Centre for Misfolding Diseases

Publications

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  • Currently displaying 1861 - 1880 of 2403 publications
Author(s)
Publication title
Journal Name
Publication year
Chemical space and biology
CM Dobson
Nature
(2004)
432
(doi: 10.1038/nature03192)
Reduced Global Cooperativity is a Common Feature Underlying the Amyloidogenicity of Pathogenic Lysozyme Mutations
M Dumoulin, D Canet, AM Last, E Pardon, DB Archer, S Muyldermans, L Wyns, A Matagne, CV Robinson, C Redfield, CM Dobson
Journal of molecular biology
(2004)
346
(doi: 10.1016/j.jmb.2004.11.020)
Biological physics: Energy, information, life
CM Dobson
Nature
(2004)
432
(doi: 10.1038/432444a)
Principal eigenvector of contact matrices and hydrophobicity profiles in proteins.
U Bastolla, M Porto, HE Roman, M Vendruscolo
Proteins Structure Function and Genetics
(2004)
58
(doi: 10.1002/prot.20240)
Comparison of the Transition States for Folding of Two Ig-like Proteins from Different Superfamilies
CD Geierhaas, E Paci, M Vendruscolo, J Clarke
Journal of molecular biology
(2004)
343
(doi: 10.1016/j.jmb.2004.08.100)
The formation of spherulites by amyloid fibrils of bovine insulin.
MRH Krebs, CE Macphee, AF Miller, IE Dunlop, CM Dobson, AM Donald
Proceedings of the National Academy of Sciences of the United States of America
(2004)
101
(doi: 10.1073/pnas.0405933101)
A study of the pozzolanic reaction by solid-state 29Si nuclear magnetic resonance using selective isotopic enrichment
AR Brough, CM Dobson, IG Richardson, GW Groves
Journal of Materials Science
(2004)
30
(doi: 10.1007/BF00351595)
In situ solid-state NMR studies of Ca3SiO5: hydration at room temperature and at elevated temperatures using 29Si enrichment
AR Brough, CM Dobson, IG Richardson, GW Groves
Journal of Materials Science
(2004)
29
(doi: 10.1007/BF00355951)
Experimental investigation of protein folding and misfolding
CM Dobson
Methods
(2004)
34
(doi: 10.1016/j.ymeth.2004.03.002)
Probing the origins, diagnosis and treatment of amyloid diseases using antibodies
M Dumoulin, CM Dobson
Biochimie
(2004)
86
(doi: 10.1016/j.biochi.2004.09.012)
Prediction of the absolute aggregation rates of amyloidogenic polypeptide chains.
KF DuBay, AP Pawar, F Chiti, J Zurdo, CM Dobson, M Vendruscolo
J Mol Biol
(2004)
341
(doi: 10.1016/j.jmb.2004.06.043)
Neuronal cell death is triggered by prefibrillar protein aggregates
M Stefani, S Baglioni, M Bucciantini, F Chiti, CM Dobson, N Taddei, F Casamenti
PROTEIN SCIENCE
(2004)
13
Amyloid disaggregation: Experiencing hierarchical grades of reversibility
M Calamai, C Canale, A Relini, M Stefani, F Chiti, CM Dobson
PROTEIN SCIENCE
(2004)
13
Low-populated folding intermediates of Fyn SH3 characterized by relaxation dispersion NMR.
DM Korzhnev, X Salvatella, M Vendruscolo, AA Di Nardo, AR Davidson, CM Dobson, LE Kay
Nature
(2004)
430
(doi: 10.1038/nature02655)
A highly amyloidogenic region of hen lysozyme.
E Frare, P Polverino De Laureto, J Zurdo, CM Dobson, A Fontana
J Mol Biol
(2004)
340
(doi: 10.1016/j.jmb.2004.05.056)
Heteronuclear NMR investigations of dynamic regions of intact Escherichia coli ribosomes
J Christodoulou, G Larsson, P Fucini, SR Connell, TA Pertinhez, CL Hanson, C Redfield, KH Nierhaus, CV Robinson, J Schleucher, CM Dobson
Proceedings of the National Academy of Sciences
(2004)
101
(doi: 10.1073/pnas.0400928101)
Molecular dynamics studies of the process of amyloid aggregation of peptide fragments of transthyretin
E Paci, J Gsponer, X Salvatella, M Vendruscolo
Journal of molecular biology
(2004)
340
(doi: 10.1016/j.jmb.2004.05.009)
Determination of protein structures consistent with NMR order parameters.
RB Best, M Vendruscolo
Journal of the American Chemical Society
(2004)
126
(doi: 10.1021/ja0396955)
The importance of loop length in the folding of an immunoglobulin domain.
CF Wright, J Christodoulou, CM Dobson, J Clarke
Protein Eng Des Sel
(2004)
17
(doi: 10.1093/proeng/gzh052)
Reconstruction of protein structures from a vectorial representation.
M Porto, U Bastolla, HE Roman, M Vendruscolo
Physical review letters
(2004)
92
(doi: 10.1103/PhysRevLett.92.218101)
Yusuf Hamied Department of Chemistry
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