The effect of caldesmon on actin-myosin interaction in skeletal muscle fibers
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics,Structural Biology
Reference44 articles.
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4. Internal Motion of F-Actin in 10−6–10−3s Time Range Studied by Transient Absorption Anisotropy: Detection of Torsional Motion
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1. The Effect of the Arg91Gly and Glu139del Mutations in β-Tropomyosin Associated with Congenital Myopathy of Human Skeletal Muscles on Actin–Myosin Interaction;Cell and Tissue Biology;2018-05
2. Caldesmon inhibits the rotation of smooth actin subdomain-1 and alters its mobility during the ATP hydrolysis cycle;Biochemical and Biophysical Research Communications;2009-12
3. Caldesmon inhibits the actin–myosin interaction by changing its spatial orientation and mobility during the ATPase activity cycle;Biochemical and Biophysical Research Communications;2007-06
4. Caldesmon freezes the structure of actin filaments during the actomyosin ATPase cycle;Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics;2006-06
5. Proteolytic cleavage of actin within the DNase-I-binding loop changes the conformation of F-actin and its sensitivity to myosin binding;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;2000-03
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