skip to content

Yusuf Hamied Department of Chemistry

 

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

Identifying A- and P-site locations on ribosome-protected mRNA fragments using Integer Programming
N Ahmed, P Sormanni, P Ciryam, M Vendruscolo, C Dobson, E O’Brien
(2018)
490755
Determination of Structural Ensembles of Proteins: Restraining vs Reweighting
R Rangan, M Bonomi, GT Heller, A Cesari, G Bussi, M Vendruscolo
– J Chem Theory Comput
(2018)
14,
6632
Bayesian Weighing of Electron Cryo-Microscopy Data for Integrative Structural Modeling.
M Bonomi, S Hanot, CH Greenberg, A Sali, M Nilges, M Vendruscolo, R Pellarin
– Structure (London, England : 1993)
(2018)
27,
175
Automated Behavioral Analysis of Large C. Elegans Populations Using a Wide Field-of-view Tracking Platform
M Perni, S Casford, FA Aprile, EA Nollen, TPJ Knowles, M Vendruscolo, CM Dobson
– Journal of visualized experiments : JoVE
(2018)
2018,
ARTN e58643
(doi: 10.3791/58643)
INFLAMMATORY MYOPATHIES P.160A bioinformatics approach to define the aggregation capacity of the myofiber proteome in inclusion body myositis
C Weihl, P Ciryam, A Guttsches, K Marcus, R Morimoto, M Vendruscolo, R Kley
– Neuromuscular Disorders
(2018)
28,
S77
SAR by kinetics for drug discovery in protein misfolding diseases.
S Chia, J Habchi, TCT Michaels, SIA Cohen, S Linse, CM Dobson, TPJ Knowles, M Vendruscolo
– Proceedings of the National Academy of Sciences of the United States of America
(2018)
115,
10245
Microfluidic deposition for resolving single-molecule protein architecture and heterogeneity
FS Ruggeri, J Charmet, T Kartanas, Q Peter, S Chia, J Habchi, CM Dobson, M Vendruscolo, TPJ Knowles
– Nature communications
(2018)
9,
3890
Determination of the conformational states of strychnine in solution using NMR residual dipolar couplings in a tensor-free approach.
G Tomba, C Camilloni, M Vendruscolo
– Methods (San Diego, Calif.)
(2018)
148,
4
Intrinsically aggregation-prone proteins form amyloid-like aggregates and contribute to tissue aging in C. elegans
C Huang, S Wagner-Valladolid, AD Stephens, R Jung, C Poudel, T Sinnige, MC Lechler, N Schlörit, RF Laine, CH Michel, M Vendruscolo, CF Kaminski, CF Kaminski, GS Kaminski Schierle, DC David
(2018)
Fast fluorescence lifetime imaging reveals the aggregation processes of α-synuclein and polyglutamine in aging Caenorhabditis elegans
R Laine, T Sinnige, KY Ma, A Haack, C Poudel, P Gaida, N Curry, M Perni, EAA Nollen, C Dobson, M Vendruscolo, G Kaminski Schierle, C Kaminski, C Kaminski
(2018)
  • <
  • 31 of 80
  • >

Research Interest Groups

Telephone number

01223 763873

Email address

mv245@cam.ac.uk