ReviewBiochemistry2026
Endoplasmic Reticulum Redoxome: Protein Folding and Beyond.
Review in Biochemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
9 citing papers in PubMed.
- Mitochondria-Directed Redox Phospholipid Polymers for Cancer Therapy.Cancer science · 2026Article
- Exacerbated expansive vascular remodeling due to disturbed flow in male mice overexpressing protein disulfide isomerase-A1.Physiological reports · 2026Article
- Review
- Enzyme-Inspired Design of Redox-Active Molecules for Promotion of Oxidative Protein Folding.Chembiochem : a European journal of chemical biology · 2026Review
- Tetrastigma Hemsleyanum Polysaccharide Suppresses Triple-Negative Breast Cancer by Disrupting the Hippo-YAP/TEAD4-PDIA4 Axis and Endoplasmic Reticulum Stress Adaptation.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- An Artemisia scoparia Extract and Rosiglitazone Have Distinct but Overlapping Effects on Adipocyte Function.Obesity (Silver Spring, Md.) · 2026Article
- Beyond Folding Enzymes: A Redox-Active "Solid Chaperone" Unlocks Recyclable, HPLC-Free Oxidative Protein Folding.JACS Au · 2026Article
- Workflow for Accurate Measurement of PDI Reductase Kinetics Using a Fluorescent Disulfide Substrate.microPublication biology · 2026Article
- The dual role of endoplasmic reticulum stress in cerebral ischemia: from adaptive protection to apoptotic induction.Frontiers in molecular neuroscience · 2026Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The endoplasmic reticulum (ER), the largest cellular organelle, is crucially dependent on its redox organization. First, to optimize disulfide bond formation in nascent proteins, it maintains a relatively oxidizing environment, reminiscent of the extracellular space. Second, it harbors several oxidoreductases from the protein disulfide isomerase (PDI) family, together with Ero1α oxidase and chaperones, which compose interplaying oxidative, reductive, and chaperone pathways to optimize protein processing. Third, disulfide formation and reshuffling in client proteins, involving thiol oxidation and disulfide exchange reactions, connect proteostasis to ER/cellular redox homeostasis. ER redox folding involves Ca
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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 Socratic graph.