标题
Review: Mechanochemistry of the kinesin-1 ATPase
作者
关键词
-
出版物
BIOPOLYMERS
Volume 105, Issue 8, Pages 476-482
出版商
Wiley
发表日期
2016-04-28
DOI
10.1002/bip.22862
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。- Direct observation of intermediate states during the stepping motion of kinesin-1
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- Reversal of axonal growth defects in an extraocular fibrosis model by engineering the kinesin–microtubule interface
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- The structure of apo-kinesin bound to tubulin links the nucleotide cycle to movement
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- High-resolution structures of kinesin on microtubules provide a basis for nucleotide-gated force-generation
- (2014) Zhiguo Shang et al. eLife
- Conserved mechanisms of microtubule-stimulated ADP release, ATP binding, and force generation in transport kinesins
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- A molecular motor finds its track
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- The kinesin-13 MCAK has an unconventional ATPase cycle adapted for microtubule depolymerization
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- The Structure of the Kinesin-1 Motor-Tail Complex Reveals the Mechanism of Autoinhibition
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- Key residues on microtubule responsible for activation of kinesin ATPase
- (2010) Seiichi Uchimura et al. EMBO JOURNAL
- ATP Hydrolysis in Eg5 Kinesin Involves a Catalytic Two-water Mechanism
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- Structural model for strain-dependent microtubule activation of Mg-ADP release from kinesin
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- Kinesin's cover-neck bundle folds forward to generate force
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