Myosin Heavy Chain Isoforms and Smooth Muscle Function
- 1 January 1991
- book chapter
- Published by Springer Nature
- Vol. 304, 139-145
- https://doi.org/10.1007/978-1-4684-6003-2_13
Abstract
Isoforms of striated muscle myosin have a long history. They have been extensively studied on biochemical and functional levels and more recently in terms of molecular biology. Under various environmental stresses the architecture of the contractile apparatus of striated muscle can be remodelled to meet the imposed demands.Keywords
This publication has 25 references indexed in Scilit:
- Myosin heavy‐chain isoforms in human smooth muscleEuropean Journal of Biochemistry, 1989
- Myosin composition and functional properties of smooth muscle from the uterus of pregnant and non-pregnant ratsPflügers Archiv - European Journal of Physiology, 1988
- Myosins of Nonmuscle CellsAnnual Review of Biophysics, 1988
- Isoforms of myosin and actin in human, monkey and rat myometriumEuropean Journal of Biochemistry, 1986
- Myosin isozymes in rabbit and human smooth muscles.Circulation Research, 1986
- Detection and distribution of myosin isozymes in vertebrate smooth muscleEuropean Journal of Biochemistry, 1985
- Changes in Myosin Isozymes during Development of Chicken Gizzard MuscleThe Journal of Biochemistry, 1983
- Thyroxine-induced redistribution of isoenzymes of rabbit ventricular myosin.Circulation Research, 1982
- Electrophoretic analysis of multiple forms of rat cardiac myosin: Effects of hypophysectomy and thyroxine replacementJournal of Molecular and Cellular Cardiology, 1978
- Actomyosin Content of the UterusNature, 1948