Evidence map›Paper›PMID 31996371›Full record

ArticleThe Journal of biological chemistry2020

Galectin 3-binding protein suppresses amyloid-β production by modulating β-cleavage of amyloid precursor protein.

Tsuneyoshi Seki, Motoi Kanagawa, Kazuhiro Kobayashi, Hisatomo Kowa, Naoki Yahata, Kei Maruyama, Nobuhisa Iwata, Haruhisa Inoue, Tatsushi Toda

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2020. 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
2.2field-weighted citation impact, top 11% 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, 44 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

9 authors at 5 institutions in 1 country.

Tsuneyoshi SekiDivision of Neurology/Molecular Brain Science, Kobe University Graduate School of Medicine, Kobe, Hyogo 650-0017, Japan.
Motoi KanagawaDivision of Neurology/Molecular Brain Science, Kobe University Graduate School of Medicine, Kobe, Hyogo 650-0017, Japan.
Kazuhiro KobayashiDivision of Neurology/Molecular Brain Science, Kobe University Graduate School of Medicine, Kobe, Hyogo 650-0017, Japan.
Hisatomo KowaDepartment of Rehabilitation Science, Kobe University Graduate School of Health Sciences, Kobe 654-0142, Japan.
Naoki YahataDepartment of Anatomy I, Fujita Health University School of Medicine, Toyoake, Aichi 470-1192, Japan; Center for iPS Cell Research and Application (CiRA), Kyoto University, Kyoto 606-8507, Japan.
Kei MaruyamaDepartment of Pharmacology, Faculty of Medicine, Saitama Medical University, Saitama 350-0495, Japan.
Nobuhisa IwataDepartment of Genome-based Drug Discovery, Graduate School of Biomedical Sciences, Nagasaki University, Nagasaki 852-8521, Japan.
Haruhisa InoueCenter for iPS Cell Research and Application (CiRA), Kyoto University, Kyoto 606-8507, Japan; iPSC-based Drug Discovery and Development Team, RIKEN BioResource Research Center (BRC), Kyoto 619-0238, Japan; Medical-risk Avoidance based on iPS Cells Team, RIKEN Center for Advanced Intelligence Project (AIP), Kyoto 606-8507, Japan.
Tatsushi TodaDivision of Neurology/Molecular Brain Science, Kobe University Graduate School of Medicine, Kobe, Hyogo 650-0017, Japan; Department of Neurology, Graduate School of Medicine, University of Tokyo, Bunkyo, Tokyo 113-8655, Japan. Electronic address: toda@m.u-tokyo.ac.jp.
Kobe University · JPFujita Health University · JPKyoto University · JPNagasaki University · JPSaitama Medical University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Alzheimer's disease (AD) is the most common type of dementia, and its pathogenesis is associated with accumulation of β-amyloid (Aβ) peptides. Aβ is produced from amyloid precursor protein (APP) that is sequentially cleaved by β- and γ-secretases. Therefore, APP processing has been a target in therapeutic strategies for managing AD; however, no effective treatment of AD patients is currently available. Here, to identify endogenous factors that modulate Aβ production, we performed a gene microarray-based transcriptome analysis of neuronal cells derived from human induced pluripotent stem cells, because Aβ production in these cells changes during neuronal differentiation. We found that expression of the glycophosphatidylinositol-specific phospholipase D1 (

Indexed as

Amyloid beta-PeptidesAntigens, NeoplasmAutocrine CommunicationBiomarkers, TumorCell DifferentiationCell LineExtracellular Matrix ProteinsHEK293 CellsHumansInduced Pluripotent Stem CellsParacrine CommunicationPhospholipase DProtein BindingAmyloid beta-PeptidesAntigens, NeoplasmBiomarkers, TumorExtracellular Matrix ProteinsLGALS3BP protein, humanPhospholipase Dphospholipase D1Alzheimer diseaseamyloid-beta (AB)amyloid precursor protein (APP)beta-secretase 1 (BACE1)galectin 3–binding protein (GAL3BP)glycophosphatidylinositol-specific phospholipase D1 (GPLD1)induced pluripotent stem cell (iPS cell) (iPSC)lectinmicroarrayneurodegeneration

Identifiers

PMID31996371
PMCPMC7076203
OpenAlexW3003984240

What OpenQuestion holds

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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.