Ionic interaction of myosin loop 2 with residues located beyond the N-terminal part of actin probed by chemical cross-linking-Reference-Cited by-同舟云学术

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Ionic interaction of myosin loop 2 with residues located beyond the N-terminal part of actin probed by chemical cross-linking

Published:2008-02 Issue:2 Volume:1784 Page:285-291
ISSN:1570-9639
Container-title:Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

Author:

Pliszka Barbara,Martin Brian M.,Karczewska Emilia

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics,Analytical Chemistry

Reference40 articles.

1. Binding manner of actin to the lysine-rich sequence of myosin subfragment 1 in the presence and absence of ATP;Yamamoto;Biochemistry,1989

2. Mapping of actin-binding sites on the heavy chain of myosin;Sutoh;Biochemistry,1983

3. Structure of the actin–myosin interface;Mornet;Nature,1981

4. Structure of the 265-kilodalton complex formed upon EDC cross-linking of subfragment 1 to F-actin;Andreeva;Biochemistry,1993

5. Mechanism of formation of actomyosin interface;Andreev;J. Mol. Biol.,2007

Cited by 2 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. Regulation of the actin-activated MgATPase activity of Acanthamoeba myosin II by phosphorylation of serine 639 in motor domain loop 2;Proceedings of the National Academy of Sciences;2012-12-17

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

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