{
  "abstract": "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. Here, we developed a quantitative chemoproteomic platform for paired redox-state isotopic stoichiometry mapping of lysine, termed PRISM-Lys. We used an Am-alkyne probe for allysine enrichment by reductive amination and developed a complementary Ald-alkyne probe to label Lys, with identical reactions generating the same chemical product. Coupling this paired-probe strategy with a quantitative chemoproteomic workflow enables global site-resolved quantification and stoichiometric analysis of Lys redox states across cells and tissues. Applied to ferroptosis, PRISM-Lys revealed bidirectional, site-selective remodeling of Lys oxidation events associated with ferroptotic progression. Together, PRISM-Lys establishes a paired-chemistry framework for global, site-resolved quantification of Lys redox states, providing a new quantitative perspective for investigating protein oxidation in biological systems.",
  "abstract_shown": true,
  "affiliations": [
    "Sylvester Comprehensive Cancer Center. University of Miami Miller School of Medicine"
  ],
  "article_type": "New results",
  "arxiv": null,
  "author_total": 8,
  "authors": [
    {
      "name": "Y.-F. Zhou"
    },
    {
      "name": "L. Zhang"
    },
    {
      "name": "D. M. N. Udayanga"
    },
    {
      "name": "X. A. WANG"
    },
    {
      "name": "H. Bakbak"
    },
    {
      "name": "H. N. Shah"
    },
    {
      "name": "N. Sharifi"
    },
    {
      "affs": [
        0
      ],
      "name": "Z. A. Wang"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/32khdg0re62jn.bib",
  "cited_by": 0,
  "doi": "10.64898/2026.11.03.764013",
  "fulltext_url": "https://www.biorxiv.org/content/10.64898/2026.11.03.764013v1.full",
  "id": "32khdg0re62jn",
  "issns": [],
  "landing_url": "https://www.biorxiv.org/content/10.64898/2026.11.03.764013v1",
  "language": null,
  "licence": "CC-BY-NC-ND",
  "licence_label": "CC BY-NC-ND",
  "licence_source": "article",
  "licence_url": "https://creativecommons.org/licenses/by-nc-nd/4.0/",
  "metadata_licence": null,
  "native_subjects": [
    [
      "biorxiv",
      "biochemistry"
    ]
  ],
  "openalex": null,
  "pdf_url": "https://www.biorxiv.org/content/10.64898/2026.11.03.764013v1.full.pdf",
  "pmcid": null,
  "pmid": null,
  "published": "2026-11-03",
  "publisher": null,
  "ris": "https://research.draconitic.com/paper/32khdg0re62jn.ris",
  "sources": [
    {
      "first_seen": "2026-11-05T00:21:36Z",
      "native_id": "10.64898/2026.11.03.764013",
      "source": "biorxiv",
      "url": "https://www.biorxiv.org/content/10.64898/2026.11.03.764013v1"
    }
  ],
  "subjects": [
    {
      "field": "biochemistry",
      "origin": "biorxiv:biochemistry",
      "subfield": "general"
    }
  ],
  "title": "Paired-probe chemoproteomic strategy enables global site-resolved quantification of lysine redox states",
  "title_text": "Paired-probe chemoproteomic strategy enables global site-resolved quantification of lysine redox states",
  "type": "preprint",
  "updated_at": "2026-11-06T00:21:25Z",
  "url": "https://research.draconitic.com/paper/32khdg0re62jn",
  "venue": "bioRxiv",
  "versions": []
}