Evidence map›Paper›PMID 33210431›Full record

ArticleAngewandte Chemie (International ed. in English)2021

Phenotypic Discovery of Neuroprotective Agents by Regulation of Tau Proteostasis via Stress-Responsive Activation of PERK Signaling.

Young-Hee Shin, Hana Cho, Bo Young Choi, Jonghoon Kim, Jaeyoung Ha, Sang Won Suh, Seung Bum Park

Open access · hybridAbstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.0field-weighted citation impact, top 27% 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

16 citing papers in PubMed, 19 citations in OpenAlex.

  1. Article
  2. Review
  3. Intercellular propagation of RIPK1/RIPK3 amyloid fibrils.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  4. Article
  5. Review
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Tau Toxicity in Neurodegeneration.Molecular neurobiology · 2022
    Review
  13. Review
  14. Article
  15. Article
  16. Article
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

7 authors at 2 institutions in 1 country.

Young-Hee ShinCRI Center for Chemical Proteomics, Department of Chemistry, Seoul National University, Seoul, 08826, Korea.ORCID 0000-0003-0235-7081
Hana ChoDepartment of Biophysics and Chemical Biology, Seoul National University, Seoul, 08826, Korea.
Bo Young ChoiDepartment of Physiology, College of Medicine, Hallym University, Chuncheon, 24252, Korea.
Jonghoon KimCRI Center for Chemical Proteomics, Department of Chemistry, Seoul National University, Seoul, 08826, Korea.ORCID 0000-0003-4951-5497
Jaeyoung HaDepartment of Biophysics and Chemical Biology, Seoul National University, Seoul, 08826, Korea.
Sang Won SuhDepartment of Physiology, College of Medicine, Hallym University, Chuncheon, 24252, Korea.
Seung Bum ParkCRI Center for Chemical Proteomics, Department of Chemistry, Seoul National University, Seoul, 08826, Korea.ORCID 0000-0003-1753-1433
Seoul National University · KRHallym University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Tau protein aggregates are a recognized neuropathological feature in Alzheimer's disease as well as many other neurodegenerative disorders, known as tauopathies. The development of tau-targeting therapies is therefore extremely important but efficient strategies or protein targets are still unclear. Here, we performed a cell-based phenotypic screening under endoplasmic reticulum (ER) stress conditions and identified a small molecule, SB1617, capable of suppressing abnormal tau protein aggregation. By applying label-free target identification technology, we revealed that the transient enhancement of protein kinase-like endoplasmic reticulum kinase (PERK) signaling pathway through the inhibition of stress-responsive SB1617 targets, PDIA3 and DNAJC3, is an effective strategy for regulating proteostasis in tauopathies. The molecular mechanism and the promising efficacy of SB1617 were demonstrated in neuronal cells and a mouse model with traumatic brain injury, a tauopathy known to involve ER stress.

Indexed as

Drug DiscoverySignal TransductionAnimalsBrain Injuries, TraumaticeIF-2 KinaseEnzyme ActivationHEK293 CellsHSP40 Heat-Shock ProteinsHumansMiceNeuroprotective AgentsProtein Disulfide-IsomerasesProteostasistau ProteinsDNAJC3 protein, humanEIF2AK3 protein, humaneIF-2 KinaseHSP40 Heat-Shock ProteinsMAPT protein, humanNeuroprotective AgentsPDIA3 protein, humanProtein Disulfide-Isomerasestau ProteinsER stress responsePERK signalingproteostasistarget Identificationtauopathies

Identifiers

PMID33210431
PMCPMC7898623
OpenAlexW3105281256

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.