Chemical properties of lipids strongly affect the kinetics of the membrane-induced aggregation of Îą-synuclein.

Galvagnion C, Brown JW, Ouberai MM, Flagmeier P, Vendruscolo M, Buell AK, Sparr E, Dobson CM

Quantitative analysis of co-oligomer formation by amyloid-beta peptide isoforms.

Iljina M, Garcia GA, Dear AJ, Flint J, Narayan P, Michaels TC, Dobson CM, Frenkel D, Knowles TP, Klenerman D

Structural Ensembles of Membrane-bound Îą-Synuclein Reveal the Molecular Determinants of Synaptic Vesicle Affinity.

Fusco G, De Simone A, Arosio P, Vendruscolo M, Veglia G, Dobson CM

Structural Effects of Two Camelid Nanobodies Directed to Distinct C-Terminal Epitopes on Îą-Synuclein.

El-Turk F, Newby FN, De Genst E, Guilliams T, Sprules T, Mittermaier A, Dobson CM, Vendruscolo M

Structural characterization of the interaction of Îą-synuclein nascent chains with the ribosomal surface and trigger factor.

Deckert A, Waudby CA, Wlodarski T, Wentink AS, Wang X, Kirkpatrick JP, Paton JF, Camilloni C, Kukic P, Dobson CM, Vendruscolo M, Cabrita LD, Christodoulou J

Effect of molecular chaperones on aberrant protein oligomers in vitro: super-versus sub-stoichiometric chaperone concentrations.

Cappelli S, Penco A, Mannini B, Cascella R, Wilson MR, Ecroyd H, Li X, Buxbaum JN, Dobson CM, Cecchi C, Relini A, Chiti F

Ca2+ is a key factor in Îą-synuclein-induced neurotoxicity.

Angelova PR, Ludtmann MH, Horrocks MH, Negoda A, Cremades N, Klenerman D, Dobson CM, Wood NW, Pavlov EV, Gandhi S, Abramov AY

A transcriptional signature of Alzheimer's disease is associated with a metastable subproteome at risk for aggregation.

Ciryam P, Kundra R, Freer R, Morimoto RI, Dobson CM, Vendruscolo M

The S/T-Rich Motif in the DNAJB6 Chaperone Delays Polyglutamine Aggregation and the Onset of Disease in a Mouse Model.

Kakkar V, MĂĽnsson C, de Mattos EP, Bergink S, van der Zwaag M, van Waarde MAWH, Kloosterhuis NJ, Melki R, van Cruchten RTP, Al-Karadaghi S, Arosio P, Dobson CM, Knowles TPJ, Bates GP, van Deursen JM, Linse S, van de Sluis B, Emanuelsson C, Kampinga HH

Nanoscopic insights into seeding mechanisms and toxicity of Îą-synuclein species in neurons.

Pinotsi D, Michel CH, Buell AK, Laine RF, Mahou P, Dobson CM, Kaminski CF, Kaminski Schierle GS

A structural ensemble of a ribosome-nascent chain complex during cotranslational protein folding.

Cabrita LD, Cassaignau AME, Launay HMM, Waudby CA, Wlodarski T, Camilloni C, Karyadi ME, Robertson AL, Wang X, Wentink AS, Goodsell L, Woolhead CA, Vendruscolo M, Dobson CM, Christodoulou J

Amyloid-β and ι-Synuclein Decrease the Level of Metal-Catalyzed Reactive Oxygen Species by Radical Scavenging and Redox Silencing.

Pedersen JT, Chen SW, Borg CB, Ness S, Bahl JM, Heegaard NH, Dobson CM, Hemmingsen L, Cremades N, Teilum K

Kinetic analysis reveals the diversity of microscopic mechanisms through which molecular chaperones suppress amyloid formation.

Arosio P, Michaels TC, Linse S, MĂĽnsson C, Emanuelsson C, Presto J, Johansson J, Vendruscolo M, Dobson CM, Knowles TP

Quantitative thermophoretic study of disease-related protein aggregates.

Wolff M, Mittag JJ, Herling TW, Genst ED, Dobson CM, Knowles TP, Braun D, Buell AK

Single-Molecule Imaging of Individual Amyloid Protein Aggregates in Human Biofluids.

Horrocks MH, Lee SF, Gandhi S, Magdalinou NK, Chen SW, Devine MJ, Tosatto L, Kjaergaard M, Beckwith JS, Zetterberg H, Iljina M, Cremades N, Dobson CM, Wood NW, Klenerman D