Functional outcomes of structural peculiarities of striated muscle tropomyosin
Author:
Funder
Russian Foundation for Basic Research
Publisher
Springer Science and Business Media LLC
Subject
Cell Biology,Biochemistry,Physiology
Link
http://link.springer.com/content/pdf/10.1007/s10974-019-09552-8.pdf
Reference121 articles.
1. Akkari PA, Song Y, Hitchcock-DeGregori S, Blechynden L, Laing N (2002) Expression and biological activity of Baculovirus generated wild-type human slow alpha tropomyosin and the Met9Arg mutant responsible for a dominant form of nemaline myopathy. Biochem Biophys Res Commun 296:300–304. https://doi.org/10.1016/s0006-291x(02)00852-5
2. Avner BS, Shioura KM, Scruggs SB, Grachoff M, Geenen DL, Helseth DL Jr, Farjah M, Goldspink PH, Solaro RJ (2012) Myocardial infarction in mice alters sarcomeric function via post-translational protein modification. Mol Cell Biochem 363:203–215. https://doi.org/10.1007/s11010-011-1172-z
3. Barua B, Fagnant PM, Winkelmann DA, Trybus KM, Hitchcock-DeGregori SE (2013) A periodic pattern of evolutionarily conserved basic and acidic residues constitutes the binding Interface of actin-tropomyosin. J Biol Chem 288:9602–9609. https://doi.org/10.1074/jbc.m113.451161
4. Behrmann E, Muller M, Penczek PA, Mannherz HG, Manstein DJ, Raunser S (2012) Structure of the rigor actin–tropomyosin–myosin complex. Cell 150:327–338. https://doi.org/10.1016/j.cell.2012.05.037
5. Bershitsky SY, Logvinova DS, Shchepkin DV, Kopylova GV, Matyushenko AM (2019) Myopathic mutations in the β-chain of tropomyosin differently affect the structural and functional properties of ββ- and αβ-dimers. FASEB J 33:1963–1971. https://doi.org/10.1096/fj.201800755R
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