Evidence map›Paper›PMID 31394034›Full record

ReviewACS chemical neuroscience2019

The Synaptic Vesicle Glycoprotein 2: Structure, Function, and Disease Relevance.

Kristen A Stout, Amy R Dunn, Carlie Hoffman, Gary W Miller

Open access · greenAbstract readReview
In one paragraph

Review in ACS chemical neuroscience, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
68citing papers in PubMed, 1 pooled it
3.9field-weighted citation impact, top 6% 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

68 citing papers in PubMed, 1 synthesis or guideline pooled it, 110 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Article
  4. Review
  5. Imaging Synaptic Vesicle Protein SV2C withACS chemical neuroscience · 2026
    Article
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8 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

4 authors at 4 institutions in 1 country.

Kristen A StoutDepartment of Physiology , Northwestern University, Feinberg School of Medicine , Chicago , Illinois , United States.ORCID 0000-0002-3641-5326
Amy R DunnThe Jackson Laboratory , Bar Harbor , Maine , United States.
Carlie HoffmanDepartment of Environmental Health, Rollins School of Public Health , Emory University , Atlanta , Georgia , United States.
Gary W MillerDepartment of Environmental Health Sciences, Mailman School of Public Health , Columbia University , New York , New York , United States.ORCID 0000-0001-8984-1284
Columbia University · USEmory University · USJackson Laboratory · USNorthwestern University · US

Funding

Graduate and Postdoctoral Training in ToxicologyT32ES012870 · NIEHS · EMORY UNIVERSITY · PI Carmen Joseph Marsit · 2004 to 2026
$9.1M
Vesicular Modulation of Dopamine Neuron ToxicityR01ES023839 · NIEHS · EMORY UNIVERSITY · PI MILLER, GARY W · 2015 to 2025
$5.0M
Estradiol reduces mitochondrial oxidant stress in SNc DA neuronsF32AG058396 · NIA · NORTHWESTERN UNIVERSITY AT CHICAGO · PI STOUT, KRISTEN · 2017 to 2019
$178k
SV2C as a novel mediator of transmitter release and neuroprotection in dopamine cellsF31NS089242 · NINDS · EMORY UNIVERSITY · PI DUNN, AMY · 2015 to 2017
$93k
SV2C: a novel target for inhibition of methamphetamine actionF31DA037652 · NIDA · EMORY UNIVERSITY · PI STOUT, KRISTEN · 2014 to 2015
$86k
VMAT2-mediated rescue of Parkinsons disease pathology and behaviorF31NS084739 · NINDS · EMORY UNIVERSITY · PI LOHR, KELLY M · 2013 to 2015
$73k
NIA NIH HHS F32 AG058396NIDA NIH HHS F31 DA037652NIEHS NIH HHS R01 ES023839NIEHS NIH HHS T32 ES012870NINDS NIH HHS F31 NS084739NINDS NIH HHS F31 NS089242
6 · The paper itself

Abstract

The synaptic vesicle glycoprotein 2 (SV2) family is comprised of three paralogues: SV2A, SV2B, and SV2C. In vertebrates, SV2s are 12-transmembrane proteins present on every secretory vesicle, including synaptic vesicles, and are critical to neurotransmission. Structural and functional studies suggest that SV2 proteins may play several roles to promote proper vesicular function. Among these roles are their potential to stabilize the transmitter content of vesicles, to maintain and orient the releasable pool of vesicles, and to regulate vesicular calcium sensitivity to ensure efficient, coordinated release of the transmitter. The SV2 family is highly relevant to human health in a number of ways. First, SV2A plays a role in neuronal excitability and as such is the specific target for the antiepileptic drug levetiracetam. SV2 proteins also act as the target by which potent neurotoxins, particularly botulinum, gain access to neurons and exert their toxicity. Both SV2B and SV2C are increasingly implicated in diseases such as Alzheimer's disease and Parkinson's disease. Interestingly, despite decades of intensive research, their exact function remains elusive. Thus, SV2 proteins are intriguing in their potentially diverse roles within the presynaptic terminal, and several recent developments have enhanced our understanding and appreciation of the protein family. Here, we review the structure and function of SV2 proteins as well as their relevance to disease and therapeutic development.

Indexed as

AnimalsHumansMembrane GlycoproteinsNerve Tissue ProteinsNervous System DiseasesProtein TransportSynaptic VesiclesMembrane GlycoproteinsNerve Tissue ProteinsSV2A protein, humanSV2B protein, humanSV2C protein, humanneurotransmissionSV2Vesicle

Identifiers

PMID31394034
PMCPMC11562936
OpenAlexW2967602434

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.