标题
Pathways of allosteric regulation in Hsp70 chaperones
作者
关键词
-
出版物
Nature Communications
Volume 6, Issue 1, Pages -
出版商
Springer Nature
发表日期
2015-09-18
DOI
10.1038/ncomms9308
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。- Substrate-binding domain conformational dynamics mediate Hsp70 allostery
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- Hsp70 chaperones are non-equilibrium machines that achieve ultra-affinity by energy consumption
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- Allosteric opening of the polypeptide-binding site when an Hsp70 binds ATP
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- The Four Hydrophobic Residues on the Hsp70 Inter-Domain Linker Have Two Distinct Roles
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- Allosteric signal transmission in the nucleotide-binding domain of 70-kDa heat shock protein (Hsp70) molecular chaperones
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- The Conformational Dynamics of the Mitochondrial Hsp70 Chaperone
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- The HSP70 chaperone machinery: J proteins as drivers of functional specificity
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- Allostery in Hsp70 Chaperones Is Transduced by Subdomain Rotations
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