Centre for Misfolding Diseases

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  • Currently displaying 2241 - 2260 of 2413 publications
Author(s)
Publication title
Journal Name
Publication year
Different subdomains are most protected from hydrogen exchange in the molten globule and native states of human alpha-lactalbumin.
BA Schulman, C Redfield, ZY Peng, CM Dobson, PS Kim
J Mol Biol
(1995)
253
(doi: 10.1006/jmbi.1995.0579)
Structural basis of the stability of a lysozyme molten globule
LA Morozova, DT Haynie, C Arico-Muendel, H Van Dael, CM Dobson
Nature structural biology
(1995)
2
(doi: 10.1038/nsb1095-871)
Following protein folding in real time using NMR spectroscopy
J Balbach, V Forge, NA van Nuland, SL Winder, PJ Hore, CM Dobson
Nature structural biology
(1995)
2
(doi: 10.1038/nsb1095-865)
Conformational properties of four peptides spanning the sequence of hen lysozyme
JJ Yang, M Buck, M Pitkeathly, M Kotik, DT Haynie, CM Dobson, SE Radford
Journal of Molecular Biology
(1995)
252
(doi: 10.1006/jmbi.1995.0513)
The crystal structure of the catalytic domain of human urokinase-type plasminogen activator
G Spraggon, C Phillips, UK Nowak, CP Ponting, D Saunders, CM Dobson, DI Stuart, EY Jones
Structure (London, England : 1993)
(1995)
3
(doi: 10.1016/S0969-2126(01)00203-9)
A Ca2+-binding Chimera of Human Lysozyme and Bovine α-Lactalbumin That Can Form a Molten Globule
E Pardon, P Haezebrouck, A De Baetselier, SD Hooke, KT Fancourt, J Desmet, CM Dobson, H Van Dael, M Joniau
J Biol Chem
(1995)
270
(doi: 10.1074/jbc.270.18.10514)
FOLDING OF HEN LYSOZYME
H LU, SE RADFORD, CM DOBSON
FASEB JOURNAL
(1995)
9
FOLDING OF A PARTIALLY FOLDED STATE OF HEN LYSOZYME IN TRIFLUOROETHANOL
LU HUI, M BUCK, SE RADFORD, CM DOBSON
FASEB JOURNAL
(1995)
9
An equilibrium partially folded state of human lysozyme at low pH
P Haezebrouck, M Joniau, H Van Dael, SD Hooke, ND Woodruff, CM Dobson
J Mol Biol
(1995)
246
(doi: 10.1006/jmbi.1994.0093)
"Kinetics of Hydration and Other Reactions of Calcium Silicates and Cements", in Applications of NMR Spectroscopy to Cement Science
AR Brough, GW Groves, IG Richardson, SA Rodger, CM Dobson
(1995)
Finding the right fold.
CM Dobson
Nature Structural Biology
(1995)
2
(doi: 10.1038/nsb0795-513)
“Protein Structures in Solution Viewed by NMR”, in Making the Most of Your Model
LJ Smith, CM Dobson
(1995)
Folding and binding
CM Dobson
Current Opinion in Structural Biology
(1995)
5
(doi: 10.1016/0959-440x(95)80009-p)
Conformation of GroEL-bound α-lactalbumin probed by mass spectrometry
CV Robinson, M Gross, SJ Eyles, JJ Ewbank, M Mayhew, FU Hartl, CM Dobson, SE Radford
Nature
(1994)
372
(doi: 10.1038/372646a0)
Crystal structure of the mutant D52S hen egg white lysozyme with an oligosaccharide product
AT Hadfield, DJ Harvey, DB Archer, DA MacKenzie, DJ Jeenes, SE Radford, G Lowe, CM Dobson, LN Johnson
Journal of molecular biology
(1994)
243
(doi: 10.1006/jmbi.1994.1688)
EVOLUTION OF THE MISSING-ROW DECONSTRUCTION ON RH(110)
D Cvetko, L Floreano, A Morgante, M Peloi, F Tommasini, KC Prince, M Vendruscolo, E Tosatti
Surface Science
(1994)
318
(doi: 10.1016/0039-6028(94)90091-4)
Solution structure of a peptide fragment of human α–lactalbumin in trifluorethanol: a model for local structure in the molten globule
LJ Smith, AT Alexandrescu, M Pitkeathly, CM Dobson
Structure
(1994)
2
(doi: 10.1016/s0969-2126(00)00071-x)
Protein folding. Solid evidence for molten globules.
CM Dobson
Curr Biol
(1994)
4
(doi: 10.1016/s0960-9822(00)00141-x)
Comparison of four independently determined structures of human recombinant interleukin–4
LJ Smith, C Redfield, RA Smith, CM Dobson, GM Clore, AM Gronenborn, MR Walter, TL Naganbushan, A Wlodawer
Nature Structural & Molecular Biology
(1994)
1
(doi: 10.1038/nsb0594-301)
Analysis of the solution structure of human interleukin-4 determined by heteronuclear three-dimensional nuclear magnetic resonance techniques
C Redfield, LJ Smith, J Boyd, GM Lawrence, RG Edwards, CJ Gershater, RA Smith, CM Dobson
Journal of molecular biology
(1994)
238
(doi: 10.1006/jmbi.1994.1265)
Yusuf Hamied Department of Chemistry
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