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Information on EC 3.4.22.52 - calpain-1 and Organism(s) Homo sapiens and UniProt Accession P07384

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     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.22 Cysteine endopeptidases
                3.4.22.52 calpain-1
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Select one or more organisms in this record:
This record set is specific for:
Homo sapiens
UNIPROT: P07384 not found.
Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
broad endopeptidase specificity
Synonyms
calcium-activated neutral protease I, calpain 1, calpain 1-gamma, calpain 1A, calpain I, calpain small subunit, calpain-1, calpain-1 (micro-form), calpain-I, calpain1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
calcium-activated neutral protease I
-
-
-
-
calpain 1
calpain I
calpain-1
247
-
calpain-I
247
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calpain1
247
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CAPN1
247
-
CAPN1 g.p. (Homo sapiens)
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-
m-CANP
247
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micro-calpain
mu-calpain
muCANP
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muI-II
247
calpain 1 protease core
CAS REGISTRY NUMBER
COMMENTARY hide
689772-75-6
-
78990-62-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(4-(4-dimethylaminophenylazo)benzoyl)-TPLKSPPPSPR-(5[(2-aminoethyl)amino]naphthalene-1-sulfonic acid) + H2O
(4-(4-dimethylaminophenylazo)benzoyl)-TPLK + SPPPSPR-(5[(2-aminoethyl)amino]naphthalene-1-sulfonic acid)
show the reaction diagram
-
-
-
-
?
(5(6)-carboxyfluorescin)-GGGQLYGG-(Nbeta-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-RRK-(5- and 6-carboxytetramethylrhodamine)-OH + H2O
(5(6)-carboxyfluorescin)-GGGQLY + GG-(Nbeta-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-RRK-(5- and 6-carboxytetramethylrhodamine)-OH
show the reaction diagram
-
-
-
-
?
(EDANS)-EALFAERK-(DABCYL) + H2O
(EDANS)-EA + LFAERK-(DABCYL)
show the reaction diagram
-
about 30% cleavage preference
-
-
?
(EDANS)-EPLFAARK-(DABCYL) + H2O
(EDANS)-EPLFA + ARK-(DABCYL)
show the reaction diagram
-
the sequence PLFAAR is an even better substrate for the calpain 1 protease core than PLFAER, 100% cleavage preference
-
-
?
(EDANS)-EPLFAERK-(DABCYL) + H2O
(EDANS)-EPLFA + ERK-(DABCYL)
show the reaction diagram
-
about 40% cleavage preference
-
-
?
(EDANS)-EPLFGERK-(DABCYL) + H2O
(EDANS)-EPLF + GERK-(DABCYL)
show the reaction diagram
-
less than 20% cleavage preference
-
-
?
(EDANS)-EPLFMERK-(DABCYL) + H2O
(EDANS)-EPLF + MERK-(DABCYL)
show the reaction diagram
-
the peptide sequence PLFMER is rapidly cleaved by the calpain 1 core at the F-M bond with about 45% cleavage preference
-
-
?
2-aminobenzoyl-EVYGMMY(3-NO2)-OH + H2O
2-aminobenzoyl-EVY + GMMY(3-NO2)-OH
show the reaction diagram
-
-
-
-
?
4,4-difluoro-5,7-dimethyl-4-bora-31,4a-diaza-s-indacene-3-propioyl-labeled casein + H2O
?
show the reaction diagram
-
-
-
-
?
5-([4,6-dichlorotriazin-2-yl]amino)fluorescin-labeled microtubule-associated protein 2 + H2O
?
show the reaction diagram
-
-
-
-
?
7-methoxycoumarin-4-acetyl-GGGNIFGG-(Nbeta-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-KK-OH + H2O
7-methoxycoumarin-4-acetyl-GGGNIF + GG-(Nbeta-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-KK-OH
show the reaction diagram
-
-
-
-
?
7-methoxycoumarin-4-acetyl-GGGNIYGG-(Nbeta-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-KK-OH + H2O
7-methoxycoumarin-4-acetyl-GGGNIY + GG-(Nbeta-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-KK-OH
show the reaction diagram
-
-
-
-
?
7-methoxycoumarin-4-acetyl-GGGNLFGG-(Nbeta-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-KK-OH + H2O
7-methoxycoumarin-4-acetyl-GGGNLF + GG-(Nbeta-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-KK-OH
show the reaction diagram
-
-
-
-
?
7-methoxycoumarin-4-acetyl-GGGNLYGG-(Nbeta-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-KK-OH + H2O
7-methoxycoumarin-4-acetyl-GGGNLY + GG-(Nbeta-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-KK-OH
show the reaction diagram
-
-
-
-
?
7-methoxycoumarin-4-acetyl-GGGQIFGG-(Nbeta-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-KK-OH + H2O
7-methoxycoumarin-4-acetyl-GGGQIF + GG-(Nbeta-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-KK-OH
show the reaction diagram
-
-
-
-
?
7-methoxycoumarin-4-acetyl-GGGQLFGG-(Nbeta-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-KK-OH + H2O
7-methoxycoumarin-4-acetyl-GGGQLF + GG-(Nbeta-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-KK-OH
show the reaction diagram
-
-
-
-
?
7-methoxycoumarin-4-acetyl-GGGQLYGG-(Nbeta-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-KK-OH + H2O
7-methoxycoumarin-4-acetyl-GGGQLY + GG-(Nbeta-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-KK-OH
show the reaction diagram
-
-
-
-
?
acetyl-Leu-Leu-Tyr-7-amido-4-trifluoromethyl coumarin + H2O
?
show the reaction diagram
-
-
-
-
?
acetyl-LLY-7-amido-4-fluoromethylcoumarin + H2O
acetyl-LLY + 7-amino-4-fluoromethylcoumarin
show the reaction diagram
-
-
-
-
?
alpha-actinin + H2O
?
show the reaction diagram
-
-
-
-
?
alpha-fodrin + H2O
?
show the reaction diagram
-
-
-
-
?
alpha-spectrin + H2O
?
show the reaction diagram
-
-
-
-
?
alpha-subunit of fodrin + H2O
150000 Da fragment + ?
show the reaction diagram
-
-
-
?
alpha-synuclein + H2O
145000 DA fragment + 150 Da fragment + ?
show the reaction diagram
-
-
-
-
?
alphaII-spectrin + H2O
?
show the reaction diagram
-
Fanconi anemia proteins play an important role in maintaining the stability of alphaII-spectrin in the cell by regulating its cleavage by mu-calpain
-
-
?
apoptosis-inducing factor + H2O
?
show the reaction diagram
beta-integrin + H2O
?
show the reaction diagram
-
-
-
-
?
BH3-only Bcl2 interacting domain + H2O
?
show the reaction diagram
-
BH3-only Bcl2 interacting domain is a direct target of a soluble active calpain 1 present in cells expressing hepatitis C virus proteins
-
-
?
casein + H2O
?
show the reaction diagram
-
-
-
-
?
caspase-7 + H2O
?
show the reaction diagram
-
recombinant caspase-7 is directly cleaved and activated by calpain-1 within the large subunit of caspase-7 to produce the large subunit p18 and p17
-
-
?
desmin + H2O
?
show the reaction diagram
-
-
-
-
?
dye-Gln-Gln-Gln-Glu-Val-Tyr-Gly-Met-Met-Pro-Arg-Asp-pSer-Ala + H2O
dye-Gln-Gln-Gln-Glu-Val-Tyr + Gly-Met-Met-Pro-Arg-Asp-pSer-Ala
show the reaction diagram
-
-
-
-
?
E-(EDANS-)PLF-AERK-(Dabcyl) + H2O
?
show the reaction diagram
-
-
-
-
?
filamin A + H2O
?
show the reaction diagram
-
-
-
-
?
fluorescin thiocarbamoyl-labeled casein + H2O
?
show the reaction diagram
-
-
-
-
?
fodrin + H2O
?
show the reaction diagram
-
-
-
-
?
human epithelial growth factor receptor 2 + H2O
75000 Da fragment + 42000 Da fragment
show the reaction diagram
-
overexpression of calpain1 or activation of endogenous calpain during adhesion or trastuzumab treatment of trastuzumab-sensitive cells induces cleavage of cytoplasmic domains of human epithelial growth factor receptor 2/phospho-human epithelial growth factor receptor 2 protein
-
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?
I-kappaBalpha polymer + H2O
?
show the reaction diagram
-
-
-
-
?
insulin-like growth factor binding protein-2 + H2O
?
show the reaction diagram
-
the primary cleavage site in insulin-like growth factor binding protein-2 is localized to the non-conserved central linker regions
-
-
?
insulin-like growth factor binding protein-3 + H2O
?
show the reaction diagram
-
the primary cleavage site in insulin-like growth factor binding protein-3 is localized to the non-conserved central linker regions. In vitro binding of mu-calpain to insulin-like growth factor binding protein-3 is a Ca2+-dependent reaction with a rapid on/off rate
-
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?
integrin + H2O
?
show the reaction diagram
-
-
-
-
?
integrin beta3 + H2O
?
show the reaction diagram
-
-
-
-
?
K-(5(6)-carboxyfluorescein)-EVYGMMK(4-(4-dimethylaminophenylazo)benzoyl)-OH + H2O
K-(5(6)-carboxyfluorescein)-EVY + GMMK(4-(4-dimethylaminophenylazo)benzoyl)-OH
show the reaction diagram
-
-
-
-
?
L-plastin + H2O
?
show the reaction diagram
-
L-plastin interaction with integrin is regulated through cleavage of beta-integrin by micro-calpain
-
-
?
MAP2 + H2O
?
show the reaction diagram
-
-
-
-
?
microtubule-associated protein 2
?
show the reaction diagram
-
-
-
-
?
microtubule-associated protein 2 + H2O
?
show the reaction diagram
-
calpain translates high-frequency Ca2+ transients into decomposition of its sensitive substrate microtubule-associated protein 2
-
-
?
N-acetyl-LLY-7-amido-4-fluoromethylcoumarin + H2O
N-acetyl-LLY + 7-amino-4-fluoromethylcoumarin
show the reaction diagram
N-benzyloxycarbonyl-L-Leu-L-Arg-4-methoxy-2-naphthylamide + H2O
N-benzyloxycarbonyl-L-Leu-L-Arg + 4-methoxy-2-naphthylamine
show the reaction diagram
-
-
-
-
?
N-benzyloxycarbonyl-L-Leu-L-Arg-7-amido-4-methylcoumarin + H2O
N-benzyloxycarbonyl-L-Leu-L-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
N-benzyloxycarbonyl-L-Leu-L-Arg-7-amido-4-trifluoromethylcoumarin + H2O
N-benzyloxycarbonyl-L-Leu-L-Arg + 7-amino-4-trifluoromethylcoumarin
show the reaction diagram
-
-
-
-
?
N-succinyl-LLVY-7-amido-4-methylcoumarin + H2O
N-succinyl-LLVY + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
neuronal calcium sensor-1 + H2O
?
show the reaction diagram
-
mu-calpain cleavage of neuronal calcium sensor-1 occurs within an N-terminal pseudoEF-hand domain (at Lys36), which is unable to bind Ca2+
-
-
?
neuronal nitric oxide synthase + H2O
?
show the reaction diagram
-
the mechanism of neuronal nitric oxide synthase activation is promoted by a calpain-mediated limited proteolysis through conversion of native 160 kDa nNOS into a fully active 130 kDa
-
-
?
p12 subunit of human DNA polymerase delta + H2O
?
show the reaction diagram
-
the proteolysis of p12 by mu-calpain may be through a DNA polymerase delta4/PCNA complex. The p12/DNA polymerase delta is a target as a nuclear substrate of mu-calpain in calcium-triggered apoptosis
-
-
?
plasma membrane Ca2+-ATPase isoform 1 + H2O
?
show the reaction diagram
-
readily and completely degraded by m-calpain
-
-
?
plasma membrane Ca2+-ATPase isoform 2 + H2O
?
show the reaction diagram
-
slow hydrolysis only to large fragments
-
-
?
plasma membrane Ca2+-ATPase isoform 4 + H2O
?
show the reaction diagram
-
slow hydrolysis only to large fragments
-
-
?
podoplanin + H2O
?
show the reaction diagram
-
podoplanin stability is post-translationally regulated by calpain-1
-
-
?
pro-interleukin-33 + H2O
interleukin-33 + ?
show the reaction diagram
-
-
-
-
?
Rad21 + H2O
?
show the reaction diagram
-
calpain-1 cleaves Rad21 at Leu192
-
-
?
recombinant procaspase-3 + H2O
?
show the reaction diagram
recombinant procaspase-9 + H2O
?
show the reaction diagram
spectrin + H2O
?
show the reaction diagram
-
-
-
-
?
striatal-enriched protein tyrosine phosphatase + H2O
?
show the reaction diagram
-
calpain-cleavage of striatal-enriched protein tyrosine phosphatase 61 is NMDAR-dependent, Cdk5 enhances calpain-mediated cleavage of striatal-enriched protein tyrosine phosphatase 61, calpain cleaves recombinant striatal-enriched protein tyrosine phosphatase 46 in a dose-dependent manner
-
-
?
succinyl-bovine serum albumin + H2O
?
show the reaction diagram
-
-
-
-
?
succinyl-casein + H2O
?
show the reaction diagram
-
-
-
-
?
succinyl-insulin B + H2O
?
show the reaction diagram
-
-
-
-
?
succinyl-L-Leu-L-Leu-L-Val-7-amido-4-methylcoumarin + H2O
succinyl-L-Leu-L-Leu-L-Val + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
succinyl-L-Leu-L-Leu-L-Val-L-Tyr-7-amido-4-methylcoumarin + H2O
succinyl-L-Leu-L-Leu-L-Val-L-Tyr + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
succinyl-L-Leu-L-Met-7-amido-4-methylcoumarin + H2O
succinyl-L-Leu-L-Met + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
succinyl-L-Leu-L-Tyr-4-methoxy-2-naphthylamide + H2O
succinyl-L-Leu-L-Tyr + 4-methoxy-2-naphthylamine
show the reaction diagram
-
-
-
-
?
succinyl-L-Leu-L-Tyr-7-amido-4-methylcoumarin + H2O
succinyl-L-Leu-L-Tyr + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
succinyl-Leu-Tyr-4-methylcoumaryl-7-amide + H2O
?
show the reaction diagram
-
-
-
-
?
succinyl-LLVY-7-amido-4-methylcoumarin + H2O
succinyl-LLVY + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
succinyl-protamine + H2O
?
show the reaction diagram
-
-
-
-
?
talin + H2O
?
show the reaction diagram
-
-
-
-
?
tau protein + H2O
?
show the reaction diagram
-
-
-
-
?
tert-butyloxycarbonyl-L-Leu-L-Met-7-amido-4-chloromethylcoumarin + H2O
tert-butyloxycarbonyl-L-Leu-L-Met + 7-amino-4-chloromethylcoumarin
show the reaction diagram
-
-
-
-
?
tert-butyloxycarbonyl-L-Leu-L-Met-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-L-Leu-L-Met + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
tert-butyloxycarbonyl-L-leucyl-L-methionine-7-amido-4-chloromethylcoumarin + H2O
tert-butyloxycarbonyl-L-leucyl-L-methionine + 7-amino-4-chloromethylcoumarin
show the reaction diagram
-
-
-
-
?
tert-butyloxycarbonyl-L-Val-L-Leu-L-Lys-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-L-Val-L-Leu-L-Lys + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
tert-butyloxycarbonyl-Leu-Met-7-amido-4-chloromethylcoumarin + H2O
tert-butyloxycarbonyl-Leu-Met + 7-amino-4-chloromethylcoumarin
show the reaction diagram
-
-
-
-
?
titin + H2O
?
show the reaction diagram
-
-
-
-
?
troponin complex + H2O
?
show the reaction diagram
-
-
-
-
?
vimentin + H2O
?
show the reaction diagram
-
-
-
-
?
[2-Abz]-Ser-Thr-Phe-Ala-Gln-Pro-[3-nitrotyrosine]-NH2 + H2O
[2-Abz]-Ser-Thr-Phe + Ala-Gln-Pro-[3-nitrotyrosine]-NH2
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
alpha-actinin + H2O
?
show the reaction diagram
-
-
-
-
?
alphaII-spectrin + H2O
?
show the reaction diagram
-
Fanconi anemia proteins play an important role in maintaining the stability of alphaII-spectrin in the cell by regulating its cleavage by mu-calpain
-
-
?
apoptosis-inducing factor + H2O
?
show the reaction diagram
-
although calpain I cleaves recombinant apoptosis-inducing factor in a cell free system, in intact cells under conditions where endogenous calpain is activated by either N-methyl-D-aspartate or N-methyl-N'-nitro-N-nitrosoguanidine administration, apoptosis-inducing factor is not cleaved
-
-
?
caspase-7 + H2O
?
show the reaction diagram
-
recombinant caspase-7 is directly cleaved and activated by calpain-1 within the large subunit of caspase-7 to produce the large subunit p18 and p17
-
-
?
desmin + H2O
?
show the reaction diagram
-
-
-
-
?
filamin A + H2O
?
show the reaction diagram
-
-
-
-
?
fodrin + H2O
?
show the reaction diagram
-
-
-
-
?
I-kappaBalpha polymer + H2O
?
show the reaction diagram
-
-
-
-
?
integrin + H2O
?
show the reaction diagram
-
-
-
-
?
MAP2 + H2O
?
show the reaction diagram
-
-
-
-
?
microtubule-associated protein 2 + H2O
?
show the reaction diagram
-
calpain translates high-frequency Ca2+ transients into decomposition of its sensitive substrate microtubule-associated protein 2
-
-
?
neuronal nitric oxide synthase + H2O
?
show the reaction diagram
-
the mechanism of neuronal nitric oxide synthase activation is promoted by a calpain-mediated limited proteolysis through conversion of native 160 kDa nNOS into a fully active 130 kDa
-
-
?
p12 subunit of human DNA polymerase delta + H2O
?
show the reaction diagram
-
the proteolysis of p12 by mu-calpain may be through a DNA polymerase delta4/PCNA complex. The p12/DNA polymerase delta is a target as a nuclear substrate of mu-calpain in calcium-triggered apoptosis
-
-
?
Rad21 + H2O
?
show the reaction diagram
-
calpain-1 cleaves Rad21 at Leu192
-
-
?
recombinant procaspase-3 + H2O
?
show the reaction diagram
-
calpain is a potential regulator of caspases and calpain promotes apoptosis-like events during platelet activation
-
-
?
recombinant procaspase-9 + H2O
?
show the reaction diagram
-
calpain is a potential regulator of caspases and calpain promotes apoptosis-like events during platelet activation
-
-
?
spectrin + H2O
?
show the reaction diagram
-
-
-
-
?
striatal-enriched protein tyrosine phosphatase + H2O
?
show the reaction diagram
-
calpain-cleavage of striatal-enriched protein tyrosine phosphatase 61 is NMDAR-dependent, Cdk5 enhances calpain-mediated cleavage of striatal-enriched protein tyrosine phosphatase 61, calpain cleaves recombinant striatal-enriched protein tyrosine phosphatase 46 in a dose-dependent manner
-
-
?
talin + H2O
?
show the reaction diagram
-
-
-
-
?
tau protein + H2O
?
show the reaction diagram
-
-
-
-
?
titin + H2O
?
show the reaction diagram
-
-
-
-
?
troponin complex + H2O
?
show the reaction diagram
-
-
-
-
?
vimentin + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mn2+
-
synergistic acivation in combination with Ca2+
Sr2+
-
synergistic acivation in combination with Ca2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(-)-epicatechin 5-gallate
-
-
(2S)-2-[[(4-fluorophenyl)sulfonyl]amino]-N-[(3S)-2-hydroxytetrahydrofuran-3-yl]-3-methylbutanamide
-
-
(2S,5S)-5-benzyl-6-hydroxy-2-(2-methylpropyl)morpholin-3-one
-
SNJ-1757
(3S)-2-hydroxytetrahydrofuran-3-yl N-[(10H-phenothiazin-2-yloxy)acetyl]-L-threonyl-L-leucinate
-
-
(3S)-2-hydroxytetrahydrofuran-3-yl N-[(2S)-2-[[(10H-phenothiazin-2-yloxy)acetyl]amino]butanoyl]-L-leucinate
-
-
(3S)-3-[[N-(10H-phenothiazin-2-ylcarbonyl)-L-norvalyl]amino]tetrahydrofuran-2-yl acetate
-
BN-82270
(4S)-3-[(4-methylphenyl)sulfonyl]-N-(1-oxo-3-phenylpropan-2-yl)-1,3-thiazolidine-4-carboxamide
-
-
(7S,10S,13S,26S)-13,26-dibenzyl-7-methyl-10-(propan-2-yl)-5,7,8,10,11,13,14,25,26,28-decahydrotetrabenzo[k,m,t,v][1,4,7,10,15,18]hexaazacyclotetracosine-6,9,12,15,24,27-hexone
-
-
1-(2-chloro-4-hydroxyphenyl)-4-oxo-7-(pyridin-4-yl)-1,4-dihydroquinoline-3-carboxamide
-
-
1-[(4-methylphenyl)sulfonyl]-N-(1-oxo-3-phenylpropan-2-yl)-D-prolinamide
-
-
2-methyl-N-[(2S)-1-oxo-3-phenylpropan-2-yl]-7,8-dihydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazine-3-carboxamide 1,1-dioxide
-
-
3,4-dichlorophenyl (2-[(3-([(2-ethyl-1,1-dioxido-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazin-3-yl)carbonyl]amino)-2-oxo-4-phenylbutanoyl)amino]ethyl)amidosulfite
-
IC50: 56 nM
3,4-dichlorophenyl (3-[(3-([(2-ethyl-1,1-dioxido-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazin-3-yl)carbonyl]amino)-2-oxo-4-phenylbutanoyl)amino]propyl)amidosulfite
-
IC50: 56 nM
3-([4-[2-(methoxymethoxy)phenyl]-4-oxobutanoyl]amino)-2-oxo-4-phenylbutanamide
-
reversible inhibitor
3-([N-[(benzyloxy)carbonyl]-L-leucyl]amino)-2-oxo-4-phenylbutanoic acid
-
reversible inhibitor
3-acetyl-2-[(2,4-dichlorophenyl)amino]-8-(trifluoromethyl)quinolin-4(1H)-one
-
-
3-acetyl-2-[(3-fluorophenyl)amino]-8-phenylquinolin-4(1H)-one
-
-
3-acetyl-2-[(4-chlorophenyl)amino]-5,8-difluoroquinolin-4(1H)-one
-
-
3-acetyl-2-[(4-tert-butylphenyl)amino]-5,8-difluoroquinolin-4(1H)-one
-
-
3-acetyl-2-[(4-tert-butylphenyl)amino]-8-chloro-6-nitroquinolin-4(1H)-one
-
-
3-acetyl-2-[[3,5-bis(trifluoromethyl)phenyl]amino]-5,8-difluoroquinolin-4(1H)-one
-
-
3-acetyl-5,8-dibromo-2-[(4-bromophenyl)amino]quinolin-4(1H)-one
-
-
3-acetyl-5,8-dichloro-2-[(2,4-dichlorophenyl)amino]quinolin-4(1H)-one
-
-
3-acetyl-6,8-difluoro-2-[(2,4,5-trifluorophenyl)amino]quinolin-4(1H)-one
-
-
3-acetyl-6-chloro-2-[(2,4-dichlorophenyl)amino]-8-nitroquinolin-4(1H)-one
-
-
3-acetyl-6-chloro-2-[(2-chloro-4-methylphenyl)amino]-8-nitroquinolin-4(1H)-one
-
-
3-acetyl-6-chloro-8-(trifluoromethyl)-2-[[4-(trifluoromethyl)phenyl]amino]quinolin-4(1H)-one
-
-
3-acetyl-7,8-dichloro-2-[[3-(trifluoromethyl)phenyl]amino]quinolin-4(1H)-one
-
-
3-acetyl-8-bromo-5-chloro-2-[(4-chlorophenyl)amino]quinolin-4(1H)-one
-
-
3-acetyl-8-chloro-2-[(2,4-dibromophenyl)amino]-5-methylquinolin-4(1H)-one
-
-
3-acetyl-8-chloro-2-[(2-fluoro-5-methylphenyl)amino]-5-(trifluoromethyl)quinolin-4(1H)-one
-
-
3-acetyl-8-chloro-2-[(3-methylphenyl)amino]-5-nitroquinolin-4(1H)-one
-
-
3-acetyl-8-chloro-2-[(4-chloro-2-fluorophenyl)amino]-5-methylquinolin-4(1H)-one
-
-
3-acetyl-8-chloro-2-[(4-chlorophenyl)amino]-6-nitroquinolin-4(1H)-one
-
-
3-acetyl-8-chloro-5-fluoro-2-(phenylamino)quinolin-4(1H)-one
-
-
3-acetyl-8-chloro-5-methyl-2-[(2,3,4-trifluorophenyl)amino]quinolin-4(1H)-one
-
-
3-acetyl-8-chloro-5-methyl-2-[(2,4,5-trifluorophenyl)amino]quinolin-4(1H)-one
-
-
4-(4-bromophenyl)-3-([N-[5-(1,2-dithiolan-3-yl)pentanoyl]-L-leucyl]amino)-2-oxobutanoic acid
-
reversible inhibitor
4-fluorophenyl (2-[(3-([(2-ethyl-1,1-dioxido-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazin-3-yl)carbonyl]amino)-2-oxo-4-phenylbutanoyl)amino]ethyl)amidosulfite
-
IC50: 29 nM
4-fluorophenyl (3-[(3-([(2-ethyl-1,1-dioxido-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazin-3-yl)carbonyl]amino)-2-oxo-4-phenylbutanoyl)amino]propyl)amidosulfite
-
IC50: 50 nM
4-nitrophenyl (2-[(3-([(2-ethyl-1,1-dioxido-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazin-3-yl)carbonyl]amino)-2-oxo-4-phenylbutanoyl)amino]ethyl)amidosulfite
-
IC50: 47 nM
4-nitrophenyl (3-[(3-([(2-ethyl-1,1-dioxido-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazin-3-yl)carbonyl]amino)-2-oxo-4-phenylbutanoyl)amino]propyl)amidosulfite
-
IC50: 50 nM
4-[([(2Z)-2-[(3S)-3-(1-methylpropyl)-1-oxo-2,3-dihydroisoquinolin-4(1H)-ylidene]acetyl]oxy)methyl]benzyl (2Z)-[(3R)-3-(1-methylpropyl)-1-oxo-2,3-dihydroisoquinolin-4(1H)-ylidene]ethanoate
-
-
5-azanylidyne-N-[[(2S,3S)-3-(ethoxycarbonyl)oxiran-2-yl]carbonyl]-L-norvalyl-L-arginyl-L-tryptophanamide
-
irreversible inhibitor
5-formyl-N-[(2S)-3-methyl-1-[[(2S)-4-methyl-1-oxopentan-2-yl]amino]-1-oxobutan-2-yl]-1H-pyrrole-2-carboxamide
-
CAT0059
5-formyl-N-[(2S)-3-methyl-1-[[(2S)-4-methyl-1-oxopentan-2-yl]amino]-1-oxobutan-2-yl]furan-2-carboxamide
-
-
5-formyl-N-[(2S)-3-methyl-1-[[(2S)-4-methyl-1-oxopentan-2-yl]amino]-1-oxobutan-2-yl]thiophene-2-carboxamide
-
-
A23187
-
-
acetyl-DPMSSTYIEE-betaAla-GKREVTIPPKYRELLA-NH2
-
-
acetyl-DPMSSTYIEELGK-NH2
-
-
acetyl-DPMSSTYIEELGKREVT-betaAla-PPKYRELLA-NH2
-
-
acetyl-DPMSSTYIEELGKREVTIPPKYR-NH2
-
-
acetyl-DPMSSTYIEELGKREVTIPPKYREL-NH2
-
-
acetyl-DPMSSTYIEELGKREVTIPPKYRELLA-NH2
-
CP1B peptide
acetyl-Leu-Leu-Nle-CHO
-
-
acetyl-REVTIPPKYRELLA-NH2
-
-
acetyl-RRMKWKKDPMSSTYIEELGKREVTIPPKYRELLA-NH2
-
-
acetyl-RYKPPITVERKGLEEIYTSS-NH2
-
-
acetyl-SSTTYIEELGKREVTIPPKYR-NH2
-
-
acetyl-SSTYIEELGK-NH-(CH2O)2-CH2C(O)-TIPPKYR-NH2
-
-
acetyl-SSTYIEELGKREVTIPPK-NH2
-
-
acetyl-SSTYIEELGKREVTIPPKYR-NH2
-
-
acetyl-SSTYIEELGKREVTIPPKYRELLA-NH2
-
-
acetyl-TYIEELGKREVTIPPKYR-NH2
-
-
acetyl-TYIEELGKREVTIPPKYRELLA-NH2
-
-
AK-275
-
reversible inhibitor
-
AK-295
-
reversible inhibitor
AK-295-D1
-
reversible inhibitor
-
AK-295-D2
-
reversible inhibitor
-
ALLM
-
reversible inhibitor
benzyl [(6S,9S,12S)-6-formyl-9-(2-methylpropyl)-8,11-dioxo-2-oxa-7,10-diazabicyclo[12.2.2]octadeca-1(16),14,17-trien-12-yl]carbamate
-
-
benzyl [(7S,10S,13S)-7-formyl-10-(2-methylpropyl)-9,12-dioxo-2-oxa-8,11-diazabicyclo[13.2.2]nonadeca-1(17),15,18-trien-13-yl]carbamate
-
CAT811
benzyl [(8S,11S,14S)-8-formyl-11-(2-methylpropyl)-10,13-dioxo-2-oxa-9,12-diazabicyclo[14.2.2]icosa-1(18),16,19-trien-14-yl]carbamate
-
-
butyl (2Z)-[(3S)-3-(butan-2-yl)-1-oxo-2,3-dihydroisoquinolin-4(1H)-ylidene]ethanoate
-
-
calpain inhibitor 1
-
synthetic calpain inhibitor
calpain inhibitor III
-
-
calpain inhibitor-1
-
-
calpastatin
-
calpastatin peptides
-
-
-
Calpeptin
CP1B peptide
-
a 20-mer peptide truncated from region B of calpastatin inhibitory domain 1, 1000fold more selective for mu-calpain than cathepsin L
-
cystatin
-
engineered cystatins. Recombinant hybrids of human stefin B with KS2 and DELTAL110 deletion mutants of chicken cystatin-KD2 hybrids. Substitution of the N-terminal contact region of stefin B by ther corresponding KD2 sequence results in a calpain inhibitor with a Ki-value of 188 nM. Deletion of L110 improves inhibition 4 to 8fold. All engineered cystatins are temporary inhibitors
-
dimethyl (2S,2'S)-2,2'-[biphenyl-2,2'-diylbis(carbonylimino)]bis(3-phenylpropanoate)
-
-
E-64
-
irreversible inhibitor
E-64c
-
irreversible inhibitor
E-64d
-
irreversible inhibitor
E64d
-
-
EDTA
-
0.25 mM, complete
EGTA
-
-
Ep-460
-
irreversible inhibitor
ethyl 3-([N-[(benzyloxy)carbonyl]-L-leucyl]amino)-2-oxo-4-phenylbutanoate
-
reversible inhibitor
ethyl 4-(4-bromophenyl)-3-([N-[5-(1,2-dithiolan-3-yl)pentanoyl]-L-leucyl]amino)-2-oxobutanoate
-
reversible inhibitor
heat shock protein 90
-
incubation of calpain-1 at a molar ratio of 1:1 with heat shock protein 90, at increasing Ca2+ concentrations, results in a significant decrease of calpain proteolytic activity at [Ca2+] up to 0.04 mM. At higher Ca2+ concentrations, the inhibiting effect of heat shock protein 90 is no more detectable
-
iodoacetic acid
-
0.25 mM, complete
ionomycin
-
-
leupeptin
MDL-28170
MDL-28710
-
complete inhibition at 100 nM
MDL28170
methyl (2-[(3-([(2-ethyl-1,1-dioxido-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazin-3-yl)carbonyl]amino)-2-oxo-4-phenylbutanoyl)amino]ethyl)amidosulfite
-
IC50: 89 nM
methyl (3S)-4-cyclohexyl-3-([(2-ethyl-1,1-dioxido-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazin-3-yl)carbonyl]amino)-2-oxobutanoate
-
IC50: 1000 nM
methyl (S,S,Z)-(3-sec-butyl-1-oxo-2,3-dihydro-1H-isoquinolin-4-ylidene)acetate
-
strong inhibitor
methyl N-[[2'-([(2S)-1-[(2'-aminobiphenyl-2-yl)amino]-1-oxo-3-phenylpropan-2-yl]carbamoyl)biphenyl-2-yl]carbonyl]-L-phenylalanyl-L-valinate
-
-
N'-((1S,2R)-1-benzyl-3-[(3,5-dimethoxybenzyl)amino]-2-hydroxypropyl)-N,N-dipropylbenzene-1,3-dicarboxamide
-
IC50: 20 nM
N-((1S)-1-benzyl-2,3-dioxo-3-[(2-phenylethyl)amino]propyl)-2-ethyl-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazine-3-carboxamide 1,1-dioxide
-
IC50: 63 nM
N-((1S)-1-benzyl-3-[(1-methylethyl)amino]-2,3-dioxopropyl)-2-ethyl-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazine-3-carboxamide 1,1-dioxide
-
IC50: 205 nM
N-((1S)-1-benzyl-3-[(2-methoxyethyl)amino]-2,3-dioxopropyl)-2-ethyl-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazine-3-carboxamide 1,1-dioxide
-
IC50: 200 nM
N-((1S)-1-benzyl-3-[(cyclopropylmethyl)amino]-2,3-dioxopropyl)-2-ethyl-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazine-3-carboxamide 1,1-dioxide
-
IC50: 286 nM
N-((1S)-1-[(butylamino)(oxo)acetyl]-3-methylbutyl)-2-ethyl-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazine-3-carboxamide 1,1-dioxide
-
-
N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-1-(1-benzothiophen-2-ylcarbonyl)piperidine-4-carboxamide
-
reversible inhibitor
N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-2-[(E)-2-[4-[(diethylamino)methyl]phenyl]ethenyl]benzamide
-
reversible inhibitor
N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-3-methyl-4-oxo-1,4-dihydroquinoline-2-carboxamide
-
reversible inhibitor
N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-3-methyl-4-oxo-4H-chromene-2-carboxamide
-
reversible inhibitor
N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-4-methyl-6-methylidene-1,6-dihydropyridine-3-carboxamide
-
reversible inhibitor
N-acetyl-Leu-Leu-Norleu-al
-
-
N-[(1S)-1-benzyl-2,3-dioxo-3-(pentylamino)propyl]-2-ethyl-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazine-3-carboxamide 1,1-dioxide
-
IC50: 150 nM
N-[(1S)-1-benzyl-2,3-dioxo-3-(prop-2-en-1-ylamino)propyl]-2-ethyl-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazine-3-carboxamide 1,1-dioxide
-
IC50: 200 nM
N-[(1S)-1-benzyl-3-(benzylamino)-2,3-dioxopropyl]-2-ethyl-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazine-3-carboxamide 1,1-dioxide
-
IC50: 81 nM
N-[(1S)-1-benzyl-3-(butylamino)-2,3-dioxopropyl]-2-ethyl-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazine-3-carboxamide 1,1-dioxide
-
-
N-[(1S)-1-benzyl-3-(ethylamino)-2,3-dioxopropyl]-2-ethyl-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazine-3-carboxamide 1,1-dioxide
-
IC50: 340 nM
N-[(2S)-1-oxo-3-phenylpropan-2-yl]-7,8-dihydro-2H-[1,4]dioxino[2,3-g][1,2,4]benzothiadiazine-3-carboxamide 1,1-dioxide
-
-
N-[(2S)-1-[[(3S)-2-hydroxytetrahydrofuran-3-yl]amino]-1-oxopentan-2-yl]-10H-phenothiazine-2-carboxamide
-
BN-82204
N-[(2S)-3,4-dioxo-1-phenyl-4-([3-[(phenylsulfonyl)amino]propyl]amino)butan-2-yl]-2-ethyl-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazine-3-carboxamide 1,1-dioxide
-
reversible inhibitor
N-[(2S)-4-(2-benzylhydrazinyl)-3,4-dioxo-1-phenylbutan-2-yl]-N2-[(benzyloxy)carbonyl]-L-leucinamide
-
reversible inhibitor
N-[(2S)-4-(butylamino)-3,4-dioxo-1-phenylbutan-2-yl]-2-ethyl-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazine-3-carboxamide 1,1-dioxide
-
reversible inhibitor
N-[(benzyloxy)carbonyl]-L-leucyl-N-[(2S)-4-fluoro-1-(4-hydroxyphenyl)-3-oxobutan-2-yl]-L-leucinamide
-
irreversible inhibitor
N-[1-(4-bromophenyl)-4-(ethylamino)-3,4-dioxobutan-2-yl]-N2-[5-(1,2-dithiolan-3-yl)pentanoyl]-L-leucinamide
-
reversible inhibitor
N-[[(2R,3R)-3-(ethoxycarbonyl)oxiran-2-yl]carbonyl]-L-histidyl-L-arginyl-L-tryptophanamide
-
irreversible inhibitor
N2-[(2S)-2-([[(2R,3R)-3-(ethoxycarbonyl)oxiran-2-yl]carbonyl]amino)pent-4-enoyl]-L-arginyl-L-tryptophanamide
-
irreversible inhibitor
N2-[(benzyloxy)carbonyl]-N-[4-(ethylamino)-3,4-dioxo-1-phenylbutan-2-yl]-L-leucinamide
-
reversible inhibitor
PCP1B peptide
-
-
-
PD-150606
-
-
PD-151746
-
-
PD150606
-
-
penetratin
-
-
penicillide
-
-
phenyl (2-[(3-([(1,1-dioxido-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazin-3-yl)carbonyl]amino)-2-oxo-4-phenylbutanoyl)amino]ethyl)amidosulfite
-
IC50: 76 nM
phenyl (2-[(3-([(2-ethyl-1,1-dioxido-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazin-3-yl)carbonyl]amino)-2-oxo-4-phenylbutanoyl)amino]ethyl)amidosulfite
-
IC50: 40 nM
phenyl (3-[(3-([(2-ethyl-1,1-dioxido-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazin-3-yl)carbonyl]amino)-2-oxo-4-phenylbutanoyl)amino]propyl)amidosulfite
-
IC50: 35 nM
SJA-6017
-
reversible inhibitor
SNJ-1715
-
reversible inhibitor
SNJ-1945
ZLLY-CH2F
-
irreversible inhibitor
additional information
-
FANCA and FANCG proteins bind directly to mu-calpain, this binding may lead to inhibition of mu-calpain activity in normal cells
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
-
required for maximal activity
Ca2+
-
required for activation of mu-calpain. Membrane-binding of mu-calpain is Ca2+-dependent. Membrane binding of mu-calpain is due to the exposed hydrophobic surface of the active site conformation and does not reduce the Ca2+ requirement for activation
NS5A protein
-
the nonstructural hepatitis C virus protein NS5Ais sufficient to activate a calpain 1
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.043
2-aminobenzoyl-EVYGMMY(3-NO2)-OH
-
pH and temperature not specified in the publication
0.00074
4,4-difluoro-5,7-dimethyl-4-bora-31,4a-diaza-s-indacene-3-propioyl-labeled casein
-
pH and temperature not specified in the publication
-
0.053
casein
-
pH and temperature not specified in the publication
0.0131
fluorescin thiocarbamoyl-labeled casein
-
pH and temperature not specified in the publication
-
0.00005
fodrin
-
pH and temperature not specified in the publication
-
0.0046
K-(5(6)-carboxyfluorescein)-EVYGMMK(4-(4-dimethylaminophenylazo)benzoyl)-OH
-
pH and temperature not specified in the publication
0.37
N-benzyloxycarbonyl-L-Leu-L-Arg-4-methoxy-2-naphthylamide
-
pH and temperature not specified in the publication
0.19
N-benzyloxycarbonyl-L-Leu-L-Arg-7-amido-4-methylcoumarin
-
pH and temperature not specified in the publication
0.46
N-benzyloxycarbonyl-L-Leu-L-Arg-7-amido-4-trifluoromethylcoumarin
-
pH and temperature not specified in the publication
0.002
succinyl-bovine serum albumin
-
pH and temperature not specified in the publication
-
0.0081
succinyl-casein
-
pH and temperature not specified in the publication
-
0.284
succinyl-insulin B
-
pH and temperature not specified in the publication
-
0.2
succinyl-L-Leu-L-Leu-L-Val-7-amido-4-methylcoumarin
-
pH and temperature not specified in the publication
0.2
succinyl-L-Leu-L-Leu-L-Val-L-Tyr-7-amido-4-methylcoumarin
-
pH and temperature not specified in the publication
1.2
succinyl-L-Leu-L-Met-7-amido-4-methylcoumarin
-
pH and temperature not specified in the publication
0.43
succinyl-L-Leu-L-Tyr-4-methoxy-2-naphthylamide
-
pH and temperature not specified in the publication
4.7
succinyl-L-Leu-L-Tyr-7-amido-4-methylcoumarin
-
pH and temperature not specified in the publication
0.063
succinyl-protamine
-
pH and temperature not specified in the publication
-
5.9
tert-butyloxycarbonyl-L-Val-L-Leu-L-Lys-7-amido-4-methylcoumarin
-
pH and temperature not specified in the publication
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.025
2-aminobenzoyl-EVYGMMY(3-NO2)-OH
-
pH and temperature not specified in the publication
0.11
K-(5(6)-carboxyfluorescein)-EVYGMMK(4-(4-dimethylaminophenylazo)benzoyl)-OH
-
pH and temperature not specified in the publication
0.52
N-benzyloxycarbonyl-L-Leu-L-Arg-4-methoxy-2-naphthylamide
-
pH and temperature not specified in the publication
0.02
N-benzyloxycarbonyl-L-Leu-L-Arg-7-amido-4-methylcoumarin
-
pH and temperature not specified in the publication
0.07
N-benzyloxycarbonyl-L-Leu-L-Arg-7-amido-4-trifluoromethylcoumarin
-
pH and temperature not specified in the publication
0.29
succinyl-L-Leu-L-Leu-L-Val-7-amido-4-methylcoumarin
-
pH and temperature not specified in the publication
0.029
succinyl-L-Leu-L-Leu-L-Val-L-Tyr-7-amido-4-methylcoumarin
-
pH and temperature not specified in the publication
0.062
succinyl-L-Leu-L-Met-7-amido-4-methylcoumarin
-
pH and temperature not specified in the publication
0.12
succinyl-L-Leu-L-Tyr-4-methoxy-2-naphthylamide
-
pH and temperature not specified in the publication
0.37
succinyl-L-Leu-L-Tyr-7-amido-4-methylcoumarin
-
pH and temperature not specified in the publication
0.49
tert-butyloxycarbonyl-L-Val-L-Leu-L-Lys-7-amido-4-methylcoumarin
-
pH and temperature not specified in the publication
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000081
1-[(4-methylphenyl)sulfonyl]-N-(1-oxo-3-phenylpropan-2-yl)-D-prolinamide
-
pH and temperature not specified in the publication
0.0000085
3-([N-[(benzyloxy)carbonyl]-L-leucyl]amino)-2-oxo-4-phenylbutanoic acid
-
pH and temperature not specified in the publication
0.00005
4-(4-bromophenyl)-3-([N-[5-(1,2-dithiolan-3-yl)pentanoyl]-L-leucyl]amino)-2-oxobutanoic acid
-
pH and temperature not specified in the publication
0.017
acetyl-DPMSSTYIEE-betaAla-GKREVTIPPKYRELLA-NH2
-
pH and temperature not specified in the publication
0.0069
acetyl-DPMSSTYIEELGK-NH2
-
pH 7.5, 12C
0.0024
acetyl-DPMSSTYIEELGKREVT-betaAla-PPKYRELLA-NH2
-
pH and temperature not specified in the publication
0.0000008
acetyl-DPMSSTYIEELGKREVTIPPKYR-NH2
-
pH 7.5, 12C
0.0000005
acetyl-DPMSSTYIEELGKREVTIPPKYREL-NH2
-
pH 7.5, 12C
0.0000002
acetyl-DPMSSTYIEELGKREVTIPPKYRELLA-NH2
-
pH and temperature not specified in the publication
0.035
acetyl-REVTIPPKYRELLA-NH2
-
pH 7.5, 12C
0.00000019
acetyl-RRMKWKKDPMSSTYIEELGKREVTIPPKYRELLA-NH2
-
pH and temperature not specified in the publication
0.726
acetyl-RYKPPITVERKGLEEIYTSS-NH2
-
pH 7.5, 12C
0.000026
acetyl-SSTTYIEELGKREVTIPPKYR-NH2
-
pH and temperature not specified in the publication
0.0117
acetyl-SSTYIEELGK-NH-(CH2O)2-CH2C(O)-TIPPKYR-NH2
-
pH 7.5, 12C
0.017
acetyl-SSTYIEELGKREVTIPPK-NH2
-
pH 7.5, 12C
0.000026
acetyl-SSTYIEELGKREVTIPPKYR-NH2
-
pH 7.5, 12C
0.0000006
acetyl-SSTYIEELGKREVTIPPKYRELLA-NH2
-
pH 7.5, 12C
0.000093
acetyl-TYIEELGKREVTIPPKYR-NH2
0.0000022
acetyl-TYIEELGKREVTIPPKYRELLA-NH2
-
pH 7.5, 12C
0.000026
CP1B peptide
-
pH and temperature not specified in the publication
-
0.0018
ethyl 3-([N-[(benzyloxy)carbonyl]-L-leucyl]amino)-2-oxo-4-phenylbutanoate
-
pH and temperature not specified in the publication
0.01
ethyl 4-(4-bromophenyl)-3-([N-[5-(1,2-dithiolan-3-yl)pentanoyl]-L-leucyl]amino)-2-oxobutanoate
-
IC50 above 0.01 mM, pH and temperature not specified in the publication
0.000009
N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-1-(1-benzothiophen-2-ylcarbonyl)piperidine-4-carboxamide
-
pH and temperature not specified in the publication
0.000027
N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-2-[(E)-2-[4-[(diethylamino)methyl]phenyl]ethenyl]benzamide
-
pH and temperature not specified in the publication
0.0000047
N-[(2S)-4-(2-benzylhydrazinyl)-3,4-dioxo-1-phenylbutan-2-yl]-N2-[(benzyloxy)carbonyl]-L-leucinamide
-
pH and temperature not specified in the publication
0.00002
N-[1-(4-bromophenyl)-4-(ethylamino)-3,4-dioxobutan-2-yl]-N2-[5-(1,2-dithiolan-3-yl)pentanoyl]-L-leucinamide
-
pH and temperature not specified in the publication
0.0002
N2-[(benzyloxy)carbonyl]-N-[4-(ethylamino)-3,4-dioxo-1-phenylbutan-2-yl]-L-leucinamide
-
pH and temperature not specified in the publication
0.0000005
PCP1B peptide
-
pH and temperature not specified in the publication
-
0.00000018
penetratin
-
pH and temperature not specified in the publication
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00088
(2S)-2-[[(4-fluorophenyl)sulfonyl]amino]-N-[(3S)-2-hydroxytetrahydrofuran-3-yl]-3-methylbutanamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0007
(2S,5S)-5-benzyl-6-hydroxy-2-(2-methylpropyl)morpholin-3-one
Homo sapiens
-
pH and temperature not specified in the publication
0.000038
(3S)-2-hydroxytetrahydrofuran-3-yl N-[(10H-phenothiazin-2-yloxy)acetyl]-L-threonyl-L-leucinate
Homo sapiens
-
pH and temperature not specified in the publication
0.000089
(3S)-2-hydroxytetrahydrofuran-3-yl N-[(2S)-2-[[(10H-phenothiazin-2-yloxy)acetyl]amino]butanoyl]-L-leucinate
Homo sapiens
-
pH and temperature not specified in the publication
0.001
(3S)-3-[[N-(10H-phenothiazin-2-ylcarbonyl)-L-norvalyl]amino]tetrahydrofuran-2-yl acetate
Homo sapiens
-
IC50 above 0.001 mM, pH and temperature not specified in the publication
0.029
(7S,10S,13S,26S)-13,26-dibenzyl-7-methyl-10-(propan-2-yl)-5,7,8,10,11,13,14,25,26,28-decahydrotetrabenzo[k,m,t,v][1,4,7,10,15,18]hexaazacyclotetracosine-6,9,12,15,24,27-hexone
Homo sapiens
-
pH and temperature not specified in the publication
0.0005
1-(2-chloro-4-hydroxyphenyl)-4-oxo-7-(pyridin-4-yl)-1,4-dihydroquinoline-3-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000006
2-methyl-N-[(2S)-1-oxo-3-phenylpropan-2-yl]-7,8-dihydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazine-3-carboxamide 1,1-dioxide
Homo sapiens
-
pH and temperature not specified in the publication
0.000056
3,4-dichlorophenyl (2-[(3-([(2-ethyl-1,1-dioxido-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazin-3-yl)carbonyl]amino)-2-oxo-4-phenylbutanoyl)amino]ethyl)amidosulfite
Homo sapiens
-
IC50: 56 nM
0.000056
3,4-dichlorophenyl (3-[(3-([(2-ethyl-1,1-dioxido-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazin-3-yl)carbonyl]amino)-2-oxo-4-phenylbutanoyl)amino]propyl)amidosulfite
Homo sapiens
-
IC50: 56 nM
0.00034
3-([4-[2-(methoxymethoxy)phenyl]-4-oxobutanoyl]amino)-2-oxo-4-phenylbutanamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0192
3-acetyl-2-[(2,4-dichlorophenyl)amino]-8-(trifluoromethyl)quinolin-4(1H)-one
Homo sapiens
-
using [2-Abz]-Ser-Thr-Phe-Ala-Gln-Pro-[3-nitrotyrosine]-NH2 as substrate, in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 5 mM beta-mercaptoethanol, pH 7.5, at 25C
0.03
3-acetyl-2-[(3-fluorophenyl)amino]-8-phenylquinolin-4(1H)-one
Homo sapiens
-
IC50 above 0.03 mM, using [2-Abz]-Ser-Thr-Phe-Ala-Gln-Pro-[3-nitrotyrosine]-NH2 as substrate, in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 5 mM beta-mercaptoethanol, pH 7.5, at 25C
0.03
3-acetyl-2-[(4-chlorophenyl)amino]-5,8-difluoroquinolin-4(1H)-one
Homo sapiens
-
IC50 above 0.03 mM, using [2-Abz]-Ser-Thr-Phe-Ala-Gln-Pro-[3-nitrotyrosine]-NH2 as substrate, in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 5 mM beta-mercaptoethanol, pH 7.5, at 25C
0.03
3-acetyl-2-[(4-tert-butylphenyl)amino]-5,8-difluoroquinolin-4(1H)-one
Homo sapiens
-
IC50 above 0.03 mM, using [2-Abz]-Ser-Thr-Phe-Ala-Gln-Pro-[3-nitrotyrosine]-NH2 as substrate, in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 5 mM beta-mercaptoethanol, pH 7.5, at 25C
0.00369 - 0.00743
3-acetyl-2-[(4-tert-butylphenyl)amino]-8-chloro-6-nitroquinolin-4(1H)-one
0.03
3-acetyl-2-[[3,5-bis(trifluoromethyl)phenyl]amino]-5,8-difluoroquinolin-4(1H)-one
Homo sapiens
-
IC50 above 0.03 mM, using [2-Abz]-Ser-Thr-Phe-Ala-Gln-Pro-[3-nitrotyrosine]-NH2 as substrate, in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 5 mM beta-mercaptoethanol, pH 7.5, at 25C
0.00169 - 0.00359
3-acetyl-5,8-dibromo-2-[(4-bromophenyl)amino]quinolin-4(1H)-one
0.00317 - 0.00399
3-acetyl-5,8-dichloro-2-[(2,4-dichlorophenyl)amino]quinolin-4(1H)-one
0.03
3-acetyl-6,8-difluoro-2-[(2,4,5-trifluorophenyl)amino]quinolin-4(1H)-one
Homo sapiens
-
IC50 above 0.03 mM, using [2-Abz]-Ser-Thr-Phe-Ala-Gln-Pro-[3-nitrotyrosine]-NH2 as substrate, in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 5 mM beta-mercaptoethanol, pH 7.5, at 25C
0.00316 - 0.00464
3-acetyl-6-chloro-2-[(2,4-dichlorophenyl)amino]-8-nitroquinolin-4(1H)-one
0.00239 - 0.00373
3-acetyl-6-chloro-2-[(2-chloro-4-methylphenyl)amino]-8-nitroquinolin-4(1H)-one
0.03
3-acetyl-6-chloro-8-(trifluoromethyl)-2-[[4-(trifluoromethyl)phenyl]amino]quinolin-4(1H)-one
Homo sapiens
-
IC50 above 0.03 mM, using [2-Abz]-Ser-Thr-Phe-Ala-Gln-Pro-[3-nitrotyrosine]-NH2 as substrate, in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 5 mM beta-mercaptoethanol, pH 7.5, at 25C
0.03
3-acetyl-7,8-dichloro-2-[[3-(trifluoromethyl)phenyl]amino]quinolin-4(1H)-one
Homo sapiens
-
IC50 above 0.03 mM, using [2-Abz]-Ser-Thr-Phe-Ala-Gln-Pro-[3-nitrotyrosine]-NH2 as substrate, in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 5 mM beta-mercaptoethanol, pH 7.5, at 25C
0.00353 - 0.00994
3-acetyl-8-bromo-5-chloro-2-[(4-chlorophenyl)amino]quinolin-4(1H)-one
0.000277 - 0.00306
3-acetyl-8-chloro-2-[(2,4-dibromophenyl)amino]-5-methylquinolin-4(1H)-one
0.03
3-acetyl-8-chloro-2-[(2-fluoro-5-methylphenyl)amino]-5-(trifluoromethyl)quinolin-4(1H)-one
Homo sapiens
-
IC50 above 0.03 mM, using [2-Abz]-Ser-Thr-Phe-Ala-Gln-Pro-[3-nitrotyrosine]-NH2 as substrate, in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 5 mM beta-mercaptoethanol, pH 7.5, at 25C
0.03
3-acetyl-8-chloro-2-[(3-methylphenyl)amino]-5-nitroquinolin-4(1H)-one
Homo sapiens
-
IC50 above 0.03 mM, using [2-Abz]-Ser-Thr-Phe-Ala-Gln-Pro-[3-nitrotyrosine]-NH2 as substrate, in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 5 mM beta-mercaptoethanol, pH 7.5, at 25C
0.03
3-acetyl-8-chloro-2-[(4-chloro-2-fluorophenyl)amino]-5-methylquinolin-4(1H)-one
Homo sapiens
-
IC50 above 0.03 mM, using [2-Abz]-Ser-Thr-Phe-Ala-Gln-Pro-[3-nitrotyrosine]-NH2 as substrate, in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 5 mM beta-mercaptoethanol, pH 7.5, at 25C
0.00456 - 0.00808
3-acetyl-8-chloro-2-[(4-chlorophenyl)amino]-6-nitroquinolin-4(1H)-one
0.03
3-acetyl-8-chloro-5-fluoro-2-(phenylamino)quinolin-4(1H)-one
Homo sapiens
-
IC50 above 0.03 mM, using [2-Abz]-Ser-Thr-Phe-Ala-Gln-Pro-[3-nitrotyrosine]-NH2 as substrate, in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 5 mM beta-mercaptoethanol, pH 7.5, at 25C
0.03
3-acetyl-8-chloro-5-methyl-2-[(2,3,4-trifluorophenyl)amino]quinolin-4(1H)-one
Homo sapiens
-
IC50 above 0.03 mM, using [2-Abz]-Ser-Thr-Phe-Ala-Gln-Pro-[3-nitrotyrosine]-NH2 as substrate, in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 5 mM beta-mercaptoethanol, pH 7.5, at 25C
0.03
3-acetyl-8-chloro-5-methyl-2-[(2,4,5-trifluorophenyl)amino]quinolin-4(1H)-one
Homo sapiens
-
IC50 above 0.03 mM, using [2-Abz]-Ser-Thr-Phe-Ala-Gln-Pro-[3-nitrotyrosine]-NH2 as substrate, in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 5 mM beta-mercaptoethanol, pH 7.5, at 25C
0.000029
4-fluorophenyl (2-[(3-([(2-ethyl-1,1-dioxido-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazin-3-yl)carbonyl]amino)-2-oxo-4-phenylbutanoyl)amino]ethyl)amidosulfite
Homo sapiens
-
IC50: 29 nM
0.00005
4-fluorophenyl (3-[(3-([(2-ethyl-1,1-dioxido-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazin-3-yl)carbonyl]amino)-2-oxo-4-phenylbutanoyl)amino]propyl)amidosulfite
Homo sapiens
-
IC50: 50 nM
0.000047
4-nitrophenyl (2-[(3-([(2-ethyl-1,1-dioxido-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazin-3-yl)carbonyl]amino)-2-oxo-4-phenylbutanoyl)amino]ethyl)amidosulfite
Homo sapiens
-
IC50: 47 nM
0.00005
4-nitrophenyl (3-[(3-([(2-ethyl-1,1-dioxido-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazin-3-yl)carbonyl]amino)-2-oxo-4-phenylbutanoyl)amino]propyl)amidosulfite
Homo sapiens
-
IC50: 50 nM
5
4-[([(2Z)-2-[(3S)-3-(1-methylpropyl)-1-oxo-2,3-dihydroisoquinolin-4(1H)-ylidene]acetyl]oxy)methyl]benzyl (2Z)-[(3R)-3-(1-methylpropyl)-1-oxo-2,3-dihydroisoquinolin-4(1H)-ylidene]ethanoate
Homo sapiens
-
-
0.00033
5-azanylidyne-N-[[(2S,3S)-3-(ethoxycarbonyl)oxiran-2-yl]carbonyl]-L-norvalyl-L-arginyl-L-tryptophanamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00029
5-formyl-N-[(2S)-3-methyl-1-[[(2S)-4-methyl-1-oxopentan-2-yl]amino]-1-oxobutan-2-yl]-1H-pyrrole-2-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00096
5-formyl-N-[(2S)-3-methyl-1-[[(2S)-4-methyl-1-oxopentan-2-yl]amino]-1-oxobutan-2-yl]furan-2-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00044
5-formyl-N-[(2S)-3-methyl-1-[[(2S)-4-methyl-1-oxopentan-2-yl]amino]-1-oxobutan-2-yl]thiophene-2-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0004
benzyl [(6S,9S,12S)-6-formyl-9-(2-methylpropyl)-8,11-dioxo-2-oxa-7,10-diazabicyclo[12.2.2]octadeca-1(16),14,17-trien-12-yl]carbamate
Homo sapiens
-
pH and temperature not specified in the publication
0.00022
benzyl [(7S,10S,13S)-7-formyl-10-(2-methylpropyl)-9,12-dioxo-2-oxa-8,11-diazabicyclo[13.2.2]nonadeca-1(17),15,18-trien-13-yl]carbamate
Homo sapiens
-
pH and temperature not specified in the publication
0.00017
benzyl [(8S,11S,14S)-8-formyl-11-(2-methylpropyl)-10,13-dioxo-2-oxa-9,12-diazabicyclo[14.2.2]icosa-1(18),16,19-trien-14-yl]carbamate
Homo sapiens
-
pH and temperature not specified in the publication
0.000064
dimethyl (2S,2'S)-2,2'-[biphenyl-2,2'-diylbis(carbonylimino)]bis(3-phenylpropanoate)
Homo sapiens
-
pH and temperature not specified in the publication
0.0015
E-64
Homo sapiens
-
-
0.000199 - 0.0002
MDL28170
0.000089
methyl (2-[(3-([(2-ethyl-1,1-dioxido-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazin-3-yl)carbonyl]amino)-2-oxo-4-phenylbutanoyl)amino]ethyl)amidosulfite
Homo sapiens
-
IC50: 89 nM
0.001
methyl (3S)-4-cyclohexyl-3-([(2-ethyl-1,1-dioxido-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazin-3-yl)carbonyl]amino)-2-oxobutanoate
Homo sapiens
-
IC50: 1000 nM
0.000025
methyl (S,S,Z)-(3-sec-butyl-1-oxo-2,3-dihydro-1H-isoquinolin-4-ylidene)acetate
Homo sapiens
-
pH and temperature not specified in the publication
0.000000087
methyl N-[[2'-([(2S)-1-[(2'-aminobiphenyl-2-yl)amino]-1-oxo-3-phenylpropan-2-yl]carbamoyl)biphenyl-2-yl]carbonyl]-L-phenylalanyl-L-valinate
Homo sapiens
-
pH and temperature not specified in the publication
0.00002
N'-((1S,2R)-1-benzyl-3-[(3,5-dimethoxybenzyl)amino]-2-hydroxypropyl)-N,N-dipropylbenzene-1,3-dicarboxamide
Homo sapiens
-
IC50: 20 nM
0.000063
N-((1S)-1-benzyl-2,3-dioxo-3-[(2-phenylethyl)amino]propyl)-2-ethyl-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazine-3-carboxamide 1,1-dioxide
Homo sapiens
-
IC50: 63 nM
0.000205
N-((1S)-1-benzyl-3-[(1-methylethyl)amino]-2,3-dioxopropyl)-2-ethyl-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazine-3-carboxamide 1,1-dioxide
Homo sapiens
-
IC50: 205 nM
0.0002
N-((1S)-1-benzyl-3-[(2-methoxyethyl)amino]-2,3-dioxopropyl)-2-ethyl-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazine-3-carboxamide 1,1-dioxide
Homo sapiens
-
IC50: 200 nM
0.000286
N-((1S)-1-benzyl-3-[(cyclopropylmethyl)amino]-2,3-dioxopropyl)-2-ethyl-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazine-3-carboxamide 1,1-dioxide
Homo sapiens
-
IC50: 286 nM
0.00071
N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-3-methyl-4-oxo-1,4-dihydroquinoline-2-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00004
N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-3-methyl-4-oxo-4H-chromene-2-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0028
N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-4-methyl-6-methylidene-1,6-dihydropyridine-3-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00015
N-[(1S)-1-benzyl-2,3-dioxo-3-(pentylamino)propyl]-2-ethyl-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazine-3-carboxamide 1,1-dioxide
Homo sapiens
-
IC50: 150 nM
0.0002
N-[(1S)-1-benzyl-2,3-dioxo-3-(prop-2-en-1-ylamino)propyl]-2-ethyl-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazine-3-carboxamide 1,1-dioxide
Homo sapiens
-
IC50: 200 nM
0.000081
N-[(1S)-1-benzyl-3-(benzylamino)-2,3-dioxopropyl]-2-ethyl-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazine-3-carboxamide 1,1-dioxide
Homo sapiens
-
IC50: 81 nM
0.00034
N-[(1S)-1-benzyl-3-(ethylamino)-2,3-dioxopropyl]-2-ethyl-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazine-3-carboxamide 1,1-dioxide
Homo sapiens
-
IC50: 340 nM
0.000028
N-[(2S)-1-oxo-3-phenylpropan-2-yl]-7,8-dihydro-2H-[1,4]dioxino[2,3-g][1,2,4]benzothiadiazine-3-carboxamide 1,1-dioxide
Homo sapiens
-
pH and temperature not specified in the publication
0.000023
N-[(2S)-1-[[(3S)-2-hydroxytetrahydrofuran-3-yl]amino]-1-oxopentan-2-yl]-10H-phenothiazine-2-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000035
N-[(2S)-3,4-dioxo-1-phenyl-4-([3-[(phenylsulfonyl)amino]propyl]amino)butan-2-yl]-2-ethyl-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazine-3-carboxamide 1,1-dioxide
Homo sapiens
-
pH and temperature not specified in the publication
0.00005
N-[(2S)-4-(butylamino)-3,4-dioxo-1-phenylbutan-2-yl]-2-ethyl-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazine-3-carboxamide 1,1-dioxide
Homo sapiens
-
pH and temperature not specified in the publication
0.00078
N2-[(2S)-2-([[(2R,3R)-3-(ethoxycarbonyl)oxiran-2-yl]carbonyl]amino)pent-4-enoyl]-L-arginyl-L-tryptophanamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000076
phenyl (2-[(3-([(1,1-dioxido-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazin-3-yl)carbonyl]amino)-2-oxo-4-phenylbutanoyl)amino]ethyl)amidosulfite
Homo sapiens
-
IC50: 76 nM
0.00004
phenyl (2-[(3-([(2-ethyl-1,1-dioxido-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazin-3-yl)carbonyl]amino)-2-oxo-4-phenylbutanoyl)amino]ethyl)amidosulfite
Homo sapiens
-
IC50: 40 nM
0.000035
phenyl (3-[(3-([(2-ethyl-1,1-dioxido-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazin-3-yl)carbonyl]amino)-2-oxo-4-phenylbutanoyl)amino]propyl)amidosulfite
Homo sapiens
-
IC50: 35 nM
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
activation of mu-calpain in platelets from patients with type 2 diabetes mellitus
Manually annotated by BRENDA team
-
from patients with recurrent miscarriage and healthy women with informed consent
Manually annotated by BRENDA team
-
rheumatic synovial cell line. mu-calpain, regulates MMP-3 release by rheumatic synovial cells, in addition to exerting its own degradative action on cartilage
Manually annotated by BRENDA team
-
NO-induced motility in osteoclasts requires regulated Ca2+ release, which activates mu-calpain. This occurs via the inositol (1,4,5)-trisphosphate receptor 1
Manually annotated by BRENDA team
-
elevated levels of calpain-1 in glaucomatous trabecular meshwork. However, calpain activity in glaucomatous trabecular meshwork is only about 50% of that in controls. Modification by iso-levuglandins renders calpain-1 inactive
Manually annotated by BRENDA team
-
neuroblastoma
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
-
calpain 1 is involved in the degradation of endothelial nitric oxide synthase and heat shock protein 90 and the phosphorylation of endothelial nitric oxide synthase
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
CAN1_HUMAN
714
0
81890
Swiss-Prot
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
28000
-
1 * 80000 + 1 * 28000, SDS-PAGE
32000
74000
80000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 80000, SDS-PAGE
dimer
heterodimer
-
1 * 80000 + 1 * 28000, SDS-PAGE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
proteolytic modification
-
autolysis of both mu-calpain and calpain-3 is tightly regulated by Ca2+ concentration in skeletal muscle across a range close to but evidently above that reached during normal activity
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C115A
-
non-autolysing active-site mutant
C115S
-
mutant without proteolytic activity of autolysis and caseinolysis
H272A
-
catalytically inactive
additional information
PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
affinity chromatography, calmodulin-like domain of the catalytic subunit expressed in E. coli
-
Ni2+-NTA-agarose column chromatography
-
purification of a 21000 Da calpain small subunit fragment
-
CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
complete amino acid sequence of the large subunit is deduced from its cDNA sequence
-
cloning of the 21000 Da small subunit and expression in Escherichia coli BL384
-
expressed in Escherichia coli BL21(DE3) cells
-
expression in Escherichia coli
-
expression of mutant enzyme C115S in insect cell using a baculovirus system
-
large catalytic subunit and two of its mutants are expressed in Escherichia coli using the baculovirus Sf9 system, the L-muCANPDELTA3 mutant lacks domain III, mutant L-muCANPDELTA4 lacks the calmodulin-like domain IV. In Sf9 cells co-expression of the inhibitor calpastatin is necessary to prevent autolysis of the L-muCANP subunit, whereas coexpression of the regulatory subunit enhances it. Only very low levels of mRNA of the truncated form L-muCANPDELTA4 are found in bacmid-transfectred Sf9 cells, and it proves impossible to isolate this mutant using the baculovirus expression system
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
after cisplatin treatment, calpain activation is an early event
-
although the levels of the calpain I isoform are higher in the soluble and insoluble fractions of tir- and wild type enteropathogenic Escherichia coli (E2348/69 O127:H6)-infected cells, their levels are not significantly different to the TTSS-negative control
-
calpain 1 activity is increased 2.5fold in FA-A, FA-D2, and FA-F cells as compared to normal cells and 3.5fold in FA-C and FA-G cells compared to normal cells
-
calpain-I is activated in human carotid plaques
-
cold storage (at 4C) induces a time dependent up-regulation of calpain 1, reflected by an increase in the autoproteolytic cleavage of calpain 1, which can be prevented by addition of EDTA or dopamine (0.025 mM) pretreatment
-
compared to control cybrids, Parkonsins disease cybrids reveal a significant increase in calpain activity
-
fatiguing jumping exercise does not change mRNA expression of calpain 1
-
mu-calpain is not activated immediately following sprint, endurance or eccentric exercise. mu-Calpain is not activated 24 h after a single bout of eccentric exercise
-
there are no significant differences on the expressions of calpain-1 at the levels of mRNA and protein in patients with and without stress urinary incontinence
-
there is no age-related change in calpain 1 protein expression in human female or male kidney samples. In the human kidney, there is no age-related change in calpain 1 mRNA expression
-
Wnt5A activates calpain-1, leading to the cleavage of filamin A
-
WNT5A knockdown decreases calpain 1 expression
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
presence of inhibitors during renaturation is necessary to prevent autolysis
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Shastri, R.; Anandaraj, M.P.J.S.
A low-calcium-requiring calcium-activated neutral proteinase from human placenta
Biochim. Biophys. Acta
873
260-266
1986
Homo sapiens
Manually annotated by BRENDA team
Aoki, K.; Imajoh, S.; Ohno, S.; Emori, Y.; Koike, M.; Kosaki, G.; Suzuki K.
Complete amino acid sequence of the large subunit of the low-Ca2+-requiring form of human Ca2+-activated neutral protease (muCANP) deduced from its cDNA sequence
FEBS Lett.
205
313-317
1986
Homo sapiens, Homo sapiens (P07384)
Manually annotated by BRENDA team
Michetti, M.; Salamino, F.; Minafra, R.; Melloni, E.; Pontremoli, S.
Calcium-binding properties of human erythrocyte calpain
Biochem. J.
325
721-726
1997
Homo sapiens
-
Manually annotated by BRENDA team
Vilei, E.M.; Calderara, S.; Anagli, J
Berardi, S.; Hitomi, K.; Maki, M: Carafoli, E.: Functional properties of recombinant calpain I and of mutants lacking domains III and IV of the catalytic subunits
J. Biol. Chem.
727
25802-25808
1997
Homo sapiens
-
Manually annotated by BRENDA team
Hitomi, K.; Uchiyama, Y.; Ohkubo, I.; Kunimatsu, M.; Sasaki, M.; Maki, M.
Purification and characterization of the active-site-mutated recombinant human mikro-calpain expressed in baculovirus-infected insect cells
Biochem. Biophys. Res. Commun.
246
681-685
1998
Homo sapiens
Manually annotated by BRENDA team
Shastri, R.; Jagadeesh, G.; Anandaraj, M.P.J.S.
Human placental calcium activated neutral proteinase: Separation and functional characterization of subunits
J. Biosci.
15
427-434
1990
Homo sapiens
-
Manually annotated by BRENDA team
Yoshimura, N.; Kikuchi, T.; Sasaki, T.; Kithara, A.; Hatanaka, M.; Murachi, T.
Two distinct Ca2+ proteases (calpain I and calpain II) purified concurrently by the same method from rat kidney
J. Biol. Chem.
258
8883-8889
1983
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Molinari, M.; maki, M.; Carafoli, E.
Purification of mu-calpain by a novel affinity chromatography approach. New insight into the mechanism of the interaction of the protease with targets
J. Biol. Chem.
270
14576-14581
1995
Homo sapiens
Manually annotated by BRENDA team
Diaz, B.G.; Gross, S.; Assfalg-Machleidt, I.; Pfeiler, D.; Gollmitzer, N.; Gabrijelcic-Geiger, D.; Stubbs, M.T.; Fritz, H.; Auerswald, E.A.; Machleidt, W.
Cystatins as calpain inhibitors: engineered chicken cystatin- and stefin B-kininogen domain 2 hybrids support a cystatin-like mode of interaction with the catalytic subunit of m-calpain
Biol. Chem.
382
97-107
2001
Homo sapiens
Manually annotated by BRENDA team
Shields, D.C.; Schaecher, K.E.; Saido, T.C.; Banik, N.L.
A putative mechanism of demyelination in multiple sclerosis by a proteolytic enzyme, calpain
Proc. Natl. Acad. Sci. USA
96
11486-11491
1999
Homo sapiens
Manually annotated by BRENDA team
Wolf, B.B.; Goldstein, J.C.; Stennicke, H.R.; Beere, H.; Amarante-Mendes, G.P.; Salvesen, G.S.; Green, D.R.
Calpain functions in a caspase-independent manner to promote apoptosis-like events during platelet activation
Blood
94
1683-1692
1999
Homo sapiens, Sus scrofa
Manually annotated by BRENDA team
Tompa, P.; Toth-Boconadi, R.; Friedrich, P.
Frequency decoding of fast calcium oscillations by calpain
Cell Calcium
29
161-170
2001
Homo sapiens
Manually annotated by BRENDA team
Rojas, F.J.; Brush, M.; Moretti-Rojas, I.
Calpain-calpastatin: a novel, complete calcium-dependent protease system in human spermatozoa
Mol. Hum. Reprod.
5
520-526
1999
Homo sapiens
Manually annotated by BRENDA team
Murphy, R.M.; Snow, R.J.; Lamb, G.D.
m-Calpain and calpain-3 are not autolyzed with exhaustive exercise in humans
Am. J. Physiol.
290
C116-C122
2006
Homo sapiens
Manually annotated by BRENDA team
Veerann, V.; Kaji, T.; Boland, B.; Odrljin, T.; Mohan, P.; Basavarajappa, B.S.; Peterhoff, C.; Cataldo, A.; Rudnicki, A.; Amin, N.; Li, B.S.; Pant, H.C.; Hungund, B.L.; Arancio, O.; Nixon, R.A.
Calpain mediates calcium-induced activation of the Erk1,2 MAPK pathway and cytoskeletal phosphorylation in neurons: Relevance to Alzheimers disease
Am. J. Pathol.
165
795-805
2004
Homo sapiens
Manually annotated by BRENDA team
Fernandez-Montalvan, A.; Assfalg-Machleidt, I.; Pfeiler, D.; Fritz, H.; Jochum, M.; Machleidt, W.
mu-Calpain binds to lipid bilayers via the exposed hydrophobic surface of its Ca2+-activated conformation
Biol. Chem.
387
617-627
2006
Homo sapiens
Manually annotated by BRENDA team
Bihovsky, R.; Tao, M.; Mallamo, J.P.; Wells, G.J.
1,2-Benzothiazine 1,1-dioxide alpha-ketoamide analogues as potent calpain I inhibitors
Bioorg. Med. Chem. Lett.
14
1035-1038
2004
Homo sapiens
Manually annotated by BRENDA team
Carragher, N.O.
Calpain inhibition: a therapeutic strategy targeting multiple disease states
Curr. Pharm. Des.
12
615-638
2006
Homo sapiens (P07384)
Manually annotated by BRENDA team
Guerini, D.; Pan, B.; Carafoli, E.
Expression, purification, and characterization of isoform 1 of the plasma membrane Ca2+ pump: focus on calpain sensitivity
J. Biol. Chem.
278
38141-38148
2003
Homo sapiens
Manually annotated by BRENDA team
Altznauer, F.; Conus, S.; Cavalli, A.; Folkers, G.; Simon, H.U.
Calpain-1 regulates Bax and subsequent Smac-dependent caspase-3 activation in neutrophil apoptosis
J. Biol. Chem.
279
5947-5957
2004
Homo sapiens
Manually annotated by BRENDA team
Kumagai, K.; Ozaki, Y.; Nakanishi, T.; Inomata, M.; Furuno, T.; Nakanishi, M.; Ogasawara, M.S.
Role of mu-calpain in human decidua for recurrent miscarriage
Am. J. Reprod. Immunol.
59
339-346
2008
Homo sapiens
Manually annotated by BRENDA team
Morita, M.; Banno, Y.; Dohjima, T.; Nozawa, S.; Fushimi, K.; Fan, D.G.; Ohno, T.; Miyazawa, K.; Liu, N.; Shimizu, K.
mu-Calpain is involved in the regulation of TNF-alpha-induced matrix metalloproteinase-3 release in a rheumatoid synovial cell line
Biochem. Biophys. Res. Commun.
343
937-942
2006
Homo sapiens
Manually annotated by BRENDA team
Govindarajan, B.; Laird, J.; Salomon, R.G.; Bhattacharya, S.K.
Isolevuglandin-modified proteins, including elevated levels of inactive calpain-1, accumulate in glaucomatous trabecular meshwork
Biochemistry
47
817-825
2008
Homo sapiens
Manually annotated by BRENDA team
Berg, U.; Bang, P.; Carlsson-Skwirut, C.
Calpain proteolysis of insulin-like growth factor binding protein (IGFBP) -2 and -3, but not of IGFBP-1
Biol. Chem.
388
859-863
2007
Homo sapiens
Manually annotated by BRENDA team
Pfizer, J.; Assfalg-Machleidt, I.; Machleidt, W.; Schaschke, N.
Inhibition of human mu-calpain by conformationally constrained calpastatin peptides
Biol. Chem.
389
83-90
2008
Homo sapiens
Manually annotated by BRENDA team
Chicharro, R.; Alonso, M.; Mazo, M.T.; Aran, V.J.; Herradon, B.
Derivatives of 3-sec-butyl-1-oxo-2,3-dihydroisoquinoline as inhibitors of micro mu-calpain
ChemMedChem
1
710-714
2006
Homo sapiens, Sus scrofa
Manually annotated by BRENDA team
Randriamboavonjy, V.; Pistrosch, F.; Boelck, B.; Schwinger, R.H.; Dixit, M.; Badenhoop, K.; Cohen, R.A.; Busse, R.; Fleming, I.
Platelet sarcoplasmic endoplasmic reticulum Ca2+-ATPase and mu-calpain activity are altered in type 2 diabetes mellitus and restored by rosiglitazone
Circulation
117
52-60
2008
Homo sapiens
Manually annotated by BRENDA team
Wu, M.; Yu, Z.; Fan, J.; Caron, A.; Whiteway, M.; Shen, S.H.
Functional dissection of human protease mu-calpain in cell migration using RNAi
FEBS Lett.
580
3246-3256
2006
Homo sapiens
Manually annotated by BRENDA team
Murphy, R.M.; Goodman, C.A.; McKenna, M.J.; Bennie, J.; Leikis, M.; Lamb, G.D.
Calpain-3 is autolyzed and hence activated in human skeletal muscle 24 h following a single bout of eccentric exercise
J. Appl. Physiol.
103
926-931
2007
Homo sapiens
Manually annotated by BRENDA team
Xu, L.; Deng, X.
Suppression of cancer cell migration and invasion by protein phosphatase 2A through dephosphorylation of micro- and m-calpains
J. Biol. Chem.
281
35567-35575
2006
Homo sapiens
Manually annotated by BRENDA team
Badugu, R.; Garcia, M.; Bondada, V.; Joshi, A.; Geddes, J.W.
N terminus of calpain 1 is a mitochondrial targeting sequence
J. Biol. Chem.
283
3409-3417
2008
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Yaroslavskiy, B.B.; Sharrow, A.C.; Wells, A.; Robinson, L.J.; Blair, H.C.
Necessity of inositol (1,4,5)-trisphosphate receptor 1 and mu-calpain in NO-induced osteoclast motility
J. Cell Sci.
120
2884-2894
2007
Homo sapiens
Manually annotated by BRENDA team
Upla, P.; Marjomaeki, V.; Nissinen, L.; Nylund, C.; Waris, M.; Hyypiae, T.; Heino, J.
Calpain 1 and 2 are required for RNA replication of echovirus 1
J. Virol.
82
1581-1590
2008
Homo sapiens
Manually annotated by BRENDA team
Covington, M.D.; Arrington, D.D.; Schnellmann, R.G.
Calpain 10 is required for cell viability and is decreased in the aging kidney
Am. J. Physiol. Renal Physiol.
296
F478-F486
2009
Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Vissing, K.; Overgaard, K.; Nedergaard, A.; Fredsted, A.; Schjerling, P.
Effects of concentric and repeated eccentric exercise on muscle damage and calpain-calpastatin gene expression in human skeletal muscle
Eur. J. Appl. Physiol.
103
323-332
2008
Homo sapiens, Homo sapiens (P07384)
Manually annotated by BRENDA team
Verburg, E.; Murphy, R.M.; Richard, I.; Lamb, G.D.
Involvement of calpains in Ca2+-induced disruption of excitation-contraction coupling in mammalian skeletal muscle fibers
Am. J. Physiol. Cell Physiol.
296
C1115-C1122
2009
Homo sapiens
Manually annotated by BRENDA team
Sergeev, I.N.
1,25-Dihydroxyvitamin D3 induces Ca2+-mediated apoptosis in adipocytes via activation of calpain and caspase-12
Biochem. Biophys. Res. Commun.
384
18-21
2009
Homo sapiens
Manually annotated by BRENDA team
Hayakawa, M.; Hayakawa, H.; Matsuyama, Y.; Tamemoto, H.; Okazaki, H.; Tominaga, S.
Mature interleukin-33 is produced by calpain-mediated cleavage in vivo
Biochem. Biophys. Res. Commun.
387
218-222
2009
Homo sapiens
Manually annotated by BRENDA team
Jiao, W.; McDonald, D.Q.; Coxon, J.M.; Parker, E.J.
Molecular modeling studies of peptide inhibitors highlight the importance of conformational prearrangement for inhibition of calpain
Biochemistry
49
5533-5539
2010
Homo sapiens
Manually annotated by BRENDA team
Zhang, P.; Sridharan, D.M.; Lambert, M.W.
Knockdown of micro-calpain in Fanconi Anemia, FA-A, cells by siRNA restores alphaII spectrin levels and corrects chromosomal instability and defective DNA interstrand cross-link repair
Biochemistry
49
5570-5581
2010
Homo sapiens
Manually annotated by BRENDA team
Mellgren, R.L.; Miyake, K.; Kramerova, I.; Spencer, M.J.; Bourg, N.; Bartoli, M.; Richard, I.; Greer, P.A.; McNeil, P.L.
Calcium-dependent plasma membrane repair requires m- or mu-calpain, but not calpain-3, the proteasome, or caspases
Biochim. Biophys. Acta
1793
1886-1893
2009
Homo sapiens
Manually annotated by BRENDA team
Kelly, J.C.; Cuerrier, D.; Graham, L.A.; Campbell, R.L.; Davies, P.L.
Profiling of calpain activity with a series of FRET-based substrates
Biochim. Biophys. Acta
1794
1505-1509
2009
Homo sapiens
Manually annotated by BRENDA team
Goncalves, I.; Nitulescu, M.; Saido, T.; Dias, N.; Pedro, L.; e Fernandes, J.; Ares, M.; Poern-Ares, I.
Activation of calpain-1 in human carotid artery atherosclerotic lesions
BMC Cardiovasc. Disord.
9
26
2009
Homo sapiens
Manually annotated by BRENDA team
Blachford, C.; Celic, A.; Petri, E.T.; Ehrlich, B.E.
Discrete proteolysis of neuronal calcium sensor-1 (NCS-1) by mu-calpain disrupts calcium binding
Cell Calcium
46
257-262
2009
Homo sapiens
Manually annotated by BRENDA team
Dean, P.; Muehlen, S.; Quitard, S.; Kenny, B.
The bacterial effectors EspG and EspG2 induce a destructive calpain activity that is kept in check by the co-delivered Tir effector
Cell. Microbiol.
12
1308-1321
2010
Homo sapiens
Manually annotated by BRENDA team
Murphy, R.M.
Calpains, skeletal muscle function and exercise
Clin. Exp. Pharmacol. Physiol.
37
385-391
2010
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Pietsch, M.; Chua, K.C.; Abell, A.D.
Calpains: attractive targets for the development of synthetic inhibitors
Curr. Top. Med. Chem.
10
270-293
2010
Homo sapiens
Manually annotated by BRENDA team
Le Goff, E.; Vallentin, A.; Harmand, P.O.; Aldrian-Herrada, G.; Rebiere, B.; Roy, C.; Benyamin, Y.; Lebart, M.C.
Characterization of L-plastin interaction with beta integrin and its regulation by micro-calpain
Cytoskeleton (Hoboken)
67
286-296
2010
Homo sapiens
Manually annotated by BRENDA team
Roumes, H.; Leloup, L.; Dargelos, E.; Brustis, J.J.; Daury, L.; Cottin, P.
Calpains: markers of tumor aggressiveness?
Exp. Cell Res.
316
1587-1599
2010
Homo sapiens
Manually annotated by BRENDA team
Ravulapalli, R.; Campbell, R.L.; Gauthier, S.Y.; Dhe-Paganon, S.; Davies, P.L.
Distinguishing between calpain heterodimerization and homodimerization
FEBS J.
276
973-982
2009
Homo sapiens
Manually annotated by BRENDA team
Simonin, Y.; Disson, O.; Lerat, H.; Antoine, E.; Biname, F.; Rosenberg, A.R.; Desagher, S.; Lassus, P.; Bioulac-Sage, P.; Hibner, U.
Calpain activation by hepatitis C virus proteins inhibits the extrinsic apoptotic signaling pathway
Hepatology
50
1370-1379
2009
Homo sapiens
Manually annotated by BRENDA team
Martin-Villar, E.; Yurrita, M.M.; Fernandez-Munoz, B.; Quintanilla, M.; Renart, J.
Regulation of podoplanin/PA2.26 antigen expression in tumour cells. Involvement of calpain-mediated proteolysis
Int. J. Biochem. Cell Biol.
41
1421-1429
2009
Homo sapiens
Manually annotated by BRENDA team
Liu, L.; Xing, D.; Chen, W.R.
Micro-calpain regulates caspase-dependent and apoptosis inducing factor-mediated caspase-independent apoptotic pathways in cisplatin-induced apoptosis
Int. J. Cancer
125
2757-2766
2009
Homo sapiens
Manually annotated by BRENDA team
Wu, Y.; Zhang, L.; Jin, H.; Zhou, J.; Xie, Z.
The role of calpain-calpastatin system in the development of stress urinary incontinence
Int. Urogynecol. J. Pelvic. Floor Dysfunct.
21
63-68
2010
Homo sapiens
Manually annotated by BRENDA team
Lehti, M.; Kivelae, R.; Komi, P.; Komulainen, J.; Kainulainen, H.; Kyroelaeinen, H.
Effects of fatiguing jumping exercise on mRNA expression of titin-complex proteins and calpains
J. Appl. Physiol.
106
1419-1424
2009
Homo sapiens
Manually annotated by BRENDA team
Gafni, J.; Cong, X.; Chen, S.F.; Gibson, B.W.; Ellerby, L.M.
Calpain-1 cleaves and activates caspase-7
J. Biol. Chem.
284
25441-25449
2009
Homo sapiens
Manually annotated by BRENDA team
OConnell, M.P.; Fiori, J.L.; Baugher, K.M.; Indig, F.E.; French, A.D.; Camilli, T.C.; Frank, B.P.; Earley, R.; Hoek, K.S.; Hasskamp, J.H.; Elias, E.G.; Taub, D.D.; Bernier, M.; Weeraratna, A.T.
Wnt5A activates the calpain-mediated cleavage of filamin A
J. Invest. Dermatol.
129
1782-1789
2009
Homo sapiens
Manually annotated by BRENDA team
Kang, D.H.; Jun, K.Y.; Lee, J.P.; Pak, C.S.; Na, Y.; Kwon, Y.
Identification of 3-acetyl-2-aminoquinolin-4-one as a novel, nonpeptidic scaffold for specific calpain inhibitory activity
J. Med. Chem.
52
3093-3097
2009
Homo sapiens
Manually annotated by BRENDA team
Averna, M.; Stifanese, R.; De Tullio, R.; Beccaria, F.; Salamino, F.; Pontremoli, S.; Melloni, E.
Calpain-mediated activation of NO synthase in human neuroblastoma SK-N-BE cells
J. Neurochem.
110
412-421
2009
Homo sapiens
Manually annotated by BRENDA team
Wang, Y.; Kim, N.S.; Li, X.; Greer, P.A.; Koehler, R.C.; Dawson, V.L.; Dawson, T.M.
Calpain activation is not required for AIF translocation in PARP-1-dependent cell death (parthanatos)
J. Neurochem.
110
687-696
2009
Homo sapiens
Manually annotated by BRENDA team
Xu, J.; Kurup, P.; Zhang, Y.; Goebel-Goody, S.M.; Wu, P.H.; Hawasli, A.H.; Baum, M.L.; Bibb, J.A.; Lombroso, P.J.
Extrasynaptic NMDA receptors couple preferentially to excitotoxicity via calpain-mediated cleavage of STEP
J. Neurosci.
29
9330-9343
2009
Homo sapiens
Manually annotated by BRENDA team
Zadran, S.; Jourdi, H.; Rostamiani, K.; Qin, Q.; Bi, X.; Baudry, M.
Brain-derived neurotrophic factor and epidermal growth factor activate neuronal m-calpain via mitogen-activated protein kinase-dependent phosphorylation
J. Neurosci.
30
1086-1095
2010
Homo sapiens
Manually annotated by BRENDA team
Ma, H.; Tochigi, A.; Shearer, T.R.; Azuma, M.
Calpain inhibitor SNJ-1945 attenuates events prior to angiogenesis in cultured human retinal endothelial cells
J. Ocul. Pharmacol. Ther.
25
409-414
2009
Homo sapiens
Manually annotated by BRENDA team
Alonso, M.; Chicharro, R.; Miranda, C.; Aran, V.J.; Maestro, M.A.; Herradon, B.
X-ray diffraction, solution structure, and computational studies on derivatives of (3-sec-butyl-2,3-dihydro-1H-isoquinolin-4-ylidene)acetic acid: compounds with activity as calpain inhibitors
J. Org. Chem.
75
342-352
2010
Homo sapiens
Manually annotated by BRENDA team
Rudic, B.; Song, H.; Breedijk, A.; Brinkkoetter, P.; Beck, G.; Yard, B.; Ponelies, N.
Hypothermic preservation up-regulates calpain expression and increases ubiquitination in cultured vascular endothelial cells: influence of dopamine pretreatment
J. Surg. Res.
160
325-332
2010
Homo sapiens
Manually annotated by BRENDA team
Esteves, A.R.; Arduino, D.M.; Swerdlow, R.H.; Oliveira, C.R.; Cardoso, S.M.
Dysfunctional mitochondria uphold calpain activation: contribution to Parkinsons disease pathology
Neurobiol. Dis.
37
723-730
2010
Homo sapiens
Manually annotated by BRENDA team
Kulkarni, S.; Reddy, K.B.; Esteva, F.J.; Moore, H.C.; Budd, G.T.; Tubbs, R.R.
Calpain regulates sensitivity to trastuzumab and survival in HER2-positive breast cancer
Oncogene
29
1339-1350
2010
Homo sapiens
Manually annotated by BRENDA team
Chandramohanadas, R.; Davis, P.H.; Beiting, D.P.; Harbut, M.B.; Darling, C.; Velmourougane, G.; Lee, M.Y.; Greer, P.A.; Roos, D.S.; Greenbaum, D.C.
Apicomplexan parasites co-opt host calpains to facilitate their escape from infected cells
Science
324
794-797
2009
Homo sapiens
Manually annotated by BRENDA team
Kim, D.S.; Han, B.G.; Park, K.S.; Lee, B.I.; Kim, S.Y.; Bae, C.D.
I-kappaBalpha depletion by transglutaminase 2 and mu-calpain occurs in parallel with the ubiquitin-proteasome pathway
Biochem. Biophys. Res. Commun.
399
300-306
2010
Homo sapiens
Manually annotated by BRENDA team
Panigrahi, A.K.; Zhang, N.; Mao, Q.; Pati, D.
Calpain-1 cleaves Rad21 to promote sister chromatid separation
Mol. Cell. Biol.
31
4335-4347
2011
Homo sapiens
Manually annotated by BRENDA team
Prangsaengtong, O.; Senda, K.; Doki, Y.; Park, J.Y.; Jo, M.; Sakurai, H.; Shibahara, N.; Saiki, I.; Koizumi, K.
Calpain 1 and -2 play opposite roles in cord formation of lymphatic endothelial cells via eNOS regulation
Hum. Cell
25
36-44
2012
Homo sapiens
Manually annotated by BRENDA team
Averna, M.; De Tullio, R.; Pedrazzi, M.; Bavestrello, M.; Pellegrini, M.; Salamino, F.; Pontremoli, S.; Melloni, E.
Interaction between calpain-1 and HSP90: new insights into the regulation of localization and activity of the protease
PLoS ONE
10
e0116738
2015
Homo sapiens
Manually annotated by BRENDA team
Fan, X.; Zhang, Q.; You, C.; Qian, Y.; Gao, J.; Liu, P.; Chen, H.; Song, H.; Chen, Y.; Chen, K.; Zhou, Y.
Proteolysis of the human DNA polymerase delta smallest subunit p12 by mu-calpain in calcium-triggered apoptotic HeLa cells
PLoS ONE
9
e93642
2014
Homo sapiens
Manually annotated by BRENDA team
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