Centre for Misfolding Diseases

Publications

Tips on using this search form

  • All search terms are case-insensitive
  • If you specify more than one search option (e.g. you search for both "Authors" and "Paper title") then the publications returned will be those that match all of your search terms
  • To reset the search form, click here
  • Currently displaying 1921 - 1940 of 2456 publications
Author(s)
Publication title
Journal Name
Publication year
A highly amyloidogenic region of hen lysozyme
E Frare, P Polverino De Laureto, J Zurdo, CM Dobson, A Fontana
Journal of Molecular Biology
(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 of the United States of America
(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 Engineering Design and Selection
(2004)
17
(doi: 10.1093/proeng/gzh052)
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
Reconstruction of protein structures from a vectorial representation.
M Porto, U Bastolla, HE Roman, M Vendruscolo
Phys Rev Lett
(2004)
92
(doi: 10.1103/PhysRevLett.92.218101)
Formation of amyloid aggregates from human lysozyme and its disease-associated variants using hydrostatic pressure.
FG De Felice, MNN Vieira, MNL Meirelles, LA Morozova-Roche, CM Dobson, ST Ferreira
FASEB Journal
(2004)
18
(doi: 10.1096/fj.03-1072fje)
Phase-resolved pulsed precessional motion at a Schottky barrier
M Buess, TPJ Knowles, U Ramsperger, D Pescia, CH Back
Physical Review B
(2004)
69
(doi: 10.1103/physrevb.69.174422)
NMR studies of molecular dynamics
DM Korzhnev, X Salvatella, M Vendruscolo, AA Di Nardo, AR Davidson, CM Dobson, L Kay
FASEB JOURNAL
(2004)
18
Prefibrillar amyloid protein aggregates share common features of cytotoxicity.
M Bucciantini, G Calloni, F Chiti, L Formigli, D Nosi, CM Dobson, M Stefani
Journal of Biological Chemistry
(2004)
279
(doi: 10.1074/jbc.M400348200)
Short amino acid stretches can mediate amyloid formation in globular proteins: The Src homology 3 (SH3) case
S Ventura, J Zurdo, S Narayanan, M Parreño, R Mangues, B Reif, F Chiti, E Giannoni, CM Dobson, FX Aviles, L Serrano
Proc Natl Acad Sci U S A
(2004)
101
(doi: 10.1073/pnas.0308249101)
Transition states for protein folding have native topologies despite high structural variability.
K Lindorff-Larsen, M Vendruscolo, E Paci, CM Dobson
Nature Structural and Molecular Biology
(2004)
11
(doi: 10.1038/nsmb765)
Local and global cooperativity in the human α-lactalbumin molten globule
CM Quezada, BA Schulman, JJ Froggatt, CM Dobson, C Redfield
J Mol Biol
(2004)
338
(doi: 10.1016/j.jmb.2004.02.045)
Three-Dimensional Structures of Translating Ribosomes by Cryo-EM
RJC Gilbert, P Fucini, S Connell, SD Fuller, KH Nierhaus, CV Robinson, CM Dobson, DI Stuart
Mol Cell
(2004)
14
(doi: 10.1016/s1097-2765(04)00163-7)
Inhibition of protein crystallization by evolutionary negative design
JPK Doye, AA Louis, M Vendruscolo
Physical Biology
(2004)
1
(doi: 10.1088/1478-3967/1/1/P02)
Exploring amyloid formation by a de novo design.
RA Kammerer, D Kostrewa, J Zurdo, A Detken, C García-Echeverría, JD Green, SA Müller, BH Meier, FK Winkler, CM Dobson, MO Steinmetz
Proc Natl Acad Sci U S A
(2004)
101
(doi: 10.1073/pnas.0306786101)
Determination of an ensemble of structures representing the denatured state of the bovine acyl-coenzyme a binding protein.
K Lindorff-Larsen, S Kristjansdottir, K Teilum, W Fieber, CM Dobson, FM Poulsen, M Vendruscolo
Journal of the American Chemical Society
(2004)
126
(doi: 10.1021/ja039250g)
Inhibition of protein crystallization by evolutionary negative design
JPK Doye, AA Louis, M Vendruscolo
Phys Biol
(2004)
1
(doi: 10.1088/1478-3967/1/1/P02)
Yusuf Hamied Department of Chemistry
Lensfield Road
Cambridge
CB2 1EW
T: +44 (0) 1223 336300
enquiries@ch.cam.ac.uk
Contacts
Directions

Privacy and cookie policy

About the Department

Departmental Services

Study at Cambridge

About the University

Research at Cambridge