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FEBS Letters|June 16, 2015
Functional advantages of dynamic protein disorderRebecca B Berlow, H Jane Dyson, Peter E WrightProceedings of the National Academy of Sciences of the United States of America|August 19, 2006
The role of hydrophobic interactions in initiation and propagation of protein foldingH Jane Dyson, Peter E Wright, Harold A ScheragaJournal of the American Chemical Society|April 28, 2009
Prediction of the rotational tumbling time for proteins with disordered segmentsSung-Hun Bae, H Jane Dyson, Peter E WrightAnnual Review of Biophysics and Biomolecular Structure|May 14, 2004
Structure, dynamics, and catalytic function of dihydrofolate reductaseJason R Schnell, H Jane Dyson, Peter E WrightJournal of Molecular Biology|April 11, 2018
Expanding the Paradigm: Intrinsically Disordered Proteins and Allosteric RegulationRebecca B Berlow, H Jane Dyson, Peter E WrightNature|March 9, 2017
Hypersensitive termination of the hypoxic response by a disordered protein switchRebecca B Berlow, H Jane Dyson, Peter E WrightBiochemistry|January 14, 2004
Effect of cofactor binding and loop conformation on side chain methyl dynamics in dihydrofolate reductaseJason R Schnell, H Jane Dyson, Peter E WrightProceedings of the National Academy of Sciences of the United States of America|November 14, 2018
Long-range regulation of p53 DNA binding by its intrinsically disordered N-terminal transactivation domainAlexander S Krois, H Jane Dyson, Peter E WrightBiochemistry|August 12, 2008
Conformational relaxation following hydride transfer plays a limiting role in dihydrofolate reductase catalysisDavid D Boehr, H Jane Dyson, Peter E WrightProceedings of the National Academy of Sciences of the United States of America|January 11, 2022
Multivalency enables unidirectional switch-like competition between intrinsically disordered proteinsRebecca B Berlow, H Jane Dyson, Peter E WrightPageof 23