Difference between revisions of "Citations"

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The following is an alphabetical list of all citations used on the relax wiki:
 
The following is an alphabetical list of all citations used on the relax wiki:
  
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* <section begin=Baldwin14/>Baldwin A. (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: [http://dx.doi.org/10.1016/j.jmr.2014.02.023 10.1016/j.jmr.2014.02.023])<section end=Baldwin14/>
+
* <section begin=Bain11/>{{citation
 +
| authors    = Bain, A. D., Anand, C. A., and Nie, Z.
 +
| title      = Exact solution of the CPMG pulse sequence with phase variation down the echo train: Application to R2 measurements
 +
| journal    = J. Magn. Reson.
 +
| volume    = 209
 +
| issue      = 2
 +
| page_start = 183
 +
| page_end  = 194
 +
| year      = 2011
 +
| doi       = 10.1016/j.jmr.2011.01.009
 +
}}<section end=Bain11/>
  
−
* <section begin=Bieri11/>Bieri, M., d'Auvergne, E., and Gooley, P. (2011).  relaxGUI: a new software for fast and simple NMR relaxation data analysis and calculation of ps-ns and μs motion of proteins. ''J. Biomol. NMR'', '''50''', 147-155. (DOI: [http://dx.doi.org/10.1007/s10858-011-9509-1 10.1007/s10858-011-9509-1])<section end=Bieri11/>
+
* <section begin=Baldwin14/>{{citation
 +
| authors    = Baldwin A. J.
 +
| title      = An exact solution for R2,eff in CPMG experiments in the case of two site chemical exchange.
 +
| journal    = J. Magn. Reson.
 +
| volume    = 244
 +
| page_start = 114
 +
| page_end  = 124
 +
| year      = 2014
 +
| doi        = 10.1016/j.jmr.2014.02.023
 +
}}<section end=Baldwin14/>
  
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* <section begin=CarverRichards72/>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'''(1), 89-105. (DOI [http://dx.doi.org/10.1016/0022-2364(72)90090-X 10.1016/0022-2364(72)90090-X])<section end=CarverRichards72/>
+
* <section begin=Bieri11/>{{citation
 +
| 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.
 +
| journal    = J. Biomol. NMR
 +
| volume    = 50
 +
| page_start = 147
 +
| page_end  = 155
 +
| year      = 2011
 +
| doi       = 10.1007/s10858-011-9509-1
 +
}}<section end=Bieri11/>
  
−
* <section begin=Clore90/>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'''(12), 4989-4991. (DOI [http://dx.doi.org/10.1021/ja00168a070 10.1021/ja00168a070])<section end=Clore90/>
+
* <section begin=BieriGooley11/>{{citation
 +
| authors    = Bieri, M. and Gooley, P.
 +
| title      = Automated NMR relaxation dispersion data analysis using NESSY.
 +
| journal    = BMC Bioinformatics
 +
| volume    = 12
 +
| page_start = 1
 +
| page_end  = 10
 +
| year      = 2011
 +
| doi       = 10.1186/1471-2105-12-421
 +
}}<section end=BieriGooley11/>
  
−
* <section begin=dAuvergneGooley03/>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'''(1), 25-39. (DOI [http://dx.doi.org/10.1023/a:1021902006114 10.1023/a:1021902006114])<section end=dAuvergneGooley03/>
+
* <section begin=CarverRichards72/>{{citation
 +
| 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.
 +
| journal    = J. Magn. Reson.
 +
| volume    = 6
 +
| issue      = 1
 +
| page_start = 89
 +
| page_end  = 105
 +
| year      = 1972
 +
| doi       = 10.1016/0022-2364(72)90090-X
 +
}}<section end=CarverRichards72/>
  
−
* <section begin=dAuvergneGooley06/>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'''(2), 117-135. (DOI [http://dx.doi.org/10.1007/s10858-006-9007-z 10.1007/s10858-006-9007-z])<section end=dAuvergneGooley06/>
+
* <section begin=Clore90/>{{citation
 +
| 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.
 +
| journal    = J. Am. Chem. Soc.
 +
| volume    = 112
 +
| issue      = 12
 +
| page_start = 4989
 +
| page_end  = 4991
 +
| year      = 1990
 +
| doi       = 10.1021/ja00168a070
 +
}}<section end=Clore90/>
  
−
* <section begin=dAuvergneGooley07/>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'''(7), 483–494. (DOI: [http://dx.doi.org/10.1039/b702202f 10.1039/b702202f])<section end=dAuvergneGooley07/>
+
* <section begin=dAuvergne06/>{{citation_thesis
 +
| author    = d'Auvergne, E. J.
 +
| title      = Protein dynamics: a study of the model-free analysis of NMR relaxation data.
 +
| type      = PhD
 +
| department = Biochemistry and Molecular Biology
 +
| university = University of Melbourne
 +
| year      = 2006
 +
| link      = https://minerva-access.unimelb.edu.au/handle/11343/39174
 +
| pdf        = https://minerva-access.unimelb.edu.au/bitstream/handle/11343/39174/67077_00002799_01_thesis.pdf?sequence=1
 +
}}<section end=dAuvergne06/>
  
−
* <section begin=dAuvergneGooley08a/>d'Auvergne, E. J. and Gooley, P. R. (2008a).  Optimisation of NMR dynamic models I. Minimisation algorithms and their performance within the model-free and Brownian rotational diffusion spaces. ''J. Biomol. NMR'', '''40'''(2), 107-119. (DOI: [http://dx.doi.org/10.1007/s10858-007-9214-2 10.1007/s10858-007-9214-2])<section end=dAuvergneGooley08a/>
+
* <section begin=dAuvergneGooley03/>{{citation
 +
| authors    = d'Auvergne, E. J. and Gooley, P. R.
 +
| title      = The use of model selection in the model-free analysis of protein dynamics.
 +
| journal    = J. Biomol. NMR
 +
| volume    = 25
 +
| issue      = 1
 +
| page_start = 25
 +
| page_end  = 39
 +
| year      = 2003
 +
| doi       = 10.1023/a:1021902006114
 +
}}<section end=dAuvergneGooley03/>
  
−
* <section begin=dAuvergneGooley08b/>d'Auvergne, E. J. and Gooley, P. R. (2008b).  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'''(2), 121-133. (DOI: [http://dx.doi.org/10.1007/s10858-007-9213-3 10.1007/s10858-007-9213-3])<section end=dAuvergneGooley08b/>
+
* <section begin=dAuvergneGooley06/>{{citation
 +
| 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.
 +
| journal    = J. Biomol. NMR
 +
| volume    = 35
 +
| issue      = 2
 +
| page_start = 117
 +
| page_end  = 135
 +
| year      = 2006
 +
| doi       = 10.1007/s10858-006-9007-z
 +
}}<section end=dAuvergneGooley06/>
  
−
* <section begin=dAuvergneGooley08c/>d'Auvergne, E. J. and Gooley, P. R. (2008c).  Optimisation of NMR dynamic models.  ''J. Biomol. NMR'', '''40'''(2), 107-133. (DOI: [http://dx.doi.org/10.1007/s10858-007-9214-2 10.1007/s10858-007-9214-2], [http://dx.doi.org/10.1007/s10858-007-9213-3 10.1007/s10858-007-9213-3])<section end=dAuvergneGooley08c/>
+
* <section begin=dAuvergneGooley07/>{{citation
 +
| 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.
 +
| journal    = Mol. BioSyst.
 +
| volume    = 3
 +
| issue      = 7
 +
| page_start = 483
 +
| page_end  = 494
 +
| year      = 2007
 +
| doi        = 10.1039/b702202f
 +
}}<section end=dAuvergneGooley07/>
  
−
* <section begin=Davis94/>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'''(3), 266-275.  (DOI [http://dx.doi.org/10.1006/jmrb.1994.1084 10.1006/jmrb.1994.1084])<section end=Davis94/>
+
* <section begin=dAuvergneGooley08a/>{{citation
 +
| 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.
 +
| journal    = J. Biomol. NMR
 +
| volume    = 40
 +
| issue      = 2
 +
| page_start = 107
 +
| page_end  = 119
 +
| year      = 2008
 +
| doi       = 10.1007/s10858-007-9214-2
 +
}}<section end=dAuvergneGooley08a/>
  
−
* <section begin=Farrow94/>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'''(19), 5984-6003. (DOI [http://dx.doi.org/10.1021/bi00185a040 10.1021/bi00185a040])<section end=Farrow04/>
+
* <section begin=dAuvergneGooley08b/>{{citation
 +
| 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.
 +
| journal    = J. Biomol. NMR
 +
| volume    = 40
 +
| issue      = 2
 +
| page_start = 121
 +
| page_end  = 133
 +
| year      = 2008
 +
| doi       = 10.1007/s10858-007-9213-3
 +
}}<section end=dAuvergneGooley08b/>
  
−
* <section begin=Fushman98/> Fushman, D., Tjandra, N., and Cowburn, D. (1998). Direct measurement of <sup>15</sup>N chemical shift anisotropy in solution. ''J. Am. Chem. Soc.'', '''120'''(42), 10947-10952. (DOI: [http://dx.doi.org/10.1021/ja981686m 10.1021/ja981686m])<section end=Fushman98/>
+
* <section begin=dAuvergneGooley08c/>{{citation
 +
| authors    = d'Auvergne, E. J. and Gooley, P. R.
 +
| title      = Optimisation of NMR dynamic models.
 +
| journal    = J. Biomol. NMR
 +
| volume    = 40
 +
| issue      = 2
 +
| page_start = 107
 +
| page_end  = 133
 +
| year      = 2008
 +
| doi       = 10.1007/s10858-007-9214-2
 +
| doi2      = 10.1007/s10858-007-9213-3
 +
}}<section end=dAuvergneGooley08c/>
  
−
* <section begin=IshimaTorchia99/>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'''(1), 41-54. (DOI [http://dx.doi.org/10.1007/s10858-005-3593-z 10.1007/s10858-005-3593-z])<section end=IshimaTorchia99/>
+
* <section begin=Davis94/>{{citation
 +
| 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.
 +
| journal    = J. Magn. Reson.
 +
| volume    = 104
 +
| issue      = 3
 +
| page_start = 266
 +
| page_end  = 275
 +
| year      = 1994
 +
| doi       = 10.1006/jmrb.1994.1084
 +
}}<section end=Davis94/>
  
−
* <section begin=LuzMeiboom63/>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'''(2), 366-370. (DOI [http://dx.doi.org/10.1063/1.1734254 10.1063/1.1734254])<section end=LuzMeiboom63/>
+
* <section begin=Erdelyi11/>{{citation
 +
| authors    = Erdélyi, M., d'Auvergne, E., Navarro-Vázquez, A., Leonov, A., and Griesinger, C.
 +
| title      = Dynamics of the glycosidic bond: conformational space of lactose.
 +
| journal    = Chem. Eur. J.
 +
| volume    = 17
 +
| issue      = 34
 +
| page_start = 9368
 +
| page_end  = 9376
 +
| year      = 2011
 +
| doi        = 10.1002/chem.201100854
 +
}}<section end=Erdelyi11/>
  
−
* <section begin=Meiboom61/>Meiboom, S. (1961). Nuclear magnetic resonance study of proton transfer in water.  ''J. Chem. Phys.'', '''34'''(2), 375-388. (DOI [http://dx.doi.org/10.1063/1.1700960 10.1063/1.1700960]).<section end=Meiboom61/>
+
* <section begin=Evenäs01/>{{citation
 +
| authors    = Evenäs, J., Malmendal, A. and Akke, M.
 +
| title      = Dynamics of the transition between open and closed conformations in a calmodulin C-terminal domain mutant.
 +
| journal    = Structure
 +
| volume    = 9
 +
| issue      = 3
 +
| page_start = 185
 +
| page_end  = 195
 +
| year      = 2001
 +
| doi       = 10.1016/S0969-2126(01)00575-5
 +
}}<section end=Evenäs01/>
  
−
* <section begin=MiloushevPalmer05/>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'''(2), 221-227. (DOI [http://dx.doi.org/10.1016/j.jmr.2005.07.023 10.1016/j.jmr.2005.07.023])<section end=MiloushevPalmer05/>
+
* <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.
 +
| title      = Backbone dynamics of a free and phosphopeptide-complexed Src homology 2 domain studied by 15N NMR relaxation.
 +
| journal    = Biochemistry
 +
| volume    = 33
 +
| issue      = 19
 +
| page_start = 5984
 +
| page_end  = 6003
 +
| year      = 1994
 +
| doi        = 10.1021/bi00185a040
 +
}}<section end=Farrow94/>
  
−
* <section begin=MorinGagné09/>Morin, S. and Gagné, S. (2009).  Simple tests for the validation of multiple field spin relaxation data. ''J. Biomol. NMR'', '''45''', 361-372. (DOI: [http://dx.doi.org/10.1007/s10858-009-9381-4 10.1007/s10858-009-9381-4])<section end=MorinGagné09/>
+
* <section begin=Fushman98/>{{citation
 +
| authors    = Fushman, D., Tjandra, N., and Cowburn, D.
 +
| title      = Direct measurement of <sup>15</sup>N chemical shift anisotropy in solution.
 +
| journal    = J. Am. Chem. Soc.
 +
| volume    = 120
 +
| issue      = 42
 +
| page_start = 10947
 +
| page_end  = 10952
 +
| year      = 1998
 +
| doi       = 10.1021/ja981686m
 +
}}<section end=Fushman98/>
  
−
* <section begin=Morin14/>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'''(15), 2219-2220.  (DOI [http://dx.doi.org/10.1093/bioinformatics/btu166 10.1093/bioinformatics/btu166])<section end=Morin14/>
+
* <section begin=Fushman99/>{{citation
 +
| authors    = Fushman, D., Tjandra, N., and Cowburn, D.
 +
| title      = 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.
 +
| journal    = J. Am. Chem. Soc.
 +
| volume    = 121
 +
| issue      = 37
 +
| page_start = 8577
 +
| page_end  = 8582
 +
| year      = 1999
 +
| doi       = 10.1021/ja9904991
 +
}}<section end=Fushman99/>
  
−
* <section begin=Orekhov99/>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'''(4), 345-356. (DOI: [http://dx.doi.org/10.1023/a:1008356809071 10.1023/a:1008356809071])<section end=Orekhov99/>
+
* <section begin=IshimaTorchia99/>{{citation
 +
| 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.
 +
| journal    = J. Biomol. NMR
 +
| volume    = 14
 +
| issue      = 4
 +
| page_start = 369
 +
| page_end  = 372
 +
| year      = 1999
 +
| doi       = 10.1023/A:1008324025406
 +
}}<section end=IshimaTorchia99/>
  
−
* <section begin=Palmer91/>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'''(12), 4371-4380. (DOI: [http://dx.doi.org/10.1021/ja00012a001 10.1021/ja00012a001])<section end=Palmer91/>
+
* <section begin=IshimaTorchia05/>{{citation
 +
| authors    = Ishima, R. and Torchia, D. A.
 +
| title      = Error estimation and global fitting in transverse-relaxation dispersion experiments to determine chemical-exchange parameters.
 +
| journal    = J. Biomol. NMR
 +
| volume    = 32
 +
| issue      = 1
 +
| page_start = 41
 +
| page_end  = 54
 +
| year      = 2005
 +
| doi       = 10.1007/s10858-005-3593-z
 +
}}<section end=IshimaTorchia99/>
  
−
* <section begin=Schurr94/>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'''(3), 211-224. (DOI: [http://dx.doi.org/10.1006/jmrb.1994.1127 10.1006/jmrb.1994.1127])<section end=Schurr94/>
+
* <section begin=KempfLoria04/>{{citation
 +
| authors    = Kempf, J. G. and Loria, J. P.
 +
| title      = Measurement of intermediate exchange phenomena.
 +
| journal    = Methods Mol. Biol.
 +
| volume    = 278
 +
| page_start = 185
 +
| page_end  = 231
 +
| year      = 2004
 +
| doi       = 10.1385/1-59259-809-9:185
 +
}}<section end=KempfLoria04/>
  
−
* <section begin=Tollinger01/>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'''(46), 11341-11352. (DOI [http://dx.doi.org/10.1021/ja011300z 10.1021/ja011300z])<section end=Tollinger01/>
+
* <section begin=Korzhnev04a/>{{citation
 +
| 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.
 +
| journal    = J. Am. Chem. Soc.
 +
| volume    = 126
 +
| issue      = 12
 +
| page_start = 3964
 +
| page_end  = 3973
 +
| year      = 2004
 +
| doi       = 10.1021/ja039587i
 +
}}<section end=Korzhnev04a/>
  
−
* <section begin=TrottPalmer02/>Trott, O. and Palmer, 3rd, A. G. (2002). R1rho relaxation outside of the fast-exchange limit. ''J. Magn. Reson.'', '''154'''(1), 157-160. (DOI [http://dx.doi.org/10.1006/jmre.2001.2466 10.1006/jmre.2001.2466])<section end=TrottPalmer02/>
+
* <section begin=Korzhnev04b/>{{citation
 +
| 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.
 +
| journal    = J. Am. Chem. Soc.
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| volume    = 126
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| issue      = 23
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| page_start = 7320
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| year      = 2004
 +
| doi       = 10.1021/ja049968b
 +
}}<section end=Korzhnev04b/>
  
−
* <section begin=Trott03/>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'''(6), 753-763. (DOI [http://dx.doi.org/10.1080/0026897021000054826 10.1080/0026897021000054826])<section end=Trott03/>
+
* <section begin=Korzhnev05a/>{{citation
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| authors    = Korzhnev, D. M., Neudecker, P., Mittermaier, A., Orekhov, V. Y., and Kay, L. E.
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| 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.
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| volume    = 127
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| issue      = 44
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| page_start = 15602
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| year      = 2005
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| doi       = 10.1021/ja054550e
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}}<section end=Korzhnev05a/>
  
−
* <section begin=Tjandra95/>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'''(3), 273-284. (DOI: [http://dx.doi.org/10.1007/bf00410326 10.1007/bf00410326])<section end=Tjandra95/>
+
* <section begin=Korzhnev05b/>{{citation
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| authors    = Korzhnev, D. M., Orekhov, V. Y., and Kay, L. E.
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| title      = Off-resonance R(1rho) NMR studies of exchange dynamics in proteins with low spin-lock fields: an application to a Fyn SH3 domain.
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| journal    = J. Am. Chem. Soc.
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| volume    = 127
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| year      = 2005
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| doi        = 10.1021/ja0446855
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}}<section end=Korzhnev05b/>
 +
 
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* <section begin=LipariSzabo82a/>{{citation
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| authors    = Lipari, G. and Szabo, A.
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| title      = Model-free approach to the interpretation of nuclear magnetic-resonance relaxation in macromolecules I. Theory and range of validity.
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| journal    = J. Am. Chem. Soc.
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| volume    = 104
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| doi        = 10.1021/ja00381a009
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}}<section end=LipariSzabo82a/>
 +
 
 +
* <section begin=LipariSzabo82b/>{{citation
 +
| authors    = Lipari, G. and Szabo, A.
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| title      = Model-free approach to the interpretation of nuclear magnetic-resonance relaxation in macromolecules II. Analysis of experimental results.
 +
| journal    = J. Am. Chem. Soc.
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| volume    = 104
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| issue      = 17
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| page_start = 4559
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| year      = 1982
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| doi        = 10.1021/ja00381a010
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}}<section end=LipariSzabo82b/>
 +
 
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* <section begin=LuzMeiboom63/>{{citation
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| authors    = Luz, Z. and Meiboom, S.
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| title      = Nuclear magnetic resonance study of protolysis of trimethylammonium ion in aqueous solution - order of reaction with respect to solvent.
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}}<section end=LuzMeiboom63/>
 +
 
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* <section begin=Mandel95/>{{citation
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| authors    = Mandel, A. M., Akke, M., and Palmer, 3rd, A. G.
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| title      = Backbone dynamics of ''Escherichia coli'' ribonuclease HI: correlations with structure and function in an active enzyme.
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| journal    = J. Mol. Biol.
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* <section begin=Massi05/>{{citation
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| authors    = Massi, F., Grey, M. J., Palmer, 3rd, A. G.
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| title      = Microsecond timescale backbone conformational dynamics in ubiquitin studied with NMR R1ρ relaxation experiments
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* <section begin=Meiboom61/>{{citation
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 +
 
 +
* <section begin=MiloushevPalmer05/>{{citation
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| authors    = Miloushev, V. Z. and Palmer, 3rd, A. G.
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| title      = R(1rho) relaxation for two-site chemical exchange: general approximations and some exact solutions.
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 +
* <section begin=MorinGagné09/>{{citation
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| authors    = Morin, S. and Gagné, S.
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| title      = Simple tests for the validation of multiple field spin relaxation data.
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| year      = 2009
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* <section begin=Morin14/>{{citation
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| title      = relax: the analysis of biomolecular kinetics and thermodynamics using NMR relaxation dispersion data.
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| doi        = 10.1093/bioinformatics/btu166
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* <section begin=MyintIshima09/>{{citation
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| authors    = Myint, W. and Ishima, R.
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| title      = Chemical exchange effects during refocusing pulses in constant-time CPMG relaxation dispersion experiments
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* <section begin=Trott03/>{{citation
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| authors    = Trott, O., Abergel, D., and Palmer, A.
 +
| title      = An average-magnetization analysis of R-1 rho relaxation outside of the fast exchange.
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* <section begin=Tjandra95/>{{citation
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| authors    = Tjandra, N., Wingfield, P., Stahl, S., and Bax, A.
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| title      = Anisotropic rotational diffusion of perdeuterated HIV protease from N-15 NMR relaxation measurements at two magnetic.
 +
| journal    = J. Biomol. NMR
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| authors    = Vallurupalli, P., Hansen, D. F., and Kay, L. E.
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| title      = Measurement of bond vector orientations in invisible excited states of proteins
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}}<section end=Vallurupalli07/>
 +
 
 +
[[Category:Documentation]]

Latest revision as of 21:52, 21 October 2020

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)
  • Bieri, M., d'Auvergne, E., and Gooley, P. (2011). relaxGUI: a new software for fast and simple NMR relaxation data analysis and calculation of ps-ns and μs motion of proteins. J. Biomol. NMR, 50, 147-155. (DOI: 10.1007/s10858-011-9509-1)
  • Bieri, M. and Gooley, P. (2011). Automated NMR relaxation dispersion data analysis using NESSY. BMC Bioinformatics, 12, 1-10. (DOI: 10.1186/1471-2105-12-421)
  • 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(1), 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(12), 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(1), 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(2), 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(7), 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(2), 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(2), 121-133. (DOI: 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(3), 266-275. (DOI: 10.1006/jmrb.1994.1084)
  • Erdélyi, M., d'Auvergne, E., Navarro-Vázquez, A., Leonov, A., and Griesinger, C. (2011). Dynamics of the glycosidic bond: conformational space of lactose. Chem. Eur. J., 17(34), 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(3), 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(19), 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(42), 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(37), 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(4), 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(1), 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(12), 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(23), 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(44), 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(2), 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(17), 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(17), 4559-4570. (DOI: 10.1021/ja00381a010)
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