ArticleHuman genomics2012
The human protein disulfide isomerase gene family.
Article in Human genomics, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 145 papers.
What it found
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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.
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.
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Who cites it
145 citing papers in PubMed, 266 citations in OpenAlex.
- Protein disulphide isomerase protects against ALS/FTD phenotypes associated with cyclin F in zebrafish and cellular models.Redox report : communications in free radical research · 2026Article
- Disulphide maintenance systems and proteostasis.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026Review
- Complementary intra- and extracellular AGR2 activities support epithelial ovarian cancer cell aggressiveness.Oncogene · 2026Article
- Distinct Interactions of Arsenite and Cadmium with Metal Homeostasis and the Cellular Stress Response in Human Bronchial Epithelial Cells.International journal of molecular sciences · 2026Article
- PDIA1 promotes androgen receptor activation and prostate cancer cell survival through enhancing HMMR stability.FEBS letters · 2026Article
- Inhibition of the QPCT-PDIA4 axis rescues ΔF508 and N1303K CFTR in cystic fibrosis.Nature communications · 2026Article
- A large-scale DNA methylation study of alcohol use identified robust associations and cell-type specific insights.Molecular psychiatry · 2026Article
- Article
- Cell surface thiol-disulfide regulation in cancer: Mechanisms, implications, and theranostic strategies.Redox biology · 2026Review
- Interactions between the 2C protein of foot-and-mouth disease virus and components of the viral replication machinery are mediated by endoplasmic reticulum-derived membranes.The Journal of general virology · 2026Article
- Proinsulin regulators identified with CRISPR screen and in vivo mouse QTL mapping.Nature communications · 2026Article
- PDIA6 promotes the cell proliferation of ESCC by enhancing the disulfide bond formation in TRAF4.Cellular & molecular biology letters · 2026Article
- The emerging role of calsequestrin 2: from calcium sensor and modulator to arrhythmia driver.Journal of physiology and biochemistry · 2026Review
- Endoplasmic Reticulum Redoxome: Protein Folding and Beyond.Biochemistry · 2026Review
- P4HB regulates tumor-associated macrophage polarization and chemotaxis by enhancing IL-6 cytokine secretion in glioblastoma.Annals of medicine and surgery (2012) · 2025Article
- PDIA3 rs2788, a risk factor for metabolic syndrome, interacted negatively with antihypertensive medications.Scientific reports · 2025Article
- Article
- Tmx2 Maintains Mitochondrial Function to Support Preimplantation Embryogenesis.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025Article
- Endoplasmic reticulum protein 29 negatively regulates platelet functions and thrombosis in mice.Thrombosis journal · 2025Article
- Comparison of Phosphoribosyl Ubiquitin Probes TargetingBioconjugate chemistry · 2025Article
85 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Enzyme-mediated disulfide bond formation is a highly conserved process affecting over one-third of all eukaryotic proteins. The enzymes primarily responsible for facilitating thiol-disulfide exchange are members of an expanding family of proteins known as protein disulfide isomerases (PDIs). These proteins are part of a larger superfamily of proteins known as the thioredoxin protein family (TRX). As members of the PDI family of proteins, all proteins contain a TRX-like structural domain and are predominantly expressed in the endoplasmic reticulum. Subcellular localization and the presence of a TRX domain, however, comprise the short list of distinguishing features required for gene family classification. To date, the PDI gene family contains 21 members, varying in domain composition, molecular weight, tissue expression, and cellular processing. Given their vital role in protein-folding, loss of PDI activity has been associated with the pathogenesis of numerous disease states, most commonly related to the unfolded protein response (UPR). Over the past decade, UPR has become a very attractive therapeutic target for multiple pathologies including Alzheimer disease, Parkinson disease, alcoholic and non-alcoholic liver disease, and type-2 diabetes. Understanding the mechanisms of protein-folding, specifically thiol-disulfide exchange, may lead to development of a novel class of therapeutics that would help alleviate a wide range of diseases by targeting the UPR.
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What OpenQuestion holds
Registered trials
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.