ArticlePloS one2014
A novel reaction of peroxiredoxin 4 towards substrates in oxidative protein folding.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 27 citations in OpenAlex.
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- Endoplasmic Reticulum Stress and the Unfolded Protein Response in Cerebral Ischemia/Reperfusion Injury.Frontiers in cellular neuroscience · 2022Review
- Redox Enzymes of the Thioredoxin Family as Potential and Novel Markers in Pemphigus.Oxidative medicine and cellular longevity · 2021Article
- Characterization of the endoplasmic reticulum-resident peroxidases GPx7 and GPx8 shows the higher oxidative activity of GPx7 and its linkage to oxidative protein folding.The Journal of biological chemistry · 2020Article
- Loss ofFrontiers in cellular neuroscience · 2019Article
- The Multifaceted Impact of Peroxiredoxins on Aging and Disease.Antioxidants & redox signaling · 2018Review
- (+)-Aeroplysinin-1 Modulates the Redox Balance of Endothelial Cells.Marine drugs · 2018Article
- Biosynthesis, structure, and folding of the insulin precursor protein.Diabetes, obesity & metabolism · 2018Review
- The role of peroxiredoxins in cancer.Molecular and clinical oncology · 2017Article
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- The circadian coordination of cell biology.The Journal of cell biology · 2016Review
- Mitochondrial ROS versus ER ROS: Which Comes First in Myocardial Calcium Dysregulation?Frontiers in cardiovascular medicine · 2016Article
- The sulfiredoxin-peroxiredoxin (Srx-Prx) axis in cell signal transduction and cancer development.Cancer letters · 2015Review
- Hydrogen peroxide - production, fate and role in redox signaling of tumor cells.Cell communication and signaling : CCS · 2015Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Peroxiredoxin 4 (Prx4) is the only endoplasmic reticulum localized peroxiredoxin. It functions not only to eliminate peroxide but also to promote oxidative protein folding via oxidizing protein disulfide isomerase (PDI). In Prx4-mediated oxidative protein folding we discovered a new reaction that the sulfenic acid form of Prx4 can directly react with thiols in folding substrates, resulting in non-native disulfide cross-linking and aggregation. We also found that PDI can inhibit this reaction by exerting its reductase and chaperone activities. This discovery discloses an off-pathway reaction in the Prx4-mediated oxidative protein folding and the quality control role of PDI.
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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 OpenQuestion graph.