Broad disorder and the allosteric mechanism of myosin II regulation by phosphorylation-Reference-Cited by-同舟云学术

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Broad disorder and the allosteric mechanism of myosin II regulation by phosphorylation

Published:2011-05-02 Issue:20 Volume:108 Page:8218-8223
ISSN:0027-8424
Container-title:Proceedings of the National Academy of Sciences
language:en
Short-container-title:Proceedings of the National Academy of Sciences

Author:

Vileno B.,Chamoun J.,Liang H.,Brewer P.,Haldeman B. D.,Facemyer K. C.,Salzameda B.,Song L.,Li H.-C.,Cremo C. R.,Fajer P. G.

Publisher

Proceedings of the National Academy of Sciences

Subject

Multidisciplinary

Reference31 articles.

1. The Mechanism of Regulation of Smooth Muscle Myosin by Phosphorylation

2. Regulation of Asymmetric Smooth Muscle Myosin II Molecules

3. A 35-Å movement of smooth muscle myosin on ADP release

4. Phosphorylation Regulates the ADP-Induced Rotation of the Light Chain Domain of Smooth Muscle Myosin

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2. Impact of regulatory light chain mutation K104E on the ATPase and motor properties of cardiac myosin;Journal of General Physiology;2021-04-23

3. Going the dHis-tance: Site-Directed Cu2+ Labeling of Proteins and Nucleic Acids;Accounts of Chemical Research;2021-01-21

4. Hybrid methods for combined experimental and computational determination of protein structure;The Journal of Chemical Physics;2020-12-28

5. Myosin lever arm orientation in muscle determined with high angular resolution using bifunctional spin labels;Journal of General Physiology;2019-06-21

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