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Michael F. Hirshman

Researcher at Harvard University

Publications -  143
Citations -  22282

Michael F. Hirshman is an academic researcher from Harvard University. The author has contributed to research in topics: Skeletal muscle & Glucose uptake. The author has an hindex of 65, co-authored 131 publications receiving 20279 citations. Previous affiliations of Michael F. Hirshman include Merck & Co. & Joslin Diabetes Center.

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Overexpression of TRB3 in muscle alters muscle fiber type and improves exercise capacity in mice

TL;DR: The findings suggest that TRB3 regulates muscle fiber type via a peroxisome proliferator-activated receptor-α (PPAR-α)-regulated miR499/miR208b pathway, revealing a novel function for TRB 3 in the regulation of skeletal muscle fibertype and exercise capacity.
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Dissociation of AMP-activated protein kinase and p38 mitogen-activated protein kinase signaling in skeletal muscle.

TL;DR: In this article, the p38 mitogen-activated protein kinase (MAPK) has been proposed to be a downstream intermediate of AMPK-mediated signaling in skeletal muscle, but it was shown that p38 MAPK is not a downstream component of AMP-mediated signalling.
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Islet transplantation restores normal levels of insulin receptor and substrate tyrosine phosphorylation and phosphatidylinositol 3-kinase activity in skeletal muscle and myocardium of streptozocin-induced diabetic rats.

TL;DR: Islet transplantation fully corrected the diabetes-induced changes in protein tyrosine phosphorylation and PI 3-kinase activity and normalized IRS-1 and IRS-2 protein content in both skeletal muscle and myocardium, suggesting that insulin delivered into the systemic circulation by pancreatic islets transplanted under the kidney capsule can adequately correct altered insulin signaling mechanisms in insulinopenic diabetes.
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Chronic growth hormone treatment in normal rats reduces post-prandial skeletal muscle plasma membrane GLUT1 content, but not glucose transport or GLUT4 expression and localization.

TL;DR: High-dose hGH treatment for 4 weeks did not alter post-prandial skeletal muscle glucose transport activity and mRNA data suggest that this reduction might result from a decrease in the synthesis of GLUT1.