Evidence map›Paper›PMID 31661838›Full record

ArticleInternational journal of molecular sciences2019

Fatty Acid-Binding Protein 3 is Critical for α-Synuclein Uptake and MPP

Ichiro Kawahata, Luc Bousset, Ronald Melki, Kohji Fukunaga

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
4.4field-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

29 citing papers in PubMed, 53 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

4 authors at 2 institutions in 2 countries.

Ichiro KawahataDepartment of Pharmacology, Graduate School of Pharmaceutical Sciences, Tohoku University, Sendai 980-8578, Japan. kawahata@tohoku.ac.jp.ORCID 0000-0002-5916-7847
Luc BoussetCEA, Institut François Jacob (MIRcen) and CNRS, Laboratory of Neurodegenerative Diseases, 18 Route du Panorama, 92265 Fontenay-aux-Roses, France. Luc.BOUSSET@cnrs.fr.
Ronald MelkiCEA, Institut François Jacob (MIRcen) and CNRS, Laboratory of Neurodegenerative Diseases, 18 Route du Panorama, 92265 Fontenay-aux-Roses, France. ronald.melki@cnrs.fr.
Kohji FukunagaDepartment of Pharmacology, Graduate School of Pharmaceutical Sciences, Tohoku University, Sendai 980-8578, Japan. kfukunaga@m.tohoku.ac.jp.ORCID 0000-0001-8526-2824
Centre National de la Recherche Scientifique · FRTohoku University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

α-Synuclein is an abundant neuronal protein that accumulates in insoluble inclusions in Parkinson's disease and other synucleinopathies. Fatty acids partially regulate α-Synuclein accumulation, and mesencephalic dopaminergic neurons highly express fatty acid-binding protein 3 (FABP3). We previously demonstrated that FABP3 knockout mice show decreased α-Synuclein oligomerization and neuronal degeneration of tyrosine hydroxylase (TH)-positive neurons

Indexed as

1-Methyl-4-phenylpyridiniumalpha-SynucleinAnimalsBiological TransportCells, CulturedDopamineDopaminergic NeuronsFatty Acid Binding Protein 3MesencephalonMiceMice, Inbred C57BLMice, KnockoutMitochondriaParkinson DiseaseReactive Oxygen SpeciesTyrosine 3-Monooxygenase1-Methyl-4-phenylpyridiniumalpha-SynucleinDopamineFabp3 protein, mouseFatty Acid Binding Protein 3Reactive Oxygen SpeciesSnca protein, mouseTyrosine 3-Monooxygenase1-methyl-4-phenylpyridinium (MPP+)fatty acid-binding protein 3mitochondriaParkinson’s diseasesynucleinopathyα-Synuclein

Identifiers

PMID31661838
PMCPMC6862506
OpenAlexW2982145395

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.