@article{rey_-synuclein_2019,
	title = {α-{Synuclein} conformational strains spread, seed and target neuronal cells differentially after injection into the olfactory bulb},
	volume = {7},
	issn = {2051-5960},
	url = {https://doi.org/10.1186/s40478-019-0859-3},
	doi = {10.1186/s40478-019-0859-3},
	abstract = {Alpha-synuclein inclusions, the hallmarks of synucleinopathies, are suggested to spread along neuronal connections in a stereotypical pattern in the brains of patients. Ample evidence now supports that pathological forms of alpha-synuclein propagate in cell culture models and in vivo in a prion-like manner. However, it is still not known why the same pathological protein targets different cell populations, propagates with different kinetics and leads to a variety of diseases (synucleinopathies) with distinct clinical features. The aggregation of the protein alpha-synuclein yields different conformational polymorphs called strains. These strains exhibit distinct biochemical, physical and structural features they are able to imprint to newly recruited alpha-synuclein. This had led to the view that the clinical heterogeneity observed in synucleinopathies might be due to distinct pathological alpha-synuclein strains.},
	number = {1},
	urldate = {2020-01-14},
	journal = {Acta Neuropathologica Communications},
	author = {Rey, Nolwen L. and Bousset, Luc and George, Sonia and Madaj, Zachary and Meyerdirk, Lindsay and Schulz, Emily and Steiner, Jennifer A. and Melki, Ronald and Brundin, Patrik},
	month = dec,
	year = {2019},
	keywords = {peer-reviewed},
	pages = {221},
}