Seeded assembly in vitro does not replicate the structures of α‐synuclein filaments from multiple system atrophy

Discriminating α-synuclein strains in Parkinson’s disease and multiple system atrophy

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The α-synuclein hereditary mutation E46K unlocks a more stable, pathogenic fibril structure

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Amyloid structure determination in RELION-3.1

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New insights on the structure of alpha-synuclein fibrils using cryo-electron microscopy

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α-Synuclein filaments from transgenic mouse and human synucleinopathy-containing brains are major seed-competent species

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Structures of α-synuclein filaments from multiple system atrophy

(2020) Manuel Schweighauser et al.   NATURE

Parkinson’s disease-related phosphorylation at Tyr39 rearranges α-synuclein amyloid fibril structure revealed by cryo-EM

(2020) Kun Zhao et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Cryo-EM structures of tau filaments

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Novel tau filament fold in chronic traumatic encephalopathy encloses hydrophobic molecules

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Heparin-induced tau filaments are polymorphic and differ from those in Alzheimer’s and Pick’s diseases

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Silver staining (Campbell-Switzer) of neuronal α-synuclein assemblies induced by multiple system atrophy and Parkinson’s disease brain extracts in transgenic mice

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Structural heterogeneity of α-synuclein fibrils amplified from patient brain extracts

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

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Cellular milieu imparts distinct pathological α-synuclein strains in α-synucleinopathies

(2018) Chao Peng et al.   NATURE

Cryo-EM structure of alpha-synuclein fibrils

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ISOLDE: a physically realistic environment for model building into low-resolution electron-density maps

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Potent prion-like behaviors of pathogenic α-synuclein and evaluation of inactivation methods

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New tools for automated high-resolution cryo-EM structure determination in RELION-3

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Helical reconstruction in RELION

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Cryo-EM structures of tau filaments from Alzheimer’s disease

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Familial Parkinson’s point mutation abolishes multiple system atrophy prion replication

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Thioflavin T as an amyloid dye: fibril quantification, optimal concentration and effect on aggregation

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The Effect of Fragmented Pathogenic α-Synuclein Seeds on Prion-like Propagation

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Solid-state NMR structure of a pathogenic fibril of full-length human α-synuclein

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Reducing C-terminal truncation mitigates synucleinopathy and neurodegeneration in a transgenic model of multiple system atrophy

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Chemical properties of lipids strongly affect the kinetics of the membrane-induced aggregation of α-synuclein

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Solid-state NMR structure of a pathogenic fibril of full-length human α-synuclein

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CTFFIND4: Fast and accurate defocus estimation from electron micrographs

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Structure of the toxic core of α-synuclein from invisible crystals

(2015) Jose A. Rodriguez et al.   NATURE

Propagation of prions causing synucleinopathies in cultured cells

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Alzheimer's and Parkinson's diseases: The prion concept in relation to assembled A , tau, and  -synuclein

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Large-scale meta-analysis of genome-wide association data identifies six new risk loci for Parkinson's disease

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Solution conditions determine the relative importance of nucleation and growth processes in  -synuclein aggregation

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Transmission of multiple system atrophy prions to transgenic mice

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Darwinian Evolution of Prions in Cell Culture

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The propagation of prion-like protein inclusions in neurodegenerative diseases

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MolProbity: all-atom structure validation for macromolecular crystallography

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Exogenous  -synuclein fibrils seed the formation of Lewy body-like intracellular inclusions in cultured cells

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Lewy bodies in grafted neurons in subjects with Parkinson's disease suggest host-to-graft disease propagation

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Lewy body–like pathology in long-term embryonic nigral transplants in Parkinson's disease

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The fold of  -synuclein fibrils

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