Evidence map›Paper›PMID 38454454›Full record

ReviewJournal of experimental & clinical cancer research : CR2024

Biological mechanisms and clinical significance of endoplasmic reticulum oxidoreductase 1 alpha (ERO1α) in human cancer.

Peng Chen, Amit Sharma, Hans Weiher, Ingo G H Schmidt-Wolf

Open access · goldAbstract readReview
In one paragraph

Review in Journal of experimental & clinical cancer research : CR, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed, 1 pooled it
10.1field-weighted citation impact, top 1% 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

21 citing papers in PubMed, 1 synthesis or guideline pooled it, 27 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Multi-omics integration identifiesTranslational andrology and urology · 2026
    Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. ERO1A-positive tumor epithelial cells in colorectal cancer progression: a multi-omics perspective.Apoptosis : an international journal on programmed cell death · 2025
    Article
  18. Article
  19. Review
  20. Review
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 at 3 institutions in 2 countries.

Peng ChenDepartment of Integrated Oncology, Center for Integrated Oncology (CIO), University Hospital Bonn, 3127, Bonn, Germany.ORCID http://orcid.org/0009-0009-6871-5786
Amit SharmaDepartment of Integrated Oncology, Center for Integrated Oncology (CIO), University Hospital Bonn, 3127, Bonn, Germany.
Hans WeiherDepartment of Applied Natural Sciences, Bonn-Rhein-Sieg University of Applied Sciences, 53359, Rheinbach, Germany.
Ingo G H Schmidt-WolfDepartment of Integrated Oncology, Center for Integrated Oncology (CIO), University Hospital Bonn, 3127, Bonn, Germany. ingo.schmidt-wolf@ukbonn.de.
University Hospital Bonn · DEHochschule Bonn-Rhein-Sieg · DEIntegrated Oncology (United States) · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A firm link between endoplasmic reticulum (ER) stress and tumors has been wildly reported. Endoplasmic reticulum oxidoreductase 1 alpha (ERO1α), an ER-resident thiol oxidoreductase, is confirmed to be highly upregulated in various cancer types and associated with a significantly worse prognosis. Of importance, under ER stress, the functional interplay of ERO1α/PDI axis plays a pivotal role to orchestrate proper protein folding and other key processes. Multiple lines of evidence propose ERO1α as an attractive potential target for cancer treatment. However, the unavailability of specific inhibitor for ERO1α, its molecular inter-relatedness with closely related paralog ERO1β and the tightly regulated processes with other members of flavoenzyme family of enzymes, raises several concerns about its clinical translation. Herein, we have provided a detailed description of ERO1α in human cancers and its vulnerability towards the aforementioned concerns. Besides, we have discussed a few key considerations that may improve our understanding about ERO1α in tumors.

Indexed as

Membrane GlycoproteinsNeoplasmsClinical RelevanceEndoplasmic ReticulumEndoplasmic Reticulum StressHumansOxidation-ReductionOxidoreductasesERO1A protein, humanMembrane GlycoproteinsOxidoreductasesCancerERO1αER stressImmune escapeInhibitorPDIPrognosis

Identifiers

PMID38454454
PMCPMC10921667
OpenAlexW4392593964

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.