Localization and characterization of a 7.3-kDa region of caldesmon which reversibly inhibits actomyosin ATPase activity.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference63 articles.
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4. Significances of Two Different Mr Caldesmons
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Cited by 17 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. The role of caldesmon in the regulation of endothelial cytoskeleton and migration;Journal of Cellular Physiology;2005
2. Influence of Ionic Strength, Actin State, and Caldesmon Construct Size on the Number of Actin Monomers in a Caldesmon Binding Site;Biochemistry;2003-05-01
3. Structure−Activity Studies of the Regulatory Interaction of the 10 Kilodalton C-Terminal Fragment of Caldesmon with Actin and the Effect of Mutation of Caldesmon Residues 691−696;Biochemistry;1998-02-01
4. Functional and Structural Relationship between the Calmodulin-binding, Actin-binding, and Actomyosin-ATPase Inhibitory Domains on the C Terminus of Smooth Muscle Caldesmon;Journal of Biological Chemistry;1997-07
5. The Inhibitory Complex of Smooth Muscle Caldesmon with Actin and Tropomyosin Involves Three Interacting Segments of the C-Terminal Domain 4;Biochemistry;1997-05-01
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