G
Gregory J. Brunn
Researcher at Mayo Clinic
Publications - 46
Citations - 6564
Gregory J. Brunn is an academic researcher from Mayo Clinic. The author has contributed to research in topics: Receptor & TLR4. The author has an hindex of 30, co-authored 46 publications receiving 6301 citations. Previous affiliations of Gregory J. Brunn include University of Navarra & University of Rochester.
Papers
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Journal ArticleDOI
Phosphorylation of the translational repressor PHAS-I by the mammalian target of rapamycin
Gregory J. Brunn,Christine C. Hudson,Aleksandar Sekulic,Aleksandar Sekulic,Aleksandar Sekulic,Josie M. Williams,Hajime Hosoi,Peter J. Houghton,John C. Lawrence,Robert T. Abraham +9 more
TL;DR: A role for mTOR in translational control is defined and further insights into the mechanism whereby rapamycin inhibits G1-phase progression in mammalian cells are offered.
Journal ArticleDOI
Isolation of a Protein Target of the FKBP12-Rapamycin Complex in Mammalian Cells
Candace J. Sabers,Mary M. Martin,Gregory J. Brunn,Josie M. Williams,Francis J. Dumont,Gregory J. Wiederrecht,Robert T. Abraham +6 more
TL;DR: The results strongly suggest that the FKBP12-rapamycin complex interacts with homologous ligands in yeast and mammalian cells and that the loss of mTOR function is directly related to the inhibitory effect of rapamycin on G1- to S-phase progression in T-lymphocytes and other sensitive cell types.
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Direct inhibition of the signaling functions of the mammalian target of rapamycin by the phosphoinositide 3-kinase inhibitors, wortmannin and LY294002.
Gregory J. Brunn,Josie M. Williams,Candace J. Sabers,Gregory J. Wiederrecht,John C. Lawrence,Robert T. Abraham +5 more
TL;DR: It is demonstrated that mTOR is a component of a cytokine‐triggered protein kinase cascade leading to the phosphorylation of the eukaryotic initiation factor‐4E (eIF‐4 E) binding protein, PHAS‐1, in activated T lymphocytes.
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Receptor-Mediated Monitoring of Tissue Well-Being Via Detection of Soluble Heparan Sulfate by Toll-Like Receptor 4
TL;DR: The findings suggest that Toll-like receptors in vertebrates may monitor tissue well-being by recognizing fragments of endogenous macromolecules.
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Evidence of insulin-stimulated phosphorylation and activation of the mammalian target of rapamycin mediated by a protein kinase B signaling pathway
TL;DR: The findings support the conclusion that insulin activates mTOR by promoting phosphorylation of the protein via a signaling pathway that contains PKB.