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Quantification of Protein Sulfenic Acid Modifications Using Isotope-Coded Dimedone and Iododimedone

Authors

  • Dr. Young Ho Seo,

    1. Department of Pharmaceutical Sciences, University of Michigan, Ann Arbor, MI 49109 (USA)
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  • Dr. Kate S. Carroll

    Corresponding author
    1. Department of Chemistry, The Scripps Research Institute, 130 Scripps Way, Jupiter, FL 33458 (USA), Fax: (+1) 561-228-2919
    • Department of Chemistry, The Scripps Research Institute, 130 Scripps Way, Jupiter, FL 33458 (USA), Fax: (+1) 561-228-2919
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  • The authors acknowledge funding from the Camile Henry Dreyfus Teacher Scholar Award (to K.S.C.) and the American Heart Association Scientist Development Award (0835419N to K.S.C.). The authors also gratefully acknowledge helpful discussions with Profs. U. Jakob and G. Micalizio.

Abstract

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Quantitative proteomics: The new technique mentioned in the title—in short, ICDID—enables quantification of sulfenic acid modifications in proteins (see picture). The approach permits S-hydroxylation site occupancy to be monitored at individual cysteines within a single protein and is compatible with peptide-based proteomic strategies.

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