Cleavage points of rabbit skeletal myosin light chains selectively modified in situ by limited proteolysis: structural characteristics of the neoformed isozymes
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(95)00743-S/fullpdf
Reference26 articles.
1. Separation of subfragment-1 isoenzymes from rabbit skeletal muscle myosin
2. Substructure of Myosin Subfragment-1 as Revealed by Digestion with Proteolytic Enzymes
3. Effect of DTNB light chain on the interaction of vertebrate skeletal myosin with actin
4. ‘Artificial’ Myosin Isozymes; Preparation and Characteristics
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2. What Limits the Velocity of Fast-skeletal Muscle Contraction in Mammals?;Journal of Molecular Biology;2006-01
3. Ca2+ binding to myosin regulatory light chain affects the conformation of the N-terminus of essential light chain and its binding to actin;Archives of Biochemistry and Biophysics;2003-09
4. Domain Motion between the Regulatory Light Chain and the Nucleotide Site in Skeletal Myosin;Journal of Structural Biology;1998-10
5. Dual effect of actin on the accessibility of myosin essential light chain A1 to papain cleavage;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;1998-03
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