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| journal = J. Magn. Reson.
| volume = 209
| number issue = 2
| page_start = 183
| page_end = 194
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| 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
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* <section begin=BieriGooley11/>{{citation
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| title = Automated NMR relaxation dispersion data analysis using NESSY.
| journal = BMC Bioinformatics
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* <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
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| 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
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| 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
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| authors = d'Auvergne, E. J. and Gooley, P. R.
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| title = Set theory formulation of the model-free problem and the diffusion seeded model-free paradigm.
| journal = Mol. BioSyst.
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* <section begin=dAuvergneGooley08a/>{{citation
| authors = d'Auvergne, E. J. and Gooley, P. R.
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| 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
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| authors = d'Auvergne, E. J. and Gooley, P. R.
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| 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
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| title = Optimisation of NMR dynamic models.
| journal = J. Biomol. NMR
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| title = Backbone dynamics of a free and phosphopeptide-complexed Src homology 2 domain studied by 15N NMR relaxation.
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