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Showing 1–3 of 3 results
Advanced filters: Author: Mark R. Ambroso Clear advanced filters

  • Lysine acetylation regulates the function of soluble proteins in vivo, yet it remains largely unexplored whether lysine acetylation regulates the function of membrane proteins. Here, the authors map lysine acetylation predominantly in membrane-interaction regions in peripheral membrane proteins and show with three candidate proteins how lysine acetylation is a regulator of membrane protein function.

    • Alan K. Okada
    • Kazuki Teranishi
    • Ralf Langen
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-12

  • O-linked N-acetyl-glucosamine (O-GlcNAc) has been identified as an endogenous modification of α-synuclein; however, its effect on the properties of the protein is unclear. Now, recombinant protein and synthetic peptides have been combined to produce both unmodified and site-specifically O-GlcNAc-modified α-synuclein. The O-GlcNAc modification at threonine 72 was shown to inhibit the aggregation and associated toxicity of α-synuclein.

    • Nicholas P. Marotta
    • Yu Hsuan Lin
    • Matthew R. Pratt
    Research
    Nature Chemistry
    Volume: 7, P: 913-920