Publications

Characteristics of a Bacillus subtilis W23 mutant temperature sensitive for chromosome replication. P. Upcroft, H.J. Dyson, & R.G. Wake (1975) J. Bacteriol. 121, 121-127. PMC285621
Spin state and unfolding equilibria of ferricytochrome c in acidic solutions. H.J. Dyson & J.K. Beattie (1982) J. Biol. Chem. 257, 2267-2273
The immunodominant site of a synthetic immunogen has a conformational preference in water for a Type-II reverse turn. H.J. Dyson, K.J. Cross, R.A. Houghten, I.A. Wilson, P.E. Wright, & R.A. Lerner (1985) Nature 318, 480-483
Antipeptide antibodies and the disorder-order phenomenon. P.E. Wright, H.J. Dyson, M. Rance, J. Ostresh, R.A. Houghten, I.A. Wilson, & R.A. Lerner (1985) In: Modern Approaches to Vaccines (R.A. Lerner, R.M. Chanock, & F. Brown Eds.) Cold Spring Harbor Laboratory, pp 15-19
Selection by site-directed antibodies of small regions of peptides which are ordered in water. H.J. Dyson, K.J. Cross, J. Ostresh, R.A. Houghten, I.A. Wilson, P.E. Wright, & R.A. Lerner (1986) In: Synthetic Peptides as Antigens, Ciba Foundation Symposium 119 (R. Porter & J. Whelan Eds.) John Wiley & Sons, Chichester. pp 58-75.
The order-disorder paradox in antigen-antibody union: anti-peptide antibodies as a probe for structured regions of small peptides. H.J. Dyson, M. Rance, R.A. Houghten, P.E. Wright, & R.A. Lerner (1987) In: Biological Organization: Macromolecular Interactions at High Resolution (R.M. Burnett & H.J. Vogel Eds.) Academic Press Inc., London. pp 227-234
Identification of folded structures in immunogenic peptides by 2D NMR. P.E. Wright, H.J. Dyson, M. Rance, R.A. Houghten, & R.A. Lerner (1987) In: Protides of the Biological Fluids, 35th Colloquium (H. Peeters Ed.) Pergamon, pp 477-480
The physical basis for induction of protein-reactive antipeptide antibodies. H.J. Dyson, R.A. Lerner, & P.E. Wright (1988) Ann. Rev. Biophys. Biophys. Chem. 17, 305-324.
Folding of immunogenic peptide fragments of proteins in water solution. I Sequence requirements for the formation of a reverse turn. H.J. Dyson, M. Rance, R.A. Houghten, R.A. Lerner, & P.E. Wright (1988) J. Mol. Biol. 201, 161-200.
Folding of immunogenic peptide fragments of proteins in water solution. II The nascent helix. H.J. Dyson, M. Rance, R.A. Houghten, P.E. Wright, & R.A. Lerner (1988) J. Mol. Biol. 201, 201-217.
Structural differences between oxidized and reduced thioredoxin monitored by two-dimensional 1H NMR spectroscopy. H.J. Dyson, A. Holmgren, & P.E. Wright (1988) FEBS Lett. 228, 254-258.
Conformation of peptide fragments of proteins in aqueous solution: implications for initiation of protein folding. P.E. Wright, H.J. Dyson, & R.A. Lerner (1988) Biochemistry 27, 7167-7175.
Assignment of the proton NMR spectrum of reduced and oxidized thioredoxin: sequence-specific assignments, secondary structure and global fold. H.J. Dyson, A. Holmgren, & P.E. Wright (1989) Biochemistry 28, 7074-7087.
1H NMR studies of the solution conformations of an analogue of the C-peptide of ribonuclease A. J.J. Osterhout,Jr., R.L. Baldwin, E.J. York, J.M. Stewart, H.J. Dyson, & P.E. Wright (1989) Biochemistry 28, 7059-7064.
Folding of peptide fragments of proteins in water solution: implications for initiation of protein folding. P.E. Wright, R.A. Lerner, & H.J. Dyson (1989) In: Advances in Protein Design (H. Blöcker, J. Collins, R.D. Schmid, & D. Schomburg Eds.) VCH Publishing, pp 13-19.
Folding of peptide fragments of proteins in aqueous solution. P.E. Wright, H.J. Dyson, V.A. Feher, L.L. Tennant, J.P. Waltho, R.A. Lerner, & D.A. Case (1990) In: Frontiers of NMR in Molecular Biology, UCLA Symposia in Molecular and Cellular Biology. New Series vol.109 (D. Live, I. Armitage, & D. Patel Eds.) Alan R. Liss, Inc., New York. pp 1-13.
Folding of peptide fragments of proteins in water solution. P.E. Wright, H.J. Dyson, J.P. Waltho, & R.A. Lerner (1990) In: Protein Folding (L.M. Gierasch & J. King Eds.) AAAS, Washington. pp 95-102.
Three-dimensional solution structure of the reduced form of Escherichia coli thioredoxin determined by nuclear magnetic resonance spectroscopy. H.J. Dyson, G.P. Gippert, D.A. Case, A. Holmgren, & P.E. Wright (1990) Biochemistry 29, 4129-4136.
Antigen-antibody interactions: an NMR approach. P.E. Wright, H.J. Dyson, R.A. Lerner, L. Riechmann, & P. Tsang (1990) Biochem. Pharm. 40, 83-88.
Conformational preferences of synthetic peptides derived from the immunodominant site of the circumsporozoite protein of Plasmodium falciparum by 1H NMR. H.J. Dyson, A.C. Satterthwait, R.A. Lerner, & P.E. Wright (1990) Biochemistry 29, 7828-7837.
The conformational restriction of synthetic vaccines for malaria. A.C. Satterthwait, L.-C. Chiang, T. Arrhenius, E. Cabezas, F. Zavala, H.J. Dyson, & P.E. Wright (1990) Bull. WHO 68, 17-25. PMC2393045
Defining solution conformations of small linear peptides. H.J. Dyson & P.E. Wright (1991) Ann. Rev. Biophys. Biophys. Chem. 20, 519-538.
Active conformation of an insect neuropeptide family. R.J. Nachman, V.A. Roberts, H.J. Dyson, G.M. Holman, & J.A. Tainer (1991) Proc. Natl. Acad. Sci. USA 88, 4518-4522. PMC51692
Proton-transfer effects in the active-site region of Escherichia coli thioredoxin using two-dimensional 1H NMR. H.J. Dyson, L.L. Tennant, & A. Holmgren (1991) Biochemistry 30, 4262-4268.
Mapping the anatomy of the immunodominant domain of the human immunodeficiency virus gp41 transmembrane protein: peptide conformation analysis using monoclonal antibodies and proton nuclear magnetic resonance spectroscopy. M.B.A. Oldstone, A. Tishon, H. Lewicki, H.J. Dyson, V.A. Feher, N. Assa-Munt, & P.E. Wright (1991) J. Virol. 65, 1727-1734. PMC239977
Assignment of the 15N NMR spectrum of reduced and oxidized Escherichia coli thioredoxin. K. Chandrasekhar, G. Krause, A. Holmgren, & H.J. Dyson (1991) FEBS Lett. 284, 178-183.
Polypeptide backbone resonance assignments and secondary structure of Bacillus subtilis Enzyme IIIglc determined by two-dimensional and three-dimensional heteronuclear NMR spectroscopy. W.J. Fairbrother, J. Cavanagh, H.J. Dyson, A.G. Palmer,III, S.L. Sutrina, J. Reizer, M.H. Saier,Jr, & P.E. Wright (1991) Biochemistry 30, 6896-6907.
Solution conformational preferences of immunogenic peptides derived from the principal neutralizing determinant of the HIV-1 envelope glycoprotein gp120. K. Chandrasekhar, A.T. Profy, & H.J. Dyson (1991) Biochemistry 30, 9187-9194.
Immunogenic peptides corresponding to the dominant antigenic region Ala597 to Cys619 in the transmembrane protein of simian immunodeficiency virus have a high folding propensity. H.J. Dyson, E. Norrby, K. Hoey, D.E. Parks, R.A. Lerner, & P.E. Wright (1992) Biochemistry 31, 1458-1463.
A comparison of the requirements for pre-formed secondary structure in proteins with different structures in the folded state. H.J. Dyson & P.E. Wright (1992) Structure and Function 2, 113-120.
Folding of peptide fragments comprising the complete sequence of proteins. Models for initiation of protein folding I. Myohemerythrin. H.J. Dyson, G. Merutka, J.P. Waltho, R.A. Lerner, & P.E. Wright (1992) J. Mol. Biol. 226, 795-817.
Folding of peptide fragments comprising the complete sequence of proteins: models for the initiation of protein folding II Plastocyanin. H.J. Dyson, J.R. Sayre, G. Merutka, H.-C. Shin, R.A. Lerner, & P.E. Wright (1992) J. Mol. Biol. 226, 819-835.
Peptide conformation and protein folding. H.J. Dyson & P.E. Wright (1993) Curr. Opin. Struct. Biol. 3, 60-65.
Comparison of backbone and tryptophan side-chain dynamics of reduced and oxidized Escherichia coli thioredoxin using 15N NMR relaxation measurements. M.J. Stone, K. Chandrasekhar, A. Holmgren, P.E. Wright, & H.J. Dyson (1993) Biochemistry 32, 426-435.
Peptide models of protein folding initiation sites. 1. Secondary structure formation by peptides corresponding to the G- and H-helices of myoglobin. J.P. Waltho, V.A. Feher, G. Merutka, H.J. Dyson, & P.E. Wright (1993) Biochemistry 32, 6337-6347.
Peptide models of protein folding initiation sites. 2. The G-H turn region of myoglobin acts as a helix stop signal. H.-C. Shin, G. Merutka, J.P. Waltho, P.E. Wright, & H.J. Dyson (1993) Biochemistry 32, 6348-6355.
Peptide models of protein folding initiation sites. 3. The G-H helical hairpin of myoglobin. H.-C. Shin, G. Merutka, J.P. Waltho, L.L. Tennant, H.J. Dyson, & P.E. Wright (1993) Biochemistry 32, 6356-6364.
Characterization of a folding intermediate of apoplastocyanin trapped by proline isomerization. S. Koide, H.J. Dyson, & P.E. Wright (1993) Biochemistry 32, 12299-12310.
Protein structure calculation using NMR restraints. H.J. Dyson & P.E. Wright (1994) In: Two-Dimensional NMR Spectrscopy: Applications for Chemists and Biochemists (W.R. Croasmun & R. Carlson Eds.) VCH Publishers, Inc., New York. pp 655-698.
Peptide structure in solution. H.J. Dyson (1994) In: Synthetic Vaccines (B.H. Nicholson Ed.) Blackwell Scientific Publications Ltd, Oxford, U.K.. pp 246-267.
Characterization by 1H NMR of a C32S,C35S double mutant of Escherichia coli thioredoxin confirms its resemblance to the reduced wild-type protein. H.J. Dyson, M.-F. Jeng, P. Model, & A. Holmgren (1994) FEBS Lett. 339, 11-17.
Effect of disulfide bridge formation on the NMR spectrum of a protein: studies on oxidized and reduced Escherichia coli thioredoxin. K. Chandrasekhar, A.P. Campbell, M.-F. Jeng, A. Holmgren, & H.J. Dyson (1994) J. Biomol. NMR 4, 411-432.
Use of chemical shifts and coupling constants in NMR structural studies on peptides and proteins. D.A. Case, H.J. Dyson, & P.E. Wright (1994) Methods Enzymol. 239, 392-416.
Detecting nascent structures in solution using NMR. H.J. Dyson, J. Yao, & P.E. Wright (1994) In: Peptides: Chemistry, Structure and Biology (R.S. Hodges & J.A. Smith Eds.) ESCOM, Leiden. pp 1093-1095.
Binding of hapten to a single-chain catalytic antibody demonstrated by ion spray mass spectrometry. G. Siuzdak, J.F. Krebs, S.J. Benkovic, & H.J. Dyson (1994) J. Am. Chem. Soc. 116, 7937-7938.
High-resolution solution structures of oxidized and reduced Escherichia coli thioredoxin. M.-F. Jeng, A.P. Campbell, T. Begley, A. Holmgren, D.A. Case, P.E. Wright, & H.J. Dyson (1994) Structure 2, 853-868.
Stabilization of a Type VI turn in a family of linear peptides in water solution. J. Yao, V.A. Feher, B.F. Espejo, M.T. Reymond, P.E. Wright, & H.J. Dyson (1994) J. Mol. Biol. 243, 736-753.
Three-dimensional structure of a Type VI turn in a linear peptide in water solution: evidence for stacking of aromatic rings as a major stabilizing factor. J. Yao, H.J. Dyson, & P.E. Wright (1994) J. Mol. Biol. 243, 754-766.
Nuclear magnetic resonance 15N and 1H resonance assignments and global fold of rusticyanin: Insights into the ligation and acid stability of the blue copper site. A.H. Hunt, A. Toy-Palmer, N. Assa-Munt, J. Cavanagh, R.C. Blake,II, & H.J. Dyson (1994) J. Mol. Biol. 244, 370-384.
The folding pathway of apomyoglobin. P.A. Jennings, H.J. Dyson, & P.E. Wright (1994) In: Statistical Mechanics, Protein Structure and Protein Substrate Interactions (S. Doniach Ed.) Plenum Press, New York. pp 7-18.
Analysis of peptide and protein structure. H.J. Dyson (1994) In: Immunological recognition of peptides in medicine and biology (N. Zegers, W. Boersma, & E. Claassen Eds.) CRC Press, London. pp 133-145.
Differential hydration of side chain protons in a short peptide in a highly populated Type VI turn conformation. J. Yao, R. Brüschweiler, H.J. Dyson, & P.E. Wright (1994) J. Am. Chem. Soc. 116, 12051-12052.
Antigenic peptides. H.J. Dyson & P.E. Wright (1995) FASEB J. 9, 37-42.
Comparison of the hydrogen exchange behavior of reduced and oxidized Escherichia coli thioredoxin. M.-F. Jeng & H.J. Dyson (1995) Biochemistry 34, 611-619.
Detection of a catalytic antibody species acylated at the active site by electrospray mass spectrometry. J.F. Krebs, G. Siuzdak, H.J. Dyson, J.D. Stewart, & S.J. Benkovic (1995) Biochemistry 34, 720-723.
Random coil H-1 chemical shifts obtained as a function of temperature and trifluoroethanol concentration for the peptide series GGXGG. G. Merutka, H.J. Dyson, & P.E. Wright (1995) J. Biomol. NMR 5, 14-24.
NMR of thioredoxin and glutaredoxin. H.J. Dyson (1995) Methods Enzymol. 252, 293-306.
Gene synthesis, high-level expression and mutagenesis of Thiobacillus ferrooxidans rusticyanin. His85 is a ligand to the blue copper center. D.R. Casimiro, A. Toy-Palmer, R.C. Blake,II, & H.J. Dyson (1995) Biochemistry 34, 6640-6648.
Complete 13C resonance assignments and coupling constants for recombinant rusticyanin: Prediction of secondary structure from patterns of chemical shifts. A. Toy-Palmer, S. Prytulla and H.J. Dyson (1995) FEBS Lett. 365, 35-41.
Proton sharing between cysteine thiols in Escherichia coli thioredoxin: implications for the mechanism of reduction of protein disulfides. M.-F. Jeng, A. Holmgren, & H.J. Dyson (1995) Biochemistry 34, 10101-10105.
1H, 13C and 15N chemical shift references in biomolecular NMR. D.S. Wishart, C.G. Bigam, J. Yao, F. Abildgaard, H.J. Dyson, E. Oldfield, J.L. Markley, & B.D. Sykes (1995) J. Biomol. NMR 6, 135-140.
Direct measurement of the Asp-26 pKa for reduced Escherichia coli thioredoxin by 13C NMR. M.-F. Jeng and H. J. Dyson (1996) Biochemistry 35, 1-6.
Folding of proteins and protein fragments. H.J. Dyson & P.E. Wright (1996) In: Encyclopedia of Nuclear Magnetic Resonance (ed. D.M. Grant and R.K. Harris) John Wiley, Chichester. pp 3811-3820.
Thioredoxin and glutaredoxin. H.J. Dyson (1996) In: Encyclopedia of Nuclear Magnetic Resonance (ed. D.M. Grant and R.K. Harris) John Wiley, Chichester. pp 4727-4733.
NMR structural studies of flexible molecules. P.E. Wright & H.J. Dyson (1996) In: NMR as a Structural Tool for Macromolecules (B.D. Nageswara Rao and M.D. Kemple, Eds) Plenum Publishing Corp, New York, pp 245-249.
Replacement of Trp-28 in Escherichia coli thioredoxin by site-directed mutagenesis affects thermodynamic stability but not function. I. Slaby, V. Cerna, M.-F. Jeng, H.J. Dyson and A. Holmgren (1996) J. Biol. Chem. 271, 3091-3096.
Solution conformation of an immunogenic peptide derived from the principal neutralizing determinant of the HIV-2 envelope glycoprotein gp125. A.P. Campbell, B.D. Sykes, E. Norrby, N. Assa-Munt and H. J. Dyson (1996) Folding and Design 1, 157-165.
Insights into protein folding from NMR. H.J. Dyson and P.E. Wright (1996) Ann. Rev. Phys. Chem. 47, 369-395.
NMR solution structure of Cu(I) rusticyanin from Thiobacillus ferrooxidans: Structural basis for the the extreme acid stability and redox potential. M. V. Botuyan, A. Toy-Palmer, J. Chung, R. C. Blake II, P. Beroza, D.A. Case & H. J. Dyson (1996) J. Mol. Biol. 263, 752-767.
Gene synthesis, high level expression and assignment of backbone 15N and 13C resonances of soybean leghemoglobin. S. Prytulla, H.J. Dyson and P.E. Wright (1996) FEBS Lett. 399, 383-289.
Structure-based design of a constrained-peptide mimic of the HIV-1 V3 loop neutralization site. J.B. Ghiara, D. Ferguson, A.C. Satterthwait, H.J. Dyson & I.A. Wilson (1997) J. Mol. Biol. 266, 31-39.
Folding propensities of peptide fragments of myoglobin. M.T. Reymond, G. Merutka, H.J. Dyson and P.E. Wright (1997) Protein Sci. 6, 706-716. PMC2143684
Effects of buried charged groups on cysteine thiol ionization and reactivity in Escherichia coli thioredoxin: Structural and functional characterization of mutants of Asp 26 and Lys 57. H.J. Dyson, M.-F. Jeng, L.L. Tennant, I. Slaby, M. Lindell, D.-S. Cui, S. Kuprin & A. Holmgren (1997) Biochemistry 36, 2622-2636.
Absence of a stable intermediate on the folding pathway of Protein A (B domain). Y. Bai, A. Karimi, H.J. Dyson and P.E. Wright (1997) Protein Sci.6, 1449-1457. PMC2143746
Contribution of increased length and intact capping sequences to the conformational preference for helix in a 31-residue peptide from the C-terminal sequence of myohemerythrin. M.T. Reymond, S. Huo, B. Duggan, P.E. Wright and H.J. Dyson (1997) Biochemistry 36, 5234-5244.
Populating the equilibrium molten globule state of apomyoglobin under conditions suitable for structural characterization by NMR. D. Eliezer, P.A. Jennings, H.J. Dyson and P.E. Wright (1997) FEBS Lett. 417, 92-96.
PCR-based gene synthesis for protein over-production. D. Casimiro, P.E. Wright and H.J. Dyson (1997) Structure 5, 1407-1412.
Electron spin envelope modulation spectra of Thiobacillus ferrooxidans rusticyanin and a mutant lacking one of the copper ligands. C.J. Bender, D. Casimiro and H.J. Dyson (1997) J. Chem. Soc. (Faraday) 93, 3967-3980.
Structure of the recombinant full-length Syrian hamster prion protein PrP(29-231): the N-terminus is highly flexible. D.G. Donne, J.H. Viles, J. Chung, D. Groth, I. Mehlhorn, F.E. Cohen, S.B. Prusiner, P.E. Wright & H.J. Dyson (1997) Proc. Natl. Acad. Sci. USA 94, 13452-13457. PMC28326
Chemical shift dispersion and secondary structure prediction in unfolded and partly-folded proteins. J. Yao, H.J. Dyson and P.E. Wright (1997) FEBS Lett. 419, 285-289.
Solution structure of the KIX domain of CBP bound to the transactivation domain of CREB: a model for activator:coactivator interactions I. Radhakrishnan, G. Perez-Alvarado, D. Parker, H.J. Dyson, M. Montminy and P.E. Wright (1997) Cell 91, 741-752.
Structural and dynamic characterization of partially folded states of apomyoglobin and implications for protein folding. D. Eliezer, J. Yao, H.J. Dyson and P.E. Wright (1998) Nature Struct. Biol. 5, 148-155.
A NOESY-HSQC simulation program SPIRIT. L. Zhu, H.J. Dyson and P.E. Wright (1998) J. Biomol. NMR 11, 17-29.
Calculations of electrostatic interactions and pKas in the active site of Escherichia coli thioredoxin. V. Dillet, H.J. Dyson and D. Bashford (1998) Biochemistry 37, 10298-10306.
Equilibrium NMR studies of unfolded and partly folded proteins. H.J. Dyson and P.E. Wright (1998) Nature Struct. Biol. 5, 499-503.
High resolution solution structure of the retinoid X receptor DNA binding domain. S.M.A. Holmbeck, M. P. Foster, D. R. Casimiro, D. Sem, H. J. Dyson and P. E. Wright (1998) J. Mol. Biol. 281, 271-284.
Sequence requirements for stabilization of a peptide reverse turn in water solution: proline is not essential for stability. H.J. Dyson, L. Bolinger, V.A. Feher, J.J. Osterhout, Jr., J. Yao, & P.E. Wright (1998) Eur. J. Biochem. 255, 462-471.
Conformational preferences in the Ser133-phosphorylated and non-phosphorylated forms of the kinase inducible transactivation domain of CREB I. Radhakrishnan, G.C. Perez-Alvarado, H.J. Dyson and P.E. Wright (1998) FEBS Lett. 430, 317-322.
1H, 13C and 15N NMR backbone assignments of 25.5 kDa metallo--lactamase from Bacteroides fragilis. S.D.B. Scrofani, P.E. Wright and H.J. Dyson (1998) J. Biomol. NMR 12, 201-202.
The identification of metal-binding ligand residues in metalloproteins using nuclear magnetic resonance spectroscopy. S.D.B. Scrofani, P.E. Wright and H.J. Dyson (1998) Protein Sci. 7, 2476-2479. PMC2143851
Glycosylation of threonine of the repeating unit of RNA polymerase II confers a structural change. E. E. Simanek, D.-H. Huang, L. Pasternack, O. Seitz, D.S. Millar, H.J. Dyson and C.-H. Wong (1998) J. Am. Chem. Soc. 120, 11567-11575.
NMR characterization of a single-cysteine mutant of Escherichia coli thioredoxin and a covalent thioredoxin-peptide complex. M.-F. Jeng, M.T. Reymond, L.L. Tennant, A. Holmgren and H.J. Dyson (1998). Eur. J. Biochem. 257, 299-308.
DNA-induced conformational changes are the basis for cooperative dimerization by the DNA binding domain of the retinoid X receptor. S.M.A. Holmbeck, H.J. Dyson and P.E. Wright (1998) J. Mol. Biol., 284, 533-539.
Quench-flow experiments combined with mass spectrometry show that apomyoglobin folds through an obligatory intermediate. V. Tsui, C. Garcia-Gonzalez, S. Cavagnero, G. Siuzdak, H.J. Dyson and P.E. Wright (1999) Protein Sci. 8, 45-49. PMC2144105
Effect of H helix destabilizing mutations on the kinetic and equilibrium folding of apomyoglobin. S. Cavagnero, H.J. Dyson and P.E. Wright. (1999) J. Mol. Biol. 285, 269-282.
Copper binding to the prion protein. Structural implications of four identical cooperative binding sites. J.H. Viles, S.B. Prusiner, F.E. Cohen, D.D. Goodin, P.E. Wright and H.J. Dyson (1999) Proc. Natl Acad. Sci. USA 96, 2042-2047. PMC26733
Improved low pH bicelle system for orienting macromolecules over a wide temperature range S. Cavagnero, H. J. Dyson and P.E. Wright (1999) J. Biomol. NMR 13, 387-391.
Structural analyses of CREB-CBP transcriptional activator-coactivator complexes by NMR spectroscopy: implications for mapping the boundaries of structural domains. I. Radhakrishnan, G.C. Perez-Alvarado, D. Parker, H.J. Dyson, M.R. Montminy and P.E. Wright (1999) J. Mol. Biol. 287, 859-865.
Association between the first two immunoglobulin-like domains of the neural cell adhesion molecule N-CAM. A. Atkins, M.J. Osborne, H.A. Lashuel, G.M. Edelman, P.E. Wright, B. A. Cunningham and H.J. Dyson (1999) FEBS Lett. 451, 162-168.
Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm. P.E. Wright and H.J. Dyson (1999) J. Mol. Biol. 293, 321-331.
Characterization of monomeric and dimeric B domain of staphylococcal protein A: Sources of stabilization of a 3-helix bundle protein. A. Karimi, M. Matsumura, P.E. Wright & H.J. Dyson. (1999) J. Pept. Res. 54, 344-352.
Inherent flexibility in a potent inhibitor of blood coagulation, recombinant nematode anticoagulant protein c2. B.M. Duggan, H.J. Dyson & P.E. Wright (1999) Eur. J. Biochem. 265, 539-548.
Assignment of 1H, 13C and 15N resonances of reduced Escherichia coli glutaredoxin 2. B. Xia, J. Chung, A. Vlamis-Gardikas, A. Holmgren, P.E. Wright and H.J. Dyson (1999) J. Biomol. NMR 14, 197-198.
NMR characterization of the metallo--lactamase from Bacteroides fragilis and its interaction with a tight-binding inhibitor: Role of an active-site loop S.D.B. Scrofani, J. Chung, J.J.A. Huntley, S. J. Benkovic, P.E. Wright and H.J. Dyson (1999) Biochemistry 38, 14507-14514.
Backbone resonance assignments for the Fv fragment of the catalytic antibody NPN43C9 with bound p-nitrophenol. G. Kroon, M. Martinez-Yamout, J.F. Krebs, John Chung, H.J. Dyson & P.E. Wright (1999) J. Biomol. NMR 15, 83-84.
Amide proton hydrogen exchange rates of sperm whale myoglobin obtained from 15N-1H NMR spectra. S. Cavagnero, Y. Thériault, S.S. Narula, H.J. Dyson & P.E. Wright. (2000) Protein Sci. 9, 186-193. PMC2144433
NMR solution structure of the inserted domain of human leukocyte function associated antigen-1. G.B. Legge, R.W. Kriwacki, J. Chung, U. Hommel, P. Ramage, D.A. Case, H.J. Dyson and P.E. Wright (2000) J. Mol. Biol. 295, 1251-1264.
DNA-induced α-helix capping in conserved linker sequences is a determinant of binding affinity in Cys2-His2 zinc fingers. J.H. Laity, H.J. Dyson and P.E. Wright (2000) J. Mol. Biol. 295, 719-727.
Spectroscopic methods. H.J. Dyson (2000) Encyclopedia of Life Sciences Macmillan Online publication www.els.net.
Backbone HN, N, C, C’ and C assignments of the 19 kDa DHFR/NADPH complex at 9°C and pH 7.6. E. Zaborowski, J. Chung, G. Kroon, H.J. Dyson and P.E. Wright (2000) J. Biomol. NMR 16, 349-350.
Assignment of 1H, 13C and 15N resonances of the I-domain of human leukocyte function associated antigen-1. R.W. Kriwacki, G.B. Legge, U. Hommel. P. Ramage, J. Chung, L.L. Tennant, P.E. Wright and H.J. Dyson (2000) J. Biomol. NMR 16, 271-272.
Native and non-native secondary structure and dynamics in the pH 4 intermediate of apomyoglobin. D. Eliezer, J. Chung, H.J. Dyson and P.E. Wright (2000) Biochemistry 39, 2894-2901.
Identification of the regions involved in DNA binding by the mouse PEBP2 protein. G.C. Perez-Alvarado, A. Munnerlyn, H.J. Dyson, R. Grosschedl and P.E. Wright (2000) FEBS Lett. 470, 125-130.
Alternative splicing of Wilms’ tumor suppressor protein modulates DNA binding activity through isoform-specific DNA-induced conformational changes. J.H. Laity, J. Chung, H.J. Dyson, P.E. Wright (2000) Biochemistry 39, 5341-5348.
Conservation of folding pathways in evolutionarily distant globin sequences. C. Nishimura, S. Prytulla, H.J. Dyson & P.E. Wright (2000) Nature Struct. Biol. 7, 679-686.
Solution structure of the cysteine-rich domain of the Escherichia coli chaperone protein DnaJ. M. Martinez-Yamout, G.B. Legge, O. Zhang, P.E. Wright and H.J. Dyson. (2000) J. Mol. Biol. 300, 805-818.
Changes in the apomyoglobin folding pathway caused by mutation of the distal histidine residue. C. Garcia, C. Nishimura, S. Cavagnero, H.J. Dyson and P.E. Wright (2000) Biochemistry 39, 11227-11237.
Solution structure of the TAZ2 (CH3) domain of the transcriptional adaptor protein CBP. R.N. De Guzman, H.Y. Liu, M. Martinez-Yamout, H.J. Dyson and P.E. Wright (2000) J. Mol. Biol. 303, 243-253.
Random coil chemical shifts in acidic 8 M urea: Implementation of random coil shift data in NMRView. S. Schwarzinger, G.J.A. Kroon, T.R. Foss, P.E. Wright and H.J. Dyson (2000) J. Biomol. NMR 18, 43-48.
Dynamics of the metallo--lactamase from Bacteroides fragilis in the presence and absence of a tight-binding inhibitor. J.J.A. Huntley, S.D.B. Scrofani, M.J. Osborne, P.E. Wright and H.J. Dyson (2000) Biochemistry 39, 13356-13364.
Molecular basis for modulation of biological function by alternate splicing of the Wilms’ tumor suppressor protein. J.H. Laity, H.J. Dyson and P.E. Wright (2000) Proc. Natl. Acad. Sci. USA 97, 11932-11935. PMC17272
Solution structure and acetyl-lysine binding activity of the GCN5 bromodomain. B.P. Hudson, M.A. Martinez-Yamout, H.J. Dyson and P.E. Wright (2000). J. Mol. Biol. 304, 335-370.
Structure of the PHD zinc finger from human Williams-Beuren Syndrome transcription factor. J. Pascual, M. Martinez-Yamout, H.J. Dyson and P.E. Wright (2000). J. Mol. Biol. 304, 723-729.
NMR methods for the elucidation of the structure and dynamics in disordered states. H.J. Dyson and P.E. Wright (2001) Methods Enzymol. 339, 258-270.
Local structural plasticity of the prion protein. Analysis of NMR relaxation dynamics. J.H. Viles, D. Donne, G.J.A. Kroon, S.B. Prusiner, F.E. Cohen, H.J. Dyson and P.E. Wright (2001) Biochemistry 40, 2743-2753.
Two different neurodegenerative diseases caused by proteins with similar structures. H. Mo, R.C. Moore, F.E. Cohen, D. Westaway, S.B. Prusiner, P.E. Wright and H.J. Dyson (2001) Proc. Natl. Acad. Sci. USA 98, 2352-2357. PMC30142
NMR structural and dynamic characterization of the acid-unfolded state of apomyoglobin: a model system for the initial steps of folding. J. Yao, J. Chung, D. Eliezer, P.E. Wright and H.J. Dyson (2001) Biochemistry 40, 3561-3571.
SANE (Structure assisted NOE evaluation): An automated model-based approach for NOE assignment. B.M. Duggan, G.B. Legge, H.J. Dyson and P.E. Wright (2001). J. Biomol. NMR 19, 321-329.
Genomic-scale comparison of sequence- and structure-based methods of function prediction: Does structure provide additional insight? J.S. Fetrow, N. Siew, J.A. Di Gennaro, M. Martinez-Yamout, H.J. Dyson and J. Skolnick (2001) Protein Sci. 10, 1005-1014. PMC2374196
Sequence-dependent correction of random coil chemical shifts. S. Schwarzinger, G.J.A. Kroon, T.R. Foss, J. Chung, P.E. Wright and H.J. Dyson (2001). J. Am. Chem. Soc. 123, 2970-2978.
Potential bias in NMR relaxation data introduced by peak intensity analysis and curve fitting methods. J.H. Viles, B.M. Duggan, E. Zaborowski, S. Schwarzinger, J.J.A. Huntley, G.J.A. Kroon, H.J. Dyson and P.E. Wright (2001). J. Biomol. NMR 21, 1-9.
Structural and dynamic characterization of an unfolded state of poplar apo-plastocyanin formed under nondenaturing conditions. Y. Bai, J. Chung, H.J. Dyson and P.E. Wright (2001) Protein Sci. 10, 1056-1066. PMC2374208
Solution structure of Escherichia coli glutaredoxin-2 shows similarity to mammalian glutathione-S-transferases. B. Xia, A. Vlamis-Gardikas, A. Holmgren, P.E. Wright and H.J. Dyson (2001) J. Mol. Biol. 310, 907-918.
Backbone dynamics in dihydrofolate reductase complexes: role of loop flexibility in the catalytic mechanism. M.J. Osborne, J. Schnell, S.J. Benkovic, H.J. Dyson and P.E. Wright (2001). Biochemistry 40, 9846-9859.
Solution structure of the third immunoglobulin domain of the neural cell adhesion molecule N-CAM: Can solution studies define the mechanism of homophilic binding? A. Atkins, J. Chung, S. Deechongkit, E. B. Little, G. M. Edelman, P. E. Wright, B. A. Cunningham and H. J. Dyson (2001) J. Mol. Biol. 311, 161-172.
Conformational and dynamic characterization of the molten-globule state of an apomyoglobin mutant with an altered folding pathway. S. Cavagnero, S. Schwarzinger, H.J. Dyson and P.E. Wright (2001). Biochemistry 40, 14459-14467.
Native and non-native secondary structure and dynamics in the pH 4 intermediate of apomyoglobin.” D. Eliezer, J. Chung, H. J. Dyson, and P.E. Wright (2001) In: “Conformational Diseases – a Compendium,” Eds. B. Solomon, A. Taraboulos, and E. Katchalski-Katzir, S. Karger Pub, pp. 113-120.
Structure and dynamics of disordered proteins. H.J. Dyson and P.E. Wright (2002) Encyclopedia of NMR 9, 449-457.
Mutual synergistic folding in recruitment of CBP/p300 by p160 nuclear receptor coactivators. S.J. Demarest, M. Martinez-Yamout, J. Chung, H. Chen, H.J. Dyson, R.M. Evans and P.E. Wright (2002) Nature 415, 549-553.
Comparison of protein solution structures refined by molecular dynamics simulation in vacuum, with a generalized Born model and with explicit water. B. Xia, V. Tsui, D.A. Case, H.J. Dyson and P.E. Wright (2002) J. Biomol. NMR 22, 317-331.
Coupling of folding and binding for unstructured proteins. H.J. Dyson and P.E. Wright (2002) Curr. Opin. Struct. Biol. 12, 54-60.
Assignment of a 15 kDa protein complex formed between the p160 coactivator ACTR and CREB binding protein. S.J. Demarest, J. Chung, H.J. Dyson and P.E. Wright (2002) J. Biomol. NMR 22, 377-378.
Structural basis for Hif-1/CBP recognition in the cellular hypoxic response. S. Dames, M. Martinez-Yamout, R. N. DeGuzman, M. Allen, H.J. Dyson and P.E. Wright (2002) Proc. Natl. Acad. Sci. USA 99, 5271-5276. PMC122759
Insights into the structure and dynamics of unfolded proteins from NMR. H. J. Dyson and P. E. Wright. (2002) Adv. Prot. Chem. 62, 311-340.
The apomyoglobin folding pathway revisited: Structural heterogeneity in the kinetic burst phase intermediate. C. Nishimura, H.J. Dyson and P.E. Wright (2002). J. Mol. Biol. 322, 483-489. (1) erratum
Mapping long-range contacts in a highly unfolded protein. M.A. Lietzow, M. Jamin, H.J. Dyson and P.E. Wright (2002). J. Mol. Biol. 322, 655-662.
Molecular hinges during protein folding: the urea-denatured state of apomyoglobin. S. Schwarzinger, P.E. Wright and H.J. Dyson. (2002) Biochemistry 41, 12681-12686.
Roles of phosphorylation and helix propensity in the binding of the KIX domain of CBP by constitutive (c-Myb) and inducible (CREB) activators. T. Zor, B.M. Mayr, H.J. Dyson and P.E. Wright (2002). J. Biol. Chem. 277, 42241-42248.
Cooperativity in transcription factor binding to the coactivator CREB-binding Protein (CBP): MLL binds to an allosteric site on the KIX domain. N.K. Goto, T. Zor, M. Martinez-Yamout, H.J. Dyson and P.E. Wright (2002). J. Biol. Chem. 277, 43168-43174.
Folding of a -sheet protein monitored by real-time NMR spectroscopy. M. Mizuguchi, G. Kroon, P.E. Wright and H.J. Dyson (2003) J. Mol. Biol. 328, 1161-1171.
Plasmodium vivax peptides display conformational preferences for folded forms in solution. T.E. Lehmann, G. Kroon, M.A. Lorenzo, H. Bermúdez, H. Perez and H.J. Dyson (2003) J. Peptide Research 61, 252-262.
Role of a solvent-exposed tryptophan in the recognition and binding of antibiotic substrates for a metallo--lactamase. J.J.A. Huntley, W. Fast, S.J. Benkovic, P.E. Wright and H.J. Dyson (2003). Protein Sci. 12, 1368-1375. PMC2323931
Monomeric complex of human orphan estrogen related receptor-2 with DNA: A pseudodimer interface mediates extended half-site recognition. M.D. Gearhart, S.M.A. Holmbeck, R.M. Evans, H.J. Dyson and P.E. Wright (2003) J. Mol. Biol. 327, 819-832.
Changes in structure and dynamics of the Fv fragment of a catalytic antibody upon binding of inhibitor. G. J.A. Kroon, H. Mo, M. A. Martinez-Yamout, H. J. Dyson and P. E. Wright (2003) Protein Sci. 12, 1386-1394. PMC2323930
Structure of the nuclear factor ALY: insights into post-transcriptional regulatory and mRNA export processes. G.C. Perez-Alvarado, M. Martinez-Yamout, M. Allen, R. Grosschedl, H.J. Dyson and P.E. Wright (2003) Biochemistry 42, 7348-7357.
Diagnostic chemical shift markers for loop conformation and substrate and cofactor binding in dihydrofolate reductase complexes. M. J. Osborne, R. P. Venkitakrishnan, H. J. Dyson and P. E. Wright (2003). Protein Science 12, 2230-2238. PMC2366930
Role of the B helix in early folding events in apomyoglobin: evidence from site-directed mutagenesis for native-like long range interactions. C. Nishimura, P.E. Wright and H.J. Dyson (2003). J. Mol. Biol. 334, 293-307.
Packing, specificity and mutability at the binding interface between the p160 coactivator and CREB-binding protein. S.J. Demarest, S. Deechongkit, H.J. Dyson, R.M. Evans and P.E. Wright (2004). Protein Sci. 13, 203-210. PMC2286511
Effect of co-factor binding and loop conformation on fast methyl dynamics in DHFR. J.R. Schnell H.J. Dyson and P.E. Wright (2004). Biochemistry 43, 374-383.
Unfolded proteins and protein folding studied by NMR. H.J. Dyson and P.E. Wright (2004). Chemical Reviews 104, 3607-3622. editorial
Structure, dynamics and catalytic function in dihydrofolate reductase. J.R. Schnell, H.J. Dyson and P.E. Wright (2004). Ann. Rev. Biophys. Biomol. Struct. 33, 119-140.
Interaction of the TAZ1 domain of CREB-binding protein with the activation domain of CITED2: Regulation by competition between intrinsically unstructured ligands for non-identical binding sites. R. N. De Guzman, M. A. Martinez-Yamout, H. J. Dyson, and P. E. Wright (2004). J. Biol. Chem. 279, 3042-3049.
Structure and function of the CBP/p300 TAZ domains. R.N. De Guzman, M.A. Martinez-Yamout, H.J. Dyson and P.E. Wright (2004). In Zinc Finger Proteins: from Atomic Contact to Cellular Function (eds. S. Iuchi and N. Kuldell) Landes Biosciences. Chapter 17, pp 1-7.
Recognition of the mRNA Type II AU-rich element by the tandem zinc finger domain of TIS11d. B.P. Hudson, M.A. Martinez-Yamout, J. Chung, H.J. Dyson, P.E. Wright (2004). Nature Struct. Biol. 11,257-264.
Solution structure of the KIX domain of CBP bound to the transactivation domain of c-Myb. T. Zor, R.N. De Guzman, H.J. Dyson and P.E. Wright (2004). J. Mol. Biol. 337, 521-534.
Activation of the redox-regulated chaperone Hsp33 by domain unfolding. P.C.F. Graf, M.A. Martinez-Yamout, S. VanHaerents, H. Lilie, H.J. Dyson and U. Jakob (2004). J. Biol. Chem. 279, 20529-20538.
Disulfide bonding arrangements in active forms of the somatomedin B domain of human vitronectin. Y. Kamikubo, R. DeGuzman, G. Kroon, S. Curriden, J. Neels, M.J. Churchill, P. Dawson, S. Oldziej, A. Jagielska, H.A. Scheraga, D.J. Loskutoff and H.J. Dyson (2004). Biochemistry 43, 6519-6534.
The CBP/p300 TAZ1 domain in its native state is not a binding partner of MDM2. T. Matt, M.A. Martinez-Yamout, H.J. Dyson and P.E. Wright (2004). Biochem. J. 381, 685-691. PMC1133877 commentary
The LEF-1 HMG domain undergoes a disorder-to-order transition upon formation of a complex with cognate DNA. J.J. Love, X. Li, J. Chung, H.J. Dyson and P.E. Wright (2004). Biochemistry 43, 8725-8734.
Structural characterization of unfolded states of apomyoglobin using residual dipolar couplings. R.M. Borges, H.J. Dyson and P.E. Wright (2004) J. Mol. Biol. 330, 1131-1142.
The zinc-dependent redox switch domain of the chaperone Hsp33 has a novel fold. H.-S. Won, L. Y. Low, R. N. De Guzman, M.A. Martinez-Yamout, U. Jakob and H.J. Dyson (2004). J. Mol. Biol. 341, 893-899.
ZZ Domain of CBP – a novel fold for a protein interaction module. G.B. Legge, M.A. Martinez-Yamout, G.J.A. Kroon, D. Hambly, H. J. Dyson and P.E. Wright (2004). J. Mol. Biol. 343, 1081-1093.
Conformational changes in the active site loops of dihydrofolate reductase during the catalytic cycle. R.P. Venkitakrishnan, E. Zaborowski, D. McElheny, S.J. Benkovic, H.J. Dyson and P.E. Wright (2004). Biochemistry 43, 16046-16055. erratum
CBP/p300 TAZ1 domain forms a structural scaffold for ligand binding. R.N. De Guzman, J.M. Wojciak, M.A. Martinez-Yamout, H.J. Dyson and P.E. Wright (2005). Biochemistry, 44, 490-497.
Generation of native-like models from limited NMR data, modern force fields and advanced conformational sampling. J. Chen, H.-S. Won, W. Im, H.J. Dyson and C.L. Brooks, III (2005). J. Biomol. NMR 31, 59-64.
Intrinsically unstructured proteins and their functions. H.J. Dyson and P.E. Wright (2005). Nature Rev. Mol. Cell Biol. 6, 197-208.
Elucidation of the protein folding landscape by NMR. H.J. Dyson and P.E. Wright (2005). Methods Enzymol. 394, 299-321.
Backbone and side chain H-1, C-13 and N-15 assignments of Escherichia coli SdiA1-171, the autoinducer binding domain of a quorum sensing protein. Y.Yao, M.A.Martinez-Yamout and H.J. Dyson (2005). J. Biomol. NMR 31, 373-374.
Enhanced picture of protein folding intermediates using organic solvents in HD exchange and quench flow experiments. C. Nishimura, H.J. Dyson and P.E. Wright (2005). Proc. Natl Acad. Sci. USA 102, 4765-4770. PMC555694
Defining the role of active-site loop fluctuations in dihydrofolate reductase catalysis. D. McElheny, J.R. Schnell, J. Lansing, H.J. Dyson and P.E. Wright (2005). Proc. Natl. Acad. Sci. USA 102, 5032-5037. PMC556001
Sequence determinants of a protein folding pathway. C. Nishimura, M.A. Lietzow, H.J. Dyson and P. E. Wright (2005). J. Mol. Biol. 351, 383-392.
Solution structure of the N-terminal zinc fingers of the Xenopus laevis double-stranded RNA-binding protein ZFa. H. M. Möller, M.A. Martinez-Yamout, H. J. Dyson and P. E. Wright (2005). J. Mol. Biol. 351, 718-730. .
Structural basis for cooperative transcription factor binding to the CBP coactivator. R.N. De Guzman, N. Goto, H.J. Dyson and P.E. Wright (2006). J. Mol. Biol. 355, 1005-1013.
NMR solution structure of the peptide fragment 1-30, derived from mouse Doppel protein, in DHPC micelles. E. Papadopoulos, K. Oglęcka, L. Mäler, J. Jarvet, P.E. Wright, H.J. Dyson, A. Gräslund (2006). Biochemistry 45, 159-166.
Identification of native and non-native structure in kinetic folding intermediates of apomyoglobin. C. Nishimura, H.J. Dyson and P.E. Wright (2006). J. Mol. Biol. 355, 139-156.
Structure of the Escherichia coli quorum sensing protein SdiA: activation of the folding switch by acyl homoserine lactones. Y. Yao, M.A. Martinez-Yamout, T.J. Dickerson, A.P. Brogan, P.E. Wright and H.J. Dyson (2006). J. Mol. Biol. 355, 262-273.
Induced fit and “lock-and-key” recognition of 5S RNA by zinc fingers of transcription factor IIIA. B.M. Lee, J. Xu, M.D. Gearhart, B.K. Clarkson, M.A. MartinezYamout, H.J. Dyson, D.A. Case, J.M. Gottesfeld, and P.E. Wright (2006). J. Mol. Biol. 357, 275-291.
The reduced and denatured form of the somatomedin B domain of vitronectin refolds into a stable, biologically active form. Y. Kamikubo, G. Kroon, S.A. Curriden, H.J. Dyson and D.J. Loskutoff (2006) Biochemistry 45, 3297-3306.
According to current textbooks, a well-defined three-dimensional structure is a prerequisite for the function of the protein. Is this correct? H.J. Dyson and P.E. Wright (2006) IUBMB Life 58, 107-109.
Localization of sites of interaction between p23 and Hsp90 in solution. M.A. Martinez-Yamout, R.P. Venkitakrishnan, N.E. Preece, G. Kroon, P.E. Wright and H.J. Dyson (2006). J. Biol. Chem. 281, 14457-14464.
An NMR perspective on enzyme dynamics. D.D. Boehr, H.J. Dyson and P.E. Wright (2006). Chem. Rev. 106, 3055-3079.
The dynamic energy landscape of dihydrofolate reductase catalysis. D.D. Boehr, D. McElheny, H. J. Dyson, P.E. Wright (2006). Science 313, 1638-1642.
The role of hydrophobic interactions in initiation and propagation of protein folding. H.J. Dyson, P.E. Wright, H.A. Scheraga (2006) Proc. Natl. Acad. Sci. USA 103, 13057-13061. PMC1559752
Solution structure of the Hdm2 C2H2C4 RING finger, a domain critical for ubiquitination of p53. M. Kostic, T. Matt, M.A. Martinez-Yamout, H.J. Dyson and P.E. Wright (2006) J. Mol. Biol. 363, 433-450.
Mechanism of coupled folding and binding of an intrinsically unstructured protein. K. Sugase, H.J. Dyson and P.E. Wright (2007) Nature 447, 1021-1025. comment
Embryonic neural inducing factor Churchill is not a DNA-binding zinc finger: solution structure reveals a solvent-exposed -sheet and zinc binuclear cluster. B.M. Lee, B.A. Buck-Koehntop, M.A. Martinez-Yamout, H.J. Dyson and P.E. Wright (2007) J. Mol. Biol. 371, 1274-1289. PMC1994575
Structure of the of the Wilms’ Tumor suppressor protein zinc finger domain bound to DNA. R. Stoll, B.M. Lee, E. Debler, J.H. Laity, I.A. Wilson, H.J. Dyson and P.E. Wright (2007) J. Mol. Biol. 372, 1227-1245.
Structure discrimination for the C-terminal domain of E. coli trigger factor in solution. Y. Yao, G. Bhabha, M. Landes and H.J. Dyson (2007) J. Biomol. NMR 40, 23-30
NMR detection of adventitious binding of xylose to the quorum-sensing protein SdiA of Escherichia coli. Y. Yao, T.J. Dickerson, M.S. Hixon and H. J. Dyson (2007). Bioorg. Med Chem. Lett. 17, 6202-6205. PMC2249169
Tailoring relaxation dispersion experiments for fast-associating protein complexes. K. Sugase, J.C. Lansing, H.J. Dyson and P.E. Wright (2007). J. Am. Chem. Soc. 129, 13406-13407. PMC2533806
NMR relaxation study of the complex formed between the nuclear coactivator binding domain of CBP and a fragment of the nuclear hormone receptor coactivator ACTR. M.-O. Ebert, S.-H. Bae, H.J. Dyson, P.E. Wright (2008) Biochemistry 47, 1299-1308.
Structural characterization of partly folded intermediates of apomyoglobin H64F. S. Schwarzinger, R. Mohana-Borges, G.J.A. Kroon, H.J. Dyson and P.E. Wright (2008) Protein Sci. 17, 313-321. PMC2222724
Modeling transient collapsed states of an unfolded protein to provide insights into early folding processes. D.J. Felitsky, M.A. Lietzow, H.J. Dyson and P.E. Wright (2008) Proc. Natl. Acad. Sci. USA 105, 6278-6283. PMC2359776
The kinetic and equilibrium molten globule intermediates of apoleghemoglobin differ in structure. C. Nishimura, H.J. Dyson and P.E. Wright (2008) J. Mol. Biol. 378, 715-725. PMC2409369
Hydrogen-deuterium exchange strategy for delineation of contact sites in protein complexes. H.J. Dyson, M. Kostic, J. Liu and M.A. Martinez-Yamout (2008) FEBS Lett. 582, 1495-1500. PMC2440508
Transfer of flexibility between ankyrin repeats in IB upon formation of the NF-B complex. S.-C. Sue, C. Cervantes, E.A. Komives and H.J. Dyson (2008) J. Mol. Biol. 380, 917-931. PMC2603615
Conformational relaxation following hydride transfer plays a limiting role in dihydrofolate reductase catalysis. D.D. Boehr, H.J. Dyson and P.E. Wright (2008) Biochemistry 47, 9227-9233. PMC2562322
Hierarchical folding mechanism of apomyoglobin revealed by ultra-fast H/D exchange coupled with 2D NMR T. Uzawa, C. Nishimura, S. Akiyama, K. Ishimori, S. Takahashi, H. J. Dyson and P. E. Wright (2008) Proc. Natl. Acad. Sci. USA 105, 13859-13864. PMC2544544
Amylin proprotein processing generates progressively more amyloidogenic peptides that initially sample the helical state. I.T. Yonemoto, G.J.A. Kroon, H.J. Dyson, W.E. Balch and J.W. Kelly (2008) Biochemistry 47, 9900-9910. PMC2662778
The intrinsically disordered RNR inhibitor Sml1 is a dynamic and globular dimer. J. Danielsson, L. Liljedahl, E. Bárány-Wallje, P. Sønderby, L.H. Kristensen, M. Martinez-Yamout, H.J. Dyson, P.E. Wright, F.M. Poulsen, L. Mäler, A. Gräslund and B.B. Kragelund (2008) Biochemistry 47, 13428-13437. PMC2747730
Linking folding and binding. P.E. Wright and H.J. Dyson (2009) Curr. Opin. Struct. Biol. 19, 31-38. PMC2675572
Mapping protein folding landscapes by NMR relaxation. P.E. Wright, D.J. Felitsky, K. Sugase and H.J. Dyson (2009). In Water and Biomolecules—Physical Chemistry of Life Phenomena (K. Kuwajima, F. Hirata, Y. Goto, M. Kataoka and M. Terazima, eds) Ch. 1. pp1-11.
Functional unfolded proteins – how, when, where and why. H.J. Dyson, S.-C. Sue and P.E. Wright (2009). In Water and Biomolecules—Physical Chemistry of Life Phenomena (K. Kuwajima, F. Hirata, Y. Goto, M. Kataoka and M. Terazima, eds) Ch. 6, pp 123-136.
Structural basis for recruitment of CBP/p300 coactivators by STAT1 and STAT2 transactivation domains. J.M. Wojciak, M.A. Martinez-Yamout, H.J. Dyson and P.E. Wright (2009) EMBO J. 28, 948-958. PMC2670858
Mapping the interactions of the p53 transactivation domain with the KIX domain of CBP. C.W. Lee, M. Arai, M.A. Martinez-Yamout, H.J. Dyson and P.E. Wright (2009) Biochemistry 28, 948-958. PMC2765525
Cooperative regulation of p53 by modulation of ternary complex formation with CBP/p300 and HDM2. J. C. Ferreon, C.W. Lee, M. Arai, M.A. Martinez-Yamout, H.J. Dyson and P.E. Wright (2009) Proc. Natl. Acad. Sci. USA 106, 6591-6596. PMC2672497
Interaction of the IκBα C-terminal PEST sequence with NF-κB: Insights into the inhibition of NF-B DNA binding by IκBα. S.C. Sue and H.J. Dyson (2009). J. Mol. Biol. 388, 824-838. PMC2688455
Prediction of the rotational tumbling for proteins with long disordered segments. S.H. Bae, H.J. Dyson and P.E. Wright (2009) J. Am. Chem. Soc. 131, 6814-6821. PMC2694746
Evaluating -turn mimics as -sheet folding nucleators. A.A. Fuller, D. Du, F. Liu, J.E. Davoren, G. Bhabha, G. Kroon, D.A. Case, H.J. Dyson, E.T. Powers, P. Wipf, M. Gruebele and J.W. Kelly (2009) Proc. Natl. Acad. Sci. USA 106, 11067-11072. PMC2708776
Functional dynamics of the folded ankyrin repeats of IB revealed by nuclear magnetic resonance C.F. Cervantes, P.R.L. Markwick, S.-C. Sue, J.A. McCammon, H.J. Dyson and E.A. Komives (2009). Biochemistry 48, 8023-8031. PMC2728578
Structural basis for subversion of cellular control mechanisms by the adenoviral E1A oncoprotein. J.C. Ferreon, M. Martinez-Yamout, H.J. Dyson, and P.E. Wright (2009) Proc. Natl. Acad. Sci. USA 106, 13260-13265. PMC2726373
Prion proteins with pathogenic and protective mutations show similar structure and dynamics. S.-H. Bae, G. Legname, A. Serban, S.B. Prusiner, P.E. Wright and H.J. Dyson (2009) Biochemistry 48, 8120-8128. PMC2762478
Millisecond timescale fluctuations in dihydrofolate reductase are exquisitely sensitive to the bound ligands. D.D. Boehr, D. McElheny, H.J. Dyson and P.E. Wright (2010) Proc. Natl. Acad. Sci. USA 107, 1373-1378. PMC2824364
Energetic frustration of apomyoglobin folding: role of the B helix. C. Nishimura, H.J. Dyson and P.E. Wright (2010) J. Mol. Biol. 396, 1319-1328. PMC2827033
Spectroscopic Techniques. H.J. Dyson (2010) In: Encyclopedia of Life Sciences John Wiley & Sons, Ltd: Chichester. http://www.els.net/ [DOI: 10.1002/9780470015902.a0002703.pub2]
Leu628 of the KIX domain of CBP is a key residue for the interaction with the MLL transactivation domain. M. Arai, H.J. Dyson and P.E. Wright (2010) FEBS Lett. 584, 4500-4504. PMC2993637
Structure of the p53 transactivation domain in complex with the nuclear receptor coactivator binding domain of CREB binding protein. C.W. Lee, M.A. Martinez-Yamout, H.J. Dyson and P.E. Wright (2010) Biochemistry 49, 9964-9971. PMC2982890
The RelA nuclear localization signal folds upon binding to IB. C.F. Cervantes, S. Bergqvist, M. Kjaergaard, G. Kroon, S.-C. Sue, H.J. Dyson and E.A. Komives (2011) J. Mol. Biol. 405, 754-764. PMC3056351
Detection of a ternary complex of NFB and IB with DNA provides insights into how IB removes NFB from transcription sites. S.C. Sue, V. Alverdi, E.A. Komives and H.J. Dyson (2011) Proc. Natl. Acad. Sci. USA 108, 1367-1372. PMC3029698
The client protein p53 forms a molten globule-like state in the presence of Hsp90. S.J. Park, M.A. Martinez-Yamout and H.J. Dyson (2011) Nature Struct. Mol. Biol. 18, 537-542. PMC3087862
A dynamic knockout reveals that conformational fluctuations influence the chemical step of catalysis. G. Bhabha, J. Lee, D.C. Ekiert, J. Gam, I.A. Wilson, H.J. Dyson, S.J. Benkovic and P.E. Wright (2011) Science 332, 234-238. PMC3151171
Dynamic interaction of Hsp90 with its client protein p53. S.J. Park, M. Kostic and H.J. Dyson. (2011) J. Mol. Biol. 411, 158-173. PMC3143201
Consequences of stabilizing the natively disordered F helix for the folding pathway of apomyoglobin. C. Nishimura, H.J. Dyson and P.E. Wright (2011) J. Mol. Biol. 411, 248-263. PMC3143293
Expanding the proteome: disordered and alternatively folded proteins. H.J. Dyson (2011) Quart. Rev. Biophysics 44, 467-518. PMC3189428
Roles of intrinsic disorder in protein-nucleic acid interactions. H.J. Dyson (2012) Mol. BioSyst. 8, 97-104. PMC3600845
Volume Introduction. H.J. Dyson (2012) In: Edward H. Egelman, editor: Comprehensive Biophysics. 1. Biophysical Techniques for Structural Characterization of Macromolecules, H. Jane Dyson. Oxford: Academic Press. p 1.
Introduction to solution-state NMR spectroscopy. H.J. Dyson and A.G. Palmer, III (2012). In: Edward H. Egelman, editor: Comprehensive Biophysics. 1. Biophysical Techniques for Structural Characterization of Macromolecules, H. J. Dyson. Oxford: Academic Press. pp 136-159.
Kaiso uses all three zinc fingers and adjacent sequence motifs for high affinity binding to sequence-specific and methyl CpG targets. B.A. Buck-Koehntop, M.A. Martinez-Yamout, H.J. Dyson and P.E. Wright (2012) FEBS Lett. 586, 734-739. PMC3309074
NMR studies of unfolded but functional proteins. H.J. Dyson (2012) RSC Biomolecular Science Series 25, Recent Developments in Biomolecular NMR (M. Clore and J. Potts, eds) Ch. 5, pp 111-128.
Homo-dimerization of the PAS-B domains of hypoxia inducible factors. J. Zhu, M.A. Martinez-Yamout, R. Cardoso, J. Yan, R.A. Love, N. Grodsky, A. Brooun and H.J. Dyson (2012) J. Phys. Chem. B 116, 6960-6965. PMC3376167
Role of disorder in IB-NFB interaction. H.J. Dyson and E.A. Komives (2012) IUBMB Life 64, 499-505. PMC3575514
Molecular basis for recognition of methylated and specific DNA sequences by the zinc finger protein Kaiso. B.A. Buck-Koehntop, R.L. Stanfield, D.C. Ekiert, M.A. Martinez-Yamout, J. Jane Dyson, I.A. Wilson and P.E. Wright (2012) Proc. Natl. Acad. Sci. USA 109, 15229-15234. PMC3458336
CheShift-2 resolves a local inconsistency between two X-ray crystal structures. J.A. Vila, S.-C. Sue, J.S. Fraser, H.A. Scheraga and H.J. Dyson (2012) J. Biomol. NMR 54, 193-198. PMC3471536
Identification of Cys 255 in HIF-1 as a novel site for development of covalent inhibitors of HIF-1/ARNT PasB domain protein-protein interaction. R. Cardoso, R. Love, C. Nilsson, S. Bergqvist, D. Nowlin, J. Yan, K. K.-C. Liu, J. Zhu, P. Chen, Y.-L. Deng, H.J. Dyson, M.J. Greig and A. Brooun (2012) Protein Sci. 21, 1885-1896. PMC3575918
Coupled folding and binding. H.J. Dyson (2013) Encyclopedia of Biophysics Springer. (Ed. G.C.K. Roberts), pp 381-385.
Long-range effects and functional consequences of stabilizing mutations in the ankyrin repeat in the ankyrin repeat domain of IB. C.F. Cervantes, L.D. Handley, S.-C. Sue, H.J. Dyson and E.A. Komives (2013) J. Mol. Biol. 425, 902-913. PMC3744861
Localized conformational excursions promote amyloidogenic conformations in transthyretin. K.H. Lim, H.J. Dyson, J.W. Kelly and P.E. Wright (2013) J. Mol. Biol. 425, 977-988. PMC3594634
What’s in a name? Why these proteins are intrinsically disordered. A.K. Dunker, M. Babu, E. Barbar, M. Blackledge, S.E. Bondos, Z. Dosztányi, H.J. Dyson, J. Forman-Kay, M. Fuxreiter, J. Gsponer, K.-H. Han, D.T. Jones, S. Longhi, S.J. Metallo, K. Nishikawa, R. Nussinov, Z. Obradovic, R. Pappu, B. Rost, P. Selenko, V. Subramaniam, J.L. Sussman, P. Tompa, V.N. Uversky (2013) Intr. Dis. Prot. 1 e24157.
Side-chain conformational heterogeneity of intermediates in the Escherichia coli dihydrofolate reductase catalytic cycle. L.M. Tuttle, H.J. Dyson, P.E. Wright (2013) Biochemistry 52, 3464-3477. (2) PMC3796204
A distal mutation perturbs the dynamic energy landscape of dihydrofolate reductase catalysis. D.D. Boehr, J.R. Schnell, D. McElheny, S.H. Bae, B.M. Duggan, S.J. Benkovic, H.J. Dyson and P.E. Wright (2013) Biochemistry 52, 4605-4619. (1) PMC3838469
The structural and energetic basis of protein-carbohydrate interactions. W. Chen, S. Enck, J.L. Price, D.L. Powers, E.T. Powers, C.H. Wong, H.J. Dyson and J.W. Kelly (2013) J. Am. Chem. Soc. 135, 9877-9884. (1) PMC3715148
The CH2 domain of CBP/p300 is a novel zinc finger. S. Park, M.A. Martinez-Yamout, H.J. Dyson, and P.E. Wright (2013) FEBS Lett. 587, 2506-2511. (1) PMC3765250
Divergent evolution of protein conformational dynamics. G. Bhabha, D.C. Ekiert, M. Jennewein, C.M. Zmasek, L.M. Tuttle, G. Kroon, H. J. Dyson, A. Godzik, I.A. Wilson and P.E. Wright (2013) Nature Struct. Mol. Biol. 20, 1243-1249. (2) PMC3823643
Side chain conformational averaging in human dihydrofolate reductase. L.M. Tuttle, H.J. Dyson and P.E. Wright (2014) Biochemistry 53, 1134-1145. PMC3985697
Structural characterization of interactions between the double-stranded RNA-binding zinc finger protein JAZ and nucleic acids. R.G. Burge, M.A. Martinez-Yamout, H.J. Dyson and P.E. Wright (2014) Biochemistry 53, 1495-1510. PMC3985865
Probing the non-native H-helix translocation in the apomyoglobin folding intermediate. P. Aoto, C. Nishimura, H.J. Dyson and P.E. Wright (2014) Biochemistry 53, 3767-3780. PMC4067146
The high-risk HPV16 E7 oncoprotein mediates interaction between the transcriptional coactivator CBP and the retinoblastoma protein pRb. A.L. Jansma, M.A. Martinez-Yamout, R. Liu, P. Sun, H.J. Dyson and P.E. Wright (2014) J. Mol. Biol. 426, 4030-4048. PMC4258470
Intrinsically disordered proteins in cellular signaling and regulation. P.E. Wright and H.J. Dyson (2015). Nat. Rev. Mol. Cell Biol. 16, 18-29. PMC4405151
Cofactor-mediated conformational dynamics promote product release from Escherichia coli dihydrofolate reductase via an allosteric pathway. D. Oyen, R.B. Fenwick, R.L. Stanfield, H.J. Dyson and P.E. Wright (2015) J. Am. Chem. Soc. 137, 9459-9468. PMC4521799
Functional advantages of protein disorder. R.B. Berlow, H.J. Dyson and P.E. Wright (2015) FEBS Lett. 589, 2433-2440. PMC4586362
The conformational propensities of intrinsically disordered proteins influence the mechanism of binding and folding. M. Arai, K. Sugase, H.J. Dyson and P.E. Wright (2015) Proc. Natl. Acad. Sci. USA 112, 9614-9619. PMC4534220
Classic analysis of biopolymer dynamics is Model-Free. R.B. Fenwick and H.J. Dyson (2016) Biophys. J. 110, 3-6. PMC4805862
Making sense of intrinsically disordered proteins. H.J. Dyson (2016) Biophys. J. 110, 1013-1016. PMC4788759
Role of intrinsic protein disorder in the function and interactions of the transcriptional coactivators CREB-binding protein (CBP) and p300. H.J. Dyson and P.E. Wright (2016) J. Biol. Chem. 291, 6714-6722. PMC4807259
NMR characterization of a 72 kDa transcription factor using differential isotopic labeling. S. Mukherjee, B. Borin, P.O. Quintas and H.J. Dyson (2016) Protein Sci. 25, 597-604. PMC4815403
Recognition of the Disordered p53 Transactivation Domain by the Transcriptional Coactivators CBP and p300. A.S. Krois, J.C. Ferreon, M.A. Martinez-Yamout, H.J. Dyson and P.E. Wright (2016) Proc. Natl. Acad. Sci. USA E1853-E1862. PMC4822595
Structural characterization of the ternary complex that mediates termination of NF-κB signaling by IκBα. S.P. Mukherjee, P.O. Quintas, R. McNulty, E.A. Komives and H.J. Dyson (2016) Proc. Natl. Acad. Sci. USA 113, 6212-6217.
Finding our way in the dark proteome. A. Bhowmick, D.H. Brookes, M. Krzeminski, S.R. Yost, H.J. Dyson, J.D. Forman-Kay, D. Gunter, M. Head-Gordon, G.L. Hura, V.S. Pande, D.E. Wemmer, P.E. Wright, T. Head-Gordon (2016) J. Am Chem. Soc. 138, 9730-9742. PMC5051545
Mapping the interactions of adenoviral E1A with the p160 nuclear receptor coactivator binding domain of CBP. P. Haberz, M.A. Martinez-Yamout, H.J. Dyson and P.E. Wright (2016) Protein Sci., 50, 2256-2267. PMC119557
The dependence of carbohydrate-aromatic interaction strengths on the structure of the carbohydrate. C.H. Hsu, S. Park, D.E. Mortensen, B.L. Foley, R.J. Woods, D.A. Case, E.T. Powers, C.H. Wong, H.J. Dyson and J.W. Kelly (2016) J. Am. Chem. Soc., 138, 7636-7648. PMC4924591
Hypersensitive termination of the hypoxic response by a disordered protein switch. R.B. Berlow, H. Jane Dyson and P.E. Wright (2017) Nature, 543, 447-451. PMC5375031
Functional importance of stripping in NFκB signaling revealed by a stripping-impaired IκBα mutant. H.E. Dembinski, K. Wismer, J.D. Vargas, N. Kern, G. Kroon, H.J. Dyson, A. Hoffmann and E.A. Komives (2017) Proc. Natl. Acad. Sci. USA, 114, 1916-1921. PMC5338369
How does your Protein Fold? Elucidating the apomyoglobin folding pathway. H.J. Dyson and P.E. Wright (2017) Acc. Chem. Res. 50, 105-111. PMC5241236
Role of the CBP catalytic core intramolecular SUMOylation and control of histone H3 acetylation. (2017) Proc. Natl. Acad. Sci., 114, E5335-E5342
Structural basis for interaction of the tandem zinc finger domains of human muscleblind with cognate RNA from human cardiac troponin T. S. Park, P.D. Phukan, M. Zeeb, M.A. Martinez-Yamout, H.J. Dyson, P.E. Wright (2017) Biochemistry, 56, 4154-4168.
Defining the structural basis for allosteric product release from E. coli Dihydrofolate reductase using NMR relaxation dispersion. D. Oyen, R. Fenwick, P. Aoto, R. Stanfield, I. Wilson, H.J. Dyson, P.E. Wright (2017) J. Amer. Chem. Soc., 139, 11233-11240.
Fluorotryptophan incorporation modulates the structure and stability of transthyretin in a site-specific manner. X. Sun, H. J. Dyson and P.E. Wright (2017) Biochemistry 56, 5570-5581.
Slow dynamics of tryptophan-water networks in proteins. R.B. Fenwick, D. Oyen, H.J. Dyson and P.E. Wright (2018) J. Am. Chem. Soc. 140, 675-682.
Characterization of an Hsp90-independent interaction between the co-chaperone p23 and the transcription factor p53. H. Wu, J. Hyun, M.A. Martinez-Yamout, S.J. Park, and H.J. Dyson (2018) Biochemistry 57, 935-944.
CH—O bonds mediate highly specific recognition of methylated CpG steps by the zinc finger protein Kaiso. E.N. Nikolova, R.L. Stanfield, M.A. Martinez-Yamout, H.J. Dyson and P.E. Wright (2018) Biochemistry 57, 2109-2120.
Expanding the paradigm: intrinsically disordered proteins and allosteric regulation. R.B. Berlow, H.J. Dyson and P.E. Wright (2018) J. Mol. Biol. 430, 2309-2320.
Kinetic analysis of the multi-step aggregation pathway of human transthyretin. X. Sun, H.J. Dyson and P.E. Wright (2018) Proc. Natl. Acad. Sci. USA 115, E6201-E6208.
How do intrinsically disordered viral proteins hijack the cell? H.J. Dyson and P.E. Wright (2018) Biochemistry 57, 4045-4046.
NMR measurements reveal the structural basis of transthyretin destabilization by pathogenic mutations. B.I. Leach, X. Zhang, J.W. Kelly, H.J. Dyson and P.E. Wright (2018) Biochemistry 57, 4421-4430.
Structural basis for cooperative regulation of KIX-mediated transcription pathways by the HTLV1 HBZ activation domain. K. Yang, R.L. Stanfield, M.A. Martinez-Yamout, H.J. Dyson and P.E. Wright (2018) Proc. Natl. Acad. Sci. USA 115, 10040-10045.
Long-range regulation of p53 DNA binding by its intrinsically disordered N-terminal transactivation domain. A.S. Krois, H.J. Dyson and P.E. Wright (2018) Proc. Natl. Acad. Sci. USA 115, E11302-E11310.
Mispacking of the F87 side chain reduces the kinetic stability of human transthyretin. X. Sun, M. Jaeger, J.W. Kelly, H.J. Dyson and P.E. Wright (2018) Biochemistry 57, 6919-6922.
Structural basis for graded inhibition of CREB:DNA interactions by multisite phosphorylation. S. Shnitkind, M.A. Martinez-Yamout, H.J. Dyson and P.E. Wright (2018) Biochemistry 57, 6964-6972.
Role of backbone dynamics in modulating the interactions of disordered ligands with the TAZ1 domain of the CREB-binding protein. R.B. Berlow, M.A. Martinez-Yamout, H.J. Dyson and Peter E. Wright (2019) Biochemistry 58, 1354-1362.
Aggregation of zinc-free p53 is inhibited by Hsp90 but not other chaperones. H. Wu and H.J. Dyson (2019) Protein Sci. 28, 2020-2023.
Perspective: the essential role of NMR in the discovery and characterization of intrinsically disordered proteins. H.J. Dyson and P.E. Wright (2019) J. Biomol. NMR, 73, 651-659
Comparison of the backbone dynamics of the p50 dimerization domain of NFkB in the homodimeric transcription factor NFkB1 and in its heterodimeric complex with RelA (p65). B. Kohl, V. Granitzka, A. Singh, P.O. Quintas, E. Xiromeriti, F. Mörtel, P.E. Wright, G.J. Kroon, H.J. Dyson, R. Stoll (2019) Protein Science, 28, 2064-2072.
A dynamic switch in inactive p38y leads to an excited state on pathway to an active kinase. P. Aoto, R. Stanfield, I. Wilson, H.J. Dyson, P.E. Wright (2019), Biochemistry, 58, 5160-5172
Management of Hsp90 dependent protein folding by small molecule targeting the Aha1 co-chaperone. J. Singh, B. Tait, D.H. Hutt, N. Guy, J.C. Sivil, D.S. Culbertson, C. Dickey, J.Y. Kuo, A. Chadli, D. Finley, H.J. Dyson, M.B. Cox, J.E. Gestwicki, W.E. Balch (2020) Cell Chem. Biol. 27, 292-305
A conformational switch in the zinc finger protein Kaiso mediates differential readout of specific and methylated DNA. E. Nikolova, R.L. Stanfield, H.J. Dyson and P.E. Wright (2020) Biochemistry 59, 1909-1926
RNA binding by the KTS splice variants of the Wilms’ tumor suppressor protein WT1. T. Nishikawa, J.M. Wojciak, H.J. Dyson and P.E. Wright (2020) Biochemistry 59, 3889-3901
Backbone and side chain chemical shift assignments of the p50 subunit of NF-κB transcription factor. A. Singh and H. J. Dyson (2021) Biomol. NMR Assign. 15, 29-33
Modeling of hidden structures using sparse chemical shift data from NMR relaxation dispersion. R. B. Fenwick, D. Oyen, H. van den Bedem, H. J. Dyson and P.E. Wright (2021) Biophys. J. 120, 296-305
A phosphorylation-dependent switch in the disordered p53 transactivation domain modulates DNA binding. X. Sun, H.J. Dyson and P.E. Wright (2021) Proc. Natl. Acad. Sci. 118, e2021456118
Thermodynamic stability and aggregation kinetics of EF helix and EF loop variants of transthyretin. J.A. Ferguson, X. Sun, H.J. Dyson, P.E. Wright (2021) Biochemistry 60, 756-764
Using NMR to identify binding regions for N and C-terminal Hsp90 inhibitors using Hsp90 domains. J.R. McConnell, H.J. Dyson and S.R. McAlpine (2021) RSC Med. Chem. 12, 410-415
Early strides in NMR dynamics measurements. H.J. Dyson (2021) Biochemistry 60, 3452-3454
NMR illuminates intrinsic disorder. H.J. Dyson and P.E. Wright (2021) Curr. Opin. Struct. Biol. 70, 44-52
The molecular basis of allostery in a facilitated dissociation process. F.D. Appling, R.B. Berlow, R.L. Stanfield, H.J. Dyson and P.E. Wright (2021) Structure 29, 1327-1338
. Role of active site loop dynamics in mediating ligand release from E. coli dihydrofolate reductase. A. Singh, R.B. Fenwick, H.J. Dyson and P.E. Wright (2021) Biochemistry 60, 2663-2671
Characterization of the high-affinity fuzzy complex between E7 from high-risk HPV and the TAZ2 domain of CBP. M. Risør, A.L. Jansma, N. Medici, B. Thomas, P.E. Wright and H.J. Dyson (2021) Biochemistry 60, 3887-3898
Multivalency enables unidirectional switch-like competition between intrinsically disordered proteins. R.B. Berlow, H.J. Dyson and P.E. Wright (2022) Proc. Natl Acad. Sci. USA 119, e2117338119
Interaction of a long non-coding RNA with the p65 subunit of NFκB: Implications for the inhibition of non-signal-related phosphorylation. A. Singh, M.A. Martinez-Yamout, P.E. Wright and H.J. Dyson (2022). Biochemistry 61, 367-376
Structural and dynamic studies of DNA recognition by NF-κB p50 RHR homodimer using methyl NMR spectroscopy. A. Singh, M.A. Martinez-Yamout, P.E. Wright and H.J. Dyson (2022). Nucleic Acids Res. 50, 7147-7160
A transthyretin monomer intermediate undergoes local unfolding and transient interaction with oligomers in a kinetically concerted aggregation pathway. X. Sun, J.A. Ferguson, H.J. Dyson, P.E. Wright (2022) J. Biol. Chem. 298, 102162
Transient on- and off-pathway protein folding intermediate states characterized with NMR relaxation dispersion. D.W. Meinhold, D.J. Felitsky, H.J. Dyson and P.E. Wright (2022) J. Phys. Chem. B 126, 9539-9548
Mapping interactions of the intrinsically disordered C-terminal regions of tetrameric p53 by segmental isotope labeling and NMR. A.S. Krois, S. Park, M.A. Martinez-Yamout, H.J. Dyson and P.E. Wright (2022) Biochemistry 61, 2709-2719
Role of conformational dynamics in pathogenic protein aggregation. X. Sun, H.J. Dyson and P.E. Wright (2023). Curr. Opin. Chem. Biol. 73, 102280
From immunogenic peptides to disordered proteins. H.J. Dyson and P.E. Wright (2023) Isr. J. Chem. 2023, e202300051
Vital for viruses: intrinsically disordered proteins. H.J. Dyson (2023) J. Mol. Biol. 435, 167860