Homology modeling study of bovine μ-calpain inhibitor-binding domains.

Exploring the Molecular Basis for Binding of Inhibitors by Threonyl-tRNA Synthetase from Brucella abortus: A Virtual Screening Study. Int J Mol Sci (2016) 0.75

Structure validation by Calpha geometry: phi,psi and Cbeta deviation. Proteins (2003) 32.38

On the size of the active site in proteases. I. Papain. Biochem Biophys Res Commun (1967) 18.32

The calpain system. Physiol Rev (2003) 9.95

Statistical potential for assessment and prediction of protein structures. Protein Sci (2006) 8.98

Evaluation of comparative protein modeling by MODELLER. Proteins (1995) 6.42

Toward the estimation of the absolute quality of individual protein structure models. Bioinformatics (2010) 5.08

Targeting proteases: successes, failures and future prospects. Nat Rev Drug Discov (2006) 4.39

Neurotoxicity induces cleavage of p35 to p25 by calpain. Nature (2000) 4.31

Calcium-activated neutral protease (calpain) system: structure, function, and regulation. Physiol Rev (1991) 3.53

Derivation of rules for comparative protein modeling from a database of protein structure alignments. Protein Sci (1994) 2.56

Structure, activation, and biology of calpain. Diabetes (2004) 2.16

On the sequential determinants of calpain cleavage. J Biol Chem (2004) 2.13

Structure of a calpain Ca(2+)-binding domain reveals a novel EF-hand and Ca(2+)-induced conformational changes. Nat Struct Biol (1997) 1.96

The PMDB Protein Model Database. Nucleic Acids Res (2006) 1.94

Calcium-bound structure of calpain and its mechanism of inhibition by calpastatin. Nature (2008) 1.84

Crystal structure of calcium bound domain VI of calpain at 1.9 A resolution and its role in enzyme assembly, regulation, and inhibitor binding. Nat Struct Biol (1997) 1.78

Crystal structure of calpain reveals the structural basis for Ca(2+)-dependent protease activity and a novel mode of enzyme activation. EMBO J (1999) 1.70

The crystal structure of calcium-free human m-calpain suggests an electrostatic switch mechanism for activation by calcium. Proc Natl Acad Sci U S A (2000) 1.65

A Ca(2+) switch aligns the active site of calpain. Cell (2002) 1.65

Activation of m-calpain (calpain II) by epidermal growth factor is limited by protein kinase A phosphorylation of m-calpain. Mol Cell Biol (2002) 1.64

Concerted multi-pronged attack by calpastatin to occlude the catalytic cleft of heterodimeric calpains. Nature (2008) 1.55

Determination of peptide substrate specificity for mu-calpain by a peptide library-based approach: the importance of primed side interactions. J Biol Chem (2005) 1.44

Calpains: an elaborate proteolytic system. Biochim Biophys Acta (2011) 1.38

Domain III of calpain is a ca2+-regulated phospholipid-binding domain. Biochem Biophys Res Commun (2001) 1.22

The therapeutic potential of the calpain family: new aspects. Drug Discov Today (2006) 1.17

Inhibition of calpain by a synthetic oligopeptide corresponding to an exon of the human calpastatin gene. J Biol Chem (1989) 1.13

Structure of a trapped intermediate of calmodulin: calcium regulation of EF-hand proteins from a new perspective. J Mol Biol (2005) 1.12

A catalytic subunit of calpain possesses full proteolytic activity. FEBS Lett (1995) 1.10

Calpain cleavage prediction using multiple kernel learning. PLoS One (2011) 1.09

Identification and characterization of inhibitory sequences in four repeating domains of the endogenous inhibitor for calcium-dependent protease. J Biochem (1989) 1.08

A structural model for the inhibition of calpain by calpastatin: crystal structures of the native domain VI of calpain and its complexes with calpastatin peptide and a small molecule inhibitor. J Mol Biol (2003) 1.07

Insights into modulation of calcium signaling by magnesium in calmodulin, troponin C and related EF-hand proteins. Biochim Biophys Acta (2011) 1.06

Mutations in calpain 3 associated with limb girdle muscular dystrophy: analysis by molecular modeling and by mutation in m-calpain. Biophys J (2001) 1.05

Calpain 8/nCL-2 and calpain 9/nCL-4 constitute an active protease complex, G-calpain, involved in gastric mucosal defense. PLoS Genet (2010) 1.03

Calpain dissociates into subunits in the presence of calcium ions. Biochem Biophys Res Commun (1995) 1.02

Crystal structures of calpain-E64 and -leupeptin inhibitor complexes reveal mobile loops gating the active site. J Mol Biol (2004) 1.02

The crystal structures of human calpains 1 and 9 imply diverse mechanisms of action and auto-inhibition. J Mol Biol (2006) 1.01

Impact of genetic insights into calpain biology. J Biochem (2011) 1.00

Regulation and physiological roles of the calpain system in muscular disorders. Cardiovasc Res (2012) 0.97

Binding of calpain fragments to calpastatin. J Biol Chem (1991) 0.97

Studies of the active site of m-calpain and the interaction with calpastatin. Biochem J (1993) 0.95

Calpains: attractive targets for the development of synthetic inhibitors. Curr Top Med Chem (2010) 0.95

Molecular diversity in amino-terminal domains of human calpastatin by exon skipping. J Biol Chem (1992) 0.94

The bovine calpastatin gene promoter and a new N-terminal region of the protein are targets for cAMP-dependent protein kinase activity. J Biol Chem (1998) 0.93

Calpain mutants with increased Ca2+ sensitivity and implications for the role of the C(2)-like domain. J Biol Chem (2000) 0.92

Amino-terminal conserved region in proteinase inhibitor domain of calpastatin potentiates its calpain inhibitory activity by interacting with calmodulin-like domain of the proteinase. J Biol Chem (1994) 0.91

Structural determinants of the calpain inhibitory activity of calpastatin peptide B27-WT. J Biol Chem (2002) 0.89

Calpain activation by cooperative Ca2+ binding at two non-EF-hand sites. J Biol Chem (2003) 0.89

Crystal structure of a micro-like calpain reveals a partially activated conformation with low Ca2+ requirement. Structure (2003) 0.89

Calpastatins: biochemical and molecular biological studies. Biomed Biochim Acta (1991) 0.87

Calpastatin simultaneously binds four calpains with different kinetic constants. FEBS Lett (2007) 0.87

Two-stage autolysis of the catalytic subunit initiates activation of calpain I. Biochim Biophys Acta (1991) 0.85

A newly classified vertebrate calpain protease, directly ancestral to CAPN1 and 2, episodically evolved a restricted physiological function in placental mammals. Mol Biol Evol (2010) 0.83

Activation of calpain by Ca2+: roles of the large subunit N-terminal and domain III-IV linker peptides. J Mol Biol (2004) 0.83

The calpain cleavage sites in the epidermal growth factor receptor kinase domain. Eur J Biochem (1994) 0.83

Origins of the difference in Ca2+ requirement for activation of mu- and m-calpain. Biochem J (2002) 0.82

Bovine skeletal muscle calpastatin: cloning, sequence analysis, and steady-state mRNA expression. J Anim Sci (1994) 0.80

Mutations in calpastatin and μ-calpain are associated with meat tenderness, flavor and juiciness in Hanwoo (Korean cattle): molecular modeling of the effects of substitutions in the calpastatin/μ-calpain complex. Meat Sci (2013) 0.79

Cardiac high molecular weight calmodulin-binding protein is homologous to calpastatin I and calpastatin II. Biochem Biophys Res Commun (2008) 0.79

Effect of nutrient restriction and re-feeding on calpain family genes in skeletal muscle of channel catfish (Ictalurus punctatus). PLoS One (2013) 0.78

Hydrolysis of protamine by calcium-activated neutral protease (CANP). J Biochem (1985) 0.76

Understanding the interaction determinants of CAPN1 inhibition by CAST4 from bovines using molecular modeling techniques. Molecules (2014) 0.77