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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

Determination of protein structural ensembles using cryo-electron microscopy
M Bonomi, M Vendruscolo
– Curr Opin Struct Biol
(2019)
56,
37
(doi: 10.1016/j.sbi.2018.10.006)
Expression of the amyloid-β peptide in a single pair of C. elegans sensory neurons modulates the associated behavioural response
T Sinnige, P Ciryam, S Casford, CM Dobson, M de Bono, M Vendruscolo
– PLoS ONE
(2019)
14,
e0217746
(doi: 10.1371/journal.pone.0217746)
Common Regulatory Pathways Mediate Activity of MicroRNAs Inducing Cardiomyocyte Proliferation
C Torrini, RJ Cubero, E Dirkx, L Braga, H Ali, G Prosdocimo, MI Gutierrez, C Collesi, D Licastro, L Zentilin, M Mano, S Zacchigna, M Vendruscolo, M Marsili, A Samal, M Giacca
– Cell Reports
(2019)
27,
2759
(doi: 10.1016/j.celrep.2019.05.005)
Probing the Origin of the Toxicity of Oligomeric Aggregates of α‑Synuclein with Antibodies
R Cascella, M Perni, SW Chen, G Fusco, C Cecchi, M Vendruscolo, F Chiti, CM Dobson, A De Simone
– ACS Chemical Biology
(2019)
14,
1352
(doi: 10.1021/acschembio.9b00312)
Effects of α-tubulin acetylation on microtubule structure and stability
L Eshun-Wilson, R Zhang, D Portran, MV Nachury, DB Toso, T Löhr, M Vendruscolo, M Bonomi, JS Fraser, E Nogales
– Proceedings of the National Academy of Sciences of the United States of America
(2019)
116,
10366
(doi: 10.1073/pnas.1900441116)
Intrinsically aggregation-prone proteins form amyloid-like aggregates and contribute to tissue aging in <i>Caenorhabditis elegans</i>.
C Huang, S Wagner-Valladolid, AD Stephens, R Jung, C Poudel, T Sinnige, MC Lechler, N Schlörit, M Lu, RF Laine, CH Michel, M Vendruscolo, CF Kaminski, GS Kaminski Schierle, DC David
– eLife
(2019)
8,
e43059
(doi: 10.7554/elife.43059)
Identifying A- and P-site locations on ribosome-protected mRNA fragments using Integer Programming.
N Ahmed, P Sormanni, P Ciryam, M Vendruscolo, CM Dobson, EP O'Brien
– Scientific reports
(2019)
9,
6256
(doi: 10.1038/s41598-019-42348-x)
Secondary nucleation and elongation occur at different sites on Alzheimer's amyloid-β aggregates.
T Scheidt, U Łapińska, JR Kumita, DR Whiten, D Klenerman, MR Wilson, SIA Cohen, S Linse, M Vendruscolo, CM Dobson, TPJ Knowles, P Arosio
– Sci Adv
(2019)
5,
eaau3112
(doi: 10.1126/sciadv.aau3112)
The free energy landscape of the oncogene protein E7 of human papillomavirus type 16 reveals a complex interplay between ordered and disordered regions
P Kukic, GM Lo Piccolo, MO Nogueira, DI Svergun, M Vendruscolo, IC Felli, R Pierattelli
– Scientific Reports
(2019)
9,
5822
(doi: 10.1038/s41598-019-41925-4)
ADSoluble aggregates present in cerebrospinal fluid change in size and mechanism of toxicity during Alzheimer’s disease progression
S De, D Whiten, F Ruggeri, C Hughes, M Rodrigues, D Sideris, C Taylor, F Aprile, S Muyldermans, T Knowles, M Vendruscolo, C Bryant, K Blennow, I Skoog, S Kern, H Zetterberg, D Klenerman
(2019)
600346
(doi: 10.1101/600346)
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Research Groups

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Telephone number

01223 763873

Email address

mv245@cam.ac.uk

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