Definition of a Dioxin Receptor Mutant That Is a Constitutive Activator of Transcription
Open accessAbstract
The intracellular dioxin (aryl hydrocarbon) receptor is a ligand-activated transcription factor that mediates the adaptive and toxic responses to environmental pollutants such as 2,3,7,8-tetrachlorodibenzo-p-dioxin and structurally related congeners. Whereas the ligand-free receptor is characterized by its association with the molecular chaperone hsp90, exposure to ligand initiates a multistep activation process involving nuclear translocation, dissociation from the hsp90 complex, and dimerization with its partner protein Arnt. In this study, we have characterized a dioxin receptor deletion mutant lacking the minimal ligand-binding domain of the receptor. This mutant did not bind ligand and localized constitutively to the nucleus. However, this protein was functionally inert since it failed to dimerize with Arnt and to bind DNA. In contrast, a dioxin receptor deletion mutant lacking the minimal PAS B motif but maintaining the N-terminal half of the ligand-binding domain showed constitutive dimerization with Arnt, bound DNA, and activated transcription in a ligand-independent manner. Interestingly, this mutant showed a more potent functional activity than the dioxin-activated wild-type receptor in several different cell lines. In conclusion, the constitutively active dioxin receptor may provide an important mechanistic tool to investigate receptor-mediated regulatory pathways in closer detail.
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Deletion of residues 287-421 results in a ligand-independent constitutively active AhR.
“Moreover, deletion of residues 287-421 results in a ligand-independent constitutively active AhR consistent the role of the AhR LBD-hsp90 complex in regulating AhR functionality (18).”
From Structural and Functional Characterization of the Aryl Hydrocarbon Receptor Ligand Binding Domain by Homology Modeling and Mutational Analysis (2007) · cites this paper as [18]
The Abstract reports that deleting amino acids 288–421 produced a constitutively active dioxin (AhR) receptor that stimulated transcription without ligand. The cited claim gives the deletion as 287–421; our copy supports the functional result but not that exact residue range. (LLM, conf=0.87)
Experimental — accuracy not yet measuredAHR mutants lacking the PAS B domain constitutively dimerize with ARNT, bind AHREs, and induce AHRE-driven genes independently of ligand.
“Early evidence from domain mapping studies demonstrated that Ahr mutants lacking the PAS B domain constitutively dimerize with ARNT, bind to AHREs, and induce transcription of AHRE-driven genes in a manner that is independent of ligand binding (Andersson et al., 2002; J. McGuire et al., 2001).”
From Rodent Genetic Models of Ah Receptor Signaling (2021) · cites this paper as J. McGuire et al., 2001
The effect of deleting residues 287-421 is consistent with the role of the AhR LBD-hsp90 complex in regulating AhR functionality.
“Moreover, deletion of residues 287-421 results in a ligand-independent constitutively active AhR consistent the role of the AhR LBD-hsp90 complex in regulating AhR functionality (18).”
From Structural and Functional Characterization of the Aryl Hydrocarbon Receptor Ligand Binding Domain by Homology Modeling and Mutational Analysis (2007) · cites this paper as [18]
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“CA-Ahr lacks the PAS-B domain, enabling it to constitutively dimerize with Arnt, bind to DNA, and activate transcription in a ligandindependent manner (McGuire et al., 2001).”
BackgroundLigand binding and activation of the Ah receptor
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A Constitutively Active Dioxin/Aryl Hydrocarbon Receptor Promotes Hepatocarcinogenesis in Mice
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“CA-AhR (8) was subcloned into pE SR containing the mouse immunoglob-”
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“This intervening region between the PAS-A and PAS-B repeats has been shown to be important for the ability of AHR to dimerize with ARNT (McGuire et al., 2001; Chapman-Smith et al., 2004).”
BackgroundResultThe Aryl Hydrocarbon Receptor Preferentially Marks and Promotes Gut Regulatory T Cells
Ye, J., Qiu, J., Bostick, J. W., Ueda, A., Schjerven, H., Li, S., Jobin, C., Chen, Z. E., & Zhou, L. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.10.114 · Cited by 180 · see citing works
“, constitutively active [CA]-Ahr) (McGuire et al., 2001).”
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“Moreover, deletion of residues 287–421 results in a ligand-independent constitutively active AhR consistent the role of the AhR LBD–hsp90 complex in regulating AhR functionality (18).”
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“, constitutively active (CA)-Ahr) [18].”
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Intrinsic AhR function underlies cross-talk of dioxins with sex hormone signalings.
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“This AhR mutant has been reported to localize to the nucleus, heterodimerize with ARNT, and activate transcription by binding xenobiotic response element sequences in a ligandindependent manner (McGuire et al., 2001).”
BackgroundMethodRole of the Per/Arnt/Sim Domains in Ligand-dependent Transformation of the Aryl Hydrocarbon Receptor
Soshilov, A., & Denison, M. S. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m802414200 · Cited by 99 · see citing works
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Effects of Aryl Hydrocarbon Receptor Signaling on the Modulation of Th1/Th2 Balance1
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“Deletion of the ligand-binding domain (PAS B domain) converts AhR into a constitutively active molecule, even in the absence of ligand (15).”
BackgroundDifferential Activities of Murine Single Minded 1 (SIM1) and SIM2 on a Hypoxic Response Element
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“1A).2 Constitutively activated human AHR was constructed by deleting the minimal ligand-binding domain of AHR.18 The liverspecific expression of CA-AHR was confirmed at both the mRNA and protein levels, without affecting the expression of endogenous AHR (Supporting Fig.”
BackgroundInfluentialIto, T., Tsukumo, S., Suzuki, N., Motohashi, H., Yamamoto, M. P., Fujii‐Kuriyama, Y., Mimura, J., Lin, T.-M., Peterson, R. E., Tohyama, C., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m402143200 · Cited by 69 · see citing works
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Role of Aryl Hydrocarbon Receptor in Circadian Clock Disruption and Metabolic Dysfunction
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“(55) recently produced Tg mice expressing a CA-AhR mutant (30), which has a structure very similar to the one we used, under the control of an Ig H chain enhancer (E ), which promotes transgene expression in both B- and T-lineage cells (56).”
BackgroundMethodGoode, G., Ballard, B., Manning, H., Freeman, M., Kang, Y.-B., & Eltom, S. E. (2013) · International Journal of Cancer · doi:10.1002/ijc.28297 · Cited by 66 · see citing works
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“This novel role for AhR is independent of ligand activation, therefore this work is distinct from, although it complements the studies using constitutively active AhR [57-59].”
BackgroundResultReitzel, A., Karchner, S., Franks, D., Evans, B. R., Nacci, D., Champlin, D., Vieira, V., & Hahn, M. (2014) · BMC Evolutionary Biology · doi:10.1186/1471-2148-14-6 · Cited by 56 · see citing works
“Two ns-SNPs were found in the Nterminal half: a ns-SNP in the N-terminal basic region results in a conservative Lys to Arg change, and a nsSNP in the PAS domain results in a non-conservative Ile to Ser change between the PAS-A and PAS-B repeats, in a region that is poorly conserved among species, but may have function…”
MECHANISMS OF CIRCADIAN CLOCK INTERACTIONS WITH ARYL HYDROCARBON RECEPTOR SIGNALING
Tischkau, S. A. (2019) · European Journal of Neuroscience · doi:10.1111/ejn.14361 · Cited by 55 · see citing works
“PAS domains in AhR bind ligands and regulate interaction with partners that are required to direct it to specific sequences on the promoters of target genes (McGuire et al., 2001; ReiszPorszasz, Probst, Fukunaga, & Hankinson, 1994).”
BackgroundRico-Leo, E., Álvarez-Barrientos, A., & Fernández-Salguero, P. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.425009 · Cited by 53 · see citing works
“This constitutively active receptor heterodimerizes with ARNT and has intrinsic transcriptional activity in a ligand-independent manner (34).”
BackgroundTanaka, T., Yamaguchi, J., Shoji, K., & Nangaku, M. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.374587 · Cited by 50 · see citing works
Cardiac Myocyte-Specific AHR Activation Phenocopies TCDD-Induced Toxicity in Zebrafish
Lanham, K. A., Plavicki, J. S., Peterson, R. E., & Heideman, W. (2014) · Toxicological Sciences · doi:10.1093/toxsci/kfu111 · Cited by 51 · see citing works
“Our initial attempts to construct a caAHR for zebrafish were based on reports that deletion of the PAS B domain of themouse Ahb-1 allele made a mouse caAHR (McGuire et al., 2001).”
BackgroundMethodInfluentialIdentification of residues in the N-terminal PAS domains important for dimerization of Arnt and AhR
Hao, N., Whitelaw, M. L., Shearwin, K. E., Dodd, I. B., & Chapman‐Smith, A. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkq1336 · Cited by 51 · see citing works
“B, the ligand binding domain, in AhR produces a constitutively active receptor more potent than the intact protein (14).”
BackgroundSelf-citationWejheden, C., Brunnberg, S., Larsson, S., Lind, P., Andersson, G., & Hanberg, A. (2010) · Toxicological Sciences · doi:10.1093/toxsci/kfp284 · Cited by 46 · see citing works
“288–421 in the ligand-binding domain and results in a constitutively active receptor (McGuire et al., 2001).”
BackgroundKarchner, S. I., Jenny, M. J., Tarrant, A. M., Evans, B. R., Kang, H. J., Bae, I., Sherr, D. H., & Hahn, M. E. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.00206-09 · Cited by 40 · see citing works
“In the AHR, this intervening region is important for dimerization with ARNT (10, 45).”
BackgroundNovel 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 · see citing works
Self-citationAHR Ligands: Promiscuity in Binding and Diversity in Response
DeGroot, D., He, G., Fraccalvieri, D., Bonati, L., Pandini, A., & Denison, M. S. (2011) · The AH Receptor in Biology and Toxicology · doi:10.1002/9781118140574.ch4 · Cited by 43 · see citing works
Corrada, D., Soshilov, A. A., Denison, M. S., & Bonati, L. (2016) · PLOS Computational Biology · doi:10.1371/journal.pcbi.1004981 · Cited by 43 · see citing works
Aryl Hydrocarbon Receptor Deficiency Alters Circadian and Metabolic Rhythmicity
Jaeger, C., Khazaal, A. Q., Xu, C., Sun, M.-W., Krager, S. L., & Tischkau, S. A. (2017) · Journal of Biological Rhythms · doi:10.1177/0748730417696786 · Cited by 36 · see citing works
“The PAS domain, characteristic of both AhR and several circadian clock proteins, acts as an interactive surface for protein-protein interaction and, in the case of AhR, functions as the binding surface for various ligands that can be endogenous, naturally occurring, and/or anthropogenic (Gu et al., 2000; McGuire et al…”
BackgroundHepatic Aryl Hydrocarbon Receptor Attenuates Fibroblast Growth Factor 21 Expression
Girer, N. G., Murray, I. A., Omiecinski, C. J., & Perdew, G. H. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.715151 · Cited by 40 · see citing works
Pollenz, R. (2007) · Biochemical Pharmacology · doi:10.1016/j.bcp.2007.03.021 · Cited by 33
A constitutively active aryl hydrocarbon receptor causes loss of peritoneal B1 cells.
Andersson, P., Ridderstad, A., McGuire, J., Pettersson, S., Poellinger, L., & Hanberg, A. (2003) · Biochemical and Biophysical Research Communications - BBRC · doi:10.1016/s0006-291x(03)00185-2 · Cited by 32 · see citing works
Self-citationBrunnberg, S., Andersson, P., Poellinger, L., & Hanberg, A. (2011) · Chemosphere · doi:10.1016/j.chemosphere.2011.09.015 · Cited by 30 · see citing works
“We have developed transgenic mice expressing a constitutively active dioxin receptor (CA-AhR) (McGuire et al., 2001).”
BackgroundSelf-citationThe LMP1 Promoter Can Be Transactivated Directly by NF-κB
Demetriades, C., & Mosialos, G. (2009) · Journal of Virology · doi:10.1128/jvi.00097-09 · Cited by 27 · see citing works
“A constitutively active form of AhR (CAAhR) (23) or ARNT alone did not affect the 40/ 328 LMP1 promoter region, whereas their combination caused a low (twofold)-level transactivation of the LMP1 promoter (Fig.”
BackgroundBonati, L., Corrada, D., Giani Tagliabue, S., & Motta, S. (2017) · Current Opinion in Toxicology · doi:10.1016/j.cotox.2017.01.011 · Cited by 27 · see citing works
The AhR‐SRC axis as a therapeutic vulnerability in BRAFi‐resistant melanoma
Paris, A., Tardif, N., Baietti, F. M., Berra, C., Leclair, H. M., Leucci, E., Galibert, M., & Corre, S. (2022) · EMBO Molecular Medicine · doi:10.15252/emmm.202215677 · Cited by 26 · see citing works
Kudo, K., Takeuchi, T., Murakami, Y., Ebina, M., & Kikuchi, H. (2009) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2009.06.003 · Cited by 25 · see citing works
Corrada, D., Denison, M. S., & Bonati, L. (2017) · Molecular BioSystems · doi:10.1039/c7mb00005g · Cited by 24 · see citing works
Artyukov, A. A., Zelepuga, E., Богданович, Л. Н., Михайловна, Л. Н., Novikov, V. L., Rutckova, T. A., & Kozlovskaya, E. P. (2020) · Journal of Clinical Medicine · doi:10.3390/jcm9051494 · Cited by 29 · see citing works
“Moreover, PAS B region was indicated by the detailed mutagenesis and deletion experiments to be responsible for ligand binding (LBD) to the cytosolic AhR [56,57].”
BackgroundKohle, C., Hassepass, I., Bock-hennig, B. S., Bock, K. W., Poellinger, L., & McGuire, J. (2002) · Archives of Biochemistry and Biophysics · doi:10.1016/s0003-9861(02)00076-0 · Cited by 24 · see citing works
Self-citationKuznetsov, N., Andersson, P., Gradin, K., von Stein, P., Dieckmann, A., Pettersson, S., Hanberg, A., & Poellinger, L. (2005) · Oncogene · doi:10.1038/sj.onc.1208529 · Cited by 23 · see citing works
“We have developed in a gain-of-function model transgenic mice expressing a constitutively active dioxin receptor, CA-AhR (McGuire et al., 2001).”
BackgroundSelf-citationSantiago-Josefat, B., & Fernández-Salguero, P. (2003) · Journal of Molecular Biology · doi:10.1016/j.jmb.2003.08.020 · Cited by 23 · see citing works
Molecular analysis of NPAS3 functional domains and variants
Luoma, L. M., & Berry, F. B. (2018) · BMC Molecular Biology · doi:10.1186/s12867-018-0117-4 · Cited by 19 · see citing works
Takacova, M., Holotnakova, T., Vondráček, J., Machala, M., Pěnčíková, K., Gradin, K., Poellinger, L., Pastorek, J., Pastoreková, S., & Kopáček, J. (2009) · Biochemical Journal · doi:10.1042/bj20080952 · Cited by 18 · see citing works
Self-citationA Dominant Negative Zebrafish Ahr2 Partially Protects Developing Zebrafish from Dioxin Toxicity
Lanham, K. A., Prasch, A. L., Weina, K. M., Peterson, R. E., & Heideman, W. (2011) · PLoS ONE · doi:10.1371/journal.pone.0028020 · Cited by 13 · see citing works
“For example, manipulation of the PAS-B domain can produce a constitutively active AHR [22].”
BackgroundFunatake, C. J., Ao, K., Suzuki, T., Murai, H., Yamamoto, M., Fujii-Kuriyama, Y., Kerkvliet, N., & Nohara, K. (2009) · Journal of Immunotoxicology · doi:10.1080/15476910903124454 · Cited by 17 · see citing works
“The minimal deletion causes the AhR to localize in the nucleus, heterodimerize with ARNT, and activate transcription by binding DRE sequences in a ligand-independent manner (McGuire et al., 2001).”
BackgroundRodent 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 · see citing works
“Early evidence from domain mapping studies demonstrated that Ahr mutants lacking the PAS B domain constitutively dimerize with ARNT, bind to AHREs, and induce transcription of AHREdriven genes in a manner that is independent of ligand binding (McGuire et al. 2001; Andersson et al. 2002).”
BackgroundKimura, E., Kubo, K.-I., Endo, T., Ling, W.-T., Nakajima, K., Kakeyama, M., & Tohyama, C. (2017) · PLoS ONE · doi:10.1371/journal.pone.0183497 · Cited by 16 · see citing works
Sakata, Y., Yoshioka, W., Tohyama, C., & Ohsako, S. (2007) · Biochemical and Biophysical Research Communications - BBRC · doi:10.1016/j.bbrc.2007.02.010 · Cited by 16
Aryl hydrocarbon receptor affects circadian-regulated lipolysis through an E-Box-dependent mechanism
Khazaal, A. Q., Haque, N., Krager, C. R., Krager, S. L., Chambers, C., Wilber, A. C., & Tischkau, S. A. (2022) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2022.111809 · Cited by 14 · see citing works
Kodama, S., Okada, K., Akimoto, K., Inui, H., & Ohkawa, H. (2009) · Plant Biotechnology Journal · doi:10.1111/j.1467-7652.2008.00378.x · Cited by 14 · see citing works
Nagai, H., Kubo, M., Abe, R., Yamamoto, M., & Nohara, K. (2006) · International Immunopharmacology · doi:10.1016/j.intimp.2005.08.015 · Cited by 14 · see citing works
Yao, G., Harstad, E. B., & Bradfield, C. A. (2003) · Springer eBooks · doi:10.1007/978-1-4615-0515-0_7 · Cited by 4 · see citing works
Annalora, A. J., Marcus, C. B., & Iversen, P. L. (2020) · Drug Metabolism and Disposition · doi:10.1124/dmd.119.089102 · Cited by 13 · see citing works
History of Research on the AHR
Gasiewicz, T. A., & Henry, E. C. (2011) · Wiley eBooks · doi:10.1002/9781118140574.ch1 · Cited by 14 · see citing works
“Since that time, an extensive literature has developed in this area, complemented by the development of mice expressing a constitutively active [385, 386] or hypomorphic AHR [387], or with AHR that can be conditionally expressed [388].”
BackgroundAnnalora, A. J., Jozic, M., Marcus, C. B., & Iversen, P. L. (2018) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2018.12.009 · Cited by 15 · see citing works
Khazaal, A. Q., Jaeger, C., Bottum, K., & Tischkau, S. A. (2018) · Journal of Receptor Ligand and Channel Research · doi:10.2147/jrlcr.s133886 · Cited by 10 · see citing works
Tkachenko, A., Bermúdez, M., Irmer-Stooff, S., Genkinger, D., Henkler, F., Wolber, G., & Luch, A. (2017) · Archives of Toxicology · doi:10.1007/s00204-017-2129-0 · Cited by 9 · see citing works
Nohara, K., Suzuki, T., Ao, K., Murai, H., Miyamoto, Y., Inouye, K., Pan, X.-Q., Motohashi, H., Fujii-Kuriyama, Y., Yamamoto, M., et al. (2009) · International Immunology · doi:10.1093/intimm/dxp045 · Cited by 10 · see citing works
Kimura, E. (2025) · Toxics · doi:10.3390/toxics13070596 · Cited by 8 · see citing works
“AHR that lacks the ligand-binding domain and the PAS-B motif functions as CA-AHR (Figure 2A), allowing the induction of transcriptional activity even in the absence of a ligand [169].”
Kewley, R., & Whitelaw, M. (2005) · Biochemical and Biophysical Research Communications - BBRC · doi:10.1016/j.bbrc.2005.08.073 · Cited by 8
Self-citationWang, H.-C., Liu, K.-Y., Wang, L.-T., Hsu, S.-H., Wang, S.-C., & Huang, S.-K. (2021) · Human Cell · doi:10.1007/s13577-021-00491-6 · Cited by 6 · see citing works
Dantsuka, A., Ichii, O., Hanberg, A., Elewa, Y. H., Otsuka-Kanazawa, S., Nakamura, T., & Kon, Y. (2019) · BMC Gastroenterology · doi:10.1186/s12876-019-1009-x · Cited by 6 · see citing works
The Aryl Hydrocarbon Receptor Regulates Mouse Fshr Promoter Activity Through an E-Box Binding Site1
Teino, I., Kuuse, S., Ingerpuu, S., Maimets, T., & Tiido, T. (2012) · Biology of Reproduction · doi:10.1095/biolreprod.111.095596 · Cited by 5 · see citing works
“The expression plasmid for the CA-AHR, consisting of the mutant AHR lacking the minimal PAS B motif, was generated by PCR cloning as described previously [17].”
MethodSanada, N., Gotoh-Kinoshita, Y., Yamashita, N., & Kizu, R. (2020) · Toxicological Research · doi:10.1093/toxres/tfaa027 · Cited by 4 · see citing works
“Constitutively active AhR (CA-AhR), a mutant AhR with a genetic defect in the minimal ligand-binding domain, is located in the nucleus and exerts transcriptional activity even in the absence of AhR agonists [35].”
BackgroundDrosophila AHR limits tumor growth and stem cell proliferation in the intestine
Tsai, M.-S., Sun, J., Alexandre, C., Shapiro, M., Franchet, A., Li, Y., Gould, A. P., Vincent, J., Stockinger, B., & Diny, N. (2023) · bioRxiv · doi:10.12688/wellcomeopenres.23515.3 · Cited by 3 · see citing works
“Ligand binding leads to release of AHR from its chaperone complex and nuclear translocation 2 .”
A Key For Hypoxia Genetic Adaptation In Alpaca Could Be A HIF1A Truncated bHLH Protein Domain
Moraga, M., C, F. A. M., & Figueroa, F. (2018) · bioRxiv · doi:10.1101/386987 · Cited by 3
“Further studies have corroborated these conclusions (Semenza et al. 1997; McGuire et al. 2001; Huang et al. 2012).”
The Aryl Hydrocarbon Receptor: A Modulator of Skeletal Muscle Health and Aging
Wimberly, K., & Ryan, T. (2025) · Biochimie · doi:10.1016/j.biochi.2025.12.012 · Cited by 2 · see citing works
Farka, R., & Polakoviová, M. (2013) · doi:10.1201/b14899-10 · Cited by 2
Andersson, P., Brunnberg, S., Wejheden, C., Poellinger, L., & Hanberg, A. (2011) · doi:10.1002/9781118140574.ch26
Self-citationPrediction of the Sensitivity of Avian Species to the Embryotoxic Effects of Dioxin-like Compounds
Reza, M., & Farahani, F. (2013) · doi:10.20381/ruor-6414
“The development of mice lacking the AHR (Lahvis and Bradfield, 1998), constitutively active AHR (McGuire et al., 2001), and conditionally expressed AHR (Walisser et al., 2005) increased our understanding of its physiological functions.”
Background
- Authors
- McGuire, J., Okamoto, K., Whitelaw, M. L., Tanaka, H., & Poellinger, L.
- Affiliations
- Karolinska Institutet (SE)
- The University of Adelaide (AU)
- Institute of Medical Science, The University of Tokyo (JP)
- Corresponding author
- Poellinger, Lorenz
- ORCID
- Whitelaw, Murray L.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2001-11
- Volume
- 276
- Issue
- 45
- Pages
- 41841-41849
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1986806772
- Cited by
- 102
- References
- 42
- Citations by year
- 2025: 5 · 2023: 1 · 2022: 2 · 2021: 4 · 2020: 4 · 2019: 3 · 2018: 3 · 2017: 6 · 2016: 4 · 2015: 4 · 2014: 3 · 2013: 4 · 2012: 1
- FWCI
- 3.90
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Adelaide Research & Scholarship (AR&S) (University of Adelaide) (submittedVersion)
- Funders
- Novartis Foundation
- European Commission
- Cancerfonden
- NOVARTIS Foundation (Japan) for the Promotion of Science
- Topics
- Physical Sciences › Environmental Science › Health, Toxicology and Mutagenesis › Toxic Organic Pollutants Impact
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Peroxisome Proliferator-Activated Receptors
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Estrogen and related hormone effects
- Keywords
- aryl hydrocarbon receptor, constitutive transcriptional activation, ligand-binding domain, HSP90, nuclear translocation, DNA binding, 2,3,7,8-tetrachlorodibenzo-p-dioxin, receptor mutants
- MeSH terms
- Animals, Binding Sites, DNA-Binding Proteins, Cricetinae, Ligands, Mutation, Transcription Factors, Trans-Activators, CHO Cells, Receptors, Aryl Hydrocarbon, Dimerization, Response Elements, Aryl Hydrocarbon Receptor Nuclear Translocator
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