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Muheeb Beg

Researcher at Central Drug Research Institute

Publications -  21
Citations -  662

Muheeb Beg is an academic researcher from Central Drug Research Institute. The author has contributed to research in topics: Insulin resistance & Insulin. The author has an hindex of 14, co-authored 21 publications receiving 476 citations. Previous affiliations of Muheeb Beg include University of Gothenburg & Cornell University.

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Distinct Akt phosphorylation states are required for insulin regulated Glut4 and Glut1-mediated glucose uptake

TL;DR: In this article, it was shown that an intact hydrophobic motif domain is required for Glut4-mediated glucose uptake, whereas Glut1-dependent glucose uptake also requires mTORC2 phosphorylation of the HM domain.
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FOXK1 and FOXK2 regulate aerobic glycolysis.

TL;DR: It is shown that the closely related fasting/starvation-induced forkhead transcription factors FOXK1 and FOXK2 induce aerobic glycolysis by upregulating the enzymatic machinery required for this, while at the same time suppressing further oxidation of pyruvate in the mitochondria by increasing the activity of pyRuvate dehydrogenase kinases 1 and 4.
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Rohitukine inhibits in vitro adipogenesis arresting mitotic clonal expansion and improves dyslipidemia in vivo

TL;DR: The strategy to identify a novel antiadipogenic molecule using CFPMA successfully resulted in identification of rohitukine, which confirmed antiadendipogenic activity and also exhibited in vivo antidyslipidemic activity.
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Disruption of Adipose Rab10-Dependent Insulin Signaling Causes Hepatic Insulin Resistance

TL;DR: It is demonstrated that both insulin-stimulated glucose uptake and GLUT4 translocation to the plasma membrane are reduced by about half in adipocytes from adipose-specific Rab10 knockout (KO) mice, underscoring the physiological significance of the precise control of insulin-regulated trafficking in adipocyte trafficking.
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Downregulation of a GPCR by β-Arrestin2-Mediated Switch from an Endosomal to a TGN Recycling Pathway.

TL;DR: A coding sequence variant of GIPR, which has been associated with metabolic alterations, has altered post-activation trafficking characterized by enhanced downregulation and prolonged desensitization.