Cited by 825Parkinson's Disease Mechanisms and TreatmentsNuclear Receptors and SignalingNeuroinflammation and Neurodegeneration Mechanisms

The function of α-synuclein

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Bendor, Jacob T., Logan, Todd P., Edwards, Robert H.·2013·Neuron

Abstract

Human genetics has indicated a causal role for the protein α-synuclein in the pathogenesis of familial Parkinson's disease (PD), and the aggregation of synuclein in essentially all patients with PD suggests a central role for this protein in the sporadic disorder. Indeed, the accumulation of misfolded α-synuclein now defines multiple forms of neural degeneration. Like many of the proteins that accumulate in other neurodegenerative disorders, however, the normal function of synuclein remains poorly understood. In this article, we review the role of synuclein at the nerve terminal and in membrane remodeling. We also consider the prion-like propagation of misfolded synuclein as a mechanism for the spread of degeneration through the neuraxis.

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Crossref · 10.1016/j.neuron.2013.09.004

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  • α-synuclein is derived from 140 amino acids and is made of three main groups: a highly conserved N-terminal, a hydrophobic non-amyloid β compound, and an unstructured C-terminus.

    “Derived from 140 amino acids, α-syn is made of three main groups: a highly conserved N-terminal, a hydrophobic non-amyloid β compound, and an unstructured C-terminus [129].”

    From The Impact of Neurotoxin Proteins Trafficked by Primary Cilia and Extracellular Vesicles in Neurodegenerative Diseases (2025) · cites this paper as [129]

    The Abstract identifies α-synuclein as a 140-amino-acid protein, and “The Structure of Synuclein” describes its highly conserved N-terminal repeats and a distinct, polar C-terminus. Our copy does not describe a hydrophobic non-amyloid β component as one of three main regions, or characterize the C-terminus specifically as unstructured. (LLM, conf=0.86)

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Authors
Bendor, J. T., Logan, T. P., & Edwards, R. H.
Affiliations
University of California, San Francisco (US)
Corresponding author
Edwards, Robert H.
Venue
Neuron
Publisher
Elsevier BV
Published
2013-09
Volume
79
Issue
6
Pages
1044-1066
ISSN
0896-6273 (ISSN-L)
OpenAlex
W2087482196
Cited by
825
References
318
Citations by year
2026: 36 · 2025: 57 · 2024: 88 · 2023: 61 · 2022: 105 · 2021: 77 · 2020: 85 · 2019: 58 · 2018: 70 · 2017: 61 · 2016: 48 · 2015: 47 · 2014: 28 · 2013: 4
FWCI
26.87
Type
journal article
Language
en
Open access
Locations
  • Neuron (publishedVersion)
  • PubMed (publishedVersion)
  • Europe PMC (PubMed Central) (acceptedVersion)
  • PubMed Central (acceptedVersion)
  • eScholarship (California Digital Library) (submittedVersion)
Funders
National Institute of Neurological Disorders and Stroke (NS062715, R01NS062715)
Topics
  • Health Sciences › Medicine › Neurology › Parkinson's Disease Mechanisms and Treatments
  • Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Nuclear Receptors and Signaling
  • Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
Keywords
alpha-synuclein, Parkinson's disease, protein aggregation, synucleinopathies, membrane remodeling, prion-like propagation, neurodegeneration, familial Parkinson's disease, sporadic Parkinson's disease
MeSH terms
Animals, Humans, Parkinson Disease, Prions, Neurodegenerative Diseases, alpha-Synuclein

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