M
Michel L. Tremblay
Researcher at McGill University
Publications - 223
Citations - 18851
Michel L. Tremblay is an academic researcher from McGill University. The author has contributed to research in topics: Protein tyrosine phosphatase & Phosphorylation. The author has an hindex of 70, co-authored 215 publications receiving 17503 citations. Previous affiliations of Michel L. Tremblay include McGill University Health Centre & National Institutes of Health.
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Journal ArticleDOI
Increased insulin sensitivity and obesity resistance in mice lacking the protein tyrosine phosphatase-1B gene.
Mounib Elchebly,Paul Payette,Eva Michaliszyn,Wanda Cromlish,Susan Collins,Ailsa Lee Loy,Denis Normandin,Alan Cheng,Jean Himms-Hagen,Chi-Chung Chan,Chidambaram Ramachandran,Michael J. Gresser,Michel L. Tremblay,Brian P. Kennedy +13 more
TL;DR: In this article, the mouse homolog of the gene encoding PTP-1B yielded healthy mice that, in the fed state, had blood glucose concentrations that were slightly lower and concentrations of circulating insulin that were one-half those of their PTP−1B+/+ littermates.
Journal ArticleDOI
Targeted ablation of the 25-hydroxyvitamin D 1α-hydroxylase enzyme: Evidence for skeletal, reproductive, and immune dysfunction
Dibyendu K. Panda,Dengshun Miao,Michel L. Tremblay,Jacinthe Sirois,Riaz Farookhi,Geoffrey N. Hendy,David Goltzman +6 more
TL;DR: A critical role for the 1α(OH)ase enzyme is established in mineral and skeletal homeostasis as well as in female reproduction and also point to an important role in regulating immune function.
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The Ity/Lsh/Bcg locus: natural resistance to infection with intracellular parasites is abrogated by disruption of the Nramp1 gene.
Silvia M. Vidal,Michel L. Tremblay,Gregory R. Govoni,Susan A. Gauthier,Giovanna Sebastiani,Danielle Malo,Emil Skamene,Martin Olivier,Serge Jothy,Philippe Gros +9 more
TL;DR: Targeted disruption of Nramp1 has pleiotropic effects on natural resistance to infection with intracellular parasites, as it eliminated resistance to Mycobacterium bovis, Leishmania donovani, and lethal Salmonella typhimurium infection, establishing that Nramps1, Bcg, Lsh, and Ity are the same locus.
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Attenuation of Leptin Action and Regulation of Obesity by Protein Tyrosine Phosphatase 1B
Alan Cheng,Noriko Uetani,Paul Daniel Simoncic,Paul Daniel Simoncic,Vikas P. Chaubey,Ailsa Lee-Loy,C. Jane McGlade,Brian P. Kennedy,Michel L. Tremblay +8 more
TL;DR: It is suggested that PTP1B negatively regulates leptin signaling, and provide one mechanism by which it may regulate obesity.
Journal ArticleDOI
TYK2 and JAK2 Are Substrates of Protein-tyrosine Phosphatase 1B
Michael P. Myers,Jannik N. Andersen,Alan Cheng,Michel L. Tremblay,Curt M. Horvath,Jean Patrick Parisien,Annette Salmeen,David Barford,Nicholas K. Tonks +8 more
TL;DR: It is demonstrated that (E/D)-pY-pY-(R/K) is a consensus substrate recognition motif for PTP1B and that the substrate recognition site within theses kinases is similar to the site of dephosphorylation previously identified within the insulin receptor.