Phosphorylation of Myosin Regulatory Light Chain Eliminates Force-Dependent Changes in Relaxation Rates in Skeletal Muscle
- 31 January 1998
- journal article
- Published by Elsevier in Biophysical Journal
- Vol. 74 (1) , 360-368
- https://doi.org/10.1016/s0006-3495(98)77793-8
Abstract
No abstract availableKeywords
This publication has 29 references indexed in Scilit:
- Cardiac Troponin I Phosphorylation Increases the Rate of Cardiac Muscle RelaxationCirculation Research, 1995
- Three-dimensional structure of myosin subfragment-1: a molecular motorScience, 1993
- Biologically useful chelators that take up calcium(2+) upon illuminationJournal of the American Chemical Society, 1989
- Variations in cross-bridge attachment rate and tension with phosphorylation of myosin in mammalian skinned skeletal muscle fibers. Implications for twitch potentiation in intact muscle.The Journal of general physiology, 1989
- Cooperative turning on of myosin subfragment 1 adenosine triphosphatase activity by the troponin-tropomyosin-actin complexBiochemistry, 1988
- Probing myosin head structure with monoclonal antibodiesJournal of Molecular Biology, 1986
- Effects of EDTA treatment upon the protein subunit composition and mechanical properties of mammalian single skeletal muscle fibersThe Journal of cell biology, 1983
- Influence of temperature upon contractile activation and isometric force production in mechanically skinned muscle fibers of the frog.The Journal of general physiology, 1982
- Mechanism of inhibition of relaxation by N-ethylmaleimide treatment of myosinBiochemistry, 1976
- Temperature‐Induced Transitions in the Conformation of Intermediates in the Hydrolytic Cycle of MyosinEuropean Journal of Biochemistry, 1975