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EC Number
BRENDA No.
Title
Journal
Volume
Pages
Year
Organism
PubMed ID
3.4.22.59
647457
Mch2, a new member of the apoptotic Ced-3/Ice cysteine protease gene family
Cancer Res.
55
2737-2742
1995
Homo sapiens
7796396
3.4.22.59
647414
The Ced-3/interleukin 1beta converting enzyme-like homolog Mch6 and the lamin-cleaving enzyme Mch2alpha are substrates for the apoptotic mediator CPP32
J. Biol. Chem.
271
27099-27106
1996
Homo sapiens
8900201
3.4.22.59
647429
A combinatorial approach defines specificities of members of the caspase family and granzyme B. Functional relationships established for key mediators of apoptosis
J. Biol. Chem.
272
17907-17911
1997
Homo sapiens
9218414
3.4.22.59
647460
Characterization of seven murine caspase family members
FEBS Lett.
403
61-69
1997
Mus musculus
9038361
3.4.22.59
647471
Substrate specificities of caspase family proteases
J. Biol. Chem.
272
9677-9682
1997
Homo sapiens
9092497
3.4.22.59
647473
Caspases are activated in a branched protease cascade and control didtinct downstream processes in fas-induced apoptosis
J. Exp. Med.
187
587-600
1998
Homo sapiens
9463409
3.4.22.59
647423
Inhibition of human caspases by peptide-based and macromolecular inhibitors
J. Biol. Chem.
273
32608-32613
1998
Homo sapiens
9829999
3.4.22.59
647472
caspase-mediated cleavage of DNA topoisomerase I at unconventional sites during apoptosis
J. Biol. Chem.
274
4335-4340
1999
Homo sapiens
9933635
3.4.22.59
647454
Proteolytic cleavage of beta-catenin by caspases: an in vitro analysis
FEBS Lett.
458
167-170
1999
Mus musculus
10481058
3.4.22.59
647424
Purification and catalytic properties of human caspase family members
Cell Death Differ.
6
362-369
1999
Homo sapiens
10381624
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