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Volumn 72, Issue 3, 2007, Pages 231-246

CAR and PXR: The xenobiotic-sensing receptors

Author keywords

Constitutive androstane receptor; Estrogen receptor; Glucocorticoid receptor; Physiology; Pregnane X receptor; Structure function relationship

Indexed keywords

CELL NUCLEUS RECEPTOR; CHEMICAL AGENT; CONSTITUTIVE ANDROSTANE RECEPTOR; ESTROGEN RECEPTOR; GLUCOCORTICOID RECEPTOR; PREGNANE X RECEPTOR; STEROID HORMONE; STEROID RECEPTOR; XENOBIOTIC AGENT;

EID: 33847024555     PISSN: 0039128X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.steroids.2006.12.006     Document Type: Review
Times cited : (371)

References (121)
  • 1
    • 33646713469 scopus 로고    scopus 로고
    • Phenobarbital confers its diverse effects by activating the orphan nuclear receptor CAR
    • Kodama S., and Negishi M. Phenobarbital confers its diverse effects by activating the orphan nuclear receptor CAR. Drug Metab Rev 38 (2006) 75-87
    • (2006) Drug Metab Rev , vol.38 , pp. 75-87
    • Kodama, S.1    Negishi, M.2
  • 2
    • 0035038008 scopus 로고    scopus 로고
    • Phenobarbital response elements of cytochrome P450 genes and nuclear receptors
    • Sueyoshi T., and Negishi M. Phenobarbital response elements of cytochrome P450 genes and nuclear receptors. Annu Rev Pharmacol Toxicol 41 (2001) 123-143
    • (2001) Annu Rev Pharmacol Toxicol , vol.41 , pp. 123-143
    • Sueyoshi, T.1    Negishi, M.2
  • 3
    • 13544258619 scopus 로고    scopus 로고
    • Novel CAR-mediated mechanism for synergistic activation of two distinct elements within the human cytochrome P450 2B6 gene in HepG2 cells
    • Swales K., Kakizaki S., Yamamoto Y., Inoue K., Kobayashi K., and Negishi M. Novel CAR-mediated mechanism for synergistic activation of two distinct elements within the human cytochrome P450 2B6 gene in HepG2 cells. J Biol Chem 280 (2005) 3458-3466
    • (2005) J Biol Chem , vol.280 , pp. 3458-3466
    • Swales, K.1    Kakizaki, S.2    Yamamoto, Y.3    Inoue, K.4    Kobayashi, K.5    Negishi, M.6
  • 4
    • 14244270349 scopus 로고    scopus 로고
    • Role of the constitutive androstane receptor in xenobiotic-induced thyroid hormone metabolism
    • Qatanani M., Zhang J., and Moore D.D. Role of the constitutive androstane receptor in xenobiotic-induced thyroid hormone metabolism. Endocrinology 146 (2005) 995-1002
    • (2005) Endocrinology , vol.146 , pp. 995-1002
    • Qatanani, M.1    Zhang, J.2    Moore, D.D.3
  • 5
    • 2442485772 scopus 로고    scopus 로고
    • The nuclear receptor CAR is a regulator of thyroid hormone metabolism during caloric restriction
    • Maglich J.M., Watson J., McMillen P.J., Goodwin B., Willson T.M., and Moore J.T. The nuclear receptor CAR is a regulator of thyroid hormone metabolism during caloric restriction. J Biol Chem 279 (2004) 19832-19838
    • (2004) J Biol Chem , vol.279 , pp. 19832-19838
    • Maglich, J.M.1    Watson, J.2    McMillen, P.J.3    Goodwin, B.4    Willson, T.M.5    Moore, J.T.6
  • 6
    • 0035042684 scopus 로고    scopus 로고
    • CYP3A regulation: from pharmacology to nuclear receptors
    • Quattrochi L.C., and Guzelian P.S. CYP3A regulation: from pharmacology to nuclear receptors. Drug Metab Dispos 29 (2001) 615-622
    • (2001) Drug Metab Dispos , vol.29 , pp. 615-622
    • Quattrochi, L.C.1    Guzelian, P.S.2
  • 7
    • 33744962967 scopus 로고    scopus 로고
    • Functional inhibitory cross-talk between constitutive androstane receptor and hepatic nuclear factor-4 in hepatic lipid/glucose metabolism is mediated by competition for binding to the DR1 motif and to the common coactivators, GRIP-1 and PGC-1α
    • Miao J., Fang S., Bae Y., and Kemper J.K. Functional inhibitory cross-talk between constitutive androstane receptor and hepatic nuclear factor-4 in hepatic lipid/glucose metabolism is mediated by competition for binding to the DR1 motif and to the common coactivators, GRIP-1 and PGC-1α. J Biol Chem 281 (2006) 14537-14546
    • (2006) J Biol Chem , vol.281 , pp. 14537-14546
    • Miao, J.1    Fang, S.2    Bae, Y.3    Kemper, J.K.4
  • 8
    • 4444246000 scopus 로고    scopus 로고
    • Nuclear receptors CAR and PXR cross talk with FOXO1 to regulate genes that encode drug-metabolizing and gluconeogenic enzymes
    • Kodama S., Koike C., Negishi M., and Yamamoto Y. Nuclear receptors CAR and PXR cross talk with FOXO1 to regulate genes that encode drug-metabolizing and gluconeogenic enzymes. Mol Cell Biol 24 (2004) 7931-7940
    • (2004) Mol Cell Biol , vol.24 , pp. 7931-7940
    • Kodama, S.1    Koike, C.2    Negishi, M.3    Yamamoto, Y.4
  • 9
    • 0021850197 scopus 로고
    • Enzyme inducers improve insulin sensitivity in non-insulin-dependent diabetic subjects
    • Lahtela J.T., Arranto A.J., and Sotaniemi E.A. Enzyme inducers improve insulin sensitivity in non-insulin-dependent diabetic subjects. Diabetes 34 (1985) 911-916
    • (1985) Diabetes , vol.34 , pp. 911-916
    • Lahtela, J.T.1    Arranto, A.J.2    Sotaniemi, E.A.3
  • 11
    • 0035853057 scopus 로고    scopus 로고
    • An essential role for nuclear receptors SXR/PXR in detoxification of cholestatic bile acids
    • Xie W., Radominska-Pandya A., Shi Y., Simon C.M., Nelson M.C., Ong E.S., et al. An essential role for nuclear receptors SXR/PXR in detoxification of cholestatic bile acids. Proc Natl Acad Sci USA 98 (2001) 3375-3380
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 3375-3380
    • Xie, W.1    Radominska-Pandya, A.2    Shi, Y.3    Simon, C.M.4    Nelson, M.C.5    Ong, E.S.6
  • 12
    • 0037422578 scopus 로고    scopus 로고
    • Identification of bile acid precursors as endogenous ligands for the nuclear xenobiotic pregnane X receptor
    • Goodwin B., Gauthier K.C., Umetani M., Watson M.A., Lochansky M.I., Collins J.L., et al. Identification of bile acid precursors as endogenous ligands for the nuclear xenobiotic pregnane X receptor. Proc Natl Acad Sci USA 100 (2003) 223-228
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 223-228
    • Goodwin, B.1    Gauthier, K.C.2    Umetani, M.3    Watson, M.A.4    Lochansky, M.I.5    Collins, J.L.6
  • 15
    • 10344224570 scopus 로고    scopus 로고
    • The constitutive androstane receptor and pregnane X receptor function coordinately to prevent bile acid-induced hepatotoxicity
    • Zhang J., Huang W., Qatanani M., Evans R.M., and Moore D.D. The constitutive androstane receptor and pregnane X receptor function coordinately to prevent bile acid-induced hepatotoxicity. J Biol Chem 279 (2004) 49517-49522
    • (2004) J Biol Chem , vol.279 , pp. 49517-49522
    • Zhang, J.1    Huang, W.2    Qatanani, M.3    Evans, R.M.4    Moore, D.D.5
  • 16
    • 0037931737 scopus 로고    scopus 로고
    • Identification of a novel human constitutive androstane receptor (CAR) agonist and its use in the identification of CAR target genes
    • Maglich J.M., Parks D.J., Moore L.B., Collins J.L., Goodwin B., Billin A.N., et al. Identification of a novel human constitutive androstane receptor (CAR) agonist and its use in the identification of CAR target genes. J Biol Chem 278 (2003) 17277-17283
    • (2003) J Biol Chem , vol.278 , pp. 17277-17283
    • Maglich, J.M.1    Parks, D.J.2    Moore, L.B.3    Collins, J.L.4    Goodwin, B.5    Billin, A.N.6
  • 17
    • 0033999734 scopus 로고    scopus 로고
    • The xenobiotic compound 1,4-bis[2-(3,5-dichloropyridyloxy)]benzene is an agonist ligand for the nuclear receptor CAR
    • Tzameli I., Pissios P., Schuetz E.G., and Moore D.D. The xenobiotic compound 1,4-bis[2-(3,5-dichloropyridyloxy)]benzene is an agonist ligand for the nuclear receptor CAR. Mol Cell Biol 20 (2000) 2951-2958
    • (2000) Mol Cell Biol , vol.20 , pp. 2951-2958
    • Tzameli, I.1    Pissios, P.2    Schuetz, E.G.3    Moore, D.D.4
  • 19
    • 0036171965 scopus 로고    scopus 로고
    • Regulation of CYP3A gene transcription by the pregnane X receptor
    • Goodwin B., Redinbo M.R., and Kliewer S.A. Regulation of CYP3A gene transcription by the pregnane X receptor. Annu Rev Pharmacol Toxicol 42 (2002) 1-23
    • (2002) Annu Rev Pharmacol Toxicol , vol.42 , pp. 1-23
    • Goodwin, B.1    Redinbo, M.R.2    Kliewer, S.A.3
  • 20
    • 0036799870 scopus 로고    scopus 로고
    • The nuclear pregnane X receptor: a key regulator of xenobiotic metabolism
    • Kliewer S.A., Goodwin B., and Willson T.M. The nuclear pregnane X receptor: a key regulator of xenobiotic metabolism. Endocr Rev 23 (2002) 687-702
    • (2002) Endocr Rev , vol.23 , pp. 687-702
    • Kliewer, S.A.1    Goodwin, B.2    Willson, T.M.3
  • 21
    • 28844498056 scopus 로고    scopus 로고
    • Localization of the nuclear receptor CAR at the cell membrane of mouse liver
    • Koike C., Moore R., and Negishi M. Localization of the nuclear receptor CAR at the cell membrane of mouse liver. FEBS Lett 579 (2005) 6733-6736
    • (2005) FEBS Lett , vol.579 , pp. 6733-6736
    • Koike, C.1    Moore, R.2    Negishi, M.3
  • 22
    • 22444448890 scopus 로고    scopus 로고
    • Characterization of activating signal cointegrator-2 as a novel transcriptional coactivator of the xenobiotic nuclear receptor constitutive androstane receptor
    • Choi E., Lee S., Yeom S.Y., Kim G.H., Lee J.W., and Kim S.W. Characterization of activating signal cointegrator-2 as a novel transcriptional coactivator of the xenobiotic nuclear receptor constitutive androstane receptor. Mol Endocrinol 19 (2005) 1711-1719
    • (2005) Mol Endocrinol , vol.19 , pp. 1711-1719
    • Choi, E.1    Lee, S.2    Yeom, S.Y.3    Kim, G.H.4    Lee, J.W.5    Kim, S.W.6
  • 23
    • 0032230234 scopus 로고    scopus 로고
    • Molecular cloning of xSRC-3, a novel transcription coactivator from Xenopus, that is related to AIB1, p/CIP, and TIF2
    • Kim H.J., Lee S.K., Na S.Y., Choi H.S., and Lee J.W. Molecular cloning of xSRC-3, a novel transcription coactivator from Xenopus, that is related to AIB1, p/CIP, and TIF2. Mol Endocrinol 12 (1998) 1038-1047
    • (1998) Mol Endocrinol , vol.12 , pp. 1038-1047
    • Kim, H.J.1    Lee, S.K.2    Na, S.Y.3    Choi, H.S.4    Lee, J.W.5
  • 24
    • 0037135532 scopus 로고    scopus 로고
    • Glucocorticoid receptor-interacting protein 1 mediates ligand-independent nuclear translocation and activation of constitutive androstane receptor in vivo
    • Min G., Kemper J.K., and Kemper B. Glucocorticoid receptor-interacting protein 1 mediates ligand-independent nuclear translocation and activation of constitutive androstane receptor in vivo. J Biol Chem 277 (2002) 26356-26363
    • (2002) J Biol Chem , vol.277 , pp. 26356-26363
    • Min, G.1    Kemper, J.K.2    Kemper, B.3
  • 25
    • 0035310906 scopus 로고    scopus 로고
    • Xenobiotic induction of cytochrome P450 2B1 (CYP2B1) is mediated by the orphan nuclear receptor constitutive androstane receptor (CAR) and requires steroid co-activator 1 (SRC-1) and the transcription factor Sp1
    • Muangmoonchai R., Smirlis D., Wong S.C., Edwards M., Phillips I.R., and Shephard E.A. Xenobiotic induction of cytochrome P450 2B1 (CYP2B1) is mediated by the orphan nuclear receptor constitutive androstane receptor (CAR) and requires steroid co-activator 1 (SRC-1) and the transcription factor Sp1. Biochem J 355 (2001) 71-78
    • (2001) Biochem J , vol.355 , pp. 71-78
    • Muangmoonchai, R.1    Smirlis, D.2    Wong, S.C.3    Edwards, M.4    Phillips, I.R.5    Shephard, E.A.6
  • 26
    • 0038514189 scopus 로고    scopus 로고
    • Activation of orphan nuclear constitutive androstane receptor requires subnuclear targeting by peroxisome proliferator-activated receptor γ coactivator-1αṡ A possible link between xenobiotic response and nutritional state
    • Shiraki T., Sakai N., Kanaya E., and Jingami H. Activation of orphan nuclear constitutive androstane receptor requires subnuclear targeting by peroxisome proliferator-activated receptor γ coactivator-1αṡ A possible link between xenobiotic response and nutritional state. J Biol Chem 278 (2003) 11344-11350
    • (2003) J Biol Chem , vol.278 , pp. 11344-11350
    • Shiraki, T.1    Sakai, N.2    Kanaya, E.3    Jingami, H.4
  • 27
    • 33747169939 scopus 로고    scopus 로고
    • Cohesin protein SMC1 represses the nuclear receptor CAR-mediated synergistic activation of a human P450 gene by xenobiotics
    • Inoue K., Borchers C.H., and Negishi M. Cohesin protein SMC1 represses the nuclear receptor CAR-mediated synergistic activation of a human P450 gene by xenobiotics. Biochem J 398 (2006) 125-133
    • (2006) Biochem J , vol.398 , pp. 125-133
    • Inoue, K.1    Borchers, C.H.2    Negishi, M.3
  • 28
    • 0032766430 scopus 로고    scopus 로고
    • Phenobarbital-responsive nuclear translocation of the receptor CAR in induction of the CYP2B gene
    • Kawamoto T., Sueyoshi T., Zelko I., Moore R., Washburn K., and Negishi M. Phenobarbital-responsive nuclear translocation of the receptor CAR in induction of the CYP2B gene. Mol Cell Biol 19 (1999) 6318-6322
    • (1999) Mol Cell Biol , vol.19 , pp. 6318-6322
    • Kawamoto, T.1    Sueyoshi, T.2    Zelko, I.3    Moore, R.4    Washburn, K.5    Negishi, M.6
  • 29
    • 0030744682 scopus 로고    scopus 로고
    • An okadaic acid-sensitive pathway involved in the phenobarbital-mediated induction of CYP2B gene expression in primary rat hepatocyte cultures
    • Sidhu J.S., and Omiecinski C.J. An okadaic acid-sensitive pathway involved in the phenobarbital-mediated induction of CYP2B gene expression in primary rat hepatocyte cultures. J Pharmacol Exp Ther 282 (1997) 1122-1129
    • (1997) J Pharmacol Exp Ther , vol.282 , pp. 1122-1129
    • Sidhu, J.S.1    Omiecinski, C.J.2
  • 30
    • 0032032380 scopus 로고    scopus 로고
    • Protein serine/threonine phosphatase inhibitors suppress phenobarbital-induced Cyp2b10 gene transcription in mouse primary hepatocytes
    • Honkakoski P., and Negishi M. Protein serine/threonine phosphatase inhibitors suppress phenobarbital-induced Cyp2b10 gene transcription in mouse primary hepatocytes. Biochem J 330 (1998) 889-895
    • (1998) Biochem J , vol.330 , pp. 889-895
    • Honkakoski, P.1    Negishi, M.2
  • 31
    • 0035076197 scopus 로고    scopus 로고
    • The peptide near the C terminus regulates receptor CAR nuclear translocation induced by xenochemicals in mouse liver
    • Zelko I., Sueyoshi T., Kawamoto T., Moore R., and Negishi M. The peptide near the C terminus regulates receptor CAR nuclear translocation induced by xenochemicals in mouse liver. Mol Cell Biol 21 (2001) 2838-2846
    • (2001) Mol Cell Biol , vol.21 , pp. 2838-2846
    • Zelko, I.1    Sueyoshi, T.2    Kawamoto, T.3    Moore, R.4    Negishi, M.5
  • 32
    • 0142210183 scopus 로고    scopus 로고
    • Cytoplasmic accumulation of the nuclear receptor CAR by a tetratricopeptide repeat protein in HepG2 cells
    • Kobayashi K., Sueyoshi T., Inoue K., Moore R., and Negishi M. Cytoplasmic accumulation of the nuclear receptor CAR by a tetratricopeptide repeat protein in HepG2 cells. Mol Pharmacol 64 (2003) 1069-1075
    • (2003) Mol Pharmacol , vol.64 , pp. 1069-1075
    • Kobayashi, K.1    Sueyoshi, T.2    Inoue, K.3    Moore, R.4    Negishi, M.5
  • 33
    • 0042236405 scopus 로고    scopus 로고
    • Identification of the nuclear receptor CAR:HSP90 complex in mouse liver and recruitment of protein phosphatase 2A in response to phenobarbital
    • Yoshinari K., Kobayashi K., Moore R., Kawamoto T., and Negishi M. Identification of the nuclear receptor CAR:HSP90 complex in mouse liver and recruitment of protein phosphatase 2A in response to phenobarbital. FEBS Lett 548 (2003) 17-20
    • (2003) FEBS Lett , vol.548 , pp. 17-20
    • Yoshinari, K.1    Kobayashi, K.2    Moore, R.3    Kawamoto, T.4    Negishi, M.5
  • 34
    • 33645109954 scopus 로고    scopus 로고
    • Serine 202 regulates the nuclear translocation of constitutive active/androstane receptor
    • Hosseinpour F., Moore R., Negishi M., and Sueyoshi T. Serine 202 regulates the nuclear translocation of constitutive active/androstane receptor. Mol Pharmacol 69 (2006) 1095-1102
    • (2006) Mol Pharmacol , vol.69 , pp. 1095-1102
    • Hosseinpour, F.1    Moore, R.2    Negishi, M.3    Sueyoshi, T.4
  • 35
    • 14844299331 scopus 로고    scopus 로고
    • Structural determinants of constitutive androstane receptor required for its glucocorticoid receptor interacting protein-1-mediated nuclear accumulation
    • Xia J., and Kemper B. Structural determinants of constitutive androstane receptor required for its glucocorticoid receptor interacting protein-1-mediated nuclear accumulation. J Biol Chem 280 (2005) 7285-7293
    • (2005) J Biol Chem , vol.280 , pp. 7285-7293
    • Xia, J.1    Kemper, B.2
  • 36
    • 24644488771 scopus 로고    scopus 로고
    • Transcription coactivator peroxisome proliferator-activated receptor-binding protein/mediator 1 deficiency abrogates acetaminophen hepatotoxicity
    • Jia Y., Guo G.L., Surapureddi S., Sarkar J., Qi C., Guo D., et al. Transcription coactivator peroxisome proliferator-activated receptor-binding protein/mediator 1 deficiency abrogates acetaminophen hepatotoxicity. Proc Natl Acad Sci USA 102 (2005) 12531-12536
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 12531-12536
    • Jia, Y.1    Guo, G.L.2    Surapureddi, S.3    Sarkar, J.4    Qi, C.5    Guo, D.6
  • 37
    • 8344219885 scopus 로고    scopus 로고
    • Cytoplasmic localization of pregnane X receptor and ligand-dependent nuclear translocation in mouse liver
    • Squires E.J., Sueyoshi T., and Negishi M. Cytoplasmic localization of pregnane X receptor and ligand-dependent nuclear translocation in mouse liver. J Biol Chem 279 (2004) 49307-49314
    • (2004) J Biol Chem , vol.279 , pp. 49307-49314
    • Squires, E.J.1    Sueyoshi, T.2    Negishi, M.3
  • 38
    • 28144459680 scopus 로고    scopus 로고
    • The nuclear xenobiotic receptor pregnane X receptor: recent insights and new challenges
    • Orans J., Teotico D.G., and Redinbo M.R. The nuclear xenobiotic receptor pregnane X receptor: recent insights and new challenges. Mol Endocrinol 19 (2005) 2891-2900
    • (2005) Mol Endocrinol , vol.19 , pp. 2891-2900
    • Orans, J.1    Teotico, D.G.2    Redinbo, M.R.3
  • 39
    • 13244291443 scopus 로고    scopus 로고
    • Induction of drug metabolism by forskolin: the role of the pregnane X receptor and the protein kinase A signal transduction pathway
    • Ding X., and Staudinger J.L. Induction of drug metabolism by forskolin: the role of the pregnane X receptor and the protein kinase A signal transduction pathway. J Pharmacol Exp Ther 312 (2005) 849-856
    • (2005) J Pharmacol Exp Ther , vol.312 , pp. 849-856
    • Ding, X.1    Staudinger, J.L.2
  • 40
    • 13844253850 scopus 로고    scopus 로고
    • Repression of PXR-mediated induction of hepatic CYP3A gene expression by protein kinase C
    • Ding X., and Staudinger J.L. Repression of PXR-mediated induction of hepatic CYP3A gene expression by protein kinase C. Biochem Pharmacol 69 (2005) 867-873
    • (2005) Biochem Pharmacol , vol.69 , pp. 867-873
    • Ding, X.1    Staudinger, J.L.2
  • 41
    • 0033652116 scopus 로고    scopus 로고
    • Estrogen activation of the nuclear orphan receptor CAR (constitutive active receptor) in induction of the mouse Cyp2b10 gene
    • Kawamoto T., Kakizaki S., Yoshinari K., and Negishi M. Estrogen activation of the nuclear orphan receptor CAR (constitutive active receptor) in induction of the mouse Cyp2b10 gene. Mol Endocrinol 14 (2000) 1897-1905
    • (2000) Mol Endocrinol , vol.14 , pp. 1897-1905
    • Kawamoto, T.1    Kakizaki, S.2    Yoshinari, K.3    Negishi, M.4
  • 42
    • 0036259008 scopus 로고    scopus 로고
    • Residue threonine 350 confers steroid hormone responsiveness to the mouse nuclear orphan receptor CAR
    • Ueda A., Kakizaki S., Negishi M., and Sueyoshi T. Residue threonine 350 confers steroid hormone responsiveness to the mouse nuclear orphan receptor CAR. Mol Pharmacol 61 (2002) 1284-1288
    • (2002) Mol Pharmacol , vol.61 , pp. 1284-1288
    • Ueda, A.1    Kakizaki, S.2    Negishi, M.3    Sueyoshi, T.4
  • 43
    • 20544458355 scopus 로고    scopus 로고
    • Thr176 regulates the activity of the mouse nuclear receptor CAR and is conserved in the NR1I subfamily members PXR and VDR
    • Ueda A., Matsui K., Yamamoto Y., Pedersen L.C., Sueyoshi T., and Negishi M. Thr176 regulates the activity of the mouse nuclear receptor CAR and is conserved in the NR1I subfamily members PXR and VDR. Biochem J 388 (2005) 623-630
    • (2005) Biochem J , vol.388 , pp. 623-630
    • Ueda, A.1    Matsui, K.2    Yamamoto, Y.3    Pedersen, L.C.4    Sueyoshi, T.5    Negishi, M.6
  • 44
    • 0036311095 scopus 로고    scopus 로고
    • A structural model of the constitutive androstane receptor defines novel interactions that mediate ligand-independent activity
    • Dussault I., Lin M., Hollister K., Fan M., Termini J., Sherman M.A., et al. A structural model of the constitutive androstane receptor defines novel interactions that mediate ligand-independent activity. Mol Cell Biol 22 (2002) 5270-5280
    • (2002) Mol Cell Biol , vol.22 , pp. 5270-5280
    • Dussault, I.1    Lin, M.2    Hollister, K.3    Fan, M.4    Termini, J.5    Sherman, M.A.6
  • 45
    • 4043173466 scopus 로고    scopus 로고
    • Agonist-dependent and agonist-independent transactivations of the human constitutive androstane receptor are modulated by specific amino acid pairs
    • Frank C., Molnar F., Matilainen M., Lempiainen H., and Carlberg C. Agonist-dependent and agonist-independent transactivations of the human constitutive androstane receptor are modulated by specific amino acid pairs. J Biol Chem 279 (2004) 33558-33566
    • (2004) J Biol Chem , vol.279 , pp. 33558-33566
    • Frank, C.1    Molnar, F.2    Matilainen, M.3    Lempiainen, H.4    Carlberg, C.5
  • 46
    • 14044269562 scopus 로고    scopus 로고
    • Amino acids important for ligand specificity of the human constitutive androstane receptor
    • Jyrkkarinne J., Windshugel B., Makinen J., Ylisirnio M., Perakyla M., Poso A., et al. Amino acids important for ligand specificity of the human constitutive androstane receptor. J Biol Chem 280 (2005) 5960-5971
    • (2005) J Biol Chem , vol.280 , pp. 5960-5971
    • Jyrkkarinne, J.1    Windshugel, B.2    Makinen, J.3    Ylisirnio, M.4    Perakyla, M.5    Poso, A.6
  • 47
    • 19944372389 scopus 로고    scopus 로고
    • A structural basis for constitutive activity in the human CAR/RXRalpha heterodimer
    • Xu R.X., Lambert M.H., Wisely B.B., Warren E.N., Weinert E.E., Waitt G.M., et al. A structural basis for constitutive activity in the human CAR/RXRalpha heterodimer. Mol Cell 16 (2004) 919-928
    • (2004) Mol Cell , vol.16 , pp. 919-928
    • Xu, R.X.1    Lambert, M.H.2    Wisely, B.B.3    Warren, E.N.4    Weinert, E.E.5    Waitt, G.M.6
  • 49
    • 0032568527 scopus 로고    scopus 로고
    • Crystallographic comparison of the estrogen and progesterone receptor's ligand binding domains
    • Tanenbaum D.M., Wang Y., Williams S.P., and Sigler P.B. Crystallographic comparison of the estrogen and progesterone receptor's ligand binding domains. Proc Natl Acad Sci USA 95 (1998) 5998-6003
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 5998-6003
    • Tanenbaum, D.M.1    Wang, Y.2    Williams, S.P.3    Sigler, P.B.4
  • 50
    • 10944250224 scopus 로고    scopus 로고
    • The nuclear xenobiotic receptor CAR: structural determinants of constitutive activation and heterodimerization
    • Suino K., Peng L., Reynolds R., Li Y., Cha J.Y., Repa J.J., et al. The nuclear xenobiotic receptor CAR: structural determinants of constitutive activation and heterodimerization. Mol Cell 16 (2004) 893-905
    • (2004) Mol Cell , vol.16 , pp. 893-905
    • Suino, K.1    Peng, L.2    Reynolds, R.3    Li, Y.4    Cha, J.Y.5    Repa, J.J.6
  • 51
    • 10944229118 scopus 로고    scopus 로고
    • Structure of the murine constitutive androstane receptor complexed to androstenol: a molecular basis for inverse agonism
    • Shan L., Vincent J., Brunzelle J.S., Dussault I., Lin M., Ianculescu I., et al. Structure of the murine constitutive androstane receptor complexed to androstenol: a molecular basis for inverse agonism. Mol Cell 16 (2004) 907-917
    • (2004) Mol Cell , vol.16 , pp. 907-917
    • Shan, L.1    Vincent, J.2    Brunzelle, J.S.3    Dussault, I.4    Lin, M.5    Ianculescu, I.6
  • 52
    • 0036707613 scopus 로고    scopus 로고
    • Insights from a three-dimensional model into ligand binding to constitutive active receptor
    • Xiao L., Cui X., Madison V., White R.E., and Cheng K.C. Insights from a three-dimensional model into ligand binding to constitutive active receptor. Drug Metab Dispos 30 (2002) 951-956
    • (2002) Drug Metab Dispos , vol.30 , pp. 951-956
    • Xiao, L.1    Cui, X.2    Madison, V.3    White, R.E.4    Cheng, K.C.5
  • 53
    • 33746924066 scopus 로고    scopus 로고
    • Ligand recognition by drug-activated nuclear receptors PXR and CAR: structural, site-directed mutagenesis and molecular modeling studies
    • Poso A., and Honkakoski P. Ligand recognition by drug-activated nuclear receptors PXR and CAR: structural, site-directed mutagenesis and molecular modeling studies. Mini Rev Med Chem 6 (2006) 937-947
    • (2006) Mini Rev Med Chem , vol.6 , pp. 937-947
    • Poso, A.1    Honkakoski, P.2
  • 54
    • 33847043360 scopus 로고    scopus 로고
    • Comparison of homology models and X-ray structures of the nuclear receptor CAR: assessing the structural basis of constitutive activity
    • Windshugel B., Jyrkkarinne J., Vanamo J., Poso A., Honkakoski P., and Sippl W. Comparison of homology models and X-ray structures of the nuclear receptor CAR: assessing the structural basis of constitutive activity. J Mol Graph Model (2006)
    • (2006) J Mol Graph Model
    • Windshugel, B.1    Jyrkkarinne, J.2    Vanamo, J.3    Poso, A.4    Honkakoski, P.5    Sippl, W.6
  • 55
    • 0036240393 scopus 로고    scopus 로고
    • Structural insights into the promiscuity and function of the human pregnane X receptor
    • Watkins R.E., Noble S.M., and Redinbo M.R. Structural insights into the promiscuity and function of the human pregnane X receptor. Curr Opin Drug Discov Dev 5 (2002) 150-158
    • (2002) Curr Opin Drug Discov Dev , vol.5 , pp. 150-158
    • Watkins, R.E.1    Noble, S.M.2    Redinbo, M.R.3
  • 56
    • 0035933511 scopus 로고    scopus 로고
    • The human nuclear xenobiotic receptor PXR: structural determinants of directed promiscuity
    • Watkins R.E., Wisely G.B., Moore L.B., Collins J.L., Lambert M.H., Williams S.P., et al. The human nuclear xenobiotic receptor PXR: structural determinants of directed promiscuity. Science 292 (2001) 2329-2333
    • (2001) Science , vol.292 , pp. 2329-2333
    • Watkins, R.E.1    Wisely, G.B.2    Moore, L.B.3    Collins, J.L.4    Lambert, M.H.5    Williams, S.P.6
  • 57
    • 17844396881 scopus 로고    scopus 로고
    • Structural disorder in the complex of human pregnane X receptor and the macrolide antibiotic rifampicin
    • Chrencik J.E., Orans J., Moore L.B., Xue Y., Peng L., Collins J.L., et al. Structural disorder in the complex of human pregnane X receptor and the macrolide antibiotic rifampicin. Mol Endocrinol 19 (2005) 1125-1134
    • (2005) Mol Endocrinol , vol.19 , pp. 1125-1134
    • Chrencik, J.E.1    Orans, J.2    Moore, L.B.3    Xue, Y.4    Peng, L.5    Collins, J.L.6
  • 58
  • 59
    • 0043168030 scopus 로고    scopus 로고
    • Coactivator binding promotes the specific interaction between ligand and the pregnane X receptor
    • Watkins R.E., Davis-Searles P.R., Lambert M.H., and Redinbo M.R. Coactivator binding promotes the specific interaction between ligand and the pregnane X receptor. J Mol Biol 331 (2003) 815-828
    • (2003) J Mol Biol , vol.331 , pp. 815-828
    • Watkins, R.E.1    Davis-Searles, P.R.2    Lambert, M.H.3    Redinbo, M.R.4
  • 60
    • 17844366538 scopus 로고    scopus 로고
    • The pregnane X receptor regulates gene expression in a ligand- and promoter-selective fashion
    • Masuyama H., Suwaki N., Tateishi Y., Nakatsukasa H., Segawa T., and Hiramatsu Y. The pregnane X receptor regulates gene expression in a ligand- and promoter-selective fashion. Mol Endocrinol 19 (2005) 1170-1180
    • (2005) Mol Endocrinol , vol.19 , pp. 1170-1180
    • Masuyama, H.1    Suwaki, N.2    Tateishi, Y.3    Nakatsukasa, H.4    Segawa, T.5    Hiramatsu, Y.6
  • 61
    • 18144399332 scopus 로고    scopus 로고
    • The human glucocorticoid receptor: one gene, multiple proteins and diverse responses
    • Zhou J., and Cidlowski J.A. The human glucocorticoid receptor: one gene, multiple proteins and diverse responses. Steroids 70 (2005) 407-417
    • (2005) Steroids , vol.70 , pp. 407-417
    • Zhou, J.1    Cidlowski, J.A.2
  • 62
    • 0028886694 scopus 로고
    • Activation of the estrogen receptor through phosphorylation by mitogen-activated protein kinase
    • Kato S., Endoh H., Masuhiro Y., Kitamoto T., Uchiyama S., Sasaki H., et al. Activation of the estrogen receptor through phosphorylation by mitogen-activated protein kinase. Science 270 (1995) 1491-1494
    • (1995) Science , vol.270 , pp. 1491-1494
    • Kato, S.1    Endoh, H.2    Masuhiro, Y.3    Kitamoto, T.4    Uchiyama, S.5    Sasaki, H.6
  • 64
    • 18144424777 scopus 로고    scopus 로고
    • Gene regulation by the glucocorticoid receptor: structure:function relationship
    • Kumar R., and Thompson E.B. Gene regulation by the glucocorticoid receptor: structure:function relationship. J Steroid Biochem Mol Biol 94 (2005) 383-394
    • (2005) J Steroid Biochem Mol Biol , vol.94 , pp. 383-394
    • Kumar, R.1    Thompson, E.B.2
  • 65
    • 0032446607 scopus 로고    scopus 로고
    • The structural basis of estrogen receptor/coactivator recognition and the antagonism of this interaction by tamoxifen
    • Shiau A.K., Barstad D., Loria P.M., Cheng L., Kushner P.J., Agard D.A., et al. The structural basis of estrogen receptor/coactivator recognition and the antagonism of this interaction by tamoxifen. Cell 95 (1998) 927-937
    • (1998) Cell , vol.95 , pp. 927-937
    • Shiau, A.K.1    Barstad, D.2    Loria, P.M.3    Cheng, L.4    Kushner, P.J.5    Agard, D.A.6
  • 66
    • 0036234964 scopus 로고    scopus 로고
    • Structural characterization of a subtype-selective ligand reveals a novel mode of estrogen receptor antagonism
    • Shiau A.K., Barstad D., Radek J.T., Meyers M.J., Nettles K.W., Katzenellenbogen B.S., et al. Structural characterization of a subtype-selective ligand reveals a novel mode of estrogen receptor antagonism. Nat Struct Biol 9 (2002) 359-364
    • (2002) Nat Struct Biol , vol.9 , pp. 359-364
    • Shiau, A.K.1    Barstad, D.2    Radek, J.T.3    Meyers, M.J.4    Nettles, K.W.5    Katzenellenbogen, B.S.6
  • 67
    • 3242876293 scopus 로고    scopus 로고
    • Structure and function of the glucocorticoid receptor ligand binding domain
    • Bledsoe R.K., Stewart E.L., and Pearce K.H. Structure and function of the glucocorticoid receptor ligand binding domain. Vitamin Horm 68 (2004) 49-91
    • (2004) Vitamin Horm , vol.68 , pp. 49-91
    • Bledsoe, R.K.1    Stewart, E.L.2    Pearce, K.H.3
  • 69
    • 33745821260 scopus 로고    scopus 로고
    • The cochaperone p23 differentially regulates estrogen receptor target genes and promotes tumor cell adhesion and invasion
    • Oxelmark E., Roth J.M., Brooks P.C., Braunstein S.E., Schneider R.J., and Garabedian M.J. The cochaperone p23 differentially regulates estrogen receptor target genes and promotes tumor cell adhesion and invasion. Mol Cell Biol 26 (2006) 5205-5213
    • (2006) Mol Cell Biol , vol.26 , pp. 5205-5213
    • Oxelmark, E.1    Roth, J.M.2    Brooks, P.C.3    Braunstein, S.E.4    Schneider, R.J.5    Garabedian, M.J.6
  • 70
    • 29244464699 scopus 로고    scopus 로고
    • Repressive domain of unliganded human estrogen receptor α associates with Hsc70
    • Ogawa S., Oishi H., Mezaki Y., Kouzu-Fujita M., Matsuyama R., Nakagomi M., et al. Repressive domain of unliganded human estrogen receptor α associates with Hsc70. Genes Cells 10 (2005) 1095-1102
    • (2005) Genes Cells , vol.10 , pp. 1095-1102
    • Ogawa, S.1    Oishi, H.2    Mezaki, Y.3    Kouzu-Fujita, M.4    Matsuyama, R.5    Nakagomi, M.6
  • 71
    • 0141592432 scopus 로고    scopus 로고
    • Genetic dissection of p23, an Hsp90 cochaperone, reveals a distinct surface involved in estrogen receptor signaling
    • Oxelmark E., Knoblauch R., Arnal S., Su L.F., Schapira M., and Garabedian M.J. Genetic dissection of p23, an Hsp90 cochaperone, reveals a distinct surface involved in estrogen receptor signaling. J Biol Chem 278 (2003) 36547-36555
    • (2003) J Biol Chem , vol.278 , pp. 36547-36555
    • Oxelmark, E.1    Knoblauch, R.2    Arnal, S.3    Su, L.F.4    Schapira, M.5    Garabedian, M.J.6
  • 72
    • 0033585002 scopus 로고    scopus 로고
    • Caveolin-1 potentiates estrogen receptor α (ERα) signaling. Caveolin-1 drives ligand-independent nuclear translocation and activation of ERα
    • Schlegel A., Wang C., Katzenellenbogen B.S., Pestell R.G., and Lisanti M.P. Caveolin-1 potentiates estrogen receptor α (ERα) signaling. Caveolin-1 drives ligand-independent nuclear translocation and activation of ERα. J Biol Chem 274 (1999) 33551-33556
    • (1999) J Biol Chem , vol.274 , pp. 33551-33556
    • Schlegel, A.1    Wang, C.2    Katzenellenbogen, B.S.3    Pestell, R.G.4    Lisanti, M.P.5
  • 73
    • 0032915424 scopus 로고    scopus 로고
    • Role for Hsp90-associated cochaperone p23 in estrogen receptor signal transduction
    • Knoblauch R., and Garabedian M.J. Role for Hsp90-associated cochaperone p23 in estrogen receptor signal transduction. Mol Cell Biol 19 (1999) 3748-3759
    • (1999) Mol Cell Biol , vol.19 , pp. 3748-3759
    • Knoblauch, R.1    Garabedian, M.J.2
  • 74
    • 0032230245 scopus 로고    scopus 로고
    • Interaction and dissociation by ligands of estrogen receptor and Hsp90: the antiestrogen RU 58668 induces a protein synthesis-dependent clustering of the receptor in the cytoplasm
    • Devin-Leclerc J., Meng X., Delahaye F., Leclerc P., Baulieu E.E., and Catelli M.G. Interaction and dissociation by ligands of estrogen receptor and Hsp90: the antiestrogen RU 58668 induces a protein synthesis-dependent clustering of the receptor in the cytoplasm. Mol Endocrinol 12 (1998) 842-854
    • (1998) Mol Endocrinol , vol.12 , pp. 842-854
    • Devin-Leclerc, J.1    Meng, X.2    Delahaye, F.3    Leclerc, P.4    Baulieu, E.E.5    Catelli, M.G.6
  • 75
    • 0027985633 scopus 로고
    • Heat shock protein 90 strongly stimulates the binding of purified estrogen receptor to its responsive element
    • Inano K., Curtis S.W., Korach K.S., Omata S., and Horigome T. Heat shock protein 90 strongly stimulates the binding of purified estrogen receptor to its responsive element. J Biochem (Tokyo) 116 (1994) 759-766
    • (1994) J Biochem (Tokyo) , vol.116 , pp. 759-766
    • Inano, K.1    Curtis, S.W.2    Korach, K.S.3    Omata, S.4    Horigome, T.5
  • 76
    • 0037643416 scopus 로고    scopus 로고
    • Molecular mechanisms of glucocorticoid action and resistance
    • Schaaf M.J., and Cidlowski J.A. Molecular mechanisms of glucocorticoid action and resistance. J Steroid Biochem Mol Biol 83 (2002) 37-48
    • (2002) J Steroid Biochem Mol Biol , vol.83 , pp. 37-48
    • Schaaf, M.J.1    Cidlowski, J.A.2
  • 77
    • 18144392361 scopus 로고    scopus 로고
    • Requirements for estrogen receptor alpha membrane localization and function
    • Evinger III A.J., and Levin E.R. Requirements for estrogen receptor alpha membrane localization and function. Steroids 70 (2005) 361-363
    • (2005) Steroids , vol.70 , pp. 361-363
    • Evinger III, A.J.1    Levin, E.R.2
  • 78
    • 12344307170 scopus 로고    scopus 로고
    • Identity of an estrogen membrane receptor coupled to a G protein in human breast cancer cells
    • Thomas P., Pang Y., Filardo E.J., and Dong J. Identity of an estrogen membrane receptor coupled to a G protein in human breast cancer cells. Endocrinology 146 (2005) 624-632
    • (2005) Endocrinology , vol.146 , pp. 624-632
    • Thomas, P.1    Pang, Y.2    Filardo, E.J.3    Dong, J.4
  • 79
    • 14844343093 scopus 로고    scopus 로고
    • A transmembrane intracellular estrogen receptor mediates rapid cell signaling
    • Revankar C.M., Cimino D.F., Sklar L.A., Arterburn J.B., and Prossnitz E.R. A transmembrane intracellular estrogen receptor mediates rapid cell signaling. Science 307 (2005) 1625-1630
    • (2005) Science , vol.307 , pp. 1625-1630
    • Revankar, C.M.1    Cimino, D.F.2    Sklar, L.A.3    Arterburn, J.B.4    Prossnitz, E.R.5
  • 80
    • 33747841976 scopus 로고    scopus 로고
    • Nature of functional estrogen receptors at the plasma membrane
    • Pedram A., Razandi M., and Levin E.R. Nature of functional estrogen receptors at the plasma membrane. Mol Endocrinol 20 (2006) 1996-2009
    • (2006) Mol Endocrinol , vol.20 , pp. 1996-2009
    • Pedram, A.1    Razandi, M.2    Levin, E.R.3
  • 81
    • 0042815093 scopus 로고    scopus 로고
    • Cofactor Tpr2 combines two TPR domains and a J domain to regulate the Hsp70/Hsp90 chaperone system
    • Brychzy A., Rein T., Winklhofer K.F., Hartl F.U., Young J.C., and Obermann W.M. Cofactor Tpr2 combines two TPR domains and a J domain to regulate the Hsp70/Hsp90 chaperone system. EMBO J 22 (2003) 3613-3623
    • (2003) EMBO J , vol.22 , pp. 3613-3623
    • Brychzy, A.1    Rein, T.2    Winklhofer, K.F.3    Hartl, F.U.4    Young, J.C.5    Obermann, W.M.6
  • 82
    • 33751552134 scopus 로고    scopus 로고
    • Kinase-specific phosphorylation of the estrogen receptor changes receptor interactions with ligand, DNA, and coregulators associated with alterations in estrogen and tamoxifen activity
    • Likhite V.S., Stossi F., Kim K., Katzenellenbogen B.S., and Katzenellenbogen J.A. Kinase-specific phosphorylation of the estrogen receptor changes receptor interactions with ligand, DNA, and coregulators associated with alterations in estrogen and tamoxifen activity. Mol Endocrinol (2006)
    • (2006) Mol Endocrinol
    • Likhite, V.S.1    Stossi, F.2    Kim, K.3    Katzenellenbogen, B.S.4    Katzenellenbogen, J.A.5
  • 83
    • 33344475383 scopus 로고    scopus 로고
    • Antagonist-induced, activation function-2-independent estrogen receptor α phosphorylation
    • Lipfert L., Fisher J.E., Wei N., Scafonas A., Su Q., Yudkovitz J., et al. Antagonist-induced, activation function-2-independent estrogen receptor α phosphorylation. Mol Endocrinol 20 (2006) 516-533
    • (2006) Mol Endocrinol , vol.20 , pp. 516-533
    • Lipfert, L.1    Fisher, J.E.2    Wei, N.3    Scafonas, A.4    Su, Q.5    Yudkovitz, J.6
  • 84
    • 0036318571 scopus 로고    scopus 로고
    • Regulation of estrogen receptor nuclear export by ligand-induced and p38-mediated receptor phosphorylation
    • Lee H., and Bai W. Regulation of estrogen receptor nuclear export by ligand-induced and p38-mediated receptor phosphorylation. Mol Cell Biol 22 (2002) 5835-5845
    • (2002) Mol Cell Biol , vol.22 , pp. 5835-5845
    • Lee, H.1    Bai, W.2
  • 85
    • 0025775736 scopus 로고
    • Identification of phosphorylated sites in the mouse glucocorticoid receptor
    • Bodwell J.E., Orti E., Coull J.M., Pappin D.J., Smith L.I., and Swift F. Identification of phosphorylated sites in the mouse glucocorticoid receptor. J Biol Chem 266 (1991) 7549-7555
    • (1991) J Biol Chem , vol.266 , pp. 7549-7555
    • Bodwell, J.E.1    Orti, E.2    Coull, J.M.3    Pappin, D.J.4    Smith, L.I.5    Swift, F.6
  • 86
    • 0029093343 scopus 로고
    • Role of acidic and phosphorylated residues in gene activation by the glucocorticoid receptor
    • Almlof T., Wright A.P., and Gustafsson J.A. Role of acidic and phosphorylated residues in gene activation by the glucocorticoid receptor. J Biol Chem 270 (1995) 17535-17540
    • (1995) J Biol Chem , vol.270 , pp. 17535-17540
    • Almlof, T.1    Wright, A.P.2    Gustafsson, J.A.3
  • 87
    • 0033523006 scopus 로고    scopus 로고
    • Inhibition of glucocorticoid receptor nucleocytoplasmic shuttling by okadaic acid requires intact cytoskeleton
    • Galigniana M.D., Housley P.R., DeFranco D.B., and Pratt W.B. Inhibition of glucocorticoid receptor nucleocytoplasmic shuttling by okadaic acid requires intact cytoskeleton. J Biol Chem 274 (1999) 16222-16227
    • (1999) J Biol Chem , vol.274 , pp. 16222-16227
    • Galigniana, M.D.1    Housley, P.R.2    DeFranco, D.B.3    Pratt, W.B.4
  • 88
    • 0037450436 scopus 로고    scopus 로고
    • The expression of CYP2B6, CYP2C9 and CYP3A4 genes: a tangle of networks of nuclear and steroid receptors
    • Pascussi J.M., Gerbal-Chaloin S., Drocourt L., Maurel P., and Vilarem M.J. The expression of CYP2B6, CYP2C9 and CYP3A4 genes: a tangle of networks of nuclear and steroid receptors. Biochim Biophys Acta 1619 (2003) 243-253
    • (2003) Biochim Biophys Acta , vol.1619 , pp. 243-253
    • Pascussi, J.M.1    Gerbal-Chaloin, S.2    Drocourt, L.3    Maurel, P.4    Vilarem, M.J.5
  • 89
    • 0035659943 scopus 로고    scopus 로고
    • Dual effect of dexamethasone on CYP3A4 gene expression in human hepatocytes. Sequential role of glucocorticoid receptor and pregnane X receptor
    • Pascussi J.M., Drocourt L., Gerbal-Chaloin S., Fabre J.M., Maurel P., and Vilarem M.J. Dual effect of dexamethasone on CYP3A4 gene expression in human hepatocytes. Sequential role of glucocorticoid receptor and pregnane X receptor. Eur J Biochem 268 (2001) 6346-6358
    • (2001) Eur J Biochem , vol.268 , pp. 6346-6358
    • Pascussi, J.M.1    Drocourt, L.2    Gerbal-Chaloin, S.3    Fabre, J.M.4    Maurel, P.5    Vilarem, M.J.6
  • 90
    • 0029871817 scopus 로고    scopus 로고
    • Phenobarbital induction of hepatic CYP2B1 and CYP2B2: pretranscriptional and post-transcriptional effects of gender, adult age, and phenobarbital dose
    • Agrawal A.K., and Shapiro B.H. Phenobarbital induction of hepatic CYP2B1 and CYP2B2: pretranscriptional and post-transcriptional effects of gender, adult age, and phenobarbital dose. Mol Pharmacol 49 (1996) 523-531
    • (1996) Mol Pharmacol , vol.49 , pp. 523-531
    • Agrawal, A.K.1    Shapiro, B.H.2
  • 91
    • 0030835437 scopus 로고    scopus 로고
    • Effect of ovariectomy and androgen on phenobarbital induction of hepatic CYP2B1 and CYP2B2 in Sprague-Dawley rats
    • Chang T.K.H., Anderson M.D., Bandiera S.M., and Bellward G.D. Effect of ovariectomy and androgen on phenobarbital induction of hepatic CYP2B1 and CYP2B2 in Sprague-Dawley rats. Drug Metab Dispos 25 (1997) 994-1000
    • (1997) Drug Metab Dispos , vol.25 , pp. 994-1000
    • Chang, T.K.H.1    Anderson, M.D.2    Bandiera, S.M.3    Bellward, G.D.4
  • 92
    • 0035132641 scopus 로고    scopus 로고
    • Nuclear receptor CAR as a regulatory factor for the sexually dimorphic induction of CYB2B1 gene by phenobarbital in rat livers
    • Yoshinari K., Sueyoshi T., Moore R., and Negishi M. Nuclear receptor CAR as a regulatory factor for the sexually dimorphic induction of CYB2B1 gene by phenobarbital in rat livers. Mol Pharmacol 59 (2001) 278-284
    • (2001) Mol Pharmacol , vol.59 , pp. 278-284
    • Yoshinari, K.1    Sueyoshi, T.2    Moore, R.3    Negishi, M.4
  • 93
    • 0037072887 scopus 로고    scopus 로고
    • Inhibitory cross-talk between estrogen receptor (ER) and constitutively activated androstane receptor (CAR). CAR inhibits ER-mediated signaling pathway by squelching p160 coactivators
    • Min G., Kim H., Bae Y., Petz L., and Kemper J.K. Inhibitory cross-talk between estrogen receptor (ER) and constitutively activated androstane receptor (CAR). CAR inhibits ER-mediated signaling pathway by squelching p160 coactivators. J Biol Chem 277 (2002) 34626-34633
    • (2002) J Biol Chem , vol.277 , pp. 34626-34633
    • Min, G.1    Kim, H.2    Bae, Y.3    Petz, L.4    Kemper, J.K.5
  • 94
    • 0033061636 scopus 로고    scopus 로고
    • Phenobarbital induction of CYP2B1/2 in primary hepatocytes: endocrine regulation and evidence for a single pathway for multiple inducers
    • Ganem L.G., Trottier E., Anderson A., and Jefcoate C.R. Phenobarbital induction of CYP2B1/2 in primary hepatocytes: endocrine regulation and evidence for a single pathway for multiple inducers. Toxicol Appl Pharmacol 155 (1999) 32-42
    • (1999) Toxicol Appl Pharmacol , vol.155 , pp. 32-42
    • Ganem, L.G.1    Trottier, E.2    Anderson, A.3    Jefcoate, C.R.4
  • 95
    • 0033039910 scopus 로고    scopus 로고
    • Mimicry in primary rat hepatocyte cultures of the in vivo perivenous induction by phenobarbital of cytochrome P-450 2B1 mRNA: role of epidermal growth factor and perivenous oxygen tension
    • Kietzmann T., Hirsch-Ernst K.I., Kahl G.F., and Jungermann K. Mimicry in primary rat hepatocyte cultures of the in vivo perivenous induction by phenobarbital of cytochrome P-450 2B1 mRNA: role of epidermal growth factor and perivenous oxygen tension. Mol Pharmacol 56 (1999) 46-53
    • (1999) Mol Pharmacol , vol.56 , pp. 46-53
    • Kietzmann, T.1    Hirsch-Ernst, K.I.2    Kahl, G.F.3    Jungermann, K.4
  • 96
    • 1642454578 scopus 로고    scopus 로고
    • Transcriptional regulation of CYP2B1 induction in primary rat hepatocyte cultures: repression by epidermal growth factor is mediated via a distal enhancer region
    • Bauer D., Wolfram N., Kahl G.F., and Hirsch-Ernst K.I. Transcriptional regulation of CYP2B1 induction in primary rat hepatocyte cultures: repression by epidermal growth factor is mediated via a distal enhancer region. Mol Pharmacol 65 (2004) 172-180
    • (2004) Mol Pharmacol , vol.65 , pp. 172-180
    • Bauer, D.1    Wolfram, N.2    Kahl, G.F.3    Hirsch-Ernst, K.I.4
  • 97
    • 4644240254 scopus 로고    scopus 로고
    • Interleukin 1beta inhibits CAR-induced expression of hepatic genes involved in drug and bilirubin clearance
    • Assenat E., Gerbal-Chaloin S., Larrey D., Saric J., Fabre J.M., Maurel P., et al. Interleukin 1beta inhibits CAR-induced expression of hepatic genes involved in drug and bilirubin clearance. Hepatology 40 (2004) 951-960
    • (2004) Hepatology , vol.40 , pp. 951-960
    • Assenat, E.1    Gerbal-Chaloin, S.2    Larrey, D.3    Saric, J.4    Fabre, J.M.5    Maurel, P.6
  • 98
    • 31144440344 scopus 로고    scopus 로고
    • Repression of cytochrome P450 activity in human hepatocytes in vitro by a novel hepatotrophic factor, augmenter of liver regeneration
    • Thasler W.E., Dayoub R., Muhlbauer M., Hellerbrand C., Singer T., Grabe A., et al. Repression of cytochrome P450 activity in human hepatocytes in vitro by a novel hepatotrophic factor, augmenter of liver regeneration. J Pharmacol Exp Ther 316 (2006) 822-829
    • (2006) J Pharmacol Exp Ther , vol.316 , pp. 822-829
    • Thasler, W.E.1    Dayoub, R.2    Muhlbauer, M.3    Hellerbrand, C.4    Singer, T.5    Grabe, A.6
  • 99
    • 0034637122 scopus 로고    scopus 로고
    • Interleukin-6 negatively regulates the expression of pregnane X receptor and constitutively activated receptor in primary human hepatocytes
    • Pascussi J.M., Gerbal-Chaloin S., Pichard-Garcia L., Daujat M., Fabre J.M., Maurel P., et al. Interleukin-6 negatively regulates the expression of pregnane X receptor and constitutively activated receptor in primary human hepatocytes. Biochem Biophys Res Commun 274 (2000) 707-713
    • (2000) Biochem Biophys Res Commun , vol.274 , pp. 707-713
    • Pascussi, J.M.1    Gerbal-Chaloin, S.2    Pichard-Garcia, L.3    Daujat, M.4    Fabre, J.M.5    Maurel, P.6
  • 100
    • 30944463481 scopus 로고    scopus 로고
    • Gadd45β is induced through a CAR-dependent, TNF-independent pathway in murine liver hyperplasia
    • Columbano A., Ledda-Columbano G.M., Pibiri M., Cossu C., Menegazzi M., Moore D.D., et al. Gadd45β is induced through a CAR-dependent, TNF-independent pathway in murine liver hyperplasia. Hepatology 42 (2005) 1118-1126
    • (2005) Hepatology , vol.42 , pp. 1118-1126
    • Columbano, A.1    Ledda-Columbano, G.M.2    Pibiri, M.3    Cossu, C.4    Menegazzi, M.5    Moore, D.D.6
  • 101
    • 0036144190 scopus 로고    scopus 로고
    • Ligands have various potential effects on the degradation of pregnane X receptor by proteasome
    • Masuyama H., Inoshita H., Hiramatsu Y., and Kudo T. Ligands have various potential effects on the degradation of pregnane X receptor by proteasome. Endocrinology 143 (2002) 55-61
    • (2002) Endocrinology , vol.143 , pp. 55-61
    • Masuyama, H.1    Inoshita, H.2    Hiramatsu, Y.3    Kudo, T.4
  • 102
    • 0033636597 scopus 로고    scopus 로고
    • Activation of estrogen receptor α by S118 phosphorylation involves a ligand-dependent interaction with TFIIH and participation of CDK7
    • Chen D., Riedl T., Washbrook E., Pace P.E., Coombes R.C., Egly J.M., et al. Activation of estrogen receptor α by S118 phosphorylation involves a ligand-dependent interaction with TFIIH and participation of CDK7. Mol Cell 6 (2000) 127-137
    • (2000) Mol Cell , vol.6 , pp. 127-137
    • Chen, D.1    Riedl, T.2    Washbrook, E.3    Pace, P.E.4    Coombes, R.C.5    Egly, J.M.6
  • 103
    • 0037051987 scopus 로고    scopus 로고
    • MAP kinase mediates growth factor-induced nuclear translocation of estrogen receptor α
    • Lu Q., Ebling H., Mittler J., Baur W.E., and Karas R.H. MAP kinase mediates growth factor-induced nuclear translocation of estrogen receptor α. FEBS Lett 516 (2002) 1-8
    • (2002) FEBS Lett , vol.516 , pp. 1-8
    • Lu, Q.1    Ebling, H.2    Mittler, J.3    Baur, W.E.4    Karas, R.H.5
  • 104
    • 0036794281 scopus 로고    scopus 로고
    • Nuclear export of glucocorticoid receptor is enhanced by c-Jun N-terminal kinase-mediated phosphorylation
    • Itoh M., Adachi M., Yasui H., Takekawa M., Tanaka H., and Imai K. Nuclear export of glucocorticoid receptor is enhanced by c-Jun N-terminal kinase-mediated phosphorylation. Mol Endocrinol 16 (2002) 2382-2392
    • (2002) Mol Endocrinol , vol.16 , pp. 2382-2392
    • Itoh, M.1    Adachi, M.2    Yasui, H.3    Takekawa, M.4    Tanaka, H.5    Imai, K.6
  • 105
    • 0026406078 scopus 로고
    • Protein phosphatase types 1 and/or 2A regulate nucleocytoplasmic shuttling of glucocorticoid receptors
    • DeFranco D.B., Qi M., Borror K.C., Garabedian M.J., and Brautigan D.L. Protein phosphatase types 1 and/or 2A regulate nucleocytoplasmic shuttling of glucocorticoid receptors. Mol Endocrinol 5 (1991) 1215-1228
    • (1991) Mol Endocrinol , vol.5 , pp. 1215-1228
    • DeFranco, D.B.1    Qi, M.2    Borror, K.C.3    Garabedian, M.J.4    Brautigan, D.L.5
  • 106
    • 28144439277 scopus 로고    scopus 로고
    • CHIP (carboxyl terminus of Hsc70-interacting protein) promotes basal and geldanamycin-induced degradation of estrogen receptor-alpha
    • Fan M., Park A., and Nephew K.P. CHIP (carboxyl terminus of Hsc70-interacting protein) promotes basal and geldanamycin-induced degradation of estrogen receptor-alpha. Mol Endocrinol 19 (2005) 2901-2914
    • (2005) Mol Endocrinol , vol.19 , pp. 2901-2914
    • Fan, M.1    Park, A.2    Nephew, K.P.3
  • 107
    • 0037351881 scopus 로고    scopus 로고
    • Cyclic, proteasome-mediated turnover of unliganded and liganded ERα on responsive promoters is an integral feature of estrogen signaling
    • Reid G., Hubner M.R., Metivier R., Brand H., Denger S., Manu D., et al. Cyclic, proteasome-mediated turnover of unliganded and liganded ERα on responsive promoters is an integral feature of estrogen signaling. Mol Cell 11 (2003) 695-707
    • (2003) Mol Cell , vol.11 , pp. 695-707
    • Reid, G.1    Hubner, M.R.2    Metivier, R.3    Brand, H.4    Denger, S.5    Manu, D.6
  • 108
    • 19944428232 scopus 로고    scopus 로고
    • Ligand-dependent switching of ubiquitin-proteasome pathways for estrogen receptor
    • Tateishi Y., Kawabe Y., Chiba T., Murata S., Ichikawa K., Murayama A., et al. Ligand-dependent switching of ubiquitin-proteasome pathways for estrogen receptor. EMBO J 23 (2004) 4813-4823
    • (2004) EMBO J , vol.23 , pp. 4813-4823
    • Tateishi, Y.1    Kawabe, Y.2    Chiba, T.3    Murata, S.4    Ichikawa, K.5    Murayama, A.6
  • 109
    • 33750338745 scopus 로고    scopus 로고
    • Turning off estrogen receptor β-mediated transcription requires estrogen-dependent receptor proteolysis
    • Tateishi Y., Sonoo R., Sekiya Y.I., Sunahara N., Kawano M., Wayama M., et al. Turning off estrogen receptor β-mediated transcription requires estrogen-dependent receptor proteolysis. Mol Cell Biol (2006)
    • (2006) Mol Cell Biol
    • Tateishi, Y.1    Sonoo, R.2    Sekiya, Y.I.3    Sunahara, N.4    Kawano, M.5    Wayama, M.6
  • 110
    • 0035146685 scopus 로고    scopus 로고
    • The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins
    • Connell P., Ballinger C.A., Jiang J., Wu Y., Thompson L.J., Hohfeld J., et al. The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins. Nat Cell Biol 3 (2001) 93-96
    • (2001) Nat Cell Biol , vol.3 , pp. 93-96
    • Connell, P.1    Ballinger, C.A.2    Jiang, J.3    Wu, Y.4    Thompson, L.J.5    Hohfeld, J.6
  • 111
    • 0035900780 scopus 로고    scopus 로고
    • Proteasome-mediated glucocorticoid receptor degradation restricts transcriptional signaling by glucocorticoids
    • Wallace A.D., and Cidlowski J.A. Proteasome-mediated glucocorticoid receptor degradation restricts transcriptional signaling by glucocorticoids. J Biol Chem 276 (2001) 42714-42721
    • (2001) J Biol Chem , vol.276 , pp. 42714-42721
    • Wallace, A.D.1    Cidlowski, J.A.2
  • 112
    • 0028786089 scopus 로고
    • Distinct functions of the 90 kDa heat-shock protein (hsp90) in oestrogen and mineralocorticosteroid receptor activity: effects of hsp90 deletion mutants
    • Binart N., Lombes M., and Baulieu E.E. Distinct functions of the 90 kDa heat-shock protein (hsp90) in oestrogen and mineralocorticosteroid receptor activity: effects of hsp90 deletion mutants. Biochem J 311 (1995) 797-804
    • (1995) Biochem J , vol.311 , pp. 797-804
    • Binart, N.1    Lombes, M.2    Baulieu, E.E.3
  • 113
    • 2442537231 scopus 로고    scopus 로고
    • Role of hsp90 and the hsp90-binding immunophilins in signalling protein movement
    • Pratt W.B., Galigniana M.D., Harrell J.M., and DeFranco D.B. Role of hsp90 and the hsp90-binding immunophilins in signalling protein movement. Cell Signal 16 (2004) 857-872
    • (2004) Cell Signal , vol.16 , pp. 857-872
    • Pratt, W.B.1    Galigniana, M.D.2    Harrell, J.M.3    DeFranco, D.B.4
  • 114
    • 0037085381 scopus 로고    scopus 로고
    • A new first step in activation of steroid receptors: hormone-induced switching of FKBP51 and FKBP52 immunophilins
    • Davies T.H., Ning Y.M., and Sanchez E.R. A new first step in activation of steroid receptors: hormone-induced switching of FKBP51 and FKBP52 immunophilins. J Biol Chem 277 (2002) 4597-4600
    • (2002) J Biol Chem , vol.277 , pp. 4597-4600
    • Davies, T.H.1    Ning, Y.M.2    Sanchez, E.R.3
  • 115
    • 22344454972 scopus 로고    scopus 로고
    • G protein beta interacts with the glucocorticoid receptor and suppresses its transcriptional activity in the nucleus
    • Kino T., Tiulpakov A., Ichijo T., Chheng L., Kozasa T., and Chrousos G.P. G protein beta interacts with the glucocorticoid receptor and suppresses its transcriptional activity in the nucleus. J Cell Biol 169 (2005) 885-896
    • (2005) J Cell Biol , vol.169 , pp. 885-896
    • Kino, T.1    Tiulpakov, A.2    Ichijo, T.3    Chheng, L.4    Kozasa, T.5    Chrousos, G.P.6
  • 116
    • 2342447986 scopus 로고    scopus 로고
    • Importin 7 and importin α/importin β are nuclear import receptors for the glucocorticoid receptor
    • Freedman N.D., and Yamamoto K.R. Importin 7 and importin α/importin β are nuclear import receptors for the glucocorticoid receptor. Mol Biol Cell 15 (2004) 2276-2286
    • (2004) Mol Biol Cell , vol.15 , pp. 2276-2286
    • Freedman, N.D.1    Yamamoto, K.R.2
  • 118
    • 0141844466 scopus 로고    scopus 로고
    • Nuclear export of the glucocorticoid receptor is accelerated by cell fusion-dependent release of calreticulin
    • Walther R.F., Lamprecht C., Ridsdale A., Groulx I., Lee S., Lefebvre Y.A., et al. Nuclear export of the glucocorticoid receptor is accelerated by cell fusion-dependent release of calreticulin. J Biol Chem 278 (2003) 37858-37864
    • (2003) J Biol Chem , vol.278 , pp. 37858-37864
    • Walther, R.F.1    Lamprecht, C.2    Ridsdale, A.3    Groulx, I.4    Lee, S.5    Lefebvre, Y.A.6
  • 119
    • 0038152840 scopus 로고    scopus 로고
    • Protein 14-3-3σ interacts with and favors cytoplasmic subcellular localization of the glucocorticoid receptor, acting as a negative regulator of the glucocorticoid signaling pathway
    • Kino T., Souvatzoglou E., De Martino M.U., Tsopanomihalu M., Wan Y., and Chrousos G.P. Protein 14-3-3σ interacts with and favors cytoplasmic subcellular localization of the glucocorticoid receptor, acting as a negative regulator of the glucocorticoid signaling pathway. J Biol Chem 278 (2003) 25651-25656
    • (2003) J Biol Chem , vol.278 , pp. 25651-25656
    • Kino, T.1    Souvatzoglou, E.2    De Martino, M.U.3    Tsopanomihalu, M.4    Wan, Y.5    Chrousos, G.P.6
  • 120
    • 0033534727 scopus 로고    scopus 로고
    • Ligand-independent activation of the glucocorticoid receptor by β2-adrenergic receptor agonists in primary human lung fibroblasts and vascular smooth muscle cells
    • Eickelberg O., Roth M., Lorx R., Bruce V., Rudiger J., Johnson M., et al. Ligand-independent activation of the glucocorticoid receptor by β2-adrenergic receptor agonists in primary human lung fibroblasts and vascular smooth muscle cells. J Biol Chem 274 (1999) 1005-1010
    • (1999) J Biol Chem , vol.274 , pp. 1005-1010
    • Eickelberg, O.1    Roth, M.2    Lorx, R.3    Bruce, V.4    Rudiger, J.5    Johnson, M.6
  • 121
    • 0029899120 scopus 로고    scopus 로고
    • Evidence using a green fluorescent protein-glucocorticoid receptor chimera that the Ran/TC4 GTPase mediates an essential function independent of nuclear protein import
    • Carey K.L., Richards S.A., Lounsbury K.M., and Macara I.G. Evidence using a green fluorescent protein-glucocorticoid receptor chimera that the Ran/TC4 GTPase mediates an essential function independent of nuclear protein import. J Cell Biol 133 (1996) 985-996
    • (1996) J Cell Biol , vol.133 , pp. 985-996
    • Carey, K.L.1    Richards, S.A.2    Lounsbury, K.M.3    Macara, I.G.4


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