Difference between revisions of "Citations"
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(Fix for the Sun et al., 2011 reference tags.) |
(Shifted the year parameter in all references to its position in the {{citation}} template.) |
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* <section begin=Bieri11/>{{citation | * <section begin=Bieri11/>{{citation | ||
| authors = Bieri, M., d'Auvergne, E., and Gooley, P. | | authors = Bieri, M., d'Auvergne, E., and Gooley, P. | ||
| − | |||
| title = relaxGUI: a new software for fast and simple NMR relaxation data analysis and calculation of ps-ns and μs motion of proteins. | | title = relaxGUI: a new software for fast and simple NMR relaxation data analysis and calculation of ps-ns and μs motion of proteins. | ||
| journal = J. Biomol. NMR | | journal = J. Biomol. NMR | ||
| Line 32: | Line 31: | ||
| page_start = 147 | | page_start = 147 | ||
| page_end = 155 | | page_end = 155 | ||
| + | | year = 2011 | ||
| doi = 10.1007/s10858-011-9509-1 | | doi = 10.1007/s10858-011-9509-1 | ||
}}<section end=Bieri11/> | }}<section end=Bieri11/> | ||
| Line 37: | Line 37: | ||
* <section begin=CarverRichards72/>{{citation | * <section begin=CarverRichards72/>{{citation | ||
| authors = Carver, J. P. and Richards, R. E. | | authors = Carver, J. P. and Richards, R. E. | ||
| − | |||
| title = General 2-site solution for chemical exchange produced dependence of T2 upon Carr-Purcell pulse separation. | | title = General 2-site solution for chemical exchange produced dependence of T2 upon Carr-Purcell pulse separation. | ||
| journal = J. Magn. Reson. | | journal = J. Magn. Reson. | ||
| Line 44: | Line 43: | ||
| page_start = 89 | | page_start = 89 | ||
| page_end = 105 | | page_end = 105 | ||
| + | | year = 1972 | ||
| doi = 10.1016/0022-2364(72)90090-X | | doi = 10.1016/0022-2364(72)90090-X | ||
}}<section end=CarverRichards72/> | }}<section end=CarverRichards72/> | ||
| Line 49: | Line 49: | ||
* <section begin=Clore90/>{{citation | * <section begin=Clore90/>{{citation | ||
| authors = Clore, G. M., Szabo, A., Bax, A., Kay, L. E., Driscoll, P. C., and Gronenborn, A. M. | | authors = Clore, G. M., Szabo, A., Bax, A., Kay, L. E., Driscoll, P. C., and Gronenborn, A. M. | ||
| − | |||
| title = Deviations from the simple 2-parameter model-free approach to the interpretation of N-15 nuclear magnetic-relaxation of proteins. | | title = Deviations from the simple 2-parameter model-free approach to the interpretation of N-15 nuclear magnetic-relaxation of proteins. | ||
| journal = J. Am. Chem. Soc. | | journal = J. Am. Chem. Soc. | ||
| Line 56: | Line 55: | ||
| page_start = 4989 | | page_start = 4989 | ||
| page_end = 4991 | | page_end = 4991 | ||
| + | | year = 1990 | ||
| doi = 10.1021/ja00168a070 | | doi = 10.1021/ja00168a070 | ||
}}<section end=Clore90/> | }}<section end=Clore90/> | ||
| Line 72: | Line 72: | ||
* <section begin=dAuvergneGooley03/>{{citation | * <section begin=dAuvergneGooley03/>{{citation | ||
| authors = d'Auvergne, E. J. and Gooley, P. R. | | authors = d'Auvergne, E. J. and Gooley, P. R. | ||
| − | |||
| title = The use of model selection in the model-free analysis of protein dynamics. | | title = The use of model selection in the model-free analysis of protein dynamics. | ||
| journal = J. Biomol. NMR | | journal = J. Biomol. NMR | ||
| Line 79: | Line 78: | ||
| page_start = 25 | | page_start = 25 | ||
| page_end = 39 | | page_end = 39 | ||
| + | | year = 2003 | ||
| doi = 10.1023/a:1021902006114 | | doi = 10.1023/a:1021902006114 | ||
}}<section end=dAuvergneGooley03/> | }}<section end=dAuvergneGooley03/> | ||
| Line 84: | Line 84: | ||
* <section begin=dAuvergneGooley06/>{{citation | * <section begin=dAuvergneGooley06/>{{citation | ||
| authors = d'Auvergne, E. J. and Gooley, P. R. | | authors = d'Auvergne, E. J. and Gooley, P. R. | ||
| − | |||
| title = Model-free model elimination: A new step in the model-free dynamic analysis of NMR relaxation data. | | title = Model-free model elimination: A new step in the model-free dynamic analysis of NMR relaxation data. | ||
| journal = J. Biomol. NMR | | journal = J. Biomol. NMR | ||
| Line 91: | Line 90: | ||
| page_start = 117 | | page_start = 117 | ||
| page_end = 135 | | page_end = 135 | ||
| + | | year = 2006 | ||
| doi = 10.1007/s10858-006-9007-z | | doi = 10.1007/s10858-006-9007-z | ||
}}<section end=dAuvergneGooley06/> | }}<section end=dAuvergneGooley06/> | ||
| Line 96: | Line 96: | ||
* <section begin=dAuvergneGooley07/>{{citation | * <section begin=dAuvergneGooley07/>{{citation | ||
| authors = d'Auvergne, E. J. and Gooley, P. R. | | authors = d'Auvergne, E. J. and Gooley, P. R. | ||
| − | |||
| title = Set theory formulation of the model-free problem and the diffusion seeded model-free paradigm. | | title = Set theory formulation of the model-free problem and the diffusion seeded model-free paradigm. | ||
| journal = Mol. BioSyst. | | journal = Mol. BioSyst. | ||
| Line 103: | Line 102: | ||
| page_start = 483 | | page_start = 483 | ||
| page_end = 494 | | page_end = 494 | ||
| + | | year = 2007 | ||
| doi = 10.1039/b702202f | | doi = 10.1039/b702202f | ||
}}<section end=dAuvergneGooley07/> | }}<section end=dAuvergneGooley07/> | ||
| Line 108: | Line 108: | ||
* <section begin=dAuvergneGooley08a/>{{citation | * <section begin=dAuvergneGooley08a/>{{citation | ||
| authors = d'Auvergne, E. J. and Gooley, P. R. | | authors = d'Auvergne, E. J. and Gooley, P. R. | ||
| − | |||
| title = Optimisation of NMR dynamic models I. Minimisation algorithms and their performance within the model-free and Brownian rotational diffusion spaces. | | title = Optimisation of NMR dynamic models I. Minimisation algorithms and their performance within the model-free and Brownian rotational diffusion spaces. | ||
| journal = J. Biomol. NMR | | journal = J. Biomol. NMR | ||
| Line 115: | Line 114: | ||
| page_start = 107 | | page_start = 107 | ||
| page_end = 119 | | page_end = 119 | ||
| + | | year = 2008 | ||
| doi = 10.1007/s10858-007-9214-2 | | doi = 10.1007/s10858-007-9214-2 | ||
}}<section end=dAuvergneGooley08a/> | }}<section end=dAuvergneGooley08a/> | ||
| Line 120: | Line 120: | ||
* <section begin=dAuvergneGooley08b/>{{citation | * <section begin=dAuvergneGooley08b/>{{citation | ||
| authors = d'Auvergne, E. J. and Gooley, P. R. | | authors = d'Auvergne, E. J. and Gooley, P. R. | ||
| − | |||
| title = Optimisation of NMR dynamic models II. A new methodology for the dual optimisation of the model-free parameters and the Brownian rotational diffusion tensor. | | title = Optimisation of NMR dynamic models II. A new methodology for the dual optimisation of the model-free parameters and the Brownian rotational diffusion tensor. | ||
| journal = J. Biomol. NMR | | journal = J. Biomol. NMR | ||
| Line 127: | Line 126: | ||
| page_start = 121 | | page_start = 121 | ||
| page_end = 133 | | page_end = 133 | ||
| + | | year = 2008 | ||
| doi = 10.1007/s10858-007-9213-3 | | doi = 10.1007/s10858-007-9213-3 | ||
}}<section end=dAuvergneGooley08b/> | }}<section end=dAuvergneGooley08b/> | ||
| Line 132: | Line 132: | ||
* <section begin=dAuvergneGooley08c/>{{citation | * <section begin=dAuvergneGooley08c/>{{citation | ||
| authors = d'Auvergne, E. J. and Gooley, P. R. | | authors = d'Auvergne, E. J. and Gooley, P. R. | ||
| − | |||
| title = Optimisation of NMR dynamic models. | | title = Optimisation of NMR dynamic models. | ||
| journal = J. Biomol. NMR | | journal = J. Biomol. NMR | ||
| Line 139: | Line 138: | ||
| page_start = 107 | | page_start = 107 | ||
| page_end = 133 | | page_end = 133 | ||
| + | | year = 2008 | ||
| doi = 10.1007/s10858-007-9214-2 | | doi = 10.1007/s10858-007-9214-2 | ||
| doi2 = 10.1007/s10858-007-9213-3 | | doi2 = 10.1007/s10858-007-9213-3 | ||
| Line 145: | Line 145: | ||
* <section begin=Davis94/>{{citation | * <section begin=Davis94/>{{citation | ||
| authors = Davis, D. G., Perlman, M. E., and London, R. E. | | authors = Davis, D. G., Perlman, M. E., and London, R. E. | ||
| − | |||
| title = Direct measurements of the dissociation-rate constant for inhibitor-enzyme complexes via the T1rho and T2 (CPMG) methods. | | title = Direct measurements of the dissociation-rate constant for inhibitor-enzyme complexes via the T1rho and T2 (CPMG) methods. | ||
| journal = J. Magn. Reson. | | journal = J. Magn. Reson. | ||
| Line 152: | Line 151: | ||
| page_start = 266 | | page_start = 266 | ||
| page_end = 275 | | page_end = 275 | ||
| + | | year = 1994 | ||
| doi = 10.1006/jmrb.1994.1084 | | doi = 10.1006/jmrb.1994.1084 | ||
}}<section end=Davis94/> | }}<section end=Davis94/> | ||
| Line 181: | Line 181: | ||
* <section begin=Farrow94/>{{citation | * <section begin=Farrow94/>{{citation | ||
| authors = Farrow, N. A., Muhandiram, R., Singer, A. U., Pascal, S. M., Kay, C. M., Gish, G., Shoelson, S. E., Pawson, T., Forman-Kay, J. D., Kay, L. E. | | authors = Farrow, N. A., Muhandiram, R., Singer, A. U., Pascal, S. M., Kay, C. M., Gish, G., Shoelson, S. E., Pawson, T., Forman-Kay, J. D., Kay, L. E. | ||
| − | |||
| title = Backbone dynamics of a free and phosphopeptide-complexed Src homology 2 domain studied by 15N NMR relaxation. | | title = Backbone dynamics of a free and phosphopeptide-complexed Src homology 2 domain studied by 15N NMR relaxation. | ||
| journal = Biochemistry | | journal = Biochemistry | ||
| Line 188: | Line 187: | ||
| page_start = 5984 | | page_start = 5984 | ||
| page_end = 6003 | | page_end = 6003 | ||
| + | | year = 1994 | ||
| doi = 10.1021/bi00185a040 | | doi = 10.1021/bi00185a040 | ||
}}<section end=Farrow94/> | }}<section end=Farrow94/> | ||
| Line 193: | Line 193: | ||
* <section begin=Fushman98/>{{citation | * <section begin=Fushman98/>{{citation | ||
| authors = Fushman, D., Tjandra, N., and Cowburn, D. | | authors = Fushman, D., Tjandra, N., and Cowburn, D. | ||
| − | |||
| title = Direct measurement of <sup>15</sup>N chemical shift anisotropy in solution. | | title = Direct measurement of <sup>15</sup>N chemical shift anisotropy in solution. | ||
| journal = J. Am. Chem. Soc. | | journal = J. Am. Chem. Soc. | ||
| Line 200: | Line 199: | ||
| page_start = 10947 | | page_start = 10947 | ||
| page_end = 10952 | | page_end = 10952 | ||
| + | | year = 1998 | ||
| doi = 10.1021/ja981686m | | doi = 10.1021/ja981686m | ||
}}<section end=Fushman98/> | }}<section end=Fushman98/> | ||
| Line 217: | Line 217: | ||
* <section begin=IshimaTorchia99/>{{citation | * <section begin=IshimaTorchia99/>{{citation | ||
| authors = Ishima, R. and Torchia, D. A. | | authors = Ishima, R. and Torchia, D. A. | ||
| − | |||
| title = Estimating the time scale of chemical exchange of proteins from measurements of transverse relaxation rates in solution. | | title = Estimating the time scale of chemical exchange of proteins from measurements of transverse relaxation rates in solution. | ||
| journal = J. Biomol. NMR | | journal = J. Biomol. NMR | ||
| Line 224: | Line 223: | ||
| page_start = 369 | | page_start = 369 | ||
| page_end = 372 | | page_end = 372 | ||
| + | | year = 1999 | ||
| doi = 10.1023/A:1008324025406 | | doi = 10.1023/A:1008324025406 | ||
}}<section end=IshimaTorchia99/> | }}<section end=IshimaTorchia99/> | ||
| Line 229: | Line 229: | ||
* <section begin=IshimaTorchia05/>{{citation | * <section begin=IshimaTorchia05/>{{citation | ||
| authors = Ishima, R. and Torchia, D. A. | | authors = Ishima, R. and Torchia, D. A. | ||
| − | |||
| title = Error estimation and global fitting in transverse-relaxation dispersion experiments to determine chemical-exchange parameters. | | title = Error estimation and global fitting in transverse-relaxation dispersion experiments to determine chemical-exchange parameters. | ||
| journal = J. Biomol. NMR | | journal = J. Biomol. NMR | ||
| Line 236: | Line 235: | ||
| page_start = 41 | | page_start = 41 | ||
| page_end = 54 | | page_end = 54 | ||
| + | | year = 2005 | ||
| doi = 10.1007/s10858-005-3593-z | | doi = 10.1007/s10858-005-3593-z | ||
}}<section end=IshimaTorchia99/> | }}<section end=IshimaTorchia99/> | ||
| Line 252: | Line 252: | ||
* <section begin=Korzhnev04a/>{{citation | * <section begin=Korzhnev04a/>{{citation | ||
| authors = Korzhnev, D. M., Kloiber, K., Kanelis, V., Tugarinov, V., and Kay, L. E. | | authors = Korzhnev, D. M., Kloiber, K., Kanelis, V., Tugarinov, V., and Kay, L. E. | ||
| − | |||
| title = Probing slow dynamics in high molecular weight proteins by methyl-TROSY NMR spectroscopy: application to a 723-residue enzyme. | | title = Probing slow dynamics in high molecular weight proteins by methyl-TROSY NMR spectroscopy: application to a 723-residue enzyme. | ||
| journal = J. Am. Chem. Soc. | | journal = J. Am. Chem. Soc. | ||
| Line 259: | Line 258: | ||
| page_start = 3964 | | page_start = 3964 | ||
| page_end = 3973 | | page_end = 3973 | ||
| + | | year = 2004 | ||
| doi = 10.1021/ja039587i | | doi = 10.1021/ja039587i | ||
}}<section end=Korzhnev04a/> | }}<section end=Korzhnev04a/> | ||
| Line 264: | Line 264: | ||
* <section begin=Korzhnev04b/>{{citation | * <section begin=Korzhnev04b/>{{citation | ||
| authors = Korzhnev, D. M., Kloiber, K., and Kay, L. E. | | authors = Korzhnev, D. M., Kloiber, K., and Kay, L. E. | ||
| − | |||
| title = Multiple-quantum relaxation dispersion NMR spectroscopy probing millisecond time-scale dynamics in proteins: theory and application. | | title = Multiple-quantum relaxation dispersion NMR spectroscopy probing millisecond time-scale dynamics in proteins: theory and application. | ||
| journal = J. Am. Chem. Soc. | | journal = J. Am. Chem. Soc. | ||
| Line 271: | Line 270: | ||
| page_start = 7320 | | page_start = 7320 | ||
| page_end = 7329 | | page_end = 7329 | ||
| + | | year = 2004 | ||
| doi = 10.1021/ja049968b | | doi = 10.1021/ja049968b | ||
}}<section end=Korzhnev04b/> | }}<section end=Korzhnev04b/> | ||
| Line 276: | Line 276: | ||
* <section begin=Korzhnev05a/>{{citation | * <section begin=Korzhnev05a/>{{citation | ||
| authors = Korzhnev, D. M., Neudecker, P., Mittermaier, A., Orekhov, V. Y., and Kay, L. E. | | authors = Korzhnev, D. M., Neudecker, P., Mittermaier, A., Orekhov, V. Y., and Kay, L. E. | ||
| − | |||
| title = Multiple-site exchange in proteins studied with a suite of six NMR relaxation dispersion experiments: an application to the folding of a Fyn SH3 domain mutant. | | title = Multiple-site exchange in proteins studied with a suite of six NMR relaxation dispersion experiments: an application to the folding of a Fyn SH3 domain mutant. | ||
| journal = J. Am. Chem. Soc. | | journal = J. Am. Chem. Soc. | ||
| Line 283: | Line 282: | ||
| page_start = 15602 | | page_start = 15602 | ||
| page_end = 15611 | | page_end = 15611 | ||
| + | | year = 2005 | ||
| doi = 10.1021/ja054550e | | doi = 10.1021/ja054550e | ||
}}<section end=Korzhnev05a/> | }}<section end=Korzhnev05a/> | ||
| Line 288: | Line 288: | ||
* <section begin=Korzhnev05b/>{{citation | * <section begin=Korzhnev05b/>{{citation | ||
| authors = Korzhnev, D. M., Orekhov, V. Y., and Kay, L. E. | | authors = Korzhnev, D. M., Orekhov, V. Y., and Kay, L. E. | ||
| − | |||
| title = Off-resonance R(1rho) NMR studies of exchange dynamics in proteins with low spin-lock fields: an application to a Fyn SH3 domain. | | title = Off-resonance R(1rho) NMR studies of exchange dynamics in proteins with low spin-lock fields: an application to a Fyn SH3 domain. | ||
| journal = J. Am. Chem. Soc. | | journal = J. Am. Chem. Soc. | ||
| Line 295: | Line 294: | ||
| page_start = 713 | | page_start = 713 | ||
| page_end = 721 | | page_end = 721 | ||
| + | | year = 2005 | ||
| doi = 10.1021/ja0446855 | | doi = 10.1021/ja0446855 | ||
}}<section end=Korzhnev05b/> | }}<section end=Korzhnev05b/> | ||
| Line 324: | Line 324: | ||
* <section begin=LuzMeiboom63/>{{citation | * <section begin=LuzMeiboom63/>{{citation | ||
| authors = Luz, Z. and Meiboom, S. | | authors = Luz, Z. and Meiboom, S. | ||
| − | |||
| title = Nuclear magnetic resonance study of protolysis of trimethylammonium ion in aqueous solution - order of reaction with respect to solvent. | | title = Nuclear magnetic resonance study of protolysis of trimethylammonium ion in aqueous solution - order of reaction with respect to solvent. | ||
| journal = J. Chem. Phys. | | journal = J. Chem. Phys. | ||
| Line 331: | Line 330: | ||
| page_start = 366 | | page_start = 366 | ||
| page_end = 370 | | page_end = 370 | ||
| + | | year = 1963 | ||
| doi = 10.1063/1.1734254 | | doi = 10.1063/1.1734254 | ||
}}<section end=LuzMeiboom63/> | }}<section end=LuzMeiboom63/> | ||
| Line 348: | Line 348: | ||
* <section begin=Meiboom61/>{{citation | * <section begin=Meiboom61/>{{citation | ||
| authors = Meiboom, S. | | authors = Meiboom, S. | ||
| − | |||
| title = Nuclear magnetic resonance study of proton transfer in water. | | title = Nuclear magnetic resonance study of proton transfer in water. | ||
| journal = J. Chem. Phys. | | journal = J. Chem. Phys. | ||
| Line 355: | Line 354: | ||
| page_start = 375 | | page_start = 375 | ||
| page_end = 388 | | page_end = 388 | ||
| + | | year = 1961 | ||
| doi = 10.1063/1.1700960 | | doi = 10.1063/1.1700960 | ||
}}<section end=Meiboom61/> | }}<section end=Meiboom61/> | ||
| Line 360: | Line 360: | ||
* <section begin=MiloushevPalmer05/>{{citation | * <section begin=MiloushevPalmer05/>{{citation | ||
| authors = Miloushev, V. Z. and Palmer, 3rd, A. G. | | authors = Miloushev, V. Z. and Palmer, 3rd, A. G. | ||
| − | |||
| title = R(1rho) relaxation for two-site chemical exchange: general approximations and some exact solutions. | | title = R(1rho) relaxation for two-site chemical exchange: general approximations and some exact solutions. | ||
| journal = J. Magn. Reson. | | journal = J. Magn. Reson. | ||
| Line 367: | Line 366: | ||
| page_start = 221 | | page_start = 221 | ||
| page_end = 227 | | page_end = 227 | ||
| + | | year = 2005 | ||
| doi = 10.1016/j.jmr.2005.07.023 | | doi = 10.1016/j.jmr.2005.07.023 | ||
}}<section end=MiloushevPalmer05/> | }}<section end=MiloushevPalmer05/> | ||
| Line 372: | Line 372: | ||
* <section begin=MorinGagné09/>{{citation | * <section begin=MorinGagné09/>{{citation | ||
| authors = Morin, S. and Gagné, S. | | authors = Morin, S. and Gagné, S. | ||
| − | |||
| title = Simple tests for the validation of multiple field spin relaxation data. | | title = Simple tests for the validation of multiple field spin relaxation data. | ||
| journal = J. Biomol. NMR | | journal = J. Biomol. NMR | ||
| Line 378: | Line 377: | ||
| page_start = 361 | | page_start = 361 | ||
| page_end = 372 | | page_end = 372 | ||
| + | | year = 2009 | ||
| doi = 10.1007/s10858-009-9381-4 | | doi = 10.1007/s10858-009-9381-4 | ||
}}<section end=MorinGagné09/> | }}<section end=MorinGagné09/> | ||
| Line 383: | Line 383: | ||
* <section begin=Morin14/>{{citation | * <section begin=Morin14/>{{citation | ||
| authors = Morin, S., Linnet, T. E., Lescanne, M., Schanda, P., Thompson, G. S., Tollinger, M., Teilum, K., Gagné, S., Marion, D., Griesinger, C., Blackledge, M., and d'Auvergne, E. J. | | authors = Morin, S., Linnet, T. E., Lescanne, M., Schanda, P., Thompson, G. S., Tollinger, M., Teilum, K., Gagné, S., Marion, D., Griesinger, C., Blackledge, M., and d'Auvergne, E. J. | ||
| − | |||
| title = relax: the analysis of biomolecular kinetics and thermodynamics using NMR relaxation dispersion data. | | title = relax: the analysis of biomolecular kinetics and thermodynamics using NMR relaxation dispersion data. | ||
| journal = Bioinformatics | | journal = Bioinformatics | ||
| Line 390: | Line 389: | ||
| page_start = 2219 | | page_start = 2219 | ||
| page_end = 2220 | | page_end = 2220 | ||
| + | | year = 2014 | ||
| doi = 10.1093/bioinformatics/btu166 | | doi = 10.1093/bioinformatics/btu166 | ||
}}<section end=Morin14/> | }}<section end=Morin14/> | ||
| Line 407: | Line 407: | ||
* <section begin=Orekhov99/>{{citation | * <section begin=Orekhov99/>{{citation | ||
| authors = Orekhov, V. Y., Korzhnev, D. M., Diercks, T., Kessler, H., and Arseniev, A. S. | | authors = Orekhov, V. Y., Korzhnev, D. M., Diercks, T., Kessler, H., and Arseniev, A. S. | ||
| − | |||
| title = H-1-N-15 NMR dynamic study of an isolated alpha-helical peptide (1-36)bacteriorhodopsin reveals the equilibrium helix-coil transitions. | | title = H-1-N-15 NMR dynamic study of an isolated alpha-helical peptide (1-36)bacteriorhodopsin reveals the equilibrium helix-coil transitions. | ||
| journal = J. Biomol. NMR | | journal = J. Biomol. NMR | ||
| Line 414: | Line 413: | ||
| page_start = 345 | | page_start = 345 | ||
| page_end = 356 | | page_end = 356 | ||
| + | | year = 1999 | ||
| doi = 10.1023/a:1008356809071 | | doi = 10.1023/a:1008356809071 | ||
}}<section end=Orekhov99/> | }}<section end=Orekhov99/> | ||
| Line 442: | Line 442: | ||
* <section begin=Palmer91/>{{citation | * <section begin=Palmer91/>{{citation | ||
| authors = Palmer, 3rd, A. G., Rance, M., and Wright, P. E. | | authors = Palmer, 3rd, A. G., Rance, M., and Wright, P. E. | ||
| − | |||
| title = Intramolecular motions of a zinc finger DNA-binding domain from Xfin characterized by proton-detected natural abundance carbon-13 heteronuclear NMR spectroscopy. | | title = Intramolecular motions of a zinc finger DNA-binding domain from Xfin characterized by proton-detected natural abundance carbon-13 heteronuclear NMR spectroscopy. | ||
| journal = J. Am. Chem. Soc. | | journal = J. Am. Chem. Soc. | ||
| Line 449: | Line 448: | ||
| page_start = 4371 | | page_start = 4371 | ||
| page_end = 4380 | | page_end = 4380 | ||
| + | | year = 1991 | ||
| doi = 10.1021/ja00012a001 | | doi = 10.1021/ja00012a001 | ||
}}<section end=Palmer91/> | }}<section end=Palmer91/> | ||
| Line 454: | Line 454: | ||
* <section begin=Schurr94/>{{citation | * <section begin=Schurr94/>{{citation | ||
| authors = Schurr, J. M., Babcock, H. P., and Fujimoto, B. S. | | authors = Schurr, J. M., Babcock, H. P., and Fujimoto, B. S. | ||
| − | |||
| title = A test of the model-free formulas. Effects of anisotropic rotational diffusion and dimerization. | | title = A test of the model-free formulas. Effects of anisotropic rotational diffusion and dimerization. | ||
| journal = J. Magn. Reson. B | | journal = J. Magn. Reson. B | ||
| Line 461: | Line 460: | ||
| page_start = 211 | | page_start = 211 | ||
| page_end = 224 | | page_end = 224 | ||
| + | | year = 1994 | ||
| doi = 10.1006/jmrb.1994.1127 | | doi = 10.1006/jmrb.1994.1127 | ||
}}<section end=Schurr94/> | }}<section end=Schurr94/> | ||
| Line 478: | Line 478: | ||
* <section begin=Tollinger01/>{{citation | * <section begin=Tollinger01/>{{citation | ||
| authors = Tollinger, M., Skrynnikov, N. R., Mulder, F. A. A., Forman-Kay, J. D., and Kay, L. E. | | authors = Tollinger, M., Skrynnikov, N. R., Mulder, F. A. A., Forman-Kay, J. D., and Kay, L. E. | ||
| − | |||
| title = Slow dynamics in folded and unfolded states of an sh3 domain. | | title = Slow dynamics in folded and unfolded states of an sh3 domain. | ||
| journal = J. Am. Chem. Soc. | | journal = J. Am. Chem. Soc. | ||
| Line 485: | Line 484: | ||
| page_start = 11341 | | page_start = 11341 | ||
| page_end = 11352 | | page_end = 11352 | ||
| + | | year = 2001 | ||
| doi = 10.1021/ja011300z | | doi = 10.1021/ja011300z | ||
}}<section end=Tollinger01/> | }}<section end=Tollinger01/> | ||
| Line 490: | Line 490: | ||
* <section begin=Trott03/>{{citation | * <section begin=Trott03/>{{citation | ||
| authors = Trott, O., Abergel, D., and Palmer, A. | | authors = Trott, O., Abergel, D., and Palmer, A. | ||
| − | |||
| title = An average-magnetization analysis of R-1 rho relaxation outside of the fast exchange. | | title = An average-magnetization analysis of R-1 rho relaxation outside of the fast exchange. | ||
| journal = Mol. Phys. | | journal = Mol. Phys. | ||
| Line 497: | Line 496: | ||
| page_start = 753 | | page_start = 753 | ||
| page_end = 763 | | page_end = 763 | ||
| + | | year = 2003 | ||
| doi = 10.1080/0026897021000054826 | | doi = 10.1080/0026897021000054826 | ||
}}<section end=Trott03/> | }}<section end=Trott03/> | ||
| Line 502: | Line 502: | ||
* <section begin=TrottPalmer02/>{{citation | * <section begin=TrottPalmer02/>{{citation | ||
| authors = Trott, O. and Palmer, 3rd, A. G. | | authors = Trott, O. and Palmer, 3rd, A. G. | ||
| − | |||
| title = R1rho relaxation outside of the fast-exchange limit. | | title = R1rho relaxation outside of the fast-exchange limit. | ||
| journal = J. Magn. Reson. | | journal = J. Magn. Reson. | ||
| Line 509: | Line 508: | ||
| page_start = 157 | | page_start = 157 | ||
| page_end = 160 | | page_end = 160 | ||
| + | | year = 2002 | ||
| doi = 10.1006/jmre.2001.2466 | | doi = 10.1006/jmre.2001.2466 | ||
}}<section end=TrottPalmer02/> | }}<section end=TrottPalmer02/> | ||
| Line 514: | Line 514: | ||
* <section begin=Tjandra95/>{{citation | * <section begin=Tjandra95/>{{citation | ||
| authors = Tjandra, N., Wingfield, P., Stahl, S., and Bax, A. | | authors = Tjandra, N., Wingfield, P., Stahl, S., and Bax, A. | ||
| − | |||
| title = Anisotropic rotational diffusion of perdeuterated HIV protease from N-15 NMR relaxation measurements at two magnetic. | | title = Anisotropic rotational diffusion of perdeuterated HIV protease from N-15 NMR relaxation measurements at two magnetic. | ||
| journal = J. Biomol. NMR | | journal = J. Biomol. NMR | ||
| Line 521: | Line 520: | ||
| page_start = 273 | | page_start = 273 | ||
| page_end = 284 | | page_end = 284 | ||
| + | | year = 1996 | ||
| doi = 10.1007/bf00410326 | | doi = 10.1007/bf00410326 | ||
}}<section end=Tjandra95/> | }}<section end=Tjandra95/> | ||
Revision as of 14:04, 4 November 2015
The following is an alphabetical list of all citations used on the relax wiki:
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- Baldwin A. J. (2014). An exact solution for R2,eff in CPMG experiments in the case of two site chemical exchange. J. Magn. Reson., 244, 114-124. (DOI: 10.1016/j.jmr.2014.02.023)
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- Carver, J. P. and Richards, R. E. (1972). General 2-site solution for chemical exchange produced dependence of T2 upon Carr-Purcell pulse separation. J. Magn. Reson., 6, 89-105. (DOI: 10.1016/0022-2364(72)90090-X)
- Clore, G. M., Szabo, A., Bax, A., Kay, L. E., Driscoll, P. C., and Gronenborn, A. M. (1990). Deviations from the simple 2-parameter model-free approach to the interpretation of N-15 nuclear magnetic-relaxation of proteins. J. Am. Chem. Soc., 112, 4989-4991. (DOI: 10.1021/ja00168a070)
- d'Auvergne, E. J. (2006). Protein dynamics: a study of the model-free analysis of NMR relaxation data. PhD thesis, Biochemistry and Molecular Biology, University of Melbourne. (Link, PDF)
- d'Auvergne, E. J. and Gooley, P. R. (2003). The use of model selection in the model-free analysis of protein dynamics. J. Biomol. NMR, 25, 25-39. (DOI: 10.1023/a:1021902006114)
- d'Auvergne, E. J. and Gooley, P. R. (2006). Model-free model elimination: A new step in the model-free dynamic analysis of NMR relaxation data. J. Biomol. NMR, 35, 117-135. (DOI: 10.1007/s10858-006-9007-z)
- d'Auvergne, E. J. and Gooley, P. R. (2007). Set theory formulation of the model-free problem and the diffusion seeded model-free paradigm. Mol. BioSyst., 3, 483-494. (DOI: 10.1039/b702202f)
- d'Auvergne, E. J. and Gooley, P. R. (2008). Optimisation of NMR dynamic models I. Minimisation algorithms and their performance within the model-free and Brownian rotational diffusion spaces. J. Biomol. NMR, 40, 107-119. (DOI: 10.1007/s10858-007-9214-2)
- d'Auvergne, E. J. and Gooley, P. R. (2008). Optimisation of NMR dynamic models II. A new methodology for the dual optimisation of the model-free parameters and the Brownian rotational diffusion tensor. J. Biomol. NMR, 40, 121-133. (DOI: 10.1007/s10858-007-9213-3)
- d'Auvergne, E. J. and Gooley, P. R. (2008). Optimisation of NMR dynamic models. J. Biomol. NMR, 40, 107-133. (DOI: 10.1007/s10858-007-9214-2, 10.1007/s10858-007-9213-3)
- Davis, D. G., Perlman, M. E., and London, R. E. (1994). Direct measurements of the dissociation-rate constant for inhibitor-enzyme complexes via the T1rho and T2 (CPMG) methods. J. Magn. Reson., 104, 266-275. (DOI: 10.1006/jmrb.1994.1084)
- Erdelyi, M., d'Auvergne, E., Navarro-Vazquez, A., Leonov, A., and Griesinger, C. (2011). Dynamics of the glycosidic bond: conformational space of lactose. Chem. Eur. J., 17, 9368-9376. (DOI: 10.1002/chem.201100854)
- Evenäs, J., Malmendal, A. and Akke, M. (2001). Dynamics of the transition between open and closed conformations in a calmodulin C-terminal domain mutant. Structure, 9, 185-195. (DOI: 10.1016/S0969-2126(01)00575-5)
- Farrow, N. A., Muhandiram, R., Singer, A. U., Pascal, S. M., Kay, C. M., Gish, G., Shoelson, S. E., Pawson, T., Forman-Kay, J. D., Kay, L. E. (1994). Backbone dynamics of a free and phosphopeptide-complexed Src homology 2 domain studied by 15N NMR relaxation. Biochemistry, 33, 5984-6003. (DOI: 10.1021/bi00185a040)
- Fushman, D., Tjandra, N., and Cowburn, D. (1998). Direct measurement of 15N chemical shift anisotropy in solution. J. Am. Chem. Soc., 120, 10947-10952. (DOI: 10.1021/ja981686m)
- Fushman, D., Tjandra, N., and Cowburn, D. (1999). An approach to direct determination of protein dynamics from 15N NMR relaxation at multiple fields, independent of variable 15N chemical shift anisotropy and chemical exchange contributions. J. Am. Chem. Soc., 121, 8577-8582. (DOI: 10.1021/ja9904991)
- Ishima, R. and Torchia, D. A. (1999). Estimating the time scale of chemical exchange of proteins from measurements of transverse relaxation rates in solution. J. Biomol. NMR, 14, 369-372. (DOI: 10.1023/A:1008324025406)
- Ishima, R. and Torchia, D. A. (2005). Error estimation and global fitting in transverse-relaxation dispersion experiments to determine chemical-exchange parameters. J. Biomol. NMR, 32, 41-54. (DOI: 10.1007/s10858-005-3593-z)
- Kempf, J. G. and Loria, J. P. (2004). Measurement of intermediate exchange phenomena. Methods Mol. Biol., 278, 185-231. (DOI: 10.1385/1-59259-809-9:185)
- Korzhnev, D. M., Kloiber, K., Kanelis, V., Tugarinov, V., and Kay, L. E. (2004). Probing slow dynamics in high molecular weight proteins by methyl-TROSY NMR spectroscopy: application to a 723-residue enzyme. J. Am. Chem. Soc., 126, 3964-3973. (DOI: 10.1021/ja039587i)
- Korzhnev, D. M., Kloiber, K., and Kay, L. E. (2004). Multiple-quantum relaxation dispersion NMR spectroscopy probing millisecond time-scale dynamics in proteins: theory and application. J. Am. Chem. Soc., 126, 7320-7329. (DOI: 10.1021/ja049968b)
- Korzhnev, D. M., Neudecker, P., Mittermaier, A., Orekhov, V. Y., and Kay, L. E. (2005). Multiple-site exchange in proteins studied with a suite of six NMR relaxation dispersion experiments: an application to the folding of a Fyn SH3 domain mutant. J. Am. Chem. Soc., 127, 15602-15611. (DOI: 10.1021/ja054550e)
- Korzhnev, D. M., Orekhov, V. Y., and Kay, L. E. (2005). Off-resonance R(1rho) NMR studies of exchange dynamics in proteins with low spin-lock fields: an application to a Fyn SH3 domain. J. Am. Chem. Soc., 127, 713-721. (DOI: 10.1021/ja0446855)
- Lipari, G. and Szabo, A. (1982). Model-free approach to the interpretation of nuclear magnetic-resonance relaxation in macromolecules I. Theory and range of validity. J. Am. Chem. Soc., 104, 4546-4559. (DOI: 10.1021/ja00381a009)
- Lipari, G. and Szabo, A. (1982). Model-free approach to the interpretation of nuclear magnetic-resonance relaxation in macromolecules II. Analysis of experimental results. J. Am. Chem. Soc., 104, 4559-4570. (DOI: 10.1021/ja00381a010)
- Luz, Z. and Meiboom, S. (1963). Nuclear magnetic resonance study of protolysis of trimethylammonium ion in aqueous solution - order of reaction with respect to solvent. J. Chem. Phys., 39, 366-370. (DOI: 10.1063/1.1734254)
- Massi, F., Grey, M. J., Palmer, 3rd, A. G. (2005). Microsecond timescale backbone conformational dynamics in ubiquitin studied with NMR R1ρ relaxation experiments Protein science, 14, 735-742. (DOI: 10.1110/ps.041139505)
- Meiboom, S. (1961). Nuclear magnetic resonance study of proton transfer in water. J. Chem. Phys., 34, 375-388. (DOI: 10.1063/1.1700960)
- Miloushev, V. Z. and Palmer, 3rd, A. G. (2005). R(1rho) relaxation for two-site chemical exchange: general approximations and some exact solutions. J. Magn. Reson., 177, 221-227. (DOI: 10.1016/j.jmr.2005.07.023)
- Morin, S. and Gagné, S. (2009). Simple tests for the validation of multiple field spin relaxation data. J. Biomol. NMR, 45, 361-372. (DOI: 10.1007/s10858-009-9381-4)
- Morin, S., Linnet, T. E., Lescanne, M., Schanda, P., Thompson, G. S., Tollinger, M., Teilum, K., Gagné, S., Marion, D., Griesinger, C., Blackledge, M., and d'Auvergne, E. J. (2014). relax: the analysis of biomolecular kinetics and thermodynamics using NMR relaxation dispersion data. Bioinformatics, 30, 2219-2220. (DOI: 10.1093/bioinformatics/btu166)
- Myint, W. and Ishima, R. (2009). Chemical exchange effects during refocusing pulses in constant-time CPMG relaxation dispersion experiments J. Biomol. NMR, 45, 207-216. (DOI: 10.1007/s10858-009-9344-9)
- Orekhov, V. Y., Korzhnev, D. M., Diercks, T., Kessler, H., and Arseniev, A. S. (1999). H-1-N-15 NMR dynamic study of an isolated alpha-helical peptide (1-36)bacteriorhodopsin reveals the equilibrium helix-coil transitions. J. Biomol. NMR, 14, 345-356. (DOI: 10.1023/a:1008356809071)
- Palmer, 3rd, A. G., Kroenke, C. D., and Loria, J. P. (2001). Nuclear magnetic resonance methods for quantifying microsecond-to-millisecond motions in biological macromolecules. Methods Enzymol., 339, 204-238. (DOI: 10.1016/S0076-6879(01)39315-1)
- Palmer, 3rd, A. G. and Massi, F. (2006). Characterization of the dynamics of biomacromolecules using rotating-frame spin relaxation NMR spectroscopy. Chem. Rev., 106, 1700-1719. (DOI: 10.1021/cr0404287)
- Palmer, 3rd, A. G., Rance, M., and Wright, P. E. (1991). Intramolecular motions of a zinc finger DNA-binding domain from Xfin characterized by proton-detected natural abundance carbon-13 heteronuclear NMR spectroscopy. J. Am. Chem. Soc., 113, 4371-4380. (DOI: 10.1021/ja00012a001)
- Schurr, J. M., Babcock, H. P., and Fujimoto, B. S. (1994). A test of the model-free formulas. Effects of anisotropic rotational diffusion and dimerization. J. Magn. Reson. B, 105, 211-224. (DOI: 10.1006/jmrb.1994.1127)
- Sun, H., d'Auvergne, E. J., Reinscheid, U. M., Dias, L. C., Andrade, C. K. Z., Rocha, R. O., and Griesinger, C. (2011). Bijvoet in solution reveals unexpected stereoselectivity in a michael addition. Chem. Eur. J., 17, 1811-1817. (DOI: 10.1002/chem.201002520)
- Tollinger, M., Skrynnikov, N. R., Mulder, F. A. A., Forman-Kay, J. D., and Kay, L. E. (2001). Slow dynamics in folded and unfolded states of an sh3 domain. J. Am. Chem. Soc., 123, 11341-11352. (DOI: 10.1021/ja011300z)
- Trott, O., Abergel, D., and Palmer, A. (2003). An average-magnetization analysis of R-1 rho relaxation outside of the fast exchange. Mol. Phys., 101, 753-763. (DOI: 10.1080/0026897021000054826)
- Trott, O. and Palmer, 3rd, A. G. (2002). R1rho relaxation outside of the fast-exchange limit. J. Magn. Reson., 154, 157-160. (DOI: 10.1006/jmre.2001.2466)
- Tjandra, N., Wingfield, P., Stahl, S., and Bax, A. (1996). Anisotropic rotational diffusion of perdeuterated HIV protease from N-15 NMR relaxation measurements at two magnetic. J. Biomol. NMR, 8, 273-284. (DOI: 10.1007/bf00410326)
- Vallurupalli, P., Hansen, D. F., and Kay, L. E. (2008). Structures of invisible, excited protein states by relaxation dispersion NMR spectroscopy Proc. Natl. Acad. Sci. USA, 105, 11766-11771. (DOI: 10.1073/pnas.0804221105)
- Vallurupalli, P., Hansen, D. F., Stollar, E., Meirovitch, E. and Kay, L. E. (2007). Measurement of bond vector orientations in invisible excited states of proteins Proc. Natl. Acad. Sci. USA, 104, 18473-18477. (DOI: 10.1073/pnas.0708296104)
