skip to content
 

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

MOAG-4 Promotes the Aggregation of α-Synuclein by Competing with Self-Protective Electrostatic Interactions
Y Yoshimura, MA Holmberg, P Kukic, CB Andersen, A Mata-Cabana, SF Falsone, M Vendruscolo, EAA Nollen, FAA Mulder
– J Biol Chem
(2017)
jbc.M116.764886
Simultaneous quantification of protein order and disorder.
P Sormanni, D Piovesan, GT Heller, M Bonomi, P Kukic, C Camilloni, M Fuxreiter, Z Dosztanyi, RV Pappu, MM Babu, S Longhi, P Tompa, AK Dunker, VN Uversky, SCE Tosatto, M Vendruscolo
– Nature Chemical Biology
(2017)
13,
339
Identification of an RNA Polymerase III Regulator Linked to Disease-Associated Protein Aggregation.
O Sin, T de Jong, A Mata-Cabana, M Kudron, MA Zaini, FA Aprile, RI Seinstra, E Stroo, RW Prins, CN Martineau, HH Wang, W Hogewerf, A Steinhof, EE Wanker, M Vendruscolo, CF Calkhoven, V Reinke, V Guryev, EAA Nollen
– Molecular Cell
(2017)
65,
1096
Inhibition of alpha-Synuclein Fibril Elongation by Hsp70 Is Governed by a Kinetic Binding Competition between alpha-Synuclein Species
FA Aprile, P Arosio, G Fusco, SW Chen, JR Kumita, A Dhulesia, P Tortora, TPJ Knowles, M Vendruscolo, CM Dobson, N Cremades
– Biochemistry
(2017)
56,
1177
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
(2017)
168,
944
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)
(2017)
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
  •  
  • 1 of 42
  • >

Research Interest Groups

Telephone number

01223 763873

Email address

mv245@cam.ac.uk