Evidence map›Paper›PMID 29632069›Full record

ArticleThe Journal of biological chemistry2018

Extracellular α-synuclein drives sphingosine 1-phosphate receptor subtype 1 out of lipid rafts, leading to impaired inhibitory G-protein signaling.

Shaymaa Mohamed Mohamed Badawy, Taro Okada, Taketoshi Kajimoto, Mitsuhiro Hirase, Shubi Ambwene Matovelo, Shunsuke Nakamura, Daisuke Yoshida, Takeshi Ijuin, Shun-Ichi Nakamura

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
4.8field-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

27 citing papers in PubMed, 42 citations in OpenAlex.

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  20. Cell Responses to Extracellular α-Synuclein.Molecules (Basel, Switzerland) · 2019
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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

9 authors at 1 institution in 1 country.

Shaymaa Mohamed Mohamed BadawyDivision of Biochemistry, Department of Biochemistry and Molecular Biology, Kobe University Graduate School of Medicine, 7-5-1 Kusunoki, Kobe 650-0017, Japan.
Taro OkadaDivision of Biochemistry, Department of Biochemistry and Molecular Biology, Kobe University Graduate School of Medicine, 7-5-1 Kusunoki, Kobe 650-0017, Japan.
Taketoshi KajimotoDivision of Biochemistry, Department of Biochemistry and Molecular Biology, Kobe University Graduate School of Medicine, 7-5-1 Kusunoki, Kobe 650-0017, Japan.
Mitsuhiro HiraseDivision of Biochemistry, Department of Biochemistry and Molecular Biology, Kobe University Graduate School of Medicine, 7-5-1 Kusunoki, Kobe 650-0017, Japan.
Shubi Ambwene MatoveloDivision of Biochemistry, Department of Biochemistry and Molecular Biology, Kobe University Graduate School of Medicine, 7-5-1 Kusunoki, Kobe 650-0017, Japan.
Shunsuke NakamuraDivision of Biochemistry, Department of Biochemistry and Molecular Biology, Kobe University Graduate School of Medicine, 7-5-1 Kusunoki, Kobe 650-0017, Japan.
Daisuke YoshidaDivision of Biochemistry, Department of Biochemistry and Molecular Biology, Kobe University Graduate School of Medicine, 7-5-1 Kusunoki, Kobe 650-0017, Japan.
Takeshi IjuinDivision of Biochemistry, Department of Biochemistry and Molecular Biology, Kobe University Graduate School of Medicine, 7-5-1 Kusunoki, Kobe 650-0017, Japan.
Shun-Ichi NakamuraDivision of Biochemistry, Department of Biochemistry and Molecular Biology, Kobe University Graduate School of Medicine, 7-5-1 Kusunoki, Kobe 650-0017, Japan. Electronic address: snakamur@kobe-u.ac.jp.
Kobe University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

α-Synuclein (α-Syn)-positive intracytoplasmic inclusions, known as Lewy bodies, are thought to be involved in the pathogenesis of Lewy body diseases, such as Parkinson's disease (PD). Although growing evidence suggests that cell-to-cell transmission of α-Syn is associated with the progression of PD and that extracellular α-Syn promotes formation of inclusion bodies, its precise mechanism of action in the extracellular space remains unclear. Here, as indicated by both conventional fractionation techniques and FRET-based protein-protein interaction analysis, we demonstrate that extracellular α-Syn causes expulsion of sphingosine 1-phosphate receptor subtype 1 (S1P

Indexed as

alpha-SynucleinCell MovementGTP-Binding Protein alpha Subunits, Gi-GoHumansMembrane MicrodomainsMultivesicular BodiesNeuroblastomaProtein TransportReceptors, LysosphingolipidSignal TransductionTumor Cells, Culturedalpha-SynucleinGTP-Binding Protein alpha Subunits, Gi-GoReceptors, LysosphingolipidSNCA protein, humangangliosidelipid raftsignal transductionsphingosine-1-phosphate (S1P)α-synuclein (α-synuclein)

Identifiers

PMID29632069
PMCPMC5971450
OpenAlexW2798044885

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.