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Professor Michele Vendruscolo

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

Phage display and kinetic selection of antibodies that specifically inhibit amyloid self-replication.
A Munke, J Persson, T Weiffert, E De Genst, G Meisl, P Arosio, A Carnerup, CM Dobson, M Vendruscolo, TPJ Knowles, S Linse
– Proceedings of the National Academy of Sciences of the United States of America
(2017)
Structural basis of synaptic vesicle assembly promoted by alpha-synuclein (vol 7, 12563, 2016)
G Fusco, T Pape, AD Stephens, P Mahou, AR Costa, CF Kaminski, GSK Schierle, M Vendruscolo, G Veglia, CM Dobson, A De Simone
– Nature Communications
(2017)
8,
15667
Amyloid-like Fibrils from an α-Helical Transmembrane Protein.
K Stroobants, JR Kumita, NJ Harris, DY Chirgadze, CM Dobson, PJ Booth, M Vendruscolo
– Biochemistry
(2017)
The rnf168 paralog rnf169 defines a new class of ubiquitylated histone reader involved in the response to dna damage
J Kitevski-LeBlanc, A Fradet-Turcotte, P Kukic, MD Wilson, G Portella, T Yuwen, S Panier, S Duan, MD Canny, H van Ingen, CH Arrowsmith, JL Rubinstein, M Vendruscolo, D Durocher, LE Kay
– eLife
(2017)
6,
ARTN e23872
Structural Characterization of the Early Events in the Nucleation-Condensation Mechanism in a Protein Folding Process
P Kukic, Y Pustovalova, C Camilloni, S Gianni, DM Korzhnev, M Vendruscolo
– Journal of the American Chemical Society
(2017)
139,
6899
Emergence and evolution of an interaction between intrinsically disordered proteins
G Hultqvist, E Åberg, C Camilloni, GN Sundell, E Andersson, J Dogan, CN Chi, M Vendruscolo, P Jemth
– eLife
(2017)
6,
ARTN e16059
Spinal motor neuron protein supersaturation patterns are associated with inclusion body formation in ALS
P Ciryam, IA Lambert-Smith, DM Bean, R Freer, F Cid, GG Tartaglia, DN Saunders, MR Wilson, SG Oliver, RI Morimoto, CM Dobson, M Vendruscolo, G Favrin, JJ Yerbury
– Proceedings of the National Academy of Sciences of the United States of America
(2017)
114,
E3935
MOAG-4 Promotes the Aggregation of α-Synuclein by Competing with Self-Protective Electrostatic Interactions
Y Yoshimura, MA Holmberg, P Kukic, CB Andersen, A Mata-Cabana, SF Falsone, M Vendruscolo, EAA Nollen, FAA Mulder
– J Biol Chem
(2017)
292,
8269
Simultaneous quantification of protein order and disorder.
P Sormanni, D Piovesan, GT Heller, M Bonomi, P Kukic, C Camilloni, M Fuxreiter, Z Dosztanyi, RV Pappu, MM Babu, S Longhi, P Tompa, AK Dunker, VN Uversky, SCE Tosatto, M Vendruscolo
– Nature Chemical Biology
(2017)
13,
339
A natural product inhibits the initiation of alpha-synuclein aggregation and suppresses its toxicity (vol 114, pg E1009, 2017)
M Perni, C Galvagnion, A Maltsev, G Meisl, MBD Mueller, PK Challa, JB Kirkegaard, P Flagmeier, SIA Cohen, R Cascella, SW Chen, R Limboker, P Sormanni, GT Heller, FA Aprile, N Cremades, C Cecchi, F Chiti, EAA Nollen, TPJ Knowles, M Vendruscolo, A Bax, M Zasloff, CM Dobson
– Proceedings of the National Academy of Sciences
(2017)
114,
E2543
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Research Interest Groups

Telephone number

01223 763873

Email address

mv245@cam.ac.uk