skip to content

Department of Chemistry

 
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

Trodusquemine enhances A beta(42) aggregation but suppresses its toxicity by displacing oligomers from cell membranes
R Limbocker, S Chia, FS Ruggeri, M Perni, R Cascella, GT Heller, G Meisl, B Mannini, J Habchi, TCT Michaels, PK Challa, M Ahn, ST Casford, N Fernando, CK Xu, ND Kloss, SIA Cohen, JR Kumita, C Cecchi, M Zasloff, S Linse, TPJ Knowles, F Chiti, M Vendruscolo, CM Dobson
– Nature Communications
(2019)
10,
225
Determination of protein structural ensembles using cryo-electron microscopy
M Bonomi, M Vendruscolo
– Current opinion in structural biology
(2018)
56,
37
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
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 Rep
(2019)
27,
2759
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,
10366
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 Chem Biol
(2019)
14,
1352
Intrinsically aggregation-prone proteins form amyloid-like aggregates and contribute to tissue aging in Caenorhabditis elegans.
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,
ARTN e43059
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
– Sci Rep
(2019)
9,
6256
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
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,
1541
  • 1 of 53
  • >

Research Interest Groups

Telephone number

01223 763873

Email address

mv245@cam.ac.uk