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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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Structural insights into µ-opioid receptor activation

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.

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 *

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.