skip to content
Home

Yusuf Hamied Department of Chemistry

 

Professor Michele Vendruscolo

Professor of Biophysics

Our research

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.

Application to neurodegenerative 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.

Watch Professor Vendruscolo discuss his research

Take a tour of the Una Finlay Laboratory in the Centre for Misfolding Diseases

Publications

Effects of the known pathogenic mutations on the aggregation pathway of the amyloidogenic peptide of apolipoprotein A-I
S Raimondi, F Guglielmi, S Giorgetti, SD Gaetano, A Arciello, DM Monti, A Relini, D Nichino, SM Doglia, A Natalello, P Pucci, P Mangione, L Obici, G Merlini, M Stoppini, P Robustelli, GG Tartaglia, M Vendruscolo, CM Dobson, R Piccoli, V Bellotti
– Journal of Molecular Biology
(2011)
407,
465
(doi: 10.1016/j.jmb.2011.01.044)
Detection of early locomotor abnormalities in a Drosophila model of Alzheimer's disease
TR Jahn, KJ Kohlhoff, M Scott, GG Tartaglia, DA Lomas, CM Dobson, M Vendruscolo, DC Crowther
– J Neurosci Methods
(2011)
197,
186
(doi: 10.1016/j.jneumeth.2011.01.026)
Effects of the known pathogenic mutations on the aggregation pathway of the amyloidogenic peptide of apolipoprotein A-I.
S Raimondi, F Guglielmi, S Giorgetti, S Di Gaetano, A Arciello, DM Monti, A Relini, D Nichino, SM Doglia, A Natalello, P Pucci, P Mangione, L Obici, G Merlini, M Stoppini, P Robustelli, GG Tartaglia, M Vendruscolo, CM Dobson, R Piccoli, V Bellotti
– J Mol Biol
(2011)
407,
465
(doi: 10.1016/j.jmb.2011.01.044)
Protein dynamics: Moore's law in molecular biology
M Vendruscolo, CM Dobson
– Current Biology
(2011)
21,
r68
(doi: 10.1016/j.cub.2010.11.062)
Amyloid-like Aggregates Sequester Numerous Metastable Proteins with Essential Cellular Functions
H Olzscha, SM Schermann, AC Woerner, S Pinkert, MH Hecht, GG Tartaglia, M Vendruscolo, M Hayer-Hartl, FU Hartl, RM Vabulas
– Cell
(2011)
144,
67
(doi: 10.1016/j.cell.2010.11.050)
New scenarios of protein folding can occur on the ribosome
EP O'Brien, J Christodoulou, M Vendruscolo, CM Dobson
– Journal of the American Chemical Society
(2011)
133,
513
(doi: 10.1021/ja107863z)
On the Effect of the Ribosome and Trigger Factor on Nascent Chain Protein Folding
EP O'Brien, J Christodoulou, C Dobson, M Vendruscolo
– BIOPHYSICAL JOURNAL
(2011)
100,
17
(link to publication)
Focus on physical principles of protein behavior in the cell.
M Porto, HE Roman, M Vendruscolo
– Proteomics
(2010)
10,
4149
(doi: 10.1002/pmic.201090102)
Interactions in the native state of monellin , which play a protective role against aggregation
O Szczepankiewicz, C Cabaleiro-Lago, GG Tartaglia, M Vendruscolo, T Hunter, GJ Hunter, H Nilsson, E Thulin, S Linse
– Molecular BioSystems
(2010)
7,
521
(doi: 10.1039/c0mb00155d)
Structural characterization of a misfolded intermediate populated during the folding process of a PDZ domain.
S Gianni, Y Ivarsson, A De Simone, C Travaglini-Allocatelli, M Brunori, M Vendruscolo
– Nature Structural & Molecular Biology
(2010)
17,
1431
(doi: 10.1038/nsmb.1956)
  • <
  • 60 of 80
  • >

Research Groups

Research Interest Groups

Telephone number

01223 763873

Email address

mv245@cam.ac.uk

    Study at Cambridge

    About the University

    Research at Cambridge