Evidence map›Paper›PMID 38007054›Full record

ReviewBiochimica et biophysica acta. Reviews on cancer2024

Fingerprint of the oxido-reductase ERO1: A protein disulfide bond producer and supporter of cancer.

Ester Zito, Luca Guarrera, Yvonne M W Janssen-Heininger

Open access · hybridAbstract readReview
In one paragraph

Review in Biochimica et biophysica acta. Reviews on cancer, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed, 1 pooled it
4.6field-weighted citation impact, top 5% 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

17 citing papers in PubMed, 1 synthesis or guideline pooled it, 22 citations in OpenAlex.

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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

3 authors at 2 institutions in 2 countries.

Ester ZitoIstituto di Ricerche Farmacologiche Mario Negri IRCCS, Milan, Italy; Department of Biomolecular Sciences, University of Urbino Carlo Bo, Urbino, Italy. Electronic address: ester.zito@marionegri.it.
Luca GuarreraIstituto di Ricerche Farmacologiche Mario Negri IRCCS, Milan, Italy.
Yvonne M W Janssen-HeiningerDepartments of Pathology and Laboratory Medicine, University of Vermont College of Medicine, Burlington, VT, USA. Electronic address: Yvonne.janssen@med.uvm.edu.
Istituti di Ricovero e Cura a Carattere Scientifico · ITUniversity of Vermont · US

Funding

Glutaredoxin, Glutathione Metabolism and Lung CancerR01CA273238 · NCI · UNIVERSITY OF VERMONT & ST AGRIC COLLEGE · PI Yvonne M. W. Janssen-Heininger · 2023 to 2026
$2.1M
NCI NIH HHS R01 CA273238
6 · The paper itself

Abstract

Endoplasmic reticulum oxidoreductin 1 (ERO1) alpha (ERO1A) is an endoplasmic reticulum (ER)-localized protein disulfide oxidoreductase, involved in the disulfide bond formation of proteins. ERO1's activity in oxidative protein folding is redundant in higher eukaryotes and its loss is well compensated. Although it is dispensable in non-cancer cells, high ERO1 levels are seen with different cancers and predict their malignant phenotype. ERO1 fosters tumor aggressiveness and the response to drug therapy in hypoxic and highly metastatic tumors. It regulates vascular endothelial growth factor (VEGF) levels, oxidative folding and N-glycosylation in hypoxic conditions, boosting tumor fitness and angiogenesis on multiple levels. In addition, ERO1 regulates protein death ligand-1 (PD-L1) on tumors, interfering with the related immune surveillance mechanism, hence acting on the tumors' response to immune check-point inhibitors (ICI). This all points to inhibition of ERO1 as an effective pharmacological tool, selectively targeting tumors while sparing non-cancer cells from cytotoxicity. The critical discussion here closely examines the molecular basis for ERO1's involvement in tumors and ERO1 inhibition strategies for their treatment.

Indexed as

NeoplasmsVascular Endothelial Growth Factor ADisulfidesEndoplasmic ReticulumHumansOxidoreductasesDisulfidesOxidoreductasesVascular Endothelial Growth Factor AAngiogenesiscancerEndoplasmic reticulum stressERO1 alphaHypoxiaMetastasisUPR (unfolded protein response)

Identifiers

PMID38007054
PMCPMC11046445
OpenAlexW4388979090

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.