R. Scott Prosser

Affiliations: 
Chemistry and Biochemistry University of Toronto, Toronto, ON, Canada 
Area:
Biophysical Chemistry, NMR Spectroscopy
Website:
http://sites.utm.utoronto.ca/prosserlab/
Google:
"R. Prosser"
Bio:

https://www.utm.utoronto.ca/cps/people/r-scott-prosser
http://sites.utm.utoronto.ca/prosserlab/

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Publications

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Frere GA, Hasabnis A, Francisco CB, et al. (2024) Next-Generation Tags for Fluorine Nuclear Magnetic Resonance: Designing Amplification of Chemical Shift Sensitivity. Journal of the American Chemical Society. 146: 3052-3064
Prosser RS, Alonzi NA. (2023) Discerning conformational dynamics and binding kinetics of GPCRs by F NMR. Current Opinion in Pharmacology. 102377
Picard LP, Prosser RS. (2021) Advances in the study of GPCRs by F NMR. Current Opinion in Structural Biology. 69: 169-176
Huang SK, Pandey A, Tran DP, et al. (2021) Delineating the conformational landscape of the adenosine A receptor during G protein coupling. Cell
Di Pietrantonio C, Pandey A, Gould J, et al. (2019) Understanding Protein Function Through an Ensemble Description: Characterization of Functional States by F NMR. Methods in Enzymology. 615: 103-130
Ye L, Neale C, Sljoka A, et al. (2018) Mechanistic insights into allosteric regulation of the A adenosine G protein-coupled receptor by physiological cations. Nature Communications. 9: 1372
Ye L, Orazietti AP, Pandey A, et al. (2018) High-Efficiency Expression of Yeast-Derived G-Protein Coupled Receptors and (19)F Labeling for Dynamical Studies. Methods in Molecular Biology (Clifton, N.J.). 1688: 407-421
Prosser RS, Ye L, Pandey A, et al. (2017) Activation processes in ligand-activated G protein-coupled receptors: A case study of the adenosine A2A receptor. Bioessays : News and Reviews in Molecular, Cellular and Developmental Biology
Brea RJ, Cole CM, Lyda BR, et al. (2017) In Situ Reconstitution of the Adenosine A2A Receptor in Spontaneously Formed Synthetic Liposomes. Journal of the American Chemical Society
Kim TH, Mehrabi P, Ren Z, et al. (2017) The role of dimer asymmetry and protomer dynamics in enzyme catalysis. Science (New York, N.Y.). 355
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