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Showing 1–4 of 4 results
Advanced filters: Author: Kevin R. W. Ngoei Clear advanced filters

  • AMPK regulates the metabolism and so drugs that activate AMPK might have potential for the treatment of metabolic disease. Here, the authors report the structure of AMPK bound to an activating compound, revealing two binding sites and indicating that dual therapy might be a good drug strategy.

    • Christopher G. Langendorf
    • Kevin R. W. Ngoei
    • Bruce E. Kemp
    ResearchOpen Access
    Nature Communications
    Volume: 7, P: 1-8

  • AMPK is involved in sensing of metabolic stress. The authors show that the autophagy initiator ULK1 phosphorylates β1-Ser108 on the regulatory β1-subunit, sensitizing AMPK to allosteric drugs, and activates signaling pathways that appear independent of Thr172 phosphorylation in the kinase activation loop.

    • Toby A. Dite
    • Naomi X. Y. Ling
    • Jonathan S. Oakhill
    ResearchOpen Access
    Nature Communications
    Volume: 8, P: 1-14

  • Steinberg and colleagues show that long-chain fatty acyl-CoA esters are endogenous ligands for the drug-binding domain of AMPK β1–containing isoforms, and that such binding is critical for enhancement of fatty acid oxidation. These data may help explain how AMPK integrates responses to ketogenic diets, fasting or endurance exercise across distinct tissues in the absence of changes in adenine nucleotides.

    • Stephen L. Pinkosky
    • John W. Scott
    • Gregory R. Steinberg
    Research
    Nature Metabolism
    Volume: 2, P: 873-881