Evidence map›Paper›PMID 25548530›Full record

ReviewExperimental neurobiology2014

Alpha-synuclein function and dysfunction on cellular membranes.

David Snead, David Eliezer

Open access · bronzeAbstract readReview
In one paragraph

Review in Experimental neurobiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 129 papers.

0numbers the graph read from it
0cells of the map it votes in
129citing papers in PubMed
12.8field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

129 citing papers in PubMed, 222 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Review
  6. Review
  7. Lipid-packing defects are sufficient to modulate membrane insertion and the bound state of α-synuclein.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  8. Article
  9. Review
  10. Parkinson disease is a fatty acidopathy.Nature reviews. Neurology · 2025
    Review
  11. Article
  12. Spatially resolved DNP-assisted NMR illuminates the conformational ensemble of α-synuclein in intact viable cells.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  13. Pathological α-Synuclein Perturbs Nuclear Integrity.bioRxiv : the preprint server for biology · 2025
    Article
  14. Article
  15. Review
  16. Article
  17. Review
  18. Article
  19. Article
  20. Article

69 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

David SneadDepartment of Biochemistry, Weill Cornell Medical College, New York, NY 10065, USA.
David EliezerDepartment of Biochemistry, Weill Cornell Medical College, New York, NY 10065, USA.
Cornell University · US

Funding

Weill Cornell/Rockefeller/Sloan-Kettering MST ProgramT32GM007739 · NIGMS · WEILL MEDICAL COLL OF CORNELL UNIV · PI HSU, KATHARINE C · 1985 to 2023
$51.1M
Structure and Function of Alpha-SynucleinR37AG019391 · NIA · WEILL MEDICAL COLL OF CORNELL UNIV · PI ELIEZER, DAVID · 2010 to 2019
$3.4M
Biophysical Characterization of Complexin C-terminal Domain Lipid InteractionsF30MH101982 · NIMH · WEILL MEDICAL COLL OF CORNELL UNIV · PI SNEAD, DAVID M · 2013 to 2016
$190k
NIA NIH HHS R37 AG019391NIGMS NIH HHS T32 GM007739NIMH NIH HHS F30 MH101982
6 · The paper itself

Abstract

Alpha-synuclein is a small neuronal protein that is closely associated with the etiology of Parkinson's disease. Mutations in and alterations in expression levels of alpha-synuclein cause autosomal dominant early onset heredity forms of Parkinson's disease, and sporadic Parkinson's disease is defined in part by the presence of Lewy bodies and Lewy neurites that are composed primarily of alpha-synuclein deposited in an aggregated amyloid fibril state. The normal function of alpha-synuclein is poorly understood, and the precise mechanisms by which it leads to toxicity and cell death are also unclear. Although alpha-synuclein is a highly soluble, cytoplasmic protein, it binds to a variety of cellular membranes of different properties and compositions. These interactions are considered critical for at least some normal functions of alpha-synuclein, and may well play critical roles in both the aggregation of the protein and its mechanisms of toxicity. Here we review the known features of alpha-synuclein membrane interactions in the context of both the putative functions of the protein and of its pathological roles in disease.

Indexed as

aggregationalpha-synucleinamyloidneurotransmissionParkinsonsynucleinopathy

Identifiers

PMID25548530
PMCPMC4276801
OpenAlexW2043846354

What Socratic holds

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LicenceCC BY-NC
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.