The DOI matches its Crossref record; 165 of the 165 references it cites were found in a registry or an index.
Crosstalk of reactive oxygen species and NF-κB signaling
Open accessAbstract
NF-κB proteins are a family of transcription factors that are of central importance in inflammation and immunity. NF-κB also plays important roles in other processes, including development, cell growth and survival, and proliferation, and is involved in many pathological conditions. Reactive Oxygen Species (ROS) are created by a variety of cellular processes as part of cellular signaling events. While certain NF-κB-regulated genes play a major role in regulating the amount of ROS in the cell, ROS have various inhibitory or stimulatory roles in NF-κB signaling. Here we review the regulation of ROS levels by NF-κB targets and various ways in which ROS have been proposed to impact NF-κB signaling pathways.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
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?
The cited source says what the claim attributes to it.
In the citing paper
“NF-κB can be co-regulated by multiple pathways including MAPK and PI3K/Akt to enhance transcriptional activity, thus promoting the expression of pro-inflammatory and pro-oxidant enzyme genes.239,243,244”
From Recent advances in Alzheimer's disease: Mechanisms, clinical trials and new drug development strategies. (2024) · cites this paper as [244]
In the citing paper
“The elevated concentrations of TNF-alpha, TNF-beta, LPS, IL-1beta and CD40 in peritoneal fluid in women with endometriosis promote processes such as adhesion, invasion, proliferation and angiogenesis that stimulate the development of the disease [155].”
From Endometriosis: Epidemiology, Classification, Pathogenesis, Treatment and Genetics (Review of Literature) (2021) · cites this paper as [155]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Shared Principles in NF-κB Signaling
Hayden, M. S., & Ghosh, S. (2008) · Cell · doi:10.1016/j.cell.2008.01.020 · Cited by 4,954
Oxidative stress: oxidants and antioxidants
Sies, H. (1997) · Experimental Physiology · doi:10.1113/expphysiol.1997.sp004024 · Cited by 4,577
NOX enzymes and the biology of reactive oxygen
Lambeth, J. D. (2004) · Nature Reviews Immunology · doi:10.1038/nri1312 · Cited by 3,125
Regulation and Function of NF-κB Transcription Factors in the Immune System
Vallabhapurapu, S., & Karin, M. (2009) · Annual Review of Immunology · doi:10.1146/annurev.immunol.021908.132641 · Cited by 2,635
The two NF-κB activation pathways and their role in innate and adaptive immunity
Bonizzi, G., & Karin, M. (2004) · Trends in Immunology · doi:10.1016/j.it.2004.03.008 · Cited by 2,535
Mammalian thioredoxin is a direct inhibitor of apoptosis signal‐regulating kinase (ASK) 1
Saitoh, M., Nishitoh, H., Fujii, M., Takeda, K., Tobiume, K., Sawada, Y., Kawabata, M., Miyazono, K., & Ichijo, H. (1998) · The EMBO Journal · doi:10.1093/emboj/17.9.2596 · Cited by 2,377
Kamata, H., Honda, S.-I., Maeda, S., Chang, L., Hirata, H., & Karin, M. (2005) · Cell · doi:10.1016/j.cell.2004.12.041 · Cited by 1,792
Dilated cardiomyopathy and neonatal lethality in mutant mice lacking manganese superoxide dismutase
Li, Y., Huang, T.-T., Carlson, E. J., Melov, S., Ursell, P. C., Olson, J. L., Noble, L. J., Yoshimura, M. P., Berger, C., Chan, P. H., et al. (1995) · Nature Genetics · doi:10.1038/ng1295-376 · Cited by 1,789
Activation by IKKα of a Second, Evolutionary Conserved, NF-κB Signaling Pathway
Senftleben, U., Cao, Y., Xiao, G., Greten, F. R., Krähn, G. M., Bonizzi, G., Chen, Y., Hu, Y., Fong, A., Sun, S., et al. (2001) · Science · doi:10.1126/science.1062677 · Cited by 1,361
Meyer, M., Schreck, R., & Baeuerle, P. A. (1993) · The EMBO Journal · doi:10.1002/j.1460-2075.1993.tb05850.x · Cited by 1,306
Flagged first, then by citations
Cited by
Sorted by citations
Items 501–600 of 1,009
Oxidative and endoplasmic reticulum stress in respiratory disease
Chen, A. C. –., Burr, L. D., & McGuckin, M. A. (2018) · Clinical & Translational Immunology · doi:10.1002/cti2.1019 · Cited by 73
Regulation of innate immunity by Nrf2
van der Horst, D., Carter-Timofte, M. E., van Grevenynghe, J., Laguette, N., Dinkova‐Kostova, A. T., & Olagnier, D. P. (2022) · Current Opinion in Immunology · doi:10.1016/j.coi.2022.102247 · Cited by 72
Nitric oxide regulation of cellular metabolism: Adaptive tuning of cellular energy
Pappas, G., Wilkinson, M. L., & Gow, A. J. (2022) · Nitric Oxide · doi:10.1016/j.niox.2022.11.006 · Cited by 74
Liu, T., Liu, W., Zhao, J., Meng, F., & Wang, H. (2016) · Cell Biology and Toxicology · doi:10.1007/s10565-016-9360-y · Cited by 71
Contreras-López, R. A., Elizondo-Vega, R. J., Paredes, M. J., Luque‐Campos, N., Torres, M. J., Téjédor, G., Vega-Letter, A. M., Figueroa‐Valdés, A. I., Pradenas, C., Oyarce, K., et al. (2020) · The FASEB Journal · doi:10.1096/fj.201902232r · Cited by 69
Emanuele, S., D’Anneo, A., Calvaruso, G., Cernigliaro, C., Giuliano, M., & Lauricella, M. (2018) · Chemical Research in Toxicology · doi:10.1021/acs.chemrestox.7b00311 · Cited by 69
Cadmium Toxicity: Oxidative Stress, Inflammation and Tissue Injury
Das, S. C., & Al‐Naemi, H. A. (2019) · Occupational Diseases and Environmental Medicine · doi:10.4236/odem.2019.74012 · Cited by 75
Jalili‐Nik, M., Sadeghi, M. M., Mohtashami, E., Mollazadeh, H., Afshari, A. R., & Sahebkar, A. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/3237983 · Cited by 69
Gerges, S. H., Wahdan, S. A., Elsherbiny, D. A., & El‐Demerdash, E. (2021) · Life Sciences · doi:10.1016/j.lfs.2021.119220 · Cited by 76
Xie, N., Fan, F., Jiang, S., Hou, Y., Zhang, Y., Cairang, N., Wang, X., & Meng, X. (2022) · Phytomedicine · doi:10.1016/j.phymed.2022.154240 · Cited by 70
Bathish, B., Robertson, H., Dillon, J. F., Dinkova‐Kostova, A. T., & Hayes, J. D. (2022) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2022.06.226 · Cited by 70
Multiple Roles of SIRT2 in Regulating Physiological and Pathological Signal Transduction
Zhu, C., Dong, X., Wang, X., Zheng, Y., Qiu, J., Peng, Y., Xu, J., Chai, Z., & Liu, C. (2022) · Genetics Research · doi:10.1155/2022/9282484 · Cited by 70
Li, Z.-C., Low, V., Luga, V., Sun, J. Y., Earlie, E. M., Parang, B., Ganesh, K. S., Cho, S., Endress, J., Schild, T., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-33862-0 · Cited by 70
Disorders of Endogenous and Exogenous Antioxidants in Neurological Diseases
Korczowska-Łącka, I., Słowikowski, B. K., Piekut, T., Hurła, M., Banaszek, N., Szymanowicz, O., Jagodziński, P. P., Kozubski, W. P., Permoda-Pachuta, A., & Dorszewska, J. (2023) · Antioxidants · doi:10.3390/antiox12101811 · Cited by 84
Yang, W., Li, K., Pan, Q. L., Huang, W., Xiao, Y., Lin, H., Liu, S., Chen, X., Lv, X., Feng, S., et al. (2024) · ACS Nano · doi:10.1021/acsnano.3c08097 · Cited by 69
Nuclear Transport: A Switch for the Oxidative Stress—Signaling Circuit?
Kodiha, M., & Stochaj, U. (2011) · Journal of Signal Transduction · doi:10.1155/2012/208650 · Cited by 72
Chen, W.-L., Wang, C.-C., Lin, Y., Wu, C., & Hsieh, C. (2015) · Journal of Translational Medicine · doi:10.1186/s12967-015-0758-8 · Cited by 72
Mesenchymal stromal/stem cells as potential therapy in diabetic retinopathy
Fiori, A., Terlizzi, V., Kremer, H., Gebauer, J. E., Hammes, H., Harmsen, M. C., & Bieback, K. (2018) · Immunobiology · doi:10.1016/j.imbio.2018.01.001 · Cited by 69
Xie, J., Hong, E., Ding, B., Jiang, W., Zheng, S., Xie, Z., Tian, D., & Chen, Y. (2020) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2020.578060 · Cited by 72
Oxidative Stress and Redox Signaling in the Pathophysiology of Liver Diseases
Mooli, R. G. R., Mukhi, D., & Ramakrishnan, S. K. (2022) · Comprehensive physiology · doi:10.1002/cphy.c200021 · Cited by 134
Salivary Redox Biomarkers in Different Stages of Dementia Severity
Klimiuk, A., Maciejczyk, M., Choromańska, M., Fejfer, K., Waszkiewicz, N., & Zalewska, A. (2019) · Journal of Clinical Medicine · doi:10.3390/jcm8060840 · Cited by 68
Systems approaches to investigate the role of NF-κB signaling in aging
Haga, M., & Okada, M. (2022) · Biochemical Journal · doi:10.1042/bcj20210547 · Cited by 67
Iorio, R., Celenza, G., & Petricca, S. (2022) · Antioxidants · doi:10.3390/antiox11061199 · Cited by 75
Lipid-lowering in diabetes: An update
Chait, A., Eckel, R. H., Vrablı́k, M., & Zambon, A. (2023) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2023.117313 · Cited by 71
Baruah, K., Norouzitallab, P., Linayati, L., Sorgeloos, P., & Bossier, P. (2014) · Developmental & Comparative Immunology · doi:10.1016/j.dci.2014.06.004 · Cited by 67
Enyedi, B., Zana, M., Donkó, Á., & Geiszt, M. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4594 · Cited by 68
Inflammation in cancer cachexia: To resolve or not to resolve (is that the question?)
Seelaender, M. C. L., Júnior, M. L. B., Lira, F. S., Silvério, R., & Fanelli, F. R. (2012) · Clinical Nutrition · doi:10.1016/j.clnu.2012.01.011 · Cited by 65
Redox Regulation of Store-Operated Ca 2+ Entry
Nunes, P., & Demaurex, N. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5615 · Cited by 70
Redox balance dynamically regulates vascular growth and remodeling
Bir, S. C., Kolluru, G. K., Fang, K., & Kevil, C. G. (2012) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2012.05.003 · Cited by 69
Hawley, B., L’Orange, C., Olsen, D. B., Marchese, A. J., & Volckens, J. (2014) · Toxicological Sciences · doi:10.1093/toxsci/kfu147 · Cited by 68
Wang, P., Qiao, Q., Li, J., Wang, W., Yao, L., & Fu, Y. (2016) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2016.05.014 · Cited by 69
Bezerra, O. C., França, C. M., Rocha, J. A., Neves, G. A., de Souza, P. R. M., Gomes, M. T., Malfitano, C., Loleiro, T. C. A., Dourado, P. M. M., Llesuy, S., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-14021-8 · Cited by 68
Functional crosstalk among oxidative stress and O-GlcNAc signaling pathways
Chen, P., Chi, J., & Boyce, M. (2018) · Glycobiology · doi:10.1093/glycob/cwy027 · Cited by 68
The role of HDAC3 and its inhibitors in regulation of oxidative stress and chronic diseases
He, R., Liu, B., Geng, B., Li, N., & Geng, Q. (2023) · Cell Death Discovery · doi:10.1038/s41420-023-01399-w · Cited by 74
Systems analysis of biological networks in skeletal muscle function
Smith, L., Meyer, G. A., & Lieber, R. L. (2012) · WIREs Systems Biology and Medicine · doi:10.1002/wsbm.1197 · Cited by 71
Novel role of 4-hydroxy-2-nonenal in AIFm2-mediated mitochondrial stress signaling
Miriyala, S., Thippakorn, C., Chaiswing, L., Xu, Y., Noel, T. J., Tovmasyan, A. G., Batinic̈‐Haberle, I., Kooi, C. W. V., Wang, C., Abdel‐Latif, A., et al. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.12.002 · Cited by 67
Slezák, J., Kura, B., Babál, P., Barančı́k, M., Ferko, M., Frimmel, K., Kaločayová, B., Kukreja, R. C., Lazou, A., Mézešová, L., et al. (2017) · Canadian Journal of Physiology and Pharmacology · doi:10.1139/cjpp-2017-0121 · Cited by 67
Kim, W.-S., Lee, K.-S., Kim, J.-H., Kim, C., Lee, G., Choe, J., Won, M., Kim, T., Jeoung, D., Lee, H., et al. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.09.001 · Cited by 68
Redox Regulation of Inflammatory Processes Is Enzymatically Controlled
Lorenzen, I., Mullen, L., Bekeschus, S., & Hanschmann, E.-M. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/8459402 · Cited by 70
Costa, M. C., Lima, T. F. O., Arcaro, C. A., Inácio, M. D., Batista-Duharte, A., Carlos, I. Z., Spolidório, L. C., Assis, R. P., Brunetti, I. L., & Baviera, A. M. (2019) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2019.108303 · Cited by 68
Li, P., Li, L., Zhang, C., Cheng, X., Zhang, Y., Guo, Y., Long, M., Yang, S., & He, J. (2019) · Molecules · doi:10.3390/molecules24132421 · Cited by 66
Reserve Flux Capacity in the Pentose Phosphate Pathway by NADPH Binding Is Conserved across Kingdoms
Christodoulou, D., Kuehne, A., Estermann, A., Fuhrer, T., Lang, P., & Sauer, U. (2019) · iScience · doi:10.1016/j.isci.2019.08.047 · Cited by 69
Zielińska‐Bliźniewska, H., Sitarek, P., Merecz-Sadowska, A., Malinowska, K., Zajdel, K., Jabłońska, M. R., Śliwiński, T., & Zajdel, R. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20184556 · Cited by 68
Zhu, F., Zhang, B., Li, J., & Zhu, L. (2020) · Poultry Science · doi:10.1016/j.psj.2019.12.044 · Cited by 71
Liu, J., Li, Y., Chen, S., Lin, Y., Lai, H., Chen, B., & Chen, T. (2020) · Frontiers in Chemistry · doi:10.3389/fchem.2020.00838 · Cited by 70
Sangaraju, R., Alavala, S., Nalban, N., Jerald, M. K., & Sistla, R. (2021) · International Immunopharmacology · doi:10.1016/j.intimp.2021.107754 · Cited by 66
Powers, S. K., & Schrager, M. A. (2022) · Redox Biology · doi:10.1016/j.redox.2022.102374 · Cited by 72
Endogenous and Exogenous Antioxidants in Skeletal Muscle Fatigue Development during Exercise
Supruniuk, E., Górski, J., & Chabowski, A. (2023) · Antioxidants · doi:10.3390/antiox12020501 · Cited by 72
Qiu, L., Ouyang, C., Zhang, W., Liu, J., Yu, L., Chen, G., & Ren, L. (2023) · Journal of Nanobiotechnology · doi:10.1186/s12951-023-01924-0 · Cited by 66
Rivas-Arancibia, S., Hernández-Zimbrón, L. F., Rodrı́guez-Martı́nez, E., Maldonado, P. D., Borgonio-Pérez, G., & Sepúlveda-Parada, M. (2015) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2015.00065 · Cited by 66
Bindu, S., Mazumder, S., Dey, S., Pal, C., Goyal, M., Alam, A., Iqbal, M. S., Sarkar, S., Siddiqui, A. A., Banerjee, C., et al. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.07.027 · Cited by 69
Nahar, P. P., Driscoll, M. V., Li, L., Slitt, A. L., & Seeram, N. P. (2013) · Journal of Functional Foods · doi:10.1016/j.jff.2013.09.026 · Cited by 66
Rafiq, R. A., Afnan, Q., Nazir, L. A., Kaiser, P. J., Ganai, B. A., & Abdullah, S. T. (2015) · PLoS ONE · doi:10.1371/journal.pone.0131253 · Cited by 66
Buemann, B., & Uvnäs-Moberg, K. (2020) · Medical Hypotheses · doi:10.1016/j.mehy.2020.109597 · Cited by 66
Qi, Y.-T., Zhang, F.-L., Tian, S.-Y., Wu, H.-Q., Zhao, Y., Zhang, X.-W., Liu, Y.-L., Fu, P., Amatore, C., & Huang, W.-H. (2024) · Nature Nanotechnology · doi:10.1038/s41565-023-01575-0 · Cited by 65
Nowak-Perlak, M., Szpadel, K., Jabłońska, I., Pizon, M., & Woźniak, M. (2022) · Molecules · doi:10.3390/molecules27030591 · Cited by 69
Guo, W. Y., Zeng, M., Zhu, S., Li, S., Qian, Y., & Wu, H. (2022) · Food & Function · doi:10.1039/d1fo02970c · Cited by 67
Recent Perspective of Lactobacillus in Reducing Oxidative Stress to Prevent Disease
Zhao, T., Wang, H., Liu, Z., Liu, Y., DeJi, Li, B., & Huang, X. (2023) · Antioxidants · doi:10.3390/antiox12030769 · Cited by 72
Self-citationRole of Uremic Toxins, Oxidative Stress, and Renal Fibrosis in Chronic Kidney Disease
Frąk, W., Dąbek, B., Balcerczyk-Lis, M., Motor, J., Radzioch, E., Młynarska, E., Rysz, J., & Franczyk, B. (2024) · Antioxidants · doi:10.3390/antiox13060687 · Cited by 76
Meseguer, S., Martínez-Zamora, A., García‐Arumí, E., Andreu, A. L., & Armengod, M. ‐. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddu427 · Cited by 63
NFκB signaling regulates embryonic and adult neurogenesis
Zhang, Y., & Hu, W. (2012) · Frontiers in Biology · doi:10.1007/s11515-012-1233-z · Cited by 64
Lisse, T. S., King, B. L., & Rieger, S. (2016) · Scientific Reports · doi:10.1038/srep20328 · Cited by 69
Nair, V. D., & Ge, Y. (2016) · Neuroscience Letters · doi:10.1016/j.neulet.2016.06.061 · Cited by 68
Mitochondrial CaMKII inhibition in airway epithelium protects against allergic asthma
Sebag, S. C., Koval, O. M., Paschke, J. D., Winters, C. J., Jaffer, O. A., Dworski, R., Sutterwala, F. S., Anderson, M. E., & Grumbach, I. M. (2017) · JCI Insight · doi:10.1172/jci.insight.88297 · Cited by 63
Phytochemicals and PI3K Inhibitors in Cancer—An Insight
Suvarna, V., Murahari, M., Khan, T. A., Chaubey, P., & Sangave, P. C. (2017) · Frontiers in Pharmacology · doi:10.3389/fphar.2017.00916 · Cited by 64
Reduced oxidative stress increases acute cold stress tolerance in zebrafish
Lu, D., Ma, Q., Sun, S.-X., Zhang, H., Chen, L., Zhang, M., & Du, Z. (2019) · Comparative Biochemistry and Physiology Part A Molecular & Integrative Physiology · doi:10.1016/j.cbpa.2019.06.009 · Cited by 64
Combined exposure to formaldehyde and PM2.5: Hematopoietic toxicity and molecular mechanism in mice
Ge, J., Yang, H., Lu, X., Wang, S., Zhao, Y. S., Huang, J., Xi, Z., Zhang, L., & Li, R. (2020) · Environment International · doi:10.1016/j.envint.2020.106050 · Cited by 64
Antioxidative Stress Mechanisms behind Resveratrol: A Multidimensional Analysis
Gu, T., Wang, N., Wu, T., Ge, Q., & Chen, L. (2021) · Journal of Food Quality · doi:10.1155/2021/5571733 · Cited by 64
Wang, M., Huang, Q., Liu, M., Zhao, T., Song, X., Chen, Q., Yang, Y., Nan, Y., Liu, Z., Zhang, Y., et al. (2023) · Advanced Materials · doi:10.1002/adma.202309370 · Cited by 66
Self-citationLu, M., Yin, J., Xu, T., Dai, X., Liu, T., Zhang, Y., Wang, S., Liu, Y., Shi, H., Zhang, Y., et al. (2023) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2023.117262 · Cited by 64
Chen, L., Li, S., Guo, X., Xie, P., & Chen, J. (2014) · Environmental Toxicology · doi:10.1002/tox.22068 · Cited by 64
Reactive oxygen species regulate the replication of porcine circovirus type 2 via NF-κB pathway
Chen, X., Ren, F., Hesketh, J. E., Shi, X., Li, J., Gan, F., & Huang, K. (2012) · Virology · doi:10.1016/j.virol.2012.01.023 · Cited by 64
Reactive oxygen species as therapeutic targets in pulmonary hypertension
Freund‐Michel, V., Guibert, C., Dubois, M., Courtois, A., Marthan, R., Savineau, J., & Müller, B. (2013) · Therapeutic Advances in Respiratory Disease · doi:10.1177/1753465812472940 · Cited by 66
Characterization of Immunomodulatory Activities of Honey Glycoproteins and Glycopeptides
Mesaik, M. A., Dastagir, N., Uddin, M. N., Rehman, K., & Azim, M. K. (2014) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf505131p · Cited by 64
Zhang, T., Zhao, G., Zhu, X., Jiang, K., Wu, H., Deng, G., & Qiu, C. (2018) · Journal of Cellular Physiology · doi:10.1002/jcp.26783 · Cited by 64
Domingues, M., Casaril, A. M., Birmann, P. T., Bampi, S. R., Lourenço, D. D. A., Vieira, B. M., Dapper, L. H., Lenardão, E. J., Sonego, M., Collares, T., et al. (2019) · Behavioural Brain Research · doi:10.1016/j.bbr.2019.03.021 · Cited by 64
Zheng, Y., Han, Y., Wang, T., Liu, H., Sun, Q., Hu, S., Chen, J., & Li, Z. (2021) · Advanced Functional Materials · doi:10.1002/adfm.202108971 · Cited by 63
Diabetic sarcopenia: metabolic and molecular appraisal
Giha, H. A., Alamin, O. A. O., & Sater, M. S. (2022) · Acta Diabetologica · doi:10.1007/s00592-022-01883-2 · Cited by 66
New Insights into NF-κB Signaling in Innate Immunity: Focus on Immunometabolic Crosstalks
Iacobazzi, D., Convertini, P., Todisco, S., Santarsiero, A., Iacobazzi, V., & Infantino, V. (2023) · Biology · doi:10.3390/biology12060776 · Cited by 69
Major Oxidative and Antioxidant Mechanisms During Heat Stress-Induced Oxidative Stress in Chickens
Aryal, B., Kwakye, J., Ariyo, O. W., Ghareeb, A. F. A., Milfort, M. C., Fuller, A. L., Khatiwada, S., Rekaya, R., & Aggrey, S. E. (2025) · Antioxidants · doi:10.3390/antiox14040471 · Cited by 85
TMEPAI regulates EMT in lung cancer cells by modulating the ROS and IRS-1 signaling pathways
Hu, Y., He, K., Wang, D., Yuan, X., Liu, Y., Ji, H., & Song, J. (2013) · Carcinogenesis · doi:10.1093/carcin/bgt132 · Cited by 64
Gao, H., Cao, Y., Xia, H., Zhu, X., & Jin, Y. J. (2020) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2020.4479 · Cited by 63
Tang, L., Zhang, C., Yang, Q., Xie, H., Liu, D., Tian, H., Lu, L., Xu, J., Li, W., Xu, G., et al. (2021) · Journal of Cellular Physiology · doi:10.1002/jcp.30269 · Cited by 58
Lu, C.-S., Lin, C., Chang, Y.-H., Chen, H., Chung, W.-C., Lai, W., Ho, C., Wang, T., Chen, C., Yeh, C.-L., et al. (2020) · Journal for ImmunoTherapy of Cancer · doi:10.1136/jitc-2020-001392 · Cited by 66
Toxic Effects of Amanitins: Repurposing Toxicities toward New Therapeutics
Daré, B. L., Ferron, P., & Gicquel, T. (2021) · Toxins · doi:10.3390/toxins13060417 · Cited by 62
Piattini, F., Matsushita, M., Muri, J., Bretscher, P., Feng, X., Freigang, S., Dalli, J., Schneider, C., & Köpf, M. (2021) · European Journal of Immunology · doi:10.1002/eji.202049114 · Cited by 64
Zhao, H., Song, G., Zhu, H., Qian, H., Pan, X., Song, X., Xie, Y., & Liu, C. (2023) · Nutrients · doi:10.3390/nu15204441 · Cited by 66
He, W., Tang, P., & Lv, H. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1571576 · Cited by 67
Merecz-Sadowska, A., Sadowski, A., Zielińska‐Bliźniewska, H., Zajdel, K., & Zajdel, R. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26146678 · Cited by 70
The Use of microRNAs to Modulate Redox and Immune Response to Stroke
Ouyang, Y., Stary, C. M., White, R., & Giffard, R. G. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5757 · Cited by 60
Appraisal of mechanisms of radioprotection and therapeutic approaches of radiation countermeasures
Mishra, K. N., Moftah, B., & Alsbeih, G. (2018) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2018.06.150 · Cited by 62
Li, J., Liang, N. N., Long, X., Zhao, J., Yang, J., Du, X., Yang, T., Yuan, P., Huang, X., Zhang, J., et al. (2019) · Cancer Letters · doi:10.1016/j.canlet.2019.07.001 · Cited by 63
NADPH Oxidase Inhibition: Preclinical and Clinical Studies in Diabetic Complications
Urner, S., Ho, F., Jha, J. C., Ziegler, D., & Jandeleit-Dahm, K. A. M. (2020) · Antioxidants and Redox Signaling · doi:10.1089/ars.2020.8047 · Cited by 66
Telomerase: Key regulator of inflammation and cancer
Wu, L., Fidan, K., Um, J., & Ahn, K. S. (2020) · Pharmacological Research · doi:10.1016/j.phrs.2020.104726 · Cited by 62
Hypertension and Erectile Dysfunction: Breaking Down the Challenges
de Oliveira, A. A., & Nunes, K. P. (2020) · American Journal of Hypertension · doi:10.1093/ajh/hpaa143 · Cited by 64
Fontagné-Dicharry, S., Larroquet, L., Dias, K., Cluzeaud, M., Heraud, C., & Corlay, D. (2017) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2017.12.039 · Cited by 61
A paradoxical role of reactive oxygen species in cancer signaling pathway: Physiology and pathology
Ramalingam, V., & Rajaram, R. (2020) · Process Biochemistry · doi:10.1016/j.procbio.2020.09.032 · Cited by 61
Abdel-Hakeem, M. A., Mongy, S., Hassan, B., Tantawi, O. I., & Badawy, I. (2021) · Journal of Pharmaceutical Sciences · doi:10.1016/j.xphs.2021.06.004 · Cited by 61
A correlation between oxidative stress and diabetic retinopathy: An updated review
Hussain, A., Ashique, S., Afzal, O., Altamimi, M. A., Malik, A., Kumar, S., Garg, A., Sharma, N., Farid, A., Khan, T., et al. (2023) · Experimental Eye Research · doi:10.1016/j.exer.2023.109650 · Cited by 70
Plant-derived and dietary phenolic cinnamic acid derivatives: Anti-inflammatory properties
Freitas, M., Ribeiro, D., Janela, J. L. S., Varela, C. L., Costa, S. C., da Silva, E. J. T., Fernandes, E. G. R., & Roleira, F. M. F. (2024) · Food Chemistry · doi:10.1016/j.foodchem.2024.140080 · Cited by 69
Metadata
- Authors
- Morgan, M. J., & Liu, Z.-G.
- Affiliations
- National Institutes of Health (US)
- Corresponding author
- Liu, Zheng-gang
- ORCID
- Liu, Zheng-gang
- Venue
- Cell Research
- Published
- 2010-12-28
- Volume
- 21
- Issue
- 1
- Pages
- 103-115
- ISSN
- 1001-0602 (ISSN-L)
- 1748-7838
- PMC
- PMC3193400
- OpenAlex
- W2086667809
- Cited by
- 3,505
- References
- 165
- Citations by year
- 2026: 409 · 2025: 401 · 2024: 364 · 2023: 321 · 2022: 330 · 2021: 282 · 2020: 234 · 2019: 210 · 2018: 229 · 2017: 179 · 2016: 139 · 2015: 113 · 2014: 96 · 2013: 81 · 2012: 92
- FWCI
- 5.10
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Cell Research (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- National Cancer Institute
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › NF-κB Signaling Pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
- Keywords
- reactive oxygen species, NF-κB signaling, redox signaling, inflammation, immunity, transcription factors, NF-κB target genes
- MeSH terms
- Antioxidants, Humans, Signal Transduction, NF-kappa B, Reactive Oxygen Species, Oxidative Stress
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