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Volumn 5, Issue OCT, 2014, Pages

AhR-mediated, non-genomic modulation of IDO1 function

Author keywords

AhR; Dendritic cells; IDO1; Immunoregulation; ITIM; L kynurenine; Tryptophan metabolism; Ubiquitin ligase complex

Indexed keywords

ANDROGEN RECEPTOR; AROMATIC HYDROCARBON RECEPTOR; BETA CATENIN; CYTOTOXIC T LYMPHOCYTE ANTIGEN 4; ESTROGEN RECEPTOR; INDOLEAMINE 2,3 DIOXYGENASE; INDOLEAMINE 2,3 DIOXYGENASE 1; INTERLEUKIN 6; KYNURENINE; STAT3 PROTEIN; SUPPRESSOR OF CYTOKINE SIGNALING 3; TRANSFORMING GROWTH FACTOR BETA; TRYPTOPHAN; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 6; UBIQUITIN PROTEIN LIGASE; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG;

EID: 84918842254     PISSN: None     EISSN: 16643224     Source Type: Journal    
DOI: 10.3389/fimmu.2014.00497     Document Type: Article
Times cited : (41)

References (45)
  • 1
    • 0032555614 scopus 로고    scopus 로고
    • Prevention of allogeneic fetal rejection by tryptophan catabolism
    • Munn DH, Zhou M, Attwood JT, Bondarev I, Conway SJ, Marshall B, et al. Prevention of allogeneic fetal rejection by tryptophan catabolism. Science (1998) 281:1191-3. doi: 10.1126/science.281.5380.1191
    • (1998) Science , vol.281 , pp. 1191-1193
    • Munn, D.H.1    Zhou, M.2    Attwood, J.T.3    Bondarev, I.4    Conway, S.J.5    Marshall, B.6
  • 2
    • 34748835898 scopus 로고    scopus 로고
    • IDO and regulatory T cells: a role for reverse signalling and non-canonical NF-kappaB activation
    • Puccetti P, Grohmann U. IDO and regulatory T cells: a role for reverse signalling and non-canonical NF-kappaB activation. Nat Rev Immunol (2007) 7:817-23. doi:10.1038/nri2163
    • (2007) Nat Rev Immunol , vol.7 , pp. 817-823
    • Puccetti, P.1    Grohmann, U.2
  • 3
    • 58549107152 scopus 로고    scopus 로고
    • SOCS3 drives proteasomal degradation of indoleamine 2,3-dioxygenase (IDO) and antagonizes IDO-dependent tolerogenesis
    • Orabona C, Pallotta MT, Volpi C, Fallarino F, Vacca C, Bianchi R, et al. SOCS3 drives proteasomal degradation of indoleamine 2,3-dioxygenase (IDO) and antagonizes IDO-dependent tolerogenesis. Proc Natl Acad Sci U S A (2008) 105:20828-33. doi:10.1073/pnas.0810278105
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 20828-20833
    • Orabona, C.1    Pallotta, M.T.2    Volpi, C.3    Fallarino, F.4    Vacca, C.5    Bianchi, R.6
  • 4
    • 80052020183 scopus 로고    scopus 로고
    • Indoleamine 2,3-dioxygenase is a signaling protein in long-term tolerance by dendritic cells
    • Pallotta MT, Orabona C, Volpi C, Vacca C, Belladonna ML, Bianchi R, et al. Indoleamine 2,3-dioxygenase is a signaling protein in long-term tolerance by dendritic cells. Nat Immunol (2011) 12:870-8. doi:10.1038/ni.2077
    • (2011) Nat Immunol , vol.12 , pp. 870-878
    • Pallotta, M.T.1    Orabona, C.2    Volpi, C.3    Vacca, C.4    Belladonna, M.L.5    Bianchi, R.6
  • 5
    • 84870476787 scopus 로고    scopus 로고
    • Different partners, opposite outcomes: a new perspective of the immunobiology of indoleamine 2,3-dioxygenase
    • Orabona C, Pallotta MT, Grohmann U. Different partners, opposite outcomes: a new perspective of the immunobiology of indoleamine 2,3-dioxygenase. Mol Med (2012) 18:834-42. doi:10.2119/molmed.2012.00029
    • (2012) Mol Med , vol.18 , pp. 834-842
    • Orabona, C.1    Pallotta, M.T.2    Grohmann, U.3
  • 6
    • 66549106623 scopus 로고    scopus 로고
    • The aryl hydrocarbon receptor: a perspective on potential roles in the immune system
    • Stevens EA, Mezrich JD, Bradfield CA. The aryl hydrocarbon receptor: a perspective on potential roles in the immune system. Immunology (2009) 127:299-311. doi:10.1111/j.1365-2567.2009.03054.x
    • (2009) Immunology , vol.127 , pp. 299-311
    • Stevens, E.A.1    Mezrich, J.D.2    Bradfield, C.A.3
  • 7
    • 0034087885 scopus 로고    scopus 로고
    • Mechanistic aspects - the dioxin (aryl hydrocarbon) receptor
    • Poellinger L. Mechanistic aspects - the dioxin (aryl hydrocarbon) receptor. Food Addit Contam (2000) 17:261-6. doi:10.1080/026520300283333
    • (2000) Food Addit Contam , vol.17 , pp. 261-266
    • Poellinger, L.1
  • 8
    • 0028987872 scopus 로고
    • The aryl hydrocarbon receptor complex
    • Hankinson O. The aryl hydrocarbon receptor complex. Annu Rev Pharmacol Toxicol (1995) 35:307-40. doi:10.1146/annurev.pa.35.040195.001515
    • (1995) Annu Rev Pharmacol Toxicol , vol.35 , pp. 307-340
    • Hankinson, O.1
  • 9
    • 33748741806 scopus 로고    scopus 로고
    • Evidence supporting the hypothesis that one of the main functions of the aryl hydrocarbon receptor is mediation of cell stress responses
    • Matsumura F, Vogel CF. Evidence supporting the hypothesis that one of the main functions of the aryl hydrocarbon receptor is mediation of cell stress responses. Biol Chem (2006) 387:1189-94. doi:10.1515/BC.2006.146
    • (2006) Biol Chem , vol.387 , pp. 1189-1194
    • Matsumura, F.1    Vogel, C.F.2
  • 10
    • 0037450429 scopus 로고    scopus 로고
    • Functional role of AhR in the expression of toxic effects by TCDD
    • Mimura J, Fujii-Kuriyama Y. Functional role of AhR in the expression of toxic effects by TCDD. Biochim Biophys Acta (2003) 1619:263-8. doi:10.1016/S0304-4165(02)00485-3
    • (2003) Biochim Biophys Acta , vol.1619 , pp. 263-268
    • Mimura, J.1    Fujii-Kuriyama, Y.2
  • 11
    • 79551688725 scopus 로고    scopus 로고
    • Kynurenic acid is a potent endogenous aryl hydrocarbon receptor ligand that synergistically induces interleukin-6 in the presence of inflammatory signaling
    • Dinatale BC, Murray IA, Schroeder JC, Flaveny CA, Lahoti TS, Laurenzana EM, et al. Kynurenic acid is a potent endogenous aryl hydrocarbon receptor ligand that synergistically induces interleukin-6 in the presence of inflammatory signaling. Toxicol Sci (2010) 115:89-97. doi:10.1093/toxsci/kfq024
    • (2010) Toxicol Sci , vol.115 , pp. 89-97
    • Dinatale, B.C.1    Murray, I.A.2    Schroeder, J.C.3    Flaveny, C.A.4    Lahoti, T.S.5    Laurenzana, E.M.6
  • 12
    • 78649880396 scopus 로고    scopus 로고
    • An interaction between kynurenine and the aryl hydrocarbon receptor can generate regulatory T cells
    • Mezrich JD, Fechner JH, Zhang X, Johnson BP, Burlingham WJ, Bradfield CA. An interaction between kynurenine and the aryl hydrocarbon receptor can generate regulatory T cells. J Immunol (2010) 185:3190-8. doi:10.4049/jimmunol.0903670
    • (2010) J Immunol , vol.185 , pp. 3190-3198
    • Mezrich, J.D.1    Fechner, J.H.2    Zhang, X.3    Johnson, B.P.4    Burlingham, W.J.5    Bradfield, C.A.6
  • 13
    • 84904216760 scopus 로고    scopus 로고
    • Aryl hydrocarbon receptor control of a disease tolerance defence pathway
    • Bessede A, Gargaro M, Pallotta MT, Matino D, Servillo G, Brunacci C, et al. Aryl hydrocarbon receptor control of a disease tolerance defence pathway. Nature (2014) 511:184-90. doi:10.1038/nature13323
    • (2014) Nature , vol.511 , pp. 184-190
    • Bessede, A.1    Gargaro, M.2    Pallotta, M.T.3    Matino, D.4    Servillo, G.5    Brunacci, C.6
  • 14
    • 34047094888 scopus 로고    scopus 로고
    • Dioxin receptor is a ligand-dependent E3 ubiquitin ligase
    • Ohtake F, Baba A, Takada I, Okada M, Iwasaki K, Miki H, et al. Dioxin receptor is a ligand-dependent E3 ubiquitin ligase. Nature (2007) 446:562-6. doi:10.1038/nature05683
    • (2007) Nature , vol.446 , pp. 562-566
    • Ohtake, F.1    Baba, A.2    Takada, I.3    Okada, M.4    Iwasaki, K.5    Miki, H.6
  • 15
    • 59149093141 scopus 로고    scopus 로고
    • AhR acts as an E3 ubiquitin ligase to modulate steroid receptor functions
    • Ohtake F, Fujii-Kuriyama Y, Kato S. AhR acts as an E3 ubiquitin ligase to modulate steroid receptor functions. Biochem Pharmacol (2009) 77:474-84. doi:10.1016/j.bcp.2008.08.034
    • (2009) Biochem Pharmacol , vol.77 , pp. 474-484
    • Ohtake, F.1    Fujii-Kuriyama, Y.2    Kato, S.3
  • 16
    • 69449101827 scopus 로고    scopus 로고
    • Aryl hydrocarbon receptor suppresses intestinal carcinogenesis in ApcMin/+ mice with natural ligands
    • Kawajiri K, Kobayashi Y, Ohtake F, Ikuta T, Matsushima Y, Mimura J, et al. Aryl hydrocarbon receptor suppresses intestinal carcinogenesis in ApcMin/+ mice with natural ligands. Proc Natl Acad Sci U S A (2009) 106:13481-6. doi:10.1073/pnas.0902132106
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 13481-13486
    • Kawajiri, K.1    Kobayashi, Y.2    Ohtake, F.3    Ikuta, T.4    Matsushima, Y.5    Mimura, J.6
  • 17
    • 0027980319 scopus 로고
    • Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules
    • Rock KL, Gramm C, Rothstein L, Clark K, Stein R, Dick L, et al. Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules. Cell (1994) 78:761-71. doi:10.1016/S0092-8674(94)90462-6
    • (1994) Cell , vol.78 , pp. 761-771
    • Rock, K.L.1    Gramm, C.2    Rothstein, L.3    Clark, K.4    Stein, R.5    Dick, L.6
  • 18
    • 33644511372 scopus 로고    scopus 로고
    • Crystal structure of human indoleamine 2,3-dioxygenase: catalytic mechanism of O2 incorporation by a heme-containing dioxygenase
    • Sugimoto H, Oda S, Otsuki T, Hino T, Yoshida T, Shiro Y. Crystal structure of human indoleamine 2,3-dioxygenase: catalytic mechanism of O2 incorporation by a heme-containing dioxygenase. Proc Natl Acad Sci U S A (2006) 103:2611-6. doi:10.1073/pnas.0508996103
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 2611-2616
    • Sugimoto, H.1    Oda, S.2    Otsuki, T.3    Hino, T.4    Yoshida, T.5    Shiro, Y.6
  • 19
    • 0032500555 scopus 로고    scopus 로고
    • Solvation, reorganization energy, and biological catalysis
    • Cannon WR, Benkovic SJ. Solvation, reorganization energy, and biological catalysis. J Biol Chem (1998) 273:26257-60. doi:10.1074/jbc.273.41.26257
    • (1998) J Biol Chem , vol.273 , pp. 26257-26260
    • Cannon, W.R.1    Benkovic, S.J.2
  • 20
  • 21
    • 36549043024 scopus 로고    scopus 로고
    • Intrinsic dynamics of enzymes in the unbound state and relation to allosteric regulation
    • Bahar I, Chennubhotla C, Tobi D. Intrinsic dynamics of enzymes in the unbound state and relation to allosteric regulation. Curr Opin Struct Biol (2007) 17:633-40. doi:10.1016/j.sbi.2007.09.011
    • (2007) Curr Opin Struct Biol , vol.17 , pp. 633-640
    • Bahar, I.1    Chennubhotla, C.2    Tobi, D.3
  • 22
    • 33947499837 scopus 로고    scopus 로고
    • SOCS3 targets Siglec 7 for proteasomal degradation and blocks Siglec 7-mediated responses
    • Orr SJ, Morgan NM, Buick RJ, Boyd CR, Elliott J, Burrows JF, et al. SOCS3 targets Siglec 7 for proteasomal degradation and blocks Siglec 7-mediated responses. J Biol Chem (2007) 282:3418-22. doi:10.1074/jbc.C600216200
    • (2007) J Biol Chem , vol.282 , pp. 3418-3422
    • Orr, S.J.1    Morgan, N.M.2    Buick, R.J.3    Boyd, C.R.4    Elliott, J.5    Burrows, J.F.6
  • 23
    • 33846864687 scopus 로고    scopus 로고
    • CD33 responses are blocked by SOCS3 through accelerated proteasomal- mediated turnover
    • Orr SJ, Morgan NM, Elliott J, Burrows JF, Scott CJ, McVicar DW, et al. CD33 responses are blocked by SOCS3 through accelerated proteasomal- mediated turnover. Blood (2007) 109:1061-8. doi:10.1182/blood-2006-05-023556
    • (2007) Blood , vol.109 , pp. 1061-1068
    • Orr, S.J.1    Morgan, N.M.2    Elliott, J.3    Burrows, J.F.4    Scott, C.J.5    McVicar, D.W.6
  • 24
    • 21044458270 scopus 로고    scopus 로고
    • Cutting edge: silencing suppressor of cytokine signaling 3 expression in dendritic cells turns CD28-Ig from immune adjuvant to suppressant
    • Orabona C, Belladonna M, Vacca C, Bianchi R, Fallarino F, Volpi C, et al. Cutting edge: silencing suppressor of cytokine signaling 3 expression in dendritic cells turns CD28-Ig from immune adjuvant to suppressant. J Immunol (2005) 174:6582-6. doi:10.4049/jimmunol.174.11.6582
    • (2005) J Immunol , vol.174 , pp. 6582-6586
    • Orabona, C.1    Belladonna, M.2    Vacca, C.3    Bianchi, R.4    Fallarino, F.5    Volpi, C.6
  • 26
    • 84859827337 scopus 로고    scopus 로고
    • Proteasomal degradation of indoleamine 2,3-dioxygenase in CD8 dendritic cells is mediated by suppressor of cytokine signaling 3 (SOCS3)
    • Pallotta MT, Orabona C, Volpi C, Grohmann U, Puccetti P, Fallarino F. Proteasomal degradation of indoleamine 2,3-dioxygenase in CD8 dendritic cells is mediated by suppressor of cytokine signaling 3 (SOCS3). Int J Tryptophan Res (2010) 3:91-7. doi:10.4137/IJTR.S3971
    • (2010) Int J Tryptophan Res , vol.3 , pp. 91-97
    • Pallotta, M.T.1    Orabona, C.2    Volpi, C.3    Grohmann, U.4    Puccetti, P.5    Fallarino, F.6
  • 27
    • 59349114674 scopus 로고    scopus 로고
    • Ah receptor and NF-kappaB interplay on the stage of epigenome
    • Tian Y. Ah receptor and NF-kappaB interplay on the stage of epigenome. Biochem Pharmacol (2009) 77:670-80. doi:10.1016/j.bcp.2008.10.023
    • (2009) Biochem Pharmacol , vol.77 , pp. 670-680
    • Tian, Y.1
  • 28
    • 43049102330 scopus 로고    scopus 로고
    • Intrinsic AhR function underlies cross-talk of dioxins with sex hormone signalings
    • Ohtake F, Baba A, Fujii-Kuriyama Y, Kato S. Intrinsic AhR function underlies cross-talk of dioxins with sex hormone signalings. Biochem Biophys Res Commun (2008) 370:541-6. doi:10.1016/j.bbrc.2008.03.054
    • (2008) Biochem Biophys Res Commun , vol.370 , pp. 541-546
    • Ohtake, F.1    Baba, A.2    Fujii-Kuriyama, Y.3    Kato, S.4
  • 29
    • 84861862669 scopus 로고    scopus 로고
    • SOCS2-induced proteasome-dependent TRAF6 degradation: a common anti-inflammatory pathway for control of innate immune responses
    • Mcberry C, Gonzalez RM, Shryock N, Dias A, Aliberti J. SOCS2-induced proteasome-dependent TRAF6 degradation: a common anti-inflammatory pathway for control of innate immune responses. PLoS One (2012) 7:e38384. doi:10.1371/journal.pone.0038384
    • (2012) PLoS One , vol.7
    • Mcberry, C.1    Gonzalez, R.M.2    Shryock, N.3    Dias, A.4    Aliberti, J.5
  • 30
    • 0038215374 scopus 로고    scopus 로고
    • Tolerance DCs and tryptophan: much ado about IDO
    • Grohmann U, Fallarino F, Puccetti P. Tolerance, DCs and tryptophan: much ado about IDO. Trends Immunol (2003) 24:242-8. doi:10.1016/S1471-4906(03)00072-3
    • (2003) Trends Immunol , vol.24 , pp. 242-248
    • Grohmann, U.1    Fallarino, F.2    Puccetti, P.3
  • 31
    • 78650560167 scopus 로고    scopus 로고
    • Aryl hydrocarbon receptor negatively regulates dendritic cell immunogenicity via a kynurenine-dependent mechanism
    • Nguyen NT, Kimura A, Nakahama T, Chinen I, Masuda K, Nohara K, et al. Aryl hydrocarbon receptor negatively regulates dendritic cell immunogenicity via a kynurenine-dependent mechanism. Proc Natl Acad Sci U S A (2010) 107:19961-6. doi:10.1073/pnas.1014465107
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 19961-19966
    • Nguyen, N.T.1    Kimura, A.2    Nakahama, T.3    Chinen, I.4    Masuda, K.5    Nohara, K.6
  • 32
    • 84874690840 scopus 로고    scopus 로고
    • Possible role of the 'IDO-AhR axis' in maternal-foetal tolerance
    • Hao K, Zhou Q, Chen W, Jia W, Zheng J, Kang J, et al. Possible role of the 'IDO-AhR axis' in maternal-foetal tolerance. Cell Biol Int (2013) 37:105-8. doi:10.1002/cbin.10023
    • (2013) Cell Biol Int , vol.37 , pp. 105-108
    • Hao, K.1    Zhou, Q.2    Chen, W.3    Jia, W.4    Zheng, J.5    Kang, J.6
  • 33
    • 84897374481 scopus 로고    scopus 로고
    • Constitutive IDO expression in human cancer is sustained by an autocrine signaling loop involving IL-6, STAT3 and the AHR
    • Litzenburger UM, Opitz CA, Sahm F, Rauschenbach KJ, Trump S, Winter M, et al. Constitutive IDO expression in human cancer is sustained by an autocrine signaling loop involving IL-6, STAT3 and the AHR. Oncotarget (2014) 5:1038-51.
    • (2014) Oncotarget , vol.5 , pp. 1038-1051
    • Litzenburger, U.M.1    Opitz, C.A.2    Sahm, F.3    Rauschenbach, K.J.4    Trump, S.5    Winter, M.6
  • 34
    • 84885459070 scopus 로고    scopus 로고
    • Aryl hydrocarbon receptor signaling regulates NF-kappaB RelB activation during dendritic-cell differentiation
    • Vogel CF, Wu D, Goth SR, Baek J, Lollies A, Domhardt R, et al. Aryl hydrocarbon receptor signaling regulates NF-kappaB RelB activation during dendritic-cell differentiation. Immunol Cell Biol (2013) 91:568-75. doi:10.1038/icb.2013.43
    • (2013) Immunol Cell Biol , vol.91 , pp. 568-575
    • Vogel, C.F.1    Wu, D.2    Goth, S.R.3    Baek, J.4    Lollies, A.5    Domhardt, R.6
  • 35
    • 45749119506 scopus 로고    scopus 로고
    • Roles of cytosolic phospholipase A2 and Src kinase in the early action of 2,3,7,8-tetrachlorodibenzo-p-dioxin through a nongenomic pathway in MCF10A cells
    • Dong B, Matsumura F. Roles of cytosolic phospholipase A2 and Src kinase in the early action of 2,3,7,8-tetrachlorodibenzo-p-dioxin through a nongenomic pathway in MCF10A cells. Mol Pharmacol (2008) 74:255-63. doi:10.1124/mol.107.044669
    • (2008) Mol Pharmacol , vol.74 , pp. 255-263
    • Dong, B.1    Matsumura, F.2
  • 36
    • 12844265289 scopus 로고    scopus 로고
    • TCDD causes suppression of growth and differentiation of MCF10A, human mammary epithelial cells by interfering with their insulin receptor signaling through c-Src kinase and ERK activation
    • Park S, Mazina O, Kitagawa A, Wong P, Matsumura F. TCDD causes suppression of growth and differentiation of MCF10A, human mammary epithelial cells by interfering with their insulin receptor signaling through c-Src kinase and ERK activation. J Biochem Mol Toxicol (2004) 18:322-31. doi:10.1002/jbt.20040
    • (2004) J Biochem Mol Toxicol , vol.18 , pp. 322-331
    • Park, S.1    Mazina, O.2    Kitagawa, A.3    Wong, P.4    Matsumura, F.5
  • 37
    • 12844257378 scopus 로고    scopus 로고
    • Studies on the mechanism of rapid activation of protein tyrosine phosphorylation activities, particularly c-Src kinase, by TCDD in MCF10A
    • Mazina O, Park S, Sano H, Wong P, Matsumura F. Studies on the mechanism of rapid activation of protein tyrosine phosphorylation activities, particularly c-Src kinase, by TCDD in MCF10A. J Biochem Mol Toxicol (2004) 18:313-21. doi:10.1002/jbt.20041
    • (2004) J Biochem Mol Toxicol , vol.18 , pp. 313-321
    • Mazina, O.1    Park, S.2    Sano, H.3    Wong, P.4    Matsumura, F.5
  • 38
    • 84884768609 scopus 로고    scopus 로고
    • IL-22 and IDO1 affect immunity and tolerance to murine and human vaginal candidiasis
    • De Luca A, Carvalho A, Cunha C, Iannitti RG, Pitzurra L, Giovannini G, et al. IL-22 and IDO1 affect immunity and tolerance to murine and human vaginal candidiasis. PLoS Pathog (2013) 9:e1003486. doi:10.1371/journal.ppat.1003486
    • (2013) PLoS Pathog , vol.9
    • De Luca, A.1    Carvalho, A.2    Cunha, C.3    Iannitti, R.G.4    Pitzurra, L.5    Giovannini, G.6
  • 39
    • 84904726496 scopus 로고    scopus 로고
    • Immune response profile and development of pathology during Plasmodium berghei Anka infection: the role of the aryl hydrocarbon receptor (AhR)
    • Brant F, Miranda AS, Esper L, Rodrigues DH, Kangussu LM, Bonaventura D, et al. Immune response profile and development of pathology during Plasmodium berghei Anka infection: the role of the aryl hydrocarbon receptor (AhR). Infect Immun (2014) 82(8):3127-40. doi:10.1128/IAI.01733-14
    • (2014) Infect Immun , vol.82 , Issue.8 , pp. 3127-3140
    • Brant, F.1    Miranda, A.S.2    Esper, L.3    Rodrigues, D.H.4    Kangussu, L.M.5    Bonaventura, D.6
  • 40
    • 33846213538 scopus 로고    scopus 로고
    • Carboxyl terminus of hsc70-interacting protein (CHIP) can remodel mature aryl hydrocarbon receptor (AhR) complexes and mediate ubiquitination of both the AhR and the 90 kDa heat-shock protein (hsp90) in vitro
    • Morales JL, Perdew GH. Carboxyl terminus of hsc70-interacting protein (CHIP) can remodel mature aryl hydrocarbon receptor (AhR) complexes and mediate ubiquitination of both the AhR and the 90 kDa heat-shock protein (hsp90) in vitro. Biochemistry (2007) 46:610-21. doi:10.1021/bi062165b
    • (2007) Biochemistry , vol.46 , pp. 610-621
    • Morales, J.L.1    Perdew, G.H.2
  • 41
    • 80053934603 scopus 로고    scopus 로고
    • Cross-talk of dioxin and estrogen receptor signals through the ubiquitin system
    • Ohtake F, Fujii-Kuriyama Y, Kawajiri K, Kato S. Cross-talk of dioxin and estrogen receptor signals through the ubiquitin system. J Steroid Biochem Mol Biol (2011) 127:102-7. doi:10.1016/j.jsbmb.2011.03.007
    • (2011) J Steroid Biochem Mol Biol , vol.127 , pp. 102-107
    • Ohtake, F.1    Fujii-Kuriyama, Y.2    Kawajiri, K.3    Kato, S.4
  • 42
    • 84902589930 scopus 로고    scopus 로고
    • Fludarabine downregulates indoleamine 2,3-dioxygenase in tumors via a proteasome-mediated degradation mechanism
    • Hanafi LA, Gauchat D, Godin-Ethier J, Possamai D, Duvignaud JB, Leclerc D, et al. Fludarabine downregulates indoleamine 2,3-dioxygenase in tumors via a proteasome-mediated degradation mechanism. PLoS One (2014) 9:e99211. doi:10.1371/journal.pone.0099211
    • (2014) PLoS One , vol.9
    • Hanafi, L.A.1    Gauchat, D.2    Godin-Ethier, J.3    Possamai, D.4    Duvignaud, J.B.5    Leclerc, D.6
  • 43
    • 84862303992 scopus 로고    scopus 로고
    • Immunological and nonimmunological effects of indoleamine 2,3-dioxygenase on breast tumor growth and spontaneous metastasis formation
    • Levina V, Su Y, Gorelik E. Immunological and nonimmunological effects of indoleamine 2,3-dioxygenase on breast tumor growth and spontaneous metastasis formation. Clin Dev Immunol (2012) 2012:173029. doi:10.1155/2012/173029
    • (2012) Clin Dev Immunol , vol.2012 , pp. 173029
    • Levina, V.1    Su, Y.2    Gorelik, E.3
  • 44
    • 84881516118 scopus 로고    scopus 로고
    • Indoleamine 2,3-dioxygenase-1 (IDO1) enhances survival and invasiveness of endometrial stromal cells via the activation of JNK signaling pathway
    • Mei J, Li MQ, Ding D, Li DJ, Jin LP, Hu WG, et al. Indoleamine 2,3-dioxygenase-1 (IDO1) enhances survival and invasiveness of endometrial stromal cells via the activation of JNK signaling pathway. Int J Clin Exp Pathol (2013) 6:431-44.
    • (2013) Int J Clin Exp Pathol , vol.6 , pp. 431-444
    • Mei, J.1    Li, M.Q.2    Ding, D.3    Li, D.J.4    Jin, L.P.5    Hu, W.G.6
  • 45
    • 84899921598 scopus 로고    scopus 로고
    • Indoleamine 2,3-dioxygenase 1 (IDO1) is up-regulated in thyroid carcinoma and drives the development of an immunosuppressant tumor microenvironment
    • Moretti S, Menicali E, Voce P, Morelli S, Cantarelli S, Sponziello M, et al. Indoleamine 2,3-dioxygenase 1 (IDO1) is up-regulated in thyroid carcinoma and drives the development of an immunosuppressant tumor microenvironment. J Clin Endocrinol Metab (2014) 99:E832-40. doi:10.1210/jc.2013-3351
    • (2014) J Clin Endocrinol Metab , vol.99 , pp. e832-e840
    • Moretti, S.1    Menicali, E.2    Voce, P.3    Morelli, S.4    Cantarelli, S.5    Sponziello, M.6


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