R. Scott Prosser - Publications

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

50 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2019 Staus DP, Wingler LM, Pichugin D, Prosser RS, Lefkowitz RJ. Detergent- and phospholipid-based reconstitution systems have differential effects on constitutive activity of G protein-coupled receptors. The Journal of Biological Chemistry. PMID 31362983 DOI: 10.1074/jbc.AC119.009848  0.6
2019 Di Pietrantonio C, Pandey A, Gould J, Hasabnis A, Prosser RS. Understanding Protein Function Through an Ensemble Description: Characterization of Functional States by F NMR. Methods in Enzymology. 615: 103-130. PMID 30638528 DOI: 10.1016/bs.mie.2018.09.029  0.48
2018 Ye L, Neale C, Sljoka A, Lyda B, Pichugin D, Tsuchimura N, Larda ST, Pomès R, García AE, Ernst OP, Sunahara RK, Prosser RS. Mechanistic insights into allosteric regulation of the A adenosine G protein-coupled receptor by physiological cations. Nature Communications. 9: 1372. PMID 29636462 DOI: 10.1038/s41467-018-03314-9  0.6
2018 Ye L, Orazietti AP, Pandey A, Prosser RS. 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. PMID 29151220 DOI: 10.1007/978-1-4939-7386-6_19  0.32
2017 Prosser RS, Ye L, Pandey A, Orazietti A. 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. PMID 28787091 DOI: 10.1002/bies.201700072  0.32
2017 Brea RJ, Cole CM, Lyda BR, Ye L, Prosser RS, Sunahara RK, Devaraj NK. In Situ Reconstitution of the Adenosine A2A Receptor in Spontaneously Formed Synthetic Liposomes. Journal of the American Chemical Society. PMID 28263576 DOI: 10.1021/jacs.6b12830  0.32
2017 Kim TH, Mehrabi P, Ren Z, Sljoka A, Ing C, Bezginov A, Ye L, Pomès R, Prosser RS, Pai EF. The role of dimer asymmetry and protomer dynamics in enzyme catalysis. Science (New York, N.Y.). 355. PMID 28104837 DOI: 10.1126/science.aag2355  0.32
2016 Staus DP, Strachan RT, Manglik A, Pani B, Kahsai AW, Kim TH, Wingler LM, Ahn S, Chatterjee A, Masoudi A, Kruse AC, Pardon E, Steyaert J, Weis WI, Prosser RS, et al. Allosteric nanobodies reveal the dynamic range and diverse mechanisms of G-protein-coupled receptor activation. Nature. PMID 27409812 DOI: 10.1038/nature18636  0.32
2016 Alvares RD, Lau JY, Macdonald PM, Cunningham CH, Prosser RS. Direct quantitative (13) C-filtered (1) H magnetic resonance imaging of PEGylated biomacromolecules in vivo. Magnetic Resonance in Medicine. PMID 27080189 DOI: 10.1002/mrm.26237  1
2016 Alvares RD, Hasabnis A, Prosser RS, Macdonald PM. Quantitative Detection of PEGylated Biomacromolecules in Biological Fluids by NMR. Analytical Chemistry. PMID 26927487 DOI: 10.1021/acs.analchem.5b04565  1
2015 Larda ST, Pichugin D, Prosser RS. Site-specific labeling of protein lysine residues and N-terminal amino groups with indoles and indole-derivatives. Bioconjugate Chemistry. PMID 26587689 DOI: 10.1021/acs.bioconjchem.5b00457  1
2015 Manglik A, Kim TH, Masureel M, Altenbach C, Yang Z, Hilger D, Lerch MT, Kobilka TS, Thian FS, Hubbell WL, Prosser RS, Kobilka BK. Structural Insights into the Dynamic Process of β2-Adrenergic Receptor Signaling. Cell. 161: 1101-11. PMID 25981665 DOI: 10.1016/J.CELL.2015.08.045  0.32
2015 Ye L, Larda ST, Frank Li YF, Manglik A, Prosser RS. A comparison of chemical shift sensitivity of trifluoromethyl tags: optimizing resolution in ¹⁹F NMR studies of proteins. Journal of Biomolecular Nmr. 62: 97-103. PMID 25813845 DOI: 10.1007/s10858-015-9922-y  1
2014 Hoang J, Prosser RS. Conformational selection and functional dynamics of calmodulin: a (19)F nuclear magnetic resonance study. Biochemistry. 53: 5727-36. PMID 25148136 DOI: 10.1021/bi500679c  1
2014 Prosser RS. New pipelines for novel allosteric GPCR modulators. Biophysical Journal. 107: 287-8. PMID 25028870 DOI: 10.1016/j.bpj.2014.06.016  1
2014 Alvares R, Gupta S, Macdonald PM, Prosser RS. Temperature and pressure based NMR studies of detergent micelle phase equilibria. The Journal of Physical Chemistry. B. 118: 5698-706. PMID 24801930 DOI: 10.1021/jp500139p  1
2013 Kitevski-Leblanc JL, Hoang J, Thach W, Larda ST, Prosser RS. ¹⁹F NMR studies of a desolvated near-native protein folding intermediate. Biochemistry. 52: 5780-9. PMID 23906334 DOI: 10.1021/bi4010057  1
2013 Larda ST, Simonetti K, Al-Abdul-Wahid MS, Sharpe S, Prosser RS. Dynamic equilibria between monomeric and oligomeric misfolded states of the mammalian prion protein measured by 19F NMR. Journal of the American Chemical Society. 135: 10533-41. PMID 23781904 DOI: 10.1021/ja404584s  1
2013 Kim TH, Chung KY, Manglik A, Hansen AL, Dror RO, Mildorf TJ, Shaw DE, Kobilka BK, Prosser RS. The role of ligands on the equilibria between functional states of a G protein-coupled receptor. Journal of the American Chemical Society. 135: 9465-74. PMID 23721409 DOI: 10.1021/ja404305k  1
2013 Nygaard R, Zou Y, Dror RO, Mildorf TJ, Arlow DH, Manglik A, Pan AC, Liu CW, Fung JJ, Bokoch MP, Thian FS, Kobilka TS, Shaw DE, Mueller L, Prosser RS, et al. The dynamic process of β(2)-adrenergic receptor activation. Cell. 152: 532-42. PMID 23374348 DOI: 10.1016/j.cell.2013.01.008  1
2013 Alvares RD, Tulumello DV, Macdonald PM, Deber CM, Prosser RS. Effects of a polar amino acid substitution on helix formation and aggregate size along the detergent-induced peptide folding pathway. Biochimica Et Biophysica Acta. 1828: 373-81. PMID 23031573 DOI: 10.1016/j.bbamem.2012.09.024  1
2012 Larda ST, Bokoch MP, Evanics F, Prosser RS. Lysine methylation strategies for characterizing protein conformations by NMR. Journal of Biomolecular Nmr. 54: 199-209. PMID 22960995 DOI: 10.1007/s10858-012-9664-z  1
2012 Chung KY, Kim TH, Manglik A, Alvares R, Kobilka BK, Prosser RS. Role of detergents in conformational exchange of a G protein-coupled receptor. The Journal of Biological Chemistry. 287: 36305-11. PMID 22893704 DOI: 10.1074/jbc.M112.406371  1
2012 Al-Abdul-Wahid MS, Demill CM, Serwin MB, Prosser RS, Stewart BA. Effect of juxtamembrane tryptophans on the immersion depth of Synaptobrevin, an integral vesicle membrane protein. Biochimica Et Biophysica Acta. 1818: 2994-9. PMID 22846509 DOI: 10.1016/j.bbamem.2012.07.018  1
2012 Beharry AA, Chen T, Al-Abdul-Wahid MS, Samanta S, Davidov K, Sadovski O, Ali AM, Chen SB, Prosser RS, Chan HS, Woolley GA. Quantitative analysis of the effects of photoswitchable distance constraints on the structure of a globular protein. Biochemistry. 51: 6421-31. PMID 22803618 DOI: 10.1021/bi300685a  1
2012 Kitevski-LeBlanc JL, Prosser RS. Current applications of 19F NMR to studies of protein structure and dynamics. Progress in Nuclear Magnetic Resonance Spectroscopy. 62: 1-33. PMID 22364614 DOI: 10.1016/j.pnmrs.2011.06.003  1
2011 Al-Abdul-Wahid MS, Verardi R, Veglia G, Prosser RS. Topology and immersion depth of an integral membrane protein by paramagnetic rates from dissolved oxygen. Journal of Biomolecular Nmr. 51: 173-83. PMID 21947925 DOI: 10.1007/s10858-011-9551-z  1
2011 Al-Abdul-Wahid MS, Evanics F, Prosser RS. Dioxygen transmembrane distributions and partitioning thermodynamics in lipid bilayers and micelles. Biochemistry. 50: 3975-83. PMID 21510612 DOI: 10.1021/bi200168n  1
2010 Bokoch MP, Zou Y, Rasmussen SG, Liu CW, Nygaard R, Rosenbaum DM, Fung JJ, Choi HJ, Thian FS, Kobilka TS, Puglisi JD, Weis WI, Pardo L, Prosser RS, Mueller L, et al. Ligand-specific regulation of the extracellular surface of a G-protein-coupled receptor. Nature. 463: 108-12. PMID 20054398 DOI: 10.1038/nature08650  1
2009 Kitevski-LeBlanc JL, Evanics F, Prosser RS. Approaches for the measurement of solvent exposure in proteins by 19F NMR. Journal of Biomolecular Nmr. 45: 255-64. PMID 19655092 DOI: 10.1007/s10858-009-9359-2  1
2009 Moriya J, Sakakura M, Tokunaga Y, Prosser RS, Shimada I. An NMR method for the determination of protein binding interfaces using TEMPOL-induced chemical shift perturbations. Biochimica Et Biophysica Acta. 1790: 1368-76. PMID 19520148 DOI: 10.1016/j.bbagen.2009.06.001  1
2009 Al-Abdul-Wahid MS, Neale C, Pomès R, Prosser RS. A solution NMR approach to the measurement of amphiphile immersion depth and orientation in membrane model systems. Journal of the American Chemical Society. 131: 6452-9. PMID 19415935 DOI: 10.1021/ja808964e  1
2009 Kitevski-LeBlanc JL, Al-Abdul-Wahid MS, Prosser RS. A mutagenesis-free approach to assignment of (19)F NMR resonances in biosynthetically labeled proteins. Journal of the American Chemical Society. 131: 2054-5. PMID 19173647 DOI: 10.1021/ja8085752  1
2009 Zhang F, Zarrine-Afsar A, Al-Abdul-Wahid MS, Prosser RS, Davidson AR, Woolley GA. Structure-based approach to the photocontrol of protein folding. Journal of the American Chemical Society. 131: 2283-9. PMID 19170498 DOI: 10.1021/ja807938v  1
2007 Prosser RS, Evanics F, Kitevski JL, Patel S. The measurement of immersion depth and topology of membrane proteins by solution state NMR. Biochimica Et Biophysica Acta. 1768: 3044-51. PMID 17976526 DOI: 10.1016/j.bbamem.2007.09.011  1
2007 Bezsonova I, Evanics F, Marsh JA, Forman-Kay JD, Prosser RS. Oxygen as a paramagnetic probe of clustering and solvent exposure in folded and unfolded states of an SH3 domain. Journal of the American Chemical Society. 129: 1826-35. PMID 17253684 DOI: 10.1021/ja065173o  1
2007 Evanics F, Kitevski JL, Bezsonova I, Forman-Kay J, Prosser RS. 19F NMR studies of solvent exposure and peptide binding to an SH3 domain. Biochimica Et Biophysica Acta. 1770: 221-30. PMID 17182189 DOI: 10.1016/j.bbagen.2006.10.017  1
2006 Evanics F, Bezsonova I, Marsh J, Kitevski JL, Forman-Kay JD, Prosser RS. Tryptophan solvent exposure in folded and unfolded states of an SH3 domain by 19F and 1H NMR. Biochemistry. 45: 14120-8. PMID 17115707 DOI: 10.1021/bi061389r  1
2006 Al-Abdul-Wahid MS, Yu CH, Batruch I, Evanics F, Pomès R, Prosser RS. A combined NMR and molecular dynamics study of the transmembrane solubility and diffusion rate profile of dioxygen in lipid bilayers. Biochemistry. 45: 10719-28. PMID 16939224 DOI: 10.1021/bi060270f  1
2006 Prosser RS, Evanics F, Kitevski JL, Al-Abdul-Wahid MS. Current applications of bicelles in NMR studies of membrane-associated amphiphiles and proteins. Biochemistry. 45: 8453-65. PMID 16834319 DOI: 10.1021/bi060615u  1
2006 Evanics F, Hwang PM, Cheng Y, Kay LE, Prosser RS. Topology of an outer-membrane enzyme: Measuring oxygen and water contacts in solution NMR studies of PagP. Journal of the American Chemical Society. 128: 8256-64. PMID 16787090 DOI: 10.1021/ja0610075  1
2006 Korzhnev DM, Bezsonova I, Evanics F, Taulier N, Zhou Z, Bai Y, Chalikian TV, Prosser RS, Kay LE. Probing the transition state ensemble of a protein folding reaction by pressure-dependent NMR relaxation dispersion. Journal of the American Chemical Society. 128: 5262-9. PMID 16608362 DOI: 10.1021/ja0601540  1
2006 Bezsonova I, Korzhnev DM, Prosser RS, Forman-Kay JD, Kay LE. Hydration and packing along the folding pathway of SH3 domains by pressure-dependent NMR. Biochemistry. 45: 4711-9. PMID 16605239 DOI: 10.1021/bi060177r  1
2005 Sakakura M, Noba S, Luchette PA, Shimada I, Prosser RS. An NMR method for the determination of protein-binding interfaces using dioxygen-induced spin-lattice relaxation enhancement. Journal of the American Chemical Society. 127: 5826-32. PMID 15839680 DOI: 10.1021/ja047825j  1
2004 Prosser RS, Luchette PA. An NMR study of the origin of dioxygen-induced spin-lattice relaxation enhancement and chemical shift perturbation. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 171: 225-32. PMID 15546748 DOI: 10.1016/j.jmr.2004.08.012  1
2002 Luchette PA, Prosser RS, Sanders CR. Oxygen as a paramagnetic probe of membrane protein structure by cysteine mutagenesis and (19)F NMR spectroscopy. Journal of the American Chemical Society. 124: 1778-81. PMID 11853456 DOI: 10.1021/ja016748e  1
2001 Prosser RS, Luchette PA, Westerman PW, Rozek A, Hancock RE. Determination of membrane immersion depth with O(2): a high-pressure (19)F NMR study. Biophysical Journal. 80: 1406-16. PMID 11222301 DOI: 10.1016/S0006-3495(01)76113-9  1
2000 Prosser RS, Luchette PA, Westerman PW. Using O2 to probe membrane immersion depth by 19F NMR. Proceedings of the National Academy of Sciences of the United States of America. 97: 9967-71. PMID 10954744 DOI: 10.1073/pnas.170295297  1
1999 Prosser RS, Bryant H, Bryant RG, Vold RR. Lanthanide chelates as bilayer alignment tools in NMR studies of membrane-associated peptides. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 141: 256-60. PMID 10579948 DOI: 10.1006/jmre.1999.1855  1
1998 Sanders CR, Prosser RS. Bicelles: a model membrane system for all seasons? Structure (London, England : 1993). 6: 1227-34. PMID 9782059  1
Show low-probability matches.