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Professor Michele Vendruscolo

Portrait of mv245


The overall objective of our research is to understand the principles governing protein homeostasis – the ability of cells to generate and regulate the levels of proteins in terms of conformations, interactions, concentrations and cellular localisation. By adopting the strategy of analysing the origins of specific diseases to inform us about normal biology, we have set up an interdisciplinary programme that involves bringing together methods and concepts from chemistry, physics, engineering, genetics and medicine. We are using a combination of in vitro, in silico and in vivo approaches to study protein homeostasis through the analysis of the effects that result from its alteration in a select group of specific proteins, from either amino acid mutations, or changes in concentration and solubility, or the interactions with other molecules.

This programme is generating new insights into the mechanism through which physical and chemical sciences can address biological questions in order to understand the normal behaviour of living systems. In addition it is increasing our understanding of the nature and consequences of the failure to maintain homeostasis, which is associated with such phenomena as ageing and neurodegenerative disorders.


A conformational ensemble derived using NMR methyl chemical shifts reveals a mechanical clamping transition that gates the binding of the HU protein to dna
A Kannan, C Camilloni, AB Sahakyan, A Cavalli, M Vendruscolo – Journal of the American Chemical Society (2014) 136, 2204
Determination of the individual roles of the linker residues in the interdomain motions of calmodulin using NMR chemical shifts.
P Kukic, C Camilloni, A Cavalli, M Vendruscolo – Journal of Molecular Biology (2014) 426, 1826
New opportunities for tensor-free calculations of residual dipolar couplings for the study of protein dynamics
R Montalvao, C Camilloni, A De Simone, M Vendruscolo – Journal of Biomolecular NMR (2014) 58, 233
The dynamics of interleukin-8 and its interaction with human CXC receptor I peptide.
AA Kendrick, MJ Holliday, NG Isern, F Zhang, C Camilloni, C Huynh, M Vendruscolo, G Armstrong, EZ Eisenmesser – Protein Science (2014) 23, 464
A simple lattice model that captures protein folding, aggregation and amyloid formation.
S Abeln, M Vendruscolo, CM Dobson, D Frenkel – PLoS One (2014) 9, e85185
Kinetic modelling indicates that fast-translating codons can coordinate cotranslational protein folding by avoiding misfolded intermediates.
EP O'Brien, M Vendruscolo, CM Dobson – Nature Communications (2014) 5, 2988
Chemical kinetics for drug discovery to combat protein aggregation diseases
P Arosio, M Vendruscolo, CM Dobson, TPJ Knowles – Trends in Pharmacological Sciences (2014) 35, 127
Chemical kinetics for drug discovery to combat protein aggregation diseases.
P Arosio, M Vendruscolo, CM Dobson, TP Knowles – Trends Pharmacol Sci (2014) 35, 127
Targeting the Intrinsically Disordered Structural Ensemble of α-Synuclein by Small Molecules as a Potential Therapeutic Strategy for Parkinson's Disease.
G Tóth, SJ Gardai, W Zago, CW Bertoncini, N Cremades, SL Roy, MA Tambe, JC Rochet, C Galvagnion, G Skibinski, S Finkbeiner, M Bova, K Regnstrom, SS Chiou, J Johnston, K Callaway, JP Anderson, MF Jobling, AK Buell, TA Yednock, TP Knowles, M Vendruscolo, J Christodoulou, CM Dobson, D Schenk, L McConlogue – PLoS One (2014) 9, e87133
A Clear View of Polymorphism, Twist, and Chirality in Amyloid Fibril Formation
LR Volpatti, M Vendruscolo, CM Dobson, TP Knowles – ACS Nano (2013) 7, 10443
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01223 763873

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