Evidence map›Paper›PMID 32228705›Full record

ArticleMolecular neurodegeneration2020

A role for α-Synuclein in axon growth and its implications in corticostriatal glutamatergic plasticity in Parkinson's disease.

Meir Schechter, Jessica Grigoletto, Suaad Abd-Elhadi, Hava Glickstein, Alexander Friedman, Geidy E Serrano, Thomas G Beach, Ronit Sharon

Open access · goldAbstract read
In one paragraph

Article in Molecular neurodegeneration, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.7field-weighted citation impact, top 12% 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

16 citing papers in PubMed, 27 citations in OpenAlex.

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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 2 institutions in 1 country.

Meir SchechterDepartment of Biochemistry and Molecular Biology, IMRIC, The Hebrew University-Hadassah Medical School, Ein Kerem, 9112001, Jerusalem, Israel.
Jessica GrigolettoDepartment of Biochemistry and Molecular Biology, IMRIC, The Hebrew University-Hadassah Medical School, Ein Kerem, 9112001, Jerusalem, Israel.
Suaad Abd-ElhadiDepartment of Biochemistry and Molecular Biology, IMRIC, The Hebrew University-Hadassah Medical School, Ein Kerem, 9112001, Jerusalem, Israel.
Hava GlicksteinElectron Microscopy Unit, The Hebrew University-Hadassah Medical School, Ein Kerem, 9112001, Jerusalem, Israel.
Alexander FriedmanMcGovern Institute for Brain Research and Department of Brain and Cognitive Sciences, Massachusetts Institute of Technology, Cambridge, MA, 02139, USA.
Geidy E SerranoBanner Sun Health Research Institute, Sun City, AZ, USA.
Thomas G BeachBanner Sun Health Research Institute, Sun City, AZ, USA.
Ronit SharonDepartment of Biochemistry and Molecular Biology, IMRIC, The Hebrew University-Hadassah Medical School, Ein Kerem, 9112001, Jerusalem, Israel. ronitsh@ekmd.huji.ac.il.
Banner Sun Health Research Institute · USMcGovern Institute for Brain Research · US

Funding

Research Education ComponentP30AG019610 · NIA · SUN HEALTH RESEARCH INSTITUTE · PI REIMAN, ERIC MICHAEL · 2001 to 2020
$32.5M
National Brain and Tissue Resource for Parkinson's Disease and Related DisordersU24NS072026 · NINDS · BANNER SUN HEALTH RESEARCH INSTITUTE · PI BEACH, THOMAS G · 2011 to 2015
$7.8M
NIA NIH HHS P30 AG019610NIA NIH HHS P30 AG19610NINDS NIH HHS U24 NS072026
6 · The paper itself

Abstract

backgroundα-Synuclein (α-Syn) is a protein implicated in the pathogenesis of Parkinson's disease (PD). α-Syn has been shown to associate with membranes and bind acidic phospholipids. However, the physiological importance of these associations to the integrity of axons is not fully clear.

methodsBiochemical, immunohistochemical and ultrastructural analyses in cultured neurons, transgenic mouse brains, PD and control human brains.

resultsWe analyzed the ultrastructure of cross-sectioned axons localized to white matter tracts (WMTs), within the dorsal striatum of old and symptomatic α-Syn transgenic mouse brains. The analysis indicated a higher density of axons of thinner diameter. Our findings in cultured cortical neurons indicate a role for α-Syn in elongation of the main axon and its collaterals, resulting in enhanced axonal arborization. We show that α-Syn effect to enhance axonal outgrowth is mediated through its activity to regulate membrane levels of the acidic phosphatidylinositol 4,5-bisphosphate (PI4,5P

conclusionsOur results show that through regulating PI4,5P

Indexed as

Parkinson Diseasealpha-SynucleinAnimalsAxonsBrainHumansMiceMice, TransgenicMicroscopy, Electron, TransmissionNeural PathwaysNeuronal PlasticityPhosphatidylinositol 4,5-DiphosphateWhite Matteralpha-SynucleinPhosphatidylinositol 4,5-DiphosphateAxonal growthAxonal injuryCorticostriatal axonsParkinson’s diseasePhosphatidylinositol 4,5-bisphosphate (PI4,5P2)White matter tracts (WMTs)α-Synuclein

Identifiers

PMID32228705
PMCPMC7104492
OpenAlexW3013577783

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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.