Structure of the shutdown state of myosin-2-Reference-Cited by-同舟云学术

Structure of the shutdown state of myosin-2

Published:2020-12-02 Issue:7838 Volume:588 Page:515-520
ISSN:0028-0836
Container-title:Nature
language:en
Short-container-title:Nature

Author:

Scarff Charlotte A.^ORCID,Carrington Glenn^ORCID,Casas-Mao David,Chalovich Joseph M.^ORCID,Knight Peter J.^ORCID,Ranson Neil A.^ORCID,Peckham Michelle^ORCID

Publisher

Springer Science and Business Media LLC

Subject

Multidisciplinary

Link

http://www.nature.com/articles/s41586-020-2990-5.pdf

Reference62 articles.

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2. Cross, R. A., Cross, K. E. & Sobieszek, A. ATP-linked monomer–polymer equilibrium of smooth muscle myosin: the free folded monomer traps ADP.Pi. EMBO J. 5, 2637–2641 (1986).

3. McLachlan, A. D. & Karn, J. Periodic charge distributions in the myosin rod amino acid sequence match cross-bridge spacings in muscle. Nature 299, 226–231 (1982).

4. Craig, R., Smith, R. & Kendrick-Jones, J. Light-chain phosphorylation controls the conformation of vertebrate non-muscle and smooth muscle myosin molecules. Nature 302, 436–439 (1983).

5. Ikebe, M., Hartshorne, D. J. & Elzinga, M. Identification, phosphorylation, and dephosphorylation of a second site for myosin light chain kinase on the 20,000-dalton light chain of smooth muscle myosin. J. Biol. Chem. 261, 36–39 (1986).

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