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Article

Two new polymorphic structures of human full-length alpha-synuclein fibrils solved by cryo-electron microscopy.

eLife - 9 Dec 2019

Guerrero-Ferreira Ricardo, Taylor Nicholas Mi, Arteni Ana-Andreea, Kumari Pratibha, Mona Daniel, Ringler Philippe, Britschgi Markus, Lauer Matthias E, Makky Ali, Verasdonck Joeri, Riek Roland, Melki Ronald, Meier Beat H, Böckmann Anja, Bousset Luc, Stahlberg Henning

Abstract excerpt

Intracellular inclusions rich in alpha-synuclein are a hallmark of several neuropathological diseases including Parkinson's disease (PD). Previously, we reported the structure of alpha-synuclein fibrils (residues 1-121), composed of two protofibrils that are connected via a densely-packed interface formed by residues 50-57 (Guerrero-Ferreira, eLife 218;7:e36402). We here report two new polymorphic atomic...

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Identifiers

PMID: 31815671
DOI: 10.7554/eLife.48907
PMCID: PMC6957273

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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