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NMR illuminates intrinsic disorder

Current opinion in structural biology, 2021-10, Vol.70, p.44-52

2021

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Making Sense of Intrinsically Disordered Proteins

Biophysical journal, 2016-03, Vol.110 (5), p.1013-1016

Dyson, H. Jane

2016

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Vital for Viruses: Intrinsically Disordered Proteins

Journal of molecular biology, 2023-06, Vol.435 (11), p.167860-167860, Article 167860

Dyson, H. Jane

2023

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Role of Intrinsic Protein Disorder in the Function and Interactions of the Transcriptional Coactivators CREB-binding Protein (CBP) and p300

The Journal of biological chemistry, 2016-03, Vol.291 (13), p.6714-6722

2016

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Long-range regulation of p53 DNA binding by its intrinsically disordered N-terminal transactivation domain

Proceedings of the National Academy of Sciences - PNAS, 2018-11, Vol.115 (48), p.E11302-E11310

2018

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Conformational propensities of intrinsically disordered proteins influence the mechanism of binding and folding

Proceedings of the National Academy of Sciences - PNAS, 2015-08, Vol.112 (31), p.9614-9619

2015

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Hypersensitive termination of the hypoxic response by a disordered protein switch

Nature (London), 2017-03, Vol.543 (7645), p.447-451

2017

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Expanding the Paradigm: Intrinsically Disordered Proteins and Allosteric Regulation

Journal of molecular biology, 2018-08, Vol.430 (16), p.2309-2320

2018

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Functional advantages of dynamic protein disorder

FEBS letters, 2015-09, Vol.589 (19), p.2433-2440

2015

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Mechanism of coupled folding and binding of an intrinsically disordered protein

Nature, 2007-06, Vol.447 (7147), p.1021-1025

2007

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Expanding the proteome: disordered and alternatively folded proteins

Quarterly reviews of biophysics, 2011-11, Vol.44 (4), p.467-518

Dyson, H. Jane

2011

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Perspective: the essential role of NMR in the discovery and characterization of intrinsically disordered proteins

Journal of biomolecular NMR, 2019-12, Vol.73 (12), p.651-659

2019

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Multivalency enables unidirectional switch-like competition between intrinsically disordered proteins

Proceedings of the National Academy of Sciences - PNAS, 2022-01, Vol.119 (3)

2022

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Kinetic analysis of the multistep aggregation pathway of human transthyretin

Proceedings of the National Academy of Sciences - PNAS, 2018-07, Vol.115 (27), p.E6201-E6208

2018

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How Does Your Protein Fold? Elucidating the Apomyoglobin Folding Pathway

Accounts of chemical research, 2017-01, Vol.50 (1), p.105-111

2017

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Dynamic Energy Landscape of Dihydrofolate Reductase Catalysis

Science (American Association for the Advancement of Science), 2006-09, Vol.313 (5793), p.1638-1642

2006

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Structural and dynamic studies of DNA recognition by NF-κB p50 RHR homodimer using methyl NMR spectroscopy

Nucleic acids research, 2022-07, Vol.50 (12), p.7147-7160

2022

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Recognition of the disordered p53 transactivation domain by the transcriptional adapter zinc finger domains of CREB-binding protein

Proceedings of the National Academy of Sciences - PNAS, 2016-03, Vol.113 (13), p.E1853-E1862

2016

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Roles of intrinsic disorder in protein-nucleic acid interactions

Molecular bioSystems, 2012-01, Vol.8 (1), p.97-104

Dyson, H Jane

2012

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Fluorotryptophan Incorporation Modulates the Structure and Stability of Transthyretin in a Site-Specific Manner

Biochemistry (Easton), 2017-10, Vol.56 (41), p.5570-5581

2017

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Divergent evolution of protein conformational dynamics in dihydrofolate reductase

Nature structural & molecular biology, 2013-11, Vol.20 (11), p.1243-1249

2013

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Defining the Structural Basis for Allosteric Product Release from E. coli Dihydrofolate Reductase Using NMR Relaxation Dispersion

Journal of the American Chemical Society, 2017-08, Vol.139 (32), p.11233-11240

2017

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The Role of Hydrophobic Interactions in Initiation and Propagation of Protein Folding

Proceedings of the National Academy of Sciences - PNAS, 2006-08, Vol.103 (35), p.13057-13061

2006

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Intrinsically disordered proteins in cellular signalling and regulation

Nature reviews. Molecular cell biology, 2015-01, Vol.16 (1), p.18-29

2015

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Mispacking of the Phe87 Side Chain Reduces the Kinetic Stability of Human Transthyretin

Biochemistry (Easton), 2018-12, Vol.57 (51), p.6919-6922

2018

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NMR illuminates intrinsic disorder

Making Sense of Intrinsically Disordered Proteins

Vital for Viruses: Intrinsically Disordered Proteins

Role of Intrinsic Protein Disorder in the Function and Interactions of the Transcriptional Coactivators CREB-binding Protein (CBP) and p300

Long-range regulation of p53 DNA binding by its intrinsically disordered N-terminal transactivation domain

Conformational propensities of intrinsically disordered proteins influence the mechanism of binding and folding

Hypersensitive termination of the hypoxic response by a disordered protein switch

Expanding the Paradigm: Intrinsically Disordered Proteins and Allosteric Regulation

Functional advantages of dynamic protein disorder

Mechanism of coupled folding and binding of an intrinsically disordered protein

Expanding the proteome: disordered and alternatively folded proteins

Perspective: the essential role of NMR in the discovery and characterization of intrinsically disordered proteins

Multivalency enables unidirectional switch-like competition between intrinsically disordered proteins

Kinetic analysis of the multistep aggregation pathway of human transthyretin

How Does Your Protein Fold? Elucidating the Apomyoglobin Folding Pathway

Dynamic Energy Landscape of Dihydrofolate Reductase Catalysis

Structural and dynamic studies of DNA recognition by NF-κB p50 RHR homodimer using methyl NMR spectroscopy

Recognition of the disordered p53 transactivation domain by the transcriptional adapter zinc finger domains of CREB-binding protein

Roles of intrinsic disorder in protein-nucleic acid interactions

Fluorotryptophan Incorporation Modulates the Structure and Stability of Transthyretin in a Site-Specific Manner

Divergent evolution of protein conformational dynamics in dihydrofolate reductase

Defining the Structural Basis for Allosteric Product Release from E. coli Dihydrofolate Reductase Using NMR Relaxation Dispersion

The Role of Hydrophobic Interactions in Initiation and Propagation of Protein Folding

Intrinsically disordered proteins in cellular signalling and regulation

Mispacking of the Phe87 Side Chain Reduces the Kinetic Stability of Human Transthyretin

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