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.
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.) John Wiley & Sons,
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.
22. Defining solution
conformations of small linear peptides. H.J. Dyson & P.E. Wright (1991) Ann. Rev. Biophys. Biophys. Chem. 20, 519-538.
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.
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.
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. Bruschweiler, 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. Peptide proton random coil
chemical shifts obtained as a function of temperature and trifluoroethanol
concentration. 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) John Wiley,
64. Thioredoxin and
glutaredoxin. H.J. Dyson (1996) In: Encyclopedia of Nuclear Magnetic Resonance
(ed. D.M. Grant and R.K. Harris) John Wiley,
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. 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 (1996) J. Mol. Biol. 266, 31-39.
71. 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, 303-306.
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.
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.
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) Biochemistry36, 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.
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 metallo-b-lactamase
from Bacteroides fragilis using NMR
spectroscopy. S.D.B. Scrofani, P.E. Wright and H.J. Dyson (1998) Protein Sci. 7, 2476-2479.
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.
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.
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.
97. Structural analysis 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 a flexible 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, John Chung, H.J. Dyson & P.E. Wright (1999) J. Biomol. NMR 15, 83-84.
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.
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 http://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 PE. Wright (2000) Proc. Natl. Acad. Sci. USA 97, 11932-11935.
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.
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.
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 characterization
of unfolded apo-plastocyanin by multi-dimensional NMR. Y. Bai, J. Chung, H.J.
Dyson and P.E. Wright (2001) Protein Sci.
10, 1056-1066.
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.
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. Structure and dynamics of
disordered proteins. H.J. Dyson and P.E. Wright (2001) Encyclopedia of NMR
(in press).
137. 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.
138. Mutual synergistic folding in recruitment of CBP/p300 by p160 nuclear receptor coactivators. S.J. Demarest, M. Martinez-Yamout, J. Chung, H. Chen, W. Xu, H.J. Dyson, R.M. Evans and P.E. Wright (2002) Nature, 415, 549-553.
139. 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.
140. Coupling of folding and binding for unstructured proteins. H.J. Dyson and P.E. Wright (2002) Curr. Opin. Struct. Biol. 12, 54-60.
141. 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.
142. Synergistic folding of the interaction domain of the hypoxia-inducible factor-1a upon binding to the CH1 domain of CREB binding protein. 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.
143. 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.
144. 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.
145. 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.
146. Molecular hinges during protein folding: residual structure and backbone dynamics of denatured states of apomyoglobin in acidic urea. S. Schwarzinger, P.E. Wright and H.J. Dyson. (2002) Biochemistry 41, 12681-12686.
147. 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.
148. Cooperativity in transcription factor binding to the coactivator 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.
149. Folding of a b-sheet protein monitored by real-time NMR spectroscopy. M. Mizuguchi, G. Kroon, H.J. Dyson and P.E. Wright (2003) J. Mol. Biol. 328, 1161-1171.
150. 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.
151. The 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.
152. Solution structure of human estrogen related receptor-2 bound to an extended DNA half-site: monomeric binding depends on intramolecular protein-protein packing. M.D. Gearhart, S.M.A. Holmbeck, R.M. Evans, H.J. Dyson and P.E. Wright (2003) J. Mol. Biol. 327, 819-832.
153. 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.
154. 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.
155. 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.
156.
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.
157. 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.
158. 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.
159. Unfolded proteins and protein folding studied by NMR. H.J. Dyson and P.E. Wright (2004). Chemical Reviews 104, 3607-3622.
160. 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.
161. 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.
162. 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.
163. Structural basis for 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.
164. 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.
165. 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.
166. 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.
167. 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
168. 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.
169. 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.
170. 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.
171. 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.
172. Conformational changes in the active site loops
of dihydrofolate reductase during the catalytic cycle. R.P. Venkitakrishnan,
173. The isolated CBP/p300 TAZ1 domain folds into a
three dimensional structure in the absence of its binding partners. R.N. De
Guzman, J.M. Wojciak, M.A.
174. 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
175. Intrinsically unstructured proteins and their functions. H.J. Dyson and P.E. Wright (2005). Nature Rev. Mol. Cell Biol. 6, 197-208.
176. Elucidation of the protein folding landscape by NMR. H.J. Dyson and P.E. Wright (2005). Methods Enzymol. 394, 299-321.
177. 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.
178. 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.
179. 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.
180. 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.
181. Solution structure of the first two zinc finger domains of the double-stranded RNA-binding protein dsRBP-zfa. H. M. Möller, Maria A. Martinez-Yamout, H. J. Dyson and P. E. Wright (2005). J. Mol. Biol. 351, 718-730.
182. 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.
183. 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.
184. 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.
185. 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.
186. 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.
187. 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. Biochemistry 45, 3297-3306.
188. 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.
189. Localization of sites of interaction between p23 with 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.
190. An NMR perspective on enzyme dynamics. D.D. Boehr, H.J. Dyson and P.E. Wright (2006). Chem. Rev. 106, 3055-3079.
191. The dynamic energy landscape of dihydrofolate reductase catalysis. D.D. Boehr, D. McElheny, H. J. Dyson, P.E. Wright (2006). Science 313, 1638-1642.
192. Role of specific hydrophobic regions in initiating protein folding. H.J. Dyson, P.E. Wright, H.A. Scheraga (2006) Proc. Natl. Acad. Sci. USA 103, 13057-13061.
193. Solution structure of the Hdm2 C2H2C4 RING finger, a domain critical for ubiquitination of p53. M. Kostic, T. Matt, H.J. Dyson and P.E. Wright (2006) J. Mol. Biol. 363, 433-450.
194. 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.
195. 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
196. Structure of the zinc finger domain of the Wilms’ Tumor suppressor protein 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.
197. Structure
discrimination for the C-terminal domain of E.
coli trigger factor in solution. Y.
198. 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.
199. 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.
200. 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.
201. Structural characterization of folding intermediates of the H64F mutant of apomyoglobin: stepwise stabilization of a native-like hydrophobic cluster. S. Schwarzinger, R. Mohana-Borges, G.J.A. Kroon, H.J. Dyson and P.E. Wright (2008) Protein Sci. 17, 313-321.
202. 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.
203. The kinetic and equilibrium molten globule
intermediates of apoleghemoglobin differ in structure. C. Nishimura, P.E. Wright and H.J. Dyson
(2008) J. Mol. Biol. 378, 715-725.
204. 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.
205. 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.
206. 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.
207. 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.
208. 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.
209. 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.
210. Linking
folding and binding. P.E. Wright and H.J. Dyson (2009) Curr. Opin. Struct. Biol. 19, 31-38.
211. 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)
212. 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)
213. 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.
214. 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.
215. 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.
216. Interaction
of the IκBα C-terminal
217. Prediction of the rotational tumbling for proteins with long disordered segments. S.H. Bae, P.E. Wright and H.J. Dyson (2009) J. Am. Chem. Soc. 131, 6814-6821.
218. Evaluation
of b-sheet folding nucleation kinetics
by b-turn mimics. 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 (in press)