Evidence map›Paper›PMID 31941659›Full record

ArticleeNeuro

Hsc70 Ameliorates the Vesicle Recycling Defects Caused by Excess α-Synuclein at Synapses.

Susan M L Banks, Audrey T Medeiros, Molly McQuillan, David J Busch, Ana Sofia Ibarraran-Viniegra, Rui Sousa, Eileen M Lafer, Jennifer R Morgan

Open access · goldAbstract read
In one paragraph

Article in eNeuro. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.4field-weighted citation impact, top 9% 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

24 citing papers in PubMed, 41 citations in OpenAlex.

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  15. The role of snare proteins in cortical development.Developmental neurobiology · 2022
    Review
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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

8 authors at 3 institutions in 1 country.

Susan M L BanksThe Eugene Bell Center for Regenerative Biology and Tissue Engineering Marine Biological Laboratory, Woods Hole, MA 02543.ORCID 0000-0001-7088-4487
Audrey T MedeirosThe Eugene Bell Center for Regenerative Biology and Tissue Engineering Marine Biological Laboratory, Woods Hole, MA 02543.ORCID 0000-0002-5562-4772
Molly McQuillanThe Eugene Bell Center for Regenerative Biology and Tissue Engineering Marine Biological Laboratory, Woods Hole, MA 02543.
David J BuschDepartment of Biomedical Engineering, The University of Texas at Austin, Austin, TX 78712.
Ana Sofia Ibarraran-ViniegraThe Eugene Bell Center for Regenerative Biology and Tissue Engineering Marine Biological Laboratory, Woods Hole, MA 02543.
Rui SousaDepartment of Biochemistry and Structural Biology and Center for Biomedical Neuroscience, the University of Texas Health Science Center at San Antonio, San Antonio, TX 79229.ORCID 0000-0003-4314-121X
Eileen M LaferDepartment of Biochemistry and Structural Biology and Center for Biomedical Neuroscience, the University of Texas Health Science Center at San Antonio, San Antonio, TX 79229.ORCID 0000-0002-0493-6522
Jennifer R MorganThe Eugene Bell Center for Regenerative Biology and Tissue Engineering Marine Biological Laboratory, Woods Hole, MA 02543 jmorgan@mbl.edu.ORCID 0000-0001-9915-6360
Marine Biological Laboratory · USThe University of Texas Health Science Center at San Antonio · USThe University of Texas at Austin · US

Funding

Mechanisms of Synaptic Dysfunction in Parkinson s and Other Synuclein-Linked DiseasesR01NS078165 · NINDS · UNIVERSITY OF TEXAS AT AUSTIN · PI Jennifer Rebecca Morgan · 2012 to 2026
$5.5M
Chaperone Mechanisms in Clathrin Mediated Neuronal Vesicle TraffickingR01GM118933 · NIGMS · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI LAFER, EILEEN M., SOUSA, RUI J. · 2016 to 2019
$1.7M
NIGMS NIH HHS R01 GM118933NINDS NIH HHS R01 NS078165
6 · The paper itself

Abstract

α-Synuclein overexpression and aggregation are linked to Parkinson's disease (PD), dementia with Lewy bodies (DLB), and several other neurodegenerative disorders. In addition to effects in the cell body, α-synuclein accumulation occurs at presynapses where the protein is normally localized. While it is generally agreed that excess α-synuclein impairs synaptic vesicle trafficking, the underlying mechanisms are unknown. We show here that acute introduction of excess human α-synuclein at a classic vertebrate synapse, the lamprey reticulospinal (RS) synapse, selectively impaired the uncoating of clathrin-coated vesicles (CCVs) during synaptic vesicle recycling, leading to an increase in endocytic intermediates and a severe depletion of synaptic vesicles. Furthermore, human α-synuclein and lamprey γ-synuclein both interact

Indexed as

alpha-SynucleinEndocytosisClathrin-Coated VesiclesHumansSynapsesSynaptic Vesiclesalpha-Synucleinauxilinchaperoneclathrinclathrin-coated vesiclesendocytosislamprey

Identifiers

PMID31941659
PMCPMC7031854
OpenAlexW2998958355

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.