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Current Opinion in Structural Biology|May 5, 2021
NMR illuminates intrinsic disorderH Jane Dyson, Peter E WrightNature|May 25, 2007
Mechanism of coupled folding and binding of an intrinsically disordered proteinKenji Sugase, H Jane Dyson, Peter E WrightJournal of Molecular Biology|June 7, 2011
Consequences of stabilizing the natively disordered f helix for the folding pathway of apomyoglobinChiaki Nishimura, H Jane Dyson, Peter E WrightJournal of Molecular Biology|November 23, 2005
Identification of native and non-native structure in kinetic folding intermediates of apomyoglobinChiaki Nishimura, H Jane Dyson, Peter E WrightJournal of Molecular Biology|January 2, 2010
Energetic frustration of apomyoglobin folding: role of the B helixChiaki Nishimura, H Jane Dyson, Peter E WrightBiochemistry|September 19, 2017
Fluorotryptophan Incorporation Modulates the Structure and Stability of Transthyretin in a Site-Specific MannerXun Sun, H Jane Dyson, Peter E WrightCurrent Opinion in Chemical Biology|March 6, 2023
Role of conformational dynamics in pathogenic protein aggregationXun Sun, H Jane Dyson, Peter E WrightBiophysical Reports|June 19, 2026
Quantifying Species-Specific Binding Affinities of Transthyretin Aggregation InhibitorsXun Sun, H Jane Dyson, Peter E WrightBiorxiv : the Preprint Server for Biology|November 28, 2024
Aggregation of Transthyretin by Fluid AgitationIrina Ritsch, H Jane Dyson, Peter E WrightProceedings of the National Academy of Sciences of the United States of America|January 14, 2021
A phosphorylation-dependent switch in the disordered p53 transactivation domain regulates DNA bindingXun Sun, H Jane Dyson, Peter E WrightPageof 21