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hsp90 结构与作用机制研究的新进展

Recent Advances in the Study of hsp90 Structure and Mechanism of Action.

机构信息

Department of Biochemistry and Molecular Biology, Mayo Clinic, 200 First Street Southwest, Rochester, MN 55905, USA.

出版信息

Trends Endocrinol Metab. 1998 Aug;9(6):238-43. doi: 10.1016/s1043-2760(98)00060-5.

Abstract

The 90kDa heat shock protein, hsp90, is a major molecular chaperone of the cell that appears to have particular significance to cellular regulatory processes. New tools and approaches have revealed a number of target proteins for hsp90, most of which are protein kinases or transcription factors. While the mechanism of action of hsp90 is not well understood, reasonable models have emerged describing some functional domains of this protein, the importance of conformational transitions for its activity and its role within a multi-component chaperoning pathway of the cell.

摘要

90kDa 热休克蛋白(hsp90)是细胞内的一种主要分子伴侣,它似乎对细胞调节过程具有特殊意义。新的工具和方法揭示了 hsp90 的许多靶蛋白,其中大多数是蛋白激酶或转录因子。虽然 hsp90 的作用机制尚不清楚,但已经出现了一些合理的模型,描述了该蛋白的一些功能域、构象转变对其活性的重要性以及它在细胞多组分伴侣途径中的作用。

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