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Centre for Misfolding Diseases

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  • Currently displaying 3081 - 3100 of 3415 publications
Atmospheric aerosols as prebiotic chemical reactors.
CM Dobson, GB Ellison, AF Tuck, V Vaida
– Proc Natl Acad Sci U S A
(2000)
97,
11864
(doi: 10.1073/pnas.200366897)
Analysis of the degradation of oligonucleotide strands during the freezing/thawing processes using MALDI-MS
DL Davis, EP O'Brien, CM Bentzley
– Analytical Chemistry
(2000)
72,
5092
(doi: 10.1021/ac000225s)
Macromolecular crowding perturbs protein refolding kinetics: Implications for folding inside the cell
B van den Berg, R Wain, CM Dobson, RJ Ellis
– The EMBO journal
(2000)
19,
3870
(doi: 10.1093/emboj/19.15.3870)
Stabilisation of alpha-helices by site-directed mutagenesis reveals the importance of secondary structure in the transition state for acylphosphatase folding.
N Taddei, F Chiti, T Fiaschi, M Bucciantini, C Capanni, M Stefani, L Serrano, CM Dobson, G Ramponi
– Journal of Molecular Biology
(2000)
300,
633
(doi: 10.1006/jmbi.2000.3870)
Formation and seeding of amyloid fibrils from wild-type hen lysozyme and a peptide fragment from the beta-domain
MR Krebs, DK Wilkins, EW Chung, MC Pitkeathly, AK Chamberlain, J Zurdo, CV Robinson, CM Dobson
– Journal of molecular biology
(2000)
300,
541
(doi: 10.1006/jmbi.2000.3862)
Understanding protein folding via free-energy surfaces from theory and experiment
AR Dinner, A Sali, LJ Smith, CM Dobson, M Karplus
– Trends in Biochemical Sciences
(2000)
25,
331
(doi: 10.1016/s0968-0004(00)01610-8)
A compact monomeric intermediate identified by NMR in the denaturation of dimeric triose phosphate isomerase.
CJ Morgan, DK Wilkins, LJ Smith, Y Kawata, CM Dobson
– Journal of Molecular Biology
(2000)
300,
11
(doi: 10.1006/jmbi.2000.3834)
Toward an energy function for the contact map representation of proteins.
K Park, M Vendruscolo, E Domany
– Proteins Structure Function and Bioinformatics
(2000)
40,
237
(doi: 10.1002/(sici)1097-0134(20000801)40:2<237::aid-prot60>3.0.co;2-p)
Detection and selective dissociation of intact ribosomes in a mass spectrometer
AA Rostom, P Fucini, DR Benjamin, R Juenemann, KH Nierhaus, FU Hartl, CM Dobson, CV Robinson
– Proc Natl Acad Sci U S A
(2000)
97,
5185
(doi: 10.1073/pnas.97.10.5185)
Improved photo-CIDNP methods for studying protein structure and folding.
K Maeda, CE Lyon, JJ Lopez, M Cemazar, CM Dobson, PJ Hore
– Journal of Biomolecular NMR
(2000)
16,
235
(doi: 10.1023/a:1008351128089)
Structurally constrained protein evolution: Results from a lattice simulation
U Bastolla, M Vendruscolo, HE Roman
– The European Physical Journal B
(2000)
15,
385
(doi: 10.1007/s100510051140)
Chemical dissection and reassembly of amyloid fibrils formed by a peptide fragment of transthyretin
CE MacPhee, CM Dobson
– Journal of Molecular Biology
(2000)
297,
1203
(doi: 10.1006/jmbi.2000.3600)
A statistical mechanical method to optimize energy functions for protein folding
U Bastolla, M Vendruscolo, EW Knapp
– Proceedings of the National Academy of Sciences of the United States of America
(2000)
97,
3977
(doi: 10.1073/pnas.97.8.3977)
Mutational analysis of the propensity for amyloid formation by a globular protein.
F Chiti, N Taddei, M Bucciantini, P White, G Ramponi, CM Dobson
– The EMBO journal
(2000)
19,
1441
(doi: 10.1093/emboj/19.7.1441)
Protein folding, misfolding, and disease.
CM Dobson
– ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY
(2000)
219,
U277
(link to publication)
A partially unfolded structure of the alkaline-denatured state of pepsin and its implication for stability of the zymogen-derived protein.
T Konno, YO Kamatari, N Tanaka, H Kamikubo, CM Dobson, K Nagayama
– Biochemistry
(2000)
39,
4182
(doi: 10.1021/bi991923d)
Thermal unfolding of an intermediate is associated with non-arrhenius kinetics in the folding of hen lysozyme
A Matagne, M Jamin, EW Chung, CV Robinson, SE Radford, CM Dobson
– Journal of Molecular Biology
(2000)
297,
193
(doi: 10.1006/jmbi.2000.3540)
Dissection of multi‐protein complexes using mass spectrometry: Subunit interactions in transthyretin and retinol‐binding protein complexes
AA Rostom, M Sunde, SJ Richardson, G Schreiber, S Jarvis, R Bateman, CM Dobson, CV Robinson
– Proteins
(2000)
Suppl 2,
3
(doi: 10.1002/(SICI)1097-0134(1998)33:2+<3::AID-PROT2>3.0.CO;2-H)
Identification of residues involved in the interaction of Staphylococcus aureus fibronectin-binding protein with the 4F15F1 module pair of human fibronectin using heteronuclear NMR spectroscopy
CJ Penkett, CM Dobson, LJ Smith, JR Bright, AR Pickford, ID Campbell, JR Potts
– Biochemistry
(2000)
39,
2887
(doi: 10.1021/bi992267k)
Can a pairwise contact potential stabilize native protein folds against decoys obtained by threading?
M Vendruscolo, R Najmanovich, E Domany
– Proteins
(2000)
38,
134
(doi: 10.1002/(sici)1097-0134(20000201)38:2<134::aid-prot3>3.0.co;2-a)

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