Mutational Analysis of the Role of Hydrophobic Residues in the 338−348 Helix on Actin in Actomyosin Interactions-Reference-Cited by-同舟云学术

Mutational Analysis of the Role of Hydrophobic Residues in the 338−348 Helix on Actin in Actomyosin Interactions

Published:1996-01-01 Issue:12 Volume:35 Page:3670-3676
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Miller Carl J.¹,Doyle Tim C.¹,Bobkova Elena¹,Botstein David¹,Reisler Emil¹

Affiliation:

1. Department of Chemistry and Biochemistry and Molecular Biology Institute, University of California, Los Angeles, California 90095, and Department of Genetics, Stanford University School of Medicine, Stanford, California 94305-5120

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi952645v

Reference37 articles.

1. Characterization of yeast-expressed beta-actins, site-specifically mutated at the tumor-related residue Gly245

2. The actomyosin engine

Cited by 38 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Cryo-EM structures reveal specialization at the myosin VI-actin interface and a mechanism of force sensitivity;eLife;2017-12-04

2. G146V Mutation at the Hinge Region of Actin Reveals a Myosin Class-specific Requirement of Actin Conformations for Motility;Journal of Biological Chemistry;2012-07

3. Myosin Binding Surface on Actin Probed by Hydroxyl Radical Footprinting and Site-Directed Labels;Journal of Molecular Biology;2011-11

4. Push and Pull of Tropomyosin’s Opposite Effects on Myosin Attachment to Actin. A Chimeric Tropomyosin Host−Guest Study;Biochemistry;2010-12-02

5. A closer look at energy transduction in muscle;Proceedings of the National Academy of Sciences;2007-07-18