The importance of C-terminal amino acid residues of actin to the inhibition of actomyosin ATPase activity by caldesmon and troponin I
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(92)80546-S/fullpdf
Reference33 articles.
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2. R. Dąbrowska A. Kotyk J. Skoda V. Paces V. Kosika Highlights of Modern biochemistry 2 1989 VSP Int Amsterdam 1011 1020
3. Thin Filament Proteins and Thin Filament-Linked Regulation of Vertebrate Muscle Contractio
4. Structural Aspects of Troponin-Tropomyosin Regulation of Skeletal Muscle Contraction
5. Structural study of gizzard caldesmon and its interaction with actin. Binding involves residues of actin also recognised by myosin subfragment 1
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1. Role of Actin C-Terminus in Regulation of Striated Muscle Thin Filament;Biophysical Journal;2008-02
2. Structural Basis for Ca2+-regulated Muscle Relaxation at Interaction Sites of Troponin with Actin and Tropomyosin;Journal of Molecular Biology;2005-09
3. Stage-specific expression of two actin genes in the yellow fever mosquito, Aedes aegypti;Insect Molecular Biology;2004-06
4. Calcium-Induced Changes in the Location and Conformation of Troponin in Skeletal Muscle Thin Filaments;Journal of Biochemistry;1999-07-01
5. Interaction of caldesmon with actin subdomain-2;European Journal of Biochemistry;1998-06-15
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