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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.




Structural effects of two camelid nanobodies directed to distinct C-terminal epitopes on α-synuclein.
F El-Turk, F Newby, EJ de Genst, T Guilliams, T Sprules, AK Mittermaier, CM Dobson, M Vendruscolo – Biochemistry (2016)
Structural characterization of the interaction of α-synuclein nascent chains with the ribosomal surface and trigger factor.
A Deckert, CA Waudby, T Wlodarski, AS Wentink, X Wang, JP Kirkpatrick, JF 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 (2016) 113, 5012
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 (2016) 113, 4753
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 (2016)
A Fragment-Based Method of Creating Small-Molecule Libraries to Target the Aggregation of Intrinsically Disordered Proteins
P Joshi, S Chia, J Habchi, TP Knowles, CM Dobson, M Vendruscolo – ACS Comb Sci (2016) 18, 144
A structural ensemble of a ribosome-nascent chain complex during cotranslational protein folding.
LD Cabrita, AM Cassaignau, HM Launay, CA Waudby, T Wlodarski, C Camilloni, ME Karyadi, AL Robertson, X Wang, AS Wentink, LS Goodsell, CA Woolhead, M Vendruscolo, CM Dobson, J Christodoulou – Nat Struct Mol Biol (2016) 23, 278
An anticancer drug suppresses the primary nucleation reaction that initiates the production of the toxic Aβ42 aggregates linked with Alzheimer's disease.
J Habchi, P Arosio, M Perni, AR Costa, M Yagi-Utsumi, P Joshi, S Chia, SI Cohen, MB Müller, S Linse, EA Nollen, CM Dobson, TP Knowles, M Vendruscolo – Sci Adv (2016) 2, e1501244
Molecular mechanisms of protein aggregation from global fitting of kinetic models.
G Meisl, JB Kirkegaard, P Arosio, TC Michaels, M Vendruscolo, CM Dobson, S Linse, TP Knowles – Nature protocols (2016) 11, 252
Hamiltonian Dynamics of Protein Filament Formation.
TC Michaels, SI Cohen, M Vendruscolo, CM Dobson, TP Knowles – Phys Rev Lett (2016) 116, 038101
Kinetic analysis reveals the diversity of microscopic mechanisms through which molecular chaperones suppress amyloid formation
P Arosio, TC Michaels, S Linse, C Månsson, C Emanuelsson, J Presto, J Johansson, M Vendruscolo, CM Dobson, TP Knowles – Nature Communications (2016) 7, 10948
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01223 763873

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