新的雷诺丁受体压力测试

IF 3.3 2区 医学 Q1 PHYSIOLOGY Journal of General Physiology Pub Date : 2024-12-02 Epub Date: 2024-11-19 DOI:10.1085/jgp.202413716
Ben Short
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引用次数: 0

摘要

JGP 研究(Steinz 等人,https://doi.org/10.1085/jgp.202313515)揭示,氧化应激可诱导 RyR1 发生稳定的翻译后修饰,增加通道的开放概率,从而破坏肌肉收缩能力。
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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A new stress test for ryanodine receptors.

JGP study (Steinz et al. https://doi.org/10.1085/jgp.202313515) reveals that oxidative stress can induce stable posttranslational modifications of RyR1 that increase the channel's open probability and could therefore disrupt muscle contractility.

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来源期刊
CiteScore
6.00
自引率
10.50%
发文量
88
审稿时长
6-12 weeks
期刊介绍: General physiology is the study of biological mechanisms through analytical investigations, which decipher the molecular and cellular mechanisms underlying biological function at all levels of organization. The mission of Journal of General Physiology (JGP) is to publish mechanistic and quantitative molecular and cellular physiology of the highest quality, to provide a best-in-class author experience, and to nurture future generations of independent researchers. The major emphasis is on physiological problems at the cellular and molecular level.
期刊最新文献
Functional role of myosin-binding protein H in thick filaments of developing vertebrate fast-twitch skeletal muscle. Mechanism of acid-sensing ion channel modulation by Hi1a. Myosin-binding protein-H: Not just filler. Piezo2 interacts with E-cadherin in specialized gastrointestinal epithelial mechanoreceptors. Stable oxidative posttranslational modifications alter the gating properties of RyR1.
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