Difference between revisions of "Citations"

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(Added the middle initial to the Baldwin14 reference.)
(All references now use the {{citation}} template.)
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* <section begin=Baldwin14/>{{citation
 
* <section begin=Baldwin14/>{{citation
−
| authors = Baldwin A. J.
+
| authors   = Baldwin A. J.
−
| title = An exact solution for R2,eff in CPMG experiments in the case of two site chemical exchange.
+
| title     = An exact solution for R2,eff in CPMG experiments in the case of two site chemical exchange.
−
| journal = J. Magn. Reson.
+
| journal   = J. Magn. Reson.
−
| volume = 244
+
| volume     = 244
 
| page_start = 114
 
| page_start = 114
 
| page_end  = 124
 
| page_end  = 124
−
| year = 2014
+
| year       = 2014
 
| doi        = 10.1016/j.jmr.2014.02.023
 
| doi        = 10.1016/j.jmr.2014.02.023
 
}}<section end=Baldwin14/>
 
}}<section end=Baldwin14/>
  
−
* <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=Bieri11/>{{citation
 +
| authors    = Bieri, M., d'Auvergne, E., and Gooley, P.
 +
| year      = 2011
 +
| 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
 +
| doi       = 10.1007/s10858-011-9509-1
 +
}}<section end=Bieri11/>
  
−
* <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=CarverRichards72/>{{citation
 +
| authors    = Carver, J. P. and Richards, R. E.
 +
| year      = 1972
 +
| title      = General 2-site solution for chemical exchange produced dependence of T2 upon Carr-Purcell pulse separation.
 +
| journal    = J. Magn. Reson.
 +
| volume    = 6
 +
| number    = 1
 +
| page_start = 89
 +
| page_end  = 105
 +
| doi       = 10.1016/0022-2364(72)90090-X
 +
}}<section end=CarverRichards72/>
  
−
* <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=Clore90/>{{citation
 +
| authors    = Clore, G. M., Szabo, A., Bax, A., Kay, L. E., Driscoll, P. C., and Gronenborn, A. M.
 +
| year      = 1990
 +
| 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
 +
| number    = 12
 +
| page_start = 4989
 +
| page_end  = 4991
 +
| doi       = 10.1021/ja00168a070
 +
}}<section end=Clore90/>
  
−
* <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=dAuvergneGooley03/>{{citation
 +
| authors    = d'Auvergne, E. J. and Gooley, P. R.
 +
| year      = 2003
 +
| title      = The use of model selection in the model-free analysis of protein dynamics.
 +
| journal    = J. Biomol. NMR
 +
| volume    = 25
 +
| number    = 1
 +
| page_start = 25
 +
| page_end  = 39
 +
| doi       = 10.1023/a:1021902006114
 +
}}<section end=dAuvergneGooley03/>
  
−
* <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=dAuvergneGooley06/>{{citation
 +
| authors    = d'Auvergne, E. J. and Gooley, P. R.
 +
| year      = 2006
 +
| title      = Model-free model elimination: A new step in the model-free dynamic analysis of NMR relaxation data.
 +
| journal    = J. Biomol. NMR
 +
| volume    = 35
 +
| number    = 2
 +
| page_start = 117
 +
| page_end  = 135
 +
| doi       = 10.1007/s10858-006-9007-z
 +
}}<section end=dAuvergneGooley06/>
  
−
* <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=dAuvergneGooley07/>{{citation
 +
| authors    = d'Auvergne, E. J. and Gooley, P. R.
 +
| year      = 2007
 +
| title      = Set theory formulation of the model-free problem and the diffusion seeded model-free paradigm.
 +
| journal    = Mol. BioSyst.
 +
| volume    = 3
 +
| number    = 7
 +
| page_start = 483
 +
| page_end  = 494
 +
| doi       = 10.1039/b702202f
 +
}}<section end=dAuvergneGooley07/>
  
−
* <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=dAuvergneGooley08a/>{{citation
 +
| authors    = d'Auvergne, E. J. and Gooley, P. R.
 +
| year      = 2008a
 +
| 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
 +
| number    = 2
 +
| page_start = 107
 +
| page_end  = 119
 +
| doi       = 10.1007/s10858-007-9214-2
 +
}}<section end=dAuvergneGooley08a/>
  
−
* <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=dAuvergneGooley08b/>{{citation
 +
| authors    = d'Auvergne, E. J. and Gooley, P. R.
 +
| year      = 2008b
 +
| 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
 +
| number    = 2
 +
| page_start = 121
 +
| page_end  = 133
 +
| doi       = 10.1007/s10858-007-9213-3
 +
}}<section end=dAuvergneGooley08b/>
  
−
* <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=dAuvergneGooley08c/>{{citation
 +
| authors    = d'Auvergne, E. J. and Gooley, P. R.
 +
| year      = 2008c
 +
| title      = Optimisation of NMR dynamic models.
 +
| journal    = J. Biomol. NMR
 +
| volume    = 40
 +
| number    = 2
 +
| page_start = 107
 +
| page_end  = 133
 +
| doi       = 10.1007/s10858-007-9214-2
 +
| doi2      = 10.1007/s10858-007-9213-3
 +
}}<section end=dAuvergneGooley08c/>
  
−
* <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=Davis94/>{{citation
 +
| authors    = Davis, D. G., Perlman, M. E., and London, R. E.
 +
| year      = 1994
 +
| 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
 +
| number    = 3
 +
| page_start = 266
 +
| page_end  = 275.
 +
| doi       = 10.1006/jmrb.1994.1084
 +
}}<section end=Davis94/>
  
−
* <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=Farrow94/>
+
* <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.
 +
| year      = 1994
 +
| title      = Backbone dynamics of a free and phosphopeptide-complexed Src homology 2 domain studied by 15N NMR relaxation.
 +
| journal    = Biochemistry
 +
| volume    = 33
 +
| number    = 19
 +
| page_start = 5984
 +
| page_end  = 6003.
 +
| doi       = 10.1021/bi00185a040
 +
}}<section end=Farrow94/>
  
−
* <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=Fushman98/>{{citation
 +
| authors    = Fushman, D., Tjandra, N., and Cowburn, D.
 +
| year      = 1998
 +
| title      = Direct measurement of <sup>15</sup>N chemical shift anisotropy in solution.
 +
| journal    = J. Am. Chem. Soc.
 +
| volume    = 120
 +
| number    = 42
 +
| page_start = 10947
 +
| page_end  = 10952
 +
| doi       = 10.1021/ja981686m
 +
}}<section end=Fushman98/>
  
−
* <section begin=Korzhnev04a/>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: [http://dx.doi.org/10.1021/ja039587i 10.1021/ja039587i])<section end=Korzhnev04a/>
+
* <section begin=Korzhnev04a/>{{citation
 +
| authors    = Korzhnev, D. M., Kloiber, K., Kanelis, V., Tugarinov, V., and Kay, L. E.
 +
| year      = 2004
 +
| 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
 +
| number    = 12
 +
| page_start = 3964
 +
| page_end  = 3973.
 +
| doi       = 10.1021/ja039587i
 +
}}<section end=Korzhnev04a/>
  
−
* <section begin=Korzhnev04b/>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: [http://dx.doi.org/10.1021/ja049968b 10.1021/ja049968b])<section end=Korzhnev04b/>
+
* <section begin=Korzhnev04b/>{{citation
 +
| authors    = Korzhnev, D. M., Kloiber, K., and Kay, L. E.
 +
| year      = 2004
 +
| title      = Multiple-quantum relaxation dispersion NMR spectroscopy probing millisecond time-scale dynamics in proteins: theory and application.
 +
| journal    = J. Am. Chem. Soc.
 +
| volume    = 126
 +
| number    = 23
 +
| page_start = 7320
 +
| page_end  = 7329.
 +
| doi       = 10.1021/ja049968b
 +
}}<section end=Korzhnev04b/>
  
−
* <section begin=Korzhnev05a/>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: [http://dx.doi.org/10.1021/ja054550e 10.1021/ja054550e])<section end=Korzhnev05a/>
+
* <section begin=Korzhnev05a/>{{citation
 +
| authors    = Korzhnev, D. M., Neudecker, P., Mittermaier, A., Orekhov, V. Y., and Kay, L. E.
 +
| year      = 2005
 +
| 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.
 +
| volume    = 127
 +
| number    = 44
 +
| page_start = 15602
 +
| page_end  = 15611.
 +
| doi       = 10.1021/ja054550e
 +
}}<section end=Korzhnev05a/>
  
−
* <section begin=Korzhnev05b/>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: [http://dx.doi.org/10.1021/ja0446855 10.1021/ja0446855])<section end=Korzhnev05b/>
+
* <section begin=Korzhnev05b/>{{citation
 +
| authors    = Korzhnev, D. M., Orekhov, V. Y., and Kay, L. E.
 +
| year      = 2005
 +
| 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.
 +
| volume    = 127
 +
| number    = 2
 +
| page_start = 713
 +
| page_end  = 721.
 +
| doi       = 10.1021/ja0446855
 +
}}<section end=Korzhnev05b/>
  
−
* <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=IshimaTorchia99/>{{citation
 +
| authors    = Ishima, R. and Torchia, D. A.
 +
| year      = 2005
 +
| title      = Error estimation and global fitting in transverse-relaxation dispersion experiments to determine chemical-exchange parameters.
 +
| journal    = J. Biomol. NMR
 +
| volume    = 32
 +
| number    = 1
 +
| page_start = 41
 +
| page_end  = 54
 +
| doi       = 10.1007/s10858-005-3593-z
 +
}}<section end=IshimaTorchia99/>
  
−
* <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=LuzMeiboom63/>{{citation
 +
| authors    = Luz, Z. and Meiboom, S.
 +
| year      = 1963
 +
| title      = Nuclear magnetic resonance study of protolysis of trimethylammonium ion in aqueous solution - order of reaction with respect to solvent.
 +
| journal    = J. Chem. Phys.
 +
| volume    = 39
 +
| number    = 2
 +
| page_start = 366
 +
| page_end  = 370
 +
| doi       = 10.1063/1.1734254
 +
}}<section end=LuzMeiboom63/>
  
−
* <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=Meiboom61/>{{citation
 +
| authors    = Meiboom, S.
 +
| year      = 1961
 +
| title      = Nuclear magnetic resonance study of proton transfer in water.
 +
| journal    = J. Chem. Phys.
 +
| volume    = 34
 +
| number    = 2
 +
| page_start = 375
 +
| page_end  = 388
 +
| doi       = 10.1063/1.1700960
 +
}}<section end=Meiboom61/>
  
−
* <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=MiloushevPalmer05/>{{citation
 +
| authors    = Miloushev, V. Z. and Palmer, 3rd, A. G.
 +
| year      = 2005
 +
| title      = R(1rho) relaxation for two-site chemical exchange: general approximations and some exact solutions.
 +
| journal    = J. Magn. Reson.
 +
| volume    = 177
 +
| number    = 2
 +
| page_start = 221
 +
| page_end  = 227
 +
| doi       = 10.1016/j.jmr.2005.07.023
 +
}}<section end=MiloushevPalmer05/>
  
−
* <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=MorinGagné09/>{{citation
 +
| authors    = Morin, S. and Gagné, S.
 +
| year      = 2009
 +
| title      = Simple tests for the validation of multiple field spin relaxation data.
 +
| journal    = J. Biomol. NMR
 +
| volume    = 45
 +
| page_start = 361
 +
| page_end  = 372
 +
| doi       = 10.1007/s10858-009-9381-4
 +
}}<section end=MorinGagné09/>
  
−
* <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=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.
 +
| year      = 2014
 +
| title      = relax: the analysis of biomolecular kinetics and thermodynamics using NMR relaxation dispersion data.
 +
| journal    = Bioinformatics
 +
| volume    = 30
 +
| number    = 15
 +
| page_start = 2219
 +
| page_end  = 2220.
 +
| doi       = 10.1093/bioinformatics/btu166
 +
}}<section end=Morin14/>
  
−
* <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=Orekhov99/>{{citation
 +
| authors    = Orekhov, V. Y., Korzhnev, D. M., Diercks, T., Kessler, H., and Arseniev, A. S.
 +
| year      = 1999
 +
| 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
 +
| volume    = 14
 +
| number    = 4
 +
| page_start = 345
 +
| page_end  = 356
 +
| doi       = 10.1023/a:1008356809071
 +
}}<section end=Orekhov99/>
  
−
* <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=Palmer91/>{{citation
 +
| authors    = Palmer, 3rd, A. G., Rance, M., and Wright, P. E.
 +
| year      = 1991
 +
| 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.
 +
| volume    = 113
 +
| number    = 12
 +
| page_start = 4371
 +
| page_end  = 4380
 +
| doi       = 10.1021/ja00012a001
 +
}}<section end=Palmer91/>
  
−
* <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=Schurr94/>{{citation
 +
| authors    = Schurr, J. M., Babcock, H. P., and Fujimoto, B. S.
 +
| year      = 1994
 +
| title      = A test of the model-free formulas. Effects of anisotropic rotational diffusion and dimerization.
 +
| journal    = J. Magn. Reson. B
 +
| volume    = 105
 +
| number    = 3
 +
| page_start = 211
 +
| page_end  = 224
 +
| doi       = 10.1006/jmrb.1994.1127
 +
}}<section end=Schurr94/>
  
−
* <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=Tollinger01/>{{citation
 +
| authors    = Tollinger, M., Skrynnikov, N. R., Mulder, F. A. A., Forman-Kay, J. D., and Kay, L. E.
 +
| year      = 2001
 +
| title      = Slow dynamics in folded and unfolded states of an sh3 domain.
 +
| journal    = J. Am. Chem. Soc.
 +
| volume    = 123
 +
| number    = 46
 +
| page_start = 11341
 +
| page_end  = 11352
 +
| doi       = 10.1021/ja011300z
 +
}}<section end=Tollinger01/>
  
−
* <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=TrottPalmer02/>{{citation
 +
| authors    = Trott, O. and Palmer, 3rd, A. G.
 +
| year      = 2002
 +
| title      = R1rho relaxation outside of the fast-exchange limit.
 +
| journal    = J. Magn. Reson.
 +
| volume    = 154
 +
| number    = 1
 +
| page_start = 157
 +
| page_end  = 160
 +
| doi       = 10.1006/jmre.2001.2466
 +
}}<section end=TrottPalmer02/>
  
−
* <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=Trott03/>{{citation
 +
| authors    = Trott, O., Abergel, D., and Palmer, A.
 +
| year      = 2003
 +
| title      = An average-magnetization analysis of R-1 rho relaxation outside of the fast exchange.
 +
| journal    = Mol. Phys.
 +
| volume    = 101
 +
| number    = 6
 +
| page_start = 753
 +
| page_end  = 763
 +
| doi       = 10.1080/0026897021000054826
 +
}}<section end=Trott03/>
  
−
* <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=Tjandra95/>{{citation
 +
| authors    = Tjandra, N., Wingfield, P., Stahl, S., and Bax, A.
 +
| year      = 1996
 +
| title      = Anisotropic rotational diffusion of perdeuterated HIV protease from N-15 NMR relaxation measurements at two magnetic.
 +
| journal    = J. Biomol. NMR
 +
| volume    = 8
 +
| number    = 3
 +
| page_start = 273
 +
| page_end  = 284
 +
| doi       = 10.1007/bf00410326
 +
}}<section end=Tjandra95/>

Revision as of 18:40, 3 November 2015

The following is an alphabetical list of all citations used on the relax wiki:

  • 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)
  • 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. 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. (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, 107-119. (DOI: 10.1007/s10858-007-9214-2)
  • 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, 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, 266-275.. (DOI: 10.1006/jmrb.1994.1084)
  • 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)
  • 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)
  • 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)
  • 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)
  • 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)
  • 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., 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)
  • 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. 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)
  • 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)
  • 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)
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