Evidence map›Paper›PMID 28533388›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2017

Selective lowering of synapsins induced by oligomeric α-synuclein exacerbates memory deficits.

Megan E Larson, Susan J Greimel, Fatou Amar, Michael LaCroix, Gabriel Boyle, Mathew A Sherman, Hallie Schley, Camille Miel, Julie A Schneider, Rakez Kayed and 4 more

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
4.7field-weighted citation impact, top 5% 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

36 citing papers in PubMed, 64 citations in OpenAlex.

  1. Article
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  10. Oligomerization by co-assembly of β-amyloid and α-synuclein.Frontiers in molecular biosciences · 2023
    Review
  11. Review
  12. Article
  13. Article
  14. α-synuclein-assisted oligomerization of β-amyloid (1-42).Archives of biochemistry and biophysics · 2022
    Article
  15. Article
  16. Article
  17. Article
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  19. 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

14 authors at 4 institutions in 2 countries.

Megan E LarsonDepartment of Neuroscience, University of Minnesota, Minneapolis, MN 55414.
Susan J GreimelDepartment of Neuroscience, University of Minnesota, Minneapolis, MN 55414.
Fatou AmarDepartment of Neuroscience, University of Minnesota, Minneapolis, MN 55414.
Michael LaCroixDepartment of Neuroscience, University of Minnesota, Minneapolis, MN 55414.
Gabriel BoyleDepartment of Neuroscience, University of Minnesota, Minneapolis, MN 55414.
Mathew A ShermanDepartment of Neuroscience, University of Minnesota, Minneapolis, MN 55414.
Hallie SchleyDepartment of Neuroscience, University of Minnesota, Minneapolis, MN 55414.
Camille MielDepartment of Neuroscience, University of Minnesota, Minneapolis, MN 55414.
Julie A SchneiderRush Alzheimer's Disease Center, Rush University Medical Center, Chicago, IL 60612.
Rakez KayedDepartment of Neurology, University of Texas Medical Branch, Galveston, TX 77555.
Fabio BenfenatiCenter for Synaptic Neuroscience, Istituto Italiano di Tecnologia, 16132 Genoa, Italy.
Michael K LeeDepartment of Neuroscience, University of Minnesota, Minneapolis, MN 55414.
David A BennettRush Alzheimer's Disease Center, Rush University Medical Center, Chicago, IL 60612.
Sylvain E LesnéDepartment of Neuroscience, University of Minnesota, Minneapolis, MN 55414; lesne002@umn.edu.ORCID 0000-0001-9411-1868
University of Minnesota · USRush University Medical Center · USItalian Institute of Technology · ITThe University of Texas Medical Branch at Galveston · US

Funding

SUPPLEMENT TO RUSH ALZHEIMERS DISEASE CENTER COREP30AG010161 · NIA · RUSH UNIVERSITY MEDICAL CENTER · PI BENNETT, DAVID ALAN · 1991 to 2020
$49.1M
RISK FACTORS, PATHOLOGY, AND CLINICAL EXPRESSIONS OF ADR01AG015819 · NIA · RUSH UNIVERSITY MEDICAL CENTER · PI BENNETT, DAVID ALAN · 1998 to 2024
$21.4M
Risk Factors, Pathology, and Clinical Expressions of ADRF1AG015819 · NIA · RUSH UNIVERSITY MEDICAL CENTER · PI BENNETT, DAVID ALAN · 2014 to 2014
$6.0M
PREDOCTORAL TRAINING OF NEUROSCIENTISTST32GM008471 · NIGMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI EBNER, TIMOTHY J · 1993 to 2017
$4.9M
Soluble αSyn is a modulator of AD pathophysiologyRF1AG044342 · NIA · UNIVERSITY OF MINNESOTA · PI LESNE, SYLVAIN E. · 2019 to 2019
$2.7M
Unfolded Protein Response in Alpha-synucleinopathiesR01NS086074 · NINDS · UNIVERSITY OF MINNESOTA · PI LEE, MICHAEL K · 2014 to 2018
$1.7M
Soluble aSyn is a modulator of AD pathophysiologyR01AG044342 · NIA · UNIVERSITY OF MINNESOTA · PI LESNE, SYLVAIN E. · 2014 to 2018
$1.5M
NIA NIH HHS P30 AG010161NIA NIH HHS R01 AG015819NIA NIH HHS R01 AG044342NIA NIH HHS RF1 AG015819NIA NIH HHS RF1 AG044342NIGMS NIH HHS T32 GM008471NINDS NIH HHS R01 NS086074
6 · The paper itself

Abstract

Mounting evidence indicates that soluble oligomeric forms of amyloid proteins linked to neurodegenerative disorders, such as amyloid-β (Aβ), tau, or α-synuclein (αSyn) might be the major deleterious species for neuronal function in these diseases. Here, we found an abnormal accumulation of oligomeric αSyn species in AD brains by custom ELISA, size-exclusion chromatography, and nondenaturing/denaturing immunoblotting techniques. Importantly, the abundance of αSyn oligomers in human brain tissue correlated with cognitive impairment and reductions in synapsin expression. By overexpressing WT human αSyn in an AD mouse model, we artificially enhanced αSyn oligomerization. These bigenic mice displayed exacerbated Aβ-induced cognitive deficits and a selective decrease in synapsins. Following isolation of various soluble αSyn assemblies from transgenic mice, we found that in vitro delivery of exogenous oligomeric αSyn but not monomeric αSyn was causing a lowering in synapsin-I/II protein abundance. For a particular αSyn oligomer, these changes were either dependent or independent on endogenous αSyn expression. Finally, at a molecular level, the expression of synapsin genes

Indexed as

alpha-SynucleinAlzheimer DiseaseAnimalsBrainCognitionCyclic AMP Response Element-Binding ProteinDisease Models, AnimalGenes, Tumor SuppressorHumansMemory DisordersMiceMice, TransgenicNuclear ProteinsNuclear Receptor Subfamily 4, Group A, Member 2Protein Structure, QuaternaryRecombinant Proteinsalpha-SynucleinCreb1 protein, mouseCyclic AMP Response Element-Binding ProteinFAM107A protein, humanNr4a2 protein, mouseNuclear ProteinsNuclear Receptor Subfamily 4, Group A, Member 2Recombinant ProteinsSNCA protein, humanSynapsinsAlzheimer’s diseasememoryoligomersynapsinsα-synuclein

Identifiers

PMID28533388
PMCPMC5468636
OpenAlexW2618220838

What OpenQuestion holds

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Registered trials

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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.