Cardiomyopathy-associated mutations in tropomyosin differently affect actin–myosin interaction at single-molecule and ensemble levels-Reference-Cited by-同舟云学术

Cardiomyopathy-associated mutations in tropomyosin differently affect actin–myosin interaction at single-molecule and ensemble levels

Published:2019-10-23 Issue:3-4 Volume:40 Page:299-308
ISSN:0142-4319
Container-title:Journal of Muscle Research and Cell Motility
language:en
Short-container-title:J Muscle Res Cell Motil

Author:

Kopylova Galina V.^ORCID,Shchepkin Daniil V.,Nabiev Salavat R.,Matyushenko Alexander M.,Koubassova Natalia A.,Levitsky Dmitrii I.,Bershitsky Sergey Y.

Funder

Russian Foundation for Basic Research

State Program

Publisher

Springer Science and Business Media LLC

Subject

Cell Biology,Biochemistry,Physiology

Link

http://link.springer.com/content/pdf/10.1007/s10974-019-09560-8.pdf

Reference62 articles.

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2. Bai F, Groth HL, Kawai M (2012) DCM-related tropomyosin mutants E40K/E54K over-inhibit the actomyosin interaction and lead to a decrease in the number of cycling cross-bridges. PLoS ONE 7(10):e47471. https://doi.org/10.1371/journal.pone.0047471

3. Bai F, Wang L, Kawai M (2013) A study of tropomyosin’s role in cardiac function and disease using thin-filament reconstituted myocardium. J Muscle Res Cell Motil 34:295–310. https://doi.org/10.1007/s10974-013-9343-z

4. Barua B, Pamula MC, Hitchcock-DeGregori SE (2011) Evolutionarily conserved surface residues constitute actin binding sites of tropomyosin. Proc Natl Acad Sci USA 108:10150–10155. https://doi.org/10.1073/pnas.1101221108

5. Behrmann E, Müller M, Penczek PA, Mannherz HG, Manstein DJ, Raunser S (2012) Structure of the rigor actin-tropomyosin-myosin complex. Cell 150(2):327–338. https://doi.org/10.1016/j.cell.2012.05.037

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