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EC Number
BRENDA No.
Title
Journal
Volume
Pages
Year
Organism
PubMed ID
3.4.24.84
638976
Reconstitution of the Ste24p-dependent N-terminal proteolytic step in yeast a-factor biogenesis
J. Biol. Chem.
275
6227-6233
2000
Saccharomyces cerevisiae
10692417
3.4.24.84
638976
Reconstitution of the Ste24p-dependent N-terminal proteolytic step in yeast a-factor biogenesis
J. Biol. Chem.
275
6227-6233
2000
Homo sapiens
10692417
3.4.24.84
735044
Requirements for efficient proteolytic cleavage of prelamin A by ZMPSTE24
PLoS ONE
7
e32120
2012
Homo sapiens
22355414
3.4.24.84
651423
Roles pf prenyl protein proteases in maturation of Saccharomyces cerevisiae
Genetics
150
95-1001
1998
Saccharomyces cerevisiae
9725832
3.4.24.84
638978
The Arabidopsis AtSTE24 is a CAAX protease with broad substrate specificity
J. Biol. Chem.
277
29856-29864
2002
Homo sapiens
12039957
3.4.24.84
638978
The Arabidopsis AtSTE24 is a CAAX protease with broad substrate specificity
J. Biol. Chem.
277
29856-29864
2002
Saccharomyces cerevisiae
12039957
3.4.24.84
638978
The Arabidopsis AtSTE24 is a CAAX protease with broad substrate specificity
J. Biol. Chem.
277
29856-29864
2002
Arabidopsis thaliana
12039957
3.4.24.84
653214
The CaaX proteases, Afc1p and Rce1p, have overlapping but distinct substrate specificities
Mol. Cell. Biol.
20
4381-4392
2000
Saccharomyces cerevisiae
10825201
3.4.24.84
638977
The multispanning membrane protein Ste24p catalyzes CAAX proteolysis and NH2-terminal processing of the yeast a-factor precursor
J. Biol. Chem.
276
46798-46806
2001
Saccharomyces cerevisiae
11581258
3.4.24.84
654005
Type II CAAX prenyl endopeptidases belong to a novel superfamily of putative membrane-bound metalloproteases
Trends Biochem. Sci.
26
275-277
2001
Saccharomyces cerevisiae
11343912
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