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Showing 1–4 of 4 results
Advanced filters: Author: "Wolfgang Peti" Clear advanced filters

  • Protein phosphatase specificity is usually achieved via interaction with regulatory partners, which can control their subcellular localization and/or enzymatic specificity. Now structural and functional work on spinophilin reveals its extensive interactions with PP1, which differentially restrict the phosphatase's ability to bind different substrates.

    • Michael J Ragusa
    • Barbara Dancheck
    • Wolfgang Peti
    Research
    Nature Structural & Molecular Biology
    Volume: 17, P: 459-464

  • NMR and ITC are used to define essential features of a p38α phosphatase interface that extend beyond the classic KIM binding site, and SAXS analysis software, incorporating NMR chemical shift data, are developed and applied to build a model of the p38α-HePTP complex.

    • Dana M Francis
    • Bartosz Różycki
    • Wolfgang Peti
    Research
    Nature Chemical Biology
    Volume: 7, P: 916-924

  • The Doc-Phd pair forms a bacterial toxin-antitoxin system, but the mechanism by which the Fic-family member Doc causes toxicity is not fully defined. New research shows that Doc unexpectedly functions as a kinase to phosphorylate elongation factor TU, thus inhibiting translation and leading to Doc-mediated growth arrest.

    • Wolfgang Peti
    • Rebecca Page
    News & Views
    Nature Chemical Biology
    Volume: 9, P: 756-757