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

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
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
(2019)
116
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
Intrinsically aggregation-prone proteins form amyloid-like aggregates and contribute to tissue aging in
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
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
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
Science advances
(2019)
5
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
ADSoluble aggregates present in cerebrospinal fluid change in size and mechanism of toxicity during Alzheimer’s disease progression
S De, DR Whiten, FS Ruggeri, C Hughes, M Rodrigues, DI Sideris, CG Taylor, FA Aprile, S Muyldermans, TPJ Knowles, M Vendruscolo, C Bryant, K Blennow, I Skoog, S Kern, H Zetterberg, D Klenerman
(2019)
Different soluble aggregates of Aβ42 can give rise to cellular toxicity through different mechanisms
S De, DC Wirthensohn, P Flagmeier, C Hughes, FA Aprile, FS Ruggeri, DR Whiten, D Emin, Z Xia, JA Varela, P Sormanni, F Kundel, TPJ Knowles, CM Dobson, C Bryant, M Vendruscolo, D Klenerman
Nat Commun
(2019)
10
The metastability of the proteome of spinal motor neurons underlies their selective vulnerability in ALS.
JJ Yerbury, L Ooi, IP Blair, P Ciryam, CM Dobson, M Vendruscolo
Neuroscience letters
(2019)
704

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Research Interest Groups

Telephone number

01223 763873

Email address