Centre for Misfolding Diseases

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  • Currently displaying 1361 - 1380 of 2338 publications
Author(s)
Publication title
Journal Name
Publication year
Fibrillogenic propensity of the GroEL apical domain: A Janus-faced minichaperone
J Chen, H Yagi, P Sormanni, M Vendruscolo, K Makabe, T Nakamura, Y Goto, K Kuwajima
FEBS Letters
(2012)
586
(doi: 10.1016/j.febslet.2012.03.019)
From macroscopic measurements to microscopic mechanisms of protein aggregation.
SIA Cohen, M Vendruscolo, CM Dobson, TPJ Knowles
Journal of Molecular Biology
(2012)
421
(doi: 10.1016/j.jmb.2012.02.031)
Determination of secondary structure populations in disordered states of proteins using nuclear magnetic resonance chemical shifts
C Camilloni, A De Simone, WF Vranken, M Vendruscolo
Biochemistry
(2012)
51
(doi: 10.1021/bi3001825)
A Novel Carbon Monoxide-Releasing Molecule Fully Protects Mice from Severe Malaria
AC Pena, N Penacho, L Mancio-Silva, R Neres, JD Seixas, AC Fernandes, CC Romão, MM Mota, GJL Bernardes, A Pamplona
Antimicrobial agents and chemotherapy
(2012)
56
(doi: 10.1128/aac.05571-11)
Characterization of the conformational equilibrium between the two major substates of RNase a using NMR chemical shifts
C Camilloni, P Robustelli, A De Simone, A Cavalli, M Vendruscolo
J Am Chem Soc
(2012)
134
(doi: 10.1021/ja210951z)
The aggregation and neurotoxicity of TDP-43 and its ALS-associated 25 kDa fragment are differentially affected by molecular chaperones in Drosophila.
JM Gregory, TP Barros, S Meehan, CM Dobson, LM Luheshi
PLoS ONE
(2012)
7
(doi: 10.1371/journal.pone.0031899)
Developing drug molecules for therapy with carbon monoxide
CC Romão, WA Blättler, JD Seixas, GJL Bernardes
Chem Soc Rev
(2012)
41
(doi: 10.1039/c2cs15317c)
Membrane lipid composition and its physicochemical properties define cell vulnerability to aberrant protein oligomers.
E Evangelisti, C Cecchi, R Cascella, C Sgromo, M Becatti, CM Dobson, F Chiti, M Stefani
J Cell Sci
(2012)
125
(doi: 10.1242/jcs.098434)
Blind testing of routine, fully automated determination of protein structures from nmr data
A Rosato, JM Aramini, C Arrowsmith, A Bagaria, D Baker, A Cavalli, JF Doreleijers, A Eletsky, A Giachetti, P Guerry, A Gutmanas, P Güntert, Y He, T Herrmann, YJ Huang, V Jaravine, HRA Jonker, MA Kennedy, OF Lange, G Liu, TE Malliavin, R Mani, B Mao, GT Montelione, M Nilges, P Rossi, G van der Schot, H Schwalbe, TA Szyperski, M Vendruscolo, R Vernon, WF Vranken, SD Vries, GW Vuister, B Wu, Y Yang, AMJJ Bonvin
Structure
(2012)
20
(doi: 10.1016/j.str.2012.01.002)
Blind testing of routine, fully automated determination of protein structures from nmr data
A Rosato, JM Aramini, C Arrowsmith, A Bagaria, D Baker, A Cavalli, JF Doreleijers, A Eletsky, A Giachetti, P Guerry, A Gutmanas, P Güntert, Y He, T Herrmann, YJ Huang, V Jaravine, HRA Jonker, MA Kennedy, OF Lange, G Liu, TE Malliavin, R Mani, B Mao, GT Montelione, M Nilges, P Rossi, G Van Der Schot, H Schwalbe, TA Szyperski, M Vendruscolo, R Vernon, WF Vranken, S De Vries, GW Vuister, B Wu, Y Yang, AMJJ Bonvin
Structure
(2012)
20
(doi: 10.1016/j.str.2012.01.002)
Proteome folding and aggregation
M Vendruscolo
Current Opinion in Structural Biology
(2012)
22
(doi: 10.1016/j.sbi.2012.01.005)
Measuring the kinetics of amyloid fibril elongation using quartz crystal microbalances
AK Buell, CM Dobson, ME Welland
Methods in Molecular Biology
(2012)
849
(doi: 10.1007/978-1-61779-551-0_8)
The nature and significance of protein aggregation phenomena
CM Dobson
PRION
(2012)
6
Co-translational folding of E. coli's cytosolic proteome exhibits kinetic effects that can significantly delay folding
P Ciryam, M Vendruscolo, CM Dobson, EP O'Brien
ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY
(2012)
244
Nanobodies as structural probes of protein misfolding and fibril formation
E De Genst, CM Dobson
Methods in Molecular Biology
(2012)
911
(doi: 10.1007/978-1-61779-968-6_34)
Fluctuations in water, the hydrophobic effect and self-assembly
PS Varilly, AJ Patel, SN Jamadagni, H Acharya, MF Hagan, S Garde, D Chandler, TPJ Knowles, D Frenkel
ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY
(2012)
244
The extracellular chaperone clusterin sequesters oligomeric forms of the amyloid-β(1-40) peptide.
P Narayan, A Orte, RW Clarke, B Bolognesi, S Hook, KA Ganzinger, S Meehan, MR Wilson, CM Dobson, D Klenerman
Nature structural & molecular biology
(2012)
19
(doi: 10.1038/nsmb.2191)
Anti-oligomer monoclonal antibodies reveal that protein aggregation modulates generalized physiological and pathological disturbances
M Tayebi, M Vendruscolo, M David
PRION
(2012)
6
Building well-defined glycoproteins
GJL Bernardes, BG Davis
ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY
(2012)
243
NMR chemical shifts and protein dynamics
C Camilloni, M Vendruscolo
FEBS JOURNAL
(2012)
279
Yusuf Hamied Department of Chemistry
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