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Centre for Misfolding Diseases

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  • Currently displaying 3101 - 3120 of 3390 publications
Characterisation of the dominant oxidative folding intermediate of hen lysozyme.
B van den Berg, EW Chung, CV Robinson, CM Dobson
– J Mol Biol
(1999)
290,
781
(doi: 10.1006/jmbi.1999.2915)
Oleg Ptitsyn (1929-99) - Obituary
CM Dobson, RJ Ellis
– NATURE
(1999)
400,
122
(doi: 10.1038/22019)
Oleg Ptitsyn (1929-99).
CM Dobson, RJ Ellis
– Nature
(1999)
400,
122
(doi: 10.1038/22019)
Two-dimensional 15N-1H photo-CIDNP as a surface probe of native and partially structured proteins
CE Lyon, JA Jones, C Redfield, CM Dobson, PJ Hore
– Journal of the American Chemical Society
(1999)
121,
6505
(doi: 10.1021/ja9907663)
Independent nucleation and heterogeneous assembly of structure during folding of equine lysozyme
LA Morozova-Roche, JA Jones, W Noppe, CM Dobson
– Journal of molecular biology
(1999)
289,
1055
(doi: 10.1006/jmbi.1999.2741)
Rapid collapse and slow structural reorganisation during the refolding of bovine alpha-lactalbumin.
V Forge, RT Wijesinha, J Balbach, K Brew, CV Robinson, C Redfield, CM Dobson
– J Mol Biol
(1999)
288,
673
(doi: 10.1006/jmbi.1999.2687)
Side-chain conformations in an unfolded protein: χ 1 distributions in denatured hen lysozyme determined by heteronuclear 13 C, 15 N NMR spectroscopy 1 1Edited by A. R. Fersht
M Hennig, W Bermel, A Spencer, CM Dobson, LJ Smith, H Schwalbe
– Journal of Molecular Biology
(1999)
288,
705
(doi: 10.1006/jmbi.1999.2722)
Mechanistic Studies of the Folding of Human Lysozyme and the Origin of Amyloidogenic Behavior in Its Disease-Related Variants
D Canet, M Sunde, AM Last, A Miranker, A Spencer, CV Robinson, CM Dobson
– Biochemistry
(1999)
38,
6419
(doi: 10.1021/bi983037t)
From Computer Simulations to Human Disease
SE Radford, CM Dobson
– Cell
(1999)
97,
291
(doi: 10.1016/s0092-8674(00)80739-4)
Mapping the structural characteristics of an ion channel in lipid bilayers: A H/D exchange MS/MS study of gramicidin A.
M Bouchard, P Tito, DR Benjamin, CV Robinson, CM Dobson
– FASEB JOURNAL
(1999)
13,
A1569
(link to publication)
Acceleration of the folding of acylphosphatase by stabilization of local secondary structure
F Chiti, N Taddei, P Webster, D Hamada, T Fiaschi, G Ramponi, CM Dobson
– Nature Structural & Molecular Biology
(1999)
6,
380
(doi: 10.1038/7616)
Designing conditions for in vitro formation of amyloid protofilaments and fibrils
F Chiti, P Webster, N Taddei, A Clark, M Stefani, G Ramponi, CM Dobson
– Proceedings of the National Academy of Sciences
(1999)
96,
3590
(doi: 10.1073/pnas.96.7.3590)
Side-chain conformational disorder in a molten globule: molecular dynamics simulations of the A-state of human α-lactalbumin 1 1 Edited by J. M. Thornton
LJ Smith, CM Dobson, WF van Gunsteren
– Journal of Molecular Biology
(1999)
286,
1567
(doi: 10.1006/jmbi.1999.2545)
Hydrophobicity and unique folding of selected polymers
M Vendruscolo
– The European Physical Journal B
(1999)
8,
323
(doi: 10.1007/s100510050695)
Cryo‐electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing
JL Jiménez, JI Guijarro, E Orlova, J Zurdo, CM Dobson, M Sunde, HR Saibil
– The EMBO journal
(1999)
18,
815
(doi: 10.1093/emboj/18.4.815)
The fundamentals of protein folding: Bringing together theory and experiment
CM Dobson, M Karplus
– Current Opinion in Structural Biology
(1999)
9,
92
(doi: 10.1016/s0959-440x(99)80012-8)
Thermodynamics and Kinetics of Folding of Common-Type Acylphosphatase: Comparison to the Highly Homologous Muscle Isoenzyme †
N Taddei, F Chiti, P Paoli, T Fiaschi, M Bucciantini, M Stefani, CM Dobson, G Ramponi
– Biochemistry
(1999)
38,
2135
(doi: 10.1021/bi9822630)
Protein folding in contact map space
M Vendruscolo, R Najmanovich, E Domany
– Physical Review Letters
(1999)
82,
656
(doi: 10.1103/PhysRevLett.82.656)
Protein folding using contact maps
M Vendruscolo, E Domany
– Vitamins and Hormones
(1999)
82,
171
(doi: 10.1103/physrevlett.82.656)
An optimal derivation of a potential for protein folding
M Vendruscolo
– Physica A: Statistical Mechanics and its Applications
(1999)
262,
35
(doi: 10.1016/S0378-4371(98)00358-6)

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