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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

Fibrillogenic propensity of the GroEL apical domain: A Janus-faced minichaperone
J Chen, H Yagi, P Sormanni, M Vendruscolo, K Makabe, T Nakamura, Y Goto, K Kuwajima
– FEBS Letters
(2012)
586,
1120
(doi: 10.1016/j.febslet.2012.03.019)
Structure of an Intermediate State in Protein Folding and Aggregation
P Neudecker, P Robustelli, A Cavalli, P Walsh, P Lundström, A Zarrine-Afsar, S Sharpe, M Vendruscolo, LE Kay
– Science (New York, N.Y.)
(2012)
336,
362
(doi: 10.1126/science.1214203)
Proteome folding and aggregation
M Vendruscolo
– Current Opinion in Structural Biology
(2012)
22,
138
(doi: 10.1016/j.sbi.2012.01.005)
1H, 13C and 15N resonance assignments of human muscle acylphosphatase
G Fusco, A De Simone, STD Hsu, F Bemporad, M Vendruscolo, F Chiti, CM Dobson
– Biomolecular NMR Assignments
(2012)
6,
27
(doi: 10.1007/s12104-011-9318-1)
Fibrillogenic propensity of the GroEL apical domain: A Janus‐faced minichaperone
J Chen, H Yagi, P Sormanni, M Vendruscolo, K Makabe, T Nakamura, Y Goto, K Kuwajima
– FEBS Lett
(2012)
586,
1120
(doi: 10.1016/j.febslet.2012.03.019)
From Macroscopic Measurements to Microscopic Mechanisms of Protein Aggregation
SIA Cohen, M Vendruscolo, CM Dobson, TPJ Knowles
– Journal of Molecular Biology
(2012)
421,
160
(doi: 10.1016/j.jmb.2012.02.031)
Determination of secondary structure populations in disordered states of proteins using nuclear magnetic resonance chemical shifts.
C Camilloni, A De Simone, WF Vranken, M Vendruscolo
– Biochemistry
(2012)
51,
2224
(doi: 10.1021/bi3001825)
Characterization of the conformational equilibrium between the two major substates of RNase a using NMR chemical shifts
C Camilloni, P Robustelli, A De Simone, A Cavalli, M Vendruscolo
– J Am Chem Soc
(2012)
134,
3968
(doi: 10.1021/ja210951z)
Blind testing of routine, fully automated determination of protein structures from nmr data
A Rosato, JM Aramini, C Arrowsmith, A Bagaria, D Baker, A Cavalli, JF Doreleijers, A Eletsky, A Giachetti, P Guerry, A Gutmanas, P Güntert, Y He, T Herrmann, YJ Huang, V Jaravine, HRA Jonker, MA Kennedy, OF Lange, G Liu, TE Malliavin, R Mani, B Mao, GT Montelione, M Nilges, P Rossi, G Van Der Schot, H Schwalbe, TA Szyperski, M Vendruscolo, R Vernon, WF Vranken, S De Vries, GW Vuister, B Wu, Y Yang, AMJJ Bonvin
– Structure
(2012)
20,
227
(doi: 10.1016/j.str.2012.01.002)
Blind testing of routine, fully automated determination of protein structures from NMR data.
A Rosato, JM Aramini, C Arrowsmith, A Bagaria, D Baker, A Cavalli, JF Doreleijers, A Eletsky, A Giachetti, P Guerry, A Gutmanas, P Güntert, Y He, T Herrmann, YJ Huang, V Jaravine, HRA Jonker, MA Kennedy, OF Lange, G Liu, TE Malliavin, R Mani, B Mao, GT Montelione, M Nilges, P Rossi, G van der Schot, H Schwalbe, TA Szyperski, M Vendruscolo, R Vernon, WF Vranken, SD Vries, GW Vuister, B Wu, Y Yang, AMJJ Bonvin
– Structure (London, England : 1993)
(2012)
20,
227
(doi: 10.1016/j.str.2012.01.002)
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Telephone number

01223 763873

Email address

mv245@cam.ac.uk

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