Scholarlink

<p>Cysteine is one of the rarest amino acids yet exerts a profound influence on biology through the exceptional chemistry of its thiol group. Tunable acidity, high nucleophilicity and access to multiple oxidation states position cysteine as both a dominant cellular redox buffer and a privileged regulatory site. Chemoproteomics has revealed a vast, dynamic cysteine redoxome in which oxidative post-translational modifications act as sensors, switches and buffers across metabolism, signaling and stress responses, respectively. This study advances the following three frameworks: (1) separating intrinsic reactivity from redox sensitivity and regulatory function; (2) using probe chemistry to capture metastable intermediates with site-level precision; and (3) integrating ratiometric measurements with occupancy, exposure and flux to decode redox dynamics. Case studies show how ratiometric chemoproteomics resolves distinct oxoform kinetics, links enzymatic repair to function and exposes the cysteine redoxome as a dynamic regulatory layer and frontier for therapeutic targeting.</p><p></p>

错误：搜索内容不能为空，请输入英文关键词
错误：关键词超出字数限制，请精简
高级检索

Defining and refining the cysteine redoxome through sulfur chemical biology

  • 期刊论文

  • 发表日期：

    2026年2月27日

查看全文
  • Kate S. Carroll,
  • Jing Yang

摘要

Cysteine is one of the rarest amino acids yet exerts a profound influence on biology through the exceptional chemistry of its thiol group. Tunable acidity, high nucleophilicity and access to multiple oxidation states position cysteine as both a dominant cellular redox buffer and a privileged regulatory site. Chemoproteomics has revealed a vast, dynamic cysteine redoxome in which oxidative post-translational modifications act as sensors, switches and buffers across metabolism, signaling and stress responses, respectively. This study advances the following three frameworks: (1) separating intrinsic reactivity from redox sensitivity and regulatory function; (2) using probe chemistry to capture metastable intermediates with site-level precision; and (3) integrating ratiometric measurements with occupancy, exposure and flux to decode redox dynamics. Case studies show how ratiometric chemoproteomics resolves distinct oxoform kinetics, links enzymatic repair to function and exposes the cysteine redoxome as a dynamic regulatory layer and frontier for therapeutic targeting.