Trapping the ATP binding state leads to a detailed understanding of the F1-ATPase mechanism
出版年份 2014 全文链接
标题
Trapping the ATP binding state leads to a detailed understanding of the F1-ATPase mechanism
作者
关键词
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出版物
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 111, Issue 50, Pages 17851-17856
出版商
Proceedings of the National Academy of Sciences
发表日期
2014-12-02
DOI
10.1073/pnas.1419486111
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。- Rotation Triggers Nucleotide-Independent Conformational Transition of the Empty β Subunit of F1-ATPase
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- The ATP synthase: the understood, the uncertain and the unknown
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- Phosphate release coupled to rotary motion of F1-ATPase
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- Structural evidence of a new catalytic intermediate in the pathway of ATP hydrolysis by F1-ATPase from bovine heart mitochondria
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- Mechanical modulation of catalytic power on F1-ATPase
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- Chemo-Mechanical Coupling in F1-ATPase Revealed by Catalytic Site Occupancy during Catalysis
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- Phosphate release in F1-ATPase catalytic cycle follows ADP release
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- CHARMM: The biomolecular simulation program
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- Torque generation and elastic power transmission in the rotary FOF1-ATPase
- (2009) Wolfgang Junge et al. NATURE
- Cooperative three-step motions in catalytic subunits of F1-ATPase correlate with 80° and 40° substep rotations
- (2008) Tomoko Masaike et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- Correlation between the conformational states of F1-ATPase as determined from its crystal structure and single-molecule rotation
- (2008) D. Okuno et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- How subunit coupling produces the -subunit rotary motion in F1-ATPase
- (2008) J. Pu et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
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