Molecular charge dominates the inhibition of actomyosin in skinned muscle fibers by SH1 peptides
- 1 August 1991
- journal article
- Published by Elsevier in Biophysical Journal
- Vol. 60 (2) , 352-359
- https://doi.org/10.1016/s0006-3495(91)82060-4
Abstract
No abstract availableKeywords
This publication has 43 references indexed in Scilit:
- Coupling of nonpolymerizable monomeric actin to the F-actin binding region of the myosin head.Proceedings of the National Academy of Sciences, 1989
- On the origin and transmission of force in actomyosin subfragment 1.Proceedings of the National Academy of Sciences, 1989
- Myosin Structure and Function in Cell MotilityAnnual Review of Cell Biology, 1987
- Measurement of interprotein distances in the acto-subfragment 1 rigor complexBiochemistry, 1987
- Measurements on permeabilized skeletal muscle fibers during continuous activationAmerican Journal of Physiology-Cell Physiology, 1987
- Actin-binding site of pig cardiac myosinBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1987
- Conserved protein domains in a myosin heavy chain gene from Dictyostelium discoideum.Proceedings of the National Academy of Sciences, 1986
- Effect of various anions on the stability of the coiled coil of skeletal muscle myosinBiochemistry, 1985
- Rapid analysis of amino acids using pre-column derivatizationJournal of Chromatography B: Biomedical Sciences and Applications, 1984
- Interaction between Myosin and F-Actin. Correlation with Actin-Binding Sites on Subfragment-11The Journal of Biochemistry, 1984