| Year |
Citation |
Score |
| 2020 |
Rosenberg MM, Yao T, Patton GC, Redfield AG, Roberts MF, Hedstrom L. Enzyme-substrate-cofactor dynamical networks revealed by high resolution field cycling relaxometry. Biochemistry. PMID 32479091 DOI: 10.1021/Acs.Biochem.0C00212 |
0.333 |
|
| 2018 |
Rosenberg MM, Redfield AG, Roberts M, Hedstrom L. Dynamic characteristics of GMP reductase complexes revealed by high resolutionP field cycling NMR relaxometry. Biochemistry. PMID 29547266 DOI: 10.1021/Acs.Biochem.8B00142 |
0.314 |
|
| 2016 |
Rosenberg MM, Redfield AG, Roberts MF, Hedstrom L. Substrate and Cofactor Dynamics on Guanosine Monophosphate Reductase Probed by High Resolution Field Cycling 31P NMR Relaxometry. The Journal of Biological Chemistry. PMID 27613871 DOI: 10.1074/Jbc.M116.739516 |
0.36 |
|
| 2015 |
Wei Y, Stec B, Redfield AG, Weerapana E, Roberts MF. Phospholipid-binding sites of phosphatase and tensin homolog (PTEN): exploring the mechanism of phosphatidylinositol 4,5-bisphosphate activation. The Journal of Biological Chemistry. 290: 1592-606. PMID 25429968 DOI: 10.1074/Jbc.M114.588590 |
0.351 |
|
| 2014 |
Gradziel CS, Wang Y, Stec B, Redfield AG, Roberts MF. Cytotoxic amphiphiles and phosphoinositides bind to two discrete sites on the Akt1 PH domain. Biochemistry. 53: 462-72. PMID 24383815 DOI: 10.1021/Bi401720V |
0.339 |
|
| 2012 |
Redfield AG. High-resolution NMR field-cycling device for full-range relaxation and structural studies of biopolymers on a shared commercial instrument. Journal of Biomolecular Nmr. 52: 159-77. PMID 22200887 DOI: 10.1007/S10858-011-9594-1 |
0.315 |
|
| 2010 |
Pu M, Orr A, Redfield AG, Roberts MF. Defining specific lipid binding sites for a peripheral membrane protein in situ using subtesla field-cycling NMR. The Journal of Biological Chemistry. 285: 26916-22. PMID 20576615 DOI: 10.1074/Jbc.M110.123083 |
0.35 |
|
| 2009 |
Pu M, Feng J, Redfield AG, Roberts MF. Enzymology with a spin-labeled phospholipase C: soluble substrate binding by 31P NMR from 0.005 to 11.7 T. Biochemistry. 48: 8282-4. PMID 19663462 DOI: 10.1021/Bi901190J |
0.364 |
|
| 2009 |
Clarkson MW, Lei M, Eisenmesser EZ, Labeikovsky W, Redfield A, Kern D. Mesodynamics in the SARS nucleocapsid measured by NMR field cycling. Journal of Biomolecular Nmr. 45: 217-25. PMID 19641854 DOI: 10.1007/S10858-009-9347-6 |
0.32 |
|
| 2009 |
Roberts MF, Redfield AG, Mohanty U. Phospholipid reorientation at the lipid/water interface measured by high resolution 31P field cycling NMR spectroscopy. Biophysical Journal. 97: 132-41. PMID 19580751 DOI: 10.1016/J.Bpj.2009.03.057 |
0.336 |
|
| 2009 |
Pu M, Fang X, Redfield AG, Gershenson A, Roberts MF. Correlation of vesicle binding and phospholipid dynamics with phospholipase C activity: insights into phosphatidylcholine activation and surface dilution inhibition. The Journal of Biological Chemistry. 284: 16099-107. PMID 19336401 DOI: 10.1074/Jbc.M809600200 |
0.312 |
|
| 2009 |
Sivanandam VN, Cai J, Redfield AG, Roberts MF. Phosphatidylcholine "wobble" in vesicles assessed by high-resolution 13C field cycling NMR spectroscopy. Journal of the American Chemical Society. 131: 3420-1. PMID 19243091 DOI: 10.1021/Ja808431H |
0.378 |
|
| 2008 |
Klauda JB, Roberts MF, Redfield AG, Brooks BR, Pastor RW. Rotation of lipids in membranes: molecular dynamics simulation, 31P spin-lattice relaxation, and rigid-body dynamics. Biophysical Journal. 94: 3074-83. PMID 18192349 DOI: 10.1529/Biophysj.107.121806 |
0.341 |
|
| 2004 |
Roberts MF, Redfield AG. Phospholipid bilayer surface configuration probed quantitatively by (31)P field-cycling NMR. Proceedings of the National Academy of Sciences of the United States of America. 101: 17066-71. PMID 15569928 DOI: 10.1073/Pnas.0407565101 |
0.382 |
|
| 2004 |
Roberts MF, Redfield AG. High-resolution 31p field cycling NMR as a probe of phospholipid dynamics. Journal of the American Chemical Society. 126: 13765-77. PMID 15493936 DOI: 10.1021/Ja046658K |
0.384 |
|
| 2004 |
Roberts MF, Cui Q, Turner CJ, Case DA, Redfield AG. High-resolution field-cycling NMR studies of a DNA octamer as a probe of phosphodiester dynamics and comparison with computer simulation. Biochemistry. 43: 3637-50. PMID 15035634 DOI: 10.1021/Bi035979Q |
0.379 |
|
| 2004 |
Ivanov D, Redfield AG. Field-cycling method with central transition readout for pure quadrupole resonance detection in dilute systems. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 166: 19-27. PMID 14675815 DOI: 10.1016/J.Jmr.2003.10.006 |
0.537 |
|
| 2003 |
Redfield AG. Shuttling device for high-resolution measurements of relaxation and related phenomena in solution at low field, using a shared commercial 500 MHz NMR instrument Magnetic Resonance in Chemistry. 41: 753-768. DOI: 10.1002/Mrc.1264 |
0.356 |
|
| 2002 |
Ivanov D, Bachovchin WW, Redfield AG. Boron-11 pure quadrupole resonance investigation of peptide boronic acid inhibitors bound to alpha-lytic protease. Biochemistry. 41: 1587-90. PMID 11814352 DOI: 10.1021/Bi011783J |
0.57 |
|
| 1998 |
Ivanov D, Redfield A. Development of a field cycling NMR system for PQR detection in biopolymers Zeitschrift Fur Naturforschung - Section a Journal of Physical Sciences. 53: 269-272. DOI: 10.1515/Zna-1998-6-703 |
0.557 |
|
| 1997 |
Hu JS, Redfield AG. Conformational and dynamic differences between N-ras P21 bound to GTPgammaS and to GMPPNP as studied by NMR. Biochemistry. 36: 5045-52. PMID 9125526 DOI: 10.1021/Bi963010E |
0.396 |
|
| 1995 |
Choi BS, Redfield AG. Proton exchange and basepair kinetics of yeast tRNA(Phe) and tRNA(Asp1). Journal of Biochemistry. 117: 515-20. PMID 7629016 DOI: 10.1093/Oxfordjournals.Jbchem.A124738 |
0.399 |
|
| 1994 |
Halkides CJ, Farrar CT, Larsen RG, Redfield AG, Singel DJ. Characterization of the active site of p21 ras by electron spin-echo envelope modulation spectroscopy with selective labeling: comparisons between GDP and GTP forms. Biochemistry. 33: 4019-35. PMID 8142406 DOI: 10.1021/Bi00179A031 |
0.367 |
|
| 1993 |
Miller AF, Halkides CJ, Redfield AG. An NMR comparison of the changes produced by different guanosine 5'-triphosphate analogs in wild-type and oncogenic mutant p21ras. Biochemistry. 32: 7367-76. PMID 8338834 DOI: 10.1021/Bi00080A006 |
0.417 |
|
| 1993 |
Hu JS, Redfield AG. Mapping the nucleotide-dependent conformational change of human N-ras p21 in solution by heteronuclear-edited proton-observed NMR methods. Biochemistry. 32: 6763-72. PMID 8329399 DOI: 10.1021/Bi00077A031 |
0.368 |
|
| 1992 |
Lowry DF, Ahmadian MR, Redfield AG, Sprinzl M. NMR study of the phosphate-binding loops of Thermus thermophilus elongation factor Tu. Biochemistry. 31: 2977-82. PMID 1550823 DOI: 10.1021/Bi00126A019 |
0.424 |
|
| 1992 |
Choi BS, Redfield AG. NMR study of nitrogen-15-labeled Escherichia coli valine transfer RNA. Biochemistry. 31: 12799-802. PMID 1463750 DOI: 10.1021/Bi00166A013 |
0.419 |
|
| 1992 |
Miller AF, Papastavros MZ, Redfield AG. NMR studies of the conformational change in human N-p21ras produced by replacement of bound GDP with the GTP analog GTP gamma S. Biochemistry. 31: 10208-16. PMID 1420142 DOI: 10.1021/Bi00157A007 |
0.396 |
|
| 1992 |
Larsen RG, Halkides CJ, Redfield AG, Singel DJ. Electron spin-echo envelope modulation spectroscopy of Mn2+.cntdot.GDP complexes of N-ras p21 with selective nitrogen-15 labeling Journal of the American Chemical Society. 114: 9608-9611. DOI: 10.1021/Ja00050A047 |
0.327 |
|
| 1991 |
Lowry DF, Cool RH, Redfield AG, Parmeggiani A. NMR study of the phosphate-binding elements of Escherichia coli elongation factor Tu catalytic domain. Biochemistry. 30: 10872-7. PMID 1932010 DOI: 10.1021/Bi00109A010 |
0.424 |
|
| 1991 |
Redfield AG. On the upper bound of spin polarization transfer Journal of Magnetic Resonance (1969). 92: 642-644. DOI: 10.1016/0022-2364(91)90363-X |
0.324 |
|
| 1990 |
McIntosh LP, Wand AJ, Lowry DF, Redfield AG, Dahlquist FW. Assignment of the backbone 1H and 15N NMR resonances of bacteriophage T4 lysozyme. Biochemistry. 29: 6341-62. PMID 2207079 DOI: 10.1021/Bi00479A003 |
0.393 |
|
| 1990 |
Redfield AG, Papastavros MZ. NMR study of the phosphoryl binding loop in purine nucleotide proteins: evidence for strong hydrogen bonding in human N-ras p21. Biochemistry. 29: 3509-14. PMID 2191717 DOI: 10.1021/Bi00466A013 |
0.393 |
|
| 1990 |
Massefski W, Redfield AG, Hare DR, Miller C. Molecular structure of charybdotoxin, a pore-directed inhibitor of potassium ion channels. Science (New York, N.Y.). 249: 521-4. PMID 1696395 DOI: 10.1126/Science.1696395 |
0.343 |
|
| 1990 |
Massefski W, Redfield A, Das Sarma U, Bannerji A, Roy S. [7-15N]guanosine-labeled oligonucleotides as nuclear magnetic resonance probes for protein-nucleic acid interaction in the major groove Journal of the American Chemical Society. 112: 5350-5351. DOI: 10.1021/Ja00169A052 |
0.395 |
|
| 1989 |
Hall KB, Sampson JR, Uhlenbeck OC, Redfield AG. Structure of an unmodified tRNA molecule. Biochemistry. 28: 5794-801. PMID 2775736 DOI: 10.1021/Bi00440A014 |
0.325 |
|
| 1989 |
Burk SC, Papastavros MZ, McCormick F, Redfield AG. Identification of resonances from an oncogenic activating locus of human N-RAS-encoded p21 protein using isotope-edited NMR. Proceedings of the National Academy of Sciences of the United States of America. 86: 817-20. PMID 2644645 DOI: 10.1073/Pnas.86.3.817 |
0.423 |
|
| 1989 |
Redfield AG, McIntosh LP, Dahlquist FW. Use of 13C and 15N isotope labels for proton nuclear magnetic resonance and nuclear Overhauser effect. Structural and dynamic studies of larger proteins and nucleic acids. Archivos De Biología Y Medicina Experimentales. 22: 129-37. PMID 2619316 |
0.353 |
|
| 1988 |
Lowry DF, Redfield AG, McIntosh LP, Dahlquist FW. One-dimensional Nuclear Overhauser Effect with two-dimensional heteronuclear multiple quantum coherence detection: Proton-proton nitrogen-15 correlation in T4 lysozyme Journal of the American Chemical Society. 110: 6885-6886. DOI: 10.1021/Ja00228A048 |
0.326 |
|
| 1988 |
Massefski W, Redfield AG. Elimination of multiple-step spin diffusion effects in two-dimensional NOE spectroscopy of nucleic acids Journal of Magnetic Resonance (1969). 78: 150-155. DOI: 10.1016/0022-2364(88)90166-7 |
0.324 |
|
| 1987 |
McIntosh LP, Dahlquist FW, Redfield AG. Proton NMR and NOE structural and dynamic studies of larger proteins and nucleic acids aided by isotope labels: T4 lysozyme. Journal of Biomolecular Structure & Dynamics. 5: 21-34. PMID 3271466 DOI: 10.1080/07391102.1987.10506372 |
0.43 |
|
| 1987 |
McIntosh LP, Griffey RH, Muchmore DC, Nielson CP, Redfield AG, Dahlquist FW. Proton NMR measurements of bacteriophage T4 lysozyme aided by 15N isotopic labeling: structural and dynamic studies of larger proteins. Proceedings of the National Academy of Sciences of the United States of America. 84: 1244-8. PMID 3029773 DOI: 10.1073/Pnas.84.5.1244 |
0.428 |
|
| 1987 |
Griffey RH, Redfield AG. Proton-detected heteronuclear edited and correlated nuclear magnetic resonance and nuclear Overhauser effect in solution. Quarterly Reviews of Biophysics. 19: 51-82. PMID 2819934 DOI: 10.1017/S0033583500004029 |
0.403 |
|
| 1986 |
Choi BS, Redfield AG. NMR study of isoleucine transfer RNA from Thermus thermophilus. Biochemistry. 25: 1529-34. PMID 3635410 DOI: 10.1021/Bi00355A010 |
0.346 |
|
| 1986 |
Griffey RH, Redfield AG, McIntosh LP, Oas TG, Dahlquist FW. Assignment of proton amide resonances of T4 lysozyme by carbon-13 and nitrogen-15 multiple isotopic labeling Journal of the American Chemical Society. 108: 6816-6817. DOI: 10.1021/Ja00281A066 |
0.354 |
|
| 1985 |
Ralph EK, Lange Y, Redfield AG. Kinetics of proton exchange of phosphatidylethanolamine in phospholipid vesicles. Biophysical Journal. 48: 1053-7. PMID 4092067 DOI: 10.1016/S0006-3495(85)83868-6 |
0.346 |
|
| 1985 |
Griffey RH, Redfield AG, Loomis RE, Dahlquist FW. Nuclear magnetic resonance observation and dynamics of specific amide protons in T4 lysozyme. Biochemistry. 24: 817-22. PMID 3888265 DOI: 10.1021/Bi00325A001 |
0.479 |
|
| 1985 |
Choi BS, Redfield AG. Nuclear magnetic resonance observation of the triple interaction between A9 and AU12 in yeast tRNAPhe. Nucleic Acids Research. 13: 5249-54. PMID 3848815 DOI: 10.1093/Nar/13.14.5249 |
0.359 |
|
| 1985 |
Griffey RH, Redfield AG. Identification of isotope-labeled resonances in two-dimensional proton-proton correlation and exchange spectroscopy with gated heteronuclear decoupling Journal of Magnetic Resonance (1969). 65: 344-347. DOI: 10.1016/0022-2364(85)90016-2 |
0.42 |
|
| 1985 |
Griffey RH, Jarema MA, Kunz S, Rosevear PR, Redfield AG. Isotopic-label-directed observation of the nuclear Overhauser effect in poorly resolved proton NMR spectra Journal of the American Chemical Society. 107: 711-712. DOI: 10.1002/Chin.198524045 |
0.41 |
|
| 1984 |
Roy S, Papastavros MZ, Sanchez V, Redfield AG. Nitrogen-15-labeled yeast tRNAPhe: double and two-dimensional heteronuclear NMR of guanosine and uracil ring NH groups. Biochemistry. 23: 4395-400. PMID 6567469 DOI: 10.1021/Bi00314A024 |
0.409 |
|
| 1983 |
Tropp JS, Redfield AG. Proton exchange rates in transfer RNA as a function of spermidine and magnesium. Nucleic Acids Research. 11: 2121-34. PMID 6340067 DOI: 10.1093/Nar/11.7.2121 |
0.33 |
|
| 1983 |
Roy S, Redfield AG. Assignment of imino proton spectra of yeast phenylalanine transfer ribonucleic acid. Biochemistry. 22: 1386-90. PMID 6301547 DOI: 10.1021/Bi00275A010 |
0.442 |
|
| 1983 |
Redfield AG. Stimulated echo NMR spectra and their use for heteronuclear two-dimensional shift correlation Chemical Physics Letters. 96: 537-540. DOI: 10.1016/0009-2614(83)80443-6 |
0.323 |
|
| 1982 |
Roy S, Papastavros MZ, Redfield AG. Procedure for C2 deuteration of nucleic acids and determination of A psi 31 pseudouridine conformation by nuclear Overhauser effect in yeast tRNAPhe. Nucleic Acids Research. 10: 8341-9. PMID 6761652 DOI: 10.1093/Nar/10.24.8341 |
0.347 |
|
| 1982 |
Schejter E, Roy S, Sánchez V, Redfield AG. Nuclear Overhauser effect study of yeast tRNAVal 1: evidence for uridine-pseudouridine base pairing. Nucleic Acids Research. 10: 8297-305. PMID 6761651 DOI: 10.1093/Nar/10.24.8297 |
0.397 |
|
| 1982 |
Roy S, Papastavros MZ, Redfield AG. Nuclear overhauser effect study of yeast aspartate transfer ribonucleic acid. Biochemistry. 21: 6081-8. PMID 6758844 DOI: 10.1021/Bi00267A009 |
0.383 |
|
| 1981 |
Johnston PD, Redfield AG. Study of transfer ribonucleic acid unfolding by dynamic nuclear magnetic resonance. Biochemistry. 20: 3996-4006. PMID 7025889 DOI: 10.1021/Bi00517A008 |
0.442 |
|
| 1981 |
Johnston PD, Redfield AG. Nuclear magnetic resonance and nuclear Overhauser effect study of yeast phenylalanine transfer ribonucleic acid imino protons. Biochemistry. 20: 1147-56. PMID 7013786 DOI: 10.1021/Bi00508A016 |
0.452 |
|
| 1981 |
Roy S, Redfield AG. Nuclear Overhauser effect study and assignment of D stem and reverse-Hoogsteen base pair proton resonances in yeast tRNAAsp. Nucleic Acids Research. 9: 7073-83. PMID 6278454 DOI: 10.1093/Nar/9.24.7073 |
0.39 |
|
| 1980 |
Sánchez V, Redfield AG, Johnston PD, Tropp J. Nuclear Overhauser effect in specifically deuterated macromolecules: NMR assay for unusual base pairing in transfer RNA. Proceedings of the National Academy of Sciences of the United States of America. 77: 5659-62. PMID 7003592 DOI: 10.1073/Pnas.77.10.5659 |
0.437 |
|
| 1980 |
Tropp J, Redfield AG. Proton magnetic resonance of NADH in water-methanol mixtures. Conformational change and behavior of exchangeable proton resonances as a function of temperature Journal of the American Chemical Society. 102: 534-538. DOI: 10.1021/Ja00522A016 |
0.404 |
|
| 1979 |
Johnston PD, Figueroa N, Redfield AG. Real-time solvent exchange studies of the imino and amino protons of yeast phenylalanine transfer RNA by Fourier transform NMR. Proceedings of the National Academy of Sciences of the United States of America. 76: 3130-4. PMID 386331 DOI: 10.1073/pnas.76.7.3130 |
0.312 |
|
| 1979 |
Stoesz JD, Malinowski DP, Redfield AG. Nuclear magnetic resonance study of solvent exchange and nuclear Overhauser effect of the histidine protons of bovine superoxide dismutase. Biochemistry. 18: 4669-75. PMID 40594 DOI: 10.1021/Bi00588A030 |
0.428 |
|
| 1979 |
Johnston PD, Redfield AG. Proton FT NMR Studies of tRNA Structure and Dynamics Cold Spring Harbor Monograph Archive. 191-206. DOI: 10.1101/087969128.9A.191 |
0.369 |
|
| 1978 |
Stoesz JD, Redfield AG. Cross relaxation and spin diffusion effects on the proton NMR of biopolymers in H2O. Solvent saturation and chemical exchange in superoxide dismutase. Febs Letters. 91: 320-4. PMID 680139 DOI: 10.1016/0014-5793(78)81201-0 |
0.382 |
|
| 1978 |
Johnston PD, Redfield AG. Pulsed FT-NMR double resonance studies of yeast tRNAPhe: specific nuclear Overhauser effects and reinterpretation of low temperature relaxation data. Nucleic Acids Research. 5: 3913-27. PMID 364421 DOI: 10.1093/Nar/5.10.3913 |
0.458 |
|
| 1977 |
Johnston PD, Redfield AG. An NMR study of the exchange rates for protons involved in the secondary and tertiary structure of yeast tRNA Phe. Nucleic Acids Research. 4: 3599-615. PMID 337239 DOI: 10.1093/Nar/4.10.3599 |
0.408 |
|
| 1977 |
Waelder SF, Redfield AG. Nuclear magnetic resonance studies of exchangeable protons. II. The solvent exchange rate of the indole nitrogen proton of tryptophan derivatives. Biopolymers. 16: 623-9. PMID 14742 DOI: 10.1002/Bip.1977.360160311 |
0.409 |
|
| 1975 |
Lange Y, Ralph EK, Redfield AG. Observation of the phosphatidyl ethanolamine amino proton magnetic resonance in phospholipid vesicles: inside/outside ratios and proton transport. Biochemical and Biophysical Research Communications. 62: 891-4. PMID 1168058 DOI: 10.1016/0006-291X(75)90406-4 |
0.412 |
|
| 1975 |
Waelder S, Lee L, Redfield AG. Letter: Nuclear magnetic resonance studies of exchangeable protons. I. Fourier transform saturation-recovery and transfer of saturation of the tryptophan indole nitrogen proton. Journal of the American Chemical Society. 97: 2927-8. PMID 1133343 DOI: 10.1021/Ja00843A066 |
0.42 |
|
| 1975 |
Genack AZ, Redfield AG. Theory of nuclear spin diffusion in a spatially varying magnetic field Physical Review B. 12: 78-87. DOI: 10.1103/Physrevb.12.78 |
0.522 |
|
| 1975 |
Redfield AG, Kunz SD, Ralph EK. Dynamic range in Fourier transform proton magnetic resonance Journal of Magnetic Resonance (1969). 19: 114-117. DOI: 10.1016/0022-2364(75)90035-9 |
0.38 |
|
| 1975 |
WAELDER S, LEE L, REDFIELD AG. ChemInform Abstract: NUCLEAR MAGNETIC RESONANCE STUDIES OF EXCHANGEABLE PROTONS PART 1, FOURIER TRANSFORM SATURATION-RECOVERY AND TRANSFER OF SATURATION OF THE TRYPTOPHAN INDOLE NITROGEN PROTON Chemischer Informationsdienst. 6: no-no. DOI: 10.1002/Chin.197530063 |
0.422 |
|
| 1974 |
Bell RM, Parsons SM, Dubravac SA, Redfield AG, Koshland DE. Characterization of slowly interconvertible states of phosphoribosyladenosine triphosphate synthetase dependent on temperature, substrates, and histidine. The Journal of Biological Chemistry. 249: 4110-8. PMID 4368489 |
0.34 |
|
| 1973 |
Genack AZ, Redfield AG. Nuclear spin diffusion and its thermodynamic quenching in the field gradients of a Type-II superconductor Physical Review Letters. 31: 1204-1207. DOI: 10.1103/Physrevlett.31.1204 |
0.521 |
|
| 1970 |
Gupta RK, Redfield AG. Double nuclear magnetic resonance observation of electron exchange between ferri- and ferrocytochrome c. Science (New York, N.Y.). 169: 1204-6. PMID 5450695 DOI: 10.1126/science.169.3951.1204 |
0.315 |
|
| 1969 |
Redfield AG. Nuclear spin thermodynamics in the rotating frame. Science (New York, N.Y.). 164: 1015-23. PMID 17796604 DOI: 10.1126/Science.164.3883.1015 |
0.319 |
|
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