Predictions of Cleavability of Calpain Proteolysis by Quantitative Structure-Activity Relationship Analysis Using Newly Determined Cleavage Sites and Catalytic Efficiencies of an Oligopeptide Array*

Abstract

Calpains are intracellular Ca(2+)-regulated cysteine proteases that are essential for various cellular functions. Mammalian conventional calpains (calpain-1 and calpain-2) modulate the structure and function of their substrates by limited proteolysis. Thus, it is critically important to determine the site(s) in proteins at which calpains cleave. However… (More)
DOI: 10.1074/mcp.M115.053413

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Cite this paper

@inproceedings{ShinkaiOuchi2016PredictionsOC, title={Predictions of Cleavability of Calpain Proteolysis by Quantitative Structure-Activity Relationship Analysis Using Newly Determined Cleavage Sites and Catalytic Efficiencies of an Oligopeptide Array* }, author={Fumiko Shinkai-Ouchi and Suguru Koyama and Yasuko Ono and Shoji Hata and Koichi Ojima and Mayumi Shindo and David duVerle and Mika Ueno and Fujiko Kitamura and Naoko Doi and Ichigaku Takigawa and Hiroshi Mamitsuka and Hiroyuki Sorimachi}, booktitle={Molecular & cellular proteomics : MCP}, year={2016} }