The Regulatory Light Chains of Myosin Modulate Cross-bridge Cycling in Skeletal Muscle
Open Access
- 1 March 1996
- journal article
- Published by Elsevier
- Vol. 271 (9) , 5246-5250
- https://doi.org/10.1074/jbc.271.9.5246
Abstract
No abstract availableKeywords
This publication has 35 references indexed in Scilit:
- Tilting of the light-chain region of myosin during step length changes and active force generation in skeletal muscleNature, 1995
- Structure of the regulatory domain of scallop myosin at 2.8 Ä resolutionNature, 1994
- Conformational changes of F-actin in myosin-free ghost single fibre induced by either phosphorylated or dephosphorylated heavy meromyosinBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1987
- Binding of phosphorylated and dephosphorylated heavy meromyosin to F‐actinFEBS Letters, 1987
- Factors influencing interaction of phosphorylated and dephosphorylated myosin with actinBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1985
- The significance of the slow dissociation of divalent metal ions from myosin ‘regulatory’ light chainsFEBS Letters, 1977
- Regulation of the actin-myosin interaction in vertebrate smooth muscle: Activation via a myosin light-chain kinase and the effect of tropomyosinJournal of Molecular Biology, 1977
- The light chains of scallop myosin as regulatory subunitsJournal of Molecular Biology, 1973
- Regulation in molluscan musclesJournal of Molecular Biology, 1970
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970