Interaction of Alkali Light Chain 1 with the Isolated 20-Kilodalton Fragment of Myosin Subfragment-1 Heavy Chain and F-Actin
Author:
Publisher
Oxford University Press (OUP)
Subject
Molecular Biology,Biochemistry,General Medicine
Link
http://academic.oup.com/jb/article-pdf/103/4/633/2334928/103-4-633.pdf
Cited by 8 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. Cleavage points of rabbit skeletal myosin light chains selectively modified in situ by limited proteolysis: structural characteristics of the neoformed isozymes;FEBS Letters;1995-08-07
2. The proteolytic susceptibility of specific sites in myosin light chains is modulated by the filament conformation;European Journal of Biochemistry;1993-08
3. Refined conditions for selective modifications of rabbit skeletal myosin light chains;Biochimie;1992-12
4. Inhibition of actomyosin subfragment 1 ATPase activity by analog peptides of the actin-binding site around the Cys(SH1) of myosin heavy chain.;Journal of Biological Chemistry;1990-03
5. Alkali light chains are involved in stabilization of myosin head;International Journal of Biochemistry;1990-01
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