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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

A natural product inhibits the initiation of α-synuclein aggregation and suppresses its toxicity
M Perni, C Galvagnion, A Maltsev, G Meisl, MBD Müller, PK Challa, JB Kirkegaard, P Flagmeier, SIA Cohen, R Cascella, SW Chen, R Limboker, P Sormanni, GT Heller, FA Aprile, N Cremades, C Cecchi, F Chiti, EAA Nollen, TPJ Knowles, M Vendruscolo, A Bax, M Zasloff, CM Dobson
– Proceedings of the National Academy of Sciences of the United States of America
(2017)
114,
E1009
Simultaneous NMR characterisation of multiple minima in the free energy landscape of an RNA UUCG tetraloop.
AN Borkar, P Vallurupalli, C Camilloni, LE Kay, M Vendruscolo
– Physical chemistry chemical physics : PCCP
(2017)
19,
2797
Principles of protein structural ensemble determination.
M Bonomi, GT Heller, C Camilloni, M Vendruscolo
– Current opinion in structural biology
(2017)
42,
106
Networks of Dynamic Allostery Regulate Enzyme Function
MJ Holliday, C Camilloni, GS Armstrong, M Vendruscolo, EZ Eisenmesser
– Structure (London, England : 1993)
(2016)
25,
276
β-Synuclein suppresses both the initiation and amplification steps of α-synuclein aggregation via competitive binding to surfaces.
JWP Brown, AK Buell, TCT Michaels, G Meisl, J Carozza, P Flagmeier, M Vendruscolo, TPJ Knowles, CM Dobson, C Galvagnion
– Scientific reports
(2016)
6,
36010
Mutations associated with familial Parkinson's disease alter the initiation and amplification steps of α-synuclein aggregation.
P Flagmeier, G Meisl, M Vendruscolo, TPJ Knowles, CM Dobson, AK Buell, C Galvagnion
– Proceedings of the National Academy of Sciences of the United States of America
(2016)
113,
10328
A protein homeostasis signature in healthy brains recapitulates tissue vulnerability to Alzheimers disease
R Freer, P Sormanni, G Vecchi, P Ciryam, CM Dobson, M Vendruscolo
– Sci Adv
(2016)
2,
e1600947
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
(2016)
113,
7065
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
(2016)
113,
7171
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
(2016)
175
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Research Interest Groups

Telephone number

01223 763873

Email address

mv245@cam.ac.uk