The application of targeted mass spectrometry-based strategies to the detection and localization of post-translational modifications.

Navin Chicooree, Richard D Unwin, John R Griffiths

    Research output: Contribution to journalArticlepeer-review

    Abstract

    This review describes some of the more interesting and imaginative ways in which mass spectrometry has been utilized to study a number of important post-translational modifications over the past two decades; from circa 1990 to 2013. A diverse range of modifications is covered, including citrullination, sulfation, hydroxylation and sumoylation. A summary of the biological role of each modification described, along with some brief mechanistic detail, is also included. Emphasis has been placed on strategies specifically aimed at detecting target modifications, as opposed to more serendipitous modification discovery approaches, which rely upon straightforward product ion scanning methods. The authors have intentionally excluded from this review both phosphorylation and glycosylation since these major modifications have been extensively reviewed elsewhere. © 2014 Wiley Periodicals, Inc. Mass Spec Rev.
    Original languageEnglish
    JournalMass spectrometry reviews
    DOIs
    Publication statusPublished - 15 Apr 2014

    Keywords

    • PTMs
    • acetylation
    • citrullination
    • hydroxylation
    • mass spectrometry
    • nitration
    • nitrosylation
    • sulfation
    • sumoylation
    • ubiquitination

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