Cited by 572Endoplasmic Reticulum Stress and DiseaseRedox biology and oxidative stressNitric Oxide and Endothelin Effects

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

Santos, Célio X.C., Tanaka, Leonardo Y., Wosniak, João, Laurindo, Francisco R.M.·2009·Antioxidants & Redox Signaling

DOI 10.1089/ars.2009.2625

Open this paper in CoChat — free account

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.

Integrity signals

Registry

Crossref · 10.1089/ars.2009.2625

Cites

135 of 135 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

1 retracted

Proapoptotic BAX and BAK Modulate the Unfolded Protein Response by a Direct Interaction with IRE1α
Hetz, C. A., Bernasconi, P., Fisher, J. K., Lee, A., Bassik, M. C., Antonsson, B. E., Brandt, G. S., Iwakoshi, N. N., Schinzel, A. C., Glimcher, L. H., et al. (2006) · Science · doi:10.1126/science.1123480 · Cited by 688
Retracted
The 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
An Integrated Stress Response Regulates Amino Acid Metabolism and Resistance to Oxidative Stress
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
THE MAMMALIAN UNFOLDED PROTEIN RESPONSE
Schröder, M., & Kaufman, R. J. (2005) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.73.011303.074134 · Cited by 3,099
CHOP induces death by promoting protein synthesis and oxidation in the stressed endoplasmic reticulumPreprint
Marciniak, S. J., Yun, C. Y., Oyadomari, S., Novoa, I., Zhang, Y., Jungreis, R., Nagata, K., Harding, H. P., & Ron, D. (2004) · Genes & Development · doi:10.1101/gad.1250704 · Cited by 2,066
From endoplasmic-reticulum stress to the inflammatory response
Zhang, K., & Kaufman, R. J. (2008) · Nature · doi:10.1038/nature07203 · Cited by 2,010
Oxidized Redox State of Glutathione in the Endoplasmic Reticulum
Hwang, C., Sinskey, A. J., & Lodish, H. F. (1992) · Science · doi:10.1126/science.1523409 · Cited by 1,968
Pathophysiology of coronary artery disease
Libby, P., & Theroux, P. (2005) · Circulation · doi:10.1161/circulationaha.105.537878 · Cited by 1,965
Gadd153 Sensitizes Cells to Endoplasmic Reticulum Stress by Down-Regulating Bcl2 and Perturbing the Cellular Redox State
McCullough, K. D., Martindale, J. L., Klotz, L., Aw, T. Y., & Holbrook, N. J. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.4.1249-1259.2001 · Cited by 1,945

Flagged first, then by citations

Show all 135 references

Research works printed but not linked: 1

Diwan A, 2009, J Clin Invest, 119, 203

Sorted by citations

Items 401–500 of 569

Redox and Inflammatory Signaling, the Unfolded Protein Response, and the Pathogenesis of Pulmonary Hypertension.
Katseff, A. S., Alhawaj, R., & Wolin, M. (2021) · Advances in Experimental Medicine and Biology · doi:10.1007/978-3-030-68748-9_17 · Cited by 14
Self-protective responses to norvaline-induced stress in a leucyl-tRNA synthetase editing-deficient yeast strain
Ji, Q., Fang, Z., Ye, Q., Chi, C., & Wang, E. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkx487 · Cited by 14
Trans-unsaturated fatty acid activates NLRP3 inflammasome in macrophages and exacerbates intestinal inflammation in mice
Higashimura, Y., Tanaka, Y., Takagi, T., Uchiyama, K., Mizushima, K., Niki, E., & Naito, Y. (2020) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2020.06.005 · Cited by 13
Regulation of reactive oxygen species in the pathogenesis of matrix vesicles induced calcification of recipient vascular smooth muscle cells
Chen, N. X., O’Neill, K. D., Dominguez, J. M., & Moe, S. M. (2021) · Vascular Medicine · doi:10.1177/1358863x211024721 · Cited by 13
Perfluorooctanoic acid-induced cellular and subcellular alterations in fish hepatocytes
Manera, M., Castaldelli, G., Fano, E. A., & Giari, L. (2020) · Environmental Toxicology and Pharmacology · doi:10.1016/j.etap.2020.103548 · Cited by 13
Fibrillin-1 mgΔlpn Marfan syndrome mutation associates with preserved proteostasis and bypass of a protein disulfide isomerase-dependent quality checkpoint
Meirelles, T., Araujo, T. L. S., Nolasco, P., Moretti, A. I. S., Guido, M. C., Debbas, V., Pereira, L. V., & Laurindo, F. R. (2016) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2015.12.009 · Cited by 10
Self-citation
Enhancing the Effect of Tumor Necrosis Factor-Related Apoptosis-Inducing Ligand Signaling and Arginine Deprivation in Melanoma
Wu, C., You, M., Nguyen, D. M., Wangpaichitr, M., Li, Y., Feun, L. G., Kuo, M. T., & Savaraj, N. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22147628 · Cited by 12
Signaling Induced by Chronic Viral Hepatitis: Dependence and Consequences
Boulahtouf, Z., Virzì, A., Baumert, T. F., Verrier, E. R., & Lupberger, J. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23052787 · Cited by 13
Profiling Impaired Hepatic Endoplasmic Reticulum Glycosylation as a Consequence of Ethanol Ingestion
Galligan, J. J., Fritz, K. S., Tipney, H., McCullough, R. L., Roede, J. R., Shearn, C. T., Hunter, L., & Petersen, D. R. (2011) · Journal of Proteome Research · doi:10.1021/pr101101s · Cited by 12
Blood-based gene expression profile of oxidative stress and antioxidant genes for identifying surrogate markers of liver tissue injury in chronic hepatitis C patients
Shahid, M., Idrees, M., Butt, A. M., Raza, S. M., Amin, I., Rasul, A., & Afzal, S. (2020) · Archives of Virology · doi:10.1007/s00705-020-04564-z · Cited by 12
A Nudibranch Marine Extract Selectively Chemosensitizes Colorectal Cancer Cells by Inducing ROS-Mediated Endoplasmic Reticulum Stress
Ruiz-Torres, V., Forsythe, N., Pérez-Sánchez, A., Schaeybroeck, S. V., Barrajón‐Catalán, E., & Micol, V. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.625946 · Cited by 11
Mitochondria inter-organelle relationships in cancer protein aggregation
Genovese, I., Fornetti, E., & Ruocco, G. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.1062993 · Cited by 11
Evaluating the effect of basic fibroblast growth factor on the progression of NASH disease by inhibiting ceramide synthesis and ER stress-related pathways
Rahimi, S., Angaji, S. A., Majd, A., Hatami, B., & Baghaei, K. (2023) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2023.175536 · Cited by 11
Acrylonitrile induced cell cycle arrest and apoptosis by promoting the formation of reactive oxygen species in human choriocarcinoma cells
Kim, S.-M., & Choi, K. (2020) · The Journal of Toxicological Sciences · doi:10.2131/jts.45.713 · Cited by 10
The endoplasmic reticulum participated in drug metabolic toxicity
Huang, Q., Chen, Y., Zhang, Z., Xue, Z., Hua, Z., Luo, X., Yang, L., Lu, C. C., Lü, A., & Liu, Y. (2022) · Cell Biology and Toxicology · doi:10.1007/s10565-021-09689-8 · Cited by 9
β Cell Stress and Endocrine Function During T1D: What Is Next to Discover?
Vived, C., Lee-Papastavros, A., Pereira, J. A. D. S., Peng, Y., & MacDonald, T. L. (2023) · Endocrinology · doi:10.1210/endocr/bqad162 · Cited by 10
Cell defense systems against oxidative stress and endoplasmic reticulum stress: Mechanisms of regulation and the effect of hepatitis C virus
Smirnova, O., Ivanov, A., Ivanova, O., Valuev-Elliston, V., & Kochetkov, S. (2011) · Molecular Biology · doi:10.1134/s0026893311010122 · Cited by 11
Endothelium and Arterial Hypertension
Consolim‐Colombo, F. M., & Bortolotto, L. A. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-812348-5.00028-3 · Cited by 10
Induction of the nicotinamide riboside kinase NAD+ salvage pathway in a model of sarcoplasmic reticulum dysfunction
Doig, C. L., Zielinska, A. E., Fletcher, R. S., Oakey, L. A., Elhassan, Y., Garten, A., Cartwright, D., Heising, S., Alsheri, A., Watson, D. G., et al. (2020) · Skeletal Muscle · doi:10.1186/s13395-019-0216-z · Cited by 13
Effects of a Red Orange and Lemon Extract in Obese Diabetic Zucker Rats: Role of Nicotinamide Adenine Dinucleotide Phosphate Oxidase
Damiano, S., Lauritano, C., Longobardi, C., Andretta, E., Elagoz, A. M., Rapisarda, P., Iorio, M. D., Florio, S., & Ciarcia, R. (2020) · Journal of Clinical Medicine · doi:10.3390/jcm9051600 · Cited by 10
Reactive Oxygen Species and Antioxidants
Tiwari, S. (2017) · Wiley eBooks · doi:10.1002/9781119324928.ch10 · Cited by 10
The Roles of Calcium Ions in Parkinson’s Disease: Calcium Channel Inhibitors as a Novel Agents?
Alam, M. R., Raj, K., & Singh, S. (2022) · Journal of Molecular Pathology · doi:10.3390/jmp3040021 · Cited by 9
Effects of hypoestrogenism and/or hyperaldosteronism on myocardial remodeling in female mice
Rouet‐Benzineb, P., Merval, R., & Polidano, E. (2018) · Physiological Reports · doi:10.14814/phy2.13912 · Cited by 9
Oxidative Stress and Redox Modifications in Nanomaterial–Cellular Interactions
Zhang, T., Gaffrey, M. J., Qian, W., & Thrall, B. D. (2020) · Molecular and integrative toxicology · doi:10.1007/978-3-030-33962-3_8 · Cited by 9
Bioactive Compound Bisacurone in the Turmeric Extract (Turcuron) Prevents Non-alcoholic Fatty Liver Disease by Reduction of Lipogenesis
Gouthamchandra, K., Sudeep, H. V., Raj, A., Ramanaih, I., Siddappa, C., & Shyamprasad, K. (2021) · Indian Journal of Pharmaceutical Education and Research · doi:10.5530/ijper.55.1s.36 · Cited by 9
Mannan-binding lectin deficiency augments hepatic endoplasmic reticulum stress through IP3R-controlled calcium release
Chen, Y., Hu, M., Deng, F., Wang, P., Lin, J., Zheng, Z., Liu, Y., Dong, L., Lu, X., Chen, Z., et al. (2021) · Cell Calcium · doi:10.1016/j.ceca.2021.102477 · Cited by 9
Tricyclodecan-9-yl-Xanthogenate (D609): Mechanism of Action and Pharmacological Applications
Bhat, A. H., Dar, K. B., Khan, A., Alshahrani, S., Alshehri, S., Ghoneim, M. M., Alam, P., & Shakeel, F. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23063305 · Cited by 9
Proteomic analyses of brain tumor cell lines amidst the unfolded protein response
Redzic, J. S., Gomez, J., Hellwinkel, J. E., Anchordoquy, T. J., & Graner, M. W. (2016) · Oncotarget · doi:10.18632/oncotarget.10032 · Cited by 10
Autophagy, Oxidative Stress, and Redox Regulation
Ma, J., Yang, L., Ren, J. T., & Yang, J. Z. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-805253-2.00020-1 · Cited by 10
FDA-approved immunosuppressants targeting staphylococcal superantigens: mechanisms and insights
Krakauer, T. (2017) · ImmunoTargets and Therapy · doi:10.2147/itt.s125429 · Cited by 9
The Evolving Concept of Oxidative Stress
Fernandes, D. D. C., Bonatto, D., & Laurindo, F. R. M. (2010) · Humana Press eBooks · doi:10.1007/978-1-60761-600-9_1 · Cited by 8
Self-citation
Magnetic nanoparticles trigger cell proliferation arrest of neuro-2a cells and ROS-mediated endoplasmic reticulum stress response
Wang, P., Chen, C., Zeng, K., Pan, W., & Song, T. (2014) · Journal of Nanoparticle Research · doi:10.1007/s11051-014-2718-2 · Cited by 8
Comparative transcriptomics across populations offers new insights into the evolution of thermal resistance in marine snails
Wang, W., Hui, J. H. L., Williams, G. A., Cartwright, S. R., Tsang, L. M., & Chu, K. H. (2016) · Marine Biology · doi:10.1007/s00227-016-2873-3 · Cited by 8
Paving the Road Toward Exploiting the Therapeutic Effects of Ginsenosides: An Emphasis on Autophagy and Endoplasmic Reticulum Stress
Ashrafizadeh, M., Tavakol, S., Mohammadinejad, R., Ahmadi, Z., Yaribeygi, H., Jamialahmadi, T., Johnston, T. P., & Sahebkar, A. (2021) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-64872-5_12 · Cited by 8
Effect of protein oxidation on the quality of abalone (Haliotis discus hannai) during frozen storage under different packaging conditions
Zhu, S., Zhang, C. Y., Liu, Y., Jiang, D., Zhao, Q., Mao, X., Hu, X., & Jiang, B. (2025) · Food Chemistry X · doi:10.1016/j.fochx.2025.102357 · Cited by 7
Glycolysis Aids in Human Lens Epithelial Cells’ Adaptation to Hypoxia
Huang, Y., Ping, X., Cui, Y., Yang, H., Bao, J., Yin, Q., Ailifeire, H., & Shentu, X. (2023) · Antioxidants · doi:10.3390/antiox12061304 · Cited by 7
Anti-oxidants as therapeutic agents for oxidative stress associated pathologies: future challenges and opportunities
Nandha, S. R., Checker, R., Patwardhan, R. S., Sharma, D., & Sandur, S. K. (2025) · Free Radical Research · doi:10.1080/10715762.2025.2450504 · Cited by 9
Biphasic Increases of Cell Surface Calreticulin Following Treatment with Mitoxantrone
Azuma, Y., Suzuki, K., Higai, K., Matsumoto, K., & Tada, S. (2020) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.b20-00319 · Cited by 7
Inhibition of Endoplasmic Reticulum Stress Improves Acetylcholine-Mediated Relaxation in the Aorta of Type-2 Diabetic Rats
Mustapha, S., Azemi, A. K., Ahmad, W. A. N. W., Rasool, A. H. G., Mustafa, M. R., & Mokhtar, S. S. (2022) · Molecules · doi:10.3390/molecules27165107 · Cited by 7
Lipoic acid, but not tempol, preserves vascular compliance and decreases medial calcification in a model of elastocalcinosis
Bassi, E., Liberman, M., Martinatti, M. K., Bortolotto, L. A., & Laurindo, F. R. M. (2014) · Brazilian Journal of Medical and Biological Research · doi:10.1590/1414-431x20133193 · Cited by 7
Self-citation
Photoinduced electron transfer reaction in mitochondria for spatiotemporal selective photo-oxidation of lipids by donor/acceptor linked molecules
Takano, Y., Hanai, E., & Imahori, H. (2017) · Nanoscale · doi:10.1039/c7nr04919f · Cited by 7
Polymorphisms of the Gene Encoding Cytochrome b-245 Beta Chain of NADPH Oxidase: Relationship with Redox Homeostasis Markers and Risk of Type 2 Diabetes Mellitus
Azarova, I. E., Klyosova, E. Y., Коломоец, И. И., Азарова, В. А., Ivakin, V. E., Konoplya, A. I., & Polonikov, A. (2020) · Russian Journal of Genetics · doi:10.1134/s1022795420070017 · Cited by 6
Molecular Underpinning of Treatment-Resistant Schizophrenia: A Putative Different Neurobiology from Treatment-Responsive Schizophrenia
Barone, A., Vellucci, L., Ciccarelli, M., Matrone, M., Simone, G. D., Iannotta, F., Iasevoli, F., & de Bartolomeis, A. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26178598 · Cited by 8
Evolutionary conservation and metabolic significance of autophagy in algae.
Laude, J., Scarsini, M., Nef, C., & Bowler, C. (2024) · PubMed Central · doi:10.1098/rstb.2023.0368 · Cited by 6
Amending in vitro culture condition to overcome oxidative stress in assisted reproduction techniques (ART)
Zavareh, S., Talebi, A., & Hasanzadeh, H. (2015) · Archives of Advances in Biosciences · doi:10.22037/jps.v6i2.9012 · Cited by 6
Mitochondria-targeted antioxidant, mitoQ protects hepatic tissue from N-nitrosodiethylamine-induced damage by modulating mitochondrial function and redox status
Qsee, H. S., Shetty, S., De, S., & Bharati, S. (2024) · Advances in Redox Research · doi:10.1016/j.arres.2024.100108 · Cited by 5
USP5-induced deubiquitination of P4HB alleviates ER stress-mediated apoptosis in intestinal ischemia/reperfusion
Ning, S., Zhong, P., Zhao, X., Zhao, Y., Yang, F., Chen, Z., Zhang, F., Guo, S., Wu, Y., Yao, J., et al. (2025) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-025-05752-3 · Cited by 5
Endoplasmic Reticulum Stress and Unfolded Protein Response Sensor ERN1 Regulates Organic Dust Induction of Lung Inflammation
Kusampudi, S., Meganathan, V., & Boggaram, V. (2025) · FASEB bioAdvances · doi:10.1096/fba.2025-00069 · Cited by 4
Chronic Epinephrine-Induced Endoplasmic Reticulum and Oxidative Stress Impairs Pancreatic β-Cells Function and Fate
Zhang, R., Yao, B., Li, R., Limesand, S. W., Zhao, Y., & Chen, X. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25137029 · Cited by 5
Phosphorylation of eIF2α suppresses the impairment of GSH/NADPH homeostasis and mitigates the activation of cell death pathways, including ferroptosis, during ER stress
Hiền, L. T. T., Kim, Y. H., Kim, M. J., Hyun, S. H., Kim, H., Chung, S. W., Joe, Y., Chung, H., Shin, D., & Back, S. H. (2025) · Molecules and Cells · doi:10.1016/j.mocell.2025.100210 · Cited by 5
An adenosine derivative promotes mitochondrial supercomplexes reorganization and restoration of mitochondria structure and bioenergetics in a diethylnitrosamine-induced hepatocellular carcinoma model
García-Carrillo, R., Molina-Pelayo, F. A., Zárate-López, D., Cabrera-Aguilar, A., Ortega-Domínguez, B., Domínguez-López, M., Chiquete‐Félix, N., Dagnino-Acosta, A., Velasco-Loyden, G., Chávez, E., et al. (2024) · Scientific Reports · doi:10.1038/s41598-024-56306-9 · Cited by 5
NAD(P)H oxidase isoforms as therapeutic targets for diabetic complications
Gray, S. P., Jha, J. C., Marco, E. D., & Jandeleit-Dahm, K. A. M. (2014) · Expert Review of Endocrinology & Metabolism · doi:10.1586/17446651.2014.887984 · Cited by 5
Oxidative Stress and Cardiac Muscle
Maejima, Y., Zablocki, D., & Sadoshima, J. (2012) · Elsevier eBooks · doi:10.1016/b978-0-12-381510-1.00023-5 · Cited by 5
Molecular Basis for Pathogenesis of Steatohepatitis: Contemporary Understanding and New Insights
Parkash, O., & Saeed, S. (2018) · InTech eBooks · doi:10.5772/intechopen.71405 · Cited by 5
No evidence of the unfolded protein response in the placenta of two rodent models of preeclampsia and intrauterine growth restriction
Denkl, B., Cordasic, N., Huebner, H., Menendez‐Castro, C., Schmidt, M., Mocker, A., Woelfle, J., Hartner, A., & Fahlbusch, F. B. (2021) · Biology of Reproduction · doi:10.1093/biolre/ioab087 · Cited by 5
Selective activation of antioxidant resources and energy deficiency in Marinesco–Sjögren syndrome fibroblasts as an adaptive biological response to Sil1 loss
Panella, V., Potenza, F., Tatone, C., Speranza, L., Amicarelli, F., & Sallese, M. (2025) · Scientific Reports · doi:10.1038/s41598-025-96467-9 · Cited by 4
Exploring the Endoplasmic Reticulum's Role in Alzheimer's Disease and Its Potential as a Therapeutic Target
Saleh, R. O., Jabir, M. S., Mohammed, J. S., Ahmad, I. S., Ganesan, S., Shankhyan, A., Nanda, A., Ray, S., Zwamel, A. H., & Hussein, A. R. (2025) · Journal of Biochemical and Molecular Toxicology · doi:10.1002/jbt.70405 · Cited by 6
ERO1α as a Potential Drug Target for Breast Cancer: A Systematic Review of Current Evidence
Khojayeva, K., Moldasheva, A., & Aljofan, M. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms262110276 · Cited by 4
Heavy metal toxicity as a driver of endoplasmic reticulum stress and dysfunction
Ghosh, P., Murumulla, L., Das, S., Alavala, S., & Challa, S. (2026) · FEBS Journal · doi:10.1111/febs.70527 · Cited by 5
The signaling pathway of NADPH oxidase and its role in glomerular diseases
Mao, S., & Huang, S. (2013) · Journal of Receptors and Signal Transduction · doi:10.3109/10799893.2013.848892 · Cited by 4
Four components of the conjugated redox system in organisms: Carbon, nitrogen, sulfur, oxygen
Tereshina, E. V., Laskavy, V. N., & Ivanenko, S. I. (2015) · Biochemistry (Moscow) · doi:10.1134/s0006297915090096 · Cited by 4
Role of NADPH Oxidase in Beta Cell Dysfunction
Weaver, J. R., & Taylor, D. (2014) · Springer eBooks · doi:10.1007/978-94-007-6884-0_46-3 · Cited by 4
Yeast MED2 is involved in the endoplasmic reticulum stress response and modulation of the replicative lifespan
Zhao, W., Liu, J., Guo, F., & Liu, X. (2020) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2020.111381 · Cited by 4
Calcium and redox homeostasis in Alzheimer's disease: a focus on the endoplasmic reticulum
(2015) · Therapeutic Targets for Neurological Diseases · doi:10.14800/ttnd.428 · Cited by 4
Protective effects of Polygonum cuspidatum bioactive constituents against cholestatic liver injury: A mechanistic review
Zhang, Z., Yang, X., Fu, Y., Wei, H., Chen, Y., Dai, A., Zhou, X., Wan, J., & Chen, W. (2025) · Fitoterapia · doi:10.1016/j.fitote.2025.106938 · Cited by 3
Importance of Oxidative Stress Mechanism in Reproductive Functions and Infertility
Onaolapo, M. C., Nzekwe, S. C., Okeleji, L. O., Amos, V., Ajayi, O. H., & Ajayi, A. F. (2022) · Biochemistry · doi:10.5772/intechopen.107839 · Cited by 3
Investigating the differences in metabolism, and the unfolded protein and apoptosis gene responses in two strains of the Pacific white shrimp, Penaeus vannamei Boone, 1931 (Decapoda, Penaeoidea) under ammonia stress
Wang, J., & Liu, J. (2023) · Crustaceana · doi:10.1163/15685403-bja10275 · Cited by 3
Relationship between cognitive dysfunction and urinary 8-OHdG levels in children with obstructive sleep apnea
Chen, B., Ji, J., Lv, M., Xu, X., & Wang, Y. (2025) · Frontiers in Neurology · doi:10.3389/fneur.2025.1502906 · Cited by 3
Effects of M. tuberculosis and HIV-1 infection on in vitro blood-brain barrier function
Proust, A. M., Wilkinson, K. A., & Wilkinson, R. J. (2025) · Journal of Neuroinflammation · doi:10.1186/s12974-025-03467-7 · Cited by 6
Cytotoxin-induced NADPH oxides activation: roles in regulation of cell death
Zhang, Y., Bi, X., & Jiang, F. (2015) · Archives of Toxicology · doi:10.1007/s00204-015-1476-y · Cited by 3
Oxidative Stress in Neonatal Lung Diseases
Teng, R. (2019) · Springer eBooks · doi:10.1007/978-981-13-8413-4_3 · Cited by 4
ER Stress Signaling Pathways in Cell Survival and Death
Verfaillie, T., Jäger, R., Samali, A., & Agostinis, P. (2012) · Springer eBooks · doi:10.1007/978-94-007-4351-9_3 · Cited by 3
Association between NAD(P)H oxidase p22phox gene variants and acute myocardial infarction in a Han Chinese population
Xu, H., Ma, S., Tang, F., Chen, Y., Zhou, H., Chen, M., Wang, B., Liu, X., & Xie, X. (2015) · Herz · doi:10.1007/s00059-015-4391-3 · Cited by 3
Endoplasmic Reticulum Stress during Mammalian Follicular Atresia
Torres‐Ramírez, N., Ortiz-Hernández, R., Escobar-Sánchez, M. L., Echeverría, O. M., & Vázquez‐Nin, G. H. (2019) · IntechOpen eBooks · doi:10.5772/intechopen.82687 · Cited by 3
Molecular Targets and Novel Therapeutics to Target Oxidative Stress in Cardiovascular Diseases
Dhawan, V., Bakshi, C., & Rather, R. A. (2019) · Springer eBooks · doi:10.1007/978-981-13-8273-4_4 · Cited by 3
Oxidase Interactions in Cardiovascular Disease
Youn, J. Y., Siu, K. L., Li, Q., Harrison, D. G., & Cai, H. “. (2014) · Springer eBooks · doi:10.1007/978-3-642-30018-9_43 · Cited by 3
Integrative chemogenomic analysis identifies small molecules that partially rescue ΔF508‐CFTR for cystic fibrosis
Hodos, R. A., Strub, M. D., Ramachandran, S. S., Meleshkevitch, E. A., Boudko, D. Y., Bridges, R. J., Dudley, J. T., & McCray, P. B. (2021) · CPT Pharmacometrics & Systems Pharmacology · doi:10.1002/psp4.12626 · Cited by 3
Reactive Species in Biological Systems
Villamena, F. A. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-420017-3.00002-5 · Cited by 2
Role of NADPH Oxidase in β Cell Dysfunction
Weaver, J. R., & Taylor, D. (2014) · Springer eBooks · doi:10.1007/978-94-007-6686-0_46 · Cited by 2
Carnosine supplementation and retinal oxidative parameters in a high-calorie diet rat model
Torres, R. J. D. A., Moreto, F., Luchini, A., Torres, R. J. D. A., Longo, S. P., Pinho, R. A., Nagashima, S., de Noronha, L., Ferron, A. J. T., Silva, C. C. V. D. A., et al. (2023) · BMC Ophthalmology · doi:10.1186/s12886-023-03255-y · Cited by 2
Serine protease inhibitor AEBSF(4-(2-aminoethyl)-benzenesulfonyl fluoride) decreased ischemic brain injury through inhibiting endoplasmic reticulum stress, oxidative stress, and autophagy in rats
An, Q., Zhu, Y., Shi, W., Li, W., Yang, X., Huang, M., Li, Y., & Zhao, Y. (2024) · Brain Research · doi:10.1016/j.brainres.2024.149382 · Cited by 2
TXNIP is a Mediator of ER Stress-Induced β-Cell Inflammation and Apoptosis: A Dissertation
Oslowski, C. M. (2012) · The Journal of the American Medical Association (JAMA) Network (American Medical Association) · doi:10.13028/mj81-rb58 · Cited by 2
Cellular Inflammatory Responses
Land, W. G. (2018) · Springer eBooks · doi:10.1007/978-3-319-78655-1_22 · Cited by 2
New properties of vitamin B6 or pyridoxine in experimental oxidative stress in the brain
Danielyan, K. E., & Chailyan, S. G. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-811907-5.00017-8 · Cited by 2
Protective Effects of Safranal Against Selenite-Induced Cataract in Rats
Mahdi, F. A., & Zalzala, M. H. (2021) · Iraqi Journal of Pharmaceutical Sciences · doi:10.31351/vol30iss1pp196-203 · Cited by 2
The oxidative and inflammatory nature of age-related macular degeneration
Torres, R. J. D. A., Torres, R. J. D. A., Luchini, A., & Ferreira, A. L. A. (2022) · Journal of Clinical Ophthalmology and Research · doi:10.4103/jcor.jcor_268_20 · Cited by 2
Sleep Loss and the Unfolded Protein Response
Naidoo, N. N. (2022) · Translational medicine research · doi:10.1007/978-94-024-2168-2_7 · Cited by 3
ER Stress and Inflammation
Garg, A. D., Kaczmarek, A., Krysko, D. V., & Vandenabeele, P. (2012) · Springer eBooks · doi:10.1007/978-94-007-4351-9_11 · Cited by 2
Contribution of Insulin Resistance in Pathogenesis of Alzheimer Disease
Erol, A. (2013) · Wiley eBooks · doi:10.1002/9781118395318.ch3 · Cited by 2
Carnosine, a therapeutic potential for critical limb ischemic.
Boakye, A. A. (2016) · doi:10.18297/etd/2517 · Cited by 2
The role of oxidative stress in C. elegans aging
Thamsen, M. (2011) · Gutenberg Open Science · doi:10.25358/openscience-4772 · Cited by 2
Redox Systems of the Plant Cell Vacuole Compared to Redox Systems of Other Subcellular Structures
Pradedova, E. V. (2025) · Russian Journal of Plant Physiology · doi:10.1134/s1021443725603295 · Cited by 1
Sources of ROS Production in Plants Under Normal and Stressed Conditions
Amiri, H. (2025) · Springer eBooks · doi:10.1007/978-981-95-3377-0_10 · Cited by 1
Nrf2 maintains reactive oxygen species at an optimal level during endoplasmic reticulum stress in HT22 cells
Hirata, Y., Kato, K., Sakaida, Y., Watanabe, H., & Kamatari, Y. O. (2026) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2026.151536 · Cited by 1
Organelle Stress and mTOR in Aging-Associated Inflammation
Pani, G. (2013) · Elsevier eBooks · doi:10.1016/b978-0-12-397803-5.00014-9 · Cited by 1
Reactive Oxygen Species in Melanoma Etiology
Liu, F. (2016) · CRC Press eBooks · doi:10.1201/b20228-25 · Cited by 1
Endoplasmic reticulum stress and associated ROS in disease pathophysiology applications
Madkour, L. H. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-822481-6.00011-6 · Cited by 2
Stress Hyperglycemia: A Problem that Cannot be Ignored
Peng, D., Zhang, Y., Cao, X., & Pu, J. (2022) · Journal of Endocrinology Research · doi:10.30564/jer.v4i1.3293 · Cited by 1
Post-treatment with apocynin at a lower dose regulates the UPR branch of eIF2α and XBP-1 pathways after stroke
Nakka, V. P., Gogada, R., Simhadri, P. K., Qadeer, M. A., & Phanithi, P. B. (2022) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2022.02.003 · Cited by 1
Rosacea Therapy
Plewig, G., Melnik, B. C., & Chen, W. (2019) · Springer eBooks · doi:10.1007/978-3-319-49274-2_15 · Cited by 1

Authors: Santos, C. X. C., Tanaka, L. Y., Wosniak, J., & Laurindo, F. R. M.
Affiliations: Universidade de São Paulo (BR)
ORCID: Tanaka, Leonardo Y.
Laurindo, Francisco R.M.
Venue: Antioxidants & Redox Signaling
Publisher: SAGE Publications
Published: 2009-10
Volume: 11
Issue: 10
Pages: 2409-2427
ISSN: 1523-0864 (ISSN-L)
1557-7716
DOI: 10.1089/ars.2009.2625
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

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

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

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks