Comparison of the 3D structures of mouse and human α-synuclein fibrils by solid-state NMR and STEM.

doi:10.1016/j.jsb.2018.04.003

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Article

Comparison of the 3D structures of mouse and human α-synuclein fibrils by solid-state NMR and STEM.

Journal of structural biology - 1 Apr 2019

Hwang Songhwan, Fricke Pascal, Zinke Maximilian, Giller Karin, Wall Joseph S, Riedel Dietmar, Becker Stefan, Lange Adam

Abstract excerpt

Intra-neuronal aggregation of α-synuclein into fibrils is the molecular basis for α-synucleinopathies, such as Parkinson's disease. The atomic structure of human α-synuclein (hAS) fibrils was recently determined by Tuttle et al. using solid-state NMR (ssNMR). The previous study found that hAS fibrils are composed of a single protofilament. Here, we have investigated the structure of mouse α-synuclein (mAS)...

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Identifiers

PMID: 29678776
DOI: 10.1016/j.jsb.2018.04.003
PMCID: PMC6470123

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.