Velocities of unloaded muscle filaments are not limited by drag forces imposed by myosin cross-bridges

Proceedings of the National Academy of Sciences of the United States of America

Volumn 112, Issue 36, 2015, Pages 11235-11240

  Brizendine, Richard K ^a   Alcala, Diego B ^a   Carter, Michael S ^a   Haldeman, Brian D ^a   Facemyer, Kevin C ^a   Baker, Josh E ^a   Cremo, Christine R ^a  

^a UNIVERSITY OF NEVADA SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATASE; F ACTIN; MYOSIN; ACTIN; ADENOSINE TRIPHOSPHATE; MYOSIN ADENOSINE TRIPHOSPHATASE; PROTEIN BINDING; RHODAMINE;

ARTICLE; ASSAY; FORCE; IN VITRO STUDY; MUSCLE LENGTH; MYOFILAMENT; PRIORITY JOURNAL; SURFACE PROPERTY; VELOCITY; ACTIN FILAMENT; ALGORITHM; ANIMAL; BIOLOGICAL MODEL; CHEMISTRY; CHICKEN; DRUG EFFECTS; ELECTRON MICROSCOPY; FLUORESCENCE MICROSCOPY; KINETICS; METABOLISM; MUSCLE CONTRACTION; PROCEDURES; RABBIT; SMOOTH MUSCLE; ULTRASTRUCTURE;

ACTIN CYTOSKELETON; ACTINS; ACTOMYOSIN; ADENOSINE TRIPHOSPHATE; ALGORITHMS; ANIMALS; CHICKENS; KINETICS; MICROSCOPY, ELECTRON; MICROSCOPY, FLUORESCENCE; MODELS, BIOLOGICAL; MUSCLE CONTRACTION; MUSCLE, SMOOTH; MYOSINS; PROTEIN BINDING; RABBITS; RHODAMINES;

EID: 84941342895     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1510241112     Document Type: Article

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