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Updated: Jun 12, 2025

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry
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Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry

Published on: June 7, 2018

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对HSP27的O-GlcNAc修饰改变了其蛋白质相互作用,并通过BAG3/HSP70协伴蛋白促进了蛋白质的重新折叠

Afraah Javed1, Oleta T Johnson2, Aaron T Balana1

  • 1Department of Chemistry, University of Southern California, Los Angeles, California, USA.

Protein science : a publication of the Protein Society
|September 18, 2024
PubMed
概括

细胞压力增加了O-GlcNAc蛋白修饰,增强了细胞生存. 这项研究表明,O-GlcNAc在HSP27上改变了它的相互作用,改善了伴侣网络功能和蛋白质重新折叠.

关键词:
在O-GlcNAcc中,它是O-GlcNAc.聚合方式 聚合方式 聚合方式热冲击蛋白质是一种热冲击蛋白质.重复折叠重新折叠的情况

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