Evidence map›Paper›PMID 28108534›Full record

ReviewCold Spring Harbor perspectives in medicine2018

Cell Biology and Pathophysiology of α-Synuclein.

Jacqueline Burré, Manu Sharma, Thomas C Südhof

Open access · bronzeAbstract readReview
In one paragraph

Review in Cold Spring Harbor perspectives in medicine, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 351 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
351citing papers in PubMed, 2 pooled it
–field-weighted citation impact
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

351 citing papers in PubMed, 2 syntheses or guidelines pooled it, 555 citations in OpenAlex.

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  5. Cellular and systemic modifiers of alpha-synuclein proteostasis.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026
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291 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

3 authors at 3 institutions in 1 country.

Jacqueline BurréAppel Institute for Alzheimer's Disease Research, Brain and Mind Research Institute, Weill Cornell Medicine, New York, New York 10021.
Manu SharmaAppel Institute for Alzheimer's Disease Research, Brain and Mind Research Institute, Weill Cornell Medicine, New York, New York 10021.
Thomas C SüdhofDepartments of Molecular and Cellular Physiology, Stanford University Medical School, Stanford, California 94305.
Cornell University · USMIND Research Institute · USStanford University · US

Funding

Mouse CoreP50NS094733 · NINDS · BRIGHAM AND WOMEN'S HOSPITAL · PI SHEN, JIE · 2015 to 2020
$7.1M
DnaJ co-chaperones which modify tau aggregation and neurodegenerationR01AG052505 · NIA · WEILL MEDICAL COLL OF CORNELL UNIV · PI SHARMA, MANU · 2016 to 2020
$1.9M
Cellular mechanism of Adult Onset Neuronal Ceroid Lipofuscinosis (ANCL) caused by mutations in cysteine string protein-alpha (CSPalpha).R01NS095988 · NINDS · WEILL MEDICAL COLL OF CORNELL UNIV · PI SHARMA, MANU · 2017 to 2021
$1.8M
NIA NIH HHS R01 AG052505NINDS NIH HHS P50 NS094733NINDS NIH HHS R01 NS095988
6 · The paper itself

Abstract

α-Synuclein is an abundant neuronal protein that is highly enriched in presynaptic nerve terminals. Genetics and neuropathology studies link α-synuclein to Parkinson's disease (PD) and other neurodegenerative disorders. Accumulation of misfolded oligomers and larger aggregates of α-synuclein defines multiple neurodegenerative diseases called synucleinopathies, but the mechanisms by which α-synuclein acts in neurodegeneration are unknown. Moreover, the normal cellular function of α-synuclein remains debated. In this perspective, we review the structural characteristics of α-synuclein, its developmental expression pattern, its cellular and subcellular localization, and its function in neurons. We also discuss recent progress on secretion of α-synuclein, which may contribute to its interneuronal spread in a prion-like fashion, and describe the neurotoxic effects of α-synuclein that are thought to be responsible for its role in neurodegeneration.

Indexed as

alpha-SynucleinAnimalsHumansMiceMice, TransgenicNeuronsParkinson DiseaseSynapsesalpha-Synuclein

Identifiers

PMID28108534
PMCPMC5519445
OpenAlexW2577340531

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.