Evidence map›Paper›PMID 31269263›Full record

ReviewJournal of neurochemistry2019

The physiological role of α-synuclein and its relationship to Parkinson's Disease.

David Sulzer, Robert H Edwards

Open access · greenAbstract readReview
In one paragraph

Review in Journal of neurochemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 198 papers, 3 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
198citing papers in PubMed, 3 pooled it
24.6field-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

198 citing papers in PubMed, 3 syntheses or guidelines pooled it, 304 citations in OpenAlex.

  1. Prevalence and impact of orthostatic hypotension in Parkinson's disease: a systematic review and meta-analysis.Clinical autonomic research : official journal of the Clinical Autonomic Research Society · 2025
    Pooled it
  2. Pooled it
  3. Association of orthostatic hypotension with Parkinson's disease: a meta-analysis.Neurological sciences : official journal of the Italian Neurological Society and of the Italian Society of Clinical Neurophysiology · 2020
    Pooled it
  4. Differential proteostasis imbalance and the molecular basis of distinct synucleinopathies and tauopathies.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026
    Review
  5. Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Heat shock protein 10 as a chaperone modulating α-synuclein amyloid fibril formation.Protein science : a publication of the Protein Society · 2026
    Article
  13. Article
  14. Review
  15. Article
  16. Exidavnemab binds to aggregated α-synuclein in human brains affected by α-synucleinopathies.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2026
    Article
  17. Review
  18. Review
  19. Review
  20. Review

138 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 SulzerDepartments of Psychiatry, Neurology and Pharmacology, Columbia University Medical Center, New York State Psychiatric Institute.
Robert H EdwardsDepartments of Neurology and Physiology, Graduate Programs in Cell Biology, Biomedical Sciences and Neuroscience, UCSF School of Medicine.ORCID 0000-0002-8650-3260
Columbia University Irving Medical Center · US

Funding

The Dopamine Synapse and Associative LearningR01DA007418 · NIDA · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI David Sulzer · 1999 to 2026
$9.4M
Autoimmune Features of Neurodegenerative DisordersR01NS095435 · NINDS · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI SETTE, ALESSANDRO, SULZER, DAVID · 2018 to 2022
$4.2M
The Function of SynucleinR01NS109295 · NINDS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI EDWARDS, ROBERT H · 2019 to 2023
$2.5M
Alpha-Synuclein and the Synaptic Vesicle CycleR01NS062715 · NINDS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI EDWARDS, ROBERT H · 2009 to 2014
$1.9M
NIDA NIH HHS R01 DA007418NINDS NIH HHS R01 NS062715NINDS NIH HHS R01 NS095435NINDS NIH HHS R01 NS109295
6 · The paper itself

Abstract

The protein α-synuclein has a central role in the pathogenesis of Parkinson's disease (PD). In this review, we discuss recent results concerning its primary function, which appears to be on cell membranes. The pre-synaptic location of synuclein has suggested a role in neurotransmitter release and it apparently associates with synaptic vesicles because of their high curvature. Indeed, synuclein over-expression inhibits synaptic vesicle exocytosis. However, loss of synuclein has not yet been shown to have a major effect on synaptic transmission. Consistent with work showing that synuclein can promote as well as sense membrane curvature, recent analysis of synuclein triple knockout mice now shows that synuclein accelerates dilation of the exocytic fusion pore. This form of regulation affects primarily the release of slowly discharged lumenal cargo such as neural peptides, but presumably also contributes to maintenance of the release site. This article is part of the Special Issue "Synuclein".

Indexed as

alpha-SynucleinAnimalsAxonsCell MembraneDisease Models, AnimalDopamineExocytosisHumansMembrane FusionMice, KnockoutMice, TransgenicMitochondriaMutation, MissenseParkinson DiseasePresynaptic TerminalsProtein Domainsalpha-SynucleinDopamineProtein IsoformsRecombinant Proteinsfusion poreLewy pathologyParkinson's diseaseregulated exocytosissynaptic vesiclesynuclein

Identifiers

PMID31269263
PMCPMC6707892
OpenAlexW2955272631

What OpenQuestion holds

Textmetadata
LicenceTDM
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 OpenQuestion graph.