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在热休克反应的途径中:蛋白质硫醇修饰导致部分折叠的蛋白质中间体的不稳定化和形成。

On the path to the heat shock response: destabilization and formation of partially folded protein intermediates, a consequence of protein thiol modification.

作者信息

Freeman M L, Borrelli M J, Meredith M J, Lepock J R

机构信息

Department of Radiation Oncology, Vanderbilt Cancer Center, Vanderbilt University School of Medicine, Nashville, TN 37232, USA.

出版信息

Free Radic Biol Med. 1999 Mar;26(5-6):737-45. doi: 10.1016/s0891-5849(98)00258-5.

Abstract

This review discusses the initial events that occur during oxidative stress that induce the synthesis of heat shock proteins. The focus is on non-native oxidation or modification of protein thiols and the destablization that can result. Proteins that contain non-native modified thiols can become destablized such that they unfold into molten globule-like intermediates at or below 37 degrees C, relieving Hsf-1 negative regulation, and inducing Hsp transcription.

摘要

本综述讨论了氧化应激期间发生的引发热休克蛋白合成的初始事件。重点是蛋白质硫醇的非天然氧化或修饰以及可能导致的稳定性破坏。含有非天然修饰硫醇的蛋白质可能会变得不稳定,以至于它们在37摄氏度或以下展开成类似熔球的中间体,解除热休克因子-1(Hsf-1)的负调控,并诱导热休克蛋白(Hsp)转录。

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