Evidence map›Paper›PMID 32496635›Full record

ArticleAging cell2020

Exploration of multi-target effects of 3-benzoyl-5-hydroxychromen-2-one in Alzheimer's disease cell and mouse models.

Te-Hsien Lin, Ya-Jen Chiu, Chih-Hsin Lin, Chung-Yin Lin, Chih-Ying Chao, Yu-Chieh Chen, Shu-Mei Yang, Wenwei Lin, Hsiu Mei Hsieh-Li, Yih-Ru Wu and 3 more

Open access · goldAbstract read
In one paragraph

Article in Aging cell, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

13 citing papers in PubMed, 15 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Using ΔK280 TauBiomolecules · 2023
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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

13 authors at 2 institutions in 1 country.

Te-Hsien LinDepartment of Life Science, National Taiwan Normal University, Taipei, Taiwan.ORCID 0000-0002-1107-772X
Ya-Jen ChiuDepartment of Life Science, National Taiwan Normal University, Taipei, Taiwan.ORCID 0000-0003-3195-2509
Chih-Hsin LinDepartment of Neurology, Chang Gung Memorial Hospital, Chang Gung University College of Medicine, Taoyuan, Taiwan.ORCID 0000-0001-9179-5846
Chung-Yin LinMedical Imaging Research Center, Institute for Radiological Research, Chang Gung University/Chang Gung Memorial Hospital, Taoyuan, Taiwan.
Chih-Ying ChaoDepartment of Neurology, Chang Gung Memorial Hospital, Chang Gung University College of Medicine, Taoyuan, Taiwan.
Yu-Chieh ChenDepartment of Neurology, Chang Gung Memorial Hospital, Chang Gung University College of Medicine, Taoyuan, Taiwan.
Shu-Mei YangDepartment of Chemistry, National Taiwan Normal University, Taipei, Taiwan.
Wenwei LinDepartment of Chemistry, National Taiwan Normal University, Taipei, Taiwan.
Hsiu Mei Hsieh-LiDepartment of Life Science, National Taiwan Normal University, Taipei, Taiwan.
Yih-Ru WuDepartment of Neurology, Chang Gung Memorial Hospital, Chang Gung University College of Medicine, Taoyuan, Taiwan.ORCID 0000-0003-1191-2542
Kuo-Hsuan ChangDepartment of Neurology, Chang Gung Memorial Hospital, Chang Gung University College of Medicine, Taoyuan, Taiwan.ORCID 0000-0003-4972-9823
Guey-Jen Lee-ChenDepartment of Life Science, National Taiwan Normal University, Taipei, Taiwan.ORCID 0000-0003-4818-9917
Chiung-Mei ChenDepartment of Neurology, Chang Gung Memorial Hospital, Chang Gung University College of Medicine, Taoyuan, Taiwan.ORCID 0000-0002-0769-0353
Chang Gung University · TWNational Taiwan Normal University · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Microtubule-associated protein Tau, abundant in the central nervous system (CNS), plays crucial roles in microtubule assembly and stabilization. Abnormal Tau phosphorylation and aggregation are a common pathogenic hallmark in Alzheimer's disease (AD). Hyperphosphorylation of Tau could change its conformation and result in self-aggregation, increased oxidative stress, and neuronal death. In this study, we examined the potential of licochalcone A (a natural chalcone) and five synthetic derivatives (LM compounds) for inhibiting Tau misfolding, scavenging reactive oxygen species (ROS) and providing neuroprotection in human cells expressing proaggregant ΔK280 Tau

Indexed as

Alzheimer DiseaseAnimalsApoptosisDisease Models, AnimalHumansMaleMiceOxidative StressUp-RegulationAlzheimer's diseaseapoptosischaperoneLM-031oxidative stressTau

Identifiers

PMID32496635
PMCPMC7433010
OpenAlexW3032884680

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.