Centre for Misfolding Diseases

Publications

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  • Currently displaying 1981 - 2000 of 2486 publications
Author(s)
Publication title
Journal Name
Publication year
Hydrophobic clustering in nonnative states of a protein: interpretation of chemical shifts in NMR spectra of denatured states of lysozyme.
PA Evans, KD Topping, DN Woolfson, CM Dobson
Proteins
(2004)
9
(doi: 10.1002/prot.340090404)
A molecular dynamics analysis of protein structural elements.
CB Post, CM Dobson, M Karplus
Proteins: Structure, Function, and Bioinformatics
(2004)
5
(doi: 10.1002/prot.340050409)
Hydrogen exchange in native and denatured states of hen egg-white lysozyme.
SE Radford, M Buck, KD Topping, CM Dobson, PA Evans
Proteins
(2004)
14
(doi: 10.1002/prot.340140210)
High-resolution molecular structure of a peptide in an amyloid fibril determined by magic angle spinning NMR spectroscopy
CP Jaroniec, CE MacPhee, VS Bajaj, MT McMahon, CM Dobson, RG Griffin
Proceedings of the National Academy of Sciences of the United States of America
(2004)
101
(doi: 10.1073/pnas.0304849101)
Structural dissection of alkaline‐denatured pepsin
YO Kamatari, CM Dobson, T Konno
Journal of Spectroscopy
(2004)
18
(doi: 10.1155/2004/769354)
Principles of protein folding, misfolding and aggregation.
CM Dobson
Seminars in cell & developmental biology
(2004)
15
(doi: 10.1016/j.semcdb.2003.12.008)
Disaggregation experiments as a tool to detect protofibrillar intermediates
M Calamai, C Canale, A Relini, M Stefani, F Chiti, CM Dobson
(2004)
Protein folding and misfolding.
CM Dobson
Nature
(2003)
426
(doi: 10.1038/nature02261)
Response of native and denatured hen lysozyme to high pressure studied by 15N/1H NMR spectroscopy
YO Kamatari, H Yamada, K Akasaka, JA Jones, CM Dobson, LJ Smith
European Journal of Biochemistry
(2003)
268
(doi: 10.1046/j.1432-1327.2001.02050.x)
Comparison of the transition state ensembles for folding of Im7 and Im9 determined using all‐atom molecular dynamics simulations with ϕ value restraints
E Paci, CT Friel, K Lindorff-Larsen, SE Radford, M Karplus, M Vendruscolo
Proteins: Structure, Function, and Bioinformatics
(2003)
54
(doi: 10.1002/prot.10595)
Myoglobin forms amyloid fibrils by association of unfolded polypeptide segments.
M Fändrich, V Forge, K Buder, M Kittler, CM Dobson, S Diekmann
Proc Natl Acad Sci U S A
(2003)
100
(doi: 10.1073/pnas.0303758100)
Rare fluctuations of native proteins sampled by equilibrium hydrogen exchange
M Vendruscolo, E Paci, CM Dobson, M Karplus
Journal of the American Chemical Society
(2003)
125
(doi: 10.1021/ja036523z)
Structures and relative free energies of partially folded states of proteins.
M Vendruscolo, E Paci, M Karplus, CM Dobson
Proceedings of the National Academy of Sciences of the United States of America
(2003)
100
(doi: 10.1073/pnas.2036516100)
Protein Aggregation and Amyloid Fibril Formation by an SH3 Domain Probed by Limited Proteolysis
P Polverino de Laureto, N Taddei, E Frare, C Capanni, S Costantini, J Zurdo, F Chiti, CM Dobson, A Fontana
Journal of Molecular Biology
(2003)
334
(doi: 10.1016/j.jmb.2003.09.024)
Amyloid Fibril Formation by Lens Crystallin Proteins and Its Implications for Cataract Formation
S Meehan, Y Berry, B Luisi, CM Dobson, JA Carver, CE MacPhee
The Journal of biological chemistry
(2003)
279
(doi: 10.1074/jbc.M308203200)
Rapid Sample-Mixing Technique for Transient NMR and Photo-CIDNP Spectroscopy:  Applications to Real-Time Protein Folding
KH Mok, T Nagashima, IJ Day, JA Jones, CJV Jones, CM Dobson, PJ Hore
Journal of the American Chemical Society
(2003)
125
(doi: 10.1021/ja036357v)
”Protein Misfolding and its Links with Human Disease”, in Molecular Informatics: Confronting Complexity
CM Dobson
(2003)
Lithostathine quadruple-helical filaments form proteinase K-resistant deposits in Creutzfeldt-Jakob disease
E Laurine, C Grégoire, M Fändrich, S Engemann, S Marchal, L Thion, M Mohr, B Monsarrat, B Michel, CM Dobson, E Wanker, M Erard, J-M Verdier
J Biol Chem
(2003)
278
(doi: 10.1074/jbc.m306767200)
Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution
M Stefani, CM Dobson
J Mol Med (Berl)
(2003)
81
(doi: 10.1007/s00109-003-0464-5)
A camelid antibody fragment inhibits the formation of amyloid fibrils by human lysozyme.
M Dumoulin, AM Last, A Desmyter, K Decanniere, D Canet, G Larsson, A Spencer, DB Archer, J Sasse, S Muyldermans, L Wyns, C Redfield, A Matagne, CV Robinson, CM Dobson
Nature
(2003)
424
(doi: 10.1038/nature01870)
Yusuf Hamied Department of Chemistry
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