标题
Molecular Mechanics of Cardiac Myosin-Binding Protein C in Native Thick Filaments
作者
关键词
-
出版物
SCIENCE
Volume 337, Issue 6099, Pages 1215-1218
出版商
American Association for the Advancement of Science (AAAS)
发表日期
2012-08-25
DOI
10.1126/science.1223602
参考文献
相关参考文献
注意:仅列出部分参考文献,下载原文获取全部文献信息。- Mechanical Unfolding of Cardiac Myosin Binding Protein-C by Atomic Force Microscopy
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- Structure and Interactions of Myosin-binding Protein C Domain C0
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- Unique single molecule binding of cardiac myosin binding protein-C to actin and phosphorylation-dependent inhibition of actomyosin motility requires 17 amino acids of the motif domain
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- Electron Microscopy and 3D Reconstruction of F-Actin Decorated with Cardiac Myosin-Binding Protein C (cMyBP-C)
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- Nonlinear Elasticity and an 8-nm Working Stroke of Single Myosin Molecules in Myofilaments
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- Cardiac Myosin Binding Protein-C Phosphorylation in a β-Myosin Heavy Chain Background
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- Acceleration of Crossbridge Kinetics by Protein Kinase A Phosphorylation of Cardiac Myosin Binding Protein C Modulates Cardiac Function
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- Myosin binding protein C phosphorylation in normal, hypertrophic and failing human heart muscle
- (2008) Adam M. Jacques et al. JOURNAL OF MOLECULAR AND CELLULAR CARDIOLOGY
- Understanding the Organisation and Role of Myosin Binding Protein C in Normal Striated Muscle by Comparison with MyBP-C Knockout Cardiac Muscle
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- Three-dimensional structure of vertebrate cardiac muscle myosin filaments
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