Phosphorylation Regulates the ADP-Induced Rotation of the Light Chain Domain of Smooth Muscle Myosin-Reference-Cited by-同舟云学术

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

Published:1999-07-10 Issue:31 Volume:38 Page:10107-10118
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Gollub Jeremy¹,Cremo Christine R.¹,Cooke Roger¹

Affiliation:

1. Graduate Group in Biophysics, Department of Biochemistry and Biophysics, and Cardiovascular Research Institute, University of California, San Francisco, California 94143-0448, and Department of Biochemistry and Biophysics, Washington State University, Pullman, Washington 99164-4660

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi990267e

Reference55 articles.

1. Myosin isoforms in smooth muscle: how may they affect function and structure?

2. The apparently negatively cooperative phosphorylation of smooth muscle myosin at low ionic strength is related to its filamentous state.

3. Mechanism of the phosphorylation-dependent regulation of smooth muscle heavy meromyosin.

4. Regulation of cytoplasmic and smooth muscle myosin

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