Evidence map›Paper›PMID 35166693›Full record

ArticleAging2022

PERK activation by SB202190 ameliorates amyloidogenesis via the TFEB-induced autophagy-lysosomal pathway.

Mihyang Do, Jeongmin Park, Yubing Chen, So-Young Rah, Thu-Hang Thi Nghiem, Jeong Heon Gong, Seong-A Ju, Byung-Sam Kim, Rina Yu, Jeong Woo Park and 5 more

Open access · hybridAbstract read
In one paragraph

Article in Aging, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

4 citing papers in PubMed, 11 citations in OpenAlex.

  1. Endothelial mitochondria in the blood-brain barrier.Fluids and barriers of the CNS · 2025
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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

15 authors at 4 institutions in 2 countries.

Mihyang DoDepartment of Biological Sciences, University of Ulsan, Ulsan 44610, Republic of Korea.
Jeongmin ParkDepartment of Biological Sciences, University of Ulsan, Ulsan 44610, Republic of Korea.
Yubing ChenDepartment of Biological Sciences, University of Ulsan, Ulsan 44610, Republic of Korea.
So-Young RahNational Creative Research Laboratory for Ca2+ Signaling Network, Chonbuk National University Medical School, Jeonju 54907, Republic of Korea.
Thu-Hang Thi NghiemDepartment of Biological Sciences, University of Ulsan, Ulsan 44610, Republic of Korea.
Jeong Heon GongDepartment of Biological Sciences, University of Ulsan, Ulsan 44610, Republic of Korea.
Seong-A JuDepartment of Biological Sciences, University of Ulsan, Ulsan 44610, Republic of Korea.
Byung-Sam KimDepartment of Biological Sciences, University of Ulsan, Ulsan 44610, Republic of Korea.
Rina YuDepartment of Food Science and Nutrition, University of Ulsan, Ulsan 44610, Republic of Korea.
Jeong Woo ParkDepartment of Biological Sciences, University of Ulsan, Ulsan 44610, Republic of Korea.
Stefan W RyterDepartment of Medicine, Weill Cornell Medicine, New York, NY 10065, USA.
Young-Joon SurhDepartment of Molecular Medicine and Biopharmaceutical Sciences, Graduate School of Convergence Science and Technology, Seoul National University, Seoul 08826, Republic of Korea.
Uh-Hyun KimNational Creative Research Laboratory for Ca2+ Signaling Network, Chonbuk National University Medical School, Jeonju 54907, Republic of Korea.
Yeonsoo JoeDepartment of Biological Sciences, University of Ulsan, Ulsan 44610, Republic of Korea.
Hun Taeg ChungDepartment of Biological Sciences, University of Ulsan, Ulsan 44610, Republic of Korea.
University of Ulsan · KRJeonbuk National University · KRCornell University · USSeoul National University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The protein kinase R (PKR)-like endoplasmic reticulum (ER) kinase (PERK), a key ER stress sensor of the unfolded protein response (UPR), can confer beneficial effects by facilitating the removal of cytosolic aggregates through the autophagy-lysosome pathway (ALP). In neurodegenerative diseases, the ALP ameliorates the accumulation of intracellular protein aggregates in the brain. Transcription factor-EB (TFEB), a master regulator of the ALP, positively regulates key genes involved in the cellular degradative pathway. However, in neurons, the role of PERK activation in mitigating amyloidogenesis by ALP remains unclear. In this study, we found that SB202190 selectively activates PERK independently of its inhibition of p38 mitogen-activated protein kinase, but not inositol-requiring transmembrane kinase/endoribonuclease-1α (IRE1α) or activating transcription factor 6 (ATF6), in human neuroblastoma cells. PERK activation by SB202190 was dependent on mitochondrial ROS production and promoted Ca

Indexed as

AmyloideIF-2 KinaseEndoribonucleasesImidazolesNeuroblastomaPyridinesAutophagyBasic Helix-Loop-Helix Leucine Zipper Transcription FactorsCalcineurinEndoplasmic Reticulum StressHumansLysosomesProtein Serine-Threonine KinasesUnfolded Protein Response4-(4-fluorophenyl)-2-(4-hydroxyphenyl)-5-(4-pyridyl)imidazoleAmyloidBasic Helix-Loop-Helix Leucine Zipper Transcription FactorsCalcineurinEIF2AK3 protein, humaneIF-2 KinaseEndoribonucleasesImidazolesProtein Serine-Threonine KinasesPyridinesTFEB protein, humanamyloidogenesisautophagy-lysosome pathwaymitochondrial reactive oxygen speciesPERKtranscription factor-EB

Identifiers

PMID35166693
PMCPMC8876914
OpenAlexW4213301066

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.