Phosphorylation of caldesmon by myosin light chain kinase increases its binding affinity for phosphorylated myosin filaments

Biological Chemistry

Volumn 391, Issue 9, 2010, Pages 1091-1104

  Sobieszek, Apolinary ^a   Sarg, Bettina ^b   Lindner, Herbert ^b   Seow, Chun Y ^c  

^a ERICH SCHMID INSTITUTE OF MATERIALS SCIENCE   (Austria)

^b INNSBRUCK MEDICAL UNIVERSITY   (Austria)

^c UNIVERSITY OF BRITISH COLUMBIA   (Canada)

Author keywords

calcium regulation; caldesmon; kinase; myosin; phosphorylation; smooth muscle

Indexed keywords

ACTIN; CALDESMON; MYOSIN; MYOSIN ADENOSINE TRIPHOSPHATASE; MYOSIN LIGHT CHAIN KINASE; PHOSPHOPEPTIDE;

ACTIN FILAMENT; ANIMAL TISSUE; ARTICLE; AVIAN STOMACH; BINDING AFFINITY; DEPHOSPHORYLATION; ENZYME PHOSPHORYLATION; MASS SPECTROMETRY; MUSCLE CONTRACTION; NONHUMAN; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; PROTEIN PURIFICATION; SMOOTH MUSCLE CONTRACTION; TURKEY (BIRD);

ANIMALS; BINDING SITES; CALMODULIN-BINDING PROTEINS; MUSCLE CONTRACTION; MUSCLE, SMOOTH, VASCULAR; MYOSIN-LIGHT-CHAIN KINASE; MYOSINS; PHOSPHOPROTEINS; PHOSPHORYLATION; PROTEIN BINDING; TURKEYS;

EID: 77957558271     PISSN: 14316730     EISSN: 14374315     Source Type: Journal    
DOI: 10.1515/BC.2010.105     Document Type: Article

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