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.
2-aminobenzoyl-GLQRALEI-Lys(dinitrophenol)-NH2 + H2O
?
the Abz-GLQRALEI-Lys(Dnp)fluorescence quenched peptide representing the P4-P4' sequence of complement C4
-
-
?
2-aminobenzoyl-Gly-Leu-Gln-Arg-Ala-Leu-Glu-Ile-Lys(dinitrophenyl)-NH2 + H2O
2-aminobenzoyl-Gly-Leu-Gln-Arg + Ala-Leu-Glu-Ile-Lys(dinitrophenyl)-NH2
2-aminobenzoyl-Gly-Tyr-Leu-Gly-Arg-Ser-Tyr-Lys-Val-Gly-Lys(dinitrophenyl)-Asp-OH + H2O
2-aminobenzoyl-Gly-Tyr-Leu-Gly-Arg + Ser-Tyr-Lys-Val-Gly-Lys(dinitrophenyl)-Asp-OH + H2O
-
substrate obtained from phage display analysis, 4.7fold higher procession than the natural C1s protease substrate (SLGRKIQI)
-
-
?
2-aminobenzoyl-Ser-Leu-Gly-Arg-Lys-Ile-Gln-Ile-Lys(dinitrophenyl)-NH2 + H2O
2-aminobenzoyl-Ser-Leu-Gly-Arg + Lys-Ile-Gln-Ile-Lys(dinitrophenyl)-NH2
2-aminobenzoyl-Ser-Val-Ala-Arg-Thr-Leu-Leu-Lys(dinitrophenyl)-NH2 + H2O
2-aminobenzoyl-Ser-Val-Ala-Arg + Thr-Leu-Leu-Lys(dinitrophenyl)-NH2 + H2O
-
-
-
-
?
Ac-Ala-P3-P2-P1-7-amino-4-carbamoylmethylcoumarin + H2O
?
-
a 722-member substrate library with combinations of all proteogenic amino acids at positions P3 and P2 was screened for cleavage, C1s preferred the small polar residues Ser, Ala and Gly at the P2 position and had a broad specificity at P3 position
-
-
?
acetyl-Gly-Lys-naphthyl ester + H2O
?
-
-
-
-
?
Benzoyl-Arg ethyl ester + H2O
?
-
-
-
-
?
benzoyl-beta-Ala-Gly-L-Arg 4-nitroanilide + H2O
benzoyl-beta-Ala-Gly-L-Arg + 4-nitroaniline
-
-
-
?
benzoyl-L-Pro-L-Phe-L-Arg 4-nitroanilide + H2O
benzoyl-L-Pro-L-Phe-L-Arg + 4-nitroaniline
-
-
-
?
benzoyl-L-Val-Gly-L-Arg 4-nitroaniline + H2O
benzoyl-L-Val-Gly-L-Arg + 4-nitroaniline
-
-
-
?
benzyloxycarbonyl-Gly-D-Ala-L-Arg 4-nitroanilide + H2O
benzyloxycarbonyl-Gly-D-Ala-L-Arg + 4-nitroaniline
-
-
-
?
benzyloxycarbonyl-Gly-L-Pro-L-Arg 4-nitroanilide + H2O
benzyloxycarbonyl-Gly-L-Pro-L-Arg + 4-nitroaniline
-
-
-
?
benzyloxycarbonyl-Gly-Leu-Gln-Arg-4-methylcoumaryl-7-amide + H2O
benzyloxycarbonyl-Gly-Leu-Gln-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-L-Arg 4-nitroanilide + H2O
benzyloxycarbonyl-L-Arg + 4-nitroaniline
-
-
-
?
benzyloxycarbonyl-L-Arg-L-Arg 4-nitroanilide + H2O
benzyloxycarbonyl-L-Arg-L-Arg + 4-nitroaniline
-
-
-
?
benzyloxycarbonyl-L-Lys 4-nitroanilide + H2O
benzyloxycarbonyl-L-Lys + 4-nitroaniline
-
-
-
?
benzyloxycarbonyl-L-Lys-L-Arg 4-nitroanilide + H2O
benzyloxycarbonyl-L-Lys-L-Arg + 4-nitroaniline
-
-
-
?
benzyloxycarbonyl-L-Phe-L-Arg 4-nitroanilide + H2O
benzyloxycarbonyl-L-Phe-L-Arg + 4-nitroaniline
-
-
-
?
benzyloxycarbonyl-L-Tyr-L-Lys-L-Arg 4-nitroanilide + H2O
benzyloxycarbonyl-L-Tyr-L-Lys-L-Arg + 4-nitroaniline
-
-
-
?
benzyloxycarbonyl-L-Val-Gly-L-Arg 4-nitroanilide + H2O
benzyloxycarbonyl-L-Val-Gly-L-Arg + 4-nitroaniline
-
-
-
?
benzyloxycarbonyl-Ser-Leu-Gly-Arg-4-methylcoumaryl-7-amide + H2O
benzyloxycarbonyl-Ser-Leu-Gly-Arg + 7-amino-4-methylcoumarin
-
-
-
?
Boc-Leu-Ser-Thr-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
?
butyloxycarbonyl-L-Leu-Gly-L-Arg 4-nitroanilide + H2O
butyloxycarbonyl-L-Leu-Gly-L-Arg + 4-nitroaniline
-
-
-
?
butyloxycarbonyl-O-benzoyl-L-Ser-Gly-Arg 4-nitroanilide + H2O
butyloxycarbonyl-O-benzoyl-L-Ser-Gly-Arg + 4-nitroaniline
-
-
-
?
C1-inhibitor P4-P1 fragment + H2O
?
-
-
-
-
?
C1-inhibitor P4-P4' fragment + H2O
?
-
-
-
-
?
C2H5CO-Lys-(epsilon-Cbz)-Gly-Arg-4-nitroanilide + H2O
C2H5CO-Lys-(epsilon-Cbz)-Gly-Arg + 4-nitroaniline
-
-
-
?
C4 complement + H2O
?
-
-
-
?
complement C1q zymogen + H2O
?
C1s-C1q Collagen interface, the three collagen-like peptides form a right-handed helix with a characteristic one residue stagger between adjacent strands, overview
-
-
?
complement C1q zymogen + H2O
active complement C1q + ?
complement C4 + H2O
?
-
-
-
?
complement C4 zymogen + H2O
active complement C4 + ?
-
-
-
?
complement C4-bound C2 zymogen + H2O
C4a + C2b
-
the fragments associate to form a C3 convertase enzyme
-
?
complement C4b-bound C2 + H2O
?
-
-
-
?
complement component C2 + H2O
?
-
-
-
-
?
complement component C2 + H2O
complement component C2a + complement component C2b
complement component C2 P4-P1 fragment + H2O
?
-
-
-
-
?
complement component C2 P4-P4' fragment + H2O
?
-
-
-
-
?
complement component C4 + H2O
?
-
-
-
-
?
complement component C4 + H2O
complement component C4a + complement component C4b
complement component C4 P4-P1 fragment + H2O
?
-
-
-
-
?
complement component C4 P4-P4' fragment + H2O
?
-
-
-
-
?
D-CHG-L-Pro-L-Arg 4-nitroanilide + H2O
D-CHG-L-Pro-L-Arg + 4-nitroaniline
-
-
-
?
D-Ile-L-Phe-L-Lys 4-nitroanilide + H2O
D-Ile-L-Phe-L-Lys + 4-nitroaniline
-
-
-
?
D-Ile-L-Pro-L-Arg 4-nitroanilide + H2O
D-Ile-L-Pro-L-Arg + 4-nitroaniline
-
-
-
?
D-Pro-L-hexahydrotyrosine-L-Arg 4-nitroanilide + H2O
D-Pro-L-hexahydrotyrosine-L-Arg + 4-nitroaniline
-
-
-
?
D-Pro-L-Phe-L-Arg 4-nitroanilide + H2O
D-Pro-L-Phe-L-Arg + 4-nitroaniline
-
-
-
?
D-Val-L-cyclohexylalanine-L-Arg 4-nitroanilide + H2O
D-Val-L-cyclohexylalanine-L-Arg + 4-nitroaniline
-
-
-
?
D-Val-L-Leu-L-Arg 4-nitroanilide + H2O
D-Val-L-Leu-L-Arg + 4-nitroaniline
-
-
-
?
D-Val-L-Leu-L-Lys 4-nitroanilide + H2O
D-Val-L-Leu-L-Lys + 4-nitroaniline
-
-
-
?
D-Val-L-Phe-L-Lys 4-nitroanilide + H2O
D-Val-L-Phe-L-Lys + 4-nitroaniline
-
-
-
?
GLQRA + H2O
GLQR + Ala
-
-
-
?
GLQRAAEI + H2O
GLQR + AAEI
-
-
-
?
GLQRAEEI + H2O
GLQR + AEEI
-
-
-
?
GLQRAFEI + H2O
GLQR + AFEI
-
-
-
?
GLQRAHEI + H2O
GLQR + AHEI
-
-
-
?
GLQRAL + H2O
GLQR + Ala-Leu
-
-
-
?
GLQRALAI + H2O
GLQR + ALAI
-
-
-
?
GLQRALE + H2O
GLQR + ALE
-
-
-
?
GLQRALEA + H2O
GLQR + ALEA
-
-
-
?
GLQRALEE + H2O
GLQR + ALEE
-
-
-
?
GLQRALEF + H2O
GLQR + ALEF
-
-
-
?
GLQRALEH + H2O
GLQR + ALEH
-
-
-
?
GLQRALEI + H2O
GLQR + ALEI
-
-
-
?
GLQRALEK + H2O
GLQR + ALEK
-
-
-
?
GLQRALEL + H2O
GLQR + ALEL
-
-
-
?
GLQRALEM + H2O
GLQR + ALEM
-
-
-
?
GLQRALEP + H2O
GLQR + ALEP
-
-
-
?
GLQRALEQ + H2O
GLQR + ALEQ
-
-
-
?
GLQRALET + H2O
GLQR + ALET
-
-
-
?
GLQRALFI + H2O
GLQR + ALFI
-
-
-
?
GLQRALHI + H2O
GLQR + ALHI
-
-
-
?
GLQRALKI + H2O
GLQR + ALKI
-
-
-
?
GLQRALLI + H2O
GLQR + ALLI
-
-
-
?
GLQRALMI + H2O
GLQR + ALMI
-
-
-
?
GLQRALPI + H2O
GLQR + ALPI
-
-
-
?
GLQRALQI + H2O
GLQR + ALQI
-
-
-
?
GLQRALTI + H2O
GLQR + ALTI
-
-
-
?
GLQRAMEI + H2O
GLQR + AMEI
-
-
-
?
GLQRAPEI + H2O
GLQR + APEI
-
-
-
?
GLQRAQEI + H2O
GLQR + AQEI
-
-
-
?
GLQRATEI + H2O
GLQR + ATEI
-
-
-
?
GLQRELEI + H2O
GLQR + ELEI
-
-
-
?
GLQRFLEI + H2O
GLQR + FLEI
-
-
-
?
GLQRHLEI + H2O
GLQR + HLEI
-
-
-
?
GLQRKLEI + H2O
GLQR + KLEI
-
-
-
?
GLQRLLEI + H2O
GLQR + LLEI
-
-
-
?
GLQRMLEI + H2O
GLQR + MLEI
-
-
-
?
GLQRQLEI + H2O
GLQR + QLEI
-
-
-
?
GLQRTLEI + H2O
GLQR + TLEI
-
-
-
?
Gly-Arg 4-nitroanilide + H2O
Gly-Arg + 4-nitroaniline
-
-
-
?
insulin-like growth factor-binding protein-5 + H2O
?
insulin-like growth factor-I binding protein-5 + H2O
?
-
C1s accounts for the proteolytic activity in human osteoarthritis fluid for insulin-like growth factor-I binding protein-5
-
-
?
kininogen I + H2O
kinin
-
very slow activity
-
?
L-Glu-Gly-L-Arg 4-nitroanilide + H2O
L-Glu-Gly-L-Arg + 4-nitroaniline
-
-
-
?
L-Glu-L-Pro-L-Arg 4-nitroanilide + H2O
L-Glu-L-Pro-L-Arg + 4-nitroaniline
-
-
-
?
methyloxycarbonyl-D-L-hexahydrotyrosine-Gly-L-Arg 4-nitroaniline + H2O
methyloxycarbonyl-D-L-hexahydrotyrosine-Gly-L-Arg + 4-nitroaniline
-
-
-
?
methyloxycarbonyl-D-Nle-Gly-L-Arg 4-nitroaniline + H2O
methyloxycarbonyl-D-Nle-Gly-L-Arg + 4-nitroaniline
-
-
-
?
methyloxycarbonyl-L-cyclohexylglycine-Gly-L-Arg 4-nitroaniline + H2O
methyloxycarbonyl-L-cyclohexylglycine-Gly-L-Arg + 4-nitroaniline
-
-
-
?
N-acetyl-Arg methyl ester + H2O
?
-
-
-
-
?
N-acetyl-Gly-Lys methyl ester + H2O
?
-
-
-
-
?
N-acetyl-Tyr ethyl ester + H2O
N-acetyl-Tyr + ethanol
-
-
-
-
?
N-benzoyl-Phe-Val-Arg p-nitroanilide + H2O
?
-
-
-
-
?
N-benzyloxycarbonyl-Gly-Arg thiobenzyl ester + H2O
?
-
-
-
-
?
N-benzyloxycarbonyl-Lys-p-nitrophenyl ester + H2O
?
N-benzyloxycarbonyl-Tyr-p-nitrophenyl ester + H2O
?
-
-
-
-
?
N2-acetyl-L-Lys-N6-benzyloxycarbonyl-Gly-L-Arg 4-nitroanilide + H2O
N2-acetyl-L-Lys-N6-benzyloxycarbonyl-Gly-L-Arg + 4-nitroaniline
best substrate
-
-
?
N2-acetyl-N6-benzyloxycarbonyl-L-Lys-Gly-L-Arg 4-nitroanilide + H2O
N2-acetyl-N6-benzyloxycarbonyl-L-Lys-Gly-L-Arg + 4-nitroaniline
-
-
-
?
N2-acetyl-N6-benzyloxycarbonyl-Lys-Gly-Arg 4-nitroanilide + H2O
N2-acetyl-N6-benzyloxycarbonyl-Lys-Gly-Arg + 4-nitroaniline
-
-
-
-
?
N6-benzyloxycarbonyl-D-Lys-L-Pro-L-Arg 4-nitroanilide + H2O
N6-benzyloxycarbonyl-D-Lys-L-Pro-L-Arg + 4-nitroaniline
-
-
-
?
Nalpha-acetyl-Tyr ethyl ester + H2O
?
-
-
-
-
?
Nalpha-tosyl-Arg methyl ester + H2O
?
-
-
-
-
?
Sar-L-Pro-L-Arg 4-nitroanilide + H2O
Sar-L-Pro-L-Arg + 4-nitroaniline
-
-
-
?
succinylated casein + H2O
?
-
-
-
?
tert-butyloxycarbonyl-Lys p-nitrophenyl ester + H2O
?
-
-
-
-
?
tert-butyloxycarbonyl-Phe p-nitrophenyl ester + H2O
?
-
-
-
-
?
tert-butyloxycarbonyl-Tyr p-nitrophenyl ester + H2O
?
-
-
-
-
?
Tosyl-Arg methyl ester + H2O
?
-
-
-
-
?
tosyl-Gly-L-Pro-L-Arg 4-nitroanilide + H2O
tosyl-Gly-L-Pro-L-Arg + 4-nitroaniline
-
-
-
?
tosyl-Gly-L-Pro-L-Lys 4-nitroanilide + H2O
tosyl-Gly-L-Pro-L-Lys + 4-nitroaniline
-
-
-
?
Z-AGLQR-7-amido-4-methylcoumarin + H2O
Z-AGLQR + 7-amino-4-methylcoumarin
-
-
-
?
Z-LGR-7-amido-4-methylcoumarin + H2O
Z-LGR + 7-amino-4-methylcoumarin
-
-
-
?
additional information
?
-
2-aminobenzoyl-Gly-Leu-Gln-Arg-Ala-Leu-Glu-Ile-Lys(dinitrophenyl)-NH2 + H2O
2-aminobenzoyl-Gly-Leu-Gln-Arg + Ala-Leu-Glu-Ile-Lys(dinitrophenyl)-NH2
-
-
-
?
2-aminobenzoyl-Gly-Leu-Gln-Arg-Ala-Leu-Glu-Ile-Lys(dinitrophenyl)-NH2 + H2O
2-aminobenzoyl-Gly-Leu-Gln-Arg + Ala-Leu-Glu-Ile-Lys(dinitrophenyl)-NH2
-
-
-
-
?
2-aminobenzoyl-Ser-Leu-Gly-Arg-Lys-Ile-Gln-Ile-Lys(dinitrophenyl)-NH2 + H2O
2-aminobenzoyl-Ser-Leu-Gly-Arg + Lys-Ile-Gln-Ile-Lys(dinitrophenyl)-NH2
-
-
-
?
2-aminobenzoyl-Ser-Leu-Gly-Arg-Lys-Ile-Gln-Ile-Lys(dinitrophenyl)-NH2 + H2O
2-aminobenzoyl-Ser-Leu-Gly-Arg + Lys-Ile-Gln-Ile-Lys(dinitrophenyl)-NH2
-
-
-
-
?
complement C1q zymogen + H2O
active complement C1q + ?
-
-
-
?
complement C1q zymogen + H2O
active complement C1q + ?
no or reduced activity with substrate mutants K59A, K61A, K58A, and K58A/K59A/K61A
-
-
?
complement component C2 + H2O
complement component C2a + complement component C2b
-
-
-
?
complement component C2 + H2O
complement component C2a + complement component C2b
-
-
-
-
?
complement component C2 + H2O
complement component C2a + complement component C2b
-
cleavage of a single bond, likely to be Lys-Lys or Arg-Lys
-
-
?
complement component C2 + H2O
complement component C2a + complement component C2b
-
the P1'-P4' substrate residues of C2 confer greater affinity of substrate for enzyme and also induce a sigmoidal dependence of enzyme velocity on substrate concentration. The substrate gives rise to homotropic positive cooperative behavior in the enzyme
-
?
complement component C4 + H2O
complement component C4a + complement component C4b
-
-
-
?
complement component C4 + H2O
complement component C4a + complement component C4b
-
-
-
-
?
complement component C4 + H2O
complement component C4a + complement component C4b
-
cleavage of a single Arg-Ala bond in the sequence Leu-Gln-Arg-Ala-Leu-Glu
-
-
?
complement component C4 + H2O
complement component C4a + complement component C4b
-
the P1'-P4' substrate residues of C4 confer greater affinity of substrate for enzyme and also induce a sigmoidal dependence of enzyme velocity on substrate concentration. The substrate gives rise to homotropic positive cooperative behavior in the enzyme
-
?
insulin-like growth factor-binding protein-5 + H2O
?
-
no activity with insulin-like growth factor-binding protein-1 through -4
-
?
insulin-like growth factor-binding protein-5 + H2O
?
-
the enzyme accounts for cleavage of insulin-like growth factor-binding protein-5 in fibroblast medium
-
?
N-benzyloxycarbonyl-Lys-p-nitrophenyl ester + H2O
?
-
-
-
-
?
N-benzyloxycarbonyl-Lys-p-nitrophenyl ester + H2O
?
-
N-alpha-benzyloxycarbonyl-L-Lys p-nitrophenyl ester
-
-
?
additional information
?
-
-
the enzyme prefers Arg at P1 3fold over Lys, does not accept citrulline
-
-
?
additional information
?
-
-
importance of the prime subsites of the C1s protease for recognition of substrates no cleavage of GLQRPLEI and GLQRAKEI
-
?
additional information
?
-
-
regulation of the synthesis of the complement enzymes. IFN-gamma increases the synthesis
-
-
?
additional information
?
-
-
binding of C1 to certain viral activators occurs through both C1s and C1q
-
-
?
additional information
?
-
-
the enzyme represents a pivotal upstream point of control in the classical pathway of complement activation
-
?
additional information
?
-
-
C1s is the executioner protease component of the C1 complex in the classical complement pathway cleaving C2 and C4 components of the system, overview
-
-
?
additional information
?
-
-
substrate and active site specificity of C1s in comparison to its equivalent MASP-2 of the lectin complement pathway, overview
-
-
?
additional information
?
-
substrate specificity, library screening, overview. The Lys residue found at the P1' position in C2 and the Gln residue found at the P2 position of C4 are likely to be prohibitive for cleavage of substrates by the C1s protease. The K628Q and K628A mutants of C1s also do not cleave these substrate pools, indicating that K628 does not play a crucial role in preventing interaction with such substrates
-
-
?
additional information
?
-
the enzyme recognizes the a short collagen-like peptide containing the sequence Hyp-Gly-Lys-Leu-Gly-Pro
-
-
?
additional information
?
-
the enzyme cleaves after Arg-/- or Lys-/- and prefers arginine at over 3fold over lysine, the enzyme does not accept citrulline. Occupancy of site S3 may yield an increase in Vmax/Km of over 10fold with the enzyme, but many residues are accepted at positions S2, S3 and S4. No activity with benzyloxycarbonyl-Gly-L-Pro-citrulline 4-nitroanilide
-
-
?
additional information
?
-
-
the enzyme cleaves after Arg-/- or Lys-/- and prefers arginine at over 3fold over lysine, the enzyme does not accept citrulline. Occupancy of site S3 may yield an increase in Vmax/Km of over 10fold with the enzyme, but many residues are accepted at positions S2, S3 and S4. No activity with benzyloxycarbonyl-Gly-L-Pro-citrulline 4-nitroanilide
-
-
?
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.
2-bromo-N-(3'-[[5-carbamimidoyl-2-(methylsulfanyl)thiophen-3-yl]sulfonyl]-2-methylbiphenyl-4-yl)acetamide
-
2-bromo-N-(3'-[[5-carbamimidoyl-2-(methylsulfanyl)thiophen-3-yl]sulfonyl]-6-methylbiphenyl-2-yl)acetamide
-
3'-[[5-carbamimidoyl-2-(methylsulfanyl)thiophen-3-yl]sulfonyl]-6-methylbiphenyl-2-carboxylic acid
-
-
3,4-dichloroisocoumarin
-
-
4-(biphenyl-3-ylsulfonyl)-5-(methylsulfanyl)thiophene-2-carboximidamide
-
-
4-chloro-3-(3-isothiureidopropoxy)isocoumarin
-
best inhibitor among substituted isocoumarins
4-chloro-3-ethoxy-7-guanidinoisocoumarin
-
-
4-chloro-7-guanidino-3-(2-phenylethoxy)isocoumarin
-
-
4-chloro-7-guanidino-3-methoxyisocoumarin
-
-
4-[(2'-chlorobiphenyl-3-yl)sulfonyl]-5-(methylsulfanyl)thiophene-2-carboximidamide
-
-
4-[(2'-ethenylbiphenyl-3-yl)sulfonyl]-5-(methylsulfanyl)thiophene-2-carboximidamide
-
-
4-[(2'-hydroxybiphenyl-3-yl)sulfonyl]-5-(methylsulfanyl)thiophene-2-carboximidamide
-
-
4-[(2'-methoxybiphenyl-3-yl)sulfonyl]-5-(methylsulfanyl)thiophene-2-carboximidamide
-
-
4-[(2'-methylbiphenyl-3-yl)sulfonyl]-5-(methylsulfanyl)thiophene-2-carboximidamide
4-[(2-amino-6-methylphenyl)sulfonyl]-5-(methylsulfanyl)thiophene-2-carboximidamide
-
-
4-[(3'-hydroxybiphenyl-3-yl)sulfonyl]-5-(methylsulfanyl)thiophene-2-carboximidamide
-
-
4-[(3'-methoxybiphenyl-3-yl)sulfonyl]-5-(methylsulfanyl)thiophene-2-carboximidamide
-
-
4-[(3'-methylbiphenyl-3-yl)sulfonyl]-5-(methylsulfanyl)thiophene-2-carboximidamide
-
-
4-[(3-bromophenyl)sulfonyl]-5-(methylsulfanyl)thiophene-2-carboximidamide
-
-
4-[(4'-hydroxybiphenyl-3-yl)sulfonyl]-5-(methylsulfanyl)thiophene-2-carboximidamide
-
-
4-[(4'-methoxybiphenyl-3-yl)sulfonyl]-5-(methylsulfanyl)thiophene-2-carboximidamide
-
-
4-[(4'-methylbiphenyl-3-yl)sulfonyl]-5-(methylsulfanyl)thiophene-2-carboximidamide
-
-
4-[[2'-(hydroxymethyl)-6'-methylbiphenyl-3-yl]sulfonyl]-5-(methylsulfanyl)thiophene-2-carboximidamide
-
-
4-[[2'-(hydroxymethyl)biphenyl-3-yl]sulfonyl]-5-(methylsulfanyl)thiophene-2-carboximidamide
-
-
4-[[3-(3-methylpyridin-2-yl)phenyl]sulfonyl]-5-(methylsulfanyl)thiophene-2-carboximidamide
-
-
5-(methylsulfanyl)-4-[[2'-methyl-6'-([[2-(2H-tetrazol-5-yl)ethyl]carbamoyl]amino)biphenyl-3-yl]sulfonyl]thiophene-2-carboximidamide
-
-
6-[(3'-[[5-carbamimidoyl-2-(methylsulfanyl)thiophen-3-yl]sulfonyl]-6-methylbiphenyl-2-yl)amino]-6-oxohexanoic acid
-
-
6-[[(3'-[[5-carbamimidoyl-2-(methylsulfanyl)thiophen-3-yl]sulfonyl]-6-methylbiphenyl-2-yl)carbamoyl]amino]hexanoic acid
-
-
7-amino-4-chloro-3-(3-isothiureidopropoxy)isocoumarin
-
-
C-1 esterase inhibitor
-
main inhibitor of C1r and C1s of the complement system
-
FUT175
-
potent C1s inhibitor
human C1-esterase inhibitor
C1-INH, a multifunctional plasma protein with a wide range of inhibitory and non-inhibitory properties, mainly recognized as a key downregulator of the complement and contact cascades. Potentiation of C1-INH by heparin and other glycosaminoglycans regulating a broad spectrum of C1-INH activities in vivo both in normal and disease states, interaction analysis via double capture SPR approach, surface plasmon resonance (using a CM5 sensor chip through amine coupling) and circular dichroism, overview. Heparin binding does not alter C1-INH secondary structure and does not affect the amidolytic activity of C1s, but does accelerate its consumption due to C1-INH potentiation
-
N-(3'-[[5-carbamimidoyl-2-(methylsulfanyl)thiophen-3-yl]sulfonyl]-6-methylbiphenyl-2-yl)-2-(methylsulfonyl)acetamide
-
-
N-(3'-[[5-carbamimidoyl-2-(methylsulfanyl)thiophen-3-yl]sulfonyl]-6-methylbiphenyl-2-yl)-4-(methylsulfonyl)butanamide
-
-
N-PEG2000 6-[[(3'-[[5-carbamimidoyl-2-(methylsulfanyl)-2,3-dihydrothiophen-3-yl]sulfonyl]-6-methylbiphenyl-2-yl)carbamoyl]amino]hexanamide
PEG size 20 kDa
N-PEG2000 N-(3'-[[5-carbamimidoyl-2-(methylsulfanyl)-2,3-dihydrothiophen-3-yl]sulfonyl]-6-methylbiphenyl-2-yl)dodecanediamide
PEG size 20 kDa
N-PEG4000 6-[[(3'-[[5-carbamimidoyl-2-(methylsulfanyl)-2,3-dihydrothiophen-3-yl]sulfonyl]-6-methylbiphenyl-2-yl)carbamoyl]amino]hexanamide
PEG size 40 kDa
N-PEG750 2-[(2-amino-2-oxoethyl)sulfanyl]-N-(3'-[[5-carbamimidoyl-2-(methylsulfanyl)-2,3-dihydrothiophen-3-yl]sulfonyl]-6-methylbiphenyl-2-yl)acetamide
PEG size 10 kDa; PEG size 20 kDa
N-PEG750 2-[(2-amino-2-oxoethyl)sulfanyl]-N-(3'-[[5-carbamimidoyl-2-(methylsulfanyl)thiophen-3-yl]sulfonyl]-2-methylbiphenyl-4-yl)acetamide
-
N-PEG750 2-[(2-amino-2-oxoethyl)sulfanyl]-N-(3'-[[5-carbamimidoyl-2-(methylsulfanyl)thiophen-3-yl]sulfonyl]-6-methylbiphenyl-2-yl)acetamide
PEG size 0.75 kDa
p-nitrophenyl-p'-guanidinobenzoate
-
-
PEG-linked bis(6-[[(4-carbamimidamido-3'-[[5-carbamimidoyl-2-(methylsulfanyl)thiophen-3-yl]sulfonyl]-6-methylbiphenyl-2-yl)carbamoyl]amino]hexanamide)
PEG size 20 kDa
PEG-linked bis(N-[6-amino-5-[(4-carbamimidamido-3'-[[5-carbamimidoyl-2-(methylsulfanyl)thiophen-3-yl]sulfonyl]-6-methylbiphenyl-2-yl)amino]hept-6-en-1-yl]-6-[[(4-carbamimidamido-3'-[[5-carbamimidoyl-2-(methylsulfanyl)thiophen-3-yl]sulfanyl]biphenyl-2-yl)carbamoyl]amino]hexanamide)
-
-
PEG-linked tetrakis(4-[[4'-carbamimidamido-2'-(carbamoylamino)biphenyl-3-yl]sulfanyl]-5-(methylsulfanyl)thiophene-2-carboximidamide)
PEG size 20 kDa
-
serine protease inhibitor 1
-
-
-
serine protease inhibitor 2
-
-
-
tert-butyl [[4-[(3-bromophenyl)sulfonyl]-5-(methylsulfanyl)thiophen-2-yl](imino)methyl]carbamate
-
binding mode in the active site, structure, overview
TNT003
a mouse monoclonal antibody targeting the CP-specific serine protease C1s. TNT003 prevents cold agglutinin-mediated deposition of complement opsonins that promote phagocytosis of red blood cells. By preventing classical pathway activation, TNT003 also prevents cold agglutinin-driven generation of anaphylatoxins
-
unconjugated bilirubin
-
inhibits C1 esterase activity at pathological concentrations (above 17 micromol) and in a dose-dependent manner, due to a direct pigment-protein interaction. Maximal inhibitory activity is reached at an 85 micromol concentration. Inhibitory action exerted by unconjugated bilirubin on the classical pathway is not only due to an impairment of the interaction of the C1q subcomponent with IgM or IgG but also to a diminished enzymatic activity of the C1 esterase
4-[(2'-methylbiphenyl-3-yl)sulfonyl]-5-(methylsulfanyl)thiophene-2-carboximidamide
-
4-[(2'-methylbiphenyl-3-yl)sulfonyl]-5-(methylsulfanyl)thiophene-2-carboximidamide
-
-
C1 esterase inhibitor
-
severe abdominal attacks are effectively reverted with C1 inhibitor plasma concentrate
-
C1 esterase inhibitor
-
C1 esterase inhibitor inhibits components of the complement (specifically C1r and C1s), C1 esterase inhibitor concentrate given intravenously at a dose of 20 units/kg is an effective and safe treatment for acute abdominal and facial attacks in patients with hereditary angioedema
-
C1 esterase inhibitor
-
-
-
C1 esterase inhibitor
-
-
-
C1 esterase inhibitor
-
administration of C1 esterase inhibitor with factor XIII and of N-acetylcysteine with tirilazad mesylate both results in reduced leucocyte adherence and reduced levels of interleukin-1beta, but increases interleukin-6 levels
-
C1-esterase inhibitor
inhibitory effect is increased by addition of heparin (5-500 nM)
-
C1-esterase inhibitor
-
-
-
C1-inhibitor
-
a serpin
-
C1bar inhibitor
-
kinetics of reaction of human C1-inhibitor with C1sbar
-
C1bar inhibitor
-
kinetics of reaction of human C1-inhibitor with C1sbar
-
C1s-INH-248
-
highly selective small molecule inhibitor. Blocking the classical complement pathway with a highly specific and potent synthetic inhibitor of the classical C1 complex appears to be an effective mean to preserve ischemic myocardium from injury following reperfusion
-
C1s-INH-248
-
highly selective small molecule inhibitor. Blocking the classical complement pathway with a highly specific and potent synthetic inhibitor of the classical C1 complex appears to be an effective mean to preserve ischemic myocardium from injury following reperfusion
-
additional information
-
optimization of thiopheneamidine-based inhibitors
-
additional information
design and synthesis of polyethylene glycol-modified biphenylsulfonyl-thiophene-carboxamidine inhibitors of the complement component C1s, overview. Pegylation strategy to improve the pharmacokinetic properties of a potent C1s inhibitor 9. Analysis of the structure-activity relationship studies on the small molecule 1
-
additional information
engineering of a potenthuman antibody inhibitor of C1s protease activity, inhibition of recombinnat enzyme fragment CCP2-SP, overview. The C1 complex is a very attractive target for selective inhibition of the classical complement pathway because it is the only member of the classical pathway that does not participate in the other complement pathways
-
additional information
-
engineering of a potenthuman antibody inhibitor of C1s protease activity, inhibition of recombinnat enzyme fragment CCP2-SP, overview. The C1 complex is a very attractive target for selective inhibition of the classical complement pathway because it is the only member of the classical pathway that does not participate in the other complement pathways
-
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.
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.
Gal, P.; Zavodzky, P.
Structure and function of the serine-protease subcomponents of C1: protein engineering studies
Immunobiology
199
317-326
1998
Homo sapiens
brenda
Sim, R.B.; Porter, R.R.; Reid, K.B.M.; Gigli, I.
The structure and enzymic activities of the C1r and C1s subcomponents of C1, the first component of human serum complement
Biochem. J.
163
219-227
1977
Homo sapiens
brenda
Sim, R.; Arlaud, G.J.; Colomb, M.G.
Kinetics of reaction of human C1bar-inhibitor with the human complement system proteases C1rbar and C1sbar
Biochim. Biophys. Acta
612
433-449
1980
Homo sapiens
brenda
Sim, R.B.
The human complement system serine proteases C1bar and C1sbar and their proenzymes
Methods Enzymol.
80
26-42
1981
Homo sapiens
brenda
Nilsson, T.; Wiman, B.
Kinetics of the reaction between human C1-esterase inhibitor and C1r or C1s
Eur. J. Biochem.
129
663-667
1983
Homo sapiens
brenda
Reboul, A.; Bensa, J.C.; Colomb, M.G.
Characteristics of complement subcomponents C1r and C1s synthesized by Hep G2 cells
Biochem. J.
233
559-564
1986
Homo sapiens
brenda
Thielens, N.M.; Aude, C.A.; Lacroix, M.B.; Gagnon, J.; Arlaud, G.J.
Ca2+ binding properties and Ca2+-dependent interactions of the isolated NH2-terminal alpha fragments of human complement proteases C1rbar and C1sbar
J. Biol. Chem.
265
14469-14475
1990
Homo sapiens
brenda
Katz, Y.; Guterman, M.; Lahat, E.
Regulation of synthesis of complement proteins in HEp2 cells
Clin. Immunol. Immunopathol.
67
117-123
1993
Homo sapiens
brenda
Zavodszky, P.; Gal, P.; Cseh, S.; Schumaker, V.N.
Protein engineering studies on C1r and C1s
Behring Inst. Mitt.
93
103-114
1993
Homo sapiens
brenda
Gulati, P.; Lemercier, C.; Guc, D.; Lappin, D.; Whaley, K.
Regulation of the synthesis of C1 subcomponents and C1-inhibitor
Behring Inst. Mitt.
93
196-203
1993
Homo sapiens
brenda
Arlaud, G.J.; Thielens, N.M.
Human complement serine proteases C1r and C1s and their proenzymes
Methods Enzymol.
223
61-82
1993
Homo sapiens
brenda
Kam, C.M.; Oglesby, T.J.; Pangburn, M.K.; Volanakis, J.E.; Powers, J.C.
Substituted isocoumarins as inhibitors of complement serine proteases
J. Immunol.
149
163-168
1992
Homo sapiens
brenda
Loos, M.; Heinz, H.P.; Clas, F.
C1sbar-esterase
Methods Enzym. Anal. , 3rd Ed. (Bergmeyer, H. U. , ed. )
5
527-536
1984
Homo sapiens
-
brenda
Morgan, P.H.; Nair, I.G.
Hydrolysis of a synthetic amide substrate by human C1 esterase (C1sbar)
J. Immunol.
119
19-25
1977
Homo sapiens
brenda
Sumi, H.; Muramatu, M.
Purification and partial characterization of human C1-esterase
Agric. Biol. Chem.
38
605-611
1974
Homo sapiens
-
brenda
Bing, D.H.
Purification of the first component of human complement and its subunit C1 esterase
Methods Enzymol.
34B
731-746
1974
Homo sapiens
brenda
Tsai, S.W.; Poon, P.H.; Schumaker, V.N.
Expression and characterization of a 159 amino acid, N-terminal fragment of human complement component C1s
Mol. Immunol.
34
1273-1280
1997
Homo sapiens
brenda
Sakiyama, H.; Nishida, M.; Sakai, N.; Nagino, K.; Miyatake, S.; Saito, T.
Site-directed mutagenesis of hamster complement C1s: characterization with an active form-specific antibody and possible involvement of cis in tumorgenicity
Int. J. Cancer
66
768-771
1996
Mesocricetus auratus
brenda
Skoog, M.T.; Mehdi, S.; Wiseman, J.S.; Bey, P.
The specificity of two proteinases that cleave adjacent to arginine, C1 esterase and acrosin, for peptide p-nitroanilide substrates
Biochim. Biophys. Acta
996
89-94
1989
Homo sapiens
brenda
O'Brien, G.; Quinsey, N.S.; Whisstock, J.C.; Pike, R.N.
Importance of the prime subsites of the C1s protease of the classical complement pathway for recognition of substrates
Biochemistry
42
14939-14945
2003
Homo sapiens
brenda
Subasinghe, N.L.; Ali, F.; Illig, C.R.; Jonathan Rudolph, M.; Klein, S.; Khalil, E.; Soll, R.M.; Bone, R.F.; Spurlino, J.C.; DesJarlais, R.L.; Crysler, C.S.; Cummings, M.D.; Morris, P.E., Jr.; Kilpatrick, J.M.; Sudhakara Babu, Y.
A novel series of potent and selective small molecule inhibitors of the complement component C1s
Bioorg. Med. Chem. Lett.
14
3043-3047
2004
Homo sapiens
brenda
Gaboriaud, C.; Rossi, V.; Bally, I.; Arlaud, G.J.; Fontecilla-Camps, J.C.
Crystal structure of the catalytic domain of human complement C1s: a serine protease with a handle
EMBO J.
19
1755-1765
2000
Homo sapiens
brenda
Busby, W.H., Jr.; Nam, T.J.; Moralez, A.; Smith, C.; Jennings, M.; Clemmons, D.R.
The complement component C1s is the protease that accounts for cleavage of insulin-like growth factor-binding protein-5 in fibroblast medium
J. Biol. Chem.
275
37638-37644
2000
Homo sapiens
brenda
Buerke, M.; Schwertz, H.; Seitz, W.; Meyer, J.; Darius, H.
Novel small molecule inhibitor of C1s exerts cardioprotective effects in ischemia-reperfusion injury in rabbits
J. Immunol.
167
5375-5380
2001
Oryctolagus cuniculus, Homo sapiens
brenda
Harmat, V.; Gal, P.; Kardos, J.; Szilagyi, K.; Ambrus, G.; Vegh, B.; Naray-Szabo, G.; Zavodszky, P.
The structure of MBL-associated serine protease-2 reveals that identical substrate specificities of C1s and MASP-2 are realized through different sets of enzyme-substrate interactions
J. Mol. Biol.
342
1533-1546
2004
Homo sapiens
brenda
Rossi, V.; Teillet, F.; Thielens, N.M.; Bally, I.; Arlaud, G.J.
Functional characterization of complement proteases C1s/mannan-binding lectin-associated serine protease-2 (MASP-2) chimeras reveals the higher C4 recognition efficacy of the MASP-2 complement control protein modules
J. Biol. Chem.
280
41811-41818
2005
Homo sapiens
brenda
Kerr, F.K.; OBrien, G.; Quinsey, N.S.; Whisstock, J.C.; Boyd, S.; de la Banda, M.G.; Kaiserman, D.; Matthews, A.Y.; Bird, P.I.; Pike, R.N.
Elucidation of the substrate specificity of the C1s protease of the classical complement pathway
J. Biol. Chem.
280
39510-39514
2005
Homo sapiens
brenda
Bally, I.; Rossi, V.; Thielens, N.M.; Gaboriaud, C.; Arlaud, G.J.
Functional role of the linker between the complement control protein modules of complement protease C1s
J. Immunol.
175
4536-4542
2005
Homo sapiens
brenda
Gosalia, D.N.; Salisbury, C.M.; Ellman, J.A.; Diamond, S.L.
High throughput substrate specificity profiling of serine and cysteine proteases using solution-phase fluorogenic peptide microarrays
Mol. Cell. Proteomics
4
626-636
2005
Homo sapiens
brenda
Gaboriaud, C.; Thielens, N.M.; Gregory, L.A.; Rossi, V.; Fontecilla-Camps, J.C.; Arlaud, G.J.
Structure and activation of the C1 complex of complement: unraveling the puzzle
Trends Immunol.
25
368-373
2004
Homo sapiens
brenda
Travins, J.M.; Ali, F.; Huang, H.; Ballentine, S.K.; Khalil, E.; Hufnagel, H.R.; Pan, W.; Gushue, J.; Leonard, K.; Bone, R.F.; Soll, R.M.; DesJarlais, R.L.; Crysler, C.S.; Ninan, N.; Kirkpatrick, J.; Cummings, M.D.; Huebert, N.; Molloy, C.J.; Gaul, M.; Tomczuk, B.E.; Subasinghe, N.L.
Biphenylsulfonyl-thiophene-carboxamidine inhibitors of the complement component C1s
Bioorg. Med. Chem. Lett.
18
1603-1606
2008
Rattus norvegicus
brenda
Kerr, F.K.; Thomas, A.R.; Wijeyewickrema, L.C.; Whisstock, J.C.; Boyd, S.E.; Kaiserman, D.; Matthews, A.Y.; Bird, P.I.; Thielens, N.M.; Rossi, V.; Pike, R.N.
Elucidation of the substrate specificity of the MASP-2 protease of the lectin complement pathway and identification of the enzyme as a major physiological target of the serpin, C1-inhibitor
Mol. Immunol.
45
670-677
2008
Homo sapiens
brenda
Boyd, S.E.; Kerr, F.K.; Albrecht, D.W.; de la Banda, M.G.; Ng, N.; Pike, R.N.
Cooperative effects in the substrate specificity of the complement protease C1s
Biol. Chem.
390
503-507
2009
unidentified
brenda
Arriaga, S.M.; Basiglio, C.L.; Mottino, A.D.; Almara, A.M.
Unconjugated bilirubin inhibits C1 esterase activity
Clin. Biochem.
42
919-921
2009
Homo sapiens
brenda
Birnbaum, J.; Klotz, E.; Spies, C.D.; Hein, O.V.; Mallin, K.; Kawka, R.; Ziemer, S.; Lehmann, C.
The combinations C1 esterase inhibitor with coagulation factor XIII and N-acetylcysteine with tirilazad mesylate reduce the leukocyte adherence in an experimental endotoxemia in rats
Clin. Hemorheol. Microcirc.
40
167-176
2008
Rattus norvegicus
brenda
Hong, S.B.; Kim, C.W.; Kim, J.H.; Kim, J.S.; Han, S.B.
A case of angioedema due to acquired C1 esterase inhibitor deficiency masquerading as suspected peritonitis: A case report
J. Emerg. Med.
41
e99-e101
2011
Homo sapiens
brenda
Abe, K.; Endo, Y.; Nakazawa, N.; Kanno, K.; Okubo, M.; Hoshino, T.; Fujita, T.
Unique phenotypes of C1s deficiency and abnormality caused by two compound heterozygosities in a Japanese family
J. Immunol.
182
1681-1688
2009
Homo sapiens (P09871)
brenda
Birnbaum, J.; Klotz, E.; Spies, C.D.; Mueller, J.; Vargas Hein, O.; Feller, J.; Lehmann, C.
Impact of combined C1 esterase inhibitor/coagulation factor XIII or N-acetylcysteine/tirilazad mesylate administration on leucocyte adherence and cytokine release in experimental endotoxaemia
J. Int. Med. Res.
36
748-759
2008
Rattus norvegicus
brenda
Busby, W.H.; Yocum, S.A.; Rowland, M.; Kellner, D.; Lazerwith, S.; Sverdrup, F.; Yates, M.; Radabaugh, M.; Clemmons, D.R.
Complement 1s is the serine protease that cleaves IGFBP-5 in human osteoarthritic joint fluid
Osteoarthritis Cartilage
17
547-555
2009
Homo sapiens
brenda
Dagen, C.; Craig, T.J.
Treatment of hereditary angioedema: items that need to be addressed in practice parameters
Allergy Asthma Clin. Immunol.
6
11
2010
Homo sapiens
brenda
Craig, T.J.; Levy, R.J.; Wasserman, R.L.; Bewtra, A.K.; Hurewitz, D.; Obtulowicz, K.; Reshef, A.; Ritchie, B.; Moldovan, D.; Shirov, T.; Grivcheva-Panovska, V.; Kiessling, P.C.; Keinecke, H.O.; Bernstein, J.A.
Efficacy of human C1 esterase inhibitor concentrate compared with placebo in acute hereditary angioedema attacks
J. Allergy Clin. Immunol.
124
801-808
2009
Homo sapiens
brenda
Grosskinsky, S.; Schott, M.; Brenner, C.; Cutler, S.J.; Simon, M.M.; Wallich, R.
Human complement regulators C4b-binding protein and C1 esterase inhibitor interact with a novel outer surface protein of Borrelia recurrentis
PLoS Negl. Trop. Dis.
4
e698
2010
Homo sapiens
brenda
Rajabi, M.; Struble, E.; Zhou, Z.; Karnaukhova, E.
Potentiation of C1-esterase inhibitor by heparin and interactions with C1s protease as assessed by surface plasmon resonance
Biochim. Biophys. Acta
1820
56-63
2011
Homo sapiens, Homo sapiens (P09871)
brenda
Brier, S.; Pflieger, D.; Le Mignon, M.; Bally, I.; Gaboriaud, C.; Arlaud, G.J.; Daniel, R.
Mapping surface accessibility of the C1r/C1s tetramer by chemical modification and mass spectrometry provides new insights into assembly of the human C1 complex
J. Biol. Chem.
285
32251-32263
2010
Homo sapiens
brenda
Subasinghe, N.L.; Khalil, E.; Travins, J.M.; Ali, F.; Ballentine, S.K.; Hufnagel, H.R.; Pan, W.; Leonard, K.; Bone, R.F.; Soll, R.M.; Crysler, C.S.; Ninan, N.; Kirkpatrick, J.; Kolpak, M.X.; Diloreto, K.A.; Eisennagel, S.H.; Huebert, N.D.; Molloy, C.J.; Tomczuk, B.E.; Gaul, M.D.
Design and synthesis of polyethylene glycol-modified biphenylsulfonyl-thiophene-carboxamidine inhibitors of the complement component C1s
Bioorg. Med. Chem. Lett.
22
5303-5307
2012
Homo sapiens (P09871)
brenda
Shi, J.; Rose, E.L.; Singh, A.; Hussain, S.; Stagliano, N.E.; Parry, G.C.; Panicker, S.
TNT003, an inhibitor of the serine protease C1s, prevents complement activation induced by cold agglutinins
Blood
123
4015-4022
2014
Homo sapiens (P09871), Homo sapiens
brenda
Wijeyewickrema, L.C.; Duncan, R.C.; Pike, R.N.
The role of the lys628 (192) residue of the complement protease, C1s, in interacting with peptide and protein substrates
Front. Immunol.
5
444
2014
Homo sapiens (P09871)
brenda
Carroll, S.; Georgiou, G.
Antibody-mediates inhibition of human C1s and the classical complement pathway
Immunobiology
218
1041-1048
2013
Homo sapiens (P09871), Homo sapiens
brenda
Wijeyewickrema, L.C.; Yongqing, T.; Tran, T.P.; Thompson, P.E.; Viljoen, J.E.; Coetzer, T.H.; Duncan, R.C.; Kass, I.; Buckle, A.M.; Pike, R.N.
Molecular determinants of the substrate specificity of the complement-initiating protease, C1r
J. Biol. Chem.
288
15571-15580
2013
Homo sapiens (P09871)
brenda
Venkatraman Girija, U.; Gingras, A.R.; Marshall, J.E.; Panchal, R.; Sheikh, M.A.; Gal, P.; Schwaeble, W.J.; Mitchell, D.A.; Moody, P.C.; Wallis, R.
Structural basis of the C1q/C1s interaction and its central role in assembly of the C1 complex of complement activation
Proc. Natl. Acad. Sci. USA
110
13916-13920
2013
Homo sapiens (P09871)
brenda
Bally, I.; Ancelet, S.; Moriscot, C.; Gonnet, F.; Mantovani, A.; Daniel, R.; Schoehn, G.; Arlaud, G.J.; Thielens, N.M.
Expression of recombinant human complement C1q allows identification of the C1r/C1s-binding sites
Proc. Natl. Acad. Sci. USA
110
8650-8655
2013
Homo sapiens (P09871)
brenda
Beveridge, A.J.; Wallis, R.; Samani, N.J.
A molecular dynamics study of C1r and C1s dimers: implications for the structure of the C1 complex
Proteins
80
1987-1997
2012
Homo sapiens (P09871)
brenda
Skoog, S.M.; Wiseman, J.S.; Bey, P.
The specificity of two proteinases that cleave adjacent to argirnine, Cl esterase and acrosin, for pepfide p-nitroanilide substrates
Biochim. Biophys. Acta
996
89.94
1989
Homo sapiens (P09871), Homo sapiens
brenda
Kapferer-Seebacher, I.; Pepin, M.; Werner, R.; Aitman, T.J.; Nordgren, A.; Stoiber, H.; Thielens, N.; Gaboriaud, C.; Amberger, A.; Schossig, A.; Gruber, R.; Giunta, C.; Bamshad, M.; Bjoerck, E.; Chen, C.; Chitayat, D.; Dorschner, M.; Schmitt-Egenolf, M.; Hale, C.J.; Hanna, D.; Hennies, H.C.; Heiss-Kisielewsky, I.
Periodontal Ehlers-Danlos syndrome is caused by mutations in C1R and C1S, which encode subcomponents C1r and C1s of complement
Am. J. Hum. Genet.
99
1005-1014
2016
Homo sapiens (P09871)
brenda
Li, S.; Yu, B.; Byrne, G.; Wright, M.; ORourke, S.; Mesa, K.; Berman, P.W.
Identification and CRISPR/Cas9 knockout of the endogenous C1s protease in CHO cells eliminates aberrant proteolysis of recombinantly expressed proteins
Biotechnol. Bioeng.
116
2130-2145
2019
Homo sapiens
brenda
Jaeger, U.; DSa, S.; Schoergenhofer, C.; Bartko, J.; Derhaschnig, U.; Sillaber, C.; Jilma-Stohlawetz, P.; Fillitz, M.; Schenk, T.; Patou, G.; Panicker, S.; Parry, G.C.; Gilbert, J.C.; Jilma, B.
Inhibition of complement C1s improves severe hemolytic anemia in cold agglutinin disease a first-in-human trial
Blood
133
893-901
2019
Homo sapiens
brenda
Nilojan, J.; Bathige, S.D.N.K.; Kugapreethan, R.; Yang, H.; Kim, M.J.; Nam, B.H.; Lee, J.
Molecular features and the transcriptional and functional delineation of complement system activators C1r and C1s from Sebastes schlegelii
Dev. Comp. Immunol.
81
279-290
2018
Sebastes schlegelii (A0A2I6BQK3)
brenda
Godahewa, G.I.; Bathige, S.D.; Herath, H.M.; Noh, J.K.; Lee, J.
Characterization of rock bream (Oplegnathus fasciatus) complement components C1r and C1s in terms of molecular aspects, genomic modulation, and immune responsive transcriptional profiles following bacterial and viral pathogen exposure
Fish Shellfish Immunol.
46
656-668
2015
Oplegnathus fasciatus (A0A0K0LFC9)
brenda
Almitairi, J.O.M.; Venkatraman Girija, U.; Furze, C.M.; Simpson-Gray, X.; Badakshi, F.; Marshall, J.E.; Schwaeble, W.J.; Mitchell, D.A.; Moody, P.C.E.; Wallis, R.
Structure of the C1r-C1s interaction of the C1 complex of complement activation
Proc. Natl. Acad. Sci. USA
115
768-773
2018
Homo sapiens (P09871)
brenda