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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 Aβ42 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
– Curr Opin Struct Biol
(2018)
56,
37
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
– Sci Rep
(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
– Nature communications
(2019)
10,
1541
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,
89
The Amyloid Phenomenon and Its Significance in Biology and Medicine.
CM Dobson, TPJ Knowles, M Vendruscolo
– Cold Spring Harbor Perspectives in Biology
(2019)
a033878
A method of predicting the in vitro fibril formation propensity of Aβ40 mutants based on their inclusion body levels in E. coli.
K Sanagavarapu, E Nüske, I Nasir, G Meisl, JN Immink, P Sormanni, M Vendruscolo, TPJ Knowles, A Malmendal, C Cabaleiro-Lago, S Linse
– Scientific reports
(2019)
9,
3680
Protein Solubility Predictions Using the CamSol Method in the Study of Protein Homeostasis
P Sormanni, M Vendruscolo
– Cold Spring Harbor perspectives in biology
(2019)
a033845
Structure and Dynamics of Alzheimer's Associated Amyloid-Beta Peptide
T Lohr, K Kohlhoff, G Heller, M Vendruscolo
– Biophysical Journal
(2019)
116,
437a
Targeting the Formation of Amyloid Oligomers using Rationally Designed Antibodies
FA Aprile, P Sormanni, M Perni, P Arosio, S Linse, TP Knowles, CM Dobson, M Vendruscolo
– Biophysical Journal
(2019)
116,
28a
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Research Interest Groups

Telephone number

01223 763873

Email address

mv245@cam.ac.uk