Hsp70 chaperones: cellular functions and molecular mechanism.
Hsp70 chaperones: cellular functions and molecular mechanism.
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DOI：
10.1007/s00018-004-4464-6
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发表时间：
2005-03
影响因子：
8
通讯作者：
Bukau, B
中科院分区：
文献类型：
--
作者：
Mayer, MP;Bukau, B
Hsp 70蛋白是分子伴侣和折叠催化剂的细胞网络的中心组分。它们通过其底物结合结构域与其底物蛋白内的短疏水肽段的瞬时缔合来协助细胞中的多种蛋白质折叠过程。底物结合和释放循环由Hsp 70在低亲和力ATP结合状态和高亲和力ADP结合状态之间的切换驱动。因此，ATP结合和水解是必不可少的，在体外和体内的伴侣活性的Hsp 70蛋白。该ATP酶循环由J结构域蛋白家族的共分子伴侣和核苷酸交换因子控制，所述共分子伴侣将Hsp 70靶向其底物，所述核苷酸交换因子决定Hsp 70-底物复合物的寿命。额外的共同监护人微调这个监护人周期。对于特定的任务，Hsp 70循环与其他分子伴侣（如Hsp 90和Hsp 100）的作用相结合。
Hsp70 proteins are central components of the cellular network of molecular chaperones and folding catalysts. They assist a large variety of protein folding processes in the cell by transient association of their substrate binding domain with short hydrophobic peptide segments within their substrate proteins. The substrate binding and release cycle is driven by the switching of Hsp70 between the low-affinity ATP bound state and the high-affinity ADP bound state. Thus, ATP binding and hydrolysis are essential in vitro and in vivo for the chaperone activity of Hsp70 proteins. This ATPase cycle is controlled by co-chaperones of the family of J-domain proteins, which target Hsp70s to their substrates, and by nucleotide exchange factors, which determine the lifetime of the Hsp70-substrate complex. Additional co-chaperones fine-tune this chaperone cycle. For specific tasks the Hsp70 cycle is coupled to the action of other chaperones, such as Hsp90 and Hsp100.
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影响因子：
11.4
作者：
Gamer, J;Multhaup, G;Bukau, B
通讯作者：
Bukau, B
影响因子：
2.9
作者：
Barouch, W;Prasad, K;Eisenberg, E
通讯作者：
Eisenberg, E
影响因子：
4.8
作者：
Buczynski, G;Slepenkov, SV;Witt, SN
通讯作者：
Witt, SN
影响因子：
56.9
作者：
FLYNN, GC;CHAPPELL, TG;ROTHMAN, JE
通讯作者：
ROTHMAN, JE
DOI：
10.1073/pnas.152330499
发表时间：
2002-12-10
影响因子：
11.1
作者：
Bonini, NM
通讯作者：
Bonini, NM