Back to search

Article

Cryo-EM structures of filaments from the brains of individuals with variants G51D and H50Q in α-synuclein

2025-05-09

Abstract excerpt

<title>Abstract</title> <p>Gene dosage and point mutations in <italic>SNCA</italic>, the a-synuclein gene, give rise to familial forms of Parkinson’s disease and dementia with Lewy bodies; an insertion mutation in <italic>SNCA</italic> causes juvenile-onset synucleinopathy. We previously reported the electron cryo-microscopy (cryo-EM) structures of a-synuclein filaments from the brains of individuals with Parkins...

Topics

Open a Topic to create a Post that cites this publication.

Identifiers and source

Literature Corpus work
6287ed1b-460b-5bc6-9018-8d5c21024acc
DOI
10.21203/rs.3.rs-6490169/v1
Open publication

Related research

Semantic proximity does not establish scientific evidence.

Click a neighbor to travelStep 1 · 12 closest
Interactive article relationship graphSelect a related publication card to move it into the centre and load its closest explainable connections. Solid lines are source-backed structured connections. Dashed lines are semantic discovery signals and are not scientific evidence.
Cryo-EM structures of filaments from the brains of individuals with variants G51D and H50Q in α-synucleinDOI 10.21203/rs.3.rs-6490169/v1
New insights on the structure of alpha-synuclein fibrils using cryo-electron microscopy.Semantic proximity
Cryo-EM structure of amyloid fibril formed by α-synuclein hereditary A53E mutationSemantic proximity
Cryo-EM structure of amyloid fibril formed by α-synuclein hereditary A53E mutation reveals a distinct protofilament interface.Semantic proximity
Cryo-EM structure of alpha-synuclein fibrils.Semantic proximity
Two new polymorphic structures of alpha-synuclein solved by cryo-electron microscopySemantic proximity
Cryo-EM structure of full-length α-synuclein amyloid fibril with Parkinson’s disease familial A53T mutationSemantic proximity
Cryo-EM structure of alpha-synuclein fibrils amplified by PMCA from PD and MSA patient brainsSemantic proximity
Cryo-EM structures of α-synuclein fibrils with the H50Q hereditary mutation reveal new polymorphsSemantic proximity
Lewy-MSA hybrid fold drives distinct neuronal α-synuclein pathologySemantic proximity
High-Resolution Cryo-EM Structure Determination of α-Synuclein – A Prototypical Amyloid FibrilSemantic proximity
Two new polymorphic structures of human full-length alpha-synuclein fibrils solved by cryo-electron microscopy.Semantic proximity
Dimerisation and twist reversal of the Lewy fold in α-synuclein mutants with Parkinson’s disease and dementiaSemantic proximity
Select a neighboring publication to make it the new centre.