Evidence map›Paper›PMID 32201313›Full record

ReviewPharmacology & therapeutics2020

Role of the ERO1-PDI interaction in oxidative protein folding and disease.

Andrea G Shergalis, Shuai Hu, Armand Bankhead, Nouri Neamati

Open access · greenAbstract readReview
In one paragraph

Review in Pharmacology & therapeutics, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 98 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
98citing papers in PubMed, 1 pooled it
8.4field-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

98 citing papers in PubMed, 1 synthesis or guideline pooled it, 181 citations in OpenAlex.

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38 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 at 2 institutions in 1 country.

Andrea G ShergalisDepartment of Medicinal Chemistry, College of Pharmacy, University of Michigan, Rogel Cancer Center, Ann Arbor, MI 48109, United States.
Shuai HuDepartment of Medicinal Chemistry, College of Pharmacy, University of Michigan, Rogel Cancer Center, Ann Arbor, MI 48109, United States; Department of Computational Medicine and Bioinformatics, University of Michigan Medical School, Ann Arbor, MI 48109, United States.
Armand BankheadDepartment of Computational Medicine and Bioinformatics, University of Michigan Medical School, Ann Arbor, MI 48109, United States; Department of Biostatistics, University of Michigan School of Public Health, Ann Arbor, MI 48109, United States.
Nouri NeamatiDepartment of Medicinal Chemistry, College of Pharmacy, University of Michigan, Rogel Cancer Center, Ann Arbor, MI 48109, United States. Electronic address: neamati@umich.edu.
U-M Rogel Cancer CenterUniversity of Michigan–Ann Arbor · US

Funding

Efficacy of PDI inhibitors in glioblastomaR01CA193690 · NCI · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI NEAMATI, NOURI, REHEMTULLA, ALNAWAZ · 2015 to 2019
$2.4M
NCI NIH HHS R01 CA193690
6 · The paper itself

Abstract

Protein folding in the endoplasmic reticulum is an oxidative process that relies on protein disulfide isomerase (PDI) and endoplasmic reticulum oxidase 1 (ERO1). Over 30% of proteins require the chaperone PDI to promote disulfide bond formation. PDI oxidizes cysteines in nascent polypeptides to form disulfide bonds and can also reduce and isomerize disulfide bonds. ERO1 recycles reduced PDI family member PDIA1 using a FAD cofactor to transfer electrons to oxygen. ERO1 dysfunction critically affects several diseases states. Both ERO1 and PDIA1 are overexpressed in cancers and implicated in diabetes and neurodegenerative diseases. Cancer-associated ERO1 promotes cell migration and invasion. Furthermore, the ERO1-PDIA1 interaction is critical for epithelial-to-mesenchymal transition. Co-expression analysis of ERO1A gene expression in cancer patients demonstrated that ERO1A is significantly upregulated in lung adenocarcinoma (LUAD), glioblastoma and low-grade glioma (GBMLGG), pancreatic ductal adenocarcinoma (PAAD), and kidney renal papillary cell carcinoma (KIRP) cancers. ERO1Α knockdown gene signature correlates with knockdown of cancer signaling proteins including IGF1R, supporting the search for novel, selective ERO1 inhibitors for the treatment of cancer. In this review, we explore the functions of ERO1 and PDI to support inhibition of this interaction in cancer and other diseases.

Indexed as

AnimalsAntineoplastic AgentsEndoplasmic ReticulumEnzyme InhibitorsGene Expression Regulation, NeoplasticGene Regulatory NetworksHumansMembrane GlycoproteinsMolecular Targeted TherapyNeoplasmsOxidation-ReductionOxidative StressOxidoreductasesProcollagen-Proline DioxygenaseProtein Disulfide-IsomerasesProtein FoldingAntineoplastic AgentsEnzyme InhibitorsERO1A protein, humanMembrane GlycoproteinsOxidoreductasesP4HB protein, humanProcollagen-Proline DioxygenaseProtein Disulfide-IsomerasesReactive Oxygen SpeciesCancerEndoplasmic reticulum OxidaseGene expressionProtein disulfide IsomeraseProtein foldingTargeted therapy

Identifiers

PMID32201313
PMCPMC7316501
OpenAlexW3012203039

What OpenQuestion holds

Textmetadata
LicenceTDM
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.