Centre for Misfolding Diseases

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  • Currently displaying 2281 - 2300 of 2450 publications
Author(s)
Publication title
Journal Name
Publication year
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)
“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)
Folding and binding
CM Dobson
Current Opinion in Structural Biology
(1995)
5
(doi: 10.1016/0959-440x(95)80009-p)
Conformation of GroEL-bound alpha-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 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)
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 three-dimensional nuclear magnetic resonance techniques
C Redfield, LJ Smith, J Boyd, GM Lawrence, RG Edwards, CJ Gershater, RA Smith, CM Dobson
J Mol Biol
(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)
Measurement of the individual pKa values of acidic residues of hen and turkey lysozymes by two-dimensional 1H NMR.
K Bartik, C Redfield, CM Dobson
Biophysical journal
(1994)
66
(doi: 10.1016/S0006-3495(94)80900-2)
The characterization of hardened alkali-activated blast-furnace slag pastes and the nature of the calcium silicate hydrate (C-S-H) phase
IG Richardson, AR Brough, GW Groves, CM Dobson
Cement and Concrete Research
(1994)
24
(doi: 10.1016/0008-8846(94)90002-7)
NMR-STUDIES ON UROKINASE-TYPE PLASMINOGEN-ACTIVATOR
UK NOWAK, RAG SMITH, CM DOBSON
JOURNAL OF CELLULAR BIOCHEMISTRY
(1994)
Structural characterization of a highly-ordered 'molten globule' at low pH.
C Redfield, RA Smith, CM Dobson
Nature Structural Biology
(1994)
1
(doi: 10.1038/nsb0194-23)
Yusuf Hamied Department of Chemistry
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