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Cited by 349

The DOI matches its Crossref record; 111 of the 111 references it cites were found in a registry or an index.

Calpains — An elaborate proteolytic system

Open access
Ono, Yasuko, Sorimachi, Hiroyuki·2012·Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
DOI 10.1016/j.bbapap.2011.08.005
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Abstract

Calpain is an intracellular Ca(2+)-dependent cysteine protease (EC 3.4.22.17; Clan CA, family C02). Recent expansion of sequence data across the species definitively shows that calpain has been present throughout evolution; calpains are found in almost all eukaryotes and some bacteria, but not in archaebacteria. Fifteen genes within the human genome encode a calpain-like protease domain. Interestingly, some human calpains, particularly those with non-classical domain structures, are very similar to calpain homologs identified in evolutionarily distant organisms. Three-dimensional structural analyses have helped to identify calpain's unique mechanism of activation; the calpain protease domain comprises two core domains that fuse to form a functional protease only when bound to Ca(2+)via well-conserved amino acids. This finding highlights the mechanistic characteristics shared by the numerous calpain homologs, despite the fact that they have divergent domain structures. In other words, calpains function through the same mechanism but are regulated independently. This article reviews the recent progress in calpain research, focusing on those studies that have helped to elucidate its mechanism of action. This article is part of a Special Issue entitled: Proteolysis 50 years after the discovery of lysosome.

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Metadata

Authors
Ono, Y., & Sorimachi, H.
Venue
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
Publisher
Elsevier BV
Published
2012-01
Volume
1824
Issue
1
Pages
224-236
ISSN
1570-9639 (ISSN-L)
DOI
10.1016/j.bbapap.2011.08.005
OpenAlex
W1997151018
Cited by
349
References
111
FWCI
7.49
Type
journal article
Language
en
Open access
hybrid

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