| Year |
Citation |
Score |
| 2024 |
Frere GA, Hasabnis A, Francisco CB, Suleiman M, Alimowska O, Rahmatullah R, Gould J, Su CY, Voznyy O, Gunning PT, Basso EA, Prosser RS. Next-Generation Tags for Fluorine Nuclear Magnetic Resonance: Designing Amplification of Chemical Shift Sensitivity. Journal of the American Chemical Society. 146: 3052-3064. PMID 38279916 DOI: 10.1021/jacs.3c09730 |
0.393 |
|
| 2023 |
Prosser RS, Alonzi NA. Discerning conformational dynamics and binding kinetics of GPCRs by F NMR. Current Opinion in Pharmacology. 102377. PMID 37612172 DOI: 10.1016/j.coph.2023.102377 |
0.375 |
|
| 2021 |
Picard LP, Prosser RS. Advances in the study of GPCRs by F NMR. Current Opinion in Structural Biology. 69: 169-176. PMID 34130235 DOI: 10.1016/j.sbi.2021.05.001 |
0.325 |
|
| 2021 |
Huang SK, Pandey A, Tran DP, Villanueva NL, Kitao A, Sunahara RK, Sljoka A, Prosser RS. Delineating the conformational landscape of the adenosine A receptor during G protein coupling. Cell. PMID 33743210 DOI: 10.1016/j.cell.2021.02.041 |
0.322 |
|
| 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 |
0.35 |
|
| 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 |
0.784 |
|
| 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 |
0.353 |
|
| 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 |
0.375 |
|
| 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 |
0.329 |
|
| 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 |
0.335 |
|
| 2017 |
Alvares RDA, Gautam A, Prosser RS, van Veggel FCJM, Macdonald PM. Shell versus Core Dy3+ Contributions to NMR Water Relaxation in Sodium Lanthanide Fluoride Core–Shell Nanoparticles. An Investigation Using O-17 and H-1 NMR The Journal of Physical Chemistry C. 121: 17552-17558. DOI: 10.1021/Acs.Jpcc.7B06954 |
0.755 |
|
| 2017 |
Fernandes DD, Ye L, Li Y, Zhang Z, Gomes G, Prosser RS, Gradinaru CC. The Role of G-Protein-Coupled Receptor Activation by Conformational Selection as Revealed by Single-Molecule Fluorescence Biophysical Journal. 112: 327a-328a. DOI: 10.1016/J.Bpj.2016.11.1772 |
0.326 |
|
| 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 |
0.332 |
|
| 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 |
0.772 |
|
| 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 |
0.778 |
|
| 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 |
0.789 |
|
| 2015 |
Prosser RS, Kim TH. Nuts and Bolts of CF3 and CH 3 NMR Toward the Understanding of Conformational Exchange of GPCRs. Methods in Molecular Biology (Clifton, N.J.). 1335: 39-51. PMID 26260593 DOI: 10.1007/978-1-4939-2914-6_4 |
0.441 |
|
| 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.2015.04.043 |
0.402 |
|
| 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 |
0.798 |
|
| 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 |
0.419 |
|
| 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 |
0.334 |
|
| 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 |
0.782 |
|
| 2013 |
Kitevski-Leblanc JL, Hoang J, Thach W, Larda ST, Prosser RS. ¹â¹F NMR studies of a desolvated near-native protein folding intermediate. Biochemistry. 52: 5780-9. PMID 23906334 DOI: 10.1021/Bi4010057 |
0.778 |
|
| 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 |
0.781 |
|
| 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 |
0.378 |
|
| 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 |
0.376 |
|
| 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 |
0.771 |
|
| 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 |
0.778 |
|
| 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 |
0.786 |
|
| 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 |
0.37 |
|
| 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 |
0.368 |
|
| 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 |
0.799 |
|
| 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 |
0.371 |
|
| 2010 |
Kitevski-LeBlanc JL, Evanics F, Prosser RS. Optimizing 19F NMR protein spectroscopy by fractional biosynthetic labeling Journal of Biomolecular Nmr. 48: 113-121. PMID 20734112 DOI: 10.1007/S10858-010-9443-7 |
0.804 |
|
| 2010 |
Kitevski-LeBlanc JL, Evanics F, Prosser RS. Approaches to the assignment of (19)F resonances from 3-fluorophenylalanine labeled calmodulin using solution state NMR. Journal of Biomolecular Nmr. 47: 113-123. PMID 20401735 DOI: 10.1007/S10858-010-9415-Y |
0.802 |
|
| 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 |
0.351 |
|
| 2010 |
Cheung ENM, Alvares RDA, Oakden W, Chaudhary R, Hill ML, Pichaandi J, Mo GCH, Yip C, MacDonald PM, Stanisz GJ, Van Veggel FCJM, Prosser RS. Polymer-stabilized lanthanide fluoride nanoparticle aggregates as contrast agents for magnetic resonance imaging and computed tomography Chemistry of Materials. 22: 4728-4739. DOI: 10.1021/Cm101036A |
0.749 |
|
| 2010 |
Bokoch MP, Nygaard R, Zou Y, Rasmussen SG, Pardo L, Prosser RS, Mueller L, Kobilka BK. Conformational Changes in GPCR Surface and Core Probed by [13C]-Methyl NMR Spectroscopy Biophysical Journal. 98: 418a. DOI: 10.1016/J.Bpj.2009.12.2257 |
0.419 |
|
| 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 |
0.802 |
|
| 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 |
0.436 |
|
| 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 |
0.385 |
|
| 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 |
0.808 |
|
| 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 |
0.34 |
|
| 2008 |
Bezsonova I, Forman-Kay J, Prosser RS. Molecular oxygen as a paramagnetic NMR probe of protein solvent exposure and topology Concepts in Magnetic Resonance Part a: Bridging Education and Research. 32: 239-253. DOI: 10.1002/Cmr.A.20118 |
0.424 |
|
| 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 |
0.393 |
|
| 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 |
0.423 |
|
| 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 |
0.447 |
|
| 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 |
0.43 |
|
| 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 |
0.342 |
|
| 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 |
0.406 |
|
| 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 |
0.36 |
|
| 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 |
0.38 |
|
| 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 |
0.379 |
|
| 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 |
0.431 |
|
| 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 |
0.411 |
|
| 2001 |
Luchette PA, Vetman TN, Prosser RS, Hancock RE, Nieh MP, Glinka CJ, Krueger S, Katsaras J. Morphology of fast-tumbling bicelles: a small angle neutron scattering and NMR study. Biochimica Et Biophysica Acta. 1513: 83-94. PMID 11470082 DOI: 10.1016/S0005-2736(01)00358-3 |
0.371 |
|
| 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 |
0.36 |
|
| 2001 |
Prosser RS, Shiyanovskaya IV. Lanthanide ion assisted magnetic alignment of model membranes and macromolecules Concepts in Magnetic Resonance. 13: 19-31. DOI: 10.1002/1099-0534(2001)13:1<19::Aid-Cmr3>3.0.Co;2-3 |
0.347 |
|
| 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 |
0.627 |
|
| 1998 |
Prosser RS, Volkov VB, Shiyanovskaya IV. Solid-state NMR studies of magnetically aligned phospholipid membranes: taming lanthanides for membrane protein studies. Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire. 76: 443-51. PMID 9923713 DOI: 10.1139/Bcb-76-2-3-443 |
0.34 |
|
| 1998 |
Prosser RS, Volkov VB, Shiyanovskaya IV. Novel chelate-induced magnetic alignment of biological membranes. Biophysical Journal. 75: 2163-9. PMID 9788910 DOI: 10.1016/S0006-3495(98)77659-3 |
0.375 |
|
| 1998 |
Prosser RS, Hwang JS, Vold RR. Magnetically aligned phospholipid bilayers with positive ordering: a new model membrane system. Biophysical Journal. 74: 2405-18. PMID 9591667 DOI: 10.1016/S0006-3495(98)77949-4 |
0.618 |
|
| 1997 |
Vold RR, Prosser RS, Deese AJ. Isotropic solutions of phospholipid bicelles: a new membrane mimetic for high-resolution NMR studies of polypeptides. Journal of Biomolecular Nmr. 9: 329-35. PMID 9229505 DOI: 10.1023/A:1018643312309 |
0.655 |
|
| 1996 |
Prosser RS, Hunt SA, DiNatale aJA, Vold RR. Magnetically Aligned Membrane Model Systems With Positive Order Parameter : Switching The Sign Of Szz With Paramagnetic Ions Journal of the American Chemical Society. 118: 269-270. DOI: 10.1021/Ja953598X |
0.578 |
|
| 1996 |
Vold RR, Prosser RS. Magnetically oriented phospholipid bilayered micelles for structural studies of polypeptides. Does the ideal bicelle exist? Journal of Magnetic Resonance - Series B. 113: 267-271. DOI: 10.1006/Jmrb.1996.0187 |
0.61 |
|
| 1995 |
Prosser RS, Hunt SA, Vold RR. Improving Sensitivity in Mechanically Oriented Phospholipid Bilayers Using Ultrathin Glass Plates - A Deuterium Solid-State NMR Study Journal of Magnetic Resonance, Series B. 109: 109-111. DOI: 10.1006/Jmrb.1995.1156 |
0.583 |
|
| 1994 |
Prosser RS, Davis JH. Dynamics of an integral membrane peptide: a deuterium NMR relaxation study of gramicidin. Biophysical Journal. 66: 1429-40. PMID 7520294 DOI: 10.1016/S0006-3495(94)80933-6 |
0.486 |
|
| 1994 |
Prosser RS, Daleman SI, Davis JH. The structure of an integral membrane peptide: a deuterium NMR study of gramicidin. Biophysical Journal. 66: 1415-28. PMID 7520293 DOI: 10.1016/S0006-3495(94)80932-4 |
0.5 |
|
| 1992 |
Prosser RS, Davis JH, Mayer C, Weisz K, Kothe G. Deuterium NMR relaxation studies of peptide-lipid interactions. Biochemistry. 31: 9355-63. PMID 1390721 DOI: 10.1021/Bi00154A005 |
0.452 |
|
| 1992 |
Katsaras J, Prosser RS, Stinson RH, Davis JH. Constant helical pitch of the gramicidin channel in phospholipid bilayers. Biophysical Journal. 61: 827-30. PMID 1380320 DOI: 10.1016/S0006-3495(92)81888-X |
0.402 |
|
| 1991 |
Prosser RS, Davis JH, Dahlquist FW, Lindorfer MA. 2H nuclear magnetic resonance of the gramicidin A backbone in a phospholipid bilayer. Biochemistry. 30: 4687-96. PMID 1709361 DOI: 10.1021/Bi00233A008 |
0.468 |
|
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