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.
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
(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
Nat Commun
(2014)
5
5219
(doi: 10.1038/ncomms6219)
The physical chemistry of the amyloid phenomenon: Thermodynamics and kinetics of fi lamentous protein aggregation
Essays in Biochemistry
(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
J Am Chem Soc
(2014)
136
3859
(doi: 10.1021/ja411577t)
Targeting the Intrinsically Disordered Structural Ensemble of α-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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