Centre for Misfolding Diseases

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  • Currently displaying 2221 - 2240 of 2393 publications
Author(s)
Publication title
Journal Name
Publication year
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 alpha-lactalbumin.
SE Radford, CM Dobson
Philos Trans R Soc Lond B Biol Sci
(1995)
348
(doi: 10.1098/rstb.1995.0041)
FOLDING OF HEN LYSOZYME
H LU, SE RADFORD, CM DOBSON
FASEB J
(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
Journal of Molecular Biology
(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)
Folding and binding
CM Dobson
Current Opinion in Structural Biology
(1995)
5
(doi: 10.1016/0959-440x(95)80009-p)
“Protein Structures in Solution Viewed by NMR”, in Making the Most of Your Model
LJ Smith, CM Dobson
(1995)
Finding the right fold.
CM Dobson
Nature structural biology
(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
J Mol Biol
(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 (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)
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 Biology
(1994)
1
(doi: 10.1038/nsb0594-301)
ANALYSIS OF THE SOLUTION STRUCTURE OF HUMAN INTERLEUKIN-4 DETERMINED BY HETERONUCLEAR 3-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)
Amide Hydrogen Exchange in a Highly Denatured State Hen Egg-white Lysozyme in Urea
M Buck, SE Radford, CM Dobson
Journal of molecular biology
(1994)
237
(doi: 10.1006/jmbi.1994.1228)
Solution structure of the kringle domain from urokinase-type plasminogen activator.
X Li, AM Bokman, M Llinás, RA Smith, CM Dobson
Journal of Molecular Biology
(1994)
235
(doi: 10.1006/jmbi.1994.1106)
1H nuclear magnetic resonance studies of hen lysozyme-N-acetylglucosamine oligosaccharide complexes in solution. Application of chemical shifts for the comparison of conformational changes in solution and in the crystal.
KJ Lumb, JC Cheetham, CM Dobson
J Mol Biol
(1994)
235
(doi: 10.1006/jmbi.1994.1058)
Characterization of a trifluoroethanol-induced partially folded state of α-lactalbumin
AT Alexandrescu, YL Ng, CM Dobson
J Mol Biol
(1994)
235
(doi: 10.1006/jmbi.1994.1015)
Yusuf Hamied Department of Chemistry
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