J
John R. Traynor
Researcher at University of Michigan
Publications - 201
Citations - 6425
John R. Traynor is an academic researcher from University of Michigan. The author has contributed to research in topics: Agonist & Opioid receptor. The author has an hindex of 41, co-authored 190 publications receiving 5734 citations. Previous affiliations of John R. Traynor include Roseman University of Health Sciences & Loughborough University.
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Journal ArticleDOI
Structural insights into µ-opioid receptor activation
Weijiao Huang,Aashish Manglik,AJ Venkatakrishnan,Toon Laeremans,Evan N. Feinberg,Adrian L. Sanborn,Hideaki E. Kato,Kathryn E. Livingston,Thor S. Thorsen,Ralf C. Kling,Sébastien Granier,Peter Gmeiner,Stephen M. Husbands,John R. Traynor,William I. Weis,Jan Steyaert,Ron O. Dror,Brian K. Kobilka +17 more
TL;DR: A 2.1 Å X-ray crystal structure of the murine μOR bound to the morphinan agonist BU72 and a G protein mimetic camelid antibody fragment is reported, revealing an extensive polar network between the ligand-binding pocket and the cytoplasmic domains appears to play a similar role in signal propagation for all three G-protein-coupled receptors.
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Nonpeptidic δ-opioid Receptor Agonists Reduce Immobility in the Forced Swim Assay in Rats
TL;DR: In this paper, the authors examined the effect of opioid receptor agonists in the rat forced swim assay and found that δ-opioid receptor agents were more active with a single dose whereas both desipramine and fluoxetine produced greater effects with sub-chronic dosing.
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Comparison of the Antinociceptive Response to Morphine and Morphine-Like Compounds in Male and Female Sprague-Dawley Rats
TL;DR: Morphinans closely related in structure to morphine, namely, codeine, heroin, hydrocodone, hydromorphone, oxymorphone, and oxycodone, were examined for antinociceptive activity in male and female Sprague-Dawley rats and compared with the structurally unrelated μ-opioid agonists methadone and fentanyl.
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Identification of small-molecule inhibitors of RGS4 using a high-throughput flow cytometry protein interaction assay.
David L. Roman,Jeffery N. Talbot,Rebecca A. Roof,Roger K. Sunahara,John R. Traynor,Richard R. Neubig +5 more
TL;DR: The first small-molecule inhibitor of an RGS protein is identified and the feasibility of targeting RGS/Gα protein-protein interactions with small molecules as a novel means to modulate GPCR-mediated signaling processes is demonstrated.
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A Spatial Focusing Model for G Protein Signals: REGULATOR OF G PROTEIN SIGNALING (RGS) PROTEIN-MEDIATED KINETIC SCAFFOLDING *
Huailing Zhong,Susan M. Wade,Peter J. Woolf,Jennifer J. Linderman,John R. Traynor,Richard R. Neubig +5 more
TL;DR: A novel RGS-mediated “kinetic scaffolding” mechanism is proposed which narrows the spatial range of active G protein around a cluster of receptors limiting the spill-over of G protein signals to more distant effector molecules, thus enhancing the specificity of Gi protein signals.