Centre for Misfolding Diseases

Publications

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  • Currently displaying 1981 - 2000 of 2520 publications
Author(s)
Publication title
Journal Name
Publication year
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)
Prinicipal eigenvector of contact matrices and hydrophobicity profiles in proteins
U Bastolla, M Porto, HE Roman, M Vendruscolo
Proteins: Structure, Function, and Bioinformatics
(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
Proc Natl Acad Sci U S A
(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 (San Diego, Calif.)
(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
Journal of molecular biology
(2004)
341
(doi: 10.1016/j.jmb.2004.06.043)
Amyloid disaggregation: Experiencing hierarchical grades of reversibility
M Calamai, C Canale, A Relini, M Stefani, F Chiti, CM Dobson
PROTEIN SCIENCE
(2004)
13
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
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
Proc Natl Acad Sci U S A
(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
J Mol Biol
(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 Engineering Design and Selection
(2004)
17
(doi: 10.1093/protein/gzh052)
Protein chemistry. In the footsteps of alchemists.
CM Dobson
Science (New York, N.Y.)
(2004)
304
(doi: 10.1126/science.1093078)
Reconstruction of protein structures from a vectorial representation
M Porto, U Bastolla, HE Roman, M Vendruscolo
Physical review letters
(2004)
92
Yusuf Hamied Department of Chemistry
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CB2 1EW
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