Evidence map›Paper›PMID 32397116›Full record

ReviewCells2020

Role of Endoplasmic Reticulum Stress Sensor IRE1α in Cellular Physiology, Calcium, ROS Signaling, and Metaflammation.

Thoufiqul Alam Riaz, Raghu Patil Junjappa, Mallikarjun Handigund, Jannatul Ferdous, Hyung-Ryong Kim, Han-Jung Chae

Open access · goldAbstract readReview
In one paragraph

Review in Cells, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
62citing papers in PubMed, 2 pooled it
5.1field-weighted citation impact, top 3% 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

62 citing papers in PubMed, 2 syntheses or guidelines pooled it, 91 citations in OpenAlex.

  1. Pooled it
  2. Pooled it
  3. Review
  4. Review
  5. Metabolites · 2026
    Article
  6. Article
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  8. Article
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  12. Article
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  18. Methylglyoxal Formation-Metabolic Routes and Consequences.Antioxidants (Basel, Switzerland) · 2025
    Review
  19. Article
  20. Review

2 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

6 authors at 3 institutions in 1 country.

Thoufiqul Alam RiazDepartment of Pharmacology, School of Medicine, Institute of New Drug Development, Jeonbuk National University, Jeonju 54907, Korea.
Raghu Patil JunjappaDepartment of Pharmacology, School of Medicine, Institute of New Drug Development, Jeonbuk National University, Jeonju 54907, Korea.
Mallikarjun HandigundDepartment of Laboratory Medicine, Jeonbuk National University, Medical School, Jeonju 54907, Korea.
Jannatul FerdousDepartment of Radiology and Research Institute of Clinical Medicine of Jeonbuk National University, Biomedical Research Institute of Jeonbuk National University Hospital, Jeonju 54907, Korea.
Hyung-Ryong KimCollege of Dentistry, Dankook University, Cheonan 31116, Korea.
Han-Jung ChaeDepartment of Pharmacology, School of Medicine, Institute of New Drug Development, Jeonbuk National University, Jeonju 54907, Korea.ORCID 0000-0003-4190-9889
Jeonbuk National University · KRDankook University · KRJeonbuk National University Hospital · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Inositol-requiring transmembrane kinase endoribonuclease-1α (IRE1α) is the most prominent and evolutionarily conserved unfolded protein response (UPR) signal transducer during endoplasmic reticulum functional upset (ER stress). A IRE1α signal pathway arbitrates yin and yang of cellular fate in objectionable conditions. It plays several roles in fundamental cellular physiology as well as in several pathological conditions such as diabetes, obesity, inflammation, cancer, neurodegeneration, and in many other diseases. Thus, further understanding of its molecular structure and mechanism of action during different cell insults helps in designing and developing better therapeutic strategies for the above-mentioned chronic diseases. In this review, recent insights into structure and mechanism of activation of IRE1α along with its complex regulating network were discussed in relation to their basic cellular physiological function. Addressing different binding partners that can modulate IRE1α function, UPRosome triggers different downstream pathways depending on the cellular backdrop. Furthermore, IRE1α are in normal cell activities outside the dominion of ER stress and activities under the weather of inflammation, diabetes, and obesity-related metaflammation. Thus, IRE1 as an ER stress sensor needs to be understood from a wider perspective for comprehensive functional meaning, which facilitates us with assembling future needs and therapeutic benefits.

Indexed as

Endoplasmic Reticulum StressSignal TransductionAnimalsCalciumHumansInflammationProtein Serine-Threonine KinasesReactive Oxygen SpeciesCalciumProtein Serine-Threonine KinasesReactive Oxygen Speciescalciumendoplasmic reticulum stressinsulin resistanceIRE1αmetaflammationobesityROStype 2 diabetes

Identifiers

PMID32397116
PMCPMC7290600
OpenAlexW3022749243

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.