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In vitro analysis of Ah receptor domains involved in ligand-activated DNA recognition.
Open accessAbstract
The Ah receptor (AHR) is a basic helix-loop-helix protein that mediates the effects of 2,3,7,8-tetrachloro-dibenzo-p-dioxin. In this report, we describe a rabbit reticulocyte system that allows functional expression of both the AHR and its dimeric partner, the AHR nuclear translocator protein (ARNT). By using this in vitro system, we were able to reconstitute agonist binding to the AHR and agonist-induced AHR-ARNT recognition of a cognate DNA enhancer sequence. Expression of AHR deletion mutants revealed the location of N-terminal domains responsible for ligand and DNA recognition and C-terminal domains that play roles in agonist-induced DNA recognition.
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“Based on previous domain mapping studies, this mutation occurs in the PAS B domain, near a region predicted to encode the ligand and chaperone binding domains (Figure 2, Figure 4) (Dolwick, Swanson, et al., 1993; Fukunaga & Hankinson, 1996).”
From Rodent Genetic Models of Ah Receptor Signaling (2021) · cites this paper as Dolwick, Swanson, et al., 1993
In the citing paper
“Interestingly, this C-ter loop also locates within a previously identified “repressor” region of ~ 200 residues that could be “depressed” by the agonist-induced receptor transformation16.”
From Structural basis for the ligand-dependent activation of heterodimeric AHR-ARNT complex (2025) · cites this paper as [16]
Citations
Cites
Molecular Cloning: A Laboratory Manual
Sambrook, J., Fritsch, E., & Maniatis, T. (1989) · UCLA - Biblioteca de Ciencias de la Salud · Cited by 133,589
LIGAND: A versatile computerized approach for characterization of ligand-binding systems
Munson, P. J., & Rodbard, D. (1980) · Analytical Biochemistry · doi:10.1016/0003-2697(80)90515-1 · Cited by 8,373
An analysis of 5'-noncoding sequences from 699 vertebrate messenger RNAs
Kozak, M. (1987) · Nucleic Acids Research · doi:10.1093/nar/15.20.8125 · Cited by 5,090
The Leucine Zipper: A Hypothetical Structure Common to a New Class of DNA Binding Proteins
Landschulz, W. H., Johnson, P. F., & McKnight, S. L. (1988) · Science · doi:10.1126/science.3289117 · Cited by 3,443
Murre, C., Page-McCaw, P., & Baltimore, D. (1989) · Cell · doi:10.1016/0092-8674(89)90682-x · Cited by 2,713
Poland, A., & Knutson, J. C. (1982) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pa.22.040182.002505 · Cited by 2,515
Max: A Helix-Loop-Helix Zipper Protein That Forms a Sequence-Specific DNA-Binding Complex with Myc
Blackwood, E. M., & Eisenman, R. N. (1991) · Science · doi:10.1126/science.2006410 · Cited by 1,681
The myoD Gene Family: Nodal Point During Specification of the Muscle Cell Lineage
Weintraub, H. M., Davis, R. L., Tapscott, S. J., Thayer, M., Krause, M., Benezra, R., Blackwell, T. K., Turner, D. L., Rupp, R. A. W., Hollenberg, S. M., et al. (1991) · Science · doi:10.1126/science.1846704 · Cited by 1,581
P450 GENES: STRUCTURE, EVOLUTION, AND REGULATION
Nebert, D. W., & Gonzalez, F. J. (1987) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.56.070187.004501 · Cited by 1,580
Poland, A., Glover, E., & Kende, A. S. (1976) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)33205-2 · Cited by 1,370
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Items 101–200 of 239
Wilhelmsson, A., Whitelaw, M. L., Gustafsson, J. A., & Poellinger, L. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)32269-x · Cited by 73
Drug–Drug Interactions Involving Intestinal and Hepatic CYP1A Enzymes
Klomp, F., Wenzel, C., Droździk, M., & Oswald, S. (2020) · Pharmaceutics · doi:10.3390/pharmaceutics12121201 · Cited by 70
Paralogous Genes Involved in Juvenile Hormone Action in Drosophila melanogaster
Baumann, A. A., Barry, J., Wang, S., Fujiwara, Y., & Wilson, T. G. (2010) · Genetics · doi:10.1534/genetics.110.116962 · Cited by 69
Identification of the Ah-Receptor Structural Determinants for Ligand Preferences
Xing, Y., Nukaya, M., Satyshur, K. A., Jiang, L., Stanevich, V., Korkmaz, E. N., Burdette, L., Kennedy, G. D., Cui, Q., & Bradfield, C. A. (2012) · Toxicological Sciences · doi:10.1093/toxsci/kfs194 · Cited by 67
Self-citationStructural basis for the ligand-dependent activation of heterodimeric AHR-ARNT complex
Diao, X., Shang, Q., Guo, M., Huang, Y., Zhang, M., Chen, X., Liang, Y., Sun, X., Zhou, F., Zhuang, J., et al. (2025) · Nature communications · doi:10.1038/s41467-025-56574-7 · Cited by 72
Mann, K. K., Matulka, R. A., Hahn, M. E., Trombino, A. F., Lawrence, B. P., Kerkvliet, N. I., & Sherr, D. H. (1999) · Toxicology and Applied Pharmacology · doi:10.1006/taap.1999.8778 · Cited by 66
Numayama‐Tsuruta, K., Kobayashi, A., Sogawa, K., & Fujii‐Kuriyama, Y. (1997) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1997.00486.x · Cited by 66
Gradin, K., Whitelaw, M. L., Toftgård, R., Poellinger, L., & Berghard, A. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)31586-7 · Cited by 66
Pollenz, R. S., & Barbour, E. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.16.6095-6104.2000 · Cited by 65
Brunskill, E. W., Witte, D. P., Shreiner, A. B., & Potter, S. S. (1999) · Mechanisms of Development · doi:10.1016/s0925-4773(99)00182-3 · Cited by 64
Rushing, S. N., & Denison, M. S. (2002) · Archives of Biochemistry and Biophysics · doi:10.1016/s0003-9861(02)00233-3 · Cited by 64
Identification of amino acid residues in the Ah receptor involved in ligand binding
Goryo, K., Suzuki, A., Carpio, C. A. D., Siizaki, K., Kuriyama, E., Mikami, Y., Kinoshita, K., Yasumoto, K., Rannug, A., Miyamoto, A., et al. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.12.227 · Cited by 64
Volkova, M., Palmeri, M., Russell, K. S., & Russell, R. R. (2011) · Cardiovascular Research · doi:10.1093/cvr/cvr007 · Cited by 62
Sun, W., Zhang, J., & Hankinson, O. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.50.31845 · Cited by 63
Hahn, M. E., & Karchner, S. I. (1995) · Biochemical Journal · doi:10.1042/bj3100383 · Cited by 58
Reitzel, A. M., Karchner, S. I., Franks, D. G., Evans, B. R., Nacci, D. E., Champlin, D. M., Vieira, V. M., & Hahn, M. E. (2014) · BMC Evolutionary Biology · doi:10.1186/1471-2148-14-6 · Cited by 58
Roman, B. L., & Peterson, R. E. (1998) · Toxicology and Applied Pharmacology · doi:10.1006/taap.1997.8362 · Cited by 57
Mapping the Protein/DNA Contact Sites of the Ah Receptor and Ah Receptor Nuclear Translocator
Swanson, H. I., & Jun-hua, Y. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.49.31657 · Cited by 54
Self-citationThe Aryl Hydrocarbon Receptor Interacts with Transcription Factor IIB
Swanson, H. I., & Yang, J.-H. (1998) · Molecular Pharmacology · doi:10.1016/s0026-895x(24)13068-4 · Cited by 53
Self-citationPowell, W. H., Karchner, S. I., Bright, R., & Hahn, M. E. (1999) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1998.0992 · Cited by 52
Cryo-EM structure of the cytosolic AhR complex.
Wen, Z., Zhang, Y., Zhang, B., Hang, Y., Xu, L., Chen, Y., Xie, Q., Zhao, Q., Zhang, L., Li, G., et al. (2023) · Structure · doi:10.1016/j.str.2022.12.013 · Cited by 51
Wong, J. M. Y., Harper, P. A., Meyer, U., Bock, K. W., Mörike, K., Lagueux, J., Ayotte, P., Tyndale, R. F., Sellers, E. M., Manchester, D., et al. (2001) · Pharmacogenetics · doi:10.1097/00008571-200102000-00010 · Cited by 50
Reick, M., Robertson, R. W., Pasco, D. S., & Fagan, J. B. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.9.5653 · Cited by 51
Borràs, M., Laı̈os, I., Khissiin, A. E., Seo, H., Lempereur, F., Legros, N., & Leclercq, G. (1996) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/0960-0760(95)00272-3 · Cited by 50
Vaziri, C., Schneider, A., Sherr, D. H., & Faller, D. V. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.42.25921 · Cited by 50
The aromatic hydrocarbon receptor, dioxin action, and endocrine homeostasis
Whitlock, J. P. (1994) · Trends in Endocrinology and Metabolism · doi:10.1016/1043-2760(94)90075-2 · Cited by 49
Korkalainen, M., Tuomisto, J., & Pohjanvirta, R. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.5317 · Cited by 47
Chan, W. K., Chu, R., Jain, S. R., Reddy, J. K., & Bradfield, C. A. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47217-1 · Cited by 48
Self-citationSpecificity of DNA binding of the c-Myc/Max and ARNT/ARNT dimers at the CACGTG recognition site
Swanson, H. I., & Yang, J.-H. (1999) · Nucleic Acids Research · doi:10.1093/nar/27.15.3205 · Cited by 47
Self-citationUnique Property of Some Synthetic Retinoids: Activation of the Aryl Hydrocarbon Receptor Pathway
Gambone, C. J., Hutcheson, J. M., Gabriel, J. L., Beard, R. L., Chandraratna, R. A. S., Soprano, K. J., & Soprano, D. R. (2002) · Molecular Pharmacology · doi:10.1016/s0026-895x(24)12866-0 · Cited by 47
Yamaguchi, K., Matulka, R. A., Shneider, A. M., Toselli, P. A., Trombino, A. F., Yang, S., Hafer, L. J., Mann, K. K., Tao, X.-J., Tilly, J. L., et al. (1997) · Toxicology and Applied Pharmacology · doi:10.1006/taap.1997.8263 · Cited by 47
Fu, C., Li, Y., Xi, H., Niu, Z., Chen, N., Wang, R., Yan, Y., Gan, X., Wang, M., Zhang, W., et al. (2022) · Frontiers in Nutrition · doi:10.3389/fnut.2022.978475 · Cited by 50
Jensen, B. A., & Hahn, M. E. (2001) · Toxicological Sciences · doi:10.1093/toxsci/64.1.41 · Cited by 44
Long, W. P., Chen, X., & Perdew, G. H. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.18.12391 · Cited by 44
Molecular characterization of the murine Hif-1 alpha locus.
Luo, G., Gu, Y.-Z., Jain, S. R., Chan, W. K., Carr, K. M., Hogenesch, J. B., & Bradfield, C. A. (1997) · Europe PMC (PubMed Central) · Cited by 44
Self-citationCharacterization of Three Splice Variants and Genomic Organization of the Mouse BMAL1 Gene
Yu, W., Ikeda, M., Abe, H., Honma, S., Ebisawa, T., Yamauchi, T., Honma, K.-I., & Nomura, M. (1999) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1999.0970 · Cited by 43
O’Driscoll, C. A., & Mezrich, J. D. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.02833 · Cited by 47
Merisalu, A., Punab, M., Altmäe, S., Haller, K., Tiido, T., Peters, M., & Salumets, A. (2007) · Fertility and Sterility · doi:10.1016/j.fertnstert.2006.12.041 · Cited by 40
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Korkalainen, M., Tuomisto, J., & Pohjanvirta, R. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.2931 · Cited by 38
Liu, N., Pan, L., Miao, J., Xu, C., & Zhang, L. (2010) · Comparative Biochemistry and Physiology Part C Toxicology & Pharmacology · doi:10.1016/j.cbpc.2010.05.004 · Cited by 38
The p53 Inhibitor Pifithrin-α Is a Potent Agonist of the Aryl Hydrocarbon Receptor
Hoagland, M. S., Hoagland, E. M., & Swanson, H. I. (2005) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.105.084186 · Cited by 40
Self-citationSoshilov, A. A., Motta, S., Bonati, L., & Denison, M. S. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21072474 · Cited by 36
Novel DNA Binding by a Basic Helix-Loop-Helix Protein
Chapman-Smith, A., & Whitelaw, M. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m512145200 · Cited by 44
Zhou, H., Qu, Y., Wu, H., Liao, C., Zheng, J., Diao, X., & Xue, Q. (2009) · Chemosphere · doi:10.1016/j.chemosphere.2009.09.012 · Cited by 37
Zordoky, B. N. M., & El‐Kadi, A. O. S. (2009) · Toxicology in Vitro · doi:10.1016/j.tiv.2009.12.002 · Cited by 36
Mechanism of Signal Transduction by the basic Helix-Loop-Helix Dioxin Receptor
Poellinger, L. (1995) · Birkhäuser Boston eBooks · doi:10.1007/978-1-4684-6840-3_6 · Cited by 33
Hankinson, O. (1994) · Trends in Endocrinology and Metabolism · doi:10.1016/1043-2760(94)p3082-i · Cited by 33
Yao, G., Craven, M. W., Drinkwater, N. R., & Bradfield, C. A. (2004) · PLoS Biology · doi:10.1371/journal.pbio.0020065 · Cited by 32
Self-citationWalsh, A. A., Tullis, K. M., Rice, R. H., & Denison, M. S. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.37.22746 · Cited by 31
FUNCTIONAL ANALYSIS OF SIX HUMAN ARYL HYDROCARBON RECEPTOR VARIANTS IN A JAPANESE POPULATION
Koyano, S., Saito, Y., Fukushima‐Uesaka, H., Ishida, S., Ozawa, S., Kamatani, N., Minami, H., Ohtsu, A., Hamaguchi, T., Shirao, K., et al. (2005) · Drug Metabolism and Disposition · doi:10.1124/dmd.105.004655 · Cited by 28
Induction of Cytochrome P450 Enzymes
Williams, S. N., Dunham, E. E., & Bradfield, C. A. (2007) · Springer eBooks · doi:10.1007/0-387-27447-2_8 · Cited by 28
Self-citationZhao, N., Li, J., Li, L., Niu, X., Jiang, M., He, X., Bian, Z., Zhang, G., & Lü, A. (2015) · Acta Pharmacologica Sinica · doi:10.1038/aps.2015.15 · Cited by 27
P450 Cytochromes and Hormonal Regulation: An Overview
Jefcoate, C. R. E. (1996) · Advances in molecular and cell biology · doi:10.1016/s1569-2558(08)60338-0 · Cited by 25
Zhang, L. (2003) · Toxicology and Applied Pharmacology · doi:10.1016/s0041-008x(03)00276-x · Cited by 24
Wu, J., Pang, T., Lin, Z., Zhao, M., & Jin, H. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.965941 · Cited by 25
Kim, E.-Y., & Hahn, M. E. (2002) · Aquatic Toxicology · doi:10.1016/s0166-445x(01)00221-1 · Cited by 22
The aryl hydrocarbon receptor as a model PAS sensor
Vazquez-Rivera, E., Rojas, B. L., Parrott, J. C., Shen, A. L., Xing, Y., Carney, P. R., & Bradfield, C. A. (2021) · Toxicology Reports · doi:10.1016/j.toxrep.2021.11.017 · Cited by 22
Self-citationCloning and chromosomal localization of a new member of the bHLH/PAS transcription factor family
Wolting, C. D., & McGlade, C. J. (1998) · Mammalian Genome · doi:10.1007/s003359900797 · Cited by 20
Cloning of Hypoxia-Inducible Factor 1α cDNA from Chick Embryonic Ventricular Myocytes
Takahashi, T., Sugishita, Y., Nojiri, T., Shimizu, T., Yao, A., Kinugawa, K., Harada, K., & Nagai, R. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.4463 · Cited by 19
Ikegwuonu, F. I., Christou, M., & Jefcoate, C. R. E. (1999) · Biochemical Pharmacology · doi:10.1016/s0006-2952(98)00344-x · Cited by 18
Yamaguchi, Y., & Kuo, M. T. (1995) · Biochemical Pharmacology · doi:10.1016/0006-2952(95)02016-6 · Cited by 18
Minsavage, G. D., Vorojeikina, D. P., & Gasiewicz, T. A. (2003) · Archives of Biochemistry and Biophysics · doi:10.1016/s0003-9861(03)00033-x · Cited by 18
Rodent Genetic Models of Ah Receptor Signaling
Wilson, R. H., & Bradfield, C. A. (2021) · Drug Metabolism Reviews · doi:10.1080/03602532.2021.1955916 · Cited by 16
“Based on previous domain mapping studies, this mutation occurs in the PAS B domain, near a region predicted to encode the ligand and chaperone binding domains (Figure 2, Figure 4; Dolwick et al. 1993; Fukunaga and Hankinson 1996).”
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Familiar and novel reproductive endocrine disruptors: xenoestrogens, dioxins and nanoparticles.
Hutz, R. J., Carvan, M. J., Larson, J. K., Liu, Q., STELZER, R., King‐Heiden, T. C., Baldridge, M. G., Shahnoor, N., & Julien, K. (2014) · PubMed · Cited by 17
Levine, S. L., & Perdew, G. H. (2001) · Molecular Pharmacology · doi:10.1124/mol.59.3.557 · Cited by 17
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Xu, C., Siu, C.-S., & Pasco, D. S. (1998) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1998.0851 · Cited by 17
Levine, S. L., Petrulis, J. R., Dubil, A., & Perdew, G. H. (2000) · Molecular Pharmacology · doi:10.1124/mol.58.6.1517 · Cited by 17
Thomae, T. L., Stevens, E. A., Liss, A. L., Drinkwater, N. R., & Bradfield, C. A. (2005) · Molecular Pharmacology · doi:10.1124/mol.105.019760 · Cited by 16
Self-citationCoumailleau, P., Penrad‐Mobayed, M., Boulangé-Lecomte, C., Bollérot, K., Simon, F., Poellinger, L., & Angelier, N. (2000) · Mechanisms of Development · doi:10.1016/s0925-4773(00)00468-8 · Cited by 16
Mo, Z., Li, P., Cao, Z., & Zhang, S. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.564948 · Cited by 15
Long, W. P., & Perdew, G. H. (1999) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1999.1452 · Cited by 16
Tumova, S., Doležel, D., & Jindra, M. (2023) · Journal of Molecular Biology · doi:10.1016/j.jmb.2023.168332 · Cited by 14
Necela, B. M., & Pollenz, R. S. (1999) · Biochemical Pharmacology · doi:10.1016/s0006-2952(99)00036-2 · Cited by 14
History of Research on the AHR
Gasiewicz, T. A., & Henry, E. C. (2011) · Wiley eBooks · doi:10.1002/9781118140574.ch1 · Cited by 14
Wang, X., Bi, S., Tang, Y., Zhang, G., Huang, C., Wan, F., Lü, Z., & Liu, W. (2023) · Open Biology · doi:10.1098/rsob.220372 · Cited by 13
Xie, J., Huang, X., Park, M. S., Pham, H. M., & Chan, W. K. (2014) · Biochemical Pharmacology · doi:10.1016/j.bcp.2014.01.021 · Cited by 13
Palatnik, A., Xin, H., & Su, E. J. (2016) · Placenta · doi:10.1016/j.placenta.2016.06.004 · Cited by 13
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Lee, S.-K., Kim, Y., Kim, M. Y., Chun, Y., & Kim, S. (2004) · Journal of Toxicology and Environmental Health · doi:10.1080/15287390490514642 · Cited by 13
DNA Binding and Transcriptional Enhancement by Purified TCDD·Ah Receptor Complex
Henry, E. C., Kent, T. A., & Gasiewicz, T. A. (1997) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1996.9873 · Cited by 12
(2005) · Humana Press eBooks · doi:10.1385/1592598323 · Cited by 11
Cho, M., Park, J.-G., Iwata, H., & Kim, E.-Y. (2021) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2021.111947 · Cited by 10
Nagyová, J., Pastorek, J., & Kopáček, J. (2004) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/j.bbaexp.2004.08.002 · Cited by 10
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Swanson, H. I. (2011) · Wiley eBooks · doi:10.1002/9781118140574.ch5 · Cited by 9
Self-citationInteractions of Procarcinogenic Heterocyclic Amines and Indolocarbazoles withthe Dioxin Receptor
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Self-citationARNT: A Key bHLH/PAS Regulatory Protein Across Multiple Pathways
Dougherty, E. J., & Pollenz, R. S. (2010) · Elsevier eBooks · doi:10.1016/b978-0-08-046884-6.00214-1 · Cited by 7
Marquez, E., Traylor‐Knowles, N., Novillo, A., & Callard, I. P. (2011) · Comparative Biochemistry and Physiology Part C Toxicology & Pharmacology · doi:10.1016/j.cbpc.2011.06.017 · Cited by 6
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Li, Y., Luu, T. C., & Chan, W. K. (2005) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2005.06.026 · Cited by 6
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Matysiak, A. (2016) · Studia Demograficzne · Cited by 6
Döhr, O., Li, W., Donat, S., Vogel, C. F. A., & Abel, J. (1996) · Advances in experimental medicine and biology · doi:10.1007/978-1-4757-9480-9_54 · Cited by 6
Wache, S., Hoagland, E. M., Zeigler, G., & Swanson, H. I. (2005) · Gene Expression · doi:10.3727/000000005783991981 · Cited by 5
Self-citationAh receptors and the mechanism of dioxin toxicity: insights from homology and phylogeny
Hahn, M. E. (1996) · Springer eBooks · doi:10.1007/978-94-009-1523-7_2 · Cited by 5
Korkalainen, M. (2005) · Työväentutkimus Vuosikirja · Cited by 5
Yao, G., Harstad, E. B., & Bradfield, C. A. (2003) · Springer eBooks · doi:10.1007/978-1-4615-0515-0_7 · Cited by 4
Self-citationLe récepteur de la dioxine : rôle endogène et médiateur de la toxicité de la dioxine
Chevallier, A., Bui, L. C., & Coumoul, X. (2011) · Cahiers de Nutrition et de Diététique · doi:10.1016/j.cnd.2011.01.002 · Cited by 4
Pharmacological interactions between phenylbenzothiazoles and aryl hydrocarbon receptor (AhR)
Bazzi, R. (2008) · Nottingham ePrints (University of Nottingham) · Cited by 4
Stem Cells, Hypoxia and Hypoxia-Inducible Factors
Watt, S. M., Tsaknakis, G., Forde, S. P., & Carpenter, L. (2009) · Humana Press eBooks · doi:10.1007/978-1-60327-227-8_18 · Cited by 4
Metadata
- Authors
- Dolwick, K. M., Swanson, H. I., & Bradfield, C. A.
- Affiliations
- Northwestern University (US)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 1993-09-15
- Volume
- 90
- Issue
- 18
- Pages
- 8566-8570
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC47398
- OpenAlex
- W1979697640
- Cited by
- 239
- References
- 37
- Citations by year
- 2026: 2 · 2025: 1 · 2023: 4 · 2022: 4 · 2021: 5 · 2020: 4 · 2019: 1 · 2018: 7 · 2017: 6 · 2016: 2 · 2015: 3 · 2014: 6 · 2013: 4 · 2012: 3
- FWCI
- 17.52
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Cancer Institute (T32 CA09560, T32CA009560)
- National Institute of Environmental Health Sciences (ES-05703, F32ES005589, ES-05589)
- Topics
- Physical Sciences › Environmental Science › Health, Toxicology and Mutagenesis › Toxic Organic Pollutants Impact
- Life Sciences › Pharmacology, Toxicology and Pharmaceutics › Pharmacology › Pharmacogenetics and Drug Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Receptors and Signaling
- Keywords
- aryl hydrocarbon receptor, ligand binding, DNA recognition, enhancers, bHLH transcription factors, 2,3,7,8-tetrachlorodibenzo-p-dioxin
- MeSH terms
- Polychlorinated Dibenzodioxins, Animals, Base Sequence, Binding Sites, Codon, DNA, Ligands, Molecular Sequence Data, Oligodeoxyribonucleotides, Rabbits, Receptors, Drug, Reticulocytes, Transcription, Genetic, Protein Biosynthesis, Blotting, Western, Polymerase Chain Reaction, Mutagenesis, Site-Directed, Sequence Deletion, Receptors, Aryl Hydrocarbon, Mice
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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