Centre for Misfolding Diseases

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  • Currently displaying 2221 - 2240 of 2399 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 α-Lactalbumin
BA Schulman, C Redfield, ZY Peng, CM Dobson, PS Kim
Journal of molecular biology
(1995)
253
(doi: 10.1006/jmbi.1995.0579)
Following protein folding in real time using NMR spectroscopy.
J Balbach, V Forge, NA van Nuland, SL Winder, PJ Hore, CM Dobson
Nature Structural & Molecular Biology
(1995)
2
(doi: 10.1038/nsb1095-865)
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)
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
J Mol Biol
(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 ALPHA-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
Journal of Biological Chemistry
(1995)
270
(doi: 10.1074/jbc.270.18.10514)
Preface
CM Dobson, AR Fersht
Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences
(1995)
348
(doi: 10.1098/rstb.1995.0038)
Insights into protein folding using physical techniques: studies of lysozyme and α-lactalbumin
SE Radford, CM Dobson
Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences
(1995)
348
(doi: 10.1098/rstb.1995.0041)
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 J
(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)
“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)
Finding the right fold
CM Dobson
Nat Struct Biol
(1995)
2
(doi: 10.1038/nsb0795-513)
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 alpha-lactalbumin in trifluoroethanol: a model for local structure in the molten globule.
LJ Smith, AT Alexandrescu, M Pitkeathly, CM Dobson
Structure (London, England : 1993)
(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)
Yusuf Hamied Department of Chemistry
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