Allosteric regulation by cooperative conformational changes of actin filaments drives mutually exclusive binding with cofilin and myosin-Reference-Cited by-同舟云学术

Allosteric regulation by cooperative conformational changes of actin filaments drives mutually exclusive binding with cofilin and myosin

Published:2016-10-20 Issue:1 Volume:6 Page:
ISSN:2045-2322
Container-title:Scientific Reports
language:en
Short-container-title:Sci Rep

Author:

Ngo Kien Xuan,Umeki Nobuhisa,Kijima Saku T.,Kodera Noriyuki,Ueno Hiroaki,Furutani-Umezu Nozomi,Nakajima Jun,Noguchi Taro Q. P.,Nagasaki Akira,Tokuraku Kiyotaka,Uyeda Taro Q. P.

Publisher

Springer Science and Business Media LLC

Subject

Multidisciplinary

Link

http://www.nature.com/articles/srep35449.pdf

Reference64 articles.

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2. Miki, M., Wahl, P. & Auchet, J. C. Fluorescence anisotropy of labeled F-actin: influence of divalent cations on the interaction between F-actin and myosin heads. Biochemistry 21, 3661–3665, doi: 10.1021/bi00258a021 (1982).

3. Loscalzo, J., Reed, G. H. & Weber, A. Conformational change and cooperativity in actin filaments free of tropomyosin. Proc Natl Acad Sci USA 72, 3412–3415, doi: 10.1073/pnas.72.9.3412 (1975).

4. Galkin, V. E., Orlova, A., Lukoyanova, N., Wriggers, W. & Egelman, E. H. Actin depolymerizing factor stabilizes an existing state of F-actin and can change the tilt of F-actin subunits. J. Cell Biol. 153, 75–86, doi: 10.1083/jcb.153.1.75 (2001).

5. McGough, A., Pope, B., Chiu, W. & Weeds, A. Cofilin changes the twist of F-actin: implications for actin filament dynamics and cellular function. J. Cell Biol. 138, 771–781, doi: 10.1083/jcb.138.4.771 (1997).

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