ReviewThe Biochemical journal1999
The protein disulphide-isomerase family: unravelling a string of folds.
Review in The Biochemical journal, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 151 papers.
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.
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.
Who cites it
151 citing papers in PubMed, 499 citations in OpenAlex.
- Protein disulfide isomerases are antibody targets during immune-mediated tumor destruction.Blood · 2009Trial
- The embryo-derived protein PDI is highly conserved among placental mammals and alters the endometrial transcriptome and secretome in vitro across species with differing implantation strategies†.Biology of reproduction · 2026Article
- Ecofriendly synthesis of iron nanoparticles and their role in mitigation of multiple abiotic stresses in fish.Scientific reports · 2026Article
- Mitigating combined toxic effects of arsenic, ammonia, and high temperature through dietary Iron in fish.Frontiers in immunology · 2026Article
- Multiomic analyses direct hypotheses for Creutzfeldt-Jakob disease risk genes.Brain : a journal of neurology · 2025Article
- Metabolically aberrant extracellular mitochondria induce oxidative endotheliopathy in traumatic brain injury.Blood advances · 2025Article
- Protein disulfide isomerase is essential for osteoblast differentiation in mice.Communications biology · 2025Article
- Decoding PDI diversity: Insights into structure, domains, and functionality in sorghum.Computational and structural biotechnology journal · 2025Article
- The protein disulfide isomerase A3 and osteopontin axis promotes influenza-induced lung remodelling.British journal of pharmacology · 2024Article
- Analysis of Punicalin and Punicalagin Interaction with PDIA3 and PDIA1.International journal of molecular sciences · 2024Article
- Protein disulfide isomerase plays a crucial role in mediating chemically-induced, glutathione depletion-associated hepatocyte injury in vitro and in vivo.Cell communication and signaling : CCS · 2024Article
- Quantitative proteomics reveals cellular responses to individual mAb expression and tunicamycin in CHO cells.Applied microbiology and biotechnology · 2024Article
- Article
- Article
- Differential Protein Expression in Response to Varlitinib Treatment in Oral Cancer Cell Line: an In Vitro Therapeutic Approach.Applied biochemistry and biotechnology · 2024Article
- Unraveling gene regulation mechanisms in fish: insights into multistress responses and mitigation through iron nanoparticles.Frontiers in immunology · 2024Article
- Article
- Biochemical mechanism of erastin-induced ferroptotic cell death in neuronal cells.Acta biochimica et biophysica Sinica · 2023Article
- An Overview of Two Old Friends Associated with Platelet Redox Signaling, the Protein Disulfide Isomerase and NADPH Oxidase.Biomolecules · 2023Article
- Differential Protein Expression ofPathogens (Basel, Switzerland) · 2023Article
91 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
No grant is acknowledged in the PubMed record.
Abstract
The mammalian protein disulphide-isomerase (PDI) family encompasses several highly divergent proteins that are involved in the processing and maturation of secretory proteins in the endoplasmic reticulum. These proteins are characterized by the presence of one or more domains of roughly 95-110 amino acids related to the cytoplasmic protein thioredoxin. All but the PDI-D subfamily are composed entirely of repeats of such domains, with at least one domain containing and one domain lacking a redox-active -Cys-Xaa-Xaa-Cys- tetrapeptide. In addition to their known roles as redox catalysts and isomerases, the last few years have revealed additional functions of the PDI proteins, including peptide binding, cell adhesion and perhaps chaperone activities. Attention is now turning to the non-redox-active domains of the PDIs, which may play an important role in all of the known activities of these proteins. Thus the presence of both redox-active and -inactive domains within these proteins portends a complexity of functions differentially accommodated by the various family members.
Indexed as
Identifiers
10085220PMC1220120W2005145242What 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.