Structural transitions modulate the chaperone activities of Grp94

IF 11.6 1区生物学 Q1 BIOCHEMISTRY & MOLECULAR BIOLOGY

Trends in Biochemical Sciences Pub Date : 2024-09-01 DOI:10.1016/j.tibs.2024.06.007

引用次数: 0

Abstract

A recent study by Amankwah et al. reports how co-chaperone proteins and ATP hydrolysis fine-tune the function of endoplasmic reticulum (ER)-resident Hsp90 paralog Grp94.

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结构转变调节了 Grp94 的伴侣活性。

Amankwah 等人最近的一项研究报告了共伴侣蛋白和 ATP 水解如何微调内质网（ER）驻留 Hsp90 旁系亲属 Grp94 的功能。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

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来源期刊

Trends in Biochemical Sciences 生物-生化与分子生物学

CiteScore

22.90

自引率

0.70%

发文量

148

审稿时长

6-12 weeks

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