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Centre for Misfolding Diseases

Dr Celine Galvagnion

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

Mutations associated with familial Parkinson’s disease alter the initiation and amplification steps of α-synuclein aggregation
P Flagmeier, G Meisl, M Vendruscolo, TPJ Knowles, CM Dobson, AK Buell, C Galvagnion
– Proceedings of the National Academy of Sciences of the United States of America
(2016)
113,
10328
(doi: 10.1073/pnas.1604645113)
Discovery of a small-molecule binder of the oncoprotein gankyrin that modulates gankyrin activity in the cell.
A Chattopadhyay, CJ O'Connor, F Zhang, C Galvagnion, WRJD Galloway, YS Tan, JE Stokes, T Rahman, C Verma, DR Spring, LS Itzhaki
– Sci Rep
(2016)
6,
23732
(doi: 10.1038/srep23732)
The inverted free energy landscape of an intrinsically disordered peptide by simulations and experiments
D Granata, F Baftizadeh, J Habchi, C Galvagnion, A De Simone, C Camilloni, A Laio, M Vendruscolo
– Scientific Reports
(2015)
5,
15449
(doi: 10.1038/srep15449)
Fundamental mechanisms of amyloid fibril formation by alpha-synuclein in Parkinson's disease: Quantitative modelling
C Galvagnion, AK Buell
– Med Sci (Paris)
(2015)
31,
597
(doi: 10.1051/medsci/20153106008)
Lipid vesicles trigger α-synuclein aggregation by stimulating primary nucleation.
C Galvagnion, AK Buell, G Meisl, TCT Michaels, M Vendruscolo, TPJ Knowles, CM Dobson
– Nat Chem Biol
(2015)
11,
229
(doi: 10.1038/nchembio.1750)
Lipid vesicles trigger α-synuclein aggregation by stimulating primary nucleation
C Galvagnion, AK Buell, G Meisl, TCT Michaels, M Vendruscolo, TPJ Knowles, CM Dobson
– Nature Chemical Biology
(2015)
11,
229
(doi: 10.1038/nchembio.1750)
Ostwald's rule of stages governs structural transitions and morphology of dipeptide supramolecular polymers
A Levin, TO Mason, L Adler-Abramovich, AK Buell, G Meisl, C Galvagnion, Y Bram, SA Stratford, CM Dobson, TPJ Knowles, E Gazit
– Nature communications
(2014)
5,
5219
(doi: 10.1038/ncomms6219)
Solution conditions determine the relative importance of nucleation and growth processes in α-synuclein aggregation.
AK Buell, C Galvagnion, R Gaspar, E Sparr, M Vendruscolo, TPJ Knowles, S Linse, CM Dobson
– Proceedings of the National Academy of Sciences of the United States of America
(2014)
111,
7671
(doi: 10.1073/pnas.1315346111)
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, J-C Rochet, C Galvagnion, G Skibinski, S Finkbeiner, M Bova, K Regnstrom, S-S Chiou, J Johnston, K Callaway, JP Anderson, MF Jobling, AK Buell, TA Yednock, TPJ Knowles, M Vendruscolo, J Christodoulou, CM Dobson, D Schenk, L McConlogue
– PLoS One
(2014)
9,
e87133
(doi: 10.1371/journal.pone.0087133)
Direct observation of heterogeneous amyloid fibril growth kinetics via two-color super-resolution microscopy.
D Pinotsi, AK Buell, C Galvagnion, CM Dobson, GS Kaminski Schierle, CF Kaminski
– Nano letters
(2013)
14,
339
(doi: 10.1021/nl4041093)
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