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

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
Nox proteins in signal transduction
Brown, D., & Griendling, K. K. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.07.023 · Cited by 837
Cross talk between mitochondria and NADPH oxidases
Dikalov, S. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.06.033 · Cited by 783
The role of fructose in the pathogenesis of NAFLD and the metabolic syndrome
Lim, J. S., Mietus-Snyder, M., Valente, A., Schwarz, J.-M., & Lustig, R. H. (2010) · Nature Reviews Gastroenterology & Hepatology · doi:10.1038/nrgastro.2010.41 · Cited by 771
New insights into the mechanism of aminoglycoside nephrotoxicity: an integrative point of view
López-Novoa, J. M., Quirós, Y., Vicente-Vicente, L., Morales, A. I., & López-Hernández, F. J. (2010) · Kidney International · doi:10.1038/ki.2010.337 · Cited by 756
Role of peroxisomes in ros/rns-metabolism: Implications for human disease
Fransen, M., Nordgren, M., Wang, B., & Apanasets, O. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2011.12.001 · Cited by 644
A Molecular Web: Endoplasmic Reticulum Stress, Inflammation, and Oxidative Stress
Chaudhari, N., Talwar, P., Parimisetty, A., Lefebvre dâ€™Hellencourt, C., & Ravanan, P. (2014) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2014.00213 · Cited by 600
Cell death and diseases related to oxidative stress: 4-hydroxynonenal (HNE) in the balance
Dalleau, S., Baradat, M., Guéraud, F., & Huc, L. (2013) · Cell Death & Differentiation · doi:10.1038/cdd.2013.138 · Cited by 580
Oxidative Stress and Hypertension
Griendling, K. K., Camargo, L. L., Rios, F. J. O., Alves-Lopes, R., Montezano, A. C. I., & Touyz, R. M. (2021) · Circulation Research · doi:10.1161/circresaha.121.318063 · Cited by 618
NADPH Oxidase-Mediated Redox Signaling: Roles in Cellular Stress Response, Stress Tolerance, and Tissue Repair
Jiang, F., Zhang, Y., & Dusting, G. J. (2011) · Pharmacological Reviews · doi:10.1124/pr.110.002980 · Cited by 585
Sleep Loss Can Cause Death through Accumulation of Reactive Oxygen Species in the Gut
Vaccaro, A., Kaplan Dor, Y., Nambara, K., Pollina, E. A., Lin, C., Greenberg, M. E., & Rogulja, D. (2020) · Cell · doi:10.1016/j.cell.2020.04.049 · Cited by 541
Endoplasmic Reticulum and the Unfolded Protein Response
Bravo, R., Parra, V., Gatica, D., Rodriguez, A. E., Torrealba, N., Paredes, F., Wang, Z. V., Antonio Zorzano, A., Hill, J. A., Jaimovich, E., et al. (2013) · International review of cytology · doi:10.1016/b978-0-12-407704-1.00005-1 · Cited by 575
Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation
Tejero, J., Shiva, S., & Gladwin, M. T. (2019) · Physiological Reviews · doi:10.1152/physrev.00036.2017 · Cited by 541
Regulation of Signal Transduction by Reactive Oxygen Species in the Cardiovascular System
Brown, D., & Griendling, K. K. (2015) · Circulation Research · doi:10.1161/circresaha.116.303584 · Cited by 498
Reactive oxygen species and vascular biology: implications in human hypertension
Touyz, R. M., & Briones, A. M. (2010) · Hypertension Research · doi:10.1038/hr.2010.201 · Cited by 488
H 2 S-Induced Sulfhydration of the Phosphatase PTP1B and Its Role in the Endoplasmic Reticulum Stress Response
Krishnan, N., Fu, C., Pappin, D., & Tonks, N. K. (2011) · Science Signaling · doi:10.1126/scisignal.2002329 · Cited by 455
Molecular machinery and interplay of apoptosis and autophagy in coronary heart disease
Dong, Y., Chen, H., Gao, J., Liu, Y., Li, J., & Wang, J. (2019) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2019.09.001 · Cited by 444
The relationship of sugar to population-level diabetes prevalence: an econometric analysis of repeated cross-sectional data
Basu, S., Yoffe, P., Hills, N., & Lustig, R. H. (2013) · PLoS ONE · doi:10.1371/journal.pone.0057873 · Cited by 435
“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].”
Background
An Involvement of Oxidative Stress in Endoplasmic Reticulum Stress and Its Associated Diseases
Bhandary, B., Marahatta, A., Kim, H., & Chae, H. (2012) · International Journal of Molecular Sciences · doi:10.3390/ijms14010434 · Cited by 418
Understanding the immunosuppressive microenvironment of glioma: mechanistic insights and clinical perspectives
Lin, H., Liu, C., Hu, A.-K., Zhang, D., Yang, H., & Mao, Y. Q. (2024) · Journal of Hematology & Oncology · doi:10.1186/s13045-024-01544-7 · Cited by 462
Oxidative Stress as a Critical Factor in Nonalcoholic Fatty Liver Disease Pathogenesis
Spahis, S., DELVIN, E. E., Borys, J.-M., & Levy, E. H. (2016) · Antioxidants and Redox Signaling · doi:10.1089/ars.2016.6776 · Cited by 394
The endoplasmic reticulum stress response in aging and age-related diseases
Brown, M. K., & Naidoo, N. N. (2012) · Frontiers in Physiology · doi:10.3389/fphys.2012.00263 · Cited by 388
ER stress regulates myeloid-derived suppressor cell fate through TRAIL-R-mediated apoptosis.
Condamine, T., Kumar, V., Ramachandran, I. R., Youn, J.-I., Celis, E., Finnberg, N., El-Deiry, W. S., Winograd, R., Vonderheide, R. H., English, N. R., et al. (2014) · Journal of Clinical Investigation · doi:10.1172/jci74056 · Cited by 365
An Unexpected Role for Uric Acid as an Inducer of T Helper 2 Cell Immunity to Inhaled Antigens and Inflammatory Mediator of Allergic Asthma
Kool, M., Willart, M. A. M., van Nimwegen, M., Bergen, I. M., Pouliot, P., Virchow, J. C., Jr., Rogers, N. C., Osorio, F., Sousa, C. R. E., Hammad, H., et al. (2011) · Immunity · doi:10.1016/j.immuni.2011.03.015 · Cited by 360
Regulation of Pichia pastoris promoters and its consequences for protein production
Vogl, T. J., & Glieder, A. (2012) · New Biotechnology · doi:10.1016/j.nbt.2012.11.010 · Cited by 333
The Role of Oxidative Stress in Physiopathology and Pharmacological Treatment with Pro- and Antioxidant Properties in Chronic Diseases
García-Sánchez, A., Miranda‐Díaz, A. G., & Cardona-Muñóz, E. G. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/2082145 · Cited by 369
Redox signaling in cardiac myocytes
Santos, C. X. C., Anilkumar, N. P., Zhang, M., Brewer, A. C., & Shah, A. M. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.01.003 · Cited by 325
Self-citation
Bidirectional crosstalk between endoplasmic reticulum stress and mTOR signaling
Appenzeller‐Herzog, C., & Hall, M. N. (2012) · Trends in Cell Biology · doi:10.1016/j.tcb.2012.02.006 · Cited by 324
Endoplasmic reticulum stress and Oxidative stress in the pathogenesis of Non-alcoholic fatty liver disease
Ashraf, N. U., & Sheikh, T. A. (2015) · Free Radical Research · doi:10.3109/10715762.2015.1078461 · Cited by 312
What is metabolic syndrome, and why are children getting it?
Weiss, R., Bremer, A. A., & Lustig, R. H. (2013) · Annals of the New York Academy of Sciences · doi:10.1111/nyas.12030 · Cited by 314
Role of endoplasmic reticulum stress in the pathogenesis of nonalcoholic fatty liver disease
Zhang, X.-Q. (2014) · World Journal of Gastroenterology · doi:10.3748/wjg.v20.i7.1768 · Cited by 302
Endoplasmic Reticulum Stress and Oxidative Stress: A Vicious Nexus Implicated in Bowel Disease Pathophysiology
Chong, W. C., Shastri, M. D., & Eri, R. D. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18040771 · Cited by 300
Ammonia exposure induces oxidative stress, endoplasmic reticulum stress and apoptosis in hepatopancreas of pacific white shrimp (Litopenaeus vannamei)
Liang, Z., Liu, R., Zhao, D., Wang, L., Sun, M., Wang, M., & Song, L. (2016) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2016.05.009 · Cited by 285
Reactive Oxygen Species and Autophagy in Plants and Algae
Pérez‐Pérez, M. E., Lemaire, S. D., & Crespo, J. L. (2012) · PLANT PHYSIOLOGY · doi:10.1104/pp.112.199992 · Cited by 269
Oxidative Stress in Pulmonary Fibrosis
Otoupalova, E., Smith, S., Cheng, G., & Thannickal, V. J. (2020) · Comprehensive physiology · doi:10.1002/cphy.c190017 · Cited by 312
Protein disulfide isomerase in redox cell signaling and homeostasis
Laurindo, F. R. M., Pescatore, L. A., & Fernandes, D. C. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.02.037 · Cited by 258
Self-citation
Pro-inflammatory hepatic macrophages generate ROS through NADPH oxidase 2 via endocytosis of monomeric TLR4–MD2 complex
Kim, S. Y., Jeong, J., Kim, S. J., Seo, W., Kim, M., Choi, W., Yoo, W., Lee, J. H., Shim, Y., Yi, H., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-02325-2 · Cited by 264
An Integrative Overview on the Mechanisms Underlying the Renal Tubular Cytotoxicity of Gentamicin
Quirós, Y., Vicente-Vicente, L., Morales, A. I., López-Novoa, J. M., & López-Hernández, F. J. (2010) · Toxicological Sciences · doi:10.1093/toxsci/kfq267 · Cited by 257
Insulin Resistance and Heart Failure
Aroor, A. R., Mandavia, C. H., & Sowers, J. R. (2012) · Heart Failure Clinics · doi:10.1016/j.hfc.2012.06.005 · Cited by 265
Oxidases and peroxidases in cardiovascular and lung disease: New concepts in reactive oxygen species signaling
Ghouleh, I. A., Khoo, N. K. H., Knaus, U. G., Griendling, K. K., Touyz, R. M., Thannickal, V. J., Barchowsky, A., Nauseef, W. M., Kelley, E. E., Bauer, P. M., et al. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.06.011 · Cited by 252
Cadmium and cellular signaling cascades: interactions between cell death and survival pathways
Thévenod, F., & Lee, W. (2013) · Archives of Toxicology · doi:10.1007/s00204-013-1110-9 · Cited by 254
Crosstalk Between Endoplasmic Reticulum Stress, Oxidative Stress, and Autophagy: Potential Therapeutic Targets for Acute CNS Injuries
Nakka, V. P., Phanithi, P.-B., & Vemuganti, R. (2014) · Molecular Neurobiology · doi:10.1007/s12035-014-9029-6 · Cited by 246
The many roles of NOX2 NADPH oxidase-derived ROS in immunity
Lam, G. Y., Huang, J., & Brumell, J. H. (2010) · Seminars in Immunopathology · doi:10.1007/s00281-010-0221-0 · Cited by 251
Ionizing radiation-induced oxidative stress, epigenetic changes and genomic instability: The pivotal role of mitochondria
Szumiel, I. (2014) · International Journal of Radiation Biology · doi:10.3109/09553002.2014.934929 · Cited by 240
Autophagy Signaling Through Reactive Oxygen Species
Huang, J., Lam, G. Y., & Brumell, J. H. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3554 · Cited by 228
Unfolding the Interactions between Endoplasmic Reticulum Stress and Oxidative Stress
Ong, G., & Logue, S. E. (2023) · Antioxidants · doi:10.3390/antiox12050981 · Cited by 228
Endoplasmic Reticulum Stress in Nonalcoholic Fatty Liver Disease
Pagliassotti, M. J. (2012) · Annual Review of Nutrition · doi:10.1146/annurev-nutr-071811-150644 · Cited by 222
Protein disulfide isomerase a multifunctional protein with multiple physiological roles
Khan, H. A., & Mutus, B. (2014) · Frontiers in Chemistry · doi:10.3389/fchem.2014.00070 · Cited by 226
Endoplasmic reticulum proteostasis impairment in aging
Martínez, G., Duran-Aniotz, C. A., Cabral‐Miranda, F., Vivar, J. P., & Hetz, C. A. (2017) · Aging Cell · doi:10.1111/acel.12599 · Cited by 213
Origin and Consequences of Necroinflammation
Sarhan, M., Land, W. G., Tonnus, W., Hugo, C., & Linkermann, A. (2018) · Physiological Reviews · doi:10.1152/physrev.00041.2016 · Cited by 217
Oxidative protein folding in the endoplasmic reticulum: Tight links to the mitochondria-associated membrane (MAM)
Simmen, T., Lynes, E. M., Gesson, K., & Thomas, G. (2010) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2010.04.009 · Cited by 217
Nanosecond-Pulsed DBD Plasma-Generated Reactive Oxygen Species Trigger Immunogenic Cell Death in A549 Lung Carcinoma Cells through Intracellular Oxidative Stress
Lin, A. G., Truong, B., Patel, S. H., Kaushik, N. K., Choi, E. H., Fridman, G., Fridman, A., & Miller, V. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18050966 · Cited by 203
Gentamicin nephrotoxicity in animals: current knowledge and future perspectives
Randjelović, P. J., Veljković, S., Stojiljković, N. I., Sokolovic, D. T., & Ilić, I. (2017) · EXCLI journal · doi:10.17179/excli2017-165 · Cited by 198
Free fatty acids as modulators of the NLRP3 inflammasome in obesity/type 2 diabetes
Legrand-Poels, S., Esser, N., L’homme, L., Scheen, A., Paquot, N., & Piette, J. (2014) · Biochemical Pharmacology · doi:10.1016/j.bcp.2014.08.013 · Cited by 194
Role of the ERO1-PDI interaction in oxidative protein folding and disease
Shergalis, A. G., Hu, S., Bankhead, A., & Neamati, N. (2020) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2020.107525 · Cited by 202
tRNA modifications regulate translation during cellular stress
Gu, C., Begley, T. J., & Dedon, P. C. (2014) · FEBS Letters · doi:10.1016/j.febslet.2014.09.038 · Cited by 202
Toward a unifying hypothesis of metabolic syndrome
Bremer, A. A., Mietus-Snyder, M., & Lustig, R. H. (2012) · PEDIATRICS · doi:10.1542/peds.2011-2912 · Cited by 186
Nox NADPH Oxidases and the Endoplasmic Reticulum
Laurindo, F. R. M., Araujo, T. L. S., & Abrahão, T. B. (2014) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5605 · Cited by 194
Self-citation
Regulation of myocardial growth and death by NADPH oxidase
Maejima, Y., Kuroda, J., Matsushima, S., Ago, T., & Sadoshima, J. (2011) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2010.12.018 · Cited by 185
Redox controls UPR to control redox
Eletto, D., Chevet, É., Argon, Y., & Appenzeller‐Herzog, C. (2014) · Journal of Cell Science · doi:10.1242/jcs.153643 · Cited by 180
Bridges between mitochondrial oxidative stress, ER stress and mTOR signaling in pancreatic β cells
Wang, J., Yang, X., & Zhang, J. (2016) · Cellular Signalling · doi:10.1016/j.cellsig.2016.05.007 · Cited by 181
Deconvoluting the role of reactive oxygen species and autophagy in human diseases
Wen, X., Wu, J., Wang, F., Liu, B., Huang, C., & Wei, Y. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.07.013 · Cited by 181
Integration of the Unfolded Protein and Oxidative Stress Responses through SKN-1/Nrf
Glover-Cutter, K. M., Lin, S., & Blackwell, T. K. (2013) · PLoS Genetics · doi:10.1371/journal.pgen.1003701 · Cited by 171
The polymorphic and contradictory aspects of intermittent hypoxia
Almendros, I., Wang, Y., & Gozal, D. (2014) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00089.2014 · Cited by 174
Oltipraz upregulates the nuclear respiratory factor 2 alpha subunit (NRF2) antioxidant system and prevents insulin resistance and obesity induced by a high-fat diet in C57BL/6J mice
Yu, Z., Shao, W., Chiang, Y., Foltz, W. D., Zhang, Z., Ling, W., Fantus, I. G., & Jin, T. (2010) · Diabetologia · doi:10.1007/s00125-010-2001-8 · Cited by 173
Circadian rhythm regulates the function of immune cells and participates in the development of tumors
Zeng, Y., Guo, Z., Wu, M., Chen, F., & Chen, L. (2024) · Cell Death Discovery · doi:10.1038/s41420-024-01960-1 · Cited by 197
Intermittent Hypoxia-Induced Cognitive Deficits Are Mediated by NADPH Oxidase Activity in a Murine Model of Sleep Apnea
Nair, D., Dayyat, E. A., Zhang, S. X. L., Wang, Y., & Gozal, D. (2011) · PLoS ONE · doi:10.1371/journal.pone.0019847 · Cited by 172
Endoplasmic Reticulum Stress Induced by Toxic Elements—a Review of Recent Developments
Rana, S. V. S. (2019) · Biological Trace Element Research · doi:10.1007/s12011-019-01903-3 · Cited by 168
Reactive Oxygen Species Scavenging Nanomedicine for the Treatment of Ischemic Heart Disease
Zhang, Z., Dalan, R., Hu, Z., Wang, J., Chew, N., Poh, K. K., Tan, R., Soong, T. W., Dai, Y., Ye, L., et al. (2022) · Advanced Materials · doi:10.1002/adma.202202169 · Cited by 174
Involvement of Endoplasmic Reticulum Stress in Myofibroblastic Differentiation of Lung Fibroblasts
Baek, H. A., Kim, D. S., Park, H. S., Jang, K. Y., Kang, M. J., Lee, D. G., Moon, W. S., Chae, H., & Chung, M. J. (2011) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2011-0121oc · Cited by 165
Transplantation and Damage-Associated Molecular Patterns (DAMPs)
Land, W. G., Agostinis, P., Gasser, S., Garg, A. D., & Linkermann, A. (2016) · American Journal of Transplantation · doi:10.1111/ajt.13963 · Cited by 171
GPx8 peroxidase prevents leakage of H2O2 from the endoplasmic reticulum
Ramming, T., Hansen, H. G., Nagata, K., Ellgaard, L., & Appenzeller‐Herzog, C. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.01.018 · Cited by 161
Hepatitis C Virus Proteins Activate NRF2/ARE Pathway by Distinct ROS-Dependent and Independent Mechanisms in HUH7 Cells
Ivanov, A. V., Smirnova, O. A., Ivanova, O. N., Masalova, O. V., Kochetkov, S. N., & Isaguliants, M. G. (2011) · PLoS ONE · doi:10.1371/journal.pone.0024957 · Cited by 160
Inflammasomes, hormesis, and antioxidants in neuroinflammation: Role of NRLP3 in Alzheimer disease
Pennisi, M., Crupi, R., Di Paola, R., Ontario, M. L., Bella, R., Calabrese, E. J., Crea, R., Cuzzocrea, S., & Calabrese, V. (2017) · Journal of Neuroscience Research · doi:10.1002/jnr.23986 · Cited by 157
Added Fructose
DiNicolantonio, J. J., O’Keefe, J. H., & Lucan, S. C. (2015) · Mayo Clinic Proceedings · doi:10.1016/j.mayocp.2014.12.019 · Cited by 162
Glutathione- and non-glutathione-based oxidant control in the endoplasmic reticulum
Appenzeller‐Herzog, C. (2011) · Journal of Cell Science · doi:10.1242/jcs.080895 · Cited by 151
Regulation of Redox Signaling by Selenoproteins
Hawkes, W. C., & Alkan, Z. (2010) · Biological Trace Element Research · doi:10.1007/s12011-010-8656-7 · Cited by 151
The Tubulointerstitial Pathophysiology of Progressive Kidney Disease
Schnaper, H. W. (2017) · Advances in Chronic Kidney Disease · doi:10.1053/j.ackd.2016.11.011 · Cited by 148
Mechanism of endoplasmic reticulum stress-induced vascular endothelial dysfunction
Galán, M., Kassan, M., Kadowitz, P. J., Trebak, M., Belmadani, S., & Matrougui, K. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.02.009 · Cited by 150
Endoplasmic reticulum stress stimulates the release of extracellular vesicles carrying danger-associated molecular pattern (DAMP) molecules
Collett, G. P., Redman, C. W. G., Sargent, I. L., & Vatish, M. (2018) · Oncotarget · doi:10.18632/oncotarget.24158 · Cited by 148
Protein disulfide isomerases: Redox connections in and out of the endoplasmic reticulum
Soares Moretti, A. I., & Martins Laurindo, F. R. (2017) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2016.11.007 · Cited by 140
Self-citation
Mechanistic Connections between Endoplasmic Reticulum (ER) Redox Control and Mitochondrial Metabolism
Fan, Y., & Simmen, T. (2019) · Cells · doi:10.3390/cells8091071 · Cited by 145
Mutant p53-Associated Molecular Mechanisms of ROS Regulation in Cancer Cells
Cordani, M., Butera, G., Pacchiana, R., Masetto, F., Mullappilly, N., Riganti, C., & Donadelli, M. (2020) · Biomolecules · doi:10.3390/biom10030361 · Cited by 145
Endoplasmic Reticulum Stress and Nox-Mediated Reactive Oxygen Species Signaling in the Peripheral Vasculature: Potential Role in Hypertension
Santos, C. X. C., Nabeebaccus, A., Shah, A. M., Camargo, L. L., Filho, S. V., & Lopes, L. R. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5262 · Cited by 143
Self-citation
Toll-like receptor 4 regulates early endothelial activation during ischemic acute kidney injury
Chen, J., John, R., Richardson, J. A., Shelton, J. M., Zhou, X. J., Wang, Y., Wu, Q., Hartono, J. R., Winterberg, P. D., & Lu, C. Y. (2010) · Kidney International · doi:10.1038/ki.2010.381 · Cited by 143
Endoplasmic Reticulum Stress in Age-Related Macular Degeneration: Trigger for Neovascularization
Salminen, A., Kauppinen, A., Hyttinen, J. M. T., Toropainen, E., & Kaarniranta, K. (2010) · Molecular Medicine · doi:10.2119/molmed.2010.00070 · Cited by 141
Oxidative Protein Folding and the Quiescin–Sulfhydryl Oxidase Family of Flavoproteins
Kodali, V. K., & Thorpe, C. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3098 · Cited by 136
Disulphide production by Ero1α–PDI relay is rapid and effectively regulated
Appenzeller‐Herzog, C., Riemer, J., Zito, E., Chin, K., Ron, D., Spiess, M., & Ellgaard, L. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.203 · Cited by 134
Endoplasmic reticulum stress in cerebral ischemia
Xin, Q., Ji, B., Cheng, B., Wang, C., Liu, H., Chen, X., Chen, J., & Bai, B. (2014) · Neurochemistry International · doi:10.1016/j.neuint.2014.02.001 · Cited by 133
Advanced research on the health benefit of reduced water
Shirahata, S., Hamasaki, T., & Teruya, K. (2011) · Trends in Food Science & Technology · doi:10.1016/j.tifs.2011.10.009 · Cited by 132
Endoplasmic reticulum stress is sufficient for the induction of IL-1β production via activation of the NF-κB and inflammasome pathways
Kim, S., Joe, Y., Jeong, S. O., Zheng, M., Back, S. H., Park, S. W., Ryter, S. W., & Chung, H. (2013) · Innate Immunity · doi:10.1177/1753425913508593 · Cited by 132
Targeting Proteotoxic Stress in Cancer: A Review of the Role that Protein Quality Control Pathways Play in Oncogenesis
Ho, M., Kavanagh, E. L., Dunne, L., Dowling, P., Zhang, L., Lindsay, S., Bazou, D., Goh, C. Y., Hanley, C., Bianchi, G., et al. (2019) · Cancers · doi:10.3390/cancers11010066 · Cited by 132
Oxidative Stress and Redox Modulation Potential in Type 1 Diabetes
Delmastro-Greenwood, M. M., & Piganelli, J. D. (2011) · Clinical and Developmental Immunology · doi:10.1155/2011/593863 · Cited by 130
Reactive Oxygen and Nitrogen Species in Steatotic Hepatocytes: A Molecular Perspective on the Pathophysiology of Ischemia-Reperfusion Injury in the Fatty Liver
Reiniers, M. J., van Golen, R. F., van Gulik, T. M., & Heger, M. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5486 · Cited by 134
Experimental evidence for therapeutic potential of taurine in the treatment of nonalcoholic fatty liver disease
Gentile, C. L., Nivala, A. M., Gonzales, J. C., Pfaffenbach, K. T., Wang, D., Wei, Y., Jiang, H. L., Orlicky, D. J., Petersen, D. R., Pagliassotti, M. J., et al. (2011) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00677.2010 · Cited by 126
The Interplay Between Respiratory Supercomplexes and ROS in Aging
Genova, M. L., & Lenaz, G. (2015) · Antioxidants and Redox Signaling · doi:10.1089/ars.2014.6214 · Cited by 129

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