相关实验视频

Updated: Sep 13, 2025

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry
10:24

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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在Hsp90中化驱动的结构变化与病理功能的增加有关.

Tilottama Chatterjee1, Alfonso Taboada2,3,4, Isabelle E Logan1,5

  • 1Department of Biochemistry and Biophysics, Oregon State University, Corvallis, OR 97331, U.S.A.

The Biochemical journal
|July 30, 2025
PubMed
概括

蛋白质氨酸化改变了热冲击蛋白90 (Hsp90) 的结构和功能. 对Y33或Y56的特定位点化会导致明显的病理变化,影响细胞过程和疾病进展.

关键词:
热冲击蛋白90 (Hsp90) 是一种热冲击蛋白.过氧尼酸盐的过氧尼酸盐翻译后修改 (PTM) 是一种方法.反应性物种 (RNS) 是一种反应性物种.结构-功能的结构-功能.铁酸化氨酸的化

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