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Calpain chronicle—an enzyme family under multidisciplinary characterization
Open accessAbstract
Calpain is an intracellular Ca2+-dependent cysteine protease (EC 3.4.22.17; Clan CA, family C02) discovered in 1964. It was also called CANP (Ca2+-activated neutral protease) as well as CASF, CDP, KAF, etc. until 1990. Calpains are found in almost all eukaryotes and a few bacteria, but not in archaebacteria. Calpains have a limited proteolytic activity, and function to transform or modulate their substrates' structures and activities; they are therefore called, "modulator proteases." In the human genome, 15 genes--CAPN1, CAPN2, etc.--encode a calpain-like protease domain. Their products are calpain homologs with divergent structures and various combinations of functional domains, including Ca2+-binding and microtubule-interaction domains. Genetic studies have linked calpain deficiencies to a variety of defects in many different organisms, including lethality, muscular dystrophies, gastropathy, and diabetes. This review of the study of calpains focuses especially on recent findings about their structure-function relationships. These discoveries have been greatly aided by the development of 3D structural studies and genetic models.
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Danial, N. N., & Korsmeyer, S. J. (2004) · Cell · doi:10.1016/s0092-8674(04)00046-7 · Cited by 4,651
A comprehensive two-hybrid analysis to explore the yeast protein interactome
Ito, T., Chiba, T., Ozawa, R., Yoshida, M., Hattori, M., & Sakaki, Y. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.061034498 · Cited by 3,566
Mitochondria and cell death: outer membrane permeabilization and beyond
Tait, S. W. G., & Green, D. R. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2952 · Cited by 2,593
Autophagy in mammalian development and differentiation
Mizushima, N., & Levine, B. (2010) · Nature Cell Biology · doi:10.1038/ncb0910-823 · Cited by 1,555
Calpain is required for macroautophagy in mammalian cells
Demarchi, F., Bertoli, C., Copetti, T., Tanida, I., Brancolini, C., Eskelinen, E.-L., & Schneider, C. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200601024 · Cited by 156
Cornet, M., Bidard, F., Schwarz, P., Da Costa, G., Blanchin-Roland, S., Dromer, F., & Gaillardin, C. (2005) · Infection and Immunity · doi:10.1128/iai.73.12.7977-7987.2005 · Cited by 70
Tonami, K., Kurihara, Y., Arima, S., Nishiyama, K., Uchijima, Y., Asano, T., Sorimachi, H., & Kurihara, H. (2011) · Journal of Cell Science · doi:10.1242/jcs.072561 · Cited by 46
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Calpains — An elaborate proteolytic system
Ono, Y., & Sorimachi, H. (2012) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2011.08.005 · Cited by 349
Self-citationKottyan, L. C., Davis, B. P., Sherrill, J. D., Liu, K., Rochman, M., Kaufman, K., Weirauch, M. T., Vaughn, S., Lazaro, S., Rupert, A. M., et al. (2014) · Nature Genetics · doi:10.1038/ng.3033 · Cited by 302
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Metadata
- Authors
- SORIMACHI, H., HATA, S., & ONO, Y.
- Venue
- Proceedings of the Japan Academy, Series B
- Publisher
- Japan Academy
- Published
- 2011
- Volume
- 87
- Issue
- 6
- Pages
- 287-327
- ISSN
- 0386-2208 (ISSN-L)
- 1349-2896
- OpenAlex
- W2004386643
- Cited by
- 158
- References
- 7
- FWCI
- 7.22
- Type
- journal article
- Language
- en
- Open access
- bronze
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
