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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.




Dynamic binding mode of a Synaptotagmin-1-SNARE complex in solution.
KD Brewer, T Bacaj, A Cavalli, C Camilloni, JD Swarbrick, J Liu, A Zhou, P Zhou, N Barlow, J Xu, AB Seven, EA Prinslow, R Voleti, D Häussinger, AM Bonvin, DR Tomchick, M Vendruscolo, B Graham, TC Südhof, J Rizo – Nature Structural & Molecular Biology (2015)
Reply to "Comment on 'A Tensor-Free Method for the Structural and Dynamic Refinement of Proteins using Residual Dipolar Couplings'".
C Camilloni, M Vendruscolo – J Phys Chem B (2015) 150601163117002
Analysis of the performance of the CHESHIRE and YAPP methods at CASD-NMR round 3.
A Cavalli, M Vendruscolo – Journal of Biomolecular NMR (2015)
Widespread Proteome Remodeling and Aggregation in Aging C. elegans
DM Walther, P Kasturi, M Zheng, S Pinkert, G Vecchi, P Ciryam, RI Morimoto, CM Dobson, M Vendruscolo, M Mann, FU Hartl – Cell (2015) 161, 919
89 Constructing free energy landscapes of RNAs at atomic resolution and characterisation of their excited states
AN Borkar, P Vallurupalli, C Camilloni, LE Kay, M Vendruscolo – Journal of biomolecular structure & dynamics (2015) 33, 58
Structure and Dynamics of GeoCyp: A Thermophilic Cyclophilin with a Novel Substrate Binding Mechanism That Functions Efficiently at Low Temperatures.
MJ Holliday, C Camilloni, GS Armstrong, NG Isern, F Zhang, M Vendruscolo, EZ Eisenmesser – Biochemistry (2015) 54, 3207
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) 23, 745
A molecular chaperone breaks the catalytic cycle that generates toxic Aβ oligomers
SIA 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, TPJ Knowles, S Linse – Nature Structural and Molecular Biology (2015) 22, 207
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
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01223 763873

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