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@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}, }