{
  "id": 18131012,
  "title": "Paired-probe chemoproteomic strategy enables global site-resolved quantification of lysine redox states",
  "url": "https://urgent.news/2026/11/04/paired-probe-chemoproteomic-strategy-enables-global-site-resolved",
  "topic": "science",
  "section": "Science",
  "published": "2026-11-04T00:00:00.000Z",
  "source": {
    "name": "bioRxiv",
    "slug": "biorxiv",
    "url": "https://www.biorxiv.org/content/10.64898/2026.11.03.764013v1?rss=1"
  },
  "original_language": "en",
  "account": "Researchers have developed a groundbreaking technique to precisely measure the redox states of lysine, an amino acid crucial for protein function, at a cellular level. Traditionally, scientists could only identify a few lysine modification sites without knowing their stoichiometry, or the ratio of different modifications. To overcome this limitation, a team of scientists created a quantitative chemoproteomic platform called PRISM-Lys.\n\nPRISM-Lys employs a unique paired-probe strategy using two complementary Am-alkyne and Ald-alkyne probes. These probes work together in identical reactions, generating the same chemical product, which enables selective enrichment of allysine, the oxidized form of lysine, and site-specific quantification of lysine redox states. This innovative approach allows for global, site-resolved analysis of lysine redox states across various biological samples, including cells and tissues.\n\nUsing PRISM-Lys, researchers observed that lysine oxidation events undergo bidirectional, site-selective remodeling during the process of ferroptosis, a type of cell death associated with iron accumulation and lipid peroxidation. By providing a new quantitative perspective on protein oxidation, PRISM-Lys opens up new avenues for investigating the role of lysine redox states in various biological systems and diseases.",
  "summary": "Site-specific quantification of lysine (Lys) redox states remains unexplored, as current approaches identify only a limited number of modification sites without determining their stoichiometry. Allysine, an oxidized form of Lys, provides a model posttranslational modification (PTM) for addressing this challenge by requiring selective enrichment and site-specific stoichiometric quantification.…",
  "key_points": [],
  "editors_take": null,
  "illustration": null,
  "coverage": {
    "outlets": 1,
    "also_reported_by": []
  },
  "ai_generated": true,
  "disclaimer": "Summaries, key points and the editor’s take are written by software from other outlets’ reporting and may contain errors — always check the linked original."
}