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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

Structure and Dynamics of the Integrin LFA-1 I-Domain in the Inactive State Underlie its Inside-Out/Outside-In Signaling and Allosteric Mechanisms.
P Kukic, HT Alvin Leung, F Bemporad, FA Aprile, JR Kumita, A De Simone, C Camilloni, M Vendruscolo – Structure (London, England : 1993) (2014)
The physical basis of protein misfolding disorders
TPJ Knowles, M Vendruscolo, CM Dobson – Physics Today (2015) 68, 36
The s2D method: Simultaneous sequence-based prediction of the statistical populations of ordered and disordered regions in proteins
P Sormanni, C Camilloni, P Fariselli, M Vendruscolo – Journal of Molecular Biology (2015) 427, 982
A molecular chaperone breaks the catalytic cycle that generates toxic Aβ oligomers
SI Cohen, P Arosio, J Presto, FR Kurudenkandy, H Biverstål, L Dolfe, C Dunning, X Yang, B Frohm, M Vendruscolo, J Johansson, CM Dobson, A Fisahn, TP Knowles, S Linse – Nature Structural & Molecular Biology (2015) 22, 207
Lipid vesicles trigger α-synuclein aggregation by stimulating primary nucleation.
C Galvagnion, AK Buell, G Meisl, TC Michaels, M Vendruscolo, TP Knowles, CM Dobson – Nature Chemical Biology (2015) 11, 229
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
Supersaturation is a major driving force for protein aggregation in neurodegenerative diseases.
P Ciryam, R Kundra, RI Morimoto, CM Dobson, M Vendruscolo – Trends Pharmacol Sci (2015) 36, 72
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
Supersaturation is a major driving force for protein aggregation in neurodegenerative diseases
P Ciryam, R Kundra, RI Morimoto, CM Dobson, M Vendruscolo – Trends in Pharmacological Sciences (2015) 36, 72
The s2D Method: Simultaneous Sequence-Based Prediction of the Statistical Populations of Ordered and Disordered Regions in Proteins
P Sormanni, C Camilloni, P Fariselli, M Vendruscolo – Journal of molecular biology (2014) 427, 982
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Research Interest Groups

Telephone number

01223 763873

Email address

mv245@cam.ac.uk