ribozymes decreases CL protein synthesis and cartilage destruction in rheumatoid arthritis.
Astrocytoma
Cathepsin L silencing increases As2O3 toxicity in malignantly transformed pilocytic astrocytoma MPA58 cells by activating caspases 3/7.
Astrocytoma
Expression and immunohistochemical localization of cathepsin L during the progression of human gliomas.
Astrocytoma
Lysosomal enzymes, cathepsins in brain tumour invasion.
Atherosclerosis
Cathepsin L deficiency reduces diet-induced atherosclerosis in low-density lipoprotein receptor-knockout mice.
Atherosclerosis
Cathepsin L expression and regulation in human abdominal aortic aneurysm, atherosclerosis, and vascular cells.
Atherosclerosis
Cathepsin L is significantly associated with apoptosis and plaque destabilization in human atherosclerosis.
Atherosclerosis
Cathepsin L stimulates autophagy and inhibits apoptosis of ox-LDL-induced endothelial cells: potential role in atherosclerosis.
Atherosclerosis
Modulation of Cathepsin L Expression in the Coronary Arteries of Atherosclerotic Swine.
Atherosclerosis
Overexpression of transferrin receptor and ferritin related to clinical symptoms and destabilization of human carotid plaques.
Atherosclerosis
Peroxisome Proliferator-activated Receptor {gamma} Induces Apoptosis and Inhibits Autophagy of Human Monocyte-derived Macrophages via Induction of Cathepsin L: POTENTIAL ROLE IN ATHEROSCLEROSIS.
Atherosclerosis
The association between serum cathepsin L and mortality in older adults.
Bacteremia
Phage lytic enzyme Cpl-1 as a novel antimicrobial for pneumococcal bacteremia.
Bacteremia
Systemic use of the endolysin Cpl-1 rescues mice with fatal pneumococcal pneumonia.
Bacterial Infections
Identification, mRNA expression profiling and activity characterization of cathepsin L from red drum (Sciaenops ocellatus).
Bacterial Infections
Immunodiagnostic/protective role of Cathepsin L cysteine proteinases secreted by Fasciola species.
Bacterial Infections
Macrobrachium rosenbergii cathepsin L: Molecular characterization and gene expression in response to viral and bacterial infections.
Bone Diseases
Cathepsin L in metastatic bone disease: therapeutic implications.
Bone Diseases, Metabolic
Soluble cathepsin-L: a marker of bone resorption and bone density?
Bone Resorption
An ultrastructural evaluation of the effects of cysteine-proteinase inhibitors on osteoclastic resorptive functions.
Bone Resorption
Cathepsin B and L activities in isolated osteoclasts.
Bone Resorption
Conditioned medium from ras oncogene-transformed NIH 3T3 cells induces bone resorption in vitro.
Bone Resorption
Distinct roles of cathepsin K and cathepsin L in osteoclastic bone resorption.
Bone Resorption
Effects of an inhibitor of cathepsin L on bone resorption in thyroparathyroidectomized and ovariectomized rats.
Bone Resorption
Effects of rat fetuin on stimulation of bone resorption in the presence of parathyroid hormone.
Bone Resorption
Immunohistochemical localization of cathepsins B, D and L in the rat osteoclast.
Bone Resorption
Localization of rat cathepsin K in osteoclasts and resorption pits: inhibition of bone resorption and cathepsin K-activity by peptidyl vinyl sulfones.
Bone Resorption
Participation of cathepsin L on bone resorption.
Bone Resorption
Potent and selective cathepsin L inhibitors do not inhibit human osteoclast resorption in vitro.
Bone Resorption
Regulation of collagenolytic cysteine protease synthesis by estrogen in osteoclasts.
Bone Resorption
Soluble cathepsin-L: a marker of bone resorption and bone density?
Bone Resorption
Structural basis for reversible and irreversible inhibition of human cathepsin L by their respective dipeptidyl glyoxal and diazomethylketone inhibitors.
Bone Resorption
Study of the functional share of lysosomal cathepsins by the development of specific inhibitors.
Bone Resorption
Synthesis of peptide aldehyde derivatives as selective inhibitors of human cathepsin L and their inhibitory effect on bone resorption.
Bone Resorption
The mechanisms and regulation of procathepsin L secretion from osteoclasts in bone resorption.
Brain Injuries, Traumatic
PLA2G4A/cPLA2-mediated lysosomal membrane damage leads to inhibition of autophagy and neurodegeneration after brain trauma.
Brain Injuries, Traumatic
The neuroprotective effect of acute moderate alcohol consumption on caspase-3 mediated neuroapoptosis in traumatic brain injury: the role of lysosomal cathepsin L and nitric oxide.
Brain Ischemia
Cathepsin L acutely alters microvessel integrity within the neurovascular unit during focal cerebral ischemia.
Brain Neoplasms
Cathepsin L affects apoptosis of glioblastoma cells: a potential implication in the design of cancer therapeutics.
Brain Neoplasms
Expression and immunohistochemical localization of cathepsin L during the progression of human gliomas.
Brain Neoplasms
Selective suppression of cathepsin L by antisense cDNA impairs human brain tumor cell invasion in vitro and promotes apoptosis.
Brain Neoplasms
[Cathepsin L from human brain tumor. Purification and contents]
Breast Neoplasms
An Active 32-kDa Cathepsin L Is Secreted Directly from HT 1080 Fibrosarcoma Cells and Not via Lysosomal Exocytosis.
Breast Neoplasms
Association of Epithelial Mesenchymal Transition with prostate and breast health disparities.
Breast Neoplasms
Bortezomib blocks the catabolic process of autophagy via a cathepsin-dependent mechanism, affects endoplasmic reticulum stress and induces caspase-dependent cell death in antiestrogen-sensitive and resistant ER+ breast cancer cells.
Breast Neoplasms
Cathepsin B, a prognostic indicator in lymph node-negative breast carcinoma patients: comparison with cathepsin D, cathepsin L, and other clinical indicators.
Breast Neoplasms
Cathepsin L inhibition by the small molecule KGP94 suppresses tumor microenvironment enhanced metastasis associated cell functions of prostate and breast cancer cells.
Breast Neoplasms
Cathepsin L interacts with CDK2-AP1 as a potential predictor of prognosis in patients with breast cancer.
Breast Neoplasms
Cathepsin L secretion by host and neoplastic cells potentiates invasion.
Breast Neoplasms
Cathepsin L splice variants in human breast cell lines.
Breast Neoplasms
CCAAT-displacement protein/cut homeobox transcription factor (CUX1) represses estrogen receptor-alpha (ER-?) in triple-negative breast cancer cells and can be antagonized by muscadine grape skin extract (MSKE).
Breast Neoplasms
Clinical Impact of Cystatin C/Cathepsin L and Follistatin/Activin A Systems in Breast Cancer Progression: A Preliminary Report.
Breast Neoplasms
Comparison of potential biological markers cathepsin B, cathepsin L, stefin A and stefin B with urokinase and plasminogen activator inhibitor-1 and clinicopathological data of breast carcinoma patients.
Breast Neoplasms
Correction for Burton et al., "Targeting the Nuclear Cathepsin L CCAAT Displacement Protein/Cut Homeobox Transcription Factor-Epithelial Mesenchymal Transition Pathway in Prostate and Breast Cancer Cells with the Z-FY-CHO Inhibitor".
Breast Neoplasms
Cystatins and cathepsins in breast carcinoma.
Breast Neoplasms
Development of a highly potent, selective, and cell-active inhibitor of cysteine cathepsin L-A hybrid design approach.
Breast Neoplasms
Differential cathepsin responses to inhibitor-induced feedback: E-64 and cystatin C elevate active cathepsin S and suppress active cathepsin L in breast cancer cells.
Breast Neoplasms
Discovery of a novel and selective cathepsin L inhibitor with anti-metastatic ability in vitro and in vivo against breast cancer cells.
Breast Neoplasms
Effects of Vacuolar H(+)-ATPase Inhibition on Activation of Cathepsin B and Cathepsin L Secreted from MDA-MB231 Breast Cancer Cells.
Breast Neoplasms
Expression of cysteine peptidase cathepsin L and its inhibitors stefins A and B in relation to tumorigenicity of breast cancer cell lines.
Breast Neoplasms
Identification of low-risk node-negative breast cancer patients by tumor biological factors PAI-1 and cathepsin L.
Breast Neoplasms
Initial evaluation of the antitumour activity of KGP94, a functionalized benzophenone thiosemicarbazone inhibitor of cathepsin L.
Breast Neoplasms
Novel roles of 1?,25(OH)2D3 on DNA repair provide new strategies for breast cancer treatment.
Breast Neoplasms
Prognostic significance of cathepsins B and L in primary human breast cancer.
Breast Neoplasms
Prognostic value of the cysteine proteases cathepsins B and cathepsin L in human breast cancer.
Breast Neoplasms
Protein C inhibitor regulates both cathepsin L activity and cell-mediated tumor cell migration.
Breast Neoplasms
Selective imaging of cathepsin L in breast cancer by fluorescent activity-based probes.
Breast Neoplasms
Snail transcription factor NLS and importin ?1 regulate the subcellular localization of Cathepsin L and Cux1.
Breast Neoplasms
Stefins and lysosomal cathepsins B, L and D in human breast carcinoma.
Breast Neoplasms
Stress-resistant Translation of Cathepsin L mRNA in Breast Cancer Progression.
Breast Neoplasms
Targeting the Nuclear Cathepsin L CCAAT Displacement Protein/Cut Homeobox Transcription Factor-Epithelial Mesenchymal Transition Pathway in Prostate and Breast Cancer Cells with the Z-FY-CHO Inhibitor.
Caliciviridae Infections
Endosomal acidification and cathepsin L activity is required for calicivirus replication.
Carcinogenesis
Alterations in cathepsin L expression in lung cancers.
Carcinogenesis
Cathepsin L interacts with CDK2-AP1 as a potential predictor of prognosis in patients with breast cancer.
Carcinogenesis
Cathepsin L suppression increases the radiosensitivity of human glioma U251 cells via G2/M cell cycle arrest and DNA damage.
Carcinogenesis
Cathepsin L-induced galectin-1 may act as a proangiogenic factor in the metastasis of high-grade serous carcinoma.
Carcinogenesis
Deficiency for the cysteine protease cathepsin L impairs Myc-induced tumorigenesis in a mouse model of pancreatic neuroendocrine cancer.
Carcinogenesis
Deficiency for the cysteine protease cathepsin L promotes tumor progression in mouse epidermis.
Carcinogenesis
Differential Impact of Cysteine Cathepsins on Genetic Mouse Models of De novo Carcinogenesis: Cathepsin B as Emerging Therapeutic Target.
Carcinogenesis
Expression of cathepsin L in normal endometrium and endometrial cancer.
Carcinogenesis
Expression of the human Cathepsin L inhibitor hurpin in mice: skin alterations and increased carcinogenesis.
Carcinogenesis
Induction of putative tumor-suppressing genes in Rat-1 fibroblasts by oncogenic Raf-1 as evidenced by robot-assisted complex hybridization.
Carcinogenesis
Mitochondria-to-nucleus stress signaling in mammalian cells: nature of nuclear gene targets, transcription regulation, and induced resistance to apoptosis.
Carcinogenesis
Nuclear cathepsin L activity is required for cell cycle progression of colorectal carcinoma cells.
Carcinogenesis
Protective role of cathepsin L in mouse skin carcinogenesis.
Carcinogenesis
Selective imaging of cathepsin L in breast cancer by fluorescent activity-based probes.
Carcinogenesis
Wild type p53-dependent transcriptional upregulation of cathepsin L expression is mediated by C/EBPα in human glioblastoma cells.
Carcinoma
Activities of serum cathepsin (B, H and L) and metalloproteinase (MMP7-ase) in patients with gastrointestinal and bronchial malignant tumours.
Carcinoma
An examination of the effects of hypoxia, acidosis, and glucose starvation on the expression of metastasis-associated genes in murine tumor cells.
Carcinoma
Assessment of cathepsin L activity by use of the inhibitor CA-074 compared to cathepsin B activity in human lung tumor tissue.
Carcinoma
Cathepsin L is associated with proliferation and clinical outcome of urothelial carcinoma of the bladder.
Carcinoma
Characterization of a cathepsin L-like enzyme secreted from human pancreatic cancer cell line HPC-YP.
Carcinoma
Concentrations of lysosomal cysteine proteases are decreased in renal cell carcinoma compared with normal kidney.
Carcinoma
Cystatin E/M Suppresses Tumor Cell Growth through Cytoplasmic Retention of NF-?B.
Carcinoma
Cystatins and cathepsins in breast carcinoma.
Carcinoma
Cysteine protease activities and tumor development in human colorectal carcinoma.
Carcinoma
Cysteine proteases and cysteine protease inhibitors in non-small cell lung cancer.
Carcinoma
Downregulation of cathepsin L suppresses cancer invasion and migration by inhibiting transforming growth factor???mediated epithelial?mesenchymal transition.
Carcinoma
Electrophoretic analysis of the "cross-class" interaction between novel inhibitory serpin, squamous cell carcinoma antigen-1 and cysteine proteinases.
Carcinoma
Expression of cathepsin L and its inhibitor hurpin in inflammatory and neoplastic skin diseases.
Carcinoma
Expression of cathepsin L in human tumors.
Carcinoma
Expression of cathepsin L in normal endometrium and endometrial cancer.
Carcinoma
Expression profiling of supraglottic carcinoma: PTEN and thrombospondin 2 are associated with inhibition of lymphatic metastasis.
Carcinoma
Functional consequences of cathepsin L deficiency in human lung epithelial cells.
Carcinoma
Immunohistochemical localization of cathepsin L and cystatin A in normal skin and skin tumors.
Carcinoma
Increase of endo-peptidases and exo-peptidases in thyroid-tumors.
Carcinoma
Inhibition of carcinoma cell invasion and liver metastases formation by the cysteine proteinase inhibitor E-64.
Carcinoma
Presence of activated ras correlates with increased cysteine proteinase activities in human colorectal carcinomas.
Carcinoma
Prognostic value of cathepsin L and its inhibitor headpin in oral squamous cell carcinoma.
Carcinoma
Prognostic value of cathepsins B, H, L, D and their endogenous inhibitors stefins A and B in head and neck carcinoma.
Carcinoma
Quantitative analysis of cathepsin L mRNA and protein expression during oral cancer progression.
Carcinoma
Role of urinary cathepsin B and L in the detection of bladder urothelial cell carcinoma.
Carcinoma
Significance and prognostic value of lysosomal enzyme activities measured in surgically operated adenocarcinomas of the gastroesophageal junction and squamous cell carcinomas of the lower third of esophagus.
Carcinoma
Squamous cell carcinoma antigen is a potent inhibitor of cysteine proteinase cathepsin L.
Carcinoma
The application value of the detection of the level of tissue polypeptide antigen, ovarian cancer antigen X1, cathepsin L and CA125 on the diagnosis of epithelial ovarian cancer.
Carcinoma
The expression of Cathepsin L in oral lichen planus.
Carcinoma
[Relationship between cathepsin L and invasion and metastasis of ovarian carcinoma cells.]
Carcinoma in Situ
Cystatin E/M Suppresses Tumor Cell Growth through Cytoplasmic Retention of NF-?B.
Carcinoma, Basal Cell
Expression of cathepsin L and its inhibitor hurpin in inflammatory and neoplastic skin diseases.
Carcinoma, Hepatocellular
Cloning, genomic organization, and chromosomal localization of human cathepsin L.
Carcinoma, Hepatocellular
Increased expression of cathepsin L: a novel independent prognostic marker of worse outcome in hepatocellular carcinoma patients.
Carcinoma, Lewis Lung
Inhibition of carcinoma cell invasion and liver metastases formation by the cysteine proteinase inhibitor E-64.
Carcinoma, Non-Small-Cell Lung
Expression, proliferation activity and clinical significance of cathepsin B and cathepsin L in operated lung cancer.
Carcinoma, Non-Small-Cell Lung
Loss of the endothelial glycocalyx is associated with increased E-selectin mediated adhesion of lung tumour cells to the brain microvascular endothelium.
Carcinoma, Non-Small-Cell Lung
Overexpression of Cathepsin L is associated with gefitinib resistance in non-small cell lung cancer.
Carcinoma, Non-Small-Cell Lung
Secretion of a latent, acid activatable cathepsin L precursor by human non-small cell lung cancer cell lines.
Carcinoma, Ovarian Epithelial
Overexpression of Cathepsin L is associated with chemoresistance and invasion of epithelial ovarian cancer.
Carcinoma, Ovarian Epithelial
The application value of the detection of the level of tissue polypeptide antigen, ovarian cancer antigen X1, cathepsin L and CA125 on the diagnosis of epithelial ovarian cancer.
Carcinoma, Ovarian Epithelial
The Potential Role of the Proteases Cathepsin D and Cathepsin L in the Progression and Metastasis of Epithelial Ovarian Cancer.
Carcinoma, Renal Cell
"Disrupted in renal carcinoma 2" (DIRC2) - a novel transporter of the lysosomal membrane - is proteolytically processed by cathepsin L.
Carcinoma, Renal Cell
Concentrations of lysosomal cysteine proteases are decreased in renal cell carcinoma compared with normal kidney.
Carcinoma, Squamous Cell
An examination of the effects of hypoxia, acidosis, and glucose starvation on the expression of metastasis-associated genes in murine tumor cells.
Carcinoma, Squamous Cell
Assessment of cathepsin L activity by use of the inhibitor CA-074 compared to cathepsin B activity in human lung tumor tissue.
Carcinoma, Squamous Cell
Electrophoretic analysis of the "cross-class" interaction between novel inhibitory serpin, squamous cell carcinoma antigen-1 and cysteine proteinases.
Carcinoma, Squamous Cell
Expression of cathepsin L and its inhibitor hurpin in inflammatory and neoplastic skin diseases.
Carcinoma, Squamous Cell
Immunohistochemical localization of cathepsin L and cystatin A in normal skin and skin tumors.
Carcinoma, Squamous Cell
Significance and prognostic value of lysosomal enzyme activities measured in surgically operated adenocarcinomas of the gastroesophageal junction and squamous cell carcinomas of the lower third of esophagus.
Carcinoma, Squamous Cell
Squamous cell carcinoma antigen is a potent inhibitor of cysteine proteinase cathepsin L.
Cardiac Output, Low
Ultrastructural changes in myocardial cells of rats fed a low protein diet.
Cardiomegaly
Cathepsin B deficiency attenuates cardiac remodeling in response to pressure overload via TNF?/ASK1/JNK pathway.
Cardiomegaly
Cathepsin-L ameliorates cardiac hypertrophy through activation of the autophagy-lysosomal dependent protein processing pathways.
Cardiomegaly
Lysosomal cysteine peptidase cathepsin L protects against cardiac hypertrophy through blocking AKT/GSK3beta signaling.
Cardiomyopathies
Lysosomal, cytoskeletal, and metabolic alterations in cardiomyopathy of cathepsin L knockout mice.
Cardiomyopathies
Microarray Analysis of Polychlorinated Biphenyl Mixture-Induced Changes in Gene Expression among Atlantic Tomcod Populations Displaying Differential Sensitivity to Halogenated Aromatic Hydrocarbons.
Cardiomyopathies
Microarray analysis of polychlorinated biphenyl mixture-induced changes in gene expression among atlantic tomcod populations displaying differential sensitivity to halogenated aromatic hydrocarbons.
Cardiomyopathy, Dilated
Cell type-specific functions of the lysosomal protease cathepsin L in the heart.
Cardiomyopathy, Dilated
Clinical significance of cathepsin L and cathepsin B in dilated cardiomyopathy.
Cardiomyopathy, Dilated
Dilated cardiomyopathy in mice deficient for the lysosomal cysteine peptidase cathepsin L.
Cardiomyopathy, Dilated
Lysosomal, cytoskeletal, and metabolic alterations in cardiomyopathy of cathepsin L knockout mice.
Cardiomyopathy, Dilated
[The expression and significance of myocardial cathepsin L in dilated cardiomyopathy]
Cardiovascular Diseases
Caspase-3 activation triggers extracellular cathepsin L release and endorepellin proteolysis.
Cardiovascular Diseases
Cystatin B, cathepsin L and D related to surrogate markers for cardiovascular disease in children.
Cardiovascular Diseases
Protein C inhibitor regulates both cathepsin L activity and cell-mediated tumor cell migration.
Cardiovascular Diseases
The association between serum cathepsin L and mortality in older adults.
Carotid Artery Injuries
Cathepsin L promotes Vascular Intimal Hyperplasia after Arterial Injury.
Carotid Artery Injuries
OS 02-05 MYD88 ON MACROPHAGE TRIGGERS CATHEPSIN L ACTIVATION DRIVEN VASCULAR INTIMAL HYPERPLASIA.
cathepsin k deficiency
Thyroid functions of mouse cathepsins B, K, and L.
cathepsin l deficiency
Cathepsin K activity-dependent regulation of osteoclast actin ring formation and bone resorption.
cathepsin l deficiency
Cathepsin L deficiency as molecular defect of furless: hyperproliferation of keratinocytes and pertubation of hair follicle cycling.
cathepsin l deficiency
Cathepsin L deficiency reduces diet-induced atherosclerosis in low-density lipoprotein receptor-knockout mice.
cathepsin l deficiency
Cathepsin L deficiency results in reactive oxygen species (ROS) accumulation and vascular cells activation.
cathepsin l deficiency
Cathepsin-L, a key molecule in the pathogenesis of drug-induced and I-cell disease-mediated gingival overgrowth: a study with cathepsin-L-deficient mice.
cathepsin l deficiency
Contribution of cathepsin L to secretome composition and cleavage pattern of mouse embryonic fibroblasts.
cathepsin l deficiency
Epidermal differentiation: the role of proteases and their inhibitors.
cathepsin l deficiency
Functional consequences of cathepsin L deficiency in human lung epithelial cells.
cathepsin l deficiency
Impaired turnover of autophagolysosomes in cathepsin L deficiency.
cathepsin l deficiency
Out-of-frame start codons prevent translation of truncated nucleo-cytosolic cathepsin L in vivo.
cathepsin s deficiency
Deficiency of cathepsin S attenuates angiotensin II-induced abdominal aortic aneurysm formation in apolipoprotein E-deficient mice.
Chagas Disease
Characterisation of Trypanosoma cruzi populations by DNA polymorphism of the cruzipain gene detected by single-stranded DNA conformation polymorphism (SSCP) and direct sequencing.
Chagas Disease
Cysteine protease isoforms from Trypanosoma cruzi, cruzipain 2 and cruzain, present different substrate preference and susceptibility to inhibitors.
Chagas Disease
Non-peptidic Cruzain Inhibitors with Trypanocidal Activity Discovered by Virtual Screening and In Vitro Assay.
Cholesteatoma
Cathepsin L activity and its inhibitor in human otitis media.
Choroidal Neovascularization
Cathepsin L in bone marrow-derived cells is required for retinal and choroidal neovascularization.
Clonorchiasis
Molecular cloning and analysis of stage and tissue-specific expression of Cathepsin L-like protease from Clonorchis sinensis.
Clonorchiasis
Serological diagnosis of clonorchiasis: using a recombinant propeptide of cathepsin L proteinase from Clonorchis sinensis as a candidate antigen.
Clostridium Infections
Immunization of hamsters against Clostridium difficile infection using the Cwp84 protease as an antigen.
Coinfection
Immuno-diagnosis of bubaline fasciolosis with Fasciola gigantica cathepsin-L and recombinant cathepsin L 1-D proteases.
Colonic Neoplasms
[Protease activities in gastric and colon cancer tissues]
Colorectal Neoplasms
Cathepsin L is highly expressed in gastrointestinal stromal tumors.
Colorectal Neoplasms
Construction of a plasmid coding for green fluorescent protein tagged cathepsin L and data on expression in colorectal carcinoma cells.
Colorectal Neoplasms
Levels of serum cathepsin L and several glycosidases in patients operated for colorectal cancer.
Colorectal Neoplasms
Localization of nuclear cathepsin L and its association with disease progression and poor outcome in colorectal cancer.
Colorectal Neoplasms
Nuclear cathepsin L activity is required for cell cycle progression of colorectal carcinoma cells.
Colorectal Neoplasms
Presence of activated ras correlates with increased cysteine proteinase activities in human colorectal carcinomas.
Colorectal Neoplasms
The role of cysteine and serine proteases in colorectal carcinoma.
Colorectal Neoplasms
Tumor marker utility and prognostic relevance of cathepsin B, cathepsin L, urokinase-type plasminogen activator, plasminogen activator inhibitor type-1, CEA and CA 19-9 in colorectal cancer.
Common Cold
Clinical Isolates of Human Coronavirus 229E Bypass the Endosome for Cell Entry.
Coronary Artery Disease
Cathepsin L is significantly associated with apoptosis and plaque destabilization in human atherosclerosis.
Coronary Artery Disease
Increased Circulating Cathepsin L in Patients with Coronary Artery Disease.
Coronary Disease
Plasma cathepsin L and its related pro/antiangiogenic factors play useful roles in predicting rich coronary collaterals in patients with coronary heart disease.
Coronary Disease
Usefulness of serum cathepsin L as an independent biomarker in patients with coronary heart disease.
Coronary Disease
[Association of cathepsin L with coronary heart disease and its risk factors]
Coronary Stenosis
Cathepsin L expression and regulation in human abdominal aortic aneurysm, atherosclerosis, and vascular cells.
Coronary Stenosis
[Association of cathepsin L with coronary heart disease and its risk factors]
COVID-19
Cathepsin L in COVID-19: From Pharmacological Evidences to Genetics.
COVID-19
Cathepsin L plays a key role in SARS-CoV-2 infection in humans and humanized mice and is a promising target for new drug development.
COVID-19
Elucidating the drug repurposing spectra of COVID-19 with its analogues SARS and MERS.
COVID-19
Hydroxychloroquine-mediated inhibition of SARS-CoV-2 entry is attenuated by TMPRSS2.
COVID-19
MPI8 is Potent against SARS-CoV-2 by Inhibiting Dually and Selectively the SARS-CoV-2 Main Protease and the Host Cathepsin L*.
COVID-19
Pan?cancer analysis of transmembrane protease serine 2 and cathepsin L that mediate cellular SARS?CoV?2 infection leading to COVID-19.
COVID-19
Potent in vitro anti-SARS-CoV-2 activity by gallinamide A and analogues via inhibition of cathepsin L.
COVID-19
Roles of existing drug and drug targets for COVID-19 management.
COVID-19
Simultaneous Treatment of COVID-19 With Serine Protease Inhibitor Camostat and/or Cathepsin L Inhibitor?
Cysticercosis
Characterization of a novel cathepsin L-like protease from Taenia solium metacestodes for the immunodiagnosis of porcine cysticercosis.
Cysticercosis
Utility of a protein fraction with cathepsin L-Like activity purified from cysticercus fluid of Taenia solium in the diagnosis of human cysticercosis.
Cysts
Alterations in cysteine proteinase content of rat lung associated with development of Pneumocystis carinii infection.
Cysts
Characterization of cysteine proteases from the carcinogenic liver fluke, Opisthorchis viverrini.
Cysts
The highly antigenic 53/25 kDa Taenia solium protein fraction with cathepsin-L like activity is present in the oncosphere/cysticercus and induces non-protective IgG antibodies in pigs.
Dermatitis, Atopic
Expression of cathepsin L and its inhibitor hurpin in inflammatory and neoplastic skin diseases.
Dermatitis, Atopic
Immunohistochemical expression of cathepsin L in atopic dermatitis and lichen planus.
Diabetes Mellitus
High glucose reduces cathepsin L activity and impairs invasion of circulating progenitor cells.
Diabetes Mellitus
Neutrophil gelatinase-associated lipocalin and Cathepsin L as early predictors of kidney dysfunction in children with type 1 diabetes.
Diabetes Mellitus, Type 1
Cathepsin L inhibition prevents murine autoimmune diabetes via suppression of CD8(+) T cell activity.
Diabetes Mellitus, Type 1
Cathepsin L is essential for onset of autoimmune diabetes in NOD mice.
Diabetes Mellitus, Type 1
Immunoreactivity of cytotoxic T-lymphocyte antigen 2 alpha in mouse pancreatic islet cells.
Diabetes Mellitus, Type 1
Neutrophil gelatinase-associated lipocalin and Cathepsin L as early predictors of kidney dysfunction in children with type 1 diabetes.
Diabetes Mellitus, Type 1
Roles for cathepsins S, L, and B in insulitis and diabetes in the NOD mouse.
Diabetes Mellitus, Type 2
High glucose reduces cathepsin L activity and impairs invasion of circulating progenitor cells.
Diabetes Mellitus, Type 2
Impaired cathepsin L gene expression in skeletal muscle is associated with type 2 diabetes.
Diabetes Mellitus, Type 2
Structure-based development of specific inhibitors for individual cathepsins and their medical applications.
Diabetes Mellitus, Type 2
Urinary cathepsin L is predictive of changes in albuminuria and correlates with glucosepane in patients with type 2 diabetes in a closed-cohort study.
Diabetic Nephropathies
Cathepsin L is crucial for the development of early experimental diabetic nephropathy.
Diabetic Nephropathies
Systemic Monocyte Chemotactic Protein-1 Inhibition Modifies Renal Macrophages and Restores Glomerular Endothelial Glycocalyx and Barrier Function in Diabetic Nephropathy.
Diabetic Retinopathy
Coexpression of heparanase activity, cathepsin L, tissue factor, tissue factor pathway inhibitor, and MMP-9 in proliferative diabetic retinopathy.
Echinococcosis
Cathepsin L cysteine proteinase in the diagnosis of bovine Fasciola gigantica infection.
Echinococcosis
Development of cathepsin-L cysteine proteinase based Dot-enzyme-linked immunosorbent assay for the diagnosis of Fasciola gigantica infection in buffaloes.
Encephalitis, Japanese
Processing of capsid protein by cathepsin L plays a crucial role in replication of Japanese encephalitis virus in neural and macrophage cells.
Encephalomyelitis
Cathepsin L regulates pathogenicCD4 T cells in experimental autoimmune encephalomyelitis.
Encephalomyelitis, Autoimmune, Experimental
Cathepsin L regulates pathogenicCD4 T cells in experimental autoimmune encephalomyelitis.
Endocarditis
Therapeutic effects of bacteriophage Cpl-1 lysin against Streptococcus pneumoniae endocarditis in rats.
Endometrial Neoplasms
Expression of cathepsin L in normal endometrium and endometrial cancer.
Endometrial Neoplasms
Expression of cysteine protease cathepsin L is increased in endometrial cancer and correlates with expression of growth regulatory genes.
Eosinophilia
Host responses during experimental infection with Fasciola gigantica and Fasciola hepatica in Merino sheep II. Development of a predictive index for Fasciola gigantica worm burden.
Epiretinal Membrane
Coexpression of heparanase activity, cathepsin L, tissue factor, tissue factor pathway inhibitor, and MMP-9 in proliferative diabetic retinopathy.
Esophageal Neoplasms
ras mutation and expression of the ras-regulated genes osteopontin and cathepsin L in human esophageal cancer.
Fascioliasis
Effectiveness of Fasciola gigantica excretory-secretory and recombinant cathepsin L antigens for rapid diagnosis of human fascioliasis using immunochromatographic devices.
Fascioliasis
Immunization with cathepsin L proteinases CL1 and CL2 secreted by Fasciola hepatica elicit a preferential type 1 response based on IgG2a antibodies in rats.
Fascioliasis
Immunological approaches for the control of fasciolosis.
Fascioliasis
Serodiagnosis of human fascioliasis by a cystatin capture enzyme-linked immunosorbent assay with recombinant Fasciola gigantica cathepsin L antigen.
Fascioliasis
The diagnosis of human fascioliasis by enzyme-linked immunosorbent assay (ELISA) using recombinant cathepsin L protease.
Fascioliasis
Vaccination with cathepsin L proteinases and with leucine aminopeptidase induces high levels of protection against fascioliasis in sheep.
Fatty Liver
Mir214-3p and Hnf4a/Hnf4? reciprocally regulate Ulk1 expression and autophagy in nonalcoholic hepatic steatosis.
Fibrosarcoma
An Active 32-kDa Cathepsin L Is Secreted Directly from HT 1080 Fibrosarcoma Cells and Not via Lysosomal Exocytosis.
Fibrosarcoma
An examination of the effects of hypoxia, acidosis, and glucose starvation on the expression of metastasis-associated genes in murine tumor cells.
Fibrosarcoma
Identification of integrins alpha6 and beta7 as c-Jun- and transformation-relevant genes in highly invasive fibrosarcoma cells.
Fibrosarcoma
Significance of 32-kDa cathepsin L secreted from cancer cells.
Folliculitis
Expression of cathepsin L and its inhibitor hurpin in inflammatory and neoplastic skin diseases.
Frontotemporal Dementia
Restoration of CTSD (cathepsin D) and lysosomal function in stroke is neuroprotective.
Frontotemporal Lobar Degeneration
The lysosomal protein cathepsin L is a progranulin protease.
Gastrointestinal Stromal Tumors
Cathepsin L is highly expressed in gastrointestinal stromal tumors.
Gastrointestinal Stromal Tumors
MicroRNA-152 inhibits tumor cell growth while inducing apoptosis via the transcriptional repression of cathepsin L in gastrointestinal stromal tumor.
Giant Cell Tumors
Estrogen modulation of osteoclast lysosomal enzyme secretion.
Gingival Hyperplasia
Phenytoin and cyclosporin A suppress the expression of MMP-1, TIMP-1, and cathepsin L, but not cathepsin B in cultured gingival fibroblasts.
Gingival Overgrowth
Cathepsin-L, a key molecule in the pathogenesis of drug-induced and I-cell disease-mediated gingival overgrowth: a study with cathepsin-L-deficient mice.
Gingival Overgrowth
Long-term cyclosporin A exposure suppresses cathepsin-B and -L activity in gingival fibroblasts.
Glioblastoma
Cathepsin L affects apoptosis of glioblastoma cells: a potential implication in the design of cancer therapeutics.
Glioblastoma
Cathepsin L in glioma progression: comparison with cathepsin B.
Glioblastoma
Cathepsin L silencing enhances arsenic trioxide mediated in vitro cytotoxicity and apoptosis in glioblastoma U87MG spheroids.
Glioblastoma
Cathepsin L silencing increases As2O3 toxicity in malignantly transformed pilocytic astrocytoma MPA58 cells by activating caspases 3/7.
Glioblastoma
Cystatin F acts as a mediator of immune suppression in glioblastoma.
Glioblastoma
Expression and immunohistochemical localization of cathepsin L during the progression of human gliomas.
Glioblastoma
Identification of secreted proteins regulated by cAMP in glioblastoma cells using glycopeptide capture and label-free quantification.
Glioblastoma
Inhibition of cathepsin L lowers the apoptotic threshold of glioblastoma cells by up-regulating p53 and transcription of caspases 3 and 7.
Glioblastoma
Lysosomal enzymes, cathepsins in brain tumour invasion.
Glioblastoma
Transcriptional upregulation of human cathepsin L by VEGF in glioblastoma cells.
Glioblastoma
Wild type p53-dependent transcriptional upregulation of cathepsin L expression is mediated by C/EBPα in human glioblastoma cells.
Glioma
Cathepsin L in glioma progression: comparison with cathepsin B.
Glioma
Cathepsin L is involved in X-ray-induced invasion and migration of human glioma U251 cells.
Glioma
Cathepsin L knockdown enhances curcumin-mediated inhibition of growth, migration, and invasion of glioma cells.
Glioma
Cathepsin L promotes ionizing radiation-induced U251 glioma cell migration and invasion through regulating the GSK-3?/CUX1 pathway.
Glioma
Cathepsin L suppression increases the radiosensitivity of human glioma U251 cells via G2/M cell cycle arrest and DNA damage.
Glioma
Expression and immunohistochemical localization of cathepsin L during the progression of human gliomas.
Glioma
Inhibition of cathepsin L sensitizes human glioma cells to ionizing radiation in vitro through NF-?B signaling pathway.
Glioma
Knockdown of Cathepsin L promotes radiosensitivity of glioma stem cells both in vivo and in vitro.
Glioma
Proteases in brain tumour progression.
Glioma
Selective suppression of cathepsin L by antisense cDNA impairs human brain tumor cell invasion in vitro and promotes apoptosis.
Glomerulonephritis
Evidence suggesting a role for cathepsin L in an experimental model of glomerulonephritis.
Glucose Intolerance
Cathepsin L activity controls adipogenesis and glucose tolerance.
Hemangioendothelioma
Generation and degradation of human endostatin proteins by various proteinases.
Hepatitis A
The unique role of domain 2A of the hepatitis A virus precursor polypeptide P1-2A in viral morphogenesis.
Herpes Simplex
Host Enzymes Heparanase and Cathepsin L Promote Herpes Simplex Virus-2 Release from Cells.
Hidradenitis Suppurativa
Expression of cathepsin L and its inhibitor hurpin in inflammatory and neoplastic skin diseases.
Huntington Disease
Restoration of CTSD (cathepsin D) and lysosomal function in stroke is neuroprotective.
Hydatidiform Mole
[Expression of cathepsins B and L in early gestational decidua and chorionic villi]
Hypercalcemia
Conditioned medium from ras oncogene-transformed NIH 3T3 cells induces bone resorption in vitro.
Hypersensitivity
Safety Studies of Pneumococcal Endolysins Cpl-1 and Pal.
Hypertension
Angiotensin II-Induced vascular remodeling and hypertension involves cathepsin L/V- MEK/ERK mediated mechanism.
Hypertension
Association Between Polymorphism in the Human Cathepsin L (CTSL1) Promoter with Hypertension in the Uygur, Kazak and Han Populations in China.
Hyperthyroidism
Experimental hyperthyroidism in rats increases the expression of the ubiquitin ligases atrogin-1 and MuRF1 and stimulates multiple proteolytic pathways in skeletal muscle.
Hypotension
Systemic use of the endolysin Cpl-1 rescues mice with fatal pneumococcal pneumonia.
Idiopathic Pulmonary Fibrosis
A novel cathepsin L inhibitor prevents the progression of idiopathic pulmonary fibrosis.
Infarction, Middle Cerebral Artery
Restoration of CTSD (cathepsin D) and lysosomal function in stroke is neuroprotective.
Infections
A small-molecule oxocarbazate inhibitor of human cathepsin L blocks severe acute respiratory syndrome and ebola pseudotype virus infection into human embryonic kidney 293T cells.
Infections
Activation of the SARS coronavirus spike protein via sequential proteolytic cleavage at two distinct sites.
Infections
Alterations in cysteine proteinase content of rat lung associated with development of Pneumocystis carinii infection.
Infections
Analysis of expressed sequence tags (ESTs) and gene expression changes under different growth conditions for the ciliate Anophryoides haemophila, the causative agent of bumper car disease in the American lobster (Homarus americanus).
Infections
Anaplasma phagocytophilum increases cathepsin L activity, thereby globally influencing neutrophil function.
Infections
Biomphalaria glabrata transcriptome: cDNA microarray profiling identifies resistant- and susceptible-specific gene expression in haemocytes from snail strains exposed to Schistosoma mansoni.
Infections
Can bacteriophage endolysins be nebulised for inhalation delivery against Streptococcus pneumoniae?
Infections
Cathepsin L and cathepsin B mediate reovirus disassembly in murine fibroblast cells.
Infections
Cathepsin L cysteine proteinase in the diagnosis of bovine Fasciola gigantica infection.
Infections
Cathepsin L Helps to Defend Mice from Infection with Influenza A.
Infections
Cathepsin L is an immune-related protein in Pacific abalone (Haliotis discus hannai)--Purification and characterization.
Infections
Cathepsin L is crucial for a Th1-type immune response during Leishmania major infection.
Infections
Cathepsin L is required for ecotropic murine leukemia virus infection in NIH3T3 cells.
Infections
Cathepsin L maturation and activity is impaired in macrophages harboring M. avium and M. tuberculosis.
Infections
Cathepsin L of the sea cucumber Apostichopus japonicus-molecular characterization and transcriptional response to Vibrio splendidus infection.
Infections
Cathepsin L promotes secretory IgA response by participating in antigen presentation pathways during Mycoplasma Hyopneumoniae infection.
Infections
Cathepsin L protects mice from mycoplasmal infection and is essential for airway lymphangiogenesis.
Infections
Cathepsin L proteinases as vaccines against infection with Fasciola hepatica (liver fluke) in ruminants.
Infections
Cathepsin S supports acid-independent infection by some reoviruses.
Infections
Characterization of cysteine proteases from the carcinogenic liver fluke, Opisthorchis viverrini.
Infections
Chemotactic and protease-inhibiting activities of antibiotic peptide precursors.
Infections
Cloning and expression of the major secreted cathepsin B-like protein from juvenile Fasciola hepatica and analysis of immunogenicity following liver fluke infection.
Infections
Cronobacter sakazakii ATCC 29544 Translocated Human Brain Microvascular Endothelial Cells via Endocytosis, Apoptosis Induction, and Disruption of Tight Junction.
Infections
Cysteine peptidases as schistosomiasis vaccines with inbuilt adjuvanticity.
Infections
Development and validation of an RNA- and DNA-based quantitative PCR assay for determination of Kudoa thyrsites infection levels in Atlantic salmon Salmo salar.
Infections
Development of cathepsin-L cysteine proteinase based Dot-enzyme-linked immunosorbent assay for the diagnosis of Fasciola gigantica infection in buffaloes.
Infections
Dissociation of ras oncogene-induced gene expression and anchorage-independent growth in a series of somatic cell mutants.
Infections
DM, but not cathepsin L, is required to control an aerosol infection with Mycobacterium tuberculosis.
Infections
Early immunodiagnosis of fasciolosis in ruminants using recombinant Fasciola hepatica cathepsin L-like protease.
Infections
Ectromelia virus suppresses expression of cathepsins and cystatins in conventional dendritic cells to efficiently execute the replication process.
Infections
Encapsulation of Cwp84 into pectin beads for oral vaccination against Clostridium difficile.
Infections
Fasciola gigantica cathepsin L proteinase-based synthetic peptide for immunodiagnosis and prevention of sheep fasciolosis.
Infections
Fasciola gigantica cathepsin-L cysteine proteinase in the detection of early experimental fasciolosis in ruminants.
Infections
Functional comparison of SARS-CoV-2 with closely related pangolin and bat coronaviruses.
Infections
High genetic diversity in field isolates of Trypanosoma theileri assessed by analysis of cathepsin L-like sequences disclosed multiple and new genotypes infecting cattle in Thailand.
Infections
Host Enzymes Heparanase and Cathepsin L Promote Herpes Simplex Virus-2 Release from Cells.
Infections
Human papillomavirus type 16 does not require cathepsin L or B for infection.
Infections
Identification of a novel Fasciola hepatica cathepsin L protease containing protective epitopes within the propeptide.
Infections
Identification, mRNA expression profiling and activity characterization of cathepsin L from red drum (Sciaenops ocellatus).
Infections
Immunization of hamsters against Clostridium difficile infection using the Cwp84 protease as an antigen.
Infections
Immuno-diagnosis of bubaline fasciolosis with Fasciola gigantica cathepsin-L and recombinant cathepsin L 1-D proteases.
Infections
Immunodiagnosis of Fasciola hepatica infection (fascioliasis) in a human population in the Bolivian Altiplano using purified cathepsin L cysteine proteinase.
Infections
Induction of protective immune responses against schistosomiasis using functionally active cysteine peptidases.
Infections
Induction of protective immunity in cattle against infection with Fasciola hepatica by vaccination with cathepsin L proteinases and with hemoglobin.
Infections
Influence of environmental conditions on the expression and the maturation process of the Clostridium difficile surface associated protease Cwp84.
Infections
Inhibitors of cathepsin L prevent severe acute respiratory syndrome coronavirus entry.
Infections
Linker Editing of Pneumococcal Lysin ClyJ Conveys Improved Bactericidal Activity.
Infections
Loop-mediated isothermal amplification method for differentiation and rapid detection of Taenia species.
Infections
Modulation of Rumen Microbes Through Extracellular Vesicle Released by the Rumen Fluke Calicophoron daubneyi.
Infections
Novel Non-Peptide Inhibitors against SmCL1 of Schistosoma mansoni: In Silico Elucidation, Implications and Evaluation via Knowledge Based Drug Discovery.
Infections
Pan?cancer analysis of transmembrane protease serine 2 and cathepsin L that mediate cellular SARS?CoV?2 infection leading to COVID-19.
Infections
Porcine deltacoronavirus enters cells via two pathways: A protease-mediated one at the cell surface and another facilitated by cathepsins in the endosome.
Infections
Processing of capsid protein by cathepsin L plays a crucial role in replication of Japanese encephalitis virus in neural and macrophage cells.
Infections
Protease-mediated entry via the endosome of human coronavirus 229E.
Infections
Protection against Fasciola gigantica infection in mice by vaccination with recombinant juvenile-specific cathepsin L.
Infections
Rapid identification of lymnaeid snails and their infection with Fasciola gigantica in Thailand.
Infections
Recognition Pattern of the Fasciola hepatica Excretome/Secretome during the Course of an Experimental Infection in Sheep by 2D Immunoproteomics.
Infections
Role of endosomal cathepsins in entry mediated by the Ebola virus glycoprotein.
Infections
Roles of existing drug and drug targets for COVID-19 management.
Infections
SARS coronavirus, but not human coronavirus NL63, utilizes cathepsin L to infect ACE2-expressing cells.
Infections
Serodiagnosis of Fasciola gigantica Infection in Buffaloes with Native Cathepsin-L Proteases and Recombinant Cathepsin L1-D.
Infections
Snake venom-derived bradykinin-potentiating peptides: A promising therapy for COVID-19?
Infections
Systemic use of the endolysin Cpl-1 rescues mice with fatal pneumococcal pneumonia.
Infections
The first characterization of a cystatin and a cathepsin L-like peptidase from Aedes aegypti and their possible role in DENV infection by the modulation of apoptosis.
Infections
TMPRSS2 activates the human coronavirus 229E for cathepsin-independent host cell entry and is expressed in viral target cells in the respiratory epithelium.
Infections
TMPRSS2 expression dictates the entry route used by SARS-CoV-2 to infect host cells.
Infections
Upregulation of gut cathepsin L during Eimeria tenella infection.
Infections
Vitamin D inhibits human immunodeficiency virus type 1 and Mycobacterium tuberculosis infection in macrophages through the induction of autophagy.
Infections
Zaire Ebola virus entry into human dendritic cells is insensitive to cathepsin L inhibition.
Infections
[Cathepsin L Cysteine Protease from Taenia solium: Its biological role in the infection and potential use for the immunodiagnosis of neurocysticercosis.]
Infertility
Expression of cathepsin L in human testis under diverse infertility conditions.
Infertility, Male
Expression of cathepsin L in human testis under diverse infertility conditions.
Influenza, Human
Cathepsin L Helps to Defend Mice from Infection with Influenza A.
Intestinal Neoplasms
Tumor cell- and microenvironment-specific roles of cysteine cathepsins in mouse models of human cancers.
Intestinal Volvulus
Cathepsin L is essential for embryogenesis and development of Caenorhabditis elegans.
Intestinal Volvulus
RNA interference targeting cathepsin L and Z-like cysteine proteases of Onchocerca volvulus confirmed their essential function during L3 molting.
Keratosis, Seborrheic
Immunohistochemical localization of cathepsin L and cystatin A in normal skin and skin tumors.
Kidney Diseases
Increased dynamin expression precedes proteinuria in glomerular disease.
Kidney Diseases
Proteolytic processing of dynamin by cytoplasmic cathepsin L is a mechanism for proteinuric kidney disease.
Kidney Neoplasms
Cloning, genomic organization, and chromosomal localization of human cathepsin L.
Leg Ulcer
Expression of cathepsin L and its inhibitor hurpin in inflammatory and neoplastic skin diseases.
Leiomyoma
Cathepsin L is highly expressed in gastrointestinal stromal tumors.
Leishmaniasis
Cathepsin L is crucial for a Th1-type immune response during Leishmania major infection.
Leishmaniasis
Cathepsin L promotes secretory IgA response by participating in antigen presentation pathways during Mycoplasma Hyopneumoniae infection.
Leishmaniasis
Improving serodiagnosis of human and canine leishmaniasis with recombinant Leishmania braziliensis cathepsin l-like protein and a synthetic peptide containing its linear B-cell epitope.
Leishmaniasis
Treatment with cathepsin L inhibitor potentiates Th2-type immune response in Leishmania major-infected BALB/c mice.
Leishmaniasis, Visceral
Canine Visceral Leishmaniasis in São Paulo, Brazil, the Most Populous City of South America: Isolation, Molecular Diagnosis, and Phylogenetic Inferences.
Leishmaniasis, Visceral
Cationic solid lipid nanoparticles loaded by cysteine proteinase genes as a novel anti-leishmaniasis DNA vaccine delivery system: characterization and in vitro evaluations.
Leukemia
Cathepsin L is required for ecotropic murine leukemia virus infection in NIH3T3 cells.
Leukemia, Myelogenous, Chronic, BCR-ABL Positive
Epigenetic Regulation of Cathepsin L Expression in Chronic Myeloid Leukemia.
Leukemia, Myeloid, Acute
Prognostic significance of cathepsin L expression in pediatric acute myeloid leukemia.
Lichen Planus
Immunohistochemical expression of cathepsin L in atopic dermatitis and lichen planus.
Lichen Planus, Oral
The expression of Cathepsin L in oral lichen planus.
Liver Cirrhosis
Cathepsin L and B as Potential Markers for Liver Fibrosis: Insights From Patients and Experimental Models.
Liver Diseases
Mir214-3p and Hnf4a/Hnf4? reciprocally regulate Ulk1 expression and autophagy in nonalcoholic hepatic steatosis.
Lung Diseases
Analysis of the Proteolytic Processing of ABCA3: Identification of Cleavage Site and Involved Proteases.
Lung Injury
A novel zebrafish model to emulate lung injury by folate deficiency-induced swim bladder defectiveness and protease/antiprotease expression imbalance.
Lung Neoplasms
Alterations in cathepsin L expression in lung cancers.
Lung Neoplasms
Association of Cigarette Smoking, COPD, and Lung Cancer With Expression of SARS-CoV-2 Entry Genes in Human Airway Epithelial Cells.
Lung Neoplasms
Detection of cathepsin B, cathepsin L, cystatin C, urokinase plasminogen activator and urokinase plasminogen activator receptor in the sera of lung cancer patients.
Lung Neoplasms
Expression, proliferation activity and clinical significance of cathepsin B and cathepsin L in operated lung cancer.
Lung Neoplasms
K-ras mutation promotes ionizing radiation-induced invasion and migration of lung cancer in part via the Cathepsin L/CUX1 pathway.
Lung Neoplasms
Loss of the endothelial glycocalyx is associated with increased E-selectin mediated adhesion of lung tumour cells to the brain microvascular endothelium.
Lung Neoplasms
Overexpression of Cathepsin L is associated with gefitinib resistance in non-small cell lung cancer.
Lung Neoplasms
Quantification of intracellular cathepsin activities in human lung tumor cell lines by flow cytometry.
Lung Neoplasms
Secretion of a latent, acid activatable cathepsin L precursor by human non-small cell lung cancer cell lines.
Lung Neoplasms
Significance of 32-kDa cathepsin L secreted from cancer cells.
Lymphatic Metastasis
Expression of cathepsin L in nasopharyngeal carcinoma and its clinical significance.
Lymphoma
Amoeboid shape change and contact guidance: T-lymphocyte crawling through fibrillar collagen is independent of matrix remodeling by MMPs and other proteases.
Lymphoma
Cytotoxic T lymphocyte antigen-2 alpha induces apoptosis of murine T-lymphoma cells and cardiac fibroblasts and is regulated by cAMP/PKA.
Lymphoma
Expression of cathepsin L in human tumor cells is under the control of distinct regulatory mechanisms.
Lymphoma, Non-Hodgkin
Cystatin C in LS lymphosarcoma and HA-1 hepatoma treated with Ukrain and cyclophosphamide and involvement of apoptosis.
Lysosomal Storage Diseases
Restoration of CTSD (cathepsin D) and lysosomal function in stroke is neuroprotective.
Malaria
Independent amino acid residues in the S2 pocket of falcipain-3 determine its specificity for P2 residues in substrates.
Malaria
Targeted disruption of Plasmodium falciparum cysteine protease, falcipain 1, reduces oocyst production, not erythrocytic stage growth.
Melanoma
Abl and Arg mediate cysteine cathepsin secretion to facilitate melanoma invasion and metastasis.
Melanoma
Acidic extracellular pH promotes experimental metastasis of human melanoma cells in athymic nude mice.
Melanoma
Cathepsin L expression is up-regulated by hypoxia in human melanoma cells: role of its 5'-untranslated region.
Melanoma
Cathepsin L increases invasion and migration of B16 melanoma.
Melanoma
Characterization of human cathepsin L promoter and identification of binding sites for NF-Y, Sp1 and Sp3 that are essential for its activity.
Melanoma
Cloning and characterization of anti-cathepsin L single chain variable fragment whose expression inhibits procathepsin L secretion in human melanoma cells.
Melanoma
Effect of cysteine proteinase inhibitors on murine B16 melanoma cell invasion in vitro.
Melanoma
Expression and prognostic significance of Cathepsin L in early cutaneous malignant melanoma.
Melanoma
Expression of cathepsin L and its inhibitor hurpin in inflammatory and neoplastic skin diseases.
Melanoma
Expression of cathepsin L in human tumor cells is under the control of distinct regulatory mechanisms.
Melanoma
Heparin enhances serpin inhibition of the cysteine protease cathepsin L.
Melanoma
Melanoma Growth and Progression After Ultraviolet A Irradiation: Impact of Lysosomal Exocytosis and Cathepsin Proteases.
Melanoma
Membrane-associated cathepsin L: a role in metastasis of melanomas.
Melanoma
Mitochondria-to-nucleus stress signaling in mammalian cells: nature of nuclear gene targets, transcription regulation, and induced resistance to apoptosis.
Melanoma
TGF-? signaling, activated stromal fibroblasts, and cysteine cathepsins B and L drive the invasive growth of human melanoma cells.
Melanoma
Tumor-associated cysteine proteinase activities in human melanoma cells and fibroblasts of different origin.
Melanoma, Amelanotic
Membrane-associated cathepsin L: a role in metastasis of melanomas.
Melanoma, Experimental
Cathepsin L increases invasion and migration of B16 melanoma.
Melanoma, Experimental
Membrane-associated cathepsin L: a role in metastasis of melanomas.
Melanoma, Experimental
The malignant phenotype and cysteine proteinases.
Meningioma
Cathepsins B and L and their inhibitors stefin B and cystatin C as markers for malignant progression of benign meningiomas.
Meningioma
Cathepsins B and L are markers for clinically invasive types of meningiomas.
Meningioma
Lysosomal enzymes, cathepsins in brain tumour invasion.
Meningioma
Toward understanding recurrent meningioma: the potential role of lysosomal cysteine proteases and their inhibitors.
Meningitis, Pneumococcal
Phage lytic enzyme Cpl-1 for antibacterial therapy in experimental pneumococcal meningitis.
Mouth Neoplasms
PlatyphyllenoneExerts Anti-Metastatic Effects on Human Oral Cancer Cells by Modulating Cathepsin L Expression, MAPK Pathway and Epithelial-Mesenchymal Transition.
Mouth Neoplasms
Possible contribution of active MMP2 to lymph-node metastasis and secreted cathepsin L to bone invasion of newly established human oral-squamous-cancer cell lines.
Mouth Neoplasms
Quantitative analysis of cathepsin L mRNA and protein expression during oral cancer progression.
Mouth Neoplasms
Variable expression of cathepsin B and D correlates with highly invasive and metastatic phenotype of oral cancer.
Mucolipidoses
Cathepsin-L, a key molecule in the pathogenesis of drug-induced and I-cell disease-mediated gingival overgrowth: a study with cathepsin-L-deficient mice.
Muscular Atrophy
Clenbuterol suppresses proteasomal and lysosomal proteolysis and atrophy-related genes in denervated rat soleus muscles independently of Akt.
Muscular Atrophy
Conditional activation of MET in differentiated skeletal muscle induces atrophy.
Muscular Atrophy
Low-dose dexamethasone prevents endotoxaemia-induced muscle protein loss and impairment of carbohydrate oxidation in rat skeletal muscle.
Muscular Atrophy
Pharmacological activation of the pyruvate dehydrogenase complex reduces statin-mediated upregulation of FOXO gene targets and protects against statin myopathy in rodents.
Muscular Atrophy
Skeletal muscle FOXO1 (FKHR) transgenic mice have less skeletal muscle mass, down-regulated Type I (slow twitch/red muscle) fiber genes, and impaired glycemic control.
Muscular Atrophy
Vitamin D Attenuates FOXO1-Target Atrophy Gene Expression in C2C12 Muscle Cells.
Muscular Diseases
Pharmacological activation of the pyruvate dehydrogenase complex reduces statin-mediated upregulation of FOXO gene targets and protects against statin myopathy in rodents.
Mycoplasma Infections
Cathepsin L promotes secretory IgA response by participating in antigen presentation pathways during Mycoplasma Hyopneumoniae infection.
Myocardial Infarction
Inhibition of myocardial cathepsin-L release during reperfusion following myocardial infarction improves cardiac function and reduces infarct size.
Myocardial Ischemia
[Cathepsin L expression in plasma after acute myocardial ischemia and ischemia-reperfusion in rats].
Nasopharyngeal Carcinoma
Expression of cathepsin L in nasopharyngeal carcinoma and its clinical significance.
Neoplasm Metastasis
A micRNA-200c/cathepsin L feedback loop determines paclitaxel resistance in human lung cancer A549 cells in vitro through regulating epithelial-mesenchymal transition.
Neoplasm Metastasis
Acidic extracellular pH promotes experimental metastasis of human melanoma cells in athymic nude mice.
Neoplasm Metastasis
Altered gene expression profiles of NIH3T3 cells regulated by human lung cancer associated gene CT120.
Neoplasm Metastasis
Cancer-associated mutations reveal a novel role for EpCAM as an inhibitor of cathepsin-L and tumor cell invasion.
Neoplasm Metastasis
Cathepsin L antisense oligonucleotides in a human osteosarcoma cell line: effects on the invasive phenotype.
Neoplasm Metastasis
Cathepsin L in metastatic bone disease: therapeutic implications.
Neoplasm Metastasis
Cathepsin L in tumor angiogenesis and its therapeutic intervention by the small molecule inhibitor KGP94.
Neoplasm Metastasis
Cathepsin L inactivation leads to multimodal inhibition of prostate cancer cell dissemination in a preclinical bone metastasis model.
Neoplasm Metastasis
Cathepsin L increases invasion and migration of B16 melanoma.
Neoplasm Metastasis
Cathepsin L induces proangiogenic changes in human omental microvascular endothelial cells via activation of the ERK1/2 pathway.
Neoplasm Metastasis
Cathepsin L inhibition by the small molecule KGP94 suppresses tumor microenvironment enhanced metastasis associated cell functions of prostate and breast cancer cells.
Neoplasm Metastasis
Cathepsin L is associated with proliferation and clinical outcome of urothelial carcinoma of the bladder.
Neoplasm Metastasis
Cathepsin L promotes angiogenesis by regulating the CDP/Cux/VEGF-D pathway in human gastric cancer.
Neoplasm Metastasis
Cathepsin L secretion by host and neoplastic cells potentiates invasion.
Neoplasm Metastasis
Cathepsin L upregulation-induced EMT phenotype is associated with the acquisition of cisplatin or paclitaxel resistance in A549 cells.
Neoplasm Metastasis
Cathepsin L, target in cancer treatment?
Neoplasm Metastasis
Characterization of a cathepsin L-like enzyme secreted from human pancreatic cancer cell line HPC-YP.
Neoplasm Metastasis
Characterization of downstream Ras signals that induce alternative protease-dependent invasive phenotypes.
Neoplasm Metastasis
Clinical Relevance of Increased Endothelial and Mesothelial Expression of Proangiogenic Proteases and VEGFA in the Omentum of Patients with Metastatic Ovarian High-Grade Serous Carcinoma.
Neoplasm Metastasis
Clinical value of combined detection of serum matrix metalloproteinase-9, heparanase, and cathepsin for determining ovarian cancer invasion and metastasis.
Neoplasm Metastasis
CSN6 Promotes the Migration and Invasion of Cervical Cancer Cells by Inhibiting Autophagic Degradation of Cathepsin L.
Neoplasm Metastasis
Cysteine and serine proteases in gastric cancer.
Neoplasm Metastasis
Differential activity of cathepsin L in human placenta at two different stages of gestation.
Neoplasm Metastasis
Effect of liver macrophage depression on the development of liver metastases of HA-1 tumor in mice.
Neoplasm Metastasis
Enhanced expression of cathepsin L in metastatic bone tumors.
Neoplasm Metastasis
Expression and immunohistochemical localization of cathepsin L during the progression of human gliomas.
Neoplasm Metastasis
Expression of Cathepsin B and L antigen and activity is associated with early colorectal cancer progression.
Neoplasm Metastasis
Expression of cathepsin L in nasopharyngeal carcinoma and its clinical significance.
Neoplasm Metastasis
Gelatin Zymography Using Leupeptin for the Detection of Various Cathepsin L Forms.
Neoplasm Metastasis
Graphene Oxide-Based Targeting of Extracellular Cathepsin D and Cathepsin L As A Novel Anti-Metastatic Enzyme Cancer Therapy.
Neoplasm Metastasis
Identification of integrins alpha6 and beta7 as c-Jun- and transformation-relevant genes in highly invasive fibrosarcoma cells.
Neoplasm Metastasis
Identification of low-risk node-negative breast cancer patients by tumor biological factors PAI-1 and cathepsin L.
Neoplasm Metastasis
Immunohistochemical localization of cathepsin L and cystatin A in normal skin and skin tumors.
Neoplasm Metastasis
Increased expression of cathepsins L and B and decreased activity of their inhibitors in metastatic, ras-transformed NIH 3T3 cells.
Neoplasm Metastasis
Inhibition of carcinoma cell invasion and liver metastases formation by the cysteine proteinase inhibitor E-64.
Neoplasm Metastasis
Mammary carcinoma cell lines of high and low metastatic potential differ not in extravasation but in subsequent migration and growth.
Neoplasm Metastasis
Membrane-associated cathepsin L: a role in metastasis of melanomas.
Neoplasm Metastasis
Molecular cloning and anti-invasive activity of cathepsin L propeptide-like protein from Calotropis procera R. Br. against cancer cells.
Neoplasm Metastasis
Neuroblastoma therapy: what is in the pipeline?
Neoplasm Metastasis
Overexpression of cysteine cathepsin L is a marker of invasion and metastasis in ovarian cancer.
Neoplasm Metastasis
Possible contribution of active MMP2 to lymph-node metastasis and secreted cathepsin L to bone invasion of newly established human oral-squamous-cancer cell lines.
Neoplasm Metastasis
Prognostic value of the cysteine proteases cathepsins B and cathepsin L in human breast cancer.
Neoplasm Metastasis
Selective suppression of cathepsin L by antisense cDNA impairs human brain tumor cell invasion in vitro and promotes apoptosis.
Neoplasm Metastasis
Significance of 32-kDa cathepsin L secreted from cancer cells.
Neoplasm Metastasis
Stress-resistant Translation of Cathepsin L mRNA in Breast Cancer Progression.
Neoplasm Metastasis
Structural basis for reversible and irreversible inhibition of human cathepsin L by their respective dipeptidyl glyoxal and diazomethylketone inhibitors.
Neoplasm Metastasis
Structure-based development of cathepsin L inhibitors and therapeutic applications for prevention of cancer metastasis and cancer-induced osteoporosis.
Neoplasm Metastasis
The heparanase system and tumor metastasis: is heparanase the seed and soil?
Neoplasm Metastasis
The Potential Role of the Proteases Cathepsin D and Cathepsin L in the Progression and Metastasis of Epithelial Ovarian Cancer.
Neoplasm Metastasis
The role of cysteine and serine proteases in colorectal carcinoma.
Neoplasm Metastasis
Truncated Human Cathepsin L, Encoded by a Novel Splice Variant, Exhibits Altered Subcellular Localization and Cytotoxicity.
Neoplasm Metastasis
[Relationship between cathepsin L and invasion and metastasis of ovarian carcinoma cells.]
Neoplasm Metastasis
[Role and behavior of cathepsin B and cathepsin L in gastric cancer]
Neoplasms
A Cathepsin-L is required for invasive behavior during Air Sac Primordium development in Drosophila melanogaster.
Neoplasms
A heparin binding motif on the pro-domain of human procathepsin L mediates zymogen destabilization and activation.
Neoplasms
A micRNA-200c/cathepsin L feedback loop determines paclitaxel resistance in human lung cancer A549 cells in vitro through regulating epithelial-mesenchymal transition.
Neoplasms
Alterations in cathepsin L expression in lung cancers.
Neoplasms
Altered gene expression profiles of NIH3T3 cells regulated by human lung cancer associated gene CT120.
Neoplasms
An Active 32-kDa Cathepsin L Is Secreted Directly from HT 1080 Fibrosarcoma Cells and Not via Lysosomal Exocytosis.
Neoplasms
Antiprotease therapy in cancer: hot or not?
Neoplasms
Antisense RNA inhibition of cathepsin L expression reduces tumorigenicity of malignant cells.
Neoplasms
Assessment of cathepsin L activity by use of the inhibitor CA-074 compared to cathepsin B activity in human lung tumor tissue.
Neoplasms
Association of Epithelial Mesenchymal Transition with prostate and breast health disparities.
Neoplasms
Biomarkers Associated With Tumor Ki67 and Cathepsin L Gene Expression in Prostate Cancer Patients Participating in a Presurgical Weight Loss Trial.
Neoplasms
Bioprinting on Live Tissue for Investigating Cancer Cell Dynamics.
Neoplasms
Cancer-associated mutations reveal a novel role for EpCAM as an inhibitor of cathepsin-L and tumor cell invasion.
Neoplasms
Cathepsin B activity in human lung tumor cell lines: ultrastructural localization, pH sensitivity, and inhibitor status at the cellular level.
Neoplasms
Cathepsin B promotes the progression of pancreatic ductal adenocarcinoma in mice.
Neoplasms
Cathepsin expression in oral squamous cell carcinoma: relationship with clinicopathologic factors.
Neoplasms
Cathepsin L activated by mutant p53 and Egr-1 promotes ionizing radiation-induced EMT in human NSCLC.
Neoplasms
Cathepsin L affects apoptosis of glioblastoma cells: a potential implication in the design of cancer therapeutics.
Neoplasms
Cathepsin L antisense oligonucleotides in a human osteosarcoma cell line: effects on the invasive phenotype.
Neoplasms
Cathepsin L expression is up-regulated by hypoxia in human melanoma cells: role of its 5'-untranslated region.
Neoplasms
Cathepsin L in glioma progression: comparison with cathepsin B.
Neoplasms
Cathepsin L in tumor angiogenesis and its therapeutic intervention by the small molecule inhibitor KGP94.
Neoplasms
Cathepsin L inactivation leads to multimodal inhibition of prostate cancer cell dissemination in a preclinical bone metastasis model.
Neoplasms
Cathepsin L increases invasion and migration of B16 melanoma.
Neoplasms
Cathepsin L inhibition by the small molecule KGP94 suppresses tumor microenvironment enhanced metastasis associated cell functions of prostate and breast cancer cells.
Neoplasms
Cathepsin L inhibition suppresses drug resistance in vitro and in vivo: a putative mechanism.
Neoplasms
Cathepsin L is associated with proliferation and clinical outcome of urothelial carcinoma of the bladder.
Neoplasms
Cathepsin L is highly expressed in gastrointestinal stromal tumors.
Neoplasms
Cathepsin L is involved in X-ray-induced invasion and migration of human glioma U251 cells.
Neoplasms
Cathepsin L knockdown enhances curcumin-mediated inhibition of growth, migration, and invasion of glioma cells.
Neoplasms
Cathepsin L promotes angiogenesis by regulating the CDP/Cux/VEGF-D pathway in human gastric cancer.
Neoplasms
Cathepsin L promotes ionizing radiation-induced U251 glioma cell migration and invasion through regulating the GSK-3?/CUX1 pathway.
Neoplasms
Cathepsin L secretion by host and neoplastic cells potentiates invasion.
Neoplasms
Cathepsin L splice variants in human breast cell lines.
Neoplasms
Cathepsin L suppression increases the radiosensitivity of human glioma U251 cells via G2/M cell cycle arrest and DNA damage.
Neoplasms
Cathepsin L targeting in cancer treatment.
Neoplasms
Cathepsin L upregulation-induced EMT phenotype is associated with the acquisition of cisplatin or paclitaxel resistance in A549 cells.
Neoplasms
Cathepsin L, target in cancer treatment?
Neoplasms
Cathepsin L-induced galectin-1 may act as a proangiogenic factor in the metastasis of high-grade serous carcinoma.
Neoplasms
Cathepsin L-mediated resistance of paclitaxel and cisplatin is mediated by distinct regulatory mechanisms.
Neoplasms
Cathepsin L2, a novel human cysteine proteinase produced by breast and colorectal carcinomas.
Neoplasms
Cathepsin-B and cathepsin-L expression levels do not correlate with sensitivity of tumour cells to TNF-alpha-mediated apoptosis.
Neoplasms
Cathepsins B and L are markers for clinically invasive types of meningiomas.
Neoplasms
Cathepsins D, B and L in breast carcinoma and in transformed human breast epithelial cells (HBEC).
Neoplasms
Cathepsins D, B, and L in malignant human lung tissue.
Neoplasms
Caught in the act: the crystal structure of cleaved cathepsin L bound to the active site of Cathepsin L.
Neoplasms
CCAAT-displacement protein/cut homeobox transcription factor (CUX1) represses estrogen receptor-alpha (ER-?) in triple-negative breast cancer cells and can be antagonized by muscadine grape skin extract (MSKE).
Neoplasms
Cells producing cathepsins D, B, and L in human breast carcinoma and their association with prognosis.
Neoplasms
Characterization of a cathepsin L-like enzyme secreted from human pancreatic cancer cell line HPC-YP.
Neoplasms
Clinical Relevance of Increased Endothelial and Mesothelial Expression of Proangiogenic Proteases and VEGFA in the Omentum of Patients with Metastatic Ovarian High-Grade Serous Carcinoma.
Neoplasms
Cloning and expression of the gene for the major excreted protein of transformed mouse fibroblasts. A secreted lysosomal protease regulated by transformation.
Neoplasms
Cloning, genomic organization, and chromosomal localization of human cathepsin L.
Neoplasms
Conditional Gene Targeting Reveals Cell Type-Specific Roles of the Lysosomal Protease Cathepsin L in Mammary Tumor Progression.
Neoplasms
Contribution of cathepsin L to secretome composition and cleavage pattern of mouse embryonic fibroblasts.
Neoplasms
Cystatin E/M Suppresses Tumor Cell Growth through Cytoplasmic Retention of NF-?B.
Neoplasms
Cystatins and cathepsins in breast carcinoma.
Neoplasms
Cysteine and serine proteases in gastric cancer.
Neoplasms
Cysteine proteases and cell differentiation: excystment of the ciliated protist Sterkiella histriomuscorum.
Neoplasms
Cysteine proteinase cathepsin H in tumours and sera of lung cancer patients: relation to prognosis and cigarette smoking.
Neoplasms
Cysteine proteinases in cancer progression and their clinical relevance for prognosis.
Neoplasms
Deficiency for the cysteine protease cathepsin L impairs Myc-induced tumorigenesis in a mouse model of pancreatic neuroendocrine cancer.
Neoplasms
Deficiency for the cysteine protease cathepsin L promotes tumor progression in mouse epidermis.
Neoplasms
Differential activity of cathepsin L in human placenta at two different stages of gestation.
Neoplasms
Dioxin-mediated tumor progression through activation of mitochondria-to-nucleus stress signaling.
Neoplasms
Downregulation of cathepsin L suppresses cancer invasion and migration by inhibiting transforming growth factor???mediated epithelial?mesenchymal transition.
Neoplasms
Downstream sequences mediate induction of the mouse cathepsin L promoter by phorbol esters.
Neoplasms
Dynamic Model of Protease State and Inhibitor Trafficking to Predict Protease Activity in Breast Cancer Cells.
Neoplasms
Effect of in-situ and ex-situ biofloc on immune response of Genetically Improved Farmed Tilapia.
Neoplasms
Effective activation of the proenzyme form of the urokinase-type plasminogen activator (pro-uPA) by the cysteine protease cathepsin L.
Neoplasms
Electrophoretic analysis of the cleaved form of serpin, squamous cell carcinoma antigen-1 in normal and malignant squamous epithelial tissues.
Neoplasms
Enhanced expression of cathepsin L in metastatic bone tumors.
Neoplasms
Enhancing effect of new biological response modifier sulfoethylated (1-->3)-beta-D-glucan on antitumor activity of cyclophosphamide in the treatment of experimental murine leukoses.
Neoplasms
Epigenetic Regulation of Cathepsin L Expression in Chronic Myeloid Leukemia.
Neoplasms
Epithelial-Mesenchymal Transition (EMT) Protein Expression in a Cohort of Stage II Colorectal Cancer Patients With Characterized Tumor Budding and Mismatch Repair Protein Status.
Neoplasms
Estrogen modulation of osteoclast lysosomal enzyme secretion.
Neoplasms
Expression and immunohistochemical localization of cathepsin L during the progression of human gliomas.
Neoplasms
Expression of cathepsin L and its inhibitor hurpin in inflammatory and neoplastic skin diseases.
Neoplasms
Expression of cathepsin L in human testis under diverse infertility conditions.
Neoplasms
Expression of cathepsin L in human tumor cells is under the control of distinct regulatory mechanisms.
Neoplasms
Expression of cathepsin L in human tumors.
Neoplasms
Expression of cathepsin L in nasopharyngeal carcinoma and its clinical significance.
Neoplasms
Expression of cathepsin L in normal endometrium and endometrial cancer.
Neoplasms
Expression of Cathepsin L in tumor cells and tumor-associated macrophages in patients with Ewing sarcoma family of tumors: a pilot study.
Neoplasms
Expression of genes that contribute to proliferative and metastatic ability in breast cancer resected during various menstrual phases.
Neoplasms
Expression profile of cathepsins indicates the potential of cathepsins B and D as prognostic factors in breast cancer patients.
Neoplasms
Expression, proliferation activity and clinical significance of cathepsin B and cathepsin L in operated lung cancer.
Neoplasms
Gelatin Zymography Using Leupeptin for the Detection of Various Cathepsin L Forms.
Neoplasms
Graphene Oxide-Based Targeting of Extracellular Cathepsin D and Cathepsin L As A Novel Anti-Metastatic Enzyme Cancer Therapy.
Neoplasms
Heparin enhances serpin inhibition of the cysteine protease cathepsin L.
Neoplasms
High levels of cathepsin D and cystatin B are associated with increased risk of coronary events.
Neoplasms
Hybridoma cells producing antibodies to cathepsin L have greatly reduced potential for tumour growth.
Neoplasms
Identification and characterization of a novel human cathepsin L splice variant.
Neoplasms
Identification of cathepsin L as a differentially expressed message associated with skeletal muscle wasting.
Neoplasms
Identification of integrins alpha6 and beta7 as c-Jun- and transformation-relevant genes in highly invasive fibrosarcoma cells.
Neoplasms
Identification of low-risk node-negative breast cancer patients by tumor biological factors PAI-1 and cathepsin L.
Neoplasms
Identification of secreted glycoproteins of human prostate and bladder stromal cells by comparative quantitative proteomics.
Neoplasms
Immunohistochemical analysis of cathepsins D, B, and L in human breast cancer.
Neoplasms
Immunohistochemical expression of cathepsin L in atopic dermatitis and lichen planus.
Neoplasms
Immunohistochemical localization of cathepsin L and cystatin A in normal skin and skin tumors.
Neoplasms
Immunostained cathepsins B and L correlate with depth of invasion and different metastatic pathways in early stage gastric carcinoma.
Neoplasms
In silico investigation of heparanase-correlated genes in breast cancer subtypes.
Neoplasms
In vivo imaging of intraperitoneally disseminated tumors in model mice by using activatable fluorescent small-molecular probes for activity of cathepsins.
Neoplasms
Inactivation of the cystatin E/M tumor suppressor gene in cervical cancer.
Neoplasms
Increased cathepsin L levels in serum in some patients with ovarian cancer: comparison with CA125 and CA72-4.
Neoplasms
Increased expression and activity of nuclear cathepsin L in cancer cells suggests a novel mechanism of cell transformation.
Neoplasms
Increased levels of cathepsin B and L, urokinase-type plasminogen activator and its inhibitor type-1 as an early event in gastric carcinogenesis.
Neoplasms
Influence of 12(S)-hydroxyeicosatetraenoic acid (12(S)-HETE) on the localization of cathepsin B and cathepsin L in human lung tumor cells.
Neoplasms
Inhibition of cathepsin L sensitizes human glioma cells to ionizing radiation in vitro through NF-?B signaling pathway.
Neoplasms
Inhibition of FoxO transcriptional activity prevents muscle fiber atrophy during cachexia and induces hypertrophy.
Neoplasms
Interaction between prostate cancer cells and prostate fibroblasts promotes accumulation and proteolytic processing of basement membrane proteins.
Neoplasms
K-ras mutation promotes ionizing radiation-induced invasion and migration of lung cancer in part via the Cathepsin L/CUX1 pathway.
Neoplasms
Knockdown of Cathepsin L promotes radiosensitivity of glioma stem cells both in vivo and in vitro.
Neoplasms
Levels of the Autophagy Related 5 Protein Affect Progression and Metastasis of Pancreatic Tumors in Mice.
Neoplasms
Localization of nuclear cathepsin L and its association with disease progression and poor outcome in colorectal cancer.
Neoplasms
Loss of cathepsin L activity promotes claudin-1 overexpression and intestinal neoplasia.
Neoplasms
Loss of the endothelial glycocalyx is associated with increased E-selectin mediated adhesion of lung tumour cells to the brain microvascular endothelium.
Neoplasms
Lysosomal cathepsins B and L and Stefin A blood levels in patients with hepatocellular carcinoma and/or liver cirrhosis: potential clinical implications.
Neoplasms
Malignant transformation and tumor promoter treatment increase levels of a transcript for a secreted glycoprotein.
Neoplasms
Mammary carcinoma cell lines of high and low metastatic potential differ not in extravasation but in subsequent migration and growth.
Neoplasms
MicroRNA-152 inhibits tumor cell growth while inducing apoptosis via the transcriptional repression of cathepsin L in gastrointestinal stromal tumor.
Neoplasms
Mitochondrial stress-induced calcium signaling, phenotypic changes and invasive behavior in human lung carcinoma A549 cells.
Neoplasms
Modeling of Halogen-Protein Interactions in Co-Solvent Molecular Dynamics Simulations.
Neoplasms
Molecular and cytogenetic analysis of glioblastoma multiforme.
Neoplasms
Molecular cloning and anti-invasive activity of cathepsin L propeptide-like protein from Calotropis procera R. Br. against cancer cells.
Neoplasms
Multiple lysosomal trafficking phenotypes in metastatic mouse mammary tumor cell lines.
Neoplasms
Muscadine grape skin extract can antagonize Snail-cathepsin L-mediated invasion, migration and osteoclastogenesis in prostate and breast cancer cells.
Neoplasms
Non-peptidic Cruzain Inhibitors with Trypanocidal Activity Discovered by Virtual Screening and In Vitro Assay.
Neoplasms
Novel Non-Congeneric Derivatives of the Choline Kinase Alpha Inhibitor ICL-CCIC-0019.
Neoplasms
Overexpression of Cathepsin L is associated with chemoresistance and invasion of epithelial ovarian cancer.
Neoplasms
P300 Participates in Ionizing Radiation-Mediated Activation of Cathepsin L by Mutant p53.
Neoplasms
Peptidomimetic 2-cyanopyrrolidines as potent selective cathepsin L inhibitors.
Neoplasms
Phorbol ester stimulated cathepsin L expression in U937 cells.
Neoplasms
PlatyphyllenoneExerts Anti-Metastatic Effects on Human Oral Cancer Cells by Modulating Cathepsin L Expression, MAPK Pathway and Epithelial-Mesenchymal Transition.
Neoplasms
Possible contribution of active MMP2 to lymph-node metastasis and secreted cathepsin L to bone invasion of newly established human oral-squamous-cancer cell lines.
Neoplasms
Post-transcriptional regulation of human cathepsin L expression.
Neoplasms
Presence of activated ras correlates with increased cysteine proteinase activities in human colorectal carcinomas.
Neoplasms
Processing and lysosomal localization of a glycoprotein whose secretion is transformation stimulated.
Neoplasms
Prognostic significance of cathepsin L expression in pediatric acute myeloid leukemia.
Neoplasms
Prognostic significance of cathepsins B and L in primary human breast cancer.
Neoplasms
Prognostic significance of cysteine proteinases cathepsins B and L and their endogenous inhibitors stefins A and B in patients with squamous cell carcinoma of the head and neck.
Neoplasms
Prognostic significance of extracellular matrix degrading enzymes-cathepsin L and matrix metalloproteases-2 [MMP-2] in human pancreatic cancer.
Neoplasms
Prognostic value of cathepsins B, H, L, D and their endogenous inhibitors stefins A and B in head and neck carcinoma.
Neoplasms
Prognostic value of the cysteine proteases cathepsins B and cathepsin L in human breast cancer.
Neoplasms
Proteases and their inhibitors in human brain tumours: a review.
Neoplasms
Proteases as prognostic markers in cancer.
Neoplasms
Protective role of cathepsin L in mouse skin carcinogenesis.
Neoplasms
Protein C inhibitor regulates both cathepsin L activity and cell-mediated tumor cell migration.
Neoplasms
Quantitative analysis of cathepsin L mRNA and protein expression during oral cancer progression.
Neoplasms
ras mutation and expression of the ras-regulated genes osteopontin and cathepsin L in human esophageal cancer.
Neoplasms
Recombinant cathepsin S propeptide attenuates cell invasion by inhibition of cathepsin L-like proteases in tumor microenvironment.
Neoplasms
Relation between the regulation of DNA synthesis and the production of two secreted glycoproteins by 12-O-tetradecanoylphorbol-13-acetate in 3T3 cells and in phorbol ester nonresponsive 3T3 variants.
Neoplasms
RNA interference targeting CML66, a novel tumor antigen, inhibits proliferation, invasion and metastasis of HeLa cells.
Neoplasms
Secreted cathepsin L generates endostatin from collagen XVIII.
Neoplasms
Selective suppression of cathepsin L by antisense cDNA impairs human brain tumor cell invasion in vitro and promotes apoptosis.
Neoplasms
Sequence analysis and distribution of two new human cathepsin L splice variants.
Neoplasms
Sequential enzyme-activated macrotheranostic probe for selective tumor mitochondria targeting.
Neoplasms
Significance of 32-kDa cathepsin L secreted from cancer cells.
Neoplasms
Small-molecule inhibitors of cathepsin L incorporating functionalized ring-fused molecular frameworks.
Neoplasms
Splice variants of human cathepsin L mRNA show different expression rates.
Neoplasms
Squamous cell carcinoma antigen is a potent inhibitor of cysteine proteinase cathepsin L.
Neoplasms
Stefins and lysosomal cathepsins B, L and D in human breast carcinoma.
Neoplasms
Stress-resistant Translation of Cathepsin L mRNA in Breast Cancer Progression.
Neoplasms
Structural basis for reversible and irreversible inhibition of human cathepsin L by their respective dipeptidyl glyoxal and diazomethylketone inhibitors.
Neoplasms
Structure-based development of cathepsin L inhibitors and therapeutic applications for prevention of cancer metastasis and cancer-induced osteoporosis.
Neoplasms
Suppression by cathepsin L inhibitors of the invasion of amnion membranes by murine cancer cells.
Neoplasms
Synovial fibroblast-like cell transfection with the SV40 large T antigen induces a transformed phenotype and permits transient tumor formation in immunodeficient mice.
Neoplasms
Synthesis and biochemical evaluation of benzoylbenzophenone thiosemicarbazone analogues as potent and selective inhibitors of cathepsin L.
Neoplasms
Synthesis and biological evaluation of a water-soluble phosphate prodrug salt and structural analogues of KGP94, a lead inhibitor of cathepsin L.
Neoplasms
Synthesis and evaluation of N?,N?-diacetyl-l-lysine-inositol conjugates as cancer-selective probes for metabolic engineering of GPIs and GPI-anchored proteins.
Neoplasms
Synthesis and Preclinical Evaluation of a Highly Improved Anticancer Prodrug Activated by Histone Deacetylases and Cathepsin L.
Neoplasms
Systemic Monocyte Chemotactic Protein-1 Inhibition Modifies Renal Macrophages and Restores Glomerular Endothelial Glycocalyx and Barrier Function in Diabetic Nephropathy.
Neoplasms
Targeting senescence pathways to reverse drug resistance in cancer.
Neoplasms
Targeting the Nuclear Cathepsin L CCAAT Displacement Protein/Cut Homeobox Transcription Factor-Epithelial Mesenchymal Transition Pathway in Prostate and Breast Cancer Cells with the Z-FY-CHO Inhibitor.
Neoplasms
The anti-angiogenic activity of NSITC, a specific cathepsin L inhibitor.
Neoplasms
The expression of Cathepsin L in oral lichen planus.
Neoplasms
The Expression of Lysosomal Proteinases and Their Inhibitors in Breast Cancer: Possible Relationship to Prognosis of the Disease.
Neoplasms
The heparanase system and tumor metastasis: is heparanase the seed and soil?
Neoplasms
The identification of active forms of cysteine proteinases in Kirsten-virus-transformed mouse fibroblasts by use of a specific radiolabelled inhibitor.
Neoplasms
The influence of Ukrain on the growth of HA-1 tumor in mice: the role of cysteine proteinases as markers of tumor malignancy.
Neoplasms
The major excreted protein of transformed fibroblasts is an activable acid-protease.
Neoplasms
Toward understanding recurrent meningioma: the potential role of lysosomal cysteine proteases and their inhibitors.
Neoplasms
Transcription of human cathepsin L mRNA species hCATL B from a novel alternative promoter in the first intron of its gene.
Neoplasms
Truncated Human Cathepsin L, Encoded by a Novel Splice Variant, Exhibits Altered Subcellular Localization and Cytotoxicity.
Neoplasms
Tumor marker utility and prognostic relevance of cathepsin B, cathepsin L, urokinase-type plasminogen activator, plasminogen activator inhibitor type-1, CEA and CA 19-9 in colorectal cancer.
Neoplasms
Tumor progression and metastasis in murine D2 hyperplastic alveolar nodule mammary tumor cell lines.
Neoplasms
Tumor promoters increase the synthesis of a 32,000-dalton protein in BALB/c 3T3 cells.
Neoplasms
Ultrasensitive internally quenched substrates of human cathepsin L.
Neoplasms
Wild type p53-dependent transcriptional upregulation of cathepsin L expression is mediated by C/EBPα in human glioblastoma cells.
Neoplasms
[Cathepsin L from human brain tumor. Purification and contents]
Neoplasms
[Characterization of an analog enzyme to cathepsin L produced by tumor cells]
Neoplasms
[Prognostic implications of biologic markers in intracranial meningiomas: 120 cases]
Neoplasms
[Prognostic significance of determining cathepsin B activity in malignant ovarian tumors]
Neoplasms
[Protease activities in gastric and colon cancer tissues]
Neoplasms
[Role and behavior of cathepsin B and cathepsin L in gastric cancer]
Neoplasms, Germ Cell and Embryonal
Expression of cathepsin L in human testis under diverse infertility conditions.
Nephritis, Interstitial
Identification and characterization of the interactive proteins with cytotoxic T-lymphocyte antigen-2?
Nephrosis
Expression of Cathepsin L and Its Intrinsic Inhibitors in Glomeruli of Rats With Puromycin Aminonucleoside Nephrosis.
Nephrosis
Podocyte migration during nephrotic syndrome requires a coordinated interplay between cathepsin L and alpha3 integrin.
Nephrotic Syndrome
Podocyte migration during nephrotic syndrome requires a coordinated interplay between cathepsin L and alpha3 integrin.
Nephrotic Syndrome
Role of cathepsin L in idiopathic nephrotic syndrome in children.
Netherton Syndrome
Epidermal differentiation: the role of proteases and their inhibitors.
Neuroblastoma
Cathepsin L is involved in 6-hydroxydopamine induced apoptosis of SH-SY5Y neuroblastoma cells.
Neuroblastoma
Identification of secreted proteins regulated by cAMP in glioblastoma cells using glycopeptide capture and label-free quantification.
Neurocysticercosis
[Cathepsin L Cysteine Protease from Taenia solium: Its biological role in the infection and potential use for the immunodiagnosis of neurocysticercosis.]
Neurodegenerative Diseases
Unique neuronal functions of cathepsin L and cathepsin B in secretory vesicles: biosynthesis of peptides in neurotransmission and neurodegenerative disease.
Neuroinflammatory Diseases
Inhibition of cathepsin L alleviates the microglia-mediated neuroinflammatory responses through caspase-8 and NF-?B pathways.
Neuronal Ceroid-Lipofuscinoses
Analysis of cathepsin B and cathepsin L treatment to clear toxic lysosomal protein aggregates in neuronal ceroid lipofuscinosis.
Neuronal Ceroid-Lipofuscinoses
Enzyme replacement therapy with recombinant pro-CTSD (cathepsin D) corrects defective proteolysis and autophagy in neuronal ceroid lipofuscinosis.
Nevus
TGF-? signaling, activated stromal fibroblasts, and cysteine cathepsins B and L drive the invasive growth of human melanoma cells.
Non-alcoholic Fatty Liver Disease
Mir214-3p and Hnf4a/Hnf4? reciprocally regulate Ulk1 expression and autophagy in nonalcoholic hepatic steatosis.
Obesity
Peripheral cathepsin L inhibition induces fat loss in C. elegans and mice through promoting central serotonin synthesis.
Osteoarthritis
Comparative analysis of cathepsin L, cathepsin D, and collagenase messenger RNA expression in synovial tissues of patients with rheumatoid arthritis and osteoarthritis, by in situ hybridization.
Osteoarthritis
Cysteine and serine proteases of synovial tissue in rheumatoid arthritis and osteoarthritis.
Osteoarthritis
Measurement of elastase and cysteine proteinases in synovial fluid of patients with rheumatoid arthritis, sero-negative spondylarthropathies, and osteoarthritis.
Osteolysis
Cathepsin K is the principal protease in giant cell tumor of bone.
Osteophyte
The relative importance of cysteine peptidases in osteoarthritis.
Osteoporosis
Caught in the act: the crystal structure of cleaved cathepsin L bound to the active site of Cathepsin L.
Osteoporosis
Soluble cathepsin-L: a marker of bone resorption and bone density?
Osteoporosis
Structure-based development of cathepsin L inhibitors and therapeutic applications for prevention of cancer metastasis and cancer-induced osteoporosis.
Osteosarcoma
Cathepsin L antisense oligonucleotides in a human osteosarcoma cell line: effects on the invasive phenotype.
Osteosarcoma
Enhanced expression of cathepsin L in metastatic bone tumors.
Otitis Media
Cathepsin L activity and its inhibitor in human otitis media.
Ovarian Neoplasms
Cathepsin L is involved in proliferation and invasion of ovarian cancer cells.
Ovarian Neoplasms
Clinical value of combined detection of serum matrix metalloproteinase-9, heparanase, and cathepsin for determining ovarian cancer invasion and metastasis.
Ovarian Neoplasms
Combined detection of serum matrix metalloproteinase 9, acetyl heparinase and cathepsin L in diagnosis of ovarian cancer.
Ovarian Neoplasms
Increased cathepsin L levels in serum in some patients with ovarian cancer: comparison with CA125 and CA72-4.
Ovarian Neoplasms
Knockdown of cathepsin L sensitizes ovarian cancer cells to chemotherapy.
Ovarian Neoplasms
Overexpression of cysteine cathepsin L is a marker of invasion and metastasis in ovarian cancer.
Ovarian Neoplasms
Quinacrine-Induced Autophagy in Ovarian Cancer Triggers Cathepsin-L Mediated Lysosomal/Mitochondrial Membrane Permeabilization and Cell Death.
Ovarian Neoplasms
Serum HE4, CA125, YKL-40, bcl-2, cathepsin-L and prediction optimal debulking surgery, response to chemotherapy in ovarian cancer.
Ovarian Neoplasms
The application value of the detection of the level of tissue polypeptide antigen, ovarian cancer antigen X1, cathepsin L and CA125 on the diagnosis of epithelial ovarian cancer.
Ovarian Neoplasms
[Relationship between cathepsin L and invasion and metastasis of ovarian carcinoma cells.]
Pancreatic Neoplasms
Characterization of a cathepsin L-like enzyme secreted from human pancreatic cancer cell line HPC-YP.
Pancreatic Neoplasms
Plasma cathepsin L: a prognostic marker for pancreatic cancer.
Pancreatitis
Cathepsin L inactivates human trypsinogen, whereas cathepsin L-deletion reduces the severity of pancreatitis in mice.
Pancreatitis
Impaired autophagic flux mediates acinar cell vacuole formation and trypsinogen activation in rodent models of acute pancreatitis.
Pancreatitis
Pathophysiology of acute and infected pancreatitis.
Pancreatitis
Transgenic expression of GFP-LC3 perturbs autophagy in exocrine pancreas and acute pancreatitis responses in mice.
Papillon-Lefevre Disease
Epidermal differentiation: the role of proteases and their inhibitors.
Parasitic Diseases
Early immunodiagnosis of fasciolosis in ruminants using recombinant Fasciola hepatica cathepsin L-like protease.
Parkinson Disease
Cathepsin L is involved in 6-hydroxydopamine induced apoptosis of SH-SY5Y neuroblastoma cells.
Parkinson Disease
Parkinson's disease involves autophagy and abnormal distribution of cathepsin L.
Parkinson Disease
Restoration of CTSD (cathepsin D) and lysosomal function in stroke is neuroprotective.
Periodontitis
Cathepsin B- and L-like activities at local gingival sites of chronic periodontitis patients.
Periodontitis
COVID-19 and Periodontitis: A Reality to Live with.
Periodontitis
Microarray and quantitative RT-PCR analyses in calcium-channel blockers induced gingival overgrowth tissues of periodontitis patients.
Persistent Infection
Cysteine protease isoforms from Trypanosoma cruzi, cruzipain 2 and cruzain, present different substrate preference and susceptibility to inhibitors.
Persistent Infection
Diagnosis of sheep fasciolosis caused by Fasciola hepatica using cathepsin L enzyme-linked immunosorbent assays (ELISA).
Pneumococcal Infections
Comprehensive evaluation of chitosan nanoparticle based phage lysin delivery system; a novel approach to counter S. pneumoniae infections.
Pneumonia, Mycoplasma
Cathepsin L Helps to Defend Mice from Infection with Influenza A.
Pneumonia, Pneumococcal
Delivery of the endolysin Cpl-1 by inhalation rescues mice with fatal pneumococcal pneumonia.
Pneumonia, Pneumococcal
Systemic use of the endolysin Cpl-1 rescues mice with fatal pneumococcal pneumonia.
Polycystic Kidney, Autosomal Dominant
Acceleration of polycystic kidney disease progression in cpk mice carrying a deletion in the homeodomain protein Cux1.
Prostatic Neoplasms
Association of Epithelial Mesenchymal Transition with prostate and breast health disparities.
Prostatic Neoplasms
Biomarkers Associated With Tumor Ki67 and Cathepsin L Gene Expression in Prostate Cancer Patients Participating in a Presurgical Weight Loss Trial.
Prostatic Neoplasms
Biotechnological Potential of Araucaria angustifolia Pine Nuts Extract and the Cysteine Protease Inhibitor AaCI-2S.
Prostatic Neoplasms
Cathepsin L inactivation leads to multimodal inhibition of prostate cancer cell dissemination in a preclinical bone metastasis model.
Prostatic Neoplasms
Quantitative Glycoproteomic Analysis of Optimal Cutting Temperature-Embedded Frozen Tissues Identifying Glycoproteins Associated with Aggressive Prostate Cancer.
Prostatic Neoplasms
Snail transcription factor NLS and importin ?1 regulate the subcellular localization of Cathepsin L and Cux1.
Proteinuria
Cathepsin L activity correlates with proteinuria in chronic kidney disease in humans.
Proteinuria
Cathepsin L is crucial for the development of early experimental diabetic nephropathy.
Proteinuria
Evidence suggesting a role for cathepsin L in an experimental model of glomerulonephritis.
Proteinuria
Expression of Cathepsin L and Its Intrinsic Inhibitors in Glomeruli of Rats With Puromycin Aminonucleoside Nephrosis.
Proteinuria
More expression, less function: cleaved dynamin in glomerular kidney disease.
Proteinuria
Proteinuria: an enzymatic disease of the podocyte?
Proteinuria
Proteinuria: is it all in the foot?
Proteinuria
Proteolytic processing of dynamin by cytoplasmic cathepsin L is a mechanism for proteinuric kidney disease.
Psoriasis
Expression of cathepsin L and its inhibitor hurpin in inflammatory and neoplastic skin diseases.
Psoriasis
Processing of cathepsins L, B and D in psoriatic epidermis.
Pulmonary Disease, Chronic Obstructive
Association of Cigarette Smoking, COPD, and Lung Cancer With Expression of SARS-CoV-2 Entry Genes in Human Airway Epithelial Cells.
Pulmonary Disease, Chronic Obstructive
Dysregulation of endocytic machinery and ACE2 in small airways of smokers and COPD patients can augment their susceptibility to SARS-CoV-2 (COVID-19) infections.
Pulmonary Emphysema
Uptake of extracellular enzyme by a novel pathway is a major determinant of cathepsin L levels in human macrophages.
Pyoderma Gangrenosum
Expression of cathepsin L and its inhibitor hurpin in inflammatory and neoplastic skin diseases.
Renal Insufficiency, Chronic
Cathepsin L activity correlates with proteinuria in chronic kidney disease in humans.
Reoviridae Infections
Genetic and pharmacologic alteration of cathepsin expression influences reovirus pathogenesis.
Reoviridae Infections
Mutant cells selected during persistent reovirus infection do not express mature cathepsin L and do not support reovirus disassembly.
Reperfusion Injury
Inhibition of myocardial cathepsin-L release during reperfusion following myocardial infarction improves cardiac function and reduces infarct size.
Retinal Degeneration
Cathepsin proteases mediate photoreceptor cell degeneration in Drosophila.
Sarcoma
Comparison of cathepsin L synthesized by normal and transformed cells at the gene, message, protein, and oligosaccharide levels.
Sarcoma
Differences in targeting and secretion of cathepsins B and L by BALB/3T3 fibroblasts and Moloney murine sarcoma virus-transformed BALB/3T3 fibroblasts.
Sarcoma
Enzymatic detection systems for non-isotopic in situ hybridization using biotinylated cDNA probes.
Sarcoma
Retrovirus transformation associated secretory phosphoproteins of mouse and mink cells.
Sarcoma, Ewing
Expression of Cathepsin L in tumor cells and tumor-associated macrophages in patients with Ewing sarcoma family of tumors: a pilot study.
Sarcoma, Yoshida
Identification of cathepsin L as a differentially expressed message associated with skeletal muscle wasting.
Schistosomiasis
Induction of protective immune responses against schistosomiasis using functionally active cysteine peptidases.
Scleroderma, Systemic
A potential contribution of altered cathepsin L expression to the development of dermal fibrosis and vasculopathy in systemic sclerosis.
Sepsis
Inhibition of FoxO transcriptional activity prevents muscle fiber atrophy during cachexia and induces hypertrophy.
Sepsis
Phage lytic enzymes as therapy for antibiotic-resistant Streptococcus pneumoniae infection in a murine sepsis model.
Sepsis
Sepsis causes right ventricular myocardial inflammation independent of pulmonary hypertension in a porcine sepsis model.
Sertoli Cell-Only Syndrome
Expression of cathepsin L in human testis under diverse infertility conditions.
Severe Acute Respiratory Syndrome
A small-molecule oxocarbazate inhibitor of human cathepsin L blocks severe acute respiratory syndrome and ebola pseudotype virus infection into human embryonic kidney 293T cells.
Severe Acute Respiratory Syndrome
Activation of the SARS coronavirus spike protein via sequential proteolytic cleavage at two distinct sites.
Severe Acute Respiratory Syndrome
Amiodarone alters late endosomes and inhibits SARS coronavirus infection at a post-endosomal level.
Severe Acute Respiratory Syndrome
Cathepsin L functionally cleaves the severe acute respiratory syndrome coronavirus class I fusion protein upstream of rather than adjacent to the fusion peptide.
Severe Acute Respiratory Syndrome
Cathepsin L in COVID-19: From Pharmacological Evidences to Genetics.
Severe Acute Respiratory Syndrome
Human eggs, zygotes, and embryos express the receptor angiotensin 1-converting enzyme 2 and transmembrane serine protease 2 protein necessary for severe acute respiratory syndrome coronavirus 2 infection.
Severe Acute Respiratory Syndrome
Inhibitors of cathepsin L prevent severe acute respiratory syndrome coronavirus entry.
Skin Diseases
Expression of cathepsin L and its inhibitor hurpin in inflammatory and neoplastic skin diseases.
Skin Diseases
Expression of the human Cathepsin L inhibitor hurpin in mice: skin alterations and increased carcinogenesis.
Spondylarthropathies
Measurement of elastase and cysteine proteinases in synovial fluid of patients with rheumatoid arthritis, sero-negative spondylarthropathies, and osteoarthritis.
Squamous Cell Carcinoma of Head and Neck
Prognostic value of cathepsin L and its inhibitor headpin in oral squamous cell carcinoma.
Squamous Cell Carcinoma of Head and Neck
Quantitative analysis of cathepsin L mRNA and protein expression during oral cancer progression.
Squamous Cell Carcinoma of Head and Neck
The expression of Cathepsin L in oral lichen planus.
ST Elevation Myocardial Infarction
Inhibition of myocardial cathepsin-L release during reperfusion following myocardial infarction improves cardiac function and reduces infarct size.
Starvation
Coordinate upregulation of proteolytic-related genes in rat muscle during late fasting.
Starvation
Effect of fasting and thyroidectomy on cysteine proteinase activities in liver and muscle.
Starvation
Salmon spawning migration and muscle protein metabolism: the August Krogh principle at work.
Starvation
The cathepsin L gene is a direct target of FOXO1 in skeletal muscle.
Stomach Neoplasms
Cathepsin L promotes angiogenesis by regulating the CDP/Cux/VEGF-D pathway in human gastric cancer.
Stomach Neoplasms
Defining the invasive phenotype of proximal gastric cancer cells.
Stomach Neoplasms
FOXO3a promotes gastric cancer cell migration and invasion through the induction of cathepsin L.
Stomach Neoplasms
Variant cathepsin L activity from gastric cancer tissue.
Stomach Neoplasms
[Protease activities in gastric and colon cancer tissues]
Stomach Neoplasms
[Role and behavior of cathepsin B and cathepsin L in gastric cancer]
Tendinopathy
Sequential, but not Concurrent, Incubation of Cathepsin K and L with Type I Collagen Results in Extended Proteolysis.
Testicular Neoplasms
Expression of cathepsin L in human testis under diverse infertility conditions.
Testicular Neoplasms
Expression of cathepsin L in human tumors.
Thrombosis
Cathepsin D and cathepsin L activities in aortic aneurysm wall and parietal thrombus.
Thyroid Neoplasms
Influence of proliferation, differentiation and dedifferentiation factors on the expression of the lysosomal cysteine proteinase cathepsin L (CL) in thyroid cancer cell lines.
Thyroid Neoplasms
Relaxin enhances the oncogenic potential of human thyroid carcinoma cells.
Toxoplasmosis
Discovery and Optimization of Triazine Nitrile Inhibitors of Toxoplasma gondii Cathepsin L for the Potential Treatment of Chronic Toxoplasmosis in the CNS.
Toxoplasmosis
Optimization of dipeptidic inhibitors of cathepsin L for improved Toxoplasma gondii selectivity and CNS permeability.
Triple Negative Breast Neoplasms
CCAAT-displacement protein/cut homeobox transcription factor (CUX1) represses estrogen receptor-alpha (ER-?) in triple-negative breast cancer cells and can be antagonized by muscadine grape skin extract (MSKE).
Trypanosomiasis, African
Repurposing a Library of Human Cathepsin L Ligands: Identification of Macrocyclic Lactams as Potent Rhodesain and Trypanosoma brucei Inhibitors.
Tuberculosis
DM, but not cathepsin L, is required to control an aerosol infection with Mycobacterium tuberculosis.
Urinary Bladder Neoplasms
Role of urinary cathepsin B and L in the detection of bladder urothelial cell carcinoma.
Uterine Cervical Neoplasms
Cathepsin L mediates resveratrol-induced autophagy and apoptotic cell death in cervical cancer cells.
Uterine Cervical Neoplasms
CSN6 Promotes the Migration and Invasion of Cervical Cancer Cells by Inhibiting Autophagic Degradation of Cathepsin L.
Uterine Cervical Neoplasms
Inactivation of the cystatin E/M tumor suppressor gene in cervical cancer.
Uterine Neoplasms
Increased cathepsin L levels in serum in some patients with ovarian cancer: comparison with CA125 and CA72-4.
Vascular Diseases
Cathepsin L deficiency results in reactive oxygen species (ROS) accumulation and vascular cells activation.
Vascular Diseases
Cathepsin L expression and regulation in human abdominal aortic aneurysm, atherosclerosis, and vascular cells.
Vesicular Stomatitis
Characterization of the envelope glycoprotein of a novel filovirus, lloviu virus.
Vesicular Stomatitis
SARS coronavirus, but not human coronavirus NL63, utilizes cathepsin L to infect ACE2-expressing cells.
Viremia
Genetic and pharmacologic alteration of cathepsin expression influences reovirus pathogenesis.
Virus Diseases
A small-molecule oxocarbazate inhibitor of human cathepsin L blocks severe acute respiratory syndrome and ebola pseudotype virus infection into human embryonic kidney 293T cells.
Virus Diseases
Cathepsin L is required for ecotropic murine leukemia virus infection in NIH3T3 cells.
Virus Diseases
Diminished intracellular invariant chain expression after vaccinia virus infection.
Virus Diseases
Identification and characterization of the v-cath gene of the baculovirus, CfMNPV.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.49
Abz-PR-acetyl-K-QLATKAARKSAK-Dnp
pH and temperature not specified in the publication
0.37
Abz-PRKQLAT-acetyl-K-AARKSAK-Dnp
pH and temperature not specified in the publication
0.51
Abz-PRKQLATKAAR-dimethyl-K-SAK-Dnp
pH and temperature not specified in the publication
0.46
Abz-PRKQLATKAARKSAK-Dnp
pH and temperature not specified in the publication
9 - 46
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
5.3
2-aminobenzoyl-Ala-Leu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
3.8
2-aminobenzoyl-Arg-Leu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
3.5
2-aminobenzoyl-Asn-Leu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
3.8
2-aminobenzoyl-Gln-Leu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
0.4
2-aminobenzoyl-Glu-Glu-epsilon-amino-caproic acid-Glu-Leu-Lys-Leu-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
4
2-aminobenzoyl-Glu-Leu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
1.2
2-aminobenzoyl-Glu-Leu-Lys-Leu-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
0.1
2-aminobenzoyl-Gly-Leu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
5.9
2-aminobenzoyl-His-Leu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
2.3
2-aminobenzoyl-Ile-Leu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
3.2
2-aminobenzoyl-Lys-Arg-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
0.4
2-aminobenzoyl-Lys-Asn-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
0.4
2-aminobenzoyl-Lys-Asp-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
1.7
2-aminobenzoyl-Lys-Gln-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
0.4
2-aminobenzoyl-Lys-Glu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
0.5
2-aminobenzoyl-Lys-Gly-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
1.3
2-aminobenzoyl-Lys-His-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
2.3
2-aminobenzoyl-Lys-Ile-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
1.1
2-aminobenzoyl-Lys-Leu-Ala-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
3.7
2-aminobenzoyl-Lys-Leu-Arg-Arg-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
6.3
2-aminobenzoyl-Lys-Leu-Arg-Asn-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
5.8
2-aminobenzoyl-Lys-Leu-Arg-Gln-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
4.9
2-aminobenzoyl-Lys-Leu-Arg-Glu-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
3.4
2-aminobenzoyl-Lys-Leu-Arg-Gly-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
7.3
2-aminobenzoyl-Lys-Leu-Arg-His-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
3.9
2-aminobenzoyl-Lys-Leu-Arg-Ile-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
4.1
2-aminobenzoyl-Lys-Leu-Arg-Ser-Ala-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
3.6
2-aminobenzoyl-Lys-Leu-Arg-Ser-Arg-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
2.3
2-aminobenzoyl-Lys-Leu-Arg-Ser-Asn-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
4.2
2-aminobenzoyl-Lys-Leu-Arg-Ser-Gln-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
4.1
2-aminobenzoyl-Lys-Leu-Arg-Ser-Glu-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
4.8
2-aminobenzoyl-Lys-Leu-Arg-Ser-Gly-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
3.7
2-aminobenzoyl-Lys-Leu-Arg-Ser-His-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
2.4
2-aminobenzoyl-Lys-Leu-Arg-Ser-Ile-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
6
2-aminobenzoyl-Lys-Leu-Arg-Ser-Pro-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
4.6
2-aminobenzoyl-Lys-Leu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
3.2
2-aminobenzoyl-Lys-Leu-Arg-Ser-Val-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
5.5
2-aminobenzoyl-Lys-Leu-Arg-Val-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
1.1
2-aminobenzoyl-Lys-Leu-Asn-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
0.2
2-aminobenzoyl-Lys-Leu-Asp-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
0.9
2-aminobenzoyl-Lys-Leu-Gln-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
2.6
2-aminobenzoyl-Lys-Leu-Glu-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
0.4
2-aminobenzoyl-Lys-Leu-Gly-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
1.3
2-aminobenzoyl-Lys-Leu-His-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
0.4
2-aminobenzoyl-Lys-Leu-Ile-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
3.1
2-aminobenzoyl-Lys-Leu-Lys-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
0.4
2-aminobenzoyl-Lys-Leu-Met-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
0.1
2-aminobenzoyl-Lys-Leu-Pro-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
1.5
2-aminobenzoyl-Lys-Leu-Ser-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
1.3
2-aminobenzoyl-Lys-Leu-Thr-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
0.5
2-aminobenzoyl-Lys-Leu-Val-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
1.9
2-aminobenzoyl-Lys-Lys-epsilon-amino-caproic acid-Glu-Leu-Lys-Leu-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
4
2-aminobenzoyl-Lys-Met-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
13.5
2-aminobenzoyl-Lys-Phe-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
1.2
2-aminobenzoyl-Lys-Pro-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
1.9
2-aminobenzoyl-Lys-Ser-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
0.4
2-aminobenzoyl-Lys-Thr-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
1.9
2-aminobenzoyl-Lys-Trp-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
7.8
2-aminobenzoyl-Lys-Tyr-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
6.4
2-aminobenzoyl-Lys-Val-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
2.1
2-aminobenzoyl-Val-Leu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
17.4
Abz-3-biphenyl-L-Ala-Arg-Ala-Ala-Tyr(3-NO2)-NH2
-
in 50 mM Mes buffer (pH 6.0) containing 5 mM dithiothreitol, at 37°C
27
Abz-3-biphenyl-L-Ala-Arg-Ala-Gln-Tyr(3-NO2)-NH2
-
in 50 mM Mes buffer (pH 6.0) containing 5 mM dithiothreitol, at 37°C
5.01
Abz-3-biphenyl-L-Ala-Arg-Ala-Ser-Tyr(3-NO2)-NH2
-
in 50 mM Mes buffer (pH 6.0) containing 5 mM dithiothreitol, at 37°C
0.01 - 0.5
benzyloxycarbonyl-Gly-Pro-Arg-7-amido-4-methylcoumarin
17.6 - 27.2
benzyloxycarbonyl-Leu-Arg-7-amido-4-methylcoumarin
10 - 50
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin 7-amide
5.4 - 20.5
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
9
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
mutant enzyme T223V/M274L/D275N/G277A/V278M
18
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
mutant enzyme T223V/DELTAE286-E289
30
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
mutant enzyme T223V/DELTAE286-N293
46
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
wild type enzyme
0.01
benzyloxycarbonyl-Gly-Pro-Arg-7-amido-4-methylcoumarin
-
wild type enzyme
0.5
benzyloxycarbonyl-Gly-Pro-Arg-7-amido-4-methylcoumarin
-
mutant enzyme L67Y/A205L
17.6
benzyloxycarbonyl-Leu-Arg-7-amido-4-methylcoumarin
-
wild type enzyme
27.2
benzyloxycarbonyl-Leu-Arg-7-amido-4-methylcoumarin
-
mutant enzyme L67Y/A205L
10
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin 7-amide
-
-
17
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin 7-amide
-
-
25.8
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin 7-amide
-
-
39
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin 7-amide
-
recombinant enzyme expressed Escherichia coli
50
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin 7-amide
-
recombinant enzyme expressed in mouse myeloma clls
5.4
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
-
wild type enzyme
20.5
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
-
mutant enzyme L67Y/A205L
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.03
biphenyl-4-yl-acetylasparagine-D-Arg-Phe-Phe-NH2
pH 5.5, 25°C
0.00021
biphenyl-4-yl-acetylcysteine-D-Arg-Abu-N-(2-phenylethyl)amide
pH 5.5, 25°C
0.0039
biphenyl-4-yl-acetylcysteine-D-Arg-Arg-N-(2-phenylethyl)amide
pH 5.5, 25°C
0.081
biphenyl-4-yl-acetylcysteine-D-Arg-N-(2-phenylethyl)amide
pH 5.5, 25°C
0.000021
biphenyl-4-yl-acetylcysteine-D-Arg-Phe-N-(2-phenylethyl)amide
pH 5.5, 25°C
0.00017
biphenyl-4-yl-acetylcysteine-D-Arg-Phe-Phe-NH2
pH 5.5, 25°C
0.000067
biphenyl-4-yl-acetylcysteine-D-Arg-Trp-N-(2-phenylethyl)amide
pH 5.5, 25°C
0.000045
biphenyl-4-yl-acetylcysteine-D-Arg-Tyr-N-(2-phenylethyl)amide
pH 5.5, 25°C
0.00027
biphenyl-4-yl-acetylmethylcysteine-D-Arg-Leu-N-(2-phenylethyl)amide
pH 5.5, 25°C
0.00024
biphenyl-4-yl-acetylmethylcysteine-D-Arg-Met-N-(2-phenylethyl)amide
pH 5.5, 25°C
0.000019
biphenyl-4-yl-acetylmethylcysteine-D-Arg-Phe-N-(2-phenylethyl)amide
pH 5.5, 25°C
0.00021
biphenyl-4-yl-acetylmethylcysteine-D-Arg-Phe-N-(3-phenylpropyl)amide
pH 5.5, 25°C
0.0066
biphenyl-4-yl-acetylmethylcysteine-D-Arg-Phe-N-(benzyl)amide
pH 5.5, 25°C
0.00007
biphenyl-4-yl-acetylmethylcysteine-D-Arg-Phe-Phe-NH2
pH 5.5, 25°C
0.0002
biphenyl-4-yl-acetylmethylcysteine-D-Orn-Phe-N-(2-phenylethyl)amide
pH 5.5, 25°C
0.00093
biphenyl-4-yl-acetylmethylcysteine-Gly-Phe-Phe-NH2
pH 5.5, 25°C
0.00049
biphenyl-4-yl-acetylnorvaline-D-Arg-Phe-N-(2-phenylethyl)amide
pH 5.5, 25°C
0.07
biphenyl-4-yl-acetylserine-D-Arg-Phe-Phe-NH2
pH 5.5, 25°C
0.000023
biphenylacetyl-(N6-biphenylacetyl)-Lys-D-Arg-Tyr-N-phenylethyl
pH and temperature not specified in the publication
0.000511
biphenylacetyl-(N6-biphenylacetyl)Lys-D-Arg-Phe-N-phenylethyl
pH and temperature not specified in the publication
0.000019
biphenylacetyl-MCys-D-Arg-Phe-N-phenylethyl
pH and temperature not specified in the publication
0.0107
KAPR-acetyl-K-QLATKAARKSAPA
pH and temperature not specified in the publication
0.00502
KAPRKQLAT-acetyl-K-AARKSAPA
pH and temperature not specified in the publication
0.00455
KAPRKQLATKAAR-dimethyl-K-SAPA
pH and temperature not specified in the publication
0.0045
KAPRKQLATKAARKSAPA
pH and temperature not specified in the publication
0.00000000552 - 0.0000000101
p41-fragment-human
-
0.0000006
Phe-Tyr-(OBut)-COCHO
pH and temperature not specified in the publication
0.0004
(2R,3R)-dibenzyl-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(S)-prolyl]-aziridine-2,3-dicarboxylate
-
-
0.0048
(2R,3R)-diethyl-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(R)-azetidine-2-carbonyl]aziridine-2,3-dicarboxylate
-
-
0.0059
(2R,3R)-diethyl-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(R)-nipecotyl]aziridine-2,3-dicarboxylate
-
-
0.0048
(2R,3R)-diethyl-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(S)-azetidine-2-carbonyl]aziridine-2,3-dicarboxylate
-
-
0.0059
(2R,3R)-diethyl-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(S)-nipecotyl]aziridine-2,3-dicarboxylate
-
-
0.0529
(2S,3S)-1-[N-(tert-butoxycarbonyl)-(R)-leucyl-(S)-nipecotyl]aziridine-2,3-dicarboxylic acid
-
-
0.026
(2S,3S)-1-[N-(tert-butoxycarbonyl)-(R)-phenylalanyl-(R)-alanyl]aziridine-2,3-dicarboxylic acid
-
-
0.0101
(2S,3S)-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(R)-nipecotyl]aziridine-2,3-dicarboxylic acid
-
-
0.0101
(2S,3S)-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(S)-nipecotyl]aziridine-2,3-dicarboxylic acid
-
-
0.0187
(2S,3S)-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(S)-prolyl]aziridine-2,3-dicarboxylic acid
-
-
0.0178
(2S,3S)-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-isonipecotyl]aziridine-2,3-dicarboxylic acid
-
-
0.0178
(2S,3S)-1-[N-(tert-butoxycarbonyl)-(S)-phenylalanyl-(R)-alanyl]aziridine-2,3-dicarboxylic acid
-
-
0.0153
(2S,3S)-1-[N-(tert-butoxycarbonyl)-(S)-phenylalanyl-(S)-alanyl]aziridine-2,3-dicarboxylic acid
-
-
0.0159
(2S,3S)-1-[N-(tert-butoxycarbonyl)-glycyl-(S)-prolyl]aziridine-2,3-dicarboxylic acid
-
-
0.0064
(2S,3S)-dibenzyl-1-[1-[N-(tert-butoxycarbonyl)-(R)-leucyl]-(S)-aziridine-2-carbonyl]aziridine-2,3-dicarboxylate
-
-
0.000013
(2S,3S)-dibenzyl-1-[1-[N-(tert-butoxycarbonyl)-(S)-leucyl]-(S)-aziridine-2-carbonyl]aziridine-2,3-dicarboxylate
-
-
0.0014
(2S,3S)-dibenzyl-1-[biotinyl-6-aminohexanoyl]-aziridine-2,3-dicarboxylate
-
-
0.0042
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-(R)-leucyl-(R)-nipecotyl]aziridine-2,3-dicarboxylate
-
-
0.0042
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-(R)-leucyl-(S)-nipecotyl]aziridine-2,3-dicarboxylate
-
-
0.004
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-(R)-leucyl-(S)-prolyl]-aziridine-2,3-dicarboxylate
-
-
0.0216
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-(R)-phenylalanyl-(R)-alanyl]aziridine-2,3-dicarboxylate
-
-
0.0147
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-(R)-phenylalanyl-(S)-alanyl]aziridine-2,3-dicarboxylate
-
-
0.0038
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(R)-azetidine-2-carbonyl]aziridine-2,3-dicarboxylate
-
-
0.0044
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(R)-nipecotyl]aziridine-2,3-dicarboxylate
-
-
0.006
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(R)-prolyl]-aziridine-2,3-dicarboxylate
-
-
0.0038
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(S)-azetidine-2-carbonyl]aziridine-2,3-dicarboxylate
-
-
0.0044
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(S)-nipecotyl]aziridine-2,3-dicarboxylate
-
-
0.0152
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-(S)-phenylalanyl-(R)-alanyl]aziridine-2,3-dicarboxylate
-
-
0.0166
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-(S)-phenylalanyl-(S)-alanyl]aziridine-2,3-dicarboxylate
-
-
0.0058
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-glycyl-(R)-nipecotyl]aziridine-2,3-dicarboxylate
-
-
0.0071
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-glycyl-(R)-prolyl]aziridine-2,3-dicarboxylate
-
-
0.0058
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-glycyl-(R+S)-nipecotyl]aziridine-2,3-dicarboxylate
-
-
0.0064
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-glycyl-(S)-pipecolyl]-aziridine-2,3-dicarboxylate
-
-
0.0158
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-glycyl-(S)-prolyl]aziridine-2,3-dicarboxylate
-
-
0.0024
(2S,3S)-diethyl-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(R)-nipecotyl]aziridine-2,3-dicarboxylate
-
-
0.0024
(2S,3S)-diethyl-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(S)-nipecotyl]aziridine-2,3-dicarboxylate
-
-
0.0077
(2S,3S)-diethyl-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(S)-prolyl]aziridine-2,3-dicarboxylate
-
-
0.0079
(2S,3S+2R,3R)-dibenzyl-1-[desthiobiotinyl-6-aminohexanoyl]-aziridine-2,3-dicarboxylate
-
-
0.0053
(E)N-[(S)1-[(S)2-cyano-1-pyrrolidinecarbonyl]-3-methylbutyl]-2,3-diphenylacrylamide
-
23°C, pH 6.0
0.023
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([2-methyl-4-[(methylsulfonyl)amino]phenyl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.002
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([3-methyl-4-[(methylsulfonyl)amino]phenyl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.0023
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([3-methyl-4-[(phenylsulfonyl)amino]phenyl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.0025
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([3-[(methylsulfonyl)amino]phenyl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.012
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([4-[(methylsulfonyl)amino]phenyl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.011
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([4-[(phenylsulfonyl)amino]phenyl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.013
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([4-[(pyridin-2-ylsulfonyl)amino]phenyl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.014
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([4-[(pyridin-3-ylsulfonyl)amino]phenyl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.013
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([4-[(pyridin-4-ylsulfonyl)amino]phenyl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.013
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([4-[(thiophen-2-ylsulfonyl)amino]phenyl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.011
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([4-[methyl(methylsulfonyl)amino]phenyl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.014
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([6-[(methylsulfonyl)amino]pyridin-3-yl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.031
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([6-[(phenylsulfonyl)amino]pyridin-3-yl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.016
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-2-([[4-([[(dimethylamino)methyl]sulfonyl]amino)phenyl]carbonyl]amino)-3-(1-methylcyclopentyl)propanoyl]amino]-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.029
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-2-[([2-methoxy-4-[(methylsulfonyl)amino]phenyl]carbonyl)amino]-3-(1-methylcyclopentyl)propanoyl]amino]-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.0078
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-2-[([3-fluoro-4-[(methylsulfonyl)amino]phenyl]carbonyl)amino]-3-(1-methylcyclopentyl)propanoyl]amino]-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.0072
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-2-[([3-methoxy-4-[(methylsulfonyl)amino]phenyl]carbonyl)amino]-3-(1-methylcyclopentyl)propanoyl]amino]-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.017
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-2-[([4-[(ethylsulfonyl)amino]phenyl]carbonyl)amino]-3-(1-methylcyclopentyl)propanoyl]amino]-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.016
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-2-[[(4-[[(2,4-dimethyl-1,3-thiazol-5-yl)sulfonyl]amino]phenyl)carbonyl]amino]-3-(1-methylcyclopentyl)propanoyl]amino]-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.011
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-2-[[(4-[[(2-fluorophenyl)sulfonyl]amino]phenyl)carbonyl]amino]-3-(1-methylcyclopentyl)propanoyl]amino]-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.0078
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-2-[[(4-[[(3-fluorophenyl)sulfonyl]amino]phenyl)carbonyl]amino]-3-(1-methylcyclopentyl)propanoyl]amino]-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.014
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-2-[[(4-[[(3-methoxyphenyl)sulfonyl]amino]phenyl)carbonyl]amino]-3-(1-methylcyclopentyl)propanoyl]amino]-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.0059
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-2-[[(4-[[(4-fluorophenyl)sulfonyl]amino]phenyl)carbonyl]amino]-3-(1-methylcyclopentyl)propanoyl]amino]-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.011
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-2-[[(4-[[(4-methoxyphenyl)sulfonyl]amino]phenyl)carbonyl]amino]-3-(1-methylcyclopentyl)propanoyl]amino]-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.015
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-3-(1-methylcyclopentyl)-2-([[4-(methylsulfamoyl)phenyl]carbonyl]amino)propanoyl]amino]-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.0091
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-3-(1-methylcyclopentyl)-2-([[4-([[4-(1-methylethyl)-1,3-thiazol-2-yl]sulfonyl]amino)phenyl]carbonyl]amino)propanoyl]amino]-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.027
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-3-(1-methylcyclopentyl)-2-[[(4-sulfamoylphenyl)carbonyl]amino]propanoyl]amino]-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.024
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-3-(1-methylcyclopentyl)-2-[[(4-[[(1-methyl-1H-imidazol-2-yl)sulfonyl]amino]phenyl)carbonyl]amino]propanoyl]amino]-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.015
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-3-(1-methylcyclopentyl)-2-[[(4-[[(1-methylethyl)sulfonyl]amino]phenyl)carbonyl]amino]propanoyl]amino]-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.015
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-3-(1-methylcyclopentyl)-2-[[(4-[[(2,2,2-trifluoroethyl)sulfonyl]amino]phenyl)carbonyl]amino]propanoyl]amino]-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.0084
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-3-(1-methylcyclopentyl)-2-[[(4-[[(2-methylphenyl)sulfonyl]amino]phenyl)carbonyl]amino]propanoyl]amino]-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.027
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-3-(1-methylcyclopentyl)-2-[[(4-[[(4-methyl-1,3-thiazol-2-yl)sulfonyl]amino]phenyl)carbonyl]amino]propanoyl]amino]-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.0087
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-3-(1-methylcyclopentyl)-2-[[(4-[[(4-methylpyridin-3-yl)sulfonyl]amino]phenyl)carbonyl]amino]propanoyl]amino]-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.017
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-3-(1-methylcyclopentyl)-2-[[(4-[[(5-methyl-1,3-thiazol-2-yl)sulfonyl]amino]phenyl)carbonyl]amino]propanoyl]amino]-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.01
1,4-anhydro-3,5,6-trideoxy-3-[[4-methyl-N-(thiophen-3-ylcarbonyl)-L-leucyl]amino]-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.00097
1,4-anhydro-3-[[(2S)-2-[([3-chloro-4-[(methylsulfonyl)amino]phenyl]carbonyl)amino]-3-(1-methylcyclopentyl)propanoyl]amino]-3,5,6-trideoxy-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.0011
1,4-anhydro-3-[[(2S)-2-[([3-chloro-4-[(phenylsulfonyl)amino]phenyl]carbonyl)amino]-3-(1-methylcyclopentyl)propanoyl]amino]-3,5,6-trideoxy-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.015
1,4-anhydro-3-[[(2S)-2-[([4-[(benzylsulfonyl)amino]phenyl]carbonyl)amino]-3-(1-methylcyclopentyl)propanoyl]amino]-3,5,6-trideoxy-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.021
1,4-anhydro-3-[[(2S)-2-[([4-[(butylsulfonyl)amino]phenyl]carbonyl)amino]-3-(1-methylcyclopentyl)propanoyl]amino]-3,5,6-trideoxy-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.012
1,4-anhydro-3-[[(2S)-2-[([4-[(cyclopropylsulfonyl)amino]phenyl]carbonyl)amino]-3-(1-methylcyclopentyl)propanoyl]amino]-3,5,6-trideoxy-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.023
1,4-anhydro-3-[[(2S)-2-[[(4-[[(2-chloropyridin-3-yl)sulfonyl]amino]phenyl)carbonyl]amino]-3-(1-methylcyclopentyl)propanoyl]amino]-3,5,6-trideoxy-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.0085
1,4-anhydro-3-[[(2S)-2-[[(4-[[(2-cyanophenyl)sulfonyl]amino]phenyl)carbonyl]amino]-3-(1-methylcyclopentyl)propanoyl]amino]-3,5,6-trideoxy-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.0068
1,4-anhydro-3-[[(2S)-2-[[(4-[[(3-cyanophenyl)sulfonyl]amino]phenyl)carbonyl]amino]-3-(1-methylcyclopentyl)propanoyl]amino]-3,5,6-trideoxy-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.0079
1,4-anhydro-3-[[(2S)-2-[[(4-[[(4-cyanophenyl)sulfonyl]amino]phenyl)carbonyl]amino]-3-(1-methylcyclopentyl)propanoyl]amino]-3,5,6-trideoxy-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.064
1,4-anhydro-3-[[(2S)-2-[[(4-[[(cyclohexylmethyl)sulfonyl]amino]phenyl)carbonyl]amino]-3-(1-methylcyclopentyl)propanoyl]amino]-3,5,6-trideoxy-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.00923
3-(hydroxyimino)masticadienoic acid
-
at pH 5.5 and 37°C
0.002
3-(hydroxyimino)oleanolic acid
-
at pH 5.5 and 37°C
0.0195
3-epiursolic acid
-
at pH 5.5 and 37°C
0.0095
3-[[(2S)-2-[([3-acetyl-4-[(methylsulfonyl)amino]phenyl]carbonyl)amino]-3-(1-methylcyclopentyl)propanoyl]amino]-1,4-anhydro-3,5,6-trideoxy-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.0091
3-[[(2S)-2-[[(4-[[(4-aminophenyl)sulfonyl]amino]phenyl)carbonyl]amino]-3-(1-methylcyclopentyl)propanoyl]amino]-1,4-anhydro-3,5,6-trideoxy-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.00000057
benzofuran-2-carboxylic acid ((S)-1-[3-oxo-1-(pyridine-2-sulfonyl)azepan-4-ylcarbamoyl]-2-naphthylen-2-yl)amide
-
-
0.0000017
benzofuran-2-carboxylic acid ((S)-1-[3-oxo-1-(pyridine-2-sulfonyl)azepan-4-ylcarbamoyl]-2-phenyl-ethyl)amide
-
-
0.0026
benzyl [(2S)-1-[[(2S)-1,6-diamino-1-oxohexan-2-yl]amino]-1-oxo-3-(1,1':4',1''-terphenyl-4-yl)propan-2-yl]carbamate
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.023
benzyl [(2S)-1-[[(2S)-1,6-diamino-1-oxohexan-2-yl]amino]-3-(2'-methylbiphenyl-4-yl)-1-oxopropan-2-yl]carbamate
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.0025
benzyl [(2S)-1-[[(2S)-1,6-diamino-1-oxohexan-2-yl]amino]-3-(3'-methylbiphenyl-4-yl)-1-oxopropan-2-yl]carbamate
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.0017
benzyl [(2S)-1-[[(2S)-1,6-diamino-1-oxohexan-2-yl]amino]-3-(4'-methylbiphenyl-4-yl)-1-oxopropan-2-yl]carbamate
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.0018
benzyl [(2S)-3-(3'-aminobiphenyl-4-yl)-1-[[(2S)-1,6-diamino-1-oxohexan-2-yl]amino]-1-oxopropan-2-yl]carbamate
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.0017
benzyl [(2S)-3-(3'-chlorobiphenyl-4-yl)-1-[[(2S)-1,6-diamino-1-oxohexan-2-yl]amino]-1-oxopropan-2-yl]carbamate
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.0024
benzyl [(2S)-3-(biphenyl-4-yl)-1-[[(2S)-1,6-diamino-1-oxohexan-2-yl]amino]-1-oxopropan-2-yl]carbamate
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.0000026
cathepsin K propeptide
-
pH 5.5, room temperature
-
0.00000012
cathepsin L propeptide
-
pH 5.5, room temperature
-
0.00000046
cathepsin S propeptide
-
pH 5.5, room temperature
-
0.0000000073
chagasin
-
-
-
0.0000022
chagasin mutant deltaT31-T32
-
-
-
0.000000045
chagasin mutant P30A
-
-
-
0.0000000039
chagasin mutant T31A
-
-
-
0.0000000018
chagasin mutant T31A/T32A
-
-
-
0.0000000049
chagasin mutant T31S
-
-
-
0.0000000097
chagasin mutant T31V
-
-
-
0.0000000068
chagasin mutant T31Y
-
-
-
0.000000014
chagasin mutant T32A
-
-
-
0.000000032
chagasin mutant T32S
-
-
-
0.00000002
chagasin mutant T32V
-
-
-
0.0000000027
chagasin mutant T32Y
-
-
-
0.000000825
chagasin mutant W93A
-
-
-
0.00000005
cystatin A, cystatin B
-
0.1 M acetate pH 5.5, 1 mM EDTA, 2 mM dithiothreitol, 100 mg/ml bovine serum albumin, 10 min
-
0.00000008
cystatin C
-
0.1 M acetate pH 5.5, 1 mM EDTA, 2 mM dithiothreitol, 100 mg/ml bovine serum albumin, 10 min
-
0.00000281
cystatin D
-
0.1 M acetate pH 5.5, 1 mM EDTA, 2 mM dithiothreitol, 100 mg/ml bovine serum albumin, 10 min
-
0.00000049
cystatin F
-
0.1 M acetate pH 5.5, 1 mM EDTA, 2 mM dithiothreitol, 100 mg/ml bovine serum albumin, 10 min
-
0.00000178
cystatin M/E
-
0.1 M acetate pH 5.5, 1 mM EDTA, 2 mM dithiothreitol, 100 mg/ml bovine serum albumin, 10 min
-
0.0000000101
fragment p41 of major histocompatibility complex class II-associated invariant chain
pH 6.0, 25°C
-
0.02
N-(2,6-dimethylbenzoyl)-L-phenylalanyl-L-lysinamide
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.0027
N-(2-chloro-5-nitrobenzoyl)-L-phenylalanyl-L-lysinamide
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.0032
N-(3-phenylpropanoyl)-L-phenylalanyl-L-lysinamide
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.0043
N-(4-biphenylacetyl)-S-methylcysteine-(D)-Arg-Phe-beta-phenethylamide
-
wild type enzyme
0.0023
N-(4-bromobenzoyl)-L-phenylalanyl-L-lysinamide
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.009
N-(biphenyl-4-ylcarbonyl)-L-phenylalanyl-L-lysinamide
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.0078
N-(cyclopent-1-en-1-ylcarbonyl)-L-phenylalanyl-L-lysinamide
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.001
N-(naphthalen-2-ylcarbonyl)-L-phenylalanyl-L-lysinamide
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.0068
N-(pentafluorobenzoyl)-L-phenylalanyl-L-lysinamide
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.0061
N-(piperidin-2-ylcarbonyl)-L-phenylalanyl-L-lysinamide
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.0055
N-(pyridin-2-ylcarbonyl)-L-phenylalanyl-L-lysinamide
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.007
N-[(2R)-2-[(2-amino-2-oxoethyl)amino]-2-[[(benzyloxy)carbonyl]amino]acetyl]-L-phenylalanyl-L-lysinamide
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.00089
N-[(2R)-2-[(3-aminopropyl)amino]-2-[[(benzyloxy)carbonyl]amino]acetyl]-L-phenylalanyl-L-lysinamide
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.00039
N-[(2R)-2-[[(benzyloxy)carbonyl]amino]-2-(3a,7a-dihydro-1H-indol-3-ylamino)acetyl]-L-phenylalanyl-L-lysinamide
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.00045
N-[(2R)-2-[[(benzyloxy)carbonyl]amino]-2-(propan-2-ylamino)acetyl]-L-phenylalanyl-L-lysinamide
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.00074
N-[(2R)-2-[[(benzyloxy)carbonyl]amino]-2-[(2-carbamimidamidoethyl)amino]acetyl]-L-phenylalanyl-L-lysinamide
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.0046
N-[(4'-carboxy-2,2'-bipyridin-4-yl)carbonyl]-L-phenylalanyl-L-lysinamide
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.005
N-[(6-aminopyridin-3-yl)carbonyl]-L-phenylalanyl-L-lysinamide
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.0031
N-[(benzyloxy)carbonyl]-3-(1H-indazol-1-yl)-L-alanyl-L-lysinamide
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.0042
N-[(benzyloxy)carbonyl]-3-(1H-indol-1-yl)-L-alanyl-L-lysinamide
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.00012
N-[(benzyloxy)carbonyl]-4-(thiophen-2-yl)-L-phenylalanyl-L-lysinamide
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.014
N-[(benzyloxy)carbonyl]-L-phenylalanyl-3-(1H-imidazol-1-yl)-L-alaninamide
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.026
N-[(benzyloxy)carbonyl]-L-phenylalanyl-4-amino-L-phenylalaninamide
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.027
N-[(benzyloxy)carbonyl]-L-phenylalanyl-6-hydroxy-L-lysinamide
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.016
N-[(benzyloxy)carbonyl]-L-phenylalanyl-L-alaninamide
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.028
N-[(benzyloxy)carbonyl]-L-phenylalanyl-L-argininamide
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.014
N-[(benzyloxy)carbonyl]-L-phenylalanyl-L-leucinamide
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.0042
N-[(benzyloxy)carbonyl]-L-phenylalanyl-L-lysinamide
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.064
N-[(benzyloxy)carbonyl]-L-phenylalanyl-L-methioninamide
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.0035
N-[(benzyloxy)carbonyl]-L-phenylalanyl-L-ornithinamide
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.017
N-[(benzyloxy)carbonyl]-L-phenylalanyl-L-valinamide
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.0026
N-[(benzyloxy)carbonyl]-L-phenylalanyl-N6-methyl-L-lysinamide
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.0014
N-[(benzyloxy)carbonyl]-L-tyrosyl-L-lysinamide
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.0025
N-[3-(4-hydroxyphenyl)propanoyl]-L-phenylalanyl-L-lysinamide
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.0024
N-[3-(acetyloxy)benzoyl]-L-phenylalanyl-L-lysinamide
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.0026
N-[4-(acetyloxy)benzoyl]-L-phenylalanyl-L-lysinamide
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.0029
N-[4-(dimethylamino)benzoyl]-L-phenylalanyl-L-lysinamide
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.001
N-[4-(trifluoromethyl)benzoyl]-L-phenylalanyl-L-lysinamide
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.028
Nalpha-[(benzyloxy)carbonyl]-N-[(1R)-1,2-diamino-2-oxoethyl]-L-phenylalaninamide
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.00000043
naphthalene-2-carboxylic acid ((S)-2-naphthalen-2-yl-1-[(S)-3-oxo-1-(pyridine-2-sulfonyl)azepan-4-ylcarbamoyl]ethyl)amide
-
-
0.0000014
naphthoic-1-carboxylic acid ((S)-1-[3-oxo-1-(pyridine-2-sulfonyl)azepan-4-ylcarbamoyl]-3-methyl-butyl)amide
-
-
0.0095
ortho-aminobenzoic acid-LFEKQ-N-[2,4-dinitrophenyl]ethylenediamine
-
at 37°C, in 0.1 M sodium acetate buffer, pH 5.5
0.005
ortho-aminobenzoic acid-VLFEKKQ-N-[2,4-dinitrophenyl]ethylenediamine
-
at 37°C, in 0.1 M sodium acetate buffer, pH 5.5
0.0002
ortho-aminobenzoic acid-VLFEKKVYLQ-N-[2,4-dinitrophenyl]ethylenediamine
-
at 37°C, in 0.1 M sodium acetate buffer, pH 5.5
0.01
ortho-aminobenzoic acid-VLFEKQ-N-[2,4-dinitrophenyl]ethylenediamine
-
at 37°C, in 0.1 M sodium acetate buffer, pH 5.5
0.000005
quinoline-2-carboxylic acid ((S)-1-[3-oxo-1-(pyridine-2-sulfonyl)azepan-4-ylcarbamoyl]-3-methyl-butyl)amide
-
-
0.0000082
quinoline-8-carboxylic acid ((S)-1-[3-oxo-1-(pyridine-2-sulfonyl)azepan-4-ylcarbamoyl]-3-methyl-butyl)amide
-
-
0.00013
RKLLW-NH2
-
pH 5.5, 37°C
0.0000007
testican-1
-
-
-
0.00000014
thyroglobulin type-1 domain
-
0.1 M sodium acetate, 1 mM EDTA, 24°C
-
additional information
additional information
-
0.00000000552
p41-fragment-human
wild-type, substrate: benzyloxycarbonyl-Phe-Arg-4-methylcoumarin-7-amide, production rate of 7-amino-4-methylcoumarin measured, excitation and emission wavelengths of 370 and 460 nm, pseudo first order reaction conditions (inhibitor concentration at least 10-fold higher than enzyme concentration)
-
0.0000000101
p41-fragment-human
G139R mutant, substrate: benzyloxycarbonyl-Phe-Arg-4-methylcoumarin-7-amide, production rate of 7-amino-4-methylcoumarin measured, excitation and emission wavelengths of 370 and 460 nm, pseudo first order reaction conditions (inhibitor concentration at least 10-fold higher than enzyme concentration)
-
additional information
additional information
inhibition kinetics of collagen with cathepsin L, overview
-
additional information
additional information
-
inhibition kinetics of collagen with cathepsin L, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.01
(2-fluorobenzophenone) thiosemicarbazone
Homo sapiens
above, pH 6.0, 37°C
0.000574
(2E)-2-(6-bromo-1,1-dioxido-2,3-dihydro-4H-thiochromen-4-ylidene)hydrazinecarbothioamide
Homo sapiens
pH 6.0, 37°C
0.000152
(2E)-2-(6-bromo-2,3-dihydro-4H-thiochromen-4-ylidene)hydrazinecarbothioamide
Homo sapiens
pH 6.0, 37°C
0.000164
(2E)-2-(6-bromo-2,3-dihydroquinolin-4(1H)-ylidene)hydrazinecarbothioamide
Homo sapiens
pH 6.0, 37°C
0.000068
(2E)-2-(6-nitro-2,3-dihydro-4H-thiochromen-4-ylidene)hydrazinecarbothioamide
Homo sapiens
pH 6.0, 37°C
0.01
(2E)-2-[6-(propan-2-yloxy)-2,3-dihydro-4H-thiochromen-4-ylidene]hydrazinecarbothioamide
Homo sapiens
above, pH 6.0, 37°C
0.0000305
(3-bromo-2'-fluoro-3'-hydroxybenzophenone) thiosemicarbazone
Homo sapiens
pH 6.0, 37°C
0.0001314
(3-bromo-3'-hydroxybenzophenone) thiosemicarbazone
Homo sapiens
pH 6.0, 37°C
0.01
(3-hydroxybenzophenone) thiosemicarbazone
Homo sapiens
above, pH 6.0, 37°C
0.00222
(4-bromo-2'-fluoro-3'-hydroxybenzophenone) thiosemicarbazone
Homo sapiens
pH 6.0, 37°C
0.000056
1,3,5-trisbenzoylbenzene thiosemicarbazone
Homo sapiens
pH 6.0, 37°C
0.0000081
1,3-bis(2-fluorobenzoyl)-5-bromobenzene thiosemicarbazone
Homo sapiens
pH 6.0, 37°C
0.01035
1,3-bis(3-bromobenzoyl)-5-bromobenzene thiosemicarbazone
Homo sapiens
pH 6.0, 37°C
0.01
1,3-bis(3-bromobenzoyl)-5-hydroxybenzene thiosemicarbazone
Homo sapiens
pH 6.0, 37°C
0.0000716
1,3-bis(3-hydroxybenzoyl)-5-bromobenzene thiosemicarbazone
Homo sapiens
pH 6.0, 37°C
0.000654
1,3-bis(3-methylbenzoyl)benzene thisosemicarbazone
Homo sapiens
pH 6.0, 37°C
0.01
1,3-bis(4-bromobenzoyl)benzene bis-thiosemicarbazone
Homo sapiens
above, pH 6.0, 37°C
0.001522
1,3-bis(4-bromobenzoyl)benzene thiosemicarbazone
Homo sapiens
pH 6.0, 37°C
0.0000144
1,3-bis(4-fluorobenzoyl)benzene thiosemicarbazone
Homo sapiens
pH 6.0, 37°C
0.00034
1,3-bis(4-hydroxybenzoyl)benzene thiosemicarbazone
Homo sapiens
pH 6.0, 37°C
0.01
1,3-bis(4-isopropoxybenzoyl)benzene thiosemicarbazone
Homo sapiens
above, pH 6.0, 37°C
0.005117
1,3-bis(4-methoxybenzoyl)benzene thiosemicarbazone
Homo sapiens
pH 6.0, 37°C
0.109
2,6-dimethoxy-4-[4-(4-phenoxyphenyl)-5-phenyl-1H-imidazol-2-yl]phenol
Homo sapiens
pH 7.4, 37°C
0.087
2,6-dimethoxy-4-[5-phenyl-4-[4-(phenylsulfanyl)phenyl]-1H-imidazol-2-yl]phenol
Homo sapiens
pH 7.4, 37°C
0.0808
2-(1,3-benzodioxol-5-yl)-5-phenyl-4-[4-(phenylsulfanyl)phenyl]-1H-imidazole
Homo sapiens
pH 7.4, 37°C
0.0863
2-(3,4-dimethoxyphenyl)-5-phenyl-4-[4-(phenylsulfanyl)phenyl]-1H-imidazole
Homo sapiens
pH 7.4, 37°C
0.074
2-(4-methoxyphenyl)-4-[8-[2-(4-methoxyphenyl)-4-phenyl-1H-imidazol-5-yl]dibenzo[b,d]furan-2-yl]-5-phenyl-1H-imidazole
Homo sapiens
pH 7.4, 37°C
0.0818
2-(4-methoxyphenyl)-5-phenyl-4-[4-(phenylsulfanyl)phenyl]-1H-imidazole
Homo sapiens
pH 7.4, 37°C
0.0927
2-(acetylamino)-N-[4-(6-[[2-(acetylamino)benzoyl]amino]-1H-benzimidazol-2-yl)phenyl]benzamide
Homo sapiens
pH 7.4, 37°C
0.0402
2-(furan-2-yl)-4-[8-[2-(furan-2-yl)-4-phenyl-1H-imidazol-5-yl]dibenzo[b,d]furan-2-yl]-5-phenyl-1H-imidazole
Homo sapiens
pH 7.4, 37°C
0.0012
2-cyano-4-(2-hydroxyethoxy)-N-methyl-6-[(spiro[3.5]non-7-ylmethyl)amino]pyrimidine-5-carboxamide
Homo sapiens
determined by a fluorometric assay with recombinant catL employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
0.0011
2-cyano-4-(cyclohexylamino)-N-(2-phenylethyl)pyrimidine-5-carboxamide
Homo sapiens
inhibition are determined by a fluorometric assay with recombinant Cat L
0.00078
2-cyano-4-(cyclohexylmethoxy)-N-(2-phenylethyl)pyrimidine-5-carboxamide
Homo sapiens
inhibition are determined by a fluorometric assay with recombinant Cat L
0.000426
2-cyano-4-[(1,4-dioxaspiro[4.5]dec-8-ylmethyl)amino]-N-methyl-6-[(1-methylpiperidin-4-yl)methoxy]pyrimidine-5-carboxamide
Homo sapiens
determined by a fluorometric assay with recombinant catL employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
0.0004
2-cyano-4-[(2-cyclopentylethyl)amino]-N-methyl-6-[(1-methylpiperidin-4-yl)methoxy]pyrimidine-5-carboxamide
Homo sapiens
determined by a fluorometric assay with recombinant catL employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
0.002
2-cyano-4-[(cyclohexylmethyl)(methyl)amino]-N-(2-phenylethyl)pyrimidine-5-carboxamide
Homo sapiens
inhibition are determined by a fluorometric assay with recombinant Cat L
0.00001
2-cyano-4-[2-(1-methylpiperidin-4-yl)ethoxy]-N-(2-phenylethyl)-6-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
Homo sapiens
inhibition are determined by a fluorometric assay with recombinant Cat L
0.0003
2-cyano-4-[[1-(2-hydroxyethyl)piperidin-4-yl]methoxy]-N-methyl-6-[(spiro[3.5]non-7-ylmethyl)amino]pyrimidine-5-carboxamide
Homo sapiens
determined by a fluorometric assay with recombinant catL employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
0.00051
2-cyano-N-(1-methyl-4-phenylpiperidin-4-yl)-4-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
Homo sapiens
inhibition are determined by a fluorometric assay with recombinant Cat L
0.00046
2-cyano-N-methyl-4-(piperidin-4-ylmethoxy)-6-[(spiro[3.5]non-7-ylmethyl)amino]pyrimidine-5-carboxamide
Homo sapiens
determined by a fluorometric assay with recombinant catL employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
0.00036
2-cyano-N-methyl-4-[(1-methylpiperidin-4-yl)methoxy]-6-[(spiro[3.5]non-7-ylmethyl)amino]pyrimidine-5-carboxamide
Homo sapiens
determined by a fluorometric assay with recombinant catL employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
0.000276
2-cyano-N-methyl-4-[(1-methylpiperidin-4-yl)methoxy]-6-[(spiro[4.5]dec-8-ylmethyl)amino]pyrimidine-5-carboxamide
Homo sapiens
determined by a fluorometric assay with recombinant catL employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
0.00139
2-cyano-N-methyl-4-[(spiro[3.5]non-7-ylmethyl)amino]-6-[(2,2,6,6-tetramethylpiperidin-4-yl)oxy]pyrimidine-5-carboxamide
Homo sapiens
determined by a fluorometric assay with recombinant catL employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
0.00012
2-cyano-N-methyl-4-[2-(1-methylpiperidin-4-yl)ethoxy]-6-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
0.00044
2-cyano-N-methyl-4-[2-(1-methylpiperidin-4-yl)ethoxy]-6-[(spiro[3.5]non-7-ylmethyl)amino]pyrimidine-5-carboxamide
Homo sapiens
determined by a fluorometric assay with recombinant catL employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
0.00033
2-cyano-N-methyl-4-[[1-(1-methylethyl)piperidin-4-yl]methoxy]-6-[(spiro[3.5]non-7-ylmethyl)amino]pyrimidine-5-carboxamide
Homo sapiens
determined by a fluorometric assay with recombinant catL employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
0.0007
2-cyano-N-[(1-methyl-4-phenylpiperidin-4-yl)methyl]-4-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
Homo sapiens
inhibition are determined by a fluorometric assay with recombinant Cat L
0.00048
2-cyano-N-[(1R)-2-pyridin-2-yl-1-(pyrrolidin-1-ylmethyl)ethyl]-4-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
Homo sapiens
inhibition are determined by a fluorometric assay with recombinant Cat L
0.00084
2-cyano-N-[5-[(1-methylpiperidin-4-yl)oxy]biphenyl-2-yl]-4-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
Homo sapiens
inhibition are determined by a fluorometric assay with recombinant Cat L
0.000007
2-[(2S)-2-[(tert-butoxycarbonyl)amino]-3-(1H-indol-3-yl)propanoyl]hydrazinecarboxylic 3,4-dihydroquinoline-1(2H)-carboxylic anhydride
Homo sapiens
in 1 mM EDTA, 5 mM cysteine at pH 5.5
0.0000238
3-benzoylbenzhydrol thiosemicarbazone
Homo sapiens
pH 6.0, 37°C
0.0847
4,4'-[methanediylbis(1H-benzimidazole-5,2-diyl)]dianiline
Homo sapiens
pH 7.4, 37°C
0.0865
4-(4-[8-[2-(4-carboxyphenyl)-4-phenyl-1H-imidazol-5-yl]dibenzo[b,d]furan-2-yl]-5-phenyl-1H-imidazol-2-yl)benzoic acid
Homo sapiens
pH 7.4, 37°C
0.0621
4-(4-[8-[2-(4-hydroxyphenyl)-4-phenyl-1H-imidazol-5-yl]dibenzo[b,d]furan-2-yl]-5-phenyl-1H-imidazol-2-yl)phenol
Homo sapiens
pH 7.4, 37°C
0.0834
4-amino-N-(4-[6-[(4-aminobenzoyl)amino]-1H-benzimidazol-2-yl]phenyl)benzamide
Homo sapiens
pH 7.4, 37°C
0.0025
4-[(1-acetylpiperidin-4-yl)methoxy]-2-cyano-N-methyl-6-[(spiro[3.5]non-7-ylmethyl)amino]pyrimidine-5-carboxamide
Homo sapiens
determined by a fluorometric assay with recombinant catL employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
0.0922
4-[(E)-benzylideneamino]-N-[4-[6-([4-[(E)-benzylideneamino]benzoyl]amino)-1H-benzimidazol-2-yl]phenyl]benzamide
Homo sapiens
pH 7.4, 37°C
0.00087
4-[2-(1-methylpiperidin-4-yl)ethoxy]-6-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-2-carbonitrile
Homo sapiens
inhibition are determined by a fluorometric assay with recombinant Cat L
0.08835
4-[4-(5,5-dioxidodibenzo[b,d]thiophen-2-yl)-5-phenyl-1H-imidazol-2-yl]-2,6-dimethoxyphenol
Homo sapiens
pH 7.4, 37°C
0.0997
4-[5-phenyl-4-[4-(phenylsulfanyl)phenyl]-1H-imidazol-2-yl]phenol
Homo sapiens
pH 7.4, 37°C
0.0655
4-[8-(2,4-diphenyl-1H-imidazol-5-yl)dibenzo[b,d]furan-2-yl]-2,5-diphenyl-1H-imidazole)
Homo sapiens
pH 7.4, 37°C
0.00028
5-bromo-4-[2-(1-methylpiperidin-4-yl)ethoxy]-6-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-2-carbonitrile
Homo sapiens
inhibition are determined by a fluorometric assay with recombinant Cat L
0.0981
5-phenyl-4-[4-(phenylsulfanyl)phenyl]-2-(2,4,5-trimethoxyphenyl)-1H-imidazole
Homo sapiens
pH 7.4, 37°C
0.0888
5-phenyl-4-[4-(phenylsulfanyl)phenyl]-2-(3,4,5-trimethoxyphenyl)-1H-imidazole
Homo sapiens
pH 7.4, 37°C
0.01
benzophenone thiosemicarbazone
Homo sapiens
above, pH 6.0, 37°C
0.0000099
benzoylbenzophenone thiosemicarbazone
Homo sapiens
pH 6.0, 37°C
0.0972
bis[2-(4-aminophenyl)-1H-benzimidazol-5-yl]methanone
Homo sapiens
pH 7.4, 37°C
0.000056
cathepsin L inhibitor 1
Homo sapiens
thiocarbazate cathepsin L inhibitor, 20 mM sodium acetate, 1 mM EDTA, 5 mM cysteine at pH 5.5
0.00018
N-(4-benzyl-1-methylpiperidin-4-yl)-2-cyano-4-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
Homo sapiens
inhibition are determined by a fluorometric assay with recombinant Cat L
0.000064
N-benzyl-2-cyano-4-[(1-methylpiperidin-4-yl)methoxy]-6-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
Homo sapiens
inhibition are determined by a fluorometric assay with recombinant Cat L
0.0001
N-benzyl-2-cyano-4-[(1-methylpiperidin-4-yl)oxy]-6-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
Homo sapiens
inhibition are determined by a fluorometric assay with recombinant Cat L
0.00027
N-benzyl-2-cyano-4-[2-(1-methylpiperidin-4-yl)ethoxy]-6-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
Homo sapiens
inhibition are determined by a fluorometric assay with recombinant Cat L
0.00015
N-[(1R)-1-benzyl-2-pyrrolidin-1-ylethyl]-2-cyano-4-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
Homo sapiens
inhibition are determined by a fluorometric assay with recombinant Cat L
0.00084
N-[(1R)-1-benzyl-2-pyrrolidin-1-ylpropyl]-2-cyano-4-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
Homo sapiens
inhibition are determined by a fluorometric assay with recombinant Cat L
0.0015
N-[(1S)-1-benzyl-2-pyrrolidin-1-ylethyl]-2-cyano-4-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
Homo sapiens
inhibition are determined by a fluorometric assay with recombinant Cat L
0.0625
N-[4-(1H-benzimidazol-2-yl)phenyl]-2,2-diphenylacetamide
Homo sapiens
pH 7.4, 37°C
0.0862
N-[4-(5-benzoyl-1H-benzimidazol-2-yl)phenyl]-2-chlorobenzamide
Homo sapiens
pH 7.4, 37°C
0.033
S-{2-[(2-ethylphenyl)amino]-2-oxoethyl} 2-[(2R)-2-[(tert-butoxycarbonyl)amino]-3-(1H-indol-3-yl)propanoyl]hydrazinecarbothioate
Homo sapiens
thiocarbazate cathepsin L inhibitor, 1 mM EDTA, 5 mM cysteine at pH 5.5
0.0082
(13alpha,17alpha,20S,24Z)-3-hydroxylanosta-7,24-dien-26-oic acid
Homo sapiens
-
at pH 5.5 and 37°C
0.0091
(13alpha,17alpha,20S,24Z)-3-oxolanosta-7,24-dien-26-oic acid
Homo sapiens
-
at pH 5.5 and 37°C
0.00246
(2E)-2-[(2-fluorophenyl)(4-fluorophenyl)methylidene]hydrazinecarbothioamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000118
(2E)-2-[(3-bromophenyl)(3,4,5-trifluorophenyl)methylidene]hydrazinecarbothioamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000415
(2E)-2-[(3-bromophenyl)(3,5-dichlorophenyl)methylidene]hydrazinecarbothioamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000594
(2E)-2-[(3-bromophenyl)(3,5-difluorophenyl)methylidene]hydrazinecarbothioamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000131
(2E)-2-[(3-bromophenyl)(3-chlorophenyl)methylidene]hydrazinecarbothioamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00025
(2E)-2-[(3-bromophenyl)(3-fluorophenyl)methylidene]hydrazinecarbothioamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000224
(2E)-2-[(3-bromophenyl)(3-methylphenyl)methylidene]hydrazinecarbothioamide
Homo sapiens
-
pH and temperature not specified in the publication
0.01
(2E)-2-[(3-bromophenyl)(4-bromophenyl)methylidene]hydrazinecarbothioamide
Homo sapiens
-
IC50 above 0.01 mM, pH and temperature not specified in the publication
0.000327
(2E)-2-[(3-bromophenyl)(4-chlorophenyl)methylidene]hydrazinecarbothioamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000796
(2E)-2-[(3-bromophenyl)(4-fluorophenyl)methylidene]hydrazinecarbothioamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00216
(2E)-2-[(3-bromophenyl)(4-methylphenyl)methylidene]hydrazinecarbothioamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000465
(2E)-2-[(3-bromophenyl)[3-(trifluoromethyl)phenyl]methylidene]hydrazinecarbothioamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000521
(2E)-2-[(3-bromophenyl)[4-(trifluoromethyl)phenyl]methylidene]hydrazinecarbothioamide
Homo sapiens
-
pH and temperature not specified in the publication
0.01
(2E)-2-[(4-bromophenyl)(4-chlorophenyl)methylidene]hydrazinecarbothioamide
Homo sapiens
-
IC50 above 0.01 mM, pH and temperature not specified in the publication
0.00332
(2E)-2-[(4-bromophenyl)(4-fluorophenyl)methylidene]hydrazinecarbothioamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00457
(2E)-2-[(4-bromophenyl)(4-methylphenyl)methylidene]hydrazinecarbothioamide
Homo sapiens
-
pH and temperature not specified in the publication
0.01
(2E)-2-[(4-bromophenyl)[4-(trifluoromethyl)phenyl]methylidene]hydrazinecarbothioamide
Homo sapiens
-
IC50 above 0.01 mM, pH and temperature not specified in the publication
0.000096
(2E)-2-[[3,5-bis(trifluoromethyl)phenyl](3-bromophenyl)methylidene]hydrazinecarbothioamide
Homo sapiens
-
pH and temperature not specified in the publication
0.5
(2E)-[(3E)-28-methoxy-28-oxours-12-en-3-ylidene]acetic acid
Homo sapiens
-
IC50 above 0.5 mM, at pH 5.5 and 37°C
0.0026
(2Z)-2-[(2-bromophenyl)(3-bromophenyl)methylidene]hydrazinecarbothioamide
Homo sapiens
-
pH and temperature not specified in the publication
0.01
(2Z)-2-[(2-bromophenyl)(4-bromophenyl)methylidene]hydrazinecarbothioamide
Homo sapiens
-
IC50 above 0.01 mM, pH and temperature not specified in the publication
0.01
(2Z)-2-[(2-fluorophenyl)(phenyl)methylidene]hydrazinecarbothioamide
Homo sapiens
-
IC50 above 0.01 mM, pH and temperature not specified in the publication
0.000233
(2Z)-2-[(3-bromo-2-fluorophenyl)(3-bromophenyl)methylidene]hydrazinecarbothioamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000114
(2Z)-2-[(3-bromo-4-fluorophenyl)(3-bromophenyl)methylidene]hydrazinecarbothioamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000632
(2Z)-2-[(3-bromophenyl)(2,3,4,5-tetrafluorophenyl)methylidene]hydrazinecarbothioamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000838
(2Z)-2-[(3-bromophenyl)(2,3-difluorophenyl)methylidene]hydrazinecarbothioamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00061
(2Z)-2-[(3-bromophenyl)(2,6-difluorophenyl)methylidene]hydrazinecarbothioamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00161
(2Z)-2-[(3-bromophenyl)(2-chlorophenyl)methylidene]hydrazinecarbothioamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000305
(2Z)-2-[(3-bromophenyl)(2-fluorophenyl)methylidene]hydrazinecarbothioamide
Homo sapiens
-
pH and temperature not specified in the publication
0.01
(2Z)-2-[(3-bromophenyl)(2-methylphenyl)methylidene]hydrazinecarbothioamide
Homo sapiens
-
IC50 above 0.01 mM, pH and temperature not specified in the publication
0.00222
(2Z)-2-[(4-bromophenyl)(2-fluorophenyl)methylidene]hydrazinecarbothioamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0097
(3E)-3-(carboxymethylidene)olean-12-en-28-oic acid
Homo sapiens
-
at pH 5.5 and 37°C
0.0123
(3E)-3-(carboxymethylidene)urs-12-en-28-oic acid
Homo sapiens
-
at pH 5.5 and 37°C
0.00045
1,3-dihydro-pyrrolo[3,4-b]quinoline-2-carbonitrile
Homo sapiens
-
IC50: 0.00045 mM
0.00001
1-cyano-3-azetidinyl cyclohexylmethyl ether
Homo sapiens
-
IC50: 0.00001 mM
0.00043
1-cyanoazetidine
Homo sapiens
-
IC50: 0.00043 mM
0.004
1-cyanopyrrolidine
Homo sapiens
-
IC50: 0.004 mM
0.000007
2-(3,4-dihydroquinolin-1(2H)-yl)-2-oxoethyl 2-[(2S)-2-[(tert-butoxycarbonyl)amino]-3-(1H-indol-3-yl)propanoyl]hydrazinecarboxylate
Homo sapiens
-
-
0.01
2-[bis(3-bromophenyl)methylidene]-N-ethylhydrazinecarbothioamide
Homo sapiens
-
IC50 above 0.01 mM, pH and temperature not specified in the publication
0.01
2-[bis(3-bromophenyl)methylidene]-N-phenylhydrazinecarbothioamide
Homo sapiens
-
IC50 above 0.01 mM, pH and temperature not specified in the publication
0.00487
2-[bis(3-fluorophenyl)methylidene]hydrazinecarbothioamide
Homo sapiens
-
pH and temperature not specified in the publication
0.01
2-[bis(4-bromophenyl)methylidene]hydrazinecarbothioamide
Homo sapiens
-
IC50 above 0.01 mM, pH and temperature not specified in the publication
0.01
2-[bis(4-fluorophenyl)methylidene]hydrazinecarbothioamide
Homo sapiens
-
IC50 above 0.01 mM, pH and temperature not specified in the publication
0.00893
2-[cyclohexyl(methyl)amino]-4H-3,1-benzothiazin-4-one
Homo sapiens
-
37°C, pH 6.0
0.00001
3-(benzyloxy)-1-cyanoazetidine
Homo sapiens
-
IC50: 0.00001 mM
0.0026
3-(hydroxyimino)masticadienoic acid
Homo sapiens
-
at pH 5.5 and 37°C
0.0024
3-(hydroxyimino)oleanolic acid
Homo sapiens
-
at pH 5.5 and 37°C
0.0065
3-epiursolic acid
Homo sapiens
-
at pH 5.5 and 37°C
0.0072
3-hydroxyolean-12-en-28-oic acid
Homo sapiens
-
at pH 5.5 and 37°C
0.0395
3-hydroxyurs-12-en-28-oic acid
Homo sapiens
-
at pH 5.5 and 37°C
0.0147
3-oxoolean-12-en-28-oic acid
Homo sapiens
-
at pH 5.5 and 37°C
0.0083
3-oxours-12-en-28-oic acid
Homo sapiens
-
at pH 5.5 and 37°C
0.00015
3-[(benzyloxy)methyl]-1-cyanopyrrolidine
Homo sapiens
-
IC50: 0.00015 mM
0.000096
6-(4-chlorobenzyl)-7-(2,2-dimethylpropyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
inhibition profiles are determined by a fluorometric assay with recombinant CAT L employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
0.00084
6-(4-chlorobenzyl)-7-(2-cycloheptylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
inhibition profiles are determined by a fluorometric assay with recombinant CAT L employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
0.00032
6-(4-chlorobenzyl)-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
inhibition profiles are determined by a fluorometric assay with recombinant CAT L employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
0.00026
6-(4-chlorobenzyl)-7-(2-cyclopentylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
inhibition profiles are determined by a fluorometric assay with recombinant CAT L employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
0.000023
6-(4-chlorobenzyl)-7-(2-phenylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
inhibition profiles are determined by a fluorometric assay with recombinant CAT L employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
0.000018
6-(4-chlorobenzyl)-7-(3,3-dimethylbutyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
inhibition profiles are determined by a fluorometric assay with recombinant CAT L employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
0.00037
6-(4-chlorobenzyl)-7-(cyclohexylmethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
inhibition profiles are determined by a fluorometric assay with recombinant CAT L employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
0.00004
6-(4-chlorobenzyl)-7-[2-(3-chlorophenyl)ethyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
inhibition profiles are determined by a fluorometric assay with recombinant CAT L employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
0.000086
6-(4-chlorobenzyl)-7-[2-(4-chlorophenyl)ethyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
inhibition profiles are determined by a fluorometric assay with recombinant CAT L employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
0.0068
6-[[4-(4-acetylpiperazin-1-yl)-2-fluorophenoxy]methyl]-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
with Z-Phe-Arg-7-amido-4-methylcoumarin as substrate
0.0052
6-[[4-(4-acetylpiperazin-1-yl)phenoxy]methyl]-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
with Z-Phe-Arg-7-amido-4-methylcoumarin as substrate
0.0023
6-[[4-(4-acetylpiperazin-1-yl)phenoxy]methyl]-7-(2-cyclopentylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
with Z-Phe-Arg-7-amido-4-methylcoumarin as substrate
0.0062
6-[[4-(4-acetylpiperazin-1-yl)phenoxy]methyl]-7-[2-(4,4-difluorocyclohexyl)ethyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
with Z-Phe-Arg-7-amido-4-methylcoumarin as substrate
0.00079
7-(2-cyclohexylethyl)-6-[(pyridin-2-yloxy)methyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
inhibition profiles are determined by a fluorometric assay with recombinant CAT K employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
0.000054
benzyl 1-cyano-3-pyrrolidinylcarbamate
Homo sapiens
-
IC50: 0.000054 mM
0.000056
CID 16725315
Homo sapiens
-
pH and temperature not specified in the publication
0.0000069
CID 23631927
Homo sapiens
-
pH and temperature not specified in the publication
0.1
diethyl-cyanamide
Homo sapiens
-
IC50 is above 0.1 mM
0.00003
E-64
Homo sapiens
-
at pH 5.5 and 37°C
0.0008
LFLTR-NH2
Homo sapiens
-
IC50: 0.0008 mM
0.0005
LLLTR-NH2
Homo sapiens
-
IC50: 0.0005 mM
0.25
methyl (13alpha,17alpha,20S,24Z)-3-hydroxylanosta-7,24-dien-26-oate
Homo sapiens
-
IC50 above 0.25 mM, at pH 5.5 and 37°C
0.5
methyl (3Z,13alpha,17alpha,20S,24Z)-3-(hydroxyimino)lanosta-7,24-dien-26-oate
Homo sapiens
-
IC50 above 0.5 mM, at pH 5.5 and 37°C
0.0386
methyl 5-acetyloxy-dinaphtho[1,2-2'3']furan-7,12-dione-6-carboxylate
Homo sapiens
-
pH 5.5, 22°C
0.0616
methyl 5-hydroxy-dinaphtho[1,2-2'3']furan-7,12-dione-6-carboxylate
Homo sapiens
-
pH 5.5, 22°C
0.00175
N-(1-cyano-3-pyrrolidinyl)benzamide
Homo sapiens
-
IC50: 0.00175 mM
0.00008
N-(1-cyano-3-pyrrolidinyl)benzenesulfonamide
Homo sapiens
-
IC50: 0.00008 mM
0.00085
N-(1-cyano-3-pyrrolidinyl)[1,1'-biphenyl]-4-carboxamide
Homo sapiens
-
IC50: 0.00085 mM
0.01
N-benzyl-2-[bis(3-bromophenyl)methylidene]hydrazinecarbothioamide
Homo sapiens
-
IC50 above 0.01 mM, pH and temperature not specified in the publication
0.023
N-[(1-cyano-2-pyrrolidinyl)methyl]benzamide
Homo sapiens
-
IC50: 0.023 mM
0.0115
N-[(1-cyano-2-pyrrolidinyl)methyl]benzenesulfonamide
Homo sapiens
-
IC50: 0.0115 mM
0.00065
N-[(1-cyano-3-azetidinyl)methyl]benzamide
Homo sapiens
-
IC50: 0.00065 mM
0.00005
N-[(1-cyano-3-azetidinyl)methyl]benzenesulfonamide
Homo sapiens
-
IC50: 0.00005 mM
0.000006
N-[(1-cyano-3-azetidinyl)methyl]cyclohexanecarboxamide
Homo sapiens
-
IC50: 0.000006 mM
0.00035
N-[(1-cyano-3-pyrrolidinyl)methyl]benzenesulfonamide
Homo sapiens
-
IC50: 0.00035 mM
0.0006
RKLLW-NH2
Homo sapiens
-
IC50: 0.0006 mM
0.014
RKLWD-NH2
Homo sapiens
-
IC50: 0.014 mM
0.0008
RKLWL-NH2
Homo sapiens
-
IC50: 0.0008 mM
0.00011
S-(2-oxo-1-phenylpyrrolidin-3-yl) 2-[(2S)-2-[(tert-butoxycarbonyl)amino]-3-(1H-indol-3-yl)propanoyl]hydrazinecarbothioate
Homo sapiens
-
-
0.000041
S-[2-(3,4-dihydroquinolin-1(2H)-yl)-2-oxoethyl] 2-[(2S)-2-[(tert-butoxycarbonyl)amino]-3-(1H-indol-3-yl)propanoyl]hydrazinecarbothioate
Homo sapiens
-
-
0.000001 - 0.000056
S-[2-[(2-ethylphenyl)amino]-2-oxoethyl] 2-[(2S)-2-[(tert-butoxycarbonyl)amino]-3-(1H-indol-3-yl)propanoyl]hydrazinecarbothioate
0.000115
S-[2-[(2-ethylphenyl)amino]-2-oxoethyl] 2-[(2S)-2-[(tert-butoxycarbonyl)amino]-3-phenylpropanoyl]hydrazinecarbothioate
Homo sapiens
-
-
additional information
2-cyano-4-[(6,8-dioxaspiro[3.5]non-7-ylmethyl)amino]-N-methyl-6-[(1-methylpiperidin-4-yl)methoxy]pyrimidine-5-carboxamide
0.00012
2-cyano-N-methyl-4-[2-(1-methylpiperidin-4-yl)ethoxy]-6-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
Homo sapiens
determined by a fluorometric assay with recombinant catL employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
0.00012
2-cyano-N-methyl-4-[2-(1-methylpiperidin-4-yl)ethoxy]-6-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
Homo sapiens
inhibition are determined by a fluorometric assay with recombinant Cat L
0.000001
S-[2-[(2-ethylphenyl)amino]-2-oxoethyl] 2-[(2S)-2-[(tert-butoxycarbonyl)amino]-3-(1H-indol-3-yl)propanoyl]hydrazinecarbothioate
Homo sapiens
-
pH 5.5, preincubation with enzyme 4 h before substrate addition
0.0000075
S-[2-[(2-ethylphenyl)amino]-2-oxoethyl] 2-[(2S)-2-[(tert-butoxycarbonyl)amino]-3-(1H-indol-3-yl)propanoyl]hydrazinecarbothioate
Homo sapiens
-
pH 5.5, preincubation with enzyme 1 h before substrate addition
0.000056
S-[2-[(2-ethylphenyl)amino]-2-oxoethyl] 2-[(2S)-2-[(tert-butoxycarbonyl)amino]-3-(1H-indol-3-yl)propanoyl]hydrazinecarbothioate
Homo sapiens
-
-
0.000056
S-[2-[(2-ethylphenyl)amino]-2-oxoethyl] 2-[(2S)-2-[(tert-butoxycarbonyl)amino]-3-(1H-indol-3-yl)propanoyl]hydrazinecarbothioate
Homo sapiens
-
pH 5.5
additional information
2-cyano-4-[(6,8-dioxaspiro[3.5]non-7-ylmethyl)amino]-N-methyl-6-[(1-methylpiperidin-4-yl)methoxy]pyrimidine-5-carboxamide
Homo sapiens
IC50 is above 0.001 mM, determined by a fluorometric assay with recombinant catL employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
additional information
2-cyano-4-[(cyclohexylmethyl)amino]-N-(2-phenylethyl)pyrimidine-5-carboxamide
Homo sapiens
IC50 is above 0.002 mM, inhibition are determined by a fluorometric assay with recombinant Cat L
additional information
2-cyano-4-[[(4,4-difluorocyclohexyl)methyl]amino]-N-(2-phenylethyl)pyrimidine-5-carboxamide
Homo sapiens
IC50 is above 0.003 mM, inhibition are determined by a fluorometric assay with recombinant Cat L
additional information
2-cyano-4-[[(4,4-dimethylcyclohexyl)methyl]amino]-N-(2-phenylethyl)pyrimidine-5-carboxamide
Homo sapiens
IC50 is above 0.003 mM inhibition are determined by a fluorometric assay with recombinant Cat L
additional information
2-cyano-N-(2-phenylethyl)-4-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
Homo sapiens
IC50 is above 0.003 mM inhibition are determined by a fluorometric assay with recombinant Cat L
additional information
2-cyano-N-(4,5-dimethoxybiphenyl-2-yl)-4-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
Homo sapiens
IC50 is above 0.003 mM inhibition are determined by a fluorometric assay with recombinant Cat L
additional information
CLIK-148
Homo sapiens
IC50 value is below 0.0001 mM, in 1 mM EDTA, 5 mM cysteine at pH 5.5
additional information
(3-[[2-cyano-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidin-6-yl]methoxy]phenyl)acetic acid
Homo sapiens
-
KI value is above 5 microM, inhibition profiles are determined by a fluorometric assay with recombinant CAT L employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
additional information
3-[[2-cyano-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidin-6-yl]methoxy]benzamide
Homo sapiens
-
KI value is above 1 microM, inhibition profiles are determined by a fluorometric assay with recombinant CAT L employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
additional information
4-[[2-cyano-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidin-6-yl]methoxy]benzamide
Homo sapiens
-
KI value is above 1 microM, inhibition profiles are determined by a fluorometric assay with recombinant CAT L employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
additional information
4-[[2-cyano-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidin-6-yl]methoxy]benzoic acid
Homo sapiens
-
KI value is above 2 microM, inhibition profiles are determined by a fluorometric assay with recombinant CAT L employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
additional information
6-(4-chlorobenzyl)-7-(2-cyclooctylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
KI value is above 1 microM, inhibition profiles are determined by a fluorometric assay with recombinant CAT L employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
additional information
6-(4-chlorobenzyl)-7-(2-piperidin-1-ylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
KI value is above 1 microM, inhibition profiles are determined by a fluorometric assay with recombinant CAT L employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
additional information
6-(4-chlorobenzyl)-7-(3-cyclohexylpropyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
KI value is above 1 microM, inhibition profiles are determined by a fluorometric assay with recombinant CAT L employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
additional information
6-(4-chlorobenzyl)-7-(4,4-dimethylpentyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
KI value is above 1 microM, inhibition profiles are determined by a fluorometric assay with recombinant CAT L employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
additional information
6-[[4-(1-acetyl-1,2,3,6-tetrahydropyridin-4-yl)phenoxy]methyl]-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
KI value is above 1 microM, inhibition profiles are determined by a fluorometric assay with recombinant CAT L employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
additional information
6-[[4-(1-acetylpiperidin-4-yl)phenoxy]methyl]-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
KI value is above 4 microM, inhibition profiles are determined by a fluorometric assay with recombinant CAT L employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
additional information
6-[[4-(4-acetyl-1,4-diazepan-1-yl)phenoxy]methyl]-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
IC50 is above 1 M, with Z-Phe-Arg-7-amido-4-methylcoumarin as substrate
additional information
6-[[4-(4-acetylpiperazin-1-yl)-3-fluorophenoxy]methyl]-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
IC50 is above 1 M, with Z-Phe-Arg-7-amido-4-methylcoumarin as substrate
additional information
6-[[4-(4-acetylpiperazin-1-yl)phenoxy]methyl]-7-(2-cycloheptylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
IC50 is above 2 M, with Z-Phe-Arg-7-amido-4-methylcoumarin as substrate
additional information
6-[[4-(4-acetylpiperazin-1-yl)phenoxy]methyl]-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
KI value is above 4 microM, inhibition profiles are determined by a fluorometric assay with recombinant CAT L employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
additional information
6-[[4-(4-acetylpiperazin-1-yl)phenoxy]methyl]-7-[2-(4-chlorophenyl)ethyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
IC50 is above 1 M, with Z-Phe-Arg-7-amido-4-methylcoumarin as substrate
additional information
7-(2-cyclohexylethyl)-6-(4-methoxybenzyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
KI value is above 1 microM, inhibition profiles are determined by a fluorometric assay with recombinant CAT L employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
additional information
7-(2-cyclohexylethyl)-6-(cyclohexylmethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
KI value is above 1 microM, inhibition profiles are determined by a fluorometric assay with recombinant CAT L employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
additional information
7-(2-cyclohexylethyl)-6-(phenoxymethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
KI value is above 1 microM, inhibition profiles are determined by a fluorometric assay with recombinant CAT L employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
additional information
7-(2-cyclohexylethyl)-6-[(phenylamino)methyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
KI value is above 1 microM, inhibition profiles are determined by a fluorometric assay with recombinant CAT L employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
additional information
7-(2-cyclohexylethyl)-6-[(pyridin-2-ylsulfanyl)methyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
KI value is above 1 microM, inhibition profiles are determined by a fluorometric assay with recombinant CAT L employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
additional information
7-(2-cyclohexylethyl)-6-[[methyl(phenyl)amino]methyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
KI value is above 1 microM, inhibition profiles are determined by a fluorometric assay with recombinant CAT L employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
additional information
N-(4-[[2-cyano-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidin-6-yl]methoxy]phenyl)acetamide
Homo sapiens
-
KI value is above 1 microM, inhibition profiles are determined by a fluorometric assay with recombinant CAT L employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
additional information
N-(4-[[2-cyano-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidin-6-yl]methoxy]phenyl)propanamide
Homo sapiens
-
KI value is above 1 microM, inhibition profiles are determined by a fluorometric assay with recombinant CAT L employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Baricos, W.H.; Zhou, Y.; Mason, R.W.; Barrett, A.J.
Human kidney cathepsins B and L. Characterization and potential role in degradation of glomerular basement membrane
Biochem. J.
252
301-304
1988
Homo sapiens
brenda
Reilly, J.J.; Mason, R.W.; Chen, P.; Joseph, L.J.; Sukhatme, V.P.; Yee, R.; Chapman, H.A.
Synthesis and processing of cathepsin L, an elastase, by human alveolar macrophages
Biochem. J.
257
493-498
1989
Homo sapiens
brenda
Crawford, C.; Mason, R.W.; Wikstrom, P.; Shaw, E.
The design of peptidyldiazomethane inhibitors to distinguish between the cysteine proteinases calpain II, cathepsin L and cathepsin B
Biochem. J.
253
751-758
1988
Homo sapiens
brenda
Maciewicz, R.E.; Etherington, D.J.
Enzyme immunoassay for cathepsin B and L in synovial fluids from patients with arthritis
Biochem. Soc. Trans.
16
812-813
1988
Homo sapiens
-
brenda
Mason, R.W.
Species variants of cathepsin L and their immunological identification
Biochem. J.
240
285-288
1986
Bos taurus, Oryctolagus cuniculus, Ovis aries, Homo sapiens, Rattus norvegicus
brenda
Mason, R.W.; Johnson, D.A.; Barrett, A.J.; Chapman, H.A.
Elastinolytic activity of human cathepsin L
Biochem. J.
233
925-927
1986
Homo sapiens
brenda
Mason, R.W.; Green, G.D.J.; Barrett, A.J.
Human liver cathepsin L
Biochem. J.
226
233-241
1985
Homo sapiens
brenda
Guncar, G.; Pungercic, G.; Klemencic, I.; Turk, V.; Turk, D.
Crystal structure of HMC class II-associated p41 li fragment bound to cathepsin I reveals the structural basis for differentiation between cathepsin L and S
EMBO J.
18
793-803
1999
Homo sapiens
brenda
Pagano, M.; Esnard, F.; Engler, R.; Gauthier, F.
Inhibition of human liver cathepsin L by alpha 2 cysteine-proteinase inhibitor and the low-Mr cysteine proteinase inhibitor from human serum
Biochem. J.
220
147-155
1984
Homo sapiens
brenda
Gal, S.; Gottesman, M.M.
Isolation and sequence of a cDNA for human pro-(cathepsin L)
Biochem. J.
253
303-306
1988
Homo sapiens
brenda
Fujishima, A.; Imai, Y.; Nomura, T.; Fujisawa, Y.; Yamamoto, Y.; Sugawara, T.
The crystal structure of human cathepsin L complexed with E-64
FEBS Lett.
407
47-50
1997
Homo sapiens
brenda
Ogrinc, T.; Dolenc, I.; Ritonja, A.; Turk, V.
Purification of the complex of cathepsin L and the MHC class II-associated invariant chain fragment from human kidney
FEBS Lett.
336
555-559
1993
Homo sapiens
brenda
Nomura, T.; Fujishima, A.; Fujisawa, Y.
Characterization and crystallization of recombinant human cathepsin L
Biochem. Biophys. Res. Commun.
228
792-796
1996
Homo sapiens
brenda
Dahl, S.W.; Halkier, T.; Lauritzen, C.; Dolenc, I.; Pedersen, J.; Turk, V.; Turk, B.
Human recombinant Pro-dipeptidyl peptidase I (cathepsin C) can be activated by cathepsins L and S but not by autocatalytic processing
Biochemistry
40
1671-1678
2001
Homo sapiens
brenda
Guay, J.; Falgueyret, J.P.; Ducret, A.; Percival, M.D.; Mancini, J.A.
Potency and selectivity of inhibition of cathepsin K, L and S by their respective propeptides
Eur. J. Biochem.
267
6311-6318
2000
Homo sapiens
brenda
Ohashi, K.; Naruto, M.; Nakaki, T.; Sano, E.
Identification of interleukin-8 converting enzyme as cathepsin L
Biochim. Biophys. Acta
1649
30-39
2003
Homo sapiens
brenda
Desmazes, C.; Gauthier, F.; Lalmanach, G.
Cathepsin L, but not cathepsin B, is a potential kininogenase
Biol. Chem.
382
811-815
2001
Homo sapiens
brenda
Brinker, A.; Weber, E.; Stoll, D.; Voigt, J.; Muller, A.; Sewald, N.; Jung, G.; Wiesmuller, K.H.; Bohley, P.
Highly potent inhibitors of human cathepsin L identified by screening combinatorial pentapeptide amide collections
Eur. J. Biochem.
267
5085-5092
2000
Homo sapiens
brenda
Bocock, J.P.; Edgell, C.J.; Marr, H.S.; Erickson, A.H.
Human proteoglycan testican-1 inhibits the lysosomal cysteine protease cathepsin L
Eur. J. Biochem.
270
4008-4015
2003
Homo sapiens
brenda
Chiva, C.; Barthe, P.; Codina, A.; Gairi, M.; Molina, F.; Granier, C.; Pugniere, M.; Inui, T.; Nishio, H.; Nishiuchi, Y.; Kimura, T.; Sakakibara, S.; Albericio, F.; Giralt, E.
Synthesis and NMR structure of p41icf, a potent inhibitor of human cathepsin L
J. Am. Chem. Soc.
125
1508-1517
2003
Homo sapiens
brenda
Falgueyret, J.P.; Oballa, R.M.; Okamoto, O.; Wesolowski, G.; Aubin, Y.; Rydzewski, R.M.; Prasit, P.; Riendeau, D.; Rodan, S.B.; Percival, M.D.
Novel, nonpeptidic cyanamides as potent and reversible inhibitors of human cathepsins K and L
J. Med. Chem.
44
94-104
2001
Homo sapiens
brenda
Chowdhury, S.F.; Sivaraman, J.; Wang, J.; Devanathan, G.; Lachance, P.; Qi, H.; Menard, R.; Lefebvre, J.; Konishi, Y.; Cygler, M.; Sulea, T.; Purisima, E.O.
Design of noncovalent inhibitors of human cathepsin L. From the 96-residue proregion to optimized tripeptides
J. Med. Chem.
45
5321-5329
2002
Homo sapiens (P07711), Homo sapiens
brenda
Klose, A.; Zigrino, P.; Dennhoefer, R.; Mauch, C.; Hunzelmann, N.
Identification and discrimination of extracellularly active cathepsins B and L in high-invasive melanoma cells
Anal. Biochem.
353
57-62
2006
Homo sapiens
brenda
Puzer, L.; Cotrin, S.S.; Alves, M.F.; Egborge, T.; Araujo, M.S.; Juliano, M.A.; Juliano, L.; Broemme, D.; Carmona, A.K.
Comparative substrate specificity analysis of recombinant human cathepsin V and cathepsin L
Arch. Biochem. Biophys.
430
274-283
2004
Homo sapiens
brenda
Hwang, S.R.; Stoka, V.; Turk, V.; Hook, V.
Resistance of cathepsin L compared to elastase to proteolysis when complexed with the serpin endopin 2C, and recovery of cathepsin L activity
Biochem. Biophys. Res. Commun.
340
1238-1243
2006
Homo sapiens
brenda
Meh, P.; Pavsic, M.; Turk, V.; Baici, A.; Lenarcic, B.
Dual concentration-dependent activity of thyroglobulin type-1 domain of testican: specific inhibitor and substrate of cathepsin L
Biol. Chem.
386
75-83
2005
Homo sapiens
brenda
Zheng, X.; Chou, P.M.; Mirkin, B.L.; Rebbaa, A.
Senescence-initiated reversal of drug resistance: specific role of cathepsin L
Cancer Res.
64
1773-1780
2004
Homo sapiens
brenda
Bylaite, M.; Moussali, H.; Marciukaitiene, I.; Ruzicka, T.; Walz, M.
Expression of cathepsin L and its inhibitor hurpin in inflammatory and neoplastic skin diseases
Exp. Dermatol.
15
110-118
2006
Homo sapiens
brenda
Laurent-Matha, V.; Derocq, D.; Prebois, C.; Katunuma, N.; Liaudet-Coopman, E.
Processing of human cathepsin D is independent of its catalytic function and auto-activation: involvement of cathepsins L and B
J. Biochem.
139
363-371
2006
Homo sapiens
brenda
Cheng, T.; Hitomi, K.; van Vlijmen-Willems, I.M.; de Jongh, G.J.; Yamamoto, K.; Nishi, K.; Watts, C.; Reinheckel, T.; Schalkwijk, J.; Zeeuwen, P.L.
Cystatin M/E is a high affinity inhibitor of cathepsin V and cathepsin L by a reactive site that is distinct from the legumain-binding site. A novel clue for the role of cystatin M/E in epidermal cornification
J. Biol. Chem.
281
15893-15899
2006
Homo sapiens
brenda
Marquis, R.W.; James, I.; Zeng, J.; Trout, R.E.; Thompson, S.; Rahman, A.; Yamashita, D.S.; Xie, R.; Ru, Y.; Gress, C.J.; Blake, S.; Lark, M.A.; Hwang, S.M.; Tomaszek, T.; Offen, P.; Head, M.S.; Cummings, M.D.; Veber, D.F.
Azepanone-based inhibitors of human cathepsin L
J. Med. Chem.
48
6870-6878
2005
Homo sapiens
brenda
Urbich, C.; Heeschen, C.; Aicher, A.; Sasaki, K.; Bruhl, T.; Farhadi, MR.; Vajkoczy, P.; Hofmann, W.K.; Peters, C.; Pennacchio, L.A.; Abolmaali, N.D.; Chavakis, E.; Reinheckel, T.; Zeiher, A.M.; Dimmeler, S.
Cathepsin L is required for endothelial progenitor cell-induced neovascularization
Nat. Med.
11
206-213
2005
Homo sapiens, Mus musculus
brenda
Wang, S.Q.; Du, Q.S.; Zhao, K.; Li, A.X.; Wei, D.Q.; Chou, K.C.
Virtual screening for finding natural inhibitor against cathepsin-L for SARS therapy
Amino Acids
33
129-135
2007
Homo sapiens
brenda
Fairhead, M.; Kelly, S.M.; van der Walle, C.F.
A heparin binding motif on the pro-domain of human procathepsin L mediates zymogen destabilization and activation
Biochem. Biophys. Res. Commun.
366
862-867
2008
Homo sapiens (P07711), Homo sapiens
brenda
Goulet, B.; Truscott, M.; Nepveu, A.
A novel proteolytically processed CDP/Cux isoform of 90 kDa is generated by cathepsin L
Biol. Chem.
387
1285-1293
2006
Homo sapiens
brenda
Caserman, S.; Kenig, S.; Sloane, B.F.; Lah, T.T.
Cathepsin L splice variants in human breast cell lines
Biol. Chem.
387
629-634
2006
Homo sapiens
brenda
Sevenich, L.; Pennacchio, L.A.; Peters, C.; Reinheckel, T.
Human cathepsin L rescues the neurodegeneration and lethality in cathepsin B/L double-deficient mice
Biol. Chem.
387
885-891
2006
Homo sapiens
brenda
Vicik, R.; Busemann, M.; Gelhaus, C.; Stiefl, N.; Scheiber, J.; Schmitz, W.; Schulz, F.; Mladenovic, M.; Engels, B.; Leippe, M.; Baumann, K.; Schirmeister, T.
Aziridide-based inhibitors of cathepsin L: synthesis, inhibition activity, and docking studies
ChemMedChem
1
1126-1141
2006
Homo sapiens
brenda
Spira, D.; Stypmann, J.; Tobin, D.J.; Petermann, I.; Mayer, C.; Hagemann, S.; Vasiljeva, O.; Guenther, T.; Schuele, R.; Peters, C.; Reinheckel, T.
Cell type-specific functions of the lysosomal protease cathepsin L in the heart
J. Biol. Chem.
282
37045-37052
2007
Homo sapiens, Mus musculus
brenda
Novinec, M.; Grass, R.N.; Stark, W.J.; Turk, V.; Baici, A.; Lenarcic, B.
Interaction between human cathepsins K, L, and S and elastins: mechanism of elastinolysis and inhibition by macromolecular inhibitors
J. Biol. Chem.
282
7893-7902
2007
Homo sapiens
brenda
Sever, S.; Altintas, M.M.; Nankoe, S.R.; Moeller, C.C.; Ko, D.; Wei, C.; Henderson, J.; del Re, E.C.; Hsing, L.; Erickson, A.; Cohen, C.D.; Kretzler, M.; Kerjaschki, D.; Rudensky, A.; Nikolic, B.; Reiser, J.
Proteolytic processing of dynamin by cytoplasmic cathepsin L is a mechanism for proteinuric kidney disease
J. Clin. Invest.
117
2095-2104
2007
Homo sapiens (P07711)
brenda
Chowdhury, S.F.; Joseph, L.; Kumar, S.; Tulsidas, S.R.; Bhat, S.; Ziomek, E.; Menard, R.; Sivaraman, J.; Purisima, E.O.
Exploring inhibitor binding at the S subsites of cathepsin L
J. Med. Chem.
51
1361-1368
2008
Homo sapiens
brenda
Yang, M.; Zhang, Y.; Pan, J.; Sun, J.; Liu, J.; Libby, P.; Sukhova, G.K.; Doria, A.; Katunuma, N.; Peroni, O.D.; Guerre-Millo, M.; Kahn, B.B.; Clement, K.; Shi, G.P.
Cathepsin L activity controls adipogenesis and glucose tolerance
Nat. Cell Biol.
9
970-977
2007
Homo sapiens
brenda
Fairhead, M.; van der Walle, C.F.
The heavy-light chain loop of human cathepsin-L modulates its activity and stability
Protein Pept. Lett.
15
47-53
2008
Homo sapiens (P07711), Homo sapiens
brenda
Lecaille, F.; Chowdhury, S.; Purisima, E.; Broemme, D.; Lalmanach, G.
The S2 subsites of cathepsins K and L and their contribution to collagen degradation
Protein Sci.
16
662-670
2007
Homo sapiens
brenda
Liu, Y.; Li, X.; Peng, D.; Tan, Z.; Liu, H.; Qing, Y.; Xue, Y.; Shi, G.P.
Usefulness of serum cathepsin L as an independent biomarker in patients with coronary heart disease
Am. J. Cardiol.
103
476-481
2009
Homo sapiens
brenda
Li, W.; Kornmark, L.; Jonasson, L.; Forssell, C.; Yuan, X.M.
Cathepsin L is significantly associated with apoptosis and plaque destabilization in human atherosclerosis
Atherosclerosis
202
92-102
2009
Homo sapiens
brenda
Jean, D.; Rousselet, N.; Frade, R.
Cathepsin L expression is up-regulated by hypoxia in human melanoma cells: role of its 5-untranslated region
Biochem. J.
413
125-134
2008
Homo sapiens
brenda
Zheng, X.; Chu, F.; Mirkin, B.L.; Sudha, T.; Mousa, S.A.; Rebbaa, A.
Role of the proteolytic hierarchy between cathepsin L, cathepsin D and caspase-3 in regulation of cellular susceptibility to apoptosis and autophagy
Biochim. Biophys. Acta
1783
2294-2300
2008
Homo sapiens
brenda
Takahashi, K.; Ueno, T.; Tanida, I.; Minematsu-Ikeguchi, N.; Murata, M.; Kominami, E.
Characterization of CAA0225, a novel inhibitor specific for cathepsin L, as a probe for autophagic proteolysis
Biol. Pharm. Bull.
32
475-479
2009
Homo sapiens, Rattus norvegicus
brenda
Myers, M.C.; Shah, P.P.; Beavers, M.P.; Napper, A.D.; Diamond, S.L.; Smith, A.B.; Huryn, D.M.
Design, synthesis, and evaluation of inhibitors of cathepsin L: Exploiting a unique thiocarbazate chemotype
Bioorg. Med. Chem. Lett.
18
3646-3651
2008
Homo sapiens
brenda
Irie, O.; Ehara, T.; Iwasaki, A.; Yokokawa, F.; Sakaki, J.; Hirao, H.; Kanazawa, T.; Teno, N.; Horiuchi, M.; Umemura, I.; Gunji, H.; Masuya, K.; Hitomi, Y.; Iwasaki, G.; Nonomura, K.; Tanabe, K.; Fukaya, H.; Kosaka, T.; Snell, C.R.; Hallett, A.
Discovery of selective and nonpeptidic cathepsin S inhibitors
Bioorg. Med. Chem. Lett.
18
3959-3962
2008
Homo sapiens
brenda
Irie, O.; Yokokawa, F.; Ehara, T.; Iwasaki, A.; Iwaki, Y.; Hitomi, Y.; Konishi, K.; Kishida, M.; Toyao, A.; Masuya, K.; Gunji, H.; Sakaki, J.; Iwasaki, G.; Hirao, H.; Kanazawa, T.; Tanabe, K.; Kosaka, T.; Hart, T.W.; Hallett, A.
4-Amino-2-cyanopyrimidines: novel scaffold for nonpeptidic cathepsin S inhibitors
Bioorg. Med. Chem. Lett.
18
4642-4646
2008
Homo sapiens (P07711)
brenda
Irie, O.; Kosaka, T.; Kishida, M.; Sakaki, J.; Masuya, K.; Konishi, K.; Yokokawa, F.; Ehara, T.; Iwasaki, A.; Iwaki, Y.; Hitomi, Y.; Toyao, A.; Gunji, H.; Teno, N.; Iwasaki, G.; Hirao, H.; Kanazawa, T.; Tanabe, K.; Hiestand, P.C.; Malcangio, M.; Fox, A.J.; Bevan, S.J.; Yaqoob, M.; Culshaw, A.J.; Hart, T.W.; Hallet, A.
Overcoming hERG issues for brain-penetrating cathepsin S inhibitors: 2-cyanopyrimidines. Part 2
Bioorg. Med. Chem. Lett.
18
5280-5284
2008
Homo sapiens (P07711)
brenda
Ayesa, S.; Lindquist, C.; Agback, T.; Benkestock, K.; Classon, B.; Henderson, I.; Hewitt, E.; Jansson, K.; Kallin, A.; Sheppard, D.; Samuelsson, B.
Solid-phase parallel synthesis and SAR of 4-amidofuran-3-one inhibitors of cathepsin S: effect of sulfonamides P3 substituents on potency and selectivity
Bioorg. Med. Chem.
17
1307-1324
2009
Homo sapiens
brenda
Herszenyi, L.; Farinati, F.; Cardin, R.; Istvan, G.; Molnar, L.D.; Hritz, I.; De Paoli, M.; Plebani, M.; Tulassay, Z.
Tumor marker utility and prognostic relevance of cathepsin B, cathepsin L, urokinase-type plasminogen activator, plasminogen activator inhibitor type-1, CEA and CA 19-9 in colorectal cancer
BMC Cancer
8
194
2008
Homo sapiens
brenda
Fairhead, M.; Johnson, K.A.; Kowatz, T.; McMahon, S.A.; Carter, L.G.; Oke, M.; Liu, H.; Naismith, J.H.; van der Walle, C.F.
Crystal structure and silica condensing activities of silicatein alpha-cathepsin L chimeras
Chem. Commun. (Camb. )
15
1765-1767
2008
Homo sapiens (P07711)
brenda
Hook, V.; Funkelstein, L.; Toneff, T.; Mosier, C.; Hwang, S.R.
Human pituitary contains dual cathepsin L and prohormone convertase processing pathway components involved in converting POMC into the peptide hormones ACTH, alpha-MSH, and beta-endorphin
Endocrine
35
429-437
2009
Homo sapiens
brenda
dos Reis, F.C.; Smith, B.O.; Santos, C.C.; Costa, T.F.; Scharfstein, J.; Coombs, G.H.; Mottram, J.C.; Lima, A.P.
The role of conserved residues of chagasin in the inhibition of cysteine peptidases
FEBS Lett.
582
485-490
2008
Homo sapiens
brenda
Thomas, V.; Samanta, S.; Fikrig, E.
Anaplasma phagocytophilum increases cathepsin L activity, thereby globally influencing neutrophil function
Infect. Immun.
76
4905-4912
2008
Homo sapiens
brenda
Sullivan, S.; Tosetto, M.; Kevans, D.; Coss, A.; Wang, L.; ODonoghue, D.; Hyland, J.; Sheahan, K.; Mulcahy, H.; OSullivan, J.
Localization of nuclear cathepsin L and its association with disease progression and poor outcome in colorectal cancer
Int. J. Cancer
125
54-61
2009
Homo sapiens
brenda
Mihelic, M.; Dobersek, A.; Guncar, G.; Turk, D.
Inhibitory fragment from the p41 form of invariant chain can regulate activity of cysteine cathepsins in antigen presentation
J. Biol. Chem.
283
14453-14460
2008
Homo sapiens, Homo sapiens (P07711), Mus musculus, Mus musculus (P06797)
brenda
Abboud-Jarrous, G.; Atzmon, R.; Peretz, T.; Palermo, C.; Gadea, B.B.; Joyce, J.A.; Vlodavsky, I.
Cathepsin L is responsible for processing and activation of proheparanase through multiple cleavages of a linker segment
J. Biol. Chem.
283
18167-18176
2008
Bos taurus, Homo sapiens
brenda
Cailhier, J.F.; Sirois, I.; Laplante, P.; Lepage, S.; Raymond, M.A.; Brassard, N.; Prat, A.; Iozzo, R.V.; Pshezhetsky, A.V.; Hebert, M.J.
Caspase-3 activation triggers extracellular cathepsin L release and endorepellin proteolysis
J. Biol. Chem.
283
27220-27229
2008
Homo sapiens
brenda
Beavers, M.P.; Myers, M.C.; Shah, P.P.; Purvis, J.E.; Diamond, S.L.; Cooperman, B.S.; Huryn, D.M.; Smith, A.B.
Molecular docking of cathepsin L inhibitors in the binding site of papain
J. Chem. Inf. Model.
48
1464-1472
2008
Homo sapiens (P07711)
brenda
Yadav, M.R.; Shinde, A.K.; Chouhan, B.S.; Giridhar, R.; Menard, R.
Peptidomimetic 2-cyanopyrrolidines as potent selective cathepsin L inhibitors
J. Enzyme Inhib. Med. Chem.
23
190-197
2008
Homo sapiens
brenda
Irie, O.; Kosaka, T.; Ehara, T.; Yokokawa, F.; Kanazawa, T.; Hirao, H.; Iwasaki, A.; Sakaki, J.; Teno, N.; Hitomi, Y.; Iwasaki, G.; Fukaya, H.; Nonomura, K.; Tanabe, K.; Koizumi, S.; Uchiyama, N.; Bevan, S.J.; Malcangio, M.; Gentry, C.; Fox, A.J.; Yaqoob, M.; Culshaw, A.J.; Allan Hallett, A.J.
Discovery of orally bioavailable cathepsin S inhibitors for the reversal of neuropathic pain
J. Med. Chem.
51
5502-5505
2008
Homo sapiens, Rattus norvegicus
brenda
Urbich, C.; Dernbach, E.; Roessig, L.; Zeiher, A.M.; Dimmeler, S.
High glucose reduces cathepsin L activity and impairs invasion of circulating progenitor cells
J. Mol. Cell. Cardiol.
45
429-436
2008
Homo sapiens
brenda
Tang, Q.; Cai, J.; Shen, D.; Bian, Z.; Yan, L.; Wang, Y.X.; Lan, J.; Zhuang, G.Q.; Ma, W.Z.; Wang, W.
Lysosomal cysteine peptidase cathepsin L protects against cardiac hypertrophy through blocking AKT/GSK3beta signaling
J. Mol. Med.
87
249-260
2009
Homo sapiens
brenda
Porotto, M.; Orefice, G.; Yokoyama, C.; Mungall, B.; Realubit, R.; Sganga, M.; Aljofan, M.; Whitt, M.; Glickman, F.; Moscona, A.
Simulating henipavirus multicycle replication in a screening assay leads to identification of a promising candidate for therapy
J. Virol.
83
5148-5155
2009
Homo sapiens
brenda
Zhu, S.; Wei, L.; Yamasaki, K.; Gallo, R.L.
Activation of cathepsin L by the cathelin-like domain of protegrin-3
Mol. Immunol.
45
2531-2536
2008
Homo sapiens
brenda
Shah, P.P.; Myers, M.C.; Beavers, M.P.; Purvis, J.E.; Jing, H.; Grieser, H.J.; Sharlow, E.R.; Napper, A.D.; Huryn, D.M.; Cooperman, B.S.; Smith, A.B.; Diamond, S.L.
Kinetic characterization and molecular docking of a novel, potent, and selective slow-binding inhibitor of human cathepsin L
Mol. Pharmacol.
74
34-41
2008
Homo sapiens
brenda
Haecker, H.G.; Grundmann, F.; Lohr, F.; Ottersbach, P.A.; Zhou, J.; Schnakenburg, G.; Guetschow, M.
2-Amino- and 2-alkylthio-4H-3,1-benzothiazin-4-ones: synthesis, interconversion and enzyme inhibitory activities
Molecules
14
378-402
2009
Homo sapiens
brenda
Park, Y.; Kong, J.Y.; Cho, H.
A furanquinone from Paulownia tomentosa stem for a new cathepsin K inhibitor
Phytother. Res.
23
1485-1488
2009
Homo sapiens
brenda
Hill, J.J.; Moreno, M.J.; Lam, J.C.; Haqqani, A.S.; Kelly, J.F.
Identification of secreted proteins regulated by cAMP in glioblastoma cells using glycopeptide capture and label-free quantification
Proteomics
9
535-549
2009
Homo sapiens
brenda
Sevenich, L.; Hagemann, S.; Stoeckle, C.; Tolosa, E.; Peters, C.; Reinheckel, T.
Expression of human cathepsin L or human cathepsin V in mouse thymus mediates positive selection of T helper cells in cathepsin L knock-out mice
Biochimie
92
1674-1680
2010
Homo sapiens
brenda
Coppini, L.P.; Barros, N.M.; Oliveira, M.; Hirata, I.Y.; Alves, M.F.; Paschoalin, T.; Assis, D.M.; Juliano, M.A.; Puzer, L.; Broemme, D.; Carmona, A.K.
Plasminogen hydrolysis by cathepsin S and identification of derived peptides as selective substrate for cathepsin V and cathepsin L inhibitor
Biol. Chem.
391
561-570
2010
Homo sapiens
brenda
Huryn, D.M.; Smith, A.B.
The identification, characterization and optimization of small molecule probes of cysteine proteases: experiences of the Penn center for molecular discovery with cathepsin B and cathepsin L
Curr. Top. Med. Chem.
9
1206-1216
2009
Homo sapiens
brenda
See, V.; Free, P.; Cesbron, Y.; Nativo, P.; Shaheen, U.; Rigden, D.J.; Spiller, D.G.; Fernig, D.G.; White, M.R.; Prior, I.A.; Brust, M.; Lounis, B.; Levy, R.
Cathepsin L digestion of nanobioconjugates upon endocytosis
ACS Nano
3
2461-2468
2009
Homo sapiens
brenda
Zheng, X.; Chu, F.; Chou, P.; Gallati, C.; Dier, U.; Mirkin, B.; Mousa, S.; Rebbaa, A.
Cathepsin L inhibition suppresses drug resistance in vitro and in vivo: A putative mechanism
Am. J. Physiol. Cell Physiol.
296
C65-C74
2009
Homo sapiens
brenda
Hsu, K.F.; Wu, C.L.; Huang, S.C.; Wu, C.M.; Hsiao, J.R.; Yo, Y.T.; Chen, Y.H.; Shiau, A.L.; Chou, C.Y.
Cathepsin L mediates resveratrol-induced autophagy and apoptotic cell death in cervical cancer cells
Autophagy
5
451-460
2009
Homo sapiens
brenda
Ueno, T.; Takahashi, K.
A cathepsin L-specific inhibitor preferentially inhibits degradation of autophagosomal LC3 and GABARAP in HeLa and Huh-7 cells
Autophagy
5
878-879
2009
Homo sapiens
brenda
Fortenberry, Y.M.; Brandal, S.; Bialas, R.C.; Church, F.C.
Protein C inhibitor regulates both cathepsin L activity and cell-mediated tumor cell migration
Biochim. Biophys. Acta
1800
580-590
2010
Homo sapiens
brenda
Schilling, K.; Krner, A.; Sehmisch, S.; Kreusch, A.; Kleint, R.; Benedix, Y.; Schlabrakowski, A.; Wiederanders, B.
Selectivity of propeptide-enzyme interaction in cathepsin L-like cysteine proteases
Biol. Chem.
390
167-174
2009
Homo sapiens
brenda
Leto, G.; Sepporta, M.V.; Crescimanno, M.; Flandina, C.; Tumminello, F.M.
Cathepsin L in metastatic bone disease: therapeutic implications
Biol. Chem.
391
655-664
2010
Homo sapiens
brenda
Asaad, N.; Bethel, P.A.; Coulson, M.D.; Dawson, J.E.; Ford, S.J.; Gerhardt, S.; Grist, M.; Hamlin, G.A.; James, M.J.; Jones, E.V.; Karoutchi, G.I.; Kenny, P.W.; Morley, A.D.; Oldham, K.; Rankine, N.; Ryan, D.; Wells, S.L.; Wood, L.; Augustin, M.; Krapp, S.; Simader, H.; Steinbacher, S.
Dipeptidyl nitrile inhibitors of Cathepsin L
Bioorg. Med. Chem. Lett.
19
4280-4283
2009
Homo sapiens
brenda
Kishore Kumar, G.D.; Chavarria, G.E.; Charlton-Sevcik, A.K.; Arispe, W.M.; Macdonough, M.T.; Strecker, T.E.; Chen, S.E.; Siim, B.G.; Chaplin, D.J.; Trawick, M.L.; Pinney, K.G.
Design, synthesis, and biological evaluation of potent thiosemicarbazone based cathepsin L inhibitors
Bioorg. Med. Chem. Lett.
20
1415-1419
2010
Homo sapiens
brenda
Martinez, O.; Johnson, J.; Manicassamy, B.; Rong, L.; Olinger, G.G.; Hensley, L.E.; Basler, C.F.
Zaire Ebola virus entry into human dendritic cells is insensitive to cathepsin L inhibition
Cell. Microbiol.
12
148-157
2010
Homo sapiens
brenda
Biswas, N.; Rodriguez-Flores, J.L.; Courel, M.; Gayen, J.R.; Vaingankar, S.M.; Mahata, M.; Torpey, J.W.; Taupenot, L.; OConnor, D.T.; Mahata, S.K.
Cathepsin L colocalizes with chromogranin a in chromaffin vesicles to generate active peptides
Endocrinology
150
3547-3557
2009
Homo sapiens
brenda
Klose, A.; Wilbrand-Hennes, A.; Brinckmann, J.; Hunzelmann, N.
Alternate trafficking of cathepsin L in dermal fibroblasts induced by UVA radiation
Exp. Dermatol.
19
e117-e123
2010
Homo sapiens
brenda
Xu, X.; Yuan, G.; Liu, W.; Zhang, Y.; Chen, W.
Expression of cathepsin L in nasopharyngeal carcinoma and its clinical significance
Exp. Oncol.
31
102-105
2009
Homo sapiens
brenda
Wartmann, T.; Mayerle, J.; Kaehne, T.; Sahin-Toth, M.; Ruthenbuerger, M.; Matthias, R.; Kruse, A.; Reinheckel, T.; Peters, C.; Weiss, F.U.; Sendler, M.; Lippert, H.; Schulz, H.U.; Aghdassi, A.; Dummer, A.; Teller, S.; Halangk, W.; Lerch, M.M.
Cathepsin L inactivates human trypsinogen, whereas cathepsin L-deletion reduces the severity of pancreatitis in mice
Gastroenterology
138
726-737
2010
Homo sapiens
brenda
Konjar, S.; Sutton, V.R.; Hoves, S.; Repnik, U.; Yagita, H.; Reinheckel, T.; Peters, C.; Turk, V.; Turk, B.; Trapani, J.A.; Kopitar-Jerala, N.
Human and mouse perforin are processed in part through cleavage by the lysosomal cysteine proteinase cathepsin L
Immunology
131
257-267
2010
Homo sapiens, Mus musculus
brenda
Ceru, S.; Konjar, S.; Maher, K.; Repnik, U.; Krizaj, I.; Bencina, M.; Renko, M.; Nepveu, A.; Zerovnik, E.; Turk, B.; Kopitar-Jerala, N.
Stefin B interacts with histones and cathepsin L in the nucleus
J. Biol. Chem.
285
10078-10086
2010
Homo sapiens
brenda
Higgins, W.J.; Fox, D.M.; Kowalski, P.S.; Nielsen, J.E.; Worrall, D.M.
Heparin enhances serpin inhibition of the cysteine protease cathepsin L
J. Biol. Chem.
285
3722-3729
2010
Homo sapiens
brenda
Puchi, M.; Garcia-Huidobro, J.; Cordova, C.; Aguilar, R.; Dufey, E.; Imschenetzky, M.; Bustos, P.; Morin, V.
A new nuclear protease with cathepsin L properties is present in Hela and Caco-2 cells
J. Cell. Biochem.
111
1099-1106
2010
Homo sapiens
brenda
Shenoy, R.T.; Chowdhury, S.F.; Kumar, S.; Joseph, L.; Purisima, E.O.; Sivaraman, J.
A combined crystallographic and molecular dynamics study of cathepsin L retrobinding inhibitors
J. Med. Chem.
52
6335-6346
2009
Homo sapiens (P07711)
brenda
Gibbons, A.; McElvaney, N.; Taggart, C.; Cryan, S.
Delivery of rSLPI in a liposomal carrier for inhalation provides protection against cathepsin L degradation
J. Microencapsul.
26
513-522
2009
Homo sapiens
brenda
Hood, C.L.; Abraham, J.; Boyington, J.C.; Leung, K.; Kwong, P.D.; Nabel, G.J.
Biochemical and structural characterization of cathepsin L-processed Ebola virus glycoprotein: implications for viral entry and immunogenicity
J. Virol.
84
2972-2982
2010
Homo sapiens
brenda
Lankelma, J.M.; Voorend, D.M.; Barwari, T.; Koetsveld, J.; Van der Spek, A.H.; De Porto, A.P.; Van Rooijen, G.; Van Noorden, C.J.
Cathepsin L, target in cancer treatment?
Life Sci.
86
225-233
2010
Homo sapiens
brenda
Urbanelli, L.; Trivelli, F.; Ercolani, L.; Sementino, E.; Magini, A.; Tancini, B.; Franceschini, R.; Emiliani, C.
Cathepsin L increased level upon Ras mutants expression: the role of p38 and p44/42 MAPK signaling pathways
Mol. Cell. Biochem.
343
49-57
2010
Homo sapiens
brenda
Shah, P.P.; Wang, T.; Kaletsky, R.L.; Myers, M.; Puvis, J.E.; Jing, H.; Huryn, D.M.; Greenbaum, D.C.; Smith, A.B.; Bates, P.; Diamond, S.L.
A small molecule oxocarbazate inhibitor of human cathepsin L blocks SARS and Ebola pseudotype virus infection into HEK 293T cells
Mol. Pharmacol.
78
319-324
2010
Homo sapiens
brenda
Sansanwal, P.; Shukla, A.A.; Das, T.K.; Chauhan, S.S.
Truncated human cathepsin L, encoded by a novel splice variant, exhibits altered subcellular localization and cytotoxicity
Protein Pept. Lett.
17
238-245
2010
Homo sapiens (Q9HBQ7), Homo sapiens
brenda
Yamaguchi, M.; Tahara, Y.; Makino, T.; Shimizu, T.; Date, A.
Comparison of cathepsin L activity in cheek and forearm stratum corneum in young female adults
Skin Res. Technol.
15
370-375
2009
Homo sapiens
brenda
Yoshii, H.; Kamiyama, H.; Minematsu, K.; Goto, K.; Mizota, T.; Oishi, K.; Katunuma, N.; Yamamoto, N.; Kubo, Y.
Cathepsin L is required for ecotropic murine leukemia virus infection in NIH3T3 cells
Virology
394
227-234
2009
Homo sapiens, Mus musculus, Rattus norvegicus
brenda
Diederich, S.; Dietzel, E.; Maisner, A.
Nipah virus fusion protein: influence of cleavage site mutations on the cleavability by cathepsin L, trypsin and furin
Virus Res.
145
300-306
2009
Homo sapiens
brenda
Shenoy, R.T.; Sivaraman, J.
Structural basis for reversible and irreversible inhibition of human cathepsin L by their respective dipeptidyl glyoxal and diazomethylketone inhibitors
J. Struct. Biol.
173
14-19
2011
Homo sapiens (P07711), Homo sapiens
brenda
Adams-Cioaba, M.A.; Krupa, J.C.; Xu, C.; Mort, J.S.; Min, J.
Structural basis for the recognition and cleavage of histone H3 by cathepsin L
Nat. Commun.
2
197
2011
Homo sapiens (P07711), Homo sapiens
brenda
Legowska, M.; Wysocka, M.; Burster, T.; Pikula, M.; Rolka, K.; Lesner, A.
Ultrasensitive internally quenched substrates of human cathepsin L
Anal. Biochem.
466
30-37
2014
Homo sapiens
brenda
Torkar, A.; Lenarcic, B.; Lah, T.; Dive, V.; Devel, L.
Identification of new peptide amides as selective cathepsin L inhibitors: the first step towards selective irreversible inhibitors?
Bioorg. Med. Chem. Lett.
23
2968-2973
2013
Homo sapiens
brenda
Ramalho, S.D.; De Sousa, L.R.; Nebo, L.; Maganhi, S.H.; Caracelli, I.; Zukerman-Schpector, J.; Lima, M.I.; Alves, M.F.; Da Silva, M.F.; Fernandes, J.B.; Vieira, P.C.
Triterpenoids as novel natural inhibitors of human cathepsin L
Chem. Biodivers.
11
1354-1363
2014
Homo sapiens
brenda
Pietra, D.; Borghini, A.; Ricci, C.; Bianucci, A.M.
Enzyme kinetics studies on 29-kDa human liver cathepsin L
Chem. Biol. Drug Des.
84
648-658
2014
Homo sapiens (P07711), Homo sapiens
brenda
Tamhane, T.; Lllukkumbura, R.; Lu, S.; Maelandsmo, G.M.; Haugen, M.H.; Brix, K.
Nuclear cathepsin L activity is required for cell cycle progression of colorectal carcinoma cells
Biochimie
122
208-218
2016
Homo sapiens (P07711)
brenda
Dana, D.; Garcia, J.; Bhuiyan, A.I.; Rathod, P.; Joo, L.; Novoa, D.A.; Paroly, S.; Fath, K.R.; Chang, E.J.; Pathak, S.K.
Cell penetrable, clickable and tagless activity-based probe of human cathepsin L
Bioorg. Chem.
85
505-514
2019
Homo sapiens (P07711), Homo sapiens
brenda
Parker, E.N.; Song, J.; Kishore Kumar, G.D.; Odutola, S.O.; Chavarria, G.E.; Charlton-Sevcik, A.K.; Strecker, T.E.; Barnes, A.L.; Sudhan, D.R.; Wittenborn, T.R.; Siemann, D.W.; Horsman, M.R.; Chaplin, D.J.; Trawick, M.L.; Pinney, K.G.
Synthesis and biochemical evaluation of benzoylbenzophenone thiosemicarbazone analogues as potent and selective inhibitors of cathepsin L
Bioorg. Med. Chem.
23
6974-6992
2015
Homo sapiens (P07711), Homo sapiens
brenda
Jefferson, T.; McShan, D.; Warfield, J.; Ogungbe, I.V.
Screening and identification of inhibitors of Trypanosoma brucei cathepsin L with antitrypanosomal activity
Chem. Biol. Drug Des.
87
154-158
2016
Homo sapiens (P07711), Homo sapiens, Trypanosoma brucei brucei (Q95PM0), Trypanosoma brucei rhodesiense (Q95PM0), Trypanosoma brucei brucei 427 (Q95PM0)
brenda
Pranjol, M.Z.I.; Gutowski, N.J.; Hannemann, M.; Whatmore, J.L.
Cathepsin L induces proangiogenic changes in human omental microvascular endothelial cells via activation of the ERK1/2 pathway
Curr. Cancer Drug Targets
19
231-242
2019
Homo sapiens (P07711), Homo sapiens
brenda
Korenc, M.; Lenarcic, B.; Novinec, M.
Human cathepsin L, a papain-like collagenase without proline specificity
FEBS J.
282
4328-4340
2015
Homo sapiens (P07711), Homo sapiens
brenda
Sosnowski, P.; Turk, D.
Caught in the act the crystal structure of cleaved cathepsin L bound to the active site of cathepsin L
FEBS Lett.
590
1253-1261
2016
Homo sapiens (P07711)
brenda
Cao, Y.; Liu, X.; Li, Y.; Lu, Y.; Zhong, H.; Jiang, W.; Chen, A.F.; Billiar, T.R.; Yuan, H.; Cai, J.
Cathepsin L activity correlates with proteinuria in chronic kidney disease in humans
Int. Urol. Nephrol.
49
1409-1417
2017
Homo sapiens (P07711), Homo sapiens
brenda
Hashimoto, Y.; Kondo, C.; Katunuma, N.
An active 32-kDa cathepsin L is secreted directly from HT 1080 fibrosarcoma cells and not via lysosomal exocytosis
PLoS ONE
10
e0145067
2015
Homo sapiens (P07711), Homo sapiens
brenda