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Volumn 1596, Issue 1, 2002, Pages 121-130
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Phosphorylation of the minimal inhibitory region at the C-terminus of caldesmon alters its structural and actin binding properties
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Author keywords
Actin binding; Caldesmon; Mitogen activated protein kinase; Nuclear magnetic resonance; Phosphorylation
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Indexed keywords
ACTIN BINDING PROTEIN;
AMINO ACID;
CALDESMON;
F ACTIN;
FUNCTIONAL GROUP;
MITOGEN ACTIVATED PROTEIN KINASE;
ARTICLE;
BINDING AFFINITY;
BINDING SITE;
CARBOXY TERMINAL SEQUENCE;
COVALENT BOND;
IONIZATION;
NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY;
PRIORITY JOURNAL;
PROTEIN BINDING;
PROTEIN DOMAIN;
PROTEIN PHOSPHORYLATION;
PROTEIN PROTEIN INTERACTION;
PROTEIN STABILITY;
PROTEIN STRUCTURE;
ACTINS;
BINDING SITES;
CALMODULIN-BINDING PROTEINS;
HUMANS;
MAGNETIC RESONANCE SPECTROSCOPY;
MOLECULAR STRUCTURE;
MYOSINS;
PEPTIDES;
PHOSPHORYLATION;
PROTEIN CONFORMATION;
SERINE;
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EID: 0036538367
PISSN: 01674838
EISSN: None
Source Type: Journal
DOI: 10.1016/S0167-4838(02)00210-8 Document Type: Article |
Times cited : (16)
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References (27)
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