D
D. Grahame Hardie
Researcher at University of Dundee
Publications - 287
Citations - 59393
D. Grahame Hardie is an academic researcher from University of Dundee. The author has contributed to research in topics: AMPK & Protein kinase A. The author has an hindex of 109, co-authored 276 publications receiving 53856 citations. Previous affiliations of D. Grahame Hardie include University of Glasgow & Newcastle University.
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AMPK: a nutrient and energy sensor that maintains energy homeostasis
TL;DR: AMP-activated protein kinase conserves ATP levels through the regulation of processes other than metabolism, such as the cell cycle and neuronal membrane excitability.
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AMP-activated protein kinase: Ancient energy gauge provides clues to modern understanding of metabolism
TL;DR: Through signaling, metabolic, and gene expression effects, AMPK enhances insulin sensitivity and fosters a metabolic milieu that may reduce the risk for obesity and type 2 diabetes.
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AMP-activated/SNF1 protein kinases: conserved guardians of cellular energy.
TL;DR: Surprisingly, recent results indicate that the AMPK system is also important in functions that go beyond the regulation of energy homeostasis, such as the maintenance of cell polarity in epithelial cells.
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Complexes between the LKB1 tumor suppressor, STRADα/β and MO25α/β are upstream kinases in the AMP-activated protein kinase cascade
Simon A. Hawley,Jérôme Boudeau,Jennifer L Reid,Kirsty J. Mustard,Lina Udd,Tomi P. Mäkelä,Dario R. Alessi,D. Grahame Hardie +7 more
TL;DR: These results provide the first description of a physiological substrate for the LKB1 tumor suppressor and suggest that it functions as an upstream regulator of AMPK.
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Calmodulin-dependent protein kinase kinase-β is an alternative upstream kinase for AMP-activated protein kinase
Simon A. Hawley,David A. Pan,Kirsty J. Mustard,Louise Ross,Jenny Bain,Arthur M. Edelman,Bruno G. Frenguelli,D. Grahame Hardie +7 more
TL;DR: It is reported that there is a significant basal activity and phosphorylation of AMPK in LKB1-deficient cells that can be stimulated by Ca2+ ionophores, and studies using the CaMKK inhibitor STO-609 and isoform-specific siRNAs show thatCaMKKbeta is required for this effect.