1. 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
2. Spin state and unfolding equilibria of ferricytochrome c in acidic solutions. H.J. Dyson & J.K. Beattie (1982) J. Biol. Chem. 257, 2267-2273.
3. 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.
4. 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.)
5. 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.)
6. 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.,
7. 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.
8. 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.
9. 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.
10. 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.
11. 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.
12. 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.
13. 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.
14.1H 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.
15. 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. Blocker, J. Collins, R.D. Schmid, & D. Schomburg Eds.) VCH Publishing, pp 13-19.
16. 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.,
17. 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.
18. 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.
19. 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.
20. 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.
21. 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
22. Defining solution conformations of small linear peptides. H.J. Dyson & P.E. Wright (1991) Ann. Rev. Biophys. Biophys. Chem. 20, 519-538. (485)
23. 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
24. 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.
25. 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
26. 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.
27. 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.
28. 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.
29. 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.
30. 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.
31. 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.
32. 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.
33. Peptide conformation and protein folding. H.J. Dyson & P.E. Wright (1993) Curr. Opin. Struct. Biol. 3, 60-65.
34. 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.
35. 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.
36. 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.
37. 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.
38. Characterization of a folding intermediate of apoplastocyanin trapped by proline isomerization. S. Koide, H.J. Dyson, & P.E. Wright (1993) Biochemistry 32, 12299-12310.
39. 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.,
40. Peptide structure in solution. H.J. Dyson (1994) In: Synthetic
Vaccines (B.H. Nicholson Ed.) Blackwell Scientific Publications Ltd,
41. 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.
42. 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.
43. 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.
44. 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,
45. 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.
46. 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.
47. 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.
48. 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.
49. 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.
50. 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,
51. Analysis of peptide and protein structure. H.J. Dyson
(1994) In: Immunological recognition of peptides in medicine and biology
(
52. 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.
53. Antigenic
peptides. H.J. Dyson & P.E. Wright (1995) FASEB J. 9, 37-42.
54. Comparison of the hydrogen exchange behavior of reduced and oxidized Escherichia coli thioredoxin. M.-F. Jeng & H.J. Dyson (1995) Biochemistry 34, 611-619.
55. Detection of a covalent intermediate in the reaction pathway of a catalytic antibody using electrospray mass spectrometry. J.F. Krebs, G. Siuzdak, H.J. Dyson, J.D. Stewart, & S.J. Benkovic (1995) Biochemistry 34, 720-723.
56. 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.
57. NMR of thioredoxin and glutaredoxin. H.J. Dyson (1995) Methods Enzymol. 252, 293-306.
58. 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.
59. 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.
60. 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.
61. 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.
62. 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.
63. 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)
64. Thioredoxin and glutaredoxin. H.J. Dyson (1996) In: Encyclopedia
of Nuclear Magnetic Resonance (ed. D.M. Grant and R.K. Harris)
65. 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.
66. 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.
67. 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.
68. Insights into protein folding from NMR. H.J. Dyson and P.E. Wright (1996) Ann Rev. Phys. Chem. 47, 369-395.
69. 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.
70. 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.
71. 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.
72. 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
73. 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
74. 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
75. 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.
76. 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.
77. PCR-based gene synthesis for protein over-production. D. Casimiro, P.E. Wright and H.J. Dyson (1997) Structure 5, 1407-1412.
78. 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.
79. 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
80. 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.
81. 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.
82. 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.
83. A NOESY-HSQC simulation program SPIRIT. L. Zhu, H.J. Dyson and P.E. Wright (1998) J. Biomol. NMR 11, 17-29.
84. 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.
85. Equilibrium NMR studies of unfolded and partly folded proteins. H.J. Dyson and P.E. Wright (1998) Nature Struct. Biol. 5, 499-503.
86. 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.
87. 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.
88. 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.
89. 1H, 13C and 15N NMR backbone assignments of 25.5 kDa metallo-b-lactamase from Bacteroides fragilis. S.D.B. Scrofani, P.E. Wright and H.J. Dyson (1998) J. Biomol. NMR 12, 201-202.
90. 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
91. 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.
92. 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.
93. 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.
94. 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
95. 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.
96. 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
97. 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.
98. 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.
99. 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.
100. Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm. P.E. Wright and H.J. Dyson (1999) J. Mol. Biol. 293, 321-331.
101. 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.
102. 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.
103. 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.
104. NMR characterization of the metallo-b-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.
105. Backbone resonance assignments for the Fv fragment of
the catalytic antibody NPN43C9 with bound p-nitrophenol.
G. Kroon, M. Martinez-Yamout, J.F. Krebs,
106. 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
107. 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.
108. 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.
109. Spectroscopic methods. H.J. Dyson (2000) Encyclopedia of Life Sciences Macmillan Online publication www.els.net.
110. Backbone HN, N, Ca, C’ and Cb 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.
111. 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.
112. 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.
113. Identification of the regions involved in DNA binding by the mouse PEBP2a protein. G.C. Perez-Alvarado, A. Munnerlyn, H.J. Dyson, R. Grosschedl and P.E. Wright (2000) FEBS Lett. 470, 125-130.
114. 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.
115. 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.
116. 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.
117. 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.
118. 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.
119. 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.
120. Dynamics of the metallo-b-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.
121. 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
122. 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.
123. 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.
124. 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.
125. 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.
126. 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
127. 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.
128. 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.
129. 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
130. 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.
131. 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.
132. 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
133. 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.
134. 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.
135. 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.
136. 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.
137. 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.
138. Structure and dynamics of disordered proteins. H.J. Dyson and P.E. Wright (2002) Encyclopedia of NMR 9, 449-457.
139. 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.
140. 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.
141. Coupling of folding and binding for unstructured proteins. H.J. Dyson and P.E. Wright (2002) Curr. Opin. Struct. Biol. 12, 54-60.
142. 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.
143. Structural basis for Hif-1a/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
144. 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.
145. 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.
146. 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.
147. 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.
148. 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.
149. 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.
150. Folding of a b-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.
151. Plasmodium vivax peptides display conformational preferences for folded forms in solution. T.E. Lehmann, G. Kroon, M.A. Lorenzo, H. Bermudez, H. Perez and H.J. Dyson (2003) J. Peptide Research 61, 252-262.
152. Role of a solvent-exposed tryptophan in the
recognition and binding of antibiotic substrates for a metallo-b-lactamase. J.J.A. Huntley, W. Fast, S.J.
Benkovic, P.E. Wright and H.J. Dyson (2003). Protein Sci. 12,
1368-1375. PMC2323931
153. 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.
154. 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
155. 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.
156. 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
157. 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.
158. 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
159. 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.
160. Unfolded proteins and protein folding studied by NMR. H.J. Dyson and P.E. Wright (2004). Chemical Reviews 104, 3607-3622.
161. 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.
162. 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.
163. 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.
164. 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.
165. 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.
166. 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.
167. 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.
168. 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
169. 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.
170. Structural characterization of unfolded and partly folded states of apomyoglobin using residual dipolar couplings. R.M. Borges, H.J. Dyson and P.E. Wright (2004) J. Mol. Biol. 330, 1131-1142.
171. 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.
172. 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.
173. Conformational changes in the active site
loops of dihydrofolate reductase during the catalytic cycle. R.P.
Venkitakrishnan,
174. CBP/p300 TAZ1 domain forms a
structural scaffold for ligand binding. R.N. De Guzman, J.M. Wojciak, M.A.
175. 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
176. Intrinsically unstructured proteins and their functions. H.J. Dyson and P.E. Wright (2005). Nature Rev. Mol. Cell Biol. 6, 197-208.
177. Elucidation of the protein folding landscape by NMR. H.J. Dyson and P.E. Wright (2005). Methods Enzymol. 394, 299-321.
178. Backbone HN, N, Ca, C′ and Cb 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.
179. 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
180. 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
181. 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.
182. 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. .
183. 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.
184. 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.
185. 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.
186. 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.
187. 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. Martinez-Yamout, H.J. Dyson, D.A.Case, J.M.Gottesfeld, and P.E.Wright (2006). J. Mol. Biol. 357, 275-291.
188. 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.
189. 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.
190. 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.
191. An NMR perspective on enzyme dynamics. D.D. Boehr, H.J. Dyson and P.E. Wright (2006). Chem. Rev. 106, 3055-3079.
192. The dynamic energy landscape of dihydrofolate reductase catalysis. D.D. Boehr, D. McElheny, H. J. Dyson, P.E. Wright (2006). Science 313, 1638-1642.
193. 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
194. 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.
195. 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.
196. Embryonic neural inducing factor Churchill is not a
DNA-binding zinc finger: solution structure reveals a solvent-exposed b-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
197. 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.
198. Structure
discrimination for the C-terminal domain of E.
coli trigger factor in solution. Y.
199. 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
200. 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
201. 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.
202. 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
203. 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
204. 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
205. 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
206. Transfer of flexibility between ankyrin repeats in IkBa upon formation of the NF-kB complex. S.-C. Sue, C. Cervantes, E.A. Komives and H.J. Dyson (2008) J. Mol. Biol. 380, 917-931. PMC2603615
207. 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
208. 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
209. 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
210. The
intrinsically disordered RNR inhibitor Sml1 is a dynamic and globular dimer. J.
Danielsson, L. Liljedahl, E. Barany-Wallje, P. Sonderby, L.H. Kristensen, M.
Martinez-Yamout, H.J. Dyson, P.E. Wright, F.M. Poulsen, L. Maler, A. Graslund
and B.B. Kragelund (2008) Biochemistry
47, 13428-13437. PMC2747730
211. Linking folding and binding. P.E. Wright and H.J. Dyson (2009) Curr. Opin. Struct. Biol. 19, 31-38. PMC2675572
212. 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)
213. 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)
214. 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
215. 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
216. 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
217. Interaction
of the IκBα C-terminal
218. 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
219. Evaluating
b-turn mimics as b-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
220. Functional dynamics of the folded ankyrin repeats of IkBa 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
221. 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
222. 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
223. 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
224. 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
225. Spectroscopic Techniques H.J.
Dyson (2010) In: Encyclopedia of Life
Sciences
226. 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
227. 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
228. The RelA nuclear localization signal folds upon binding to IkBa. 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
229. Detection of a ternary complex of NFkB and IkBa with DNA provides insights into how IkBa removes NFkB 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
230. 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
231. 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
232. Dynamic
interaction of Hsp90 with its client protein p53.
233. 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
234. Expanding the proteome: disordered and alternatively
folded proteins. H.J. Dyson (2011) Quart.
Rev. Biophysics 44, 467-518. PMC3189428
235. NMR studies of intrinsic disorder in protein-nucleic acid
interactions. H.J. Dyson (2012) Mol.
BioSyst. 8, 97-104.
236. 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.
237. 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. Jane Dyson. Oxford: Academic Press. pp 136-159.
238. 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
239. NMR studies of unfolded but functional proteins. H.J. Dyson (2012) In “Recent Developments in Biomolecular NMR” RSC Biomolecular Science Series Chapter 5, pp 111-129.
240. 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.
241. Role of disorder in IkB-NFkB interaction. H.J. Dyson and E.A. Komives (2012) IUBMB Life 64, 499-505.
242. Coupled folding and binding. H.J. Dyson (2012) Encyclopedia of Biophysics Springer. (in press)