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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.

 

 

Publications

The CamSol method of rational design of protein mutants with enhanced solubility
P Sormanni, FA Aprile, M Vendruscolo – Journal of Molecular Biology (2015) 427, 478
Structure of a low-population intermediate state in the release of an enzyme product.
A De Simone, FA Aprile, A Dhulesia, CM Dobson, M Vendruscolo – eLife (2015) 4
Simultaneous Sequence-Based Prediction of the Statistical Populations of Ordered and Disordered Regions in Proteins.
P Sormanni, C Camilloni, P Fariselli, M Vendruscolo – J Mol Biol (2014)
Characterization of the conformational fluctuations in the josephin domain of ataxin-3.
D Sanfelice, A De Simone, A Cavalli, S Faggiano, M Vendruscolo, A Pastore – Biophys J (2014) 107, 2923
The H50Q mutation induces a tenfold decrease in the solubility of α-synuclein.
R Porcari, C Proukakis, CA Waudby, B Bolognesi, PP Mangione, JF Paton, S Mullin, LD Cabrita, A Penco, A Relini, G Verona, M Vendruscolo, M Stoppini, GG Tartaglia, C Camilloni, J Christodoulou, AH Schapira, V Bellotti – J Biol Chem (2014)
Erratum to ADP ribosylation adapts an ER chaperone response to short-term fluctuations in unfolded protein load [198 3 (2012) 371-385] doi 10.1083/jcb.20120200511112014c
JE Chambers, K Petrova, G Tomba, M Vendruscolo, D Ron – The Journal of cell biology (2014) 207, 569
A Relationship between the Transient Structure in the Monomeric State and the Aggregation Propensities of α-Synuclein and β-Synuclein
JR Allison, RC Rivers, JC Christodoulou, M Vendruscolo, CM Dobson – Biochemistry (2014) 53, 7170
Understanding the frustration arising from the competition between function, misfolding, and aggregation in a globular protein.
S Gianni, C Camilloni, R Giri, A Toto, D Bonetti, A Morrone, P Sormanni, M Brunori, M Vendruscolo – Proceedings of the National Academy of Sciences of the United States of America (2014) 111, 14141
Identification and characterization of PKCγ, a kinase associated with SCA14, as an amyloidogenic protein.
H Takahashi, N Adachi, T Shirafuji, S Danno, T Ueyama, M Vendruscolo, AN Shuvaev, T Sugimoto, T Seki, D Hamada, K Irie, H Hirai, N Sakai, N Saito – Hum Mol Genet (2014) 24, 525
Equilibrium simulations of proteins using molecular fragment replacement and NMR chemical shifts
W Boomsma, P Tian, J Frellsen, J Ferkinghoff-Borg, T Hamelryck, K Lindorff-Larsen, M Vendruscolo – Proceedings of the National Academy of Sciences of the United States of America (2014) 111, 13852
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Research Interest Groups

Telephone number

01223 763873

Email address

mv245@cam.ac.uk