Aryl Hydrocarbon Receptor in Oxidative Stress as a Double Agent and Its Biological and Therapeutic Significance
Open accessAbstract
The aryl hydrocarbon receptor (AhR) has long been implicated in the induction of a battery of genes involved in the metabolism of xenobiotics and endogenous compounds. AhR is a ligand-activated transcription factor necessary for the launch of transcriptional responses important in health and disease. In past decades, evidence has accumulated that AhR is associated with the cellular response to oxidative stress, and this property of AhR must be taken into account during investigations into a mechanism of action of xenobiotics that is able to activate AhR or that is susceptible to metabolic activation by enzymes encoded by the genes that are under the control of AhR. In this review, we examine various mechanisms by which AhR takes part in the oxidative-stress response, including antioxidant and prooxidant enzymes and cytochrome P450. We also show that AhR, as a participant in the redox balance and as a modulator of redox signals, is being increasingly studied as a target for a new class of therapeutic compounds and as an explanation for the pathogenesis of some disorders.
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AhR ligands can also signal through Nrf2, a pleiotropic transcription factor involved in redox homeostasis, metabolism, and immune modulation.
“AhR ligands can also signal via Nuclear factor erythroid 2-related factor 2 (Nrf2)48–51, a pleiotropic transcription factor involved in redox homeostasis, metabolism, and immune modulation52.”
From Exercise-induced microbiota metabolite enhances CD8 T cell antitumor immunity promoting immunotherapy efficacy (2025) · cites this paper as [51]
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Free radicals and antioxidants in normal physiological functions and human disease
Valko, M., Leibfritz, D., Moncol, J., Cronin, M. T. D., Mazur, M., & Telser, J. (2007) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2006.07.001 · Cited by 14,269 · see citing works
Free Radicals in the Physiological Control of Cell Function
Dröge, W. (2002) · Physiological Reviews · doi:10.1152/physrev.00018.2001 · Cited by 9,855 · see citing works
Oxidants, oxidative stress and the biology of ageing
Finkel, T., & Holbrook, N. J. (2000) · Nature · doi:10.1038/35041687 · Cited by 9,413 · see citing works
How mitochondria produce reactive oxygen species
Murphy, M. P. (2009) · Biochemical Journal · doi:10.1042/bj20081386 · Cited by 8,207 · see citing works
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 · see citing works
Oxidative stress, inflammation, and cancer: How are they linked?
Reuter, S., Gupta, S. C., Chaturvedi, M. M., & Aggarwal, B. B. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.09.006 · Cited by 5,441 · see citing works
Oxyl radicals, redox-sensitive signalling cascades and antioxidants
Genestra, M. (2007) · Cellular Signalling · doi:10.1016/j.cellsig.2007.04.009 · Cited by 4,930 · see citing works
Oxidative Stress: Harms and Benefits for Human Health
Pizzino, G., Irrera, N., Cucinotta, M., Pallio, G., Mannino, F., Arcoraci, V., Squadrito, F., Altavilla, D., & Bitto, A. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/8416763 · Cited by 4,837 · see citing works
Itoh, K., Chiba, T., Takahashi, S., Ishii, T., Igarashi, K., Katoh, Y., Oyake, T., Hayashi, N., Satoh, K., Hatayama, I., et al. (1997) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1997.6943 · Cited by 3,999 · see citing works
Uttara, B., Singh, A., Zamboni, P., & Mahajan, R. (2009) · Current Neuropharmacology · doi:10.2174/157015909787602823 · Cited by 3,378 · see citing works
Free Radicals, Antioxidants in Disease and Health
Department of Pharmacy, L. S. P. C. H., Pham-Huy, L. A., He, H., Department of Analytical Chemistry, C. P. U., Pham-Huyc, C., & Laboratory of Toxicology, F. O. P. (2008) · International Journal of Biomedical Science · doi:10.59566/ijbs.2008.4089 · Cited by 3,058 · see citing works
NAD(P)H Oxidase: Role in Cardiovascular Biology and Disease
Griendling, K. K., Sorescu, D., & Ushio-Fukai, M. (2000) · Circulation Research · doi:10.1161/01.res.86.5.494 · Cited by 2,886 · see citing works
Poland, A., & Knutson, J. C. (1982) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pa.22.040182.002505 · Cited by 2,515 · see citing works
Oxidative Stress: A Key Modulator in Neurodegenerative Diseases
Singh, A., Kukreti, R., Saso, L., & Kukreti, S. (2019) · Molecules · doi:10.3390/molecules24081583 · Cited by 2,305 · see citing works
Transcriptional Regulation by Nrf2
Tonelli, C., Chio, I. I. C., & Tuveson, D. A. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7342 · Cited by 2,206 · see citing works
The Nrf2 regulatory network provides an interface between redox and intermediary metabolism
Hayes, J. D., & Dinkova‐Kostova, A. T. (2014) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2014.02.002 · Cited by 2,158 · see citing works
Oxidative Stress and Inflammation: What Polyphenols Can Do for Us?
Hussain, T., Tan, B., Yin, Y., Blachier, F., Tossou, M. C. B., & Rahu, N. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/7432797 · Cited by 2,088 · see citing works
The Role of Oxidative Stress in the Pathogenesis of Age-Related Macular Degeneration
Beatty, S., Koh, H.-H., Phil, M., Henson, D., & Boulton, M. (2000) · Survey of Ophthalmology · doi:10.1016/s0039-6257(00)00140-5 · Cited by 2,051 · see citing works
30 Years of NF-κB: A Blossoming of Relevance to Human Pathobiology
Zhang, Q., Lenardo, M. J., & Baltimore, D. (2017) · Cell · doi:10.1016/j.cell.2016.12.012 · Cited by 1,979 · see citing works
Sharifi-Rad, M., Anil Kumar, N. V., Zucca, P., Varoni, E. M., Dini, L., Panzarini, E., Rajkovic, J., Tsouh Fokou, P. V., Azzini, E., Peluso, I., et al. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.00694 · Cited by 1,971 · see citing works
The KEAP1-NRF2 system: a thiol-based sensor-effector apparatus for maintaining redox homeostasis
Yamamoto, M., Kensler, T. W., & Motohashi, H. (2018) · Physiological Reviews · doi:10.1152/physrev.00023.2017 · Cited by 1,968 · see citing works
Control of Treg and TH17 cell differentiation by the aryl hydrocarbon receptor
Quintana, F. J., Basso, A. S., Iglesias, A. H., Korn, T., Farez, M. F., Bettelli, E., Caccamo, M., Oukka, M., & Weiner, H. L. (2008) · Nature · doi:10.1038/nature06880 · Cited by 1,865 · see citing works
NRF2, a Transcription Factor for Stress Response and Beyond
He, F., Ru, X., & Wen, T. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21134777 · Cited by 1,820 · see citing works
Role of Genes and Environments for Explaining Alzheimer Disease
Gatz, M., Reynolds, C. A., Fratiglioni, L., Johansson, B., Mortimer, J. A., Berg, S., Fiske, A., & Pedersen, N. L. (2006) · Archives of General Psychiatry · doi:10.1001/archpsyc.63.2.168 · Cited by 1,798 · see citing works
Inflammatory mechanisms in patients with chronic obstructive pulmonary disease
Barnes, P. J. (2016) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2016.05.011 · Cited by 1,697 · see citing works
Role of ROS and RNS Sources in Physiological and Pathological Conditions
Meo, S. D., Reed, T. T., Venditti, P., & Víctor, V. M. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/1245049 · Cited by 1,638 · see citing works
Rothhammer, V., Mascanfroni, I. D., Bunse, L., Takenaka, M. C., Kenison, J. E., Mayo, L., Chao, C.-C., Patel, B., Yan, R., Blain, M., et al. (2016) · Nature Medicine · doi:10.1038/nm.4106 · Cited by 1,559 · see citing works
Seibert, K., Zhang, Y., Leahy, K., Hauser, S. D., Masferrer, J. L., Perkins, W., Lee, L., & Isakson, P. C. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.25.12013 · Cited by 1,551 · see citing works
Therapeutic targeting of the NRF2 and KEAP1 partnership in chronic diseases
Cuadrado, A., Rojo, A. I., Wells, G., Hayes, J. D., Cousin, S. P., Rumsey, W. L., Attucks, O. C., Franklin, S., Levonen, A., Kensler, T. W., et al. (2019) · Nature Reviews Drug Discovery · doi:10.1038/s41573-018-0008-x · Cited by 1,474 · see citing works
Rushmore, T. H., Morton, M. R., & Pickett, C. B. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)99004-6 · Cited by 1,464 · see citing works
Alterations of the human gut microbiome in multiple sclerosis
Jangi, S., Gandhi, R., Cox, L. M., Li, N., von Glehn, F., Yan, R., Patel, B., Mazzola, M. A., Liu, S., Glanz, B. L., et al. (2016) · Nature Communications · doi:10.1038/ncomms12015 · Cited by 1,307 · see citing works
Gelboin, H. V. (1980) · Physiological Reviews · doi:10.1152/physrev.1980.60.4.1107 · Cited by 1,280 · see citing works
Nrf2 signaling in coordinated activation of antioxidant gene expression
Jaiswal, A. K. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.02.074 · Cited by 1,254 · see citing works
Regulatory Mechanisms Controlling Gene Expression Mediated by the Antioxidant Response Element
Nguyen, T., Sherratt, P. J., & Pickett, C. B. (2003) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.43.100901.140229 · Cited by 1,232 · see citing works
Rothhammer, V., & Quintana, F. J. (2019) · Nature Reviews Immunology · doi:10.1038/s41577-019-0125-8 · Cited by 1,197 · see citing works
(2002) · PubMed · Cited by 1,190 · see citing works
Antioxidants and Prevention of Chronic Disease
Willcox, J. K., Ash, S. L., & Catignani, G. L. (2004) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408690490468489 · Cited by 1,183 · see citing works
Masella, R., Benedetto, R. D., Varı́, R., Filesi, C., & Giovannini, C. (2005) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2005.05.013 · Cited by 1,109 · see citing works
Ramos-Gomez, M., Kwak, M.-K., Dolan, P. M., Itoh, K., Yamamoto, M., Talalay, P., & Kensler, T. W. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.051618798 · Cited by 1,102 · see citing works
Mechanistic Studies of the Nrf2-Keap1 Signaling Pathway
Zhang, D. D. (2006) · Drug Metabolism Reviews · doi:10.1080/03602530600971974 · Cited by 1,091 · see citing works
Microglial control of astrocytes in response to microbial metabolites
Rothhammer, V., Borucki, D. M., Tjon, E. C., Takenaka, M. C., Chao, C.-C., Ardura-Fabregat, A., de Lima, K. A., Gutiérrez-Vázquez, C., Hewson, P., Staszewski, O., et al. (2018) · Nature · doi:10.1038/s41586-018-0119-x · Cited by 1,051 · see citing works
Nebert, D. W., Roe, A. L., Dieter, M. Z., Solis, W. A., Yang, Y., & Dalton, T. P. (2000) · Biochemical Pharmacology · doi:10.1016/s0006-2952(99)00310-x · Cited by 997 · see citing works
Regulation of the immune response by the aryl hydrocarbon receptor
Gutiérrez-Vázquez, C., & Quintana, F. J. (2018) · Immunity · doi:10.1016/j.immuni.2017.12.012 · Cited by 985 · see citing works
Cloning of a Factor Required for Activity of the Ah (Dioxin) Receptor
Hoffman, E. C., Reyes, H., Chu, F., Sander, F. C., Conley, L. H., Brooks, B. A., & Hankinson, O. (1991) · Science · doi:10.1126/science.1852076 · Cited by 958 · see citing works
The aryl hydrocarbon receptor: multitasking in the immune system
Stockinger, B., Meglio, P. D., Gialitakis, M., & Duarte, J. H. (2014) · Annual Review of Immunology · doi:10.1146/annurev-immunol-032713-120245 · Cited by 909 · see citing works
AH RECEPTOR SIGNALING PATHWAYS
Schmidt, J. V., & Bradfield, C. A. (1996) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.12.1.55 · Cited by 899 · see citing works
Aryl hydrocarbon receptor ligands in cancer: friend and foe
Murray, I. A., Patterson, A. D., & Perdew, G. H. (2014) · Nature reviews. Cancer · doi:10.1038/nrc3846 · Cited by 889 · see citing works
Tobacco smoking leads to extensive genome-wide changes in DNA methylation
Zeilinger, S., Kühnel, B., Klopp, N., Baurecht, H., Kleinschmidt, A., Gieger, C., Weidinger, S., Lattka, E., Adamski, J., Peters, A., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0063812 · Cited by 824 · see citing works
Polycyclic Aromatic Hydrocarbons: From Metabolism to Lung Cancer
Moorthy, B., Chu, C., & Carlin, D. J. (2015) · Toxicological Sciences · doi:10.1093/toxsci/kfv040 · Cited by 807 · see citing works
Denison, M. S., Soshilov, A. A., He, G., DeGroot, D. E., & Zhao, B. (2011) · Toxicological Sciences · doi:10.1093/toxsci/kfr218 · Cited by 748 · see citing works
Functional role of AhR in the expression of toxic effects by TCDD
Mimura, J., & Fujii‐Kuriyama, Y. (2003) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/s0304-4165(02)00485-3 · Cited by 746 · see citing works
Jones, D. A., Carlton, D. P., McIntyre, T. M., Zimmerman, G. A., & Prescott, S. M. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)52976-8 · Cited by 705 · see citing works
Microbial tryptophan metabolites regulate gut barrier function via the aryl hydrocarbon receptor
Scott, S. A., Fu, J., & Chang, P. V. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2000047117 · Cited by 696 · see citing works
Indole and Tryptophan Metabolism: Endogenous and Dietary Routes to Ah Receptor Activation
Hubbard, T. D., Murray, I. A., & Perdew, G. H. (2015) · Drug Metabolism and Disposition · doi:10.1124/dmd.115.064246 · Cited by 646 · see citing works
AhR signaling pathways and regulatory functions
Larigot, L., Juricek, L., Dairou, J., & Coumoul, X. (2018) · Biochimie Open · doi:10.1016/j.biopen.2018.05.001 · Cited by 563 · see citing works
Oxidative stress and lung inflammation in airways disease
MacNee, W. (2001) · European Journal of Pharmacology · doi:10.1016/s0014-2999(01)01320-6 · Cited by 557 · see citing works
Mechanisms that regulate production of reactive oxygen species by cytochrome P450
Zangar, R. C. (2004) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2004.01.018 · Cited by 555 · see citing works
Miao, W., Hu, L., Scrivens, P. J., & Batist, G. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m412081200 · Cited by 541 · see citing works
Kimura, A., Naka, T., Nohara, K., Fujii‐Kuriyama, Y., & Kishimoto, T. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0804231105 · Cited by 540 · see citing works
Modulating NRF2 in Disease: Timing Is Everything
Dodson, M. B., de la Vega, M. R., Cholanians, A. B., Schmidlin, C. J., Chapman, E., & Zhang, D. D. (2018) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010818-021856 · Cited by 540 · see citing works
Aryl hydrocarbon receptor and intestinal immunity
Lamas, B., Natividad, J. M., & Sokol, H. (2018) · Mucosal Immunology · doi:10.1038/s41385-018-0019-2 · Cited by 530 · see citing works
Vogel, C. F. A., Winkle, L. S. V., Esser, C., & Haarmann‐Stemmann, T. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101530 · Cited by 515 · see citing works
The Aryl Hydrocarbon Receptor in Barrier Organ Physiology, Immunology, and Toxicology
Esser, C., & Rannug, A. (2015) · Pharmacological Reviews · doi:10.1124/pr.114.009001 · Cited by 501 · see citing works
Transcriptional regulation of the rat NAD(P)H:quinone reductase gene
Favreau, L. V., & Pickett, C. B. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)64358-7 · Cited by 497 · see citing works
Cyclooxygenase-2 and carcinogenesis
Prescott, S. M., & Fitzpatrick, F. A. (2000) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/s0304-419x(00)00006-8 · Cited by 476 · see citing works
The Nox Family of NAD(P)H Oxidases: Host Defense and Beyond
Geiszt, M., & Leto, T. L. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.r400024200 · Cited by 452 · see citing works
Denison, M. S., Fisher, J. M., & Whitlock, J. P. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)77819-3 · Cited by 451 · see citing works
The complexity of the Nrf2 pathway: beyond the antioxidant response
Huang, Y. S., Li, W., Su, Z., & Kong, A. T. (2015) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2015.08.001 · Cited by 449 · see citing works
Fritsche, E., Schäfer, C., Calles, C., Bernsmann, T., Bernshausen, T., Wurm, M., Hübenthal, U., Cline, J. E., Hajimiragha, H., Schroeder, P., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0701764104 · Cited by 437 · see citing works
Mitochondrial free radical production and cell signaling
Cadenas, E. (2004) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2004.02.005 · Cited by 430 · see citing works
Sun, Y., Meng, Q., Zeibecoglou, K., Robinson, D. S., Macfarlane, A., Humbert, M. J. C., & Kay, A. B. (1999) · The Journal of Immunology · doi:10.4049/jimmunol.163.11.6321 · Cited by 411 · see citing works
The aryl hydrocarbon receptor cross-talks with multiple signal transduction pathways
Puga, A., Ma, C., & Marlowe, J. L. (2008) · Biochemical Pharmacology · doi:10.1016/j.bcp.2008.08.031 · Cited by 409 · see citing works
The role of antioxidants in photoprotection: A critical review
Chen, L., Hu, J. Y., & Wang, S. Q. (2012) · Journal of the American Academy of Dermatology · doi:10.1016/j.jaad.2012.02.009 · Cited by 402 · see citing works
Ciolino, H. P., Daschner, P. J., & Yeh, G. C. (1999) · Biochemical Journal · doi:10.1042/bj3400715 · Cited by 391 · see citing works
Wirthgen, E., Hoeflich, A., Rebl, A., & Günther, J. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2017.01957 · Cited by 381 · see citing works
Chronic Kidney Disease as Oxidative Stress- and Inflammatory-Mediated Cardiovascular Disease
Podkowińska, A., & Formanowicz, D. (2020) · Antioxidants · doi:10.3390/antiox9080752 · Cited by 378 · see citing works
Activation of the Aryl Hydrocarbon Receptor Dampens the Severity of Inflammatory Skin Conditions
Di Meglio, P., Duarte, J. H., Ahlfors, H., Owens, N. D. L., Li, Y., Villanova, F., Tosi, I., Hirota, K., Nestle, F. O., Mrowietz, U., et al. (2014) · Immunity · doi:10.1016/j.immuni.2014.04.019 · Cited by 373 · see citing works
Coal tar induces AHR-dependent skin barrier repair in atopic dermatitis
van den Bogaard, E. H., Bergboer, J. G. M., Vonk-Bergers, M., van Vlijmen-Willems, I. M. J. J., Hato, S. V., van der Valk, P. G. M., Schröder, J. M., Joosten, I., Zeeuwen, P. L. J. M., & Schalkwijk, J. (2013) · Journal of Clinical Investigation · doi:10.1172/jci65642 · Cited by 373 · see citing works
Role of cytochrome P450s in the generation and metabolism of reactive oxygen species
Veith, A. C., & Moorthy, B. (2017) · Current Opinion in Toxicology · doi:10.1016/j.cotox.2017.10.003 · Cited by 366 · see citing works
NRF2 Modulates Aryl Hydrocarbon Receptor Signaling: Influence on Adipogenesis
Shin, S., Wakabayashi, N., Misra, V., Biswal, S., Lee, G., Agoston, E., Yamamoto, M., & Kensler, T. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.00915-07 · Cited by 355 · see citing works
Mammalian Per-Arnt-Sim Proteins in Environmental Adaptation
McIntosh, B. E., Hogenesch, J. B., & Bradfield, C. A. (2010) · Annual Review of Physiology · doi:10.1146/annurev-physiol-021909-135922 · Cited by 352 · see citing works
Cloning and expression of a human Ah receptor cDNA.
Dolwick, K. M., Schmidt, J. V., Carver, L. A., Swanson, H. I., & Bradfield, C. A. (1993) · Molecular Pharmacology · doi:10.1016/s0026-895x(25)13282-3 · Cited by 348 · see citing works
Coordinate regulation of Phase I and II xenobiotic metabolisms by the Ah receptor and Nrf2
Köhle, C., & Bock, K. W. (2007) · Biochemical Pharmacology · doi:10.1016/j.bcp.2007.01.009 · Cited by 346 · see citing works
The multitasking organ: recent insights into skin immune function.
Meglio, P. D., Perera, G., & Nestle, F. (2011) · Immunity · doi:10.1016/j.immuni.2011.12.003 · Cited by 343 · see citing works
Cross talk between ER stress, oxidative stress, and inflammation in health and disease.
Dandekar, A. P., Mendez, R., & Zhang, K.-Z. (2015) · Methods in molecular biology · doi:10.1007/978-1-4939-2522-3_15 · Cited by 341 · see citing works
Natural product-derived pharmacological modulators of Nrf2/ARE pathway for chronic diseases
Kumar, H., Kim, I., More, S. V., Kim, B.-W., & Choi, D. (2013) · Natural Product Reports · doi:10.1039/c3np70065h · Cited by 334 · see citing works
Jin, U.-H., Lee, S., Sridharan, G. V., Lee, K., Davidson, L. A., Jayaraman, A., Chapkin, R. S., Alaniz, R. C., & Safe, S. H. (2014) · Molecular Pharmacology · doi:10.1124/mol.113.091165 · Cited by 330 · see citing works
RelB, a New Partner of Aryl Hydrocarbon Receptor-Mediated Transcription
Vogel, C. F. A., Sciullo, E. M., Li, W., Wong, P., Lazennec, G., & Matsumura, F. (2007) · Molecular Endocrinology · doi:10.1210/me.2007-0211 · Cited by 320 · see citing works
Activation of the Ah Receptor Signal Transduction Pathway by Bilirubin and Biliverdin
Phelan, D., Winter, G. M., Rogers, W. J., Lam, J., & Denison, M. S. (1998) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1998.0814 · Cited by 318 · see citing works
Puga, A., Barnes, S., Dalton, T. P., Chang, C., Knudsen, E. S., & Maier, M. A. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.4.2943 · Cited by 315 · see citing works
Fujisawa‐Sehara, A., Sogawa, K., Yamane, M., & Fujii‐Kuriyama, Y. (1987) · Nucleic Acids Research · doi:10.1093/nar/15.10.4179 · Cited by 313 · see citing works
The Role of the Aryl Hydrocarbon Receptor (AHR) in Immune and Inflammatory Diseases
Neavin, D. R., Liu, D., Ray, B., & Weinshilboum, R. M. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19123851 · Cited by 310 · see citing works
An introduction to the molecular basics of aryl hydrocarbon receptor biology
Abel, J., & Haarmann‐Stemmann, T. (2010) · Biological Chemistry · doi:10.1515/bc.2010.128 · Cited by 297 · see citing works
Tumour promotion by TCDD in skin of HRS/J hairless mice
Poland, A., Palen, D., & Glover, E. A. (1982) · Nature · doi:10.1038/300271a0 · Cited by 294 · see citing works
Prostaglandin H Synthase and Xenobiotic Oxidation
Eling, T. E., Thompson, D. C., Foureman, G. L., Curtis, J. F., & Hughes, M. F. (1990) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pa.30.040190.000245 · Cited by 282 · see citing works
Kim, D. W., Gazourian, L., Quadri, S. A., Raphaëlle, Sherr, D. H., & Sonenshein, G. E. (2000) · Oncogene · doi:10.1038/sj.onc.1203945 · Cited by 280 · see citing works
Nebert, D. W. (2017) · Progress in Lipid Research · doi:10.1016/j.plipres.2017.06.001 · Cited by 278 · see citing works
Hidaka, T., Ogawa, E., Kobayashi, E. H., Suzuki, T., Funayama, R., Nagashima, T., Fujimura, T., Aiba, S., Nakayama, K., Okuyama, R., et al. (2017) · Nature Immunology · doi:10.1038/ni.3614 · Cited by 274 · see citing works
Role of inducible cyclooxygenase (COX-2) in inflammation.
Seibert, K., & Masferrer, J. L. (1994) · PubMed · Cited by 273 · see citing works
Perrais, M., Pigny, P., Copin, M., Aubert, J., & SEUNINGEN, I. V. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m204862200 · Cited by 271 · see citing works
Redox signaling across cell membranes
Fisher, A. B. (2009) · Antioxidants & Redox Signaling · doi:10.1089/ars.2008.2378 · Cited by 269 · see citing works
Introducing the “TCDD-Inducible AhR-Nrf2 Gene Battery”
Yeager, R. L., Reisman, S. A., Aleksunes, L. M., & Klaassen, C. D. (2009) · Toxicological Sciences · doi:10.1093/toxsci/kfp115 · Cited by 267 · see citing works
Lipoxin A4: A New Class of Ligand for the Ah Receptor
Schaldach, C., Riby, J. E., & Bjeldanes, L. F. (1999) · Biochemistry · doi:10.1021/bi982861e · Cited by 265 · see citing works
A Direct Interaction between the Aryl Hydrocarbon Receptor and Retinoblastoma Protein
Ge, N.-L., & Elferink, C. J. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.35.22708 · Cited by 258 · see citing works
Sallée, M., Dou, L., Cérini, C., Poitevin, S., Brunet, P., & Burtey, S. (2014) · Toxins · doi:10.3390/toxins6030934 · Cited by 255 · see citing works
New Trends in Aryl Hydrocarbon Receptor Biology
Mulero‐Navarro, S., & Fernández‐Salguero, P. M. (2016) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2016.00045 · Cited by 254 · see citing works
Yao, H., & Rahman, I. (2011) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2009.10.022 · Cited by 250 · see citing works
Proinflammatory Properties of Coplanar PCBs: In Vitro and in Vivo Evidence
Hennig, B., Meerarani, P., Slim, R. M., Toborek, M. J., Daugherty, A., Silverstone, A. E., & Robertson, L. W. (2002) · Toxicology and Applied Pharmacology · doi:10.1006/taap.2002.9408 · Cited by 247 · see citing works
Role of Oxidants in Lung Injury During Sepsis
Guo, R., & Ward, P. A. (2007) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1785 · Cited by 246 · see citing works
Loss of Mitochondrial Function Impairs Lysosomes
Demers-Lamarche, J., Guillebaud, G., Tlili, M., Todkar, K. J., Bélanger, N., Grondin, M., Nguyen, A., Michel, J. J. C., & Germain, M. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.695825 · Cited by 242 · see citing works
Cyclooxygenase-2 and prostate carcinogenesis
Hussain, T., Gupta, S., & Mukhtar, H. (2003) · Cancer Letters · doi:10.1016/s0304-3835(02)00524-4 · Cited by 239 · see citing works
Yoshikawa, T., & Naito, Y. (2002) · Cited by 237 · see citing works
Penning, T. M., Ohnishi, S. T., Ohnishi, T., & Harvey, R. G. (1996) · Chemical Research in Toxicology · doi:10.1021/tx950055s · Cited by 234 · see citing works
Endogenous and Exogenous Ligands of Aryl Hydrocarbon Receptor: Current State of Art
Stejskalová, L., Dvořák, Z., & Pávek, P. (2011) · Current Drug Metabolism · doi:10.2174/138920011795016818 · Cited by 231 · see citing works
Datla, K. P., Christidou, M., Widmer, W. W., ROOPRAI, H. K., & Dexter, D. T. (2001) · Neuroreport · doi:10.1097/00001756-200112040-00053 · Cited by 224 · see citing works
(2007) · CRC Press eBooks · doi:10.1201/9781420005523 · Cited by 222 · see citing works
Ebert, B., Seidel, A., & Lampen, A. (2005) · Carcinogenesis · doi:10.1093/carcin/bgi139 · Cited by 221 · see citing works
The emerging roles of AhR in physiology and immunity
Hao, N., & Whitelaw, M. L. (2013) · Biochemical Pharmacology · doi:10.1016/j.bcp.2013.07.004 · Cited by 218 · see citing works
Ma, Q., Kinneer, K., Bi, Y., Chan, J. Y., & Kan, Y. W. (2004) · Biochemical Journal · doi:10.1042/bj20031123 · Cited by 217 · see citing works
Liu, J., Miao, H., Deng, D.-Q., Vaziri, N. D., Li, P., & Zhao, Y. (2020) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03645-1 · Cited by 216 · see citing works
Wincent, E., Bengtsson, J., Mohammadi‐Bardbori, A., Alsberg, T. E., Luecke-Johansson, S., Rannug, U., & Rannug, A. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1118467109 · Cited by 215 · see citing works
Possible role of oxidative stress in the pathogenesis of hypertension
Ceriello, A. (2008) · Diabetes Care · doi:10.2337/dc08-s245 · Cited by 215 · see citing works
Tsuji, G., Takahara, M., Uchi, H., Takeuchi, S., Mitoma, C., Moroi, Y., & Furue, M. (2011) · Journal of Dermatological Science · doi:10.1016/j.jdermsci.2010.10.017 · Cited by 209 · see citing works
Fukui, S., Iwamoto, N., Takatani, A., Igawa, T., Shimizu, T., Umeda, M., Nishino, A., Horai, Y., Hirai, Y., Koga, T., et al. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2017.01958 · Cited by 209 · see citing works
Biosynthetic Manipulation of Tryptophan in Bacteria: Pathways and Mechanisms
Alkhalaf, L. M., & Ryan, K. S. (2015) · Chemistry & Biology · doi:10.1016/j.chembiol.2015.02.005 · Cited by 206 · see citing works
Serum Antioxidants, Inflammation, and Total Mortality in Older Women
Walston, J. D., Xue, Q., Semba, R. D., Ferrucci, L., Cappola, A. R., Ricks, M. O., Guralnik, J. M., & Fried, L. P. (2005) · American Journal of Epidemiology · doi:10.1093/aje/kwj007 · Cited by 205 · see citing works
Comparative analysis of dioxin response elements in human, mouse and rat genomic sequences
Sun, Y., Boverhof, D. R., Burgoon, L. D., Fielden, M. R., & Zacharewski, T. R. (2004) · Nucleic Acids Research · doi:10.1093/nar/gkh782 · Cited by 201 · see citing works
Gao, X., Dinkova‐Kostova, A. T., & Talalay, P. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.261572998 · Cited by 198 · see citing works
Marshall, N. B., & Kerkvliet, N. I. (2010) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2009.05125.x · Cited by 197 · see citing works
Oxidase and Oxygenase Function of the Microsomal Cytochrome P450 Monooxygenase System
Kuthan, H., & Ullrich, V. (1982) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1982.tb06820.x · Cited by 197 · see citing works
Vasiliou, V., & Gonzalez, F. J. (2007) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.48.061807.154729 · Cited by 193 · see citing works
Cytochrome P450 1 family and cancers
Go, R., Hwang, K., & Choi, K. (2014) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2014.11.003 · Cited by 189 · see citing works
Burczynski, M. E., Hseuh-Kung, L. I. N., & Penning, T. M. (1999) · PubMed · Cited by 189 · see citing works
Lee, C.-W., Lin, Z.-C., Hu, S. C.-S., Chiang, Y.-C., Hsu, L.-F., Lin, Y.-C., Lee, I.-T., Tsai, M.-H., & Fang, J.-Y. (2016) · Scientific Reports · doi:10.1038/srep27995 · Cited by 188 · see citing works
Induction of cellular oxidative stress by aryl hydrocarbon receptor activation
Dalton, T. P., Puga, A., & Shertzer, H. G. (2002) · Chemico-Biological Interactions · doi:10.1016/s0009-2797(02)00067-4 · Cited by 188 · see citing works
Functions of the aryl hydrocarbon receptor in the skin
Esser, C., Bargen, I., Weighardt, H., Haarmann-Stemmann, T., & Krutmann, J. (2013) · Seminars in Immunopathology · doi:10.1007/s00281-013-0394-4 · Cited by 187 · see citing works
Matsumura, F. (2008) · Biochemical Pharmacology · doi:10.1016/j.bcp.2008.10.013 · Cited by 186 · see citing works
Smoking: effects on multiple sclerosis susceptibility and disease progression
Wingerchuk, D. M. (2011) · Therapeutic Advances in Neurological Disorders · doi:10.1177/1756285611425694 · Cited by 181 · see citing works
The role of transcription factor Nrf2 in skin cells metabolism
Gęgotek, A., & Skrzydlewska, E. (2015) · Archives of Dermatological Research · doi:10.1007/s00403-015-1554-2 · Cited by 180 · see citing works
Balancing the generation and elimination of reactive oxygen species
Rodriguez, R. J., & Redman, R. S. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0500367102 · Cited by 177 · see citing works
Role of the aryl hydrocarbon receptor in carcinogenesis and potential as an anti-cancer drug target
Kolluri, S. K., Jin, U.-H., & Safe, S. H. (2017) · Archives of Toxicology · doi:10.1007/s00204-017-1981-2 · Cited by 173 · see citing works
Free Radicals and Antioxidants in Cardiovascular Health and Disease
Bahoran, T., Soobrattee, M. A., Luximon‐Ramma, A., & Aruoma, O. I. (2007) · Internet Journal of Medical Update - EJOURNAL · doi:10.4314/ijmu.v1i2.39839 · Cited by 172 · see citing works
Thatcher, T. H., Maggirwar, S. B., Baglole, C. J., Lakatos, H. F., Gasiewicz, T. A., Phipps, R. P., & Sime, P. J. (2007) · American Journal Of Pathology · doi:10.2353/ajpath.2007.060391 · Cited by 171 · see citing works
Tsuji, G., Takahara, M., Uchi, H., Matsuda, T., Chiba, T., Takeuchi, S., Yasukawa, F., Moroi, Y., & Furue, M. (2012) · Journal of Investigative Dermatology · doi:10.1038/jid.2011.194 · Cited by 169 · see citing works
Haarmann‐Stemmann, T., Bothe, H., & Abel, J. (2008) · Biochemical Pharmacology · doi:10.1016/j.bcp.2008.09.013 · Cited by 169 · see citing works
Dioxins and Cardiovascular Disease Mortality
Humblet, O., Birnbaum, L. S., Rimm, E. B., Mittleman, M. A., & Hauser, R. B. (2008) · Environmental Health Perspectives · doi:10.1289/ehp.11579 · Cited by 167 · see citing works
Vogel, C. F. A., Sciullo, E. M., Wong, P., Kuzmicky, P. A., Kado, N. Y., & Matsumura, F. (2005) · Environmental Health Perspectives · doi:10.1289/ehp.8094 · Cited by 166 · see citing works
Nebert, D. W., & Karp, C. L. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.r800053200 · Cited by 165 · see citing works
The role of TDP-43 in amyotrophic lateral sclerosis and frontotemporal dementia
Mackenzie, I., & Rademakers, R. (2008) · Current Opinion in Neurology · doi:10.1097/wco.0b013e3283168d1d · Cited by 160 · see citing works
Marlowe, J. L., Knudsen, E. S., Schwemberger, S. J., & Puga, A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m404315200 · Cited by 159 · see citing works
Blank, V. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.11.074 · Cited by 154 · see citing works
Endosomal nox2 oxidase exacerbates virus pathogenicity and is a target for antiviral therapy
To, E. E., Vlahos, R., Luong, R., Halls, M. L., Reading, P. C., King, P. T., Chan, C., Drummond, G. R., Sobey, C. G., Broughton, B. R. S., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-00057-x · Cited by 154 · see citing works
Pulmonary epithelium, cigarette smoke, and chronic obstructive pulmonary disease.
Thorley, A. J., & Tetley, T. D. (2007) · Europe PMC (PubMed Central) · Cited by 151 · see citing works
Nadeem, A., Masood, A., & Siddiqui, N. M. (2008) · Therapeutic Advances in Respiratory Disease · doi:10.1177/1753465808094971 · Cited by 148 · see citing works
Ryu, Y. S., Kang, K. A., Piao, M. J., Ahn, M. J., Yi, J. M., Hyun, Y., Kim, S. H., Ko, M. K., Park, C. O., & Hyun, J. W. (2018) · Redox Biology · doi:10.1016/j.redox.2018.101080 · Cited by 147 · see citing works
Expression of the Human Aryl Hydrocarbon Receptor Complex in Yeast
Miller, C. A. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.52.32824 · Cited by 146 · see citing works
AhR and ARNT modulate ER signaling
Swedenborg, E., & Pongratz, I. (2009) · Toxicology · doi:10.1016/j.tox.2009.09.007 · Cited by 146 · see citing works
Structural Basis for Aryl Hydrocarbon Receptor-Mediated Gene Activation
Schulte, K. W., Green, E., Wilz, A., Platten, M., & Daumke, O. (2017) · Structure · doi:10.1016/j.str.2017.05.008 · Cited by 145 · see citing works
Reynolds, L. M., Wan, M., Ding, J., Taylor, J. R., Lohman, K., Su, D., Bennett, B. D., Porter, D. K., Gimple, R. C., Pittman, G. S., et al. (2015) · Circulation Cardiovascular Genetics · doi:10.1161/circgenetics.115.001097 · Cited by 144 · see citing works
Han, S. G., Han, S., Toborek, M. J., & Hennig, B. (2012) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2012.03.024 · Cited by 141 · see citing works
Kaye, J., Piryatinsky, V., Birnberg, T., Hingaly, T., Raymond, E., Kashi, R., Amit‐Romach, E., Caballero, I. S., Towfic, F., Ator, M. A., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1607843113 · Cited by 141 · see citing works
Barhoover, M. A., Hall, J. M., Greenlee, W. F., & Thomas, R. S. (2009) · Molecular Pharmacology · doi:10.1124/mol.109.059675 · Cited by 140 · see citing works
Aryl hydrocarbon receptor is activated in patients and mice with chronic kidney disease
Dou, L., Poitevin, S., Sallée, M., Addi, T., Gondouin, B., McKay, N., Denison, M. S., Jourde‐Chiche, N., Duval-Sabatier, A., Cérini, C., et al. (2018) · Kidney International · doi:10.1016/j.kint.2017.11.010 · Cited by 139 · see citing works
Burczynski, M. E., Harvey, R. G., & Penning, T. M. (1998) · Biochemistry · doi:10.1021/bi972725u · Cited by 134 · see citing works
Nakahama, T., Kimura, A., Nguyen, N. T., Chinen, I., Hanieh, H., Nohara, K., Fujii‐Kuriyama, Y., & Kishimoto, T. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1111786108 · Cited by 132 · see citing works
Denison, M. S., & Faber, S. C. (2017) · Current Opinion in Toxicology · doi:10.1016/j.cotox.2017.01.006 · Cited by 131 · see citing works
The Tumor Suppressor Kruppel-Like Factor 6 Is a Novel Aryl Hydrocarbon Receptor DNA Binding Partner
Wilson, S. R., Joshi, A., & Elferink, C. J. (2013) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.113.203786 · Cited by 131 · see citing works
Guo, Y. L., Yu, M. L., Hsu, C. C., & Rogan, W. J. (1999) · Environmental Health Perspectives · doi:10.1289/ehp.99107715 · Cited by 130 · see citing works
Kawajiri, K., & Fujii‐Kuriyama, Y. (2016) · EXPERIMENTAL ANIMALS · doi:10.1538/expanim.16-0092 · Cited by 130 · see citing works
Pathak, S., Sharma, R. A., Steward, W. P., Mellon, J. K., Griffiths, T. R. L., & Gescher, A. (2004) · European Journal of Cancer · doi:10.1016/j.ejca.2004.09.028 · Cited by 129 · see citing works
Alexandrov, K., Rojas, M., & Satarug, S. (2010) · Toxicology Letters · doi:10.1016/j.toxlet.2010.04.009 · Cited by 129 · see citing works
Soshilov, A. A., & Denison, M. S. (2014) · Molecular and Cellular Biology · doi:10.1128/mcb.01183-13 · Cited by 128 · see citing works
Fujii‐Kuriyama, Y., & Kawajiri, K. (2010) · Proceedings of the Japan Academy Series B · doi:10.2183/pjab.86.40 · Cited by 128 · see citing works
Iqbal, J., Sun, L., Cao, J., Yuen, T., Lu, P., Bab, I., Leu, N. A., Srinivasan, S., Wagage, S., Hunter, C. A., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1220919110 · Cited by 126 · see citing works
Quattrochi, L. C., & Tukey, R. H. (1993) · Molecular Pharmacology · doi:10.1016/s0026-895x(25)13403-2 · Cited by 126 · see citing works
Human Aldo-Keto Reductases and the Metabolic Activation of Polycyclic Aromatic Hydrocarbons
Penning, T. M. (2014) · Chemical Research in Toxicology · doi:10.1021/tx500298n · Cited by 125 · see citing works
Hockley, S. L., Arlt, V. M., Brewer, D. S., Giddings, I., & Phillips, D. H. (2006) · BMC Genomics · doi:10.1186/1471-2164-7-260 · Cited by 124 · see citing works
Duarte, J. H., Meglio, P. D., Hirota, K., Ahlfors, H., & Stockinger, B. (2013) · PLoS ONE · doi:10.1371/journal.pone.0079819 · Cited by 124 · see citing works
Smirnova, A. V., Wincent, E., Bergander, L. V., Alsberg, T. E., Bergman, J., Rannug, A., & Rannug, U. (2015) · Chemical Research in Toxicology · doi:10.1021/acs.chemrestox.5b00416 · Cited by 122 · see citing works
Aryl Hydrocarbon Receptor–Dependent Induction of Liver Fibrosis by Dioxin
Pierre, S., Chevallier, A., Teixeira-Clerc, F., Ambolet-Camoit, A., Bui, L. C., Bats, A., Fournet, J., Fernández‐Salguero, P. M., Aggerbeck, Μ., Lotersztajn, S., et al. (2013) · Toxicological Sciences · doi:10.1093/toxsci/kft236 · Cited by 121 · see citing works
Clinical management of the uraemic syndrome in chronic kidney disease
Vanholder, R., Fouque, D. P., Glorieux, G., Heine, G. H., Kanbay, M., Mallamaci, F., Massy, Z. A., Ortíz, A., Rossignol, P., Więcek, A., et al. (2016) · The Lancet Diabetes & Endocrinology · doi:10.1016/s2213-8587(16)00033-4 · Cited by 121 · see citing works
Telakowski-Hopkins, C. A., King, R. G., & Pickett, C. B. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.4.1000 · Cited by 120 · see citing works
Park, J., Troxel, A. B., Harvey, R. G., & Penning, T. M. (2006) · Chemical Research in Toxicology · doi:10.1021/tx0600245 · Cited by 120 · see citing works
Palackal, N. T., Burczynski, M. E., Harvey, R. G., & Penning, T. M. (2001) · Biochemistry · doi:10.1021/bi010872t · Cited by 120 · see citing works
Huang, P., Rannug, A., Ahlbom, E., Håkansson, H., & Ceccatelli, S. (2000) · Toxicology and Applied Pharmacology · doi:10.1006/taap.2000.9064 · Cited by 118 · see citing works
The activation mechanism of the aryl hydrocarbon receptor (AhR) by molecular chaperone HSP90
Tsuji, N., Fukuda, K., Nagata, Y., Okada, H., Haga, A., Hatakeyama, S., Yoshida, S., Okamoto, T., Hosaka, M., Sekine, K., et al. (2014) · FEBS Open Bio · doi:10.1016/j.fob.2014.09.003 · Cited by 117 · see citing works
Signal Transduction-mediated Activation of the Aryl Hydrocarbon Receptor in Rat Hepatoma H4IIE Cells
Backlund, M., Johansson, I., Mkrtchian, S., & Ingelman‐Sundberg, M. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.50.31755 · Cited by 115 · see citing works
Podocyte Injury Caused by Indoxyl Sulfate, a Uremic Toxin and Aryl-Hydrocarbon Receptor Ligand
Ichii, O., Otsuka-Kanazawa, S., Nakamura, T., Masaaki, U., Kon, Y., Chen, W., Rosenberg, A. Z., & Kopp, J. B. (2014) · PLoS ONE · doi:10.1371/journal.pone.0108448 · Cited by 114 · see citing works
Redox regulation of proteasome function
Lefaki, M., Papaevgeniou, N., & Chondrogianni, N. (2017) · Redox Biology · doi:10.1016/j.redox.2017.07.005 · Cited by 114 · see citing works
Chopra, M., & Schrenk, D. (2011) · Critical Reviews in Toxicology · doi:10.3109/10408444.2010.524635 · Cited by 113 · see citing works
Masai, N., Tatebe, J., Yoshino, G., & Morita, T. (2010) · Circulation Journal · doi:10.1253/circj.cj-10-0117 · Cited by 113 · see citing works
Furue, M., Uchi, H., Mitoma, C., Hashimoto-Hachiya, A., Chiba, T., Ito, T., Nakahara, T., & Tsuji, G. (2017) · Nutrients · doi:10.3390/nu9030223 · Cited by 113 · see citing works
Shou, M., Harvey, R. G., & Penning, T. M. (1993) · Carcinogenesis · doi:10.1093/carcin/14.3.475 · Cited by 113 · see citing works
Kubli, S. P., Bassi, C., Roux, C., Wakeham, A. C., Göbl, C., Zhou, W., Jafari, S. M., Snow, B. E., Jones, L., Palomero, L., et al. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1815126116 · Cited by 112 · see citing works
The relationships between cytochromes P450 and H 2 O 2 : Production, reaction, and inhibition
Albertolle, M. E., & Guengerich, F. P. (2018) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2018.05.014 · Cited by 111 · see citing works
Bock, K. W. (2019) · Biochemical Pharmacology · doi:10.1016/j.bcp.2019.06.015 · Cited by 110 · see citing works
PCB-induced oxidative stress in endothelial cells: modulation by nutrients
Hennig, B., Hammock, B. D., Slim, R. M., Toborek, M. J., Saraswathi, V., & Robertson, L. W. (2002) · International Journal of Hygiene and Environmental Health · doi:10.1078/1438-4639-00134 · Cited by 109 · see citing works
ANTIOXIDANTS AND RHEUMATOID ARTHRITIS
Mahajan, A., & Tandon, V. (2004) · Cited by 108 · see citing works
Oxidative Stress in Chronic Obstructive Pulmonary Disease: A Lung and Systemic Process
van Eeden, S. F., & Sin, D. D. (2013) · Canadian Respiratory Journal · doi:10.1155/2013/509130 · Cited by 108 · see citing works
Yamamoto, J., Ihara, K., Nakayama, H., Hikino, S., Satoh, K., Kubo, N., Iida, T., Fujii, Y., & Hara, T. (2003) · Life Sciences · doi:10.1016/j.lfs.2003.07.022 · Cited by 107 · see citing works
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- [270]Gemma C. Vila J. Bachstetter A. Bickford P.C. Oxidative Stress and the Aging Brain: From Theory to Prevention Brain Aging: Models, Methods, and Mechanisms Riddle D.R. Frontiers in Neuroscience Boca Raton, FL, USA 2007 21204345
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Sorted by citations
Functions of the aryl hydrocarbon receptor (AHR) beyond the canonical AHR/ARNT signaling pathway
Sondermann, N. C., Faßbender, S., Hartung, F., Hätälä, A. M., Rolfes, K. M., Vogel, C. F. A., & Haarmann‐Stemmann, T. (2022) · Biochemical Pharmacology · doi:10.1016/j.bcp.2022.115371 · Cited by 190 · see citing works
Extracellular Matrix Regulation in Physiology and in Brain Disease
Soles, A., Selimovic, A., Sbrocco, K., Ghannoum, F. J., Hamel, K. A., Labrada-Moncada, F. E., Gilliat, S., & Cvetanović, M. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24087049 · Cited by 157 · see citing works
Bahman, F., Choudhry, K., Al‐Rashed, F., Al‐Mulla, F., Sindhu, S. T. A. K., & Ahmad, R. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1421346 · Cited by 98 · see citing works
Environmental Air Pollutants Affecting Skin Functions with Systemic Implications
Bocheva, G., Slominski, R. M., & Slominski, A. T. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241310502 · Cited by 94 · see citing works
Phelps, C. M., Willis, N. B., Duan, T., Lee, A. H., Zhang, Y., Rodriguez J, D. M., Pandey, S. P., Laughlin, C. R., Rosen, A. B. I., McPherson, A. C., et al. (2025) · Cell · doi:10.1016/j.cell.2025.06.018 · Cited by 91 · see citing works
Exploring the Thioredoxin System as a Therapeutic Target in Cancer: Mechanisms and Implications
Seitz, R., Tümen, D., Kunst, C., Heumann, P., Schmid, S. A., Kandulski, A., Müller, M., & Gülow, K. (2024) · Antioxidants · doi:10.3390/antiox13091078 · Cited by 72 · see citing works
Aryl hydrocarbon receptor: The master regulator of immune responses in allergic diseases
Riaz, F., Pan, F., & Wei, P. Y. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.1057555 · Cited by 65 · see citing works
Heavy metals, oxidative stress, and the role of AhR signaling
Kou, Z., Tran, F., & Dai, W. (2023) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2023.116769 · Cited by 47 · see citing works
Anderson-Bain, K., Roberts, C., Kohlman, E., Ji, X., Alcaraz, A. J., Miller, J. G. P., Gangur-Powell, T., Weber, L. P., Janz, D. M., Hecker, M., et al. (2023) · Comparative Biochemistry and Physiology Part C Toxicology & Pharmacology · doi:10.1016/j.cbpc.2023.109697 · Cited by 45 · see citing works
Microbiota, Oxidative Stress, and Skin Cancer: An Unexpected Triangle
Azzimonti, B., Ballacchino, C., Zanetta, P., Cucci, M. A., Monge, C., Grattarola, M., Dianzani, C., Barrera, G., & Pizzimenti, S. (2023) · Antioxidants · doi:10.3390/antiox12030546 · Cited by 38 · see citing works
AhR and Wnt/β-Catenin Signaling Pathways and Their Interplay
Grishanova, A. Y., Klyushova, L. S., & Perepechaeva, M. L. (2023) · Current Issues in Molecular Biology · doi:10.3390/cimb45050248 · Cited by 34 · see citing works
Self-citationDey, K. K., Kamila, S., Das, T., & Chattopadhyay, A. (2024) · Environmental Toxicology and Pharmacology · doi:10.1016/j.etap.2024.104396 · Cited by 34 · see citing works
Oxidative Stress and the Nrf2/PPARγ Axis in the Endometrium: Insights into Female Fertility
Artimovič, P., Badovská, Z., Toporcerová, S., Špaková, I., Smolko, L., Sabolová, G., Kriváková, E., & Rabajdová, M. (2024) · Cells · doi:10.3390/cells13131081 · Cited by 34 · see citing works
Solan, M. E., & Lavado, R. (2023) · Current Research in Toxicology · doi:10.1016/j.crtox.2023.100116 · Cited by 33 · see citing works
Ryu, J. Y., & Hong, D. H. (2024) · Scientific Reports · doi:10.1038/s41598-024-58263-9 · Cited by 31 · see citing works
Ribeiro, M. M., Alvarenga, L., Cardozo, L., Baptista, B. G., Nascimento, D., Esgalhado, M., & Mafra, D. (2025) · Current Nutrition Reports · doi:10.1007/s13668-025-00645-0 · Cited by 29 · see citing works
Role of Ischemia/Reperfusion and Oxidative Stress in Shock State
Vázquez-Galán, Y. I., Guzmán-Silahua, S., Trujillo-Rangel, W. Á., & Rodríguez-Lara, S. Q. (2025) · Cells · doi:10.3390/cells14110808 · Cited by 27 · see citing works
Current state of knowledge of triclosan (TCS)-dependent reactive oxygen species (ROS) production
Kosińska, K., & Szychowski, K. A. (2024) · Environmental Research · doi:10.1016/j.envres.2024.118532 · Cited by 26 · see citing works
Sublethal effects of early-life exposure to common and emerging contaminants in birds
Grace, J. K., Duran, E., Ottinger, M. A., & Maness, T. J. (2024) · Current Research in Toxicology · doi:10.1016/j.crtox.2024.100190 · Cited by 25 · see citing works
Huchzermeier, R., & van der Vorst, E. P. C. (2025) · Biochemical Pharmacology · doi:10.1016/j.bcp.2025.116785 · Cited by 25 · see citing works
Zhang, L., Chen, W., Han, X., Wang, H., Gao, P.-Z., Wang, D., Cao, Z., Sun, C.-H., Cheng, D., Bai, J., et al. (2024) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2024.175877 · Cited by 23 · see citing works
Wang, J., Peng, Y., Liu, Y., Lian, Z., Cai, Z., Chen, Y., He, H., Yang, M., & Zhao, J. (2025) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2025.04.020 · Cited by 22 · see citing works
The clinical, mechanistic, and social impacts of air pollution on atopic dermatitis
Zeldin, J., Ratley, G., Shobnam, N., & Myles, I. A. (2024) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2024.07.027 · Cited by 22 · see citing works
Dicks, L. M. T. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26146744 · Cited by 21 · see citing works
Ruggeri, R. M., Minuti, A., Gianì, F., Masto, R., Romano, D., Aliquò, F., Campennì, A., Campo, S., Cannavò, S., & D’Ascola, A. (2024) · Endocrine · doi:10.1007/s12020-024-04005-w · Cited by 21 · see citing works
Szaefer, H., Licznerska, B. E., & Baer‐Dubowska, W. (2024) · Molecules · doi:10.3390/molecules29184283 · Cited by 20 · see citing works
The role of aryl hydrocarbon receptor in vitiligo: a review
Li, Y., Zeng, Y., Chen, Z., Tan, X., Mei, X., & Wu, Z. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1291556 · Cited by 19 · see citing works
Alharbi, A., & Alhujaily, M. M. (2024) · Metabolites · doi:10.3390/metabo14120697 · Cited by 18 · see citing works
Unraveling the Core of Endometriosis: The Impact of Endocrine Disruptors
Moustakli, E., Potiris, A., Grigoriadis, T., Zikopoulos, A., Drakaki, Ε., Zouganeli, I., Theofanakis, C., Gerede, A., Zachariou, A., Domali, E., et al. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26157600 · Cited by 17 · see citing works
Banerjee, O., Singh, S., Prasad, S. K., Bhattacharjee, A., Seal, T., Mandal, J., Sinha, S., Banerjee, A., Maji, B. K., & Mukherjee, S. (2023) · Toxicology · doi:10.1016/j.tox.2023.153693 · Cited by 13 · see citing works
The AHR–NRF2–JDP2 gene battery: Ligand–induced AHR transcriptional activation
Wuputra, K., Hsu, W., Ku, C., Yang, Y.-H., Kuo, K., Yu, F., Yu, H.-S., Nagata, K., Wu, D., Kuo, C., et al. (2025) · Biochemical Pharmacology · doi:10.1016/j.bcp.2025.116761 · Cited by 12 · see citing works
Coronel, P. M. V., Pereira, I. C., Basilio, D. C. L. S., Espinoça, I. T., de Souza, K. F. S., Ota, R. S. N., de Almeida, E. B., Paredes‐Gamero, E. J., Filho, D. W., Perdomo, R. T., et al. (2023) · Microbial Pathogenesis · doi:10.1016/j.micpath.2023.106339 · Cited by 11 · see citing works
Jaikang, C., Konguthaithip, G., Amornlertwatana, Y., Autsavapromporn, N., Rattanachitthawat, S., & Monum, T. (2024) · Biomedicines · doi:10.3390/biomedicines12091947 · Cited by 11 · see citing works
Sarkar, O., Islam, S., Mukherjee, S., & Chattopadhyay, A. (2025) · Journal of Applied Toxicology · doi:10.1002/jat.4776 · Cited by 11 · see citing works
AhR and STAT3: A Dangerous Duo in Chemical Carcinogenesis
Minacori, M., Fiorini, S., Perugini, M., Iannetta, A., Meschiari, G., Chichiarelli, S., Fabio Altieri, F., Natali, P. G., & Eufemi, M. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26062744 · Cited by 10 · see citing works
Szychowski, K. A. (2025) · Oxygen · doi:10.3390/oxygen5030016 · Cited by 10 · see citing works
Kövesi, B., Kulcsár, S., Ancsin, Z., Erdélyi, M., Zándoki, E., Gömbös, P., Balogh, K., & Mézes, M. (2024) · Toxins · doi:10.3390/toxins16030154 · Cited by 10 · see citing works
Reactive Oxygen Species - Advances and Developments
Ahmad, R. (2023) · Biochemistry · doi:10.5772/intechopen.107774 · Cited by 9 · see citing works
Multi-Fusarium mycotoxin exposure activates Nrf2 and Ahr pathway in the liver of laying hens
Kövesi, B., Kulcsár, S., Ancsin, Z., Erdélyi, M., Zándoki, E., Gömbös, P., Balogh, K., & Mézes, M. (2023) · Toxicology Letters · doi:10.1016/j.toxlet.2023.12.006 · Cited by 9 · see citing works
Lu, C., Feng, Y., Tang, Z., Jia, R., Xia, F., Yu, T., Wang, H., Mo, H., Shi, D., & Lu, F. (2024) · Theriogenology · doi:10.1016/j.theriogenology.2024.11.014 · Cited by 9 · see citing works
Eshaq, S. B., Taneera, J., Anjum, S., Mohammed, A. K., Semreen, M. H., Alzoubi, K. H., Eladl, M. A., Bustanji, Y. K., Abu‐Gharbieh, E., & El‐Huneidi, W. (2025) · Cells · doi:10.3390/cells14010057 · Cited by 8 · see citing works
Abdulai, P. M., Bede-Ojimadu, O. O., Onyena, A. P., Frazzoli, C., Mogborukor, N. A., Ekhator, O. C., Udom, G. J., Nwanaforo, E. O., & Orisakwe, O. E. (2025) · Environmental Health Insights · doi:10.1177/11786302251343767 · Cited by 8 · see citing works
Sim, W., Lee, E., Yun, S., Lim, W., & Lim, T. (2023) · Journal of Functional Foods · doi:10.1016/j.jff.2023.105593 · Cited by 8 · see citing works
Fotschki, B., Sójka, M., Kosmala, M., & Juśkiewicz, J. (2023) · Nutrients · doi:10.3390/nu15143115 · Cited by 8 · see citing works
Malešević, A., Tucović, D., Kulaš, J. B., Mirkov, I. I., Popović, D., Čakić-Milošević, M., & Aleksandrov, A. P. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25168631 · Cited by 7 · see citing works
Liao, Z., Huang, M., Zhang, Y., Huang, S., Lei, W., & Shui, X. (2025) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2025.5597 · Cited by 6 · see citing works
Fitriana, I., Wu, C.-H., Hsu, T.-J., Chan, Y.-J., Li, C.-H., Lee, C., Hsiao, G., & Cheng, Y. (2023) · Biochemical Pharmacology · doi:10.1016/j.bcp.2023.115700 · Cited by 6 · see citing works
Szychowski, K. A., Skóra, B., & Wójtowicz, A. K. (2024) · Toxicology · doi:10.1016/j.tox.2024.154031 · Cited by 6 · see citing works
Strojny, B., Pruchniewski, M., Sosnowska, M., Szczepaniak, J., & Wierzbicki, M. (2025) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2025.179211 · Cited by 6 · see citing works
Ng, H. Y., Wu, Y. S., Biswas, M., & Sim, M. S. (2025) · Biogerontology · doi:10.1007/s10522-025-10296-x · Cited by 6 · see citing works
Saha, K., Ganapathy, A. S., Wang, A., Priya, A., Morris, N. M., Harris, L., Yochum, G. S., Koltun, W. A., Perdew, G. H., Nighot, M., et al. (2023) · Mucosal Immunology · doi:10.1016/j.mucimm.2023.09.003 · Cited by 6 · see citing works
Eucalyptus Wood Smoke Extract Elicits a Dose-Dependent Effect in Brain Endothelial Cells
You, D. J., Gorman, B. M., Goshi, N., Hum, N. R., Sebastian, A., Kim, Y. H., Enright, H. A., & Buchholz, B. A. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms251910288 · Cited by 5 · see citing works
Wang, Y., Wu, D., Guo, Z., Xiu, C., Li, Y., Tan, Y., Ye, Z., Liu, Y., Huo, Y., Li, Q. X., et al. (2025) · Journal of Hazardous Materials · doi:10.1016/j.jhazmat.2025.139784 · Cited by 5 · see citing works
Qin, Y., Shen, D., Guo, K., Meng, X., Cui, X., Li, Y., & Jia, Y. (2026) · Cell Cycle · doi:10.1080/15384101.2025.2609649 · Cited by 5 · see citing works
Unveiling the role of sex in the metabolism of indoxyl sulfate and apixaban
Pina-Beltrán, B., Dimitrov, D., McKay, N., Giot, M., Zdráhal, Z., Potěšil, D., Pustka, V., Peinado‐Izaguerri, J., Sáez-Rodríguez, J., Poitevin, S., et al. (2025) · Scientific Reports · doi:10.1038/s41598-025-90405-5 · Cited by 5 · see citing works
Merza, M., Oghenemaro, E. F., Asiri, M., Baldaniya, L. H., Hjazi, A. M., Kaur, P., Kholjigitova, M., Rathore, G., Kumar, M. R., & Najafi, M. L. (2025) · Environmental Sciences Europe · doi:10.1186/s12302-025-01076-y · Cited by 5 · see citing works
Agarwal, M., Roth, K., Yang, Z., Sharma, R., Maddipati, K. R., Westrick, J. A., & Petriello, M. C. (2024) · Environmental Research · doi:10.1016/j.envres.2024.118492 · Cited by 5 · see citing works
TnP and AHR-CYP1A1 Signaling Crosstalk in an Injury-Induced Zebrafish Inflammation Model
Disner, G. R., Fernandes, T. A. D. M., Nishiyama, M. Y., Lima, C., Wincent, E., & Lopes‐Ferreira, M. (2024) · Pharmaceuticals · doi:10.3390/ph17091155 · Cited by 5 · see citing works
Role of 4-Thiazolidinone–Pyrazoline/Indoline Hybrids Les-4369 and Les-3467 in BJ and A549 Cell Lines
Kosińska, K., Skóra, B., Holota, S. M., Shepeta, Y., Tabęcka-Łonczyńska, A., Lesyk, R., & Szychowski, K. A. (2024) · Cells · doi:10.3390/cells13121007 · Cited by 5 · see citing works
Lu, C.-L., Tseng, Y.-S., Wu, W., Liao, C., & Ma, M. (2025) · Antioxidants and Redox Signaling · doi:10.1089/ars.2024.0833 · Cited by 4 · see citing works
Poźniak, O., Sitarz, R., Sitarz, M., Kowalczuk, D., Słoń, E., & Dudzińska, E. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26189160 · Cited by 4 · see citing works
ElHady, S. A., Abd‐Elmawla, M. A., Shamaa, M. M., & Abdelgawad, H. M. (2025) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2025.109156 · Cited by 4 · see citing works
Strategies for the Development of NK Cell-Based Therapies for Cancer Treatment
Budagova, T., Efremova, A. S., Maiak, M. A., & Goldshtein, D. V. (2025) · Cells · doi:10.3390/cells14231858 · Cited by 4 · see citing works
Veroni, C., Olla, S., Brignone, M. S., Siguri, C., Formato, A., Marra, M., Manzoli, R., Macario, M. C., Ambrosini, E., Moro, E., et al. (2024) · Biomolecules · doi:10.3390/biom14040443 · Cited by 4 · see citing works
Lieke, T., Jung‐Schroers, V., & Rebl, A. (2025) · Journal of Hazardous Materials · doi:10.1016/j.jhazmat.2025.137260 · Cited by 3 · see citing works
Li, X., Ma, N.-S., He, C., Zou, L., Zhang, J., Ni, Z., & Yang, L. (2025) · Journal of Enzyme Inhibition and Medicinal Chemistry · doi:10.1080/14756366.2025.2579675 · Cited by 3 · see citing works
Wu, L., Wu, S., Deng, Y., Li, J., Zhang, C., Wang, Y., Zhao, C., & Gao, L. (2026) · Inflammation · doi:10.1007/s10753-025-02371-9 · Cited by 3 · see citing works
Kazensky, L., Štefiček, M. J. L., Kašuba, V., Novak, M., Belingar, K., Matković, K., Gerić, M., Rinkovec, J., Jakovljević, I., Baralić, K., et al. (2026) · Environmental Research · doi:10.1016/j.envres.2026.124252 · Cited by 3 · see citing works
Sarkar, O., Islam, S., Mukherjee, S., & Chattopadhyay, A. (2026) · Environmental Toxicology and Pharmacology · doi:10.1016/j.etap.2026.105044 · Cited by 3 · see citing works
Mahdianipur, S., Maralani, M., Mohammadi, S., Khandoozi, S. R., Jafari, A., & Davoodi, H. (2024) · Cureus · doi:10.7759/cureus.70912 · Cited by 3 · see citing works
Aryl-hydrocarbon receptor in smooth muscle cells protects against dioxin-induced atherosclerosis
Qin, G. T., Zhao, Q., Fujita, A., Damiani, I., Easwaran, M., Basu, S., Gu, W., Bahia, G. K., Zheng, S., Li, D. Y., et al. (2026) · Communications Medicine · doi:10.1038/s43856-026-01871-5 · Cited by 3 · see citing works
Zhao, Y., Meijer, J., Walker, D. I., Kim, J., Portengen, L., Jones, D. P., Hosnijeh, F. S., Vlaanderen, J. J., & Vermeulen, R. C. H. (2023) · Environmental Science & Technology · doi:10.1021/acs.est.3c07588 · Cited by 3 · see citing works
Jang, H., Sohn, J., Kim, H. J., Seo, S. W., Noh, Y., Koh, S. B., Cho, J., & Kim, C. (2024) · Heliyon · doi:10.1016/j.heliyon.2024.e35614 · Cited by 3 · see citing works
Ufimtseva, E., Gileva, M. S., Kostenko, R. V., Kozlov, V. V., & Gulyaeva, L. F. (2024) · Cancers · doi:10.3390/cancers16162886 · Cited by 3 · see citing works
Kaleniuk, E., Holota, S. M., Skóra, B., Khyluk, D., Tabęcka-Łonczyńska, A., Lesyk, R., & Szychowski, K. A. (2024) · Applied Sciences · doi:10.3390/app14177692 · Cited by 3 · see citing works
Improving hydrocarbon toxicity tolerance in poultry: role of genes and antioxidants
Oleforuh-Okoleh, V. U., Sikiru, A. B., Kakulu, I. I., Fakae, B. B., Obianwuna, U. E., Shoyombo, A. J., Adeolu, A. I., Ollor, O. A., & Emeka, O. C. (2023) · Frontiers in Genetics · doi:10.3389/fgene.2023.1060138 · Cited by 3 · see citing works
Song, Y., Yen, S., Southam, K. A., Gaskin, S. E., Hoy, R. F., & Zosky, G. R. (2024) · Journal of Applied Toxicology · doi:10.1002/jat.4653 · Cited by 3 · see citing works
Smoke Signals: Unraveling the Link between Cigarette Smoking and Serum Liver Markers
Barapatre, A. R., Yadav, S. H., Vengurlekar, S. G., Shah, M. P., Kinage, K. G., Shardhul, J. P., & Pathare, S. S. (2024) · Asian Journal of Biochemistry Genetics and Molecular Biology · doi:10.9734/ajbgmb/2024/v16i3363 · Cited by 2 · see citing works
Synthesis and Evaluation of the AhR Activity of Indolo[3,2-b]carbazole Derivatives
Mexia, N., Tsakou, S., & Magiatis, P. (2025) · Molecules · doi:10.3390/molecules30030690 · Cited by 2 · see citing works
Herbet, M., Tkaczyk‐Wlizło, A., Wicha-Komsta, K., Twarowski, B., Ślaska, B., Kocki, T., Kowal, K., & Piątkowska‐Chmiel, I. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26209883 · Cited by 2 · see citing works
Cha, J., Gwak, J., Lee, J., Mok, S., Moon, H., Han, G. M., Hong, S. H., Khim, J. S., & Hong, S. (2025) · Environment International · doi:10.1016/j.envint.2025.109868 · Cited by 2 · see citing works
Plant proteins modulate m6A RNA methylation via the regulation of gut microbiota
Zhou, Y., Qin, Y., He, R., Cao, Y., Ye, H., Xu, W., & Peng, Y. (2026) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2026.151641 · Cited by 2 · see citing works
Zhu, G., & Man, J. (2026) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2026.1884283 · Cited by 2 · see citing works
Banerjee, O., Paul, T., Singh, S., Maji, B. K., & Mukherjee, S. (2024) · Naunyn-Schmiedeberg s Archives of Pharmacology · doi:10.1007/s00210-024-03506-9 · Cited by 2 · see citing works
RetractedThe AhR Is a Critical Regulator of the Pulmonary Response to Cannabis Smoke
Wilson, E. T., Gorgani, R., Heimbach, N. S., Bartolomucci, A., Tsering, T., Burnier, J. V., Eidelman, D. H., & Baglole, C. J. (2025) · The FASEB Journal · doi:10.1096/fj.202501533r · Cited by 1 · see citing works
Camacho‐Jiménez, L., Leyva‐Carrillo, L., Gómez‐Jiménez, S., & Yepiz-Plascencia, G. M. (2025) · Environmental Toxicology and Pharmacology · doi:10.1016/j.etap.2025.104854 · Cited by 1 · see citing works
Le, P., Hao, L. V., Nhat, T., Le, H.-S., & Le, T. A. D. (2025) · Environmental Toxicology and Pharmacology · doi:10.1016/j.etap.2025.104911 · Cited by 1 · see citing works
Avaltroni, F., Bürki, C., Weichmann, F., Percoco, G., Peno‐Mazzarino, L., & Lati, E. (2026) · Cosmetics · doi:10.3390/cosmetics13010026 · Cited by 1 · see citing works
Kim, M.-S., Kim, Y.-I., Kim, S., & Chang, S.-Y. (2026) · Environment International · doi:10.1016/j.envint.2026.110140 · Cited by 1 · see citing works
Rammal, H., Noonan, A. M., Rivas, D., Sibai, D. S., Marcangeli, V., & Duque, G. (2026) · Biochimie · doi:10.1016/j.biochi.2026.02.016 · Cited by 1 · see citing works
Life-Course Programming of Kidney Disease: Roles of Gut Microbiota Dysbiosis and Oxidative Stress
Hsu, C., & Tain, Y. (2026) · Antioxidants · doi:10.3390/antiox15060707 · Cited by 1 · see citing works
Gök, M., Çiçek, Ç., Sarı, S., Sönmez, G., & Bodur, E. (2026) · European Journal of Therapeutics · doi:10.58600/eurjther3107 · Cited by 1 · see citing works
El-Bouhy, Z. M., Rahman, A. N. A., Mohamed, F. A. S., Elashhab, M. W. A., Khamis, T., & Reda, R. M. (2026) · Scientific Reports · doi:10.1038/s41598-026-57004-4 · Cited by 1 · see citing works
Aryl Hydrocarbon Receptor Signaling in Aging: A Key Modulator of Brain Homeostasis
Juárez-Solano, H., Martínez‐Coria, H., Pérez‐Osorio, I. N., Hernández-Esquivel, R. A., & Torres-Ramos, M. (2026) · Molecular Neurobiology · doi:10.1007/s12035-026-05874-0 · Cited by 1 · see citing works
The gut microbiome and mitochondrial function in metabolism, immunity, and disease
Han, E. J., Kim, D., Lee, J. H., & Chung, H. (2026) · Gut Microbes · doi:10.1080/19490976.2026.2699451 · Cited by 1 · see citing works
Wu, H., Cao, H., Ye, Z., Li, Z., Chang, M., Zhang, W., Xu, T., Wang, L., Yang, T., Deng, X., et al. (2026) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2026.1836387 · Cited by 1 · see citing works
A Perfect Storm of Pollutants: Environmental Mixtures in the Pathogenesis of Atherosclerosis
Gorini, F., Palazzo, M., Simonini, L., Tonacci, A., Rizza, A., Wu, H., Minichilli, F., & Borghini, A. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27177624 · Cited by 1 · see citing works
Kang, J., Seo, D. S., Ahmad, Y., Park, S., Yoo, J., Lee, J. H., Baek, S., Joo, S., Kwon, H., Bae, H. J., et al. (2025) · Life Sciences · doi:10.1016/j.lfs.2025.123811 · Cited by 1 · see citing works
Roumak, V. S., Мышлявкина, Т. А., Lavrenov, A. R., Шелепчиков, А. А., & Umnova, N. V. (2023) · Russian Journal of Occupational Health and Industrial Ecology · doi:10.31089/1026-9428-2023-63-9-617-626
Алексеевна, Н. Н., & Dolgikh, О. V. (2023) · Hygiene and Sanitation · doi:10.47470/0016-9900-2023-102-11-1204-1209
- Authors
- Grishanova, A. Y., & Perepechaeva, M. L.
- Affiliations
- Federal Research Center of Fundamental and Translational Medicine (RU)
- Corresponding author
- Perepechaeva, Maria L.
- Venue
- International Journal of Molecular Sciences
- Publisher
- MDPI AG
- Published
- 2022-06-16
- Volume
- 23
- Issue
- 12
- Pages
- 6719
- ISSN
- 1422-0067 (ISSN-L)
- PMC
- PMC9224361
- OpenAlex
- W4283017800
- Cited by
- 130
- References
- 379
- Citations by year
- 2026: 38 · 2025: 39 · 2024: 32 · 2023: 19 · 2022: 2
- FWCI
- 2.24
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- International Journal of Molecular Sciences (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- budgetary financing project (FGMU-2022-0004, N1021050601082-2-1.6.4;3.1.6)
- Topics
- Physical Sciences › Environmental Science › Health, Toxicology and Mutagenesis › Toxic Organic Pollutants Impact
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics, phytochemicals, and oxidative stress
- Life Sciences › Pharmacology, Toxicology and Pharmaceutics › Pharmacology › Pharmacogenetics and Drug Metabolism
- Keywords
- aryl hydrocarbon receptor, oxidative stress, xenobiotic metabolism, cytochrome P450, antioxidant enzymes, redox signaling, transcriptional regulation, therapeutic target, pathogenesis
- MeSH terms
- Gene Expression Regulation, Humans, Xenobiotics, Reactive Oxygen Species, Receptors, Aryl Hydrocarbon, 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 ›
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