Evidence map›Paper›PMID 33558590›Full record

ReviewExperimental & molecular medicine2021

The aftermath of the interplay between the endoplasmic reticulum stress response and redox signaling.

Kashi Raj Bhattarai, Thoufiqul Alam Riaz, Hyung-Ryong Kim, Han-Jung Chae

Abstract readReview
In one paragraph

Review in Experimental & molecular medicine, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 204 papers.

0numbers the graph read from it
0cells of the map it votes in
204citing papers in PubMed
–field-weighted citation impact
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

204 citing papers in PubMed.

  1. Trial
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  9. Metabolomics Effects of Folding Correction in Retinitis Pigmentosa Rhodopsin Mutant P23A.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026
    Article
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144 more citing papers are in PubMed but not listed here.

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

4 authors.

Kashi Raj Bhattarai *School of Pharmacy and Institute of New Drug Development, Jeonbuk National University, Jeonju, 54896, Republic of Korea.ORCID http://orcid.org/0000-0003-4781-9067
Thoufiqul Alam Riaz *Department of Pharmacology and Institute of New Drug Development, Jeonbuk National University Medical School, Jeonju, 54896, Republic of Korea.
Hyung-Ryong KimCollege of Dentistry, Dankook University, Cheonan, 31116, Republic of Korea. hrkimdp@gmail.com.
Han-Jung ChaeSchool of Pharmacy and Institute of New Drug Development, Jeonbuk National University, Jeonju, 54896, Republic of Korea. hjchae@jbnu.ac.kr.ORCID http://orcid.org/0000-0003-4190-9889

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The endoplasmic reticulum (ER) is an essential organelle of eukaryotic cells. Its main functions include protein synthesis, proper protein folding, protein modification, and the transportation of synthesized proteins. Any perturbations in ER function, such as increased demand for protein folding or the accumulation of unfolded or misfolded proteins in the ER lumen, lead to a stress response called the unfolded protein response (UPR). The primary aim of the UPR is to restore cellular homeostasis; however, it triggers apoptotic signaling during prolonged stress. The core mechanisms of the ER stress response, the failure to respond to cellular stress, and the final fate of the cell are not yet clear. Here, we discuss cellular fate during ER stress, cross talk between the ER and mitochondria and its significance, and conditions that can trigger ER stress response failure. We also describe how the redox environment affects the ER stress response, and vice versa, and the aftermath of the ER stress response, integrating a discussion on redox imbalance-induced ER stress response failure progressing to cell death and dynamic pathophysiological changes.

Indexed as

Endoplasmic Reticulum StressOxidation-ReductionSignal TransductionAnimalsDisease ProgressionDisease SusceptibilityEndoplasmic ReticulumHumansMitochondriaProtein TransportReactive Oxygen SpeciesUnfolded Protein ResponseReactive Oxygen Species

Identifiers

PMID33558590
PMCPMC8080639

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.