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Volumn 88, Issue 2, 2014, Pages 253-265

Differential suppression of the aryl hydrocarbon receptor nuclear translocator-dependent function by an aryl hydrocarbon receptor PAS-A-derived inhibitory molecule

Author keywords

AhR; AhR deletion constructs; Arnt; DRE binding; HIF 1

Indexed keywords

3 METHYLCHOLANTHRENE; AROMATIC HYDROCARBON RECEPTOR; COBALT CHLORIDE; CYTOCHROME P450 1A1; CYTOCHROME P450 1B1; DIOXIN; FRUCTOSE BISPHOSPHATE ALDOLASE; HETERODIMER; HYPOXIA INDUCIBLE FACTOR 1; HYPOXIA INDUCIBLE FACTOR 1ALPHA; HYPOXIA INDUCIBLE FACTOR 1BETA; LACTATE DEHYDROGENASE; OLIGONUCLEOTIDE; POLYCLONAL ANTIBODY; VASCULOTROPIN;

EID: 84895561591     PISSN: 00062952     EISSN: 18732968     Source Type: Journal    
DOI: 10.1016/j.bcp.2014.01.021     Document Type: Article
Times cited : (11)

References (59)
  • 2
    • 0030854391 scopus 로고    scopus 로고
    • Ah receptor regulation of CYP1B1 expression in primary mouse embryo-derived cells
    • D.L. Alexander, S.E. Eltom, and C.R. Jefcoate Ah receptor regulation of CYP1B1 expression in primary mouse embryo-derived cells Cancer Res 57 1997 4498 4506
    • (1997) Cancer Res , vol.57 , pp. 4498-4506
    • Alexander, D.L.1    Eltom, S.E.2    Jefcoate, C.R.3
  • 3
    • 84883139105 scopus 로고    scopus 로고
    • Role of the aryl hydrocarbon receptor in carcinogenesis and potential as a drug target
    • S. Safe, S.O. Lee, and U.H. Jin Role of the aryl hydrocarbon receptor in carcinogenesis and potential as a drug target Toxicol Sci 135 2013 1 16
    • (2013) Toxicol Sci , vol.135 , pp. 1-16
    • Safe, S.1    Lee, S.O.2    Jin, U.H.3
  • 4
    • 77955903212 scopus 로고    scopus 로고
    • The aryl hydrocarbon receptor interacts with c-Maf to promote the differentiation of type 1 regulatory T cells induced by IL-27
    • L. Apetoh, F.J. Quintana, C. Pot, N. Joller, S. Xiao, and D. Kumar et al. The aryl hydrocarbon receptor interacts with c-Maf to promote the differentiation of type 1 regulatory T cells induced by IL-27 Nat Immunol 11 2010 854 861
    • (2010) Nat Immunol , vol.11 , pp. 854-861
    • Apetoh, L.1    Quintana, F.J.2    Pot, C.3    Joller, N.4    Xiao, S.5    Kumar, D.6
  • 5
    • 42649095378 scopus 로고    scopus 로고
    • Control of T(reg) and T(H)17 cell differentiation by the aryl hydrocarbon receptor
    • F.J. Quintana, A.S. Basso, A.H. Iglesias, T. Korn, M.F. Farez, and E. Bettelli et al. Control of T(reg) and T(H)17 cell differentiation by the aryl hydrocarbon receptor Nature 453 2008 65 71
    • (2008) Nature , vol.453 , pp. 65-71
    • Quintana, F.J.1    Basso, A.S.2    Iglesias, A.H.3    Korn, T.4    Farez, M.F.5    Bettelli, E.6
  • 6
    • 77956519710 scopus 로고    scopus 로고
    • Aryl hydrocarbon receptor antagonists promote the expansion of human hematopoietic stem cells
    • A.E. Boitano, J. Wang, R. Romeo, L.C. Bouchez, A.E. Parker, and S.E. Sutton et al. Aryl hydrocarbon receptor antagonists promote the expansion of human hematopoietic stem cells Science 329 2010 1345 1348
    • (2010) Science , vol.329 , pp. 1345-1348
    • Boitano, A.E.1    Wang, J.2    Romeo, R.3    Bouchez, L.C.4    Parker, A.E.5    Sutton, S.E.6
  • 7
    • 74549144224 scopus 로고    scopus 로고
    • Arylhydrocarbon receptor activation in NCI-H441 cells and C57BL/6 mice: Possible mechanisms for lung dysfunction
    • P.S. Wong, C.F. Vogel, K. Kokosinski, and F. Matsumura Arylhydrocarbon receptor activation in NCI-H441 cells and C57BL/6 mice: possible mechanisms for lung dysfunction Am J Resp Cell Mol Biol 42 2010 210 217
    • (2010) Am J Resp Cell Mol Biol , vol.42 , pp. 210-217
    • Wong, P.S.1    Vogel, C.F.2    Kokosinski, K.3    Matsumura, F.4
  • 8
    • 83355169701 scopus 로고    scopus 로고
    • Genetic ablation of the aryl hydrocarbon receptor causes cigarette smoke-induced mitochondrial dysfunction and apoptosis
    • A. Rico de Souza, M. Zago, S.J. Pollock, P.J. Sime, R.P. Phipps, and C.J. Baglole Genetic ablation of the aryl hydrocarbon receptor causes cigarette smoke-induced mitochondrial dysfunction and apoptosis J Biol Chem 286 2011 43214 43228
    • (2011) J Biol Chem , vol.286 , pp. 43214-43228
    • Rico De Souza, A.1    Zago, M.2    Pollock, S.J.3    Sime, P.J.4    Phipps, R.P.5    Baglole, C.J.6
  • 9
    • 82755192186 scopus 로고    scopus 로고
    • Aryl hydrocarbon receptor deficiency enhances insulin sensitivity and reduces PPAR-alpha pathway activity in mice
    • C. Wang, C.X. Xu, S.L. Krager, K.M. Bottum, D.F. Liao, and S.A. Tischkau Aryl hydrocarbon receptor deficiency enhances insulin sensitivity and reduces PPAR-alpha pathway activity in mice Environ Health Perspect 119 2011 1739 1744
    • (2011) Environ Health Perspect , vol.119 , pp. 1739-1744
    • Wang, C.1    Xu, C.X.2    Krager, S.L.3    Bottum, K.M.4    Liao, D.F.5    Tischkau, S.A.6
  • 10
    • 0025157272 scopus 로고
    • The specific DNA binding activity of the dioxin receptor is modulated by the 90 kd heat shock protein
    • A. Wilhelmsson, S. Cuthill, M. Denis, A.C. Wikstr:om, J.A. Gustafsson, and L. Poellinger The specific DNA binding activity of the dioxin receptor is modulated by the 90 kd heat shock protein Embo J 9 1990 69 76
    • (1990) Embo J , vol.9 , pp. 69-76
    • Wilhelmsson, A.1    Cuthill, S.2    Denis, M.3    Wikstr4    Om, A.C.5    Gustafsson, J.A.6    Poellinger, L.7
  • 11
    • 0030324952 scopus 로고    scopus 로고
    • A pathway of multi-chaperone interactions common to diverse regulatory proteins: Estrogen receptor, Fes tyrosine kinase, heat shock transcription factor Hsf1, and the aryl hydrocarbon receptor
    • S.C. Nair, E.J. Toran, R.A. Rimerman, S. Hjermstad, T.E. Smithgall, and D.F. Smith A pathway of multi-chaperone interactions common to diverse regulatory proteins: estrogen receptor, Fes tyrosine kinase, heat shock transcription factor Hsf1, and the aryl hydrocarbon receptor Cell Stress Chaperones 1 1996 237 250
    • (1996) Cell Stress Chaperones , vol.1 , pp. 237-250
    • Nair, S.C.1    Toran, E.J.2    Rimerman, R.A.3    Hjermstad, S.4    Smithgall, T.E.5    Smith, D.F.6
  • 12
    • 0030897705 scopus 로고    scopus 로고
    • Ligand-dependent interaction of the aryl hydrocarbon receptor with a novel immunophilin homolog in vivo
    • L.A. Carver, and C.A. Bradfield Ligand-dependent interaction of the aryl hydrocarbon receptor with a novel immunophilin homolog in vivo J Biol Chem 272 1997 11452 11456
    • (1997) J Biol Chem , vol.272 , pp. 11452-11456
    • Carver, L.A.1    Bradfield, C.A.2
  • 13
    • 0031002895 scopus 로고    scopus 로고
    • A novel cytoplasmic protein that interacts with the Ah receptor, contains tetratricopeptide repeat motifs, and augments the transcriptional response to 2,3,7,8-tetrachlorodibenzo-p-dioxin
    • Q. Ma, and J.P. Whitlock Jr. A novel cytoplasmic protein that interacts with the Ah receptor, contains tetratricopeptide repeat motifs, and augments the transcriptional response to 2,3,7,8-tetrachlorodibenzo-p-dioxin J Biol Chem 272 1997 8878 8884
    • (1997) J Biol Chem , vol.272 , pp. 8878-8884
    • Ma, Q.1    Whitlock, Jr.J.P.2
  • 14
    • 0037462747 scopus 로고    scopus 로고
    • The hsp90 Co-chaperone XAP2 alters importin beta recognition of the bipartite nuclear localization signal of the Ah receptor and represses transcriptional activity
    • J.R. Petrulis, A. Kusnadi, P. Ramadoss, B. Hollingshead, and G.H. Perdew The hsp90 Co-chaperone XAP2 alters importin beta recognition of the bipartite nuclear localization signal of the Ah receptor and represses transcriptional activity J Biol Chem 278 2003 2677 2685
    • (2003) J Biol Chem , vol.278 , pp. 2677-2685
    • Petrulis, J.R.1    Kusnadi, A.2    Ramadoss, P.3    Hollingshead, B.4    Perdew, G.H.5
  • 15
    • 0035104164 scopus 로고    scopus 로고
    • The hsp90 chaperone complex regulates intracellular localization of the dioxin receptor
    • A. Kazlauskas, S. Sundstrom, L. Poellinger, and I. Pongratz The hsp90 chaperone complex regulates intracellular localization of the dioxin receptor Mol Cell Biol 21 2001 2594 2607
    • (2001) Mol Cell Biol , vol.21 , pp. 2594-2607
    • Kazlauskas, A.1    Sundstrom, S.2    Poellinger, L.3    Pongratz, I.4
  • 16
    • 0033531928 scopus 로고    scopus 로고
    • Evidence that the co-chaperone p23 regulates ligand responsiveness of the dioxin (Aryl hydrocarbon) receptor
    • A. Kazlauskas, L. Poellinger, and I. Pongratz Evidence that the co-chaperone p23 regulates ligand responsiveness of the dioxin (Aryl hydrocarbon) receptor J Biol Chem 274 1999 13519 13524
    • (1999) J Biol Chem , vol.274 , pp. 13519-13524
    • Kazlauskas, A.1    Poellinger, L.2    Pongratz, I.3
  • 17
    • 0036261821 scopus 로고    scopus 로고
    • Recruitment of the NCoA/SRC-1/p160 family of transcriptional coactivators by the aryl hydrocarbon receptor/aryl hydrocarbon receptor nuclear translocator complex
    • T.V. Beischlag, S. Wang, D.W. Rose, J. Torchia, S. Reisz-Porszasz, and K. Muhammad et al. Recruitment of the NCoA/SRC-1/p160 family of transcriptional coactivators by the aryl hydrocarbon receptor/aryl hydrocarbon receptor nuclear translocator complex Mol Cell Biol 22 2002 4319 4333
    • (2002) Mol Cell Biol , vol.22 , pp. 4319-4333
    • Beischlag, T.V.1    Wang, S.2    Rose, D.W.3    Torchia, J.4    Reisz-Porszasz, S.5    Muhammad, K.6
  • 18
    • 11144232325 scopus 로고    scopus 로고
    • Recruitment of thyroid hormone receptor/retinoblastoma-interacting protein 230 by the aryl hydrocarbon receptor nuclear translocator is required for the transcriptional response to both dioxin and hypoxia
    • T.V. Beischlag, R.T. Taylor, D.W. Rose, D. Yoon, Y. Chen, and W.H. Lee et al. Recruitment of thyroid hormone receptor/retinoblastoma-interacting protein 230 by the aryl hydrocarbon receptor nuclear translocator is required for the transcriptional response to both dioxin and hypoxia J Biol Chem 279 2004 54620 54628
    • (2004) J Biol Chem , vol.279 , pp. 54620-54628
    • Beischlag, T.V.1    Taylor, R.T.2    Rose, D.W.3    Yoon, D.4    Chen, Y.5    Lee, W.H.6
  • 19
    • 0030098235 scopus 로고    scopus 로고
    • Xenobiotic metabolism enzyme gene expression in human bronchial epithelial and alveolar macrophage cells
    • J.C. Willey, E. Coy, C. Brolly, M.J. Utell, M.W. Frampton, and J. Hammersley et al. Xenobiotic metabolism enzyme gene expression in human bronchial epithelial and alveolar macrophage cells Am J Resp Cell Mol Biol 14 1996 262 271
    • (1996) Am J Resp Cell Mol Biol , vol.14 , pp. 262-271
    • Willey, J.C.1    Coy, E.2    Brolly, C.3    Utell, M.J.4    Frampton, M.W.5    Hammersley, J.6
  • 20
    • 0032077398 scopus 로고    scopus 로고
    • Characterisation of xenobiotic-metabolising enzyme expression in human bronchial mucosa and peripheral lung tissues
    • K. Mace, E.D. Bowman, P. Vautravers, P.G. Shields, C.C. Harris, and A.M. Pfeifer Characterisation of xenobiotic-metabolising enzyme expression in human bronchial mucosa and peripheral lung tissues Eur J Cancer 34 1998 914 920
    • (1998) Eur J Cancer , vol.34 , pp. 914-920
    • Mace, K.1    Bowman, E.D.2    Vautravers, P.3    Shields, P.G.4    Harris, C.C.5    Pfeifer, A.M.6
  • 21
    • 0029806936 scopus 로고    scopus 로고
    • Preferential formation of benzo[a]pyrene adducts at lung cancer mutational hotspots in P53
    • M.F. Denissenko, A. Pao, M. Tang, and G.P. Pfeifer Preferential formation of benzo[a]pyrene adducts at lung cancer mutational hotspots in P53 Science 274 1996 430 432
    • (1996) Science , vol.274 , pp. 430-432
    • Denissenko, M.F.1    Pao, A.2    Tang, M.3    Pfeifer, G.P.4
  • 22
    • 60349097752 scopus 로고    scopus 로고
    • Differential induction of cytochrome P450 1A1 and 1B1 mRNA in primary cultured bovine hepatocytes treated with TCDD, PBDD/Fs and feed ingredients
    • K.S. Guruge, N. Yamanaka, J. Hasegawa, and S. Miyazaki Differential induction of cytochrome P450 1A1 and 1B1 mRNA in primary cultured bovine hepatocytes treated with TCDD, PBDD/Fs and feed ingredients Toxicol Lett 185 2009 193 196
    • (2009) Toxicol Lett , vol.185 , pp. 193-196
    • Guruge, K.S.1    Yamanaka, N.2    Hasegawa, J.3    Miyazaki, S.4
  • 24
    • 84869849711 scopus 로고    scopus 로고
    • Xenobiotics and loss of cell adhesion drive distinct transcriptional outcomes by aryl hydrocarbon receptor signaling
    • N. Hao, K.L. Lee, S.G. Furness, C. Bosdotter, L. Poellinger, and M.L. Whitelaw Xenobiotics and loss of cell adhesion drive distinct transcriptional outcomes by aryl hydrocarbon receptor signaling Mol Pharmacol 82 2012 1082 1093
    • (2012) Mol Pharmacol , vol.82 , pp. 1082-1093
    • Hao, N.1    Lee, K.L.2    Furness, S.G.3    Bosdotter, C.4    Poellinger, L.5    Whitelaw, M.L.6
  • 25
    • 0031927210 scopus 로고    scopus 로고
    • Differential expression of CYP1A1 and CYP1B1 in human breast epithelial cells and breast tumor cells
    • D.C. Spink, B.C. Spink, J.Q. Cao, J.A. DePasquale, B.T. Pentecost, and M.J. Fasco et al. Differential expression of CYP1A1 and CYP1B1 in human breast epithelial cells and breast tumor cells Carcinogenesis 19 1998 291 298
    • (1998) Carcinogenesis , vol.19 , pp. 291-298
    • Spink, D.C.1    Spink, B.C.2    Cao, J.Q.3    Depasquale, J.A.4    Pentecost, B.T.5    Fasco, M.J.6
  • 26
    • 44649093884 scopus 로고    scopus 로고
    • Preferential induction of cytochrome P450 1A1 over cytochrome P450 1B1 in human breast epithelial cells following exposure to quercetin
    • S.M. Mense, J. Chhabra, and H.K. Bhat Preferential induction of cytochrome P450 1A1 over cytochrome P450 1B1 in human breast epithelial cells following exposure to quercetin J Steroid Biochem Mol Biol 110 2008 157 162
    • (2008) J Steroid Biochem Mol Biol , vol.110 , pp. 157-162
    • Mense, S.M.1    Chhabra, J.2    Bhat, H.K.3
  • 27
    • 84867619803 scopus 로고    scopus 로고
    • Aryl hydrocarbon receptor (AHR)-active pharmaceuticals are selective AHR modulators in MDA-MB-468 and BT474 breast cancer cells
    • U.H. Jin, S.O. Lee, and S. Safe Aryl hydrocarbon receptor (AHR)-active pharmaceuticals are selective AHR modulators in MDA-MB-468 and BT474 breast cancer cells J Pharmacol Exp Ther 343 2012 333 341
    • (2012) J Pharmacol Exp Ther , vol.343 , pp. 333-341
    • Jin, U.H.1    Lee, S.O.2    Safe, S.3
  • 28
    • 79960313393 scopus 로고    scopus 로고
    • Differential ligand-dependent activation and a role for Y322 in aryl hydrocarbon receptor-mediated regulation of gene expression
    • M. Powis, T. Celius, and J. Matthews Differential ligand-dependent activation and a role for Y322 in aryl hydrocarbon receptor-mediated regulation of gene expression Biochem Biophys Res Commun 410 2011 859 865
    • (2011) Biochem Biophys Res Commun , vol.410 , pp. 859-865
    • Powis, M.1    Celius, T.2    Matthews, J.3
  • 29
    • 33846228762 scopus 로고    scopus 로고
    • A truncated Ah receptor blocks the hypoxia and estrogen receptor signaling pathways: A viable approach for breast cancer treatment
    • K.A. Jensen, T.C. Luu, and W.K. Chan A truncated Ah receptor blocks the hypoxia and estrogen receptor signaling pathways: a viable approach for breast cancer treatment Mol Pharm 3 2006 695 703
    • (2006) Mol Pharm , vol.3 , pp. 695-703
    • Jensen, K.A.1    Luu, T.C.2    Chan, W.K.3
  • 30
    • 0027169125 scopus 로고
    • In vitro analysis of Ah receptor domains involved in ligand-activated DNA recognition
    • K.M. Dolwick, H.I. Swanson, and C.A. Bradfield In vitro analysis of Ah receptor domains involved in ligand-activated DNA recognition Proc Natl Acad Sci U S A 90 1993 8566 8570
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 8566-8570
    • Dolwick, K.M.1    Swanson, H.I.2    Bradfield, C.A.3
  • 31
    • 69949184848 scopus 로고    scopus 로고
    • A truncated human Ah receptor suppresses growth of human cervical tumor xenografts by interfering with hypoxia signaling
    • D. Wang, J.S. Faridi, Y. Li, and W.K. Chan A truncated human Ah receptor suppresses growth of human cervical tumor xenografts by interfering with hypoxia signaling FEBS Lett 583 2009 3039 3044
    • (2009) FEBS Lett , vol.583 , pp. 3039-3044
    • Wang, D.1    Faridi, J.S.2    Li, Y.3    Chan, W.K.4
  • 32
    • 23944448563 scopus 로고    scopus 로고
    • A novel Arnt-interacting protein Ainp2 enhances the aryl hydrocarbon receptor signalling
    • Y. Li, T.C. Luu, and W.K. Chan A novel Arnt-interacting protein Ainp2 enhances the aryl hydrocarbon receptor signalling Arch Biochem Biophys 441 2005 84 95
    • (2005) Arch Biochem Biophys , vol.441 , pp. 84-95
    • Li, Y.1    Luu, T.C.2    Chan, W.K.3
  • 33
    • 84876000338 scopus 로고    scopus 로고
    • A cell-penetrating peptide suppresses the hypoxia inducible factor-1 function by binding to the helix-loop-helix domain of the aryl hydrocarbon receptor nuclear translocator
    • Y. Wang, J.D. Thompson, and W.K. Chan A cell-penetrating peptide suppresses the hypoxia inducible factor-1 function by binding to the helix-loop-helix domain of the aryl hydrocarbon receptor nuclear translocator Chem-Biol Interact 203 2013 401 411
    • (2013) Chem-Biol Interact , vol.203 , pp. 401-411
    • Wang, Y.1    Thompson, J.D.2    Chan, W.K.3
  • 34
    • 84862813024 scopus 로고    scopus 로고
    • Suppression of the hypoxia inducible factor-1 function by redistributing the aryl hydrocarbon receptor nuclear translocator from nucleus to cytoplasm
    • Y. Wang, Y. Li, D. Wang, Y. Li, A. Chang, and W.K. Chan Suppression of the hypoxia inducible factor-1 function by redistributing the aryl hydrocarbon receptor nuclear translocator from nucleus to cytoplasm Cancer Lett 320 2012 111 121
    • (2012) Cancer Lett , vol.320 , pp. 111-121
    • Wang, Y.1    Li, Y.2    Wang, D.3    Li, Y.4    Chang, A.5    Chan, W.K.6
  • 35
    • 77956342161 scopus 로고    scopus 로고
    • The aryl hydrocarbon receptor nuclear translocator-interacting protein 2 suppresses the estrogen receptor signaling via an Arnt-dependent mechanism
    • Y. Li, Y. Li, T. Zhang, and W.K. Chan The aryl hydrocarbon receptor nuclear translocator-interacting protein 2 suppresses the estrogen receptor signaling via an Arnt-dependent mechanism Arch Biochem Biophys 502 2010 121 129
    • (2010) Arch Biochem Biophys , vol.502 , pp. 121-129
    • Li, Y.1    Li, Y.2    Zhang, T.3    Chan, W.K.4
  • 36
    • 0037212635 scopus 로고    scopus 로고
    • Synthesis of 32P-labelled protein probes using a modified thioredoxin fusion protein expression system in Escherichia coli
    • A.B. Delucchi, K.A. Jensen, and W.K. Chan Synthesis of 32P-labelled protein probes using a modified thioredoxin fusion protein expression system in Escherichia coli Biomol Eng 20 2003 1 5
    • (2003) Biomol Eng , vol.20 , pp. 1-5
    • Delucchi, A.B.1    Jensen, K.A.2    Chan, W.K.3
  • 37
    • 0027973453 scopus 로고
    • Baculovirus expression of the Ah receptor and Ah receptor nuclear translocator. Evidence for additional dioxin responsive element-binding species and factors required for signaling
    • W.K. Chan, R. Chu, S. Jain, J.K. Reddy, and C.A. Bradfield Baculovirus expression of the Ah receptor and Ah receptor nuclear translocator. Evidence for additional dioxin responsive element-binding species and factors required for signaling J Biol Chem 269 1994 26464 26471
    • (1994) J Biol Chem , vol.269 , pp. 26464-26471
    • Chan, W.K.1    Chu, R.2    Jain, S.3    Reddy, J.K.4    Bradfield, C.A.5
  • 38
    • 0035710746 scopus 로고    scopus 로고
    • Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) Method
    • K.J. Livak, and T.D. Schmittgen Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) Method Methods 25 2001 402 408
    • (2001) Methods , vol.25 , pp. 402-408
    • Livak, K.J.1    Schmittgen, T.D.2
  • 39
    • 84864919456 scopus 로고    scopus 로고
    • P23 co-chaperone protects the aryl hydrocarbon receptor from degradation in mouse and human cell lines
    • P.M. Nguyen, D. Wang, Y. Wang, Y. Li, J.A. Uchizono, and W.K. Chan p23 co-chaperone protects the aryl hydrocarbon receptor from degradation in mouse and human cell lines Biochem Pharmacol 84 2012 838 850
    • (2012) Biochem Pharmacol , vol.84 , pp. 838-850
    • Nguyen, P.M.1    Wang, D.2    Wang, Y.3    Li, Y.4    Uchizono, J.A.5    Chan, W.K.6
  • 40
    • 79956017554 scopus 로고    scopus 로고
    • Identification of residues in the N-terminal PAS domains important for dimerization of Arnt and AhR
    • N. Hao, M.L. Whitelaw, K.E. Shearwin, I.B. Dodd, and A. Chapman-Smith Identification of residues in the N-terminal PAS domains important for dimerization of Arnt and AhR Nucleic Acids Res 2011 1 15
    • (2011) Nucleic Acids Res , pp. 1-15
    • Hao, N.1    Whitelaw, M.L.2    Shearwin, K.E.3    Dodd, I.B.4    Chapman-Smith, A.5
  • 41
    • 84880359790 scopus 로고    scopus 로고
    • A cyclic peptide inhibitor of HIF-1 heterodimerization that inhibits hypoxia signaling in cancer cells
    • E. Miranda, I. Nordgren, A. Male, C. Lawrence, F. Hoakwie, and F. Cuda et al. A cyclic peptide inhibitor of HIF-1 heterodimerization that inhibits hypoxia signaling in cancer cells J Am Chem Soc 135 2013 10418 10425
    • (2013) J Am Chem Soc , vol.135 , pp. 10418-10425
    • Miranda, E.1    Nordgren, I.2    Male, A.3    Lawrence, C.4    Hoakwie, F.5    Cuda, F.6
  • 42
    • 84875779831 scopus 로고    scopus 로고
    • MgcRacGAP, a cytoskeleton regulator, inhibits HIF-1 transcriptional activity by blocking its dimerization
    • A. Lyberopoulou, I. Mylonis, G. Papachristos, D. Sagris, A. Kalousi, and C. Befani et al. MgcRacGAP, a cytoskeleton regulator, inhibits HIF-1 transcriptional activity by blocking its dimerization Biochim Biophys Acta 1833 2013 1378 1387
    • (2013) Biochim Biophys Acta , vol.1833 , pp. 1378-1387
    • Lyberopoulou, A.1    Mylonis, I.2    Papachristos, G.3    Sagris, D.4    Kalousi, A.5    Befani, C.6
  • 43
    • 84874605449 scopus 로고    scopus 로고
    • Development of inhibitors of the PAS-B domain of the HIF-2alpha transcription factor
    • J.L. Rogers, L. Bayeh, T.H. Scheuermann, J. Longgood, J. Key, and J. Naidoo et al. Development of inhibitors of the PAS-B domain of the HIF-2alpha transcription factor J Med Chem 56 2013 1739 1747
    • (2013) J Med Chem , vol.56 , pp. 1739-1747
    • Rogers, J.L.1    Bayeh, L.2    Scheuermann, T.H.3    Longgood, J.4    Key, J.5    Naidoo, J.6
  • 45
    • 84886878172 scopus 로고    scopus 로고
    • Structure and dimerization properties of the aryl hydrocarbon receptor PAS-A domain
    • D. Wu, N. Potluri, Y. Kim, and F. Rastinejad Structure and dimerization properties of the aryl hydrocarbon receptor PAS-A domain Mol Cell Biol 33 2013 4346 4356
    • (2013) Mol Cell Biol , vol.33 , pp. 4346-4356
    • Wu, D.1    Potluri, N.2    Kim, Y.3    Rastinejad, F.4
  • 46
    • 12144255434 scopus 로고    scopus 로고
    • Induced alpha-helix structure in the aryl hydrocarbon receptor transactivation domain modulates protein-protein interactions
    • K. Watt, T.J. Jess, S.M. Kelly, N.C. Price, and I.J. McEwan Induced alpha-helix structure in the aryl hydrocarbon receptor transactivation domain modulates protein-protein interactions Biochemistry 44 2005 734 743
    • (2005) Biochemistry , vol.44 , pp. 734-743
    • Watt, K.1    Jess, T.J.2    Kelly, S.M.3    Price, N.C.4    McEwan, I.J.5
  • 47
    • 0032402989 scopus 로고    scopus 로고
    • Functional analysis of the human cytochrome P4501A1 (CYP1A1) gene enhancer
    • S. Kress, J. Reichert, and M. Schwarz Functional analysis of the human cytochrome P4501A1 (CYP1A1) gene enhancer Eur J Biochem 258 1998 803 812
    • (1998) Eur J Biochem , vol.258 , pp. 803-812
    • Kress, S.1    Reichert, J.2    Schwarz, M.3
  • 48
    • 58049209785 scopus 로고    scopus 로고
    • Roles of coactivator proteins in dioxin induction of CYP1A1 and CYP1B1 in human breast cancer cells
    • R.T. Taylor, F. Wang, E.L. Hsu, and O. Hankinson Roles of coactivator proteins in dioxin induction of CYP1A1 and CYP1B1 in human breast cancer cells Toxicol Sci 107 2009 1 8
    • (2009) Toxicol Sci , vol.107 , pp. 1-8
    • Taylor, R.T.1    Wang, F.2    Hsu, E.L.3    Hankinson, O.4
  • 49
    • 77957879217 scopus 로고    scopus 로고
    • Functional analysis of six human aryl hydrocarbon receptor variants in human breast cancer and mouse hepatoma cell lines
    • T. Celius, and J. Matthews Functional analysis of six human aryl hydrocarbon receptor variants in human breast cancer and mouse hepatoma cell lines Toxicology 277 2010 59 65
    • (2010) Toxicology , vol.277 , pp. 59-65
    • Celius, T.1    Matthews, J.2
  • 50
    • 0038308553 scopus 로고    scopus 로고
    • Critical enhancer region to which AhR/ARNT and Sp1 bind in the human CYP1B1 gene
    • Y. Tsuchiya, M. Nakajima, and T. Yokoi Critical enhancer region to which AhR/ARNT and Sp1 bind in the human CYP1B1 gene J Biochem 133 2003 583 592
    • (2003) J Biochem , vol.133 , pp. 583-592
    • Tsuchiya, Y.1    Nakajima, M.2    Yokoi, T.3
  • 51
    • 0034629105 scopus 로고    scopus 로고
    • Transcriptional regulation of the human CYP1B1 gene. Evidence for involvement of an aryl hydrocarbon receptor response element in constitutive expression
    • S.E. Shehin, R.O. Stephenson, and W.F. Greenlee Transcriptional regulation of the human CYP1B1 gene. Evidence for involvement of an aryl hydrocarbon receptor response element in constitutive expression J Biol Chem 275 2000 6770 6776
    • (2000) J Biol Chem , vol.275 , pp. 6770-6776
    • Shehin, S.E.1    Stephenson, R.O.2    Greenlee, W.F.3
  • 52
    • 84884956374 scopus 로고    scopus 로고
    • Estrogen receptor alpha can selectively repress dioxin receptor-mediated gene expression by targeting DNA methylation
    • M. Marques, L. Laflamme, and L. Gaudreau Estrogen receptor alpha can selectively repress dioxin receptor-mediated gene expression by targeting DNA methylation Nucleic Acids Res 41 2013 8094 8106
    • (2013) Nucleic Acids Res , vol.41 , pp. 8094-8106
    • Marques, M.1    Laflamme, L.2    Gaudreau, L.3
  • 53
    • 0038100188 scopus 로고    scopus 로고
    • Modulation of oestrogen receptor signalling by association with the activated dioxin receptor
    • F. Ohtake, K. Takeyama, T. Matsumoto, H. Kitagawa, Y. Yamamoto, and K. Nohara et al. Modulation of oestrogen receptor signalling by association with the activated dioxin receptor Nature 423 2003 545 550
    • (2003) Nature , vol.423 , pp. 545-550
    • Ohtake, F.1    Takeyama, K.2    Matsumoto, T.3    Kitagawa, H.4    Yamamoto, Y.5    Nohara, K.6
  • 54
    • 77957242787 scopus 로고    scopus 로고
    • Role of epigenetic mechanisms in differential regulation of the dioxin-inducible human CYP1A1 and CYP1B1 genes
    • S.R. Beedanagari, R.T. Taylor, P. Bui, F. Wang, D.W. Nickerson, and O. Hankinson Role of epigenetic mechanisms in differential regulation of the dioxin-inducible human CYP1A1 and CYP1B1 genes Mol Pharmacol 78 2010 608 616
    • (2010) Mol Pharmacol , vol.78 , pp. 608-616
    • Beedanagari, S.R.1    Taylor, R.T.2    Bui, P.3    Wang, F.4    Nickerson, D.W.5    Hankinson, O.6
  • 55
    • 67649419039 scopus 로고    scopus 로고
    • CYP1B1, but not CYP1A1, is downregulated by promoter methylation in colorectal cancers
    • W. Habano, T. Gamo, T. Sugai, K. Otsuka, G. Wakabayashi, and S. Ozawa CYP1B1, but not CYP1A1, is downregulated by promoter methylation in colorectal cancers Int J Oncol 34 2009 1085 1091
    • (2009) Int J Oncol , vol.34 , pp. 1085-1091
    • Habano, W.1    Gamo, T.2    Sugai, T.3    Otsuka, K.4    Wakabayashi, G.5    Ozawa, S.6
  • 57
    • 0035872478 scopus 로고    scopus 로고
    • Differential regulation of cytochrome P450 1A1 and 1B1 by a combination of dioxin and pesticides in the breast tumor cell line MCF-7
    • X. Coumoul, M. Diry, C. Robillot, and R. Barouki Differential regulation of cytochrome P450 1A1 and 1B1 by a combination of dioxin and pesticides in the breast tumor cell line MCF-7 Cancer Res 61 2001 3942 3948
    • (2001) Cancer Res , vol.61 , pp. 3942-3948
    • Coumoul, X.1    Diry, M.2    Robillot, C.3    Barouki, R.4
  • 58
    • 0028865103 scopus 로고
    • DNA binding specificities and pairing rules of the Ah receptor, ARNT, and SIM proteins
    • H.I. Swanson, W.K. Chan, and C.A. Bradfield DNA binding specificities and pairing rules of the Ah receptor, ARNT, and SIM proteins J Biol Chem 270 1995 26292 26302
    • (1995) J Biol Chem , vol.270 , pp. 26292-26302
    • Swanson, H.I.1    Chan, W.K.2    Bradfield, C.A.3
  • 59
    • 0029859749 scopus 로고    scopus 로고
    • Mapping the protein/DNA contact sites of the Ah receptor and Ah receptor nuclear translocator
    • H.I. Swanson, and J. Yang Mapping the protein/DNA contact sites of the Ah receptor and Ah receptor nuclear translocator J Biol Chem 271 1996 31657 31665
    • (1996) J Biol Chem , vol.271 , pp. 31657-31665
    • Swanson, H.I.1    Yang, J.2


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