Ventricular myosin modifies in vitro step-size when phosphorylated

Journal of Molecular and Cellular Cardiology

Volumn 72, Issue , 2014, Pages 231-237

  Wang, Yihua ^a   Ajtai, Katalin ^a   Burghardt, Thomas P ^a  

^a Department of Biochemistry and Molecular Biology ^*  (United States)

Author keywords

Actin activated ATPase; Cardiac myosin RLC phosphorylation; In vitro motility; Qdot assay; Ventricular myosin step size

Indexed keywords

ACTIN; ADENOSINE TRIPHOSPHATASE; CARDIAC MYOSIN; MYOSIN HEAVY CHAIN BETA; MYOSIN LIGHT CHAIN KINASE; QUANTUM DOT; ADENOSINE TRIPHOSPHATE; MYOSIN LIGHT CHAIN; VENTRICULAR MYOSIN;

ARTICLE; CARDIOVASCULAR PARAMETERS; ENZYME ACTIVATION; HEART CONTRACTION; HEART VENTRICLE; LIGHT CHAIN; PRIORITY JOURNAL; PROTEIN DETERMINATION; PROTEIN FUNCTION; PROTEIN PHOSPHORYLATION; PROTEIN STABILITY; PROTEIN STRUCTURE; QUANTUM DOT ASSAY; VENTRICULAR MYOSIN STEP SIZE; ANIMAL; BIOMECHANICS; CELL MOTION; CHEMISTRY; HEART MUSCLE; METABOLISM; PHOSPHORYLATION; PHYSIOLOGY; RABBIT; SKELETAL MUSCLE; SWINE;

ACTINS; ADENOSINE TRIPHOSPHATE; ANIMALS; BIOMECHANICAL PHENOMENA; CELL MOVEMENT; HEART VENTRICLES; MUSCLE, SKELETAL; MYOCARDIAL CONTRACTION; MYOCARDIUM; MYOSIN LIGHT CHAINS; PHOSPHORYLATION; QUANTUM DOTS; RABBITS; SWINE; VENTRICULAR MYOSINS;

EID: 84901335911     PISSN: 00222828     EISSN: 10958584     Source Type: Journal    
DOI: 10.1016/j.yjmcc.2014.03.022     Document Type: Article

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