The DOI matches its Crossref record; 135 of the 135 references it cites were found in a registry or an index.
Mechanisms and Implications of Reactive Oxygen Species Generation During the Unfolded Protein Response: Roles of Endoplasmic Reticulum Oxidoreductases, Mitochondrial Electron Transport, and NADPH Oxidase
Abstract
Cellular mechanisms governing redox homeostasis likely involve their integration with other stresses. Endoplasmic reticulum (ER) stress triggers complex adaptive or proapoptotic signaling defined as the unfolded protein response (UPR), involved in several pathophysiological processes. Since protein folding is highly redox-dependent, convergence between ER stress and oxidative stress has attracted interest. Evidence suggests that ROS production and oxidative stress are not only coincidental to ER stress, but are integral UPR components, being triggered by distinct types of ER stressors and contributing to support proapoptotic, as well as proadaptive UPR signaling. Thus, ROS generation can be upstream or downstream UPR targets and may display a UPR-specific plus a nonspecific component. Enzymatic mechanisms of ROS generation during UPR include: (a) Multiple thiol-disulfide exchanges involving ER oxidoreductases including flavooxidase Ero1 and protein disulfide isomerase (PDI); (b) Mitochondrial electron transport; (c) Nox4 NADPH oxidase complex, particularly Nox4. Understanding the roles of such mechanisms and how they interconnect with the UPR requires more investigation. Integration among such ROS sources may depend on Ca(2+) levels, ROS themselves, and PDI, which associates with NADPH oxidase and regulates its function. Oxidative stress may frequently integrate with a background of ER stress/UPR in several diseases; here we discuss a focus in the vascular system.
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“The signaling mechanisms of hydrogen peroxide in ECs (941) lead to the increased activity of eNOS and other enzymes (121, 141, 193, 251, 815, 940).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [815]
In the citing paper
“Reactive oxygen species are produced by the Maillard reaction [20], [21], damaging pancreatic beta cells, and leading to a subcellular stress response (the “unfolded protein response” in the endoplasmic reticulum) that drives insulin inadequacy [22], [23].”
From The relationship of sugar to population-level diabetes prevalence: an econometric analysis of repeated cross-sectional data (2013) · cites this paper as [22]
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1 retracted
Proapoptotic BAX and BAK Modulate the Unfolded Protein Response by a Direct Interaction with IRE1α
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RetractedThe NOX Family of ROS-Generating NADPH Oxidases: Physiology and Pathophysiology
Bedard, K., & Krause, K.-H. (2007) · Physiological Reviews · doi:10.1152/physrev.00044.2005 · Cited by 6,989
Signal integration in the endoplasmic reticulum unfolded protein response
Ron, D., & Walter, P. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2199 · Cited by 6,431
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Harding, H. P., Zhang, Y., Zeng, H., Novoa, I., Lu, P. D., Calfon, M. A., Sadri, N., Yun, C., Popko, B., Paules, R. S., et al. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00105-9 · Cited by 3,336
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Zhang, K., & Kaufman, R. J. (2008) · Nature · doi:10.1038/nature07203 · Cited by 2,010
Oxidized Redox State of Glutathione in the Endoplasmic Reticulum
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Research works printed but not linked: 1
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Sorted by citations
Integrating the mechanisms of apoptosis induced by endoplasmic reticulum stress
Tabas, I. A., & Ron, D. (2011) · Nature Cell Biology · doi:10.1038/ncb0311-184 · Cited by 2,655
Endoplasmic Reticulum Stress and Oxidative Stress in Cell Fate Decision and Human Disease
Cao, S. S., & Kaufman, R. J. (2014) · Antioxidants and Redox Signaling · doi:10.1089/ars.2014.5851 · Cited by 1,393
Endoplasmic Reticulum Stress and Associated ROS
Zeeshan, H. M. A., Lee, K. H., Kim, H., & Chae, H. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17030327 · Cited by 976
ROS Generation and Antioxidant Defense Systems in Normal and Malignant Cells
Snezhkina, A. V., Kudryavtseva, A. V., Kardymon, O. L., Savvateeva, M. V., Melnikova, N. V., Krasnov, G. S., & Dmitriev, A. A. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/6175804 · Cited by 934
Combating oxidative stress in vascular disease: NADPH oxidases as therapeutic targets
Drummond, G. R., Selemidis, S., Griendling, K. K., & Sobey, C. G. (2011) · Nature Reviews Drug Discovery · doi:10.1038/nrd3403 · Cited by 899
Metadata
- Authors
- Santos, C. X. C., Tanaka, L. Y., Wosniak, J., & Laurindo, F. R. M.
- Affiliations
- Universidade de São Paulo (BR)
- Venue
- Antioxidants & Redox Signaling
- Publisher
- SAGE Publications
- Published
- 2009-10
- Volume
- 11
- Issue
- 10
- Pages
- 2409-2427
- ISSN
- 1523-0864 (ISSN-L)
- 1557-7716
- OpenAlex
- W2064194224
- Cited by
- 572
- References
- 135
- Citations by year
- 2026: 10 · 2025: 20 · 2024: 22 · 2023: 25 · 2022: 27 · 2021: 31 · 2020: 43 · 2019: 36 · 2018: 40 · 2017: 37 · 2016: 36 · 2015: 44 · 2014: 46 · 2013: 40 · 2012: 41
- FWCI
- 2.86
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Antioxidants and Redox Signaling (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Endoplasmic Reticulum Stress and Disease
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Health Sciences › Medicine › Physiology (medical) › Nitric Oxide and Endothelin Effects
- Keywords
- unfolded protein response, endoplasmic reticulum stress, reactive oxygen species, oxidative stress, redox homeostasis, Ero1, protein disulfide isomerase, mitochondrial electron transport chain, NADPH oxidase, NOX4, thiol-disulfide exchange, calcium signaling, vascular disease
- MeSH terms
- Electron Transport, Endoplasmic Reticulum, Enzyme Activation, Homeostasis, Isoenzymes, Mitochondria, Oxidation-Reduction, Oxidoreductases, Stress, Physiological, Vascular Diseases, Signal Transduction, Apoptosis, Reactive Oxygen Species, NADPH Oxidases, Protein Disulfide-Isomerases
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