Publications
Lipid vesicles trigger α-synuclein aggregation by stimulating primary nucleation.
– Nature Chemical Biology
(2015)
11,
229
(doi: 10.1038/nchembio.1750)
Lipid vesicles trigger α-synuclein aggregation by stimulating primary nucleation
– Nature Chemical Biology
(2015)
11,
229
(doi: 10.1038/nchembio.1750)
Influence of the protein context on the polyglutamine length-dependent elongation of amyloid fibrils.
– Biochim Biophys Acta
(2014)
1854,
239
(doi: 10.1016/j.bbapap.2014.12.002)
Ostwald's rule of stages governs structural transitions and morphology of dipeptide supramolecular polymers
– Nature Communications
(2014)
5,
5219
(doi: 10.1038/ncomms6219)
The physical chemistry of the amyloid phenomenon: thermodynamics and kinetics of filamentous protein aggregation
– Essays Biochem
(2014)
56,
11
(doi: 10.1042/bse0560011)
Solution conditions determine the relative importance of nucleation and growth processes in α-synuclein aggregation.
– Proceedings of the National Academy of Sciences of the United States of America
(2014)
111,
7671
(doi: 10.1073/pnas.1315346111)
Spatial propagation of protein polymerization
– Physical Review Letters
(2014)
112,
098101
The Role of Stable α-Synuclein Oligomers in the Molecular Events Underlying Amyloid Formation
– Journal of the American Chemical Society
(2014)
136,
3859
(doi: 10.1021/ja411577t)
Targeting the intrinsically disordered structural ensemble of a-synuclein by small molecules as a potential therapeutic strategy for Parkinson's disease
– PloS one
(2014)
9,
e87133
(doi: 10.1371/journal.pone.0087133)
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