α-Synuclein strains cause distinct synucleinopathies after local and systemic administration

By W. Peelaerts, Luc Bousset, A. Perren, A. Moskalyuk, Rocco Pulizzi, M. Giugliano, C. V. Haute, R. Melki, V. Baekelandt. Nature, 2015

1,057 citations recorded by the source corpus.

Subfields: Neurology

View Paper: https://www.semanticscholar.org/paper/219f1fa22784159f0b99faa87673b3259f501300

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In Neurology

1. Fabrizio Chiti
2. M. Hasegawa
3. Christopher M. Dobson
4. M. Goedert

Citations in the corpus

• Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade. (2017, background): “A similar pattern of behavior has been observed for many other systems, such as two types of insulin fibrils (118) and αs fibrillar assemblies (119).”
• Structures of α-Synuclein Filaments from Multiple System Atrophy (2020, background): “Assemblies of recombinant α-synuclein with different morphologies displayed distinct seeding capacities (49).”