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Robert V. Farese
Researcher at Harvard University
Publications - 484
Citations - 54181
Robert V. Farese is an academic researcher from Harvard University. The author has contributed to research in topics: Insulin & Protein kinase C. The author has an hindex of 115, co-authored 473 publications receiving 48754 citations. Previous affiliations of Robert V. Farese include University of South Florida & University at Buffalo.
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Activation of the ERK Pathway and Atypical Protein Kinase C Isoforms in Exercise- and Aminoimidazole-4-carboxamide- 1-β-d-riboside (AICAR)-stimulated Glucose Transport
Hubert Chen,Gautam Bandyopadhyay,Mini P. Sajan,Yoshinori Kanoh,Mary L. Standaert,Robert V. Farese +5 more
TL;DR: The findings suggest that effects of exercise on glucose transport that are dependent on AMPK are mediated via PYK2, the ERK pathway, PLD, and aPKCs.
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The Problem of Establishing Relationships between Hepatic Steatosis and Hepatic Insulin Resistance
TL;DR: A perspective is provided by defining the problem and its challenges, analyzing the possible causative relationships, and drawing some conclusions about the relationship between liver disease and insulin resistance.
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Progranulin protects against amyloid β deposition and toxicity in Alzheimer's disease mouse models
S. Sakura Minami,Sang-Won Min,Grietje Krabbe,Chao Wang,Yungui Zhou,Rustam Asgarov,Yaqiao Li,Lauren Herl Martens,Lisa P Elia,Michael E. Ward,Lennart Mucke,Robert V. Farese,Li Gan +12 more
TL;DR: It is shown that PGRN inhibits amyloid β (Aβ) deposition and protected against Aβ toxicity and is proposed as a potential treatment for P GRN-deficient FTLD and AD.
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Luteinizing hormone increases inositol trisphosphate and cytosolic free Ca2+ in isolated bovine luteal cells.
TL;DR: It is demonstrated that LH can rapidly raise levels of IP3 and [Ca2+]i, as well as, cAMP in bovine luteal cells, and suggest that at least two second messenger systems exist to mediate the action of LH in the corpus luteum.
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MGAT2, a Monoacylglycerol Acyltransferase Expressed in the Small Intestine
TL;DR: The identification of homologous genes in humans and mice encoding MGAT2 will facilitate studies to determine the functional role of MGAT1 in fat absorption in the intestine and to determine whether blocking MGAT activity in enterocytes is a feasible approach to inhibit fat absorption and treat obesity.