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Professor Michele Vendruscolo

Portrait of mv245


In the last 15 years our research has been focused on the development of methods of characterising the structure, dynamics and interactions of proteins in previously inaccessible states. These methods are based on the use of experimental data, in particular from nuclear magnetic resonance spectroscopy, as structural restraints in molecular dynamics simulations. Through this approach it is possible to obtain information about a variety of protein conformations, as for example those populated during the folding process, and about protein interactions in complex environments, including those generating aggregate species that are associated with neurodegenerative disorders such as Alzheimer's and Parkinson's diseases.

More recently, these studies have led us to investigate the physico-chemical principles of proteins homeostasis and their application to the development of therapeutic strategies against neurodegenerative diseases. Starting from the observation that proteins are expressed in the cell at levels close to their solubility limits, we are developing approaches to prevent or delay misfolding disorders based on the enhancement of our quality control mechanisms against protein aggregation.




A protein homeostasis signature in healthy brains recapitulates tissue vulnerability to Alzheimer's disease.
R Freer, P Sormanni, G Vecchi, P Ciryam, CM Dobson, M Vendruscolo
– Sci Adv
Chemical properties of lipids strongly affect the kinetics of the membrane-induced aggregation of alpha-synuclein
C Galvagnion, JWP Brown, MM Ouberai, P Flagmeier, M Vendruscolo, AK Buell, E Sparr, CM Dobson
– Proceedings of the National Academy of Sciences of the United States of America
Structure of a low-population binding intermediate in protein-RNA recognition.
AN Borkar, MF Bardaro, C Camilloni, FA Aprile, G Varani, M Vendruscolo
– Proceedings of the National Academy of Sciences of the United States of America
Particle-Based Monte-Carlo Simulations of Steady-State Mass Transport at Intermediate Péclet Numbers
T Müller, P Arosio, L Rajah, SIA Cohen, EV Yates, M Vendruscolo, CM Dobson, TPJ Knowles
– International Journal of Nonlinear Sciences and Numerical Simulation
Structural Effects of Two Camelid Nanobodies Directed to Distinct C-Terminal Epitopes on α-Synuclein.
F El-Turk, FN Newby, E De Genst, T Guilliams, T Sprules, A Mittermaier, CM Dobson, M Vendruscolo
– Biochemistry
Structural characterization of the interaction of alpha-synuclein nascent chains with the ribosomal surface and trigger factor
A Deckert, CA Waudby, T Wlodarski, AS Wentink, X Wang, JP Kirkpatrick, JFS Paton, C Camilloni, P Kukic, CM Dobson, M Vendruscolo, LD Cabrita, J Christodoulou
– Proceedings of the National Academy of Sciences of the United States of America
A transcriptional signature of Alzheimer's disease is associated with a metastable subproteome at risk for aggregation.
P Ciryam, R Kundra, R Freer, RI Morimoto, CM Dobson, M Vendruscolo
– Proceedings of the National Academy of Sciences of the United States of America
Identification and Structural Characterization of an Intermediate in the Folding of the Measles Virus X Domain.
D Bonetti, C Camilloni, L Visconti, S Longhi, M Brunori, M Vendruscolo, S Gianni
– J Biol Chem
A Fragment-Based Method of Creating Small-Molecule Libraries to Target the Aggregation of Intrinsically Disordered Proteins
P Joshi, S Chia, J Habchi, TPJ Knowles, CM Dobson, M Vendruscolo
– ACS Comb Sci
A structural ensemble of a ribosome-nascent chain complex during cotranslational protein folding.
LD Cabrita, AME Cassaignau, HMM Launay, CA Waudby, T Wlodarski, C Camilloni, M-E Karyadi, AL Robertson, X Wang, AS Wentink, LS Goodsell, CA Woolhead, M Vendruscolo, CM Dobson, J Christodoulou
– Nature Structural & Molecular Biology
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01223 763873

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