The proteins that inhibit peptidases are of great importance in medicine and biotechnology,
but there has never been a comprehensive system of classification for them. Some of the …

The calpains are a conserved family of cysteine proteinases that catalyse the controlled
proteolysis of many specific substrates. Calpain activity is implicated in several fundamental …

Mitochondrial activity is critical for efficient function of the cardiovascular system. In response
to cardiovascular injury, mitochondrial dysfunction occurs and can lead to apoptosis and …

Calpains are non-lysosomal calcium-dependent cysteine proteinases that selectively cleave
proteins in response to calcium signals and thereby control cellular functions such as …

Calpains are a family of complex multi-domain intracellular enzymes that share a calcium-
dependent cysteine protease core. These are not degradative enzymes, but instead carry …

Peptide-protein interactions contribute a significant fraction of the protein-protein
interactome. Accurate modeling of these interactions is challenging due to the vast …

Calpastatin is a multiheaded inhibitor capable of inhibiting more than one calpain molecule.
Each inhibitory domain of calpastatin has three subdomains, A, B, and C; A binds to domain …

The calpain family is named for the calcium dependence of the papain-like, thiol protease
activity of the well-studied ubiquitous vertebrate enzymes calpain-1 (μ-calpain) and calpain …

Oxygen-compromised environments, such as high altitude, air travel, and sports, and
pathological conditions, such as solid tumors, have been suggested to be prothrombotic …

The calpains represent a well-conserved family of calcium-dependent cysteine proteases.
They consist of several ubiquitous and tissue specific isoforms and exhibit broad substrate …