Evidence map›Paper›PMID 31843052›Full record

ArticleeLife2019

Cell-based HTS identifies a chemical chaperone for preventing ER protein aggregation and proteotoxicity.

Keisuke Kitakaze, Shusuke Taniuchi, Eri Kawano, Yoshimasa Hamada, Masato Miyake, Miho Oyadomari, Hirotatsu Kojima, Hidetaka Kosako, Tomoko Kuribara, Suguru Yoshida and 2 more

Open access · goldAbstract read
In one paragraph

Article in eLife, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

14 citing papers in PubMed, 26 citations in OpenAlex.

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  10. Wolfram Syndrome 1: From Genetics to Therapy.International journal of environmental research and public health · 2022
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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

12 authors at 4 institutions in 1 country.

Keisuke KitakazeDivision of Molecular Biology, Institute for Genome Research, Institute of Advanced Medical Sciences, Tokushima University, Tokushima, Japan.ORCID 0000-0002-4852-1257
Shusuke TaniuchiDivision of Molecular Biology, Institute for Genome Research, Institute of Advanced Medical Sciences, Tokushima University, Tokushima, Japan.
Eri KawanoDivision of Molecular Biology, Institute for Genome Research, Institute of Advanced Medical Sciences, Tokushima University, Tokushima, Japan.
Yoshimasa HamadaDivision of Molecular Biology, Institute for Genome Research, Institute of Advanced Medical Sciences, Tokushima University, Tokushima, Japan.
Masato MiyakeDivision of Molecular Biology, Institute for Genome Research, Institute of Advanced Medical Sciences, Tokushima University, Tokushima, Japan.
Miho OyadomariDivision of Molecular Biology, Institute for Genome Research, Institute of Advanced Medical Sciences, Tokushima University, Tokushima, Japan.
Hirotatsu KojimaDrug Discovery Initiative (DDI), The University of Tokyo, Tokyo, Japan.
Hidetaka KosakoFujii Memorial Institute of Medical Sciences, Institute of Advanced Medical Sciences, Tokushima University, Tokushima, Japan.
Tomoko KuribaraLaboratory of Chemical Bioscience, Institute of Biomaterials and Bioengineering, Tokyo Medical and Dental University (TMDU), Tokyo, Japan.
Suguru YoshidaLaboratory of Chemical Bioscience, Institute of Biomaterials and Bioengineering, Tokyo Medical and Dental University (TMDU), Tokyo, Japan.ORCID 0000-0001-5888-9330
Takamitsu HosoyaLaboratory of Chemical Bioscience, Institute of Biomaterials and Bioengineering, Tokyo Medical and Dental University (TMDU), Tokyo, Japan.
Seiichi OyadomariDivision of Molecular Biology, Institute for Genome Research, Institute of Advanced Medical Sciences, Tokushima University, Tokushima, Japan.ORCID 0000-0001-6766-1485
Tokushima University · JPTokyo Medical and Dental University · JPKawasaki Medical School · JPThe University of Tokyo · JP

Funding

a Grant-in-Aid for Scientific Research from the Ministry of Education, Culture, Sports, Science and Technology of Japan 16H05222Japan Agency for Medical Research and Development JP17am0101086Japan Agency for Medical Research and Development JP18am0101098Japan Agency for Medical Research and Development JP18nk0101336Japan Society for the Promotion of Science 16H05222 (Grant-in-Aid for Scientific Research)Platform Project for Supporting Drug Discovery and Life Science Research, Basis for Supporting Innovative Drug Discovery and Life Science Research JP18am0101098
6 · The paper itself

Abstract

The endoplasmic reticulum (ER) is responsible for folding secretory and membrane proteins, but disturbed ER proteostasis may lead to protein aggregation and subsequent cellular and clinical pathologies. Chemical chaperones have recently emerged as a potential therapeutic approach for ER stress-related diseases. Here, we identified 2-phenylimidazo[2,1-

Indexed as

BenzothiazolesEndoplasmic ReticulumEndoplasmic Reticulum StressHEK293 CellsHigh-Throughput Screening AssaysHumansPrion ProteinsProtein Aggregation, PathologicalProteostasisUnfolded Protein ResponsebenzothiazoleBenzothiazolesPrion Proteinsbiochemistrycell biologychemical biologychemical chaperoneER stresshumanproteotoxicity

Identifiers

PMID31843052
PMCPMC6922633
OpenAlexW2996275353

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.