Replacement of Lys-75 of calmodulin affects its interaction with smooth muscle caldesmon-Reference-Cited by-同舟云学术

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Replacement of Lys-75 of calmodulin affects its interaction with smooth muscle caldesmon

Published:2001-01 Issue:1-2 Volume:1544 Page:143-150
ISSN:0167-4838
Container-title:Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology

Author:

Medvedeva Marina V.,Djemuchadze David R.,Watterson D.Martin,Marston Steven B.,Gusev Nikolai B.

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics,Structural Biology

Reference41 articles.

1. S.B. Marston and P.A. Huber (1996) in: M. Barany (Ed.), Biochemistry of Smooth Muscle Contraction, Academic Press, San Diego, CA, 1996, pp. 77–90.

2. Caldesmon, a novel regulatory protein in smooth muscle and nonmuscle actomyosin systems

3. Utilization of troponin C as a model calcium-binding protein for mapping of the calmodulin-binding sites of caldesmon

4. Interaction of isoforms of S100 protein with smooth muscle caldesmon

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. References;Calcium Binding Proteins;2010-11-04

2. Some properties of caldesmon and calponin and the participation of these proteins in regulation of smooth muscle contraction and cytoskeleton formation;Biochemistry (Moscow);2001

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