Inhibition of cross-bridge binding to actin by caldesmon fragments in skinned skeletal muscle fibers
- 31 March 1997
- journal article
- Published by Elsevier in Biophysical Journal
- Vol. 72 (3) , 1287-1294
- https://doi.org/10.1016/s0006-3495(97)78775-7
Abstract
No abstract availableKeywords
This publication has 58 references indexed in Scilit:
- Localization of the calmodulin- and the actin-binding sites of caldesmonJournal of Biological Chemistry, 1991
- Structural and functional relationships between h- and l-caldesmons.Journal of Biological Chemistry, 1991
- Caldesmon is a Ca2+-regulatory component of native smooth-muscle thin filamentsBiochemical Journal, 1985
- The influence of caldesmon on ATPase activity of the skeletal muscle actomyosin and bundling of actin filamentsBiochimica et Biophysica Acta (BBA) - General Subjects, 1985
- Purification and properties of Ca2+-regulated thin filaments and F-actin from sheep aorta smooth muscleJournal of Muscle Research and Cell Motility, 1984
- Technique for stabilizing the striation pattern in maximally calcium-activated skinned rabbit psoas fibersBiophysical Journal, 1983
- Evidence for cross-bridge attachment in relaxed muscle at low ionic strength.Proceedings of the National Academy of Sciences, 1982
- Inhibition of actomyosin ATPase activity by troponin-tropomyosin without blocking the binding of myosin to actin.Journal of Biological Chemistry, 1982
- Separation of subfragment-1 isoenzymes from rabbit skeletal muscle myosinNature, 1975
- Troponin-tropomyosin complex. Column chromatographic separation and activity of the three, active troponin components with and without tropomyosin present.1974