Comparison of Functional Characteristics of Myosin in Fast and Slow Skeletal Muscles-Reference-Cited by-同舟云学术

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Comparison of Functional Characteristics of Myosin in Fast and Slow Skeletal Muscles

Published:2020-07 Issue:3 Volume:169 Page:338-341
ISSN:0007-4888
Container-title:Bulletin of Experimental Biology and Medicine
language:en
Short-container-title:Bull Exp Biol Med

Author:

Shchepkin D. V.,Nabiev S. R.,Koubassova N. A.,Bershitsky S. Y.,Kopylova G. V.

Publisher

Springer Science and Business Media LLC

Subject

General Biochemistry, Genetics and Molecular Biology,General Medicine

Link

https://link.springer.com/content/pdf/10.1007/s10517-020-04882-x.pdf

Reference14 articles.

1. Canepari M, Maffei M, Longa E, Geeves M, Bottinelli R. Actomyosin kinetics of pure fast and slow rat myosin isoforms studied by in vitro motility assay approach. Exp. Physiol. 2012;97(7):873-881.

2. Geiger PC, Cody MJ, Sieck GC. Force-calcium relationship depends on myosin heavy chain and troponin isoforms in rat diaphragm muscle fibers. J. Appl. Physiol. (1985). 1999;87(5):1894-1900.

3. Iorga B, Adamek N, Geeves MA. The slow skeletal muscle isoform of myosin shows kinetic features common to smooth and non-muscle myosins. J. Biol. Chem. 2007;282(6):3559-3570.

4. Kad NM, Kim S, Warshaw DM, VanBuren P, Baker JE. Single-myosin crossbridge interactions with actin filaments regulated by troponin-tropomyosin. Proc. Natl Acad. Sci. USA. 2005;102(47):16,990-16,995.

5. Kopylova G, Nabiev S, Nikitina L, Shchepkin D, Bershit-sky S. The properties of the actin-myosin interaction in the heart muscle depend on the isoforms of myosin but not of α-actin. Biochem. Biophys. Res. Commun. 2016;476(4):648-653.

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