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Centre for Misfolding Diseases

My main research interests focus on understanding the early onset and proliferation of Parkinson’s disease.

In fact, alpha synuclein (a-syn) is a small presynaptic protein involved in neuronal and synaptic vesicle plasticity but its aggregation to form amyloid fibrils is the hallmark of Parkinson’s disease. My current research focuses on establishing the molecular mechanism by which the interaction between a-syn and vesicles trigger amyloid formation by the former. In addition, I am particularly interested in understanding how a change in bilayer properties would affect the behavior of the protein at the membrane interface. Such an understanding would allow us to shed light on the mechanism by which the balance between functional interactions of a-syn with lipid membranes and deleterious ones that can generate pathogenicity, can be affected in vivo.

Publications

α-Synuclein Senses Lipid Packing Defects and Induces Lateral Expansion of Lipids Leading to Membrane Remodeling
MM Ouberai, J Wang, MJ Swann, C Galvagnion, T Guilliams, CM Dobson, ME Welland
– The Journal of biological chemistry
(2013)
288,
20883
Production and initial structural characterization of the TM4TM5 helix-loop-helix domain of the translocator protein
C Galvagnion, P Montaville, Y-M Coïc, N Jamin
– Journal of peptide science : an official publication of the European Peptide Society
(2013)
19,
102
NMR structural studies of a double transmembrane domain of the translocator protein
C Galvagnion, P Montaville, YM Coic, N Jamin
– FEBS JOURNAL
(2011)
278,
455
Folding and association of thermophilic dimeric and trimeric DsrEFH proteins: Tm0979 and Mth1491.
C Galvagnion, MTJ Smith, A Broom, KA Vassall, G Meglei, JA Gaspar, PB Stathopulos, B Cheyne, EM Meiering
– Biochemistry
(2009)
48,
2891
Conformational stability and folding mechanisms of dimeric proteins.
JAO Rumfeldt, C Galvagnion, KA Vassall, EM Meiering
– Progress in biophysics and molecular biology
(2008)
98,
61
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Postdoctoral researcher

Telephone number

01223 761083