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Volumn 3, Issue 10, 2014, Pages e957994-1-e957994-10

Trial watch: IDO inhibitors in cancer therapy

Author keywords

1 methyl D tryptophan; INCB024360; indoximod; interferon ; NLG919; peptide based anticancer vaccines

Indexed keywords

4 AMINO N (3 CHLORO 4 FLUOROPHENYL) N' HYDROXY 1,2,5 OXADIAZOLE 3 CARBOXIMIDAMIDE; ALANINE AMINOTRANSFERASE; ANTINEOPLASTIC AGENT; DOCETAXEL; GEMCITABINE; HLA ANTIGEN; INDOLEAMINE 2,3 DIOXYGENASE; INDOLEAMINE 2,3 DIOXYGENASE 1; INDOLEAMINE 2,3 DIOXYGENASE INHIBITOR; INDOXIMOD; IPILIMUMAB; NLG 919; PACLITAXEL; PROGRAMMED DEATH 1 RECEPTOR; SIPULEUCEL T; TEMOZOLOMIDE; TOLL LIKE RECEPTOR 7; UNCLASSIFIED DRUG; VEMURAFENIB;

EID: 84921398751     PISSN: 21624011     EISSN: 2162402X     Source Type: Journal    
DOI: 10.4161/21624011.2014.957994     Document Type: Article
Times cited : (194)

References (177)
  • 1
    • 67649432744 scopus 로고    scopus 로고
    • Inhibitors of indoleamine-2,3-dioxygenase for cancer therapy: can we see the wood for the trees?
    • 19461669
    • S.Lob, A.Konigsrainer, H.G.Rammensee, G.Opelz, P.Terness. Inhibitors of indoleamine-2,3-dioxygenase for cancer therapy: can we see the wood for the trees? Nat Rev Cancer 2009; 9:445-52; PMID:19461669; http://dx.doi.org/10.1038/nrc2639
    • (2009) Nat Rev Cancer , vol.9 , pp. 445-452
    • Lob, S.1    Konigsrainer, A.2    Rammensee, H.G.3    Opelz, G.4    Terness, P.5
  • 2
    • 0042848767 scopus 로고    scopus 로고
    • Tryptophan and the immune response
    • 12848846
    • J.R.Moffett, M.A.Namboodiri. Tryptophan and the immune response. Immunol Cell Biol 2003; 81:247-65; PMID:12848846; http://dx.doi.org/10.1046/j.1440-1711.2003.t01-1-01177.x
    • (2003) Immunol Cell Biol , vol.81 , pp. 247-265
    • Moffett, J.R.1    Namboodiri, M.A.2
  • 3
    • 0004370865 scopus 로고
    • The conversion of tryptophan to kynurenine in liver. II. The enzymatic hydrolysis of formylkynurenine
    • 14794728
    • A.H.Mehler, W.E.Knox. The conversion of tryptophan to kynurenine in liver. II. The enzymatic hydrolysis of formylkynurenine. J Biol Chem 1950; 187:431-38; PMID:14794728
    • (1950) J Biol Chem , vol.187 , pp. 431-438
    • Mehler, A.H.1    Knox, W.E.2
  • 4
    • 78651013065 scopus 로고
    • The conversion of tryptophan to kynurenine in liver. I. The coupled tryptophan peroxidase-oxidase system forming formylkynurenine
    • 14794727
    • W.E.Knox, A.H.Mehler. The conversion of tryptophan to kynurenine in liver. I. The coupled tryptophan peroxidase-oxidase system forming formylkynurenine. J Biol Chem 1950; 187:419-30; PMID:14794727
    • (1950) J Biol Chem , vol.187 , pp. 419-430
    • Knox, W.E.1    Mehler, A.H.2
  • 5
    • 54849418903 scopus 로고    scopus 로고
    • IDO1 and IDO2 are expressed in human tumors: levo- but not dextro-1-methyl tryptophan inhibits tryptophan catabolism
    • 18418598
    • S.Lob, A.Konigsrainer, D.Zieker, B.L.Brucher, H.G.Rammensee, G.Opelz, P.Terness. IDO1 and IDO2 are expressed in human tumors: levo- but not dextro-1-methyl tryptophan inhibits tryptophan catabolism. Cancer Immunol Immunother 2009; 58:153-57; PMID:18418598; http://dx.doi.org/10.1007/s00262-008-0513-6
    • (2009) Cancer Immunol Immunother , vol.58 , pp. 153-157
    • Lob, S.1    Konigsrainer, A.2    Zieker, D.3    Brucher, B.L.4    Rammensee, H.G.5    Opelz, G.6    Terness, P.7
  • 6
    • 34547643025 scopus 로고    scopus 로고
    • Novel tryptophan catabolic enzyme IDO2 is the preferred biochemical target of the antitumor indoleamine 2,3-dioxygenase inhibitory compound D-1-methyl-tryptophan
    • 17671174
    • R.Metz, J.B.Duhadaway, U.Kamasani, L.Laury-Kleintop, A.J.Muller, G.C.Prendergast. Novel tryptophan catabolic enzyme IDO2 is the preferred biochemical target of the antitumor indoleamine 2,3-dioxygenase inhibitory compound D-1-methyl-tryptophan. Cancer Res 2007; 67:7082-87; PMID:17671174; http://dx.doi.org/10.1158/0008-5472.CAN-07-1872
    • (2007) Cancer Res , vol.67 , pp. 7082-7087
    • Metz, R.1    Duhadaway, J.B.2    Kamasani, U.3    Laury-Kleintop, L.4    Muller, A.J.5    Prendergast, G.C.6
  • 7
    • 59149092788 scopus 로고    scopus 로고
    • Exploring the mechanism of tryptophan 2,3-dioxygenase
    • 19021508
    • S.J.Thackray, C.G.Mowat, S.K.Chapman. Exploring the mechanism of tryptophan 2,3-dioxygenase. Biochem Soc Trans 2008; 36:1120-23; PMID:19021508; http://dx.doi.org/10.1042/BST0361120
    • (2008) Biochem Soc Trans , vol.36 , pp. 1120-1123
    • Thackray, S.J.1    Mowat, C.G.2    Chapman, S.K.3
  • 8
    • 0018261932 scopus 로고
    • Specific induction of pulmonary indoleamine 2,3-dioxygenase by bacterial lipopolysaccharide
    • 258162
    • O.Hayaishi, R.Yoshida. Specific induction of pulmonary indoleamine 2,3-dioxygenase by bacterial lipopolysaccharide. Ciba Found Symp 1978:199-203; PMID:258162
    • (1978) Ciba Found Symp , pp. 199-203
    • Hayaishi, O.1    Yoshida, R.2
  • 9
    • 0018179447 scopus 로고
    • Induction of pulmonary indoleamine 2,3-dioxygenase by intraperitoneal injection of bacterial lipopolysaccharide
    • 279015
    • R.Yoshida, O.Hayaishi. Induction of pulmonary indoleamine 2,3-dioxygenase by intraperitoneal injection of bacterial lipopolysaccharide. Proc Natl Acad Sci U S A 1978; 75:3998-4000; PMID:279015; http://dx.doi.org/10.1073/pnas.75.8.3998
    • (1978) Proc Natl Acad Sci U S A , vol.75 , pp. 3998-4000
    • Yoshida, R.1    Hayaishi, O.2
  • 10
    • 0020628063 scopus 로고
    • Induction of indoleamine 2,3-dioxygenase in alveolar interstitial cells of mouse lung by bacterial lipopolysaccharide
    • 6343379
    • Y.Urade, R.Yoshida, H.Kitamura, O.Hayaishi. Induction of indoleamine 2,3-dioxygenase in alveolar interstitial cells of mouse lung by bacterial lipopolysaccharide. J Biol Chem 1983; 258:6621-27; PMID:6343379
    • (1983) J Biol Chem , vol.258 , pp. 6621-6627
    • Urade, Y.1    Yoshida, R.2    Kitamura, H.3    Hayaishi, O.4
  • 11
    • 0000056144 scopus 로고
    • Interferon gamma blocks the growth of Toxoplasma gondii in human fibroblasts by inducing the host cells to degrade tryptophan
    • 6422465
    • E.R.Pfefferkorn. Interferon gamma blocks the growth of Toxoplasma gondii in human fibroblasts by inducing the host cells to degrade tryptophan. Proc Natl Acad Sci U S A 1984; 81:908-12; PMID:6422465; http://dx.doi.org/10.1073/pnas.81.3.908
    • (1984) Proc Natl Acad Sci U S A , vol.81 , pp. 908-912
    • Pfefferkorn, E.R.1
  • 12
    • 0033519278 scopus 로고    scopus 로고
    • Inhibition of T cell proliferation by macrophage tryptophan catabolism
    • 10224276
    • D.H.Munn, E.Shafizadeh, J.T.Attwood, I.Bondarev, A.Pashine, A.L.Mellor. Inhibition of T cell proliferation by macrophage tryptophan catabolism. J Exp Med 1999; 189:1363-72; PMID:10224276; http://dx.doi.org/10.1084/jem.189.9.1363
    • (1999) J Exp Med , vol.189 , pp. 1363-1372
    • Munn, D.H.1    Shafizadeh, E.2    Attwood, J.T.3    Bondarev, I.4    Pashine, A.5    Mellor, A.L.6
  • 13
    • 34147112868 scopus 로고    scopus 로고
    • CD40Ig treatment results in allograft acceptance mediated by CD8CD45RC T cells, IFN-gamma, and indoleamine 2,3-dioxygenase
    • 17404623
    • C.Guillonneau, M.Hill, F.X.Hubert, E.Chiffoleau, C.Herve, X.L.Li, M.Heslan, C.Usal, L.Tesson, S.Ménoret CD40Ig treatment results in allograft acceptance mediated by CD8CD45RC T cells, IFN-gamma, and indoleamine 2,3-dioxygenase. J Clin Invest 2007; 117:1096-106; PMID:17404623; http://dx.doi.org/10.1172/JCI28801
    • (2007) J Clin Invest , vol.117 , pp. 1096-1106
    • Guillonneau, C.1    Hill, M.2    Hubert, F.X.3    Chiffoleau, E.4    Herve, C.5    Li, X.L.6    Heslan, M.7    Usal, C.8    Tesson, L.9    Ménoret, S.10
  • 14
    • 0034176031 scopus 로고    scopus 로고
    • Indoleamine 2,3-dioxygenase production by human dendritic cells results in the inhibition of T cell proliferation
    • 10725715
    • P.Hwu, M.X.Du, R.Lapointe, M.Do, M.W.Taylor, H.A.Young. Indoleamine 2,3-dioxygenase production by human dendritic cells results in the inhibition of T cell proliferation. J Immunol 2000; 164:3596-99; PMID:10725715; http://dx.doi.org/10.4049/jimmu-nol.164.7.3596
    • (2000) J Immunol , vol.164 , pp. 3596-3599
    • Hwu, P.1    Du, M.X.2    Lapointe, R.3    Do, M.4    Taylor, M.W.5    Young, H.A.6
  • 15
    • 84901725844 scopus 로고    scopus 로고
    • Chronic lymphocytic leukemia nurse-like cells express hepatocyte growth factor receptor (c-MET) and indoleamine 2,3-dioxygenase and display features of immunosuppressive type 2 skewed macrophages
    • 24561793
    • P.Giannoni, G.Pietra, G.Travaini, R.Quarto, G.Shyti, R.Benelli, L.Ottaggio, M.C.Mingari, S.Zupo, G.Cutrona Chronic lymphocytic leukemia nurse-like cells express hepatocyte growth factor receptor (c-MET) and indoleamine 2,3-dioxygenase and display features of immunosuppressive type 2 skewed macrophages. Haematologica 2014; 99:1078-87; PMID:24561793; http://dx.doi.org/10.3324/haematol.2013.091405
    • (2014) Haematologica , vol.99 , pp. 1078-1087
    • Giannoni, P.1    Pietra, G.2    Travaini, G.3    Quarto, R.4    Shyti, G.5    Benelli, R.6    Ottaggio, L.7    Mingari, M.C.8    Zupo, S.9    Cutrona, G.10
  • 16
    • 84860247174 scopus 로고    scopus 로고
    • IFN-gamma-driven IDO production from macrophages protects IL-4Ralpha-deficient mice against lethality during Schistosoma mansoni infection
    • 22426339
    • R.Rani, M.B.Jordan, S.Divanovic, D.R.Herbert. IFN-gamma-driven IDO production from macrophages protects IL-4Ralpha-deficient mice against lethality during Schistosoma mansoni infection. Am J Pathol 2012; 180:2001-08; PMID:22426339; http://dx.doi.org/10.1016/j.ajpath.2012.01.013
    • (2012) Am J Pathol , vol.180 , pp. 2001-2008
    • Rani, R.1    Jordan, M.B.2    Divanovic, S.3    Herbert, D.R.4
  • 17
    • 27144489077 scopus 로고    scopus 로고
    • Inhibition of indoleamine 2,3-dioxygenase (IDO) enhances elimination of virus-infected macrophages in an animal model of HIV-1 encephalitis
    • 15961516
    • R.Potula, L.Poluektova, B.Knipe, J.Chrastil, D.Heilman, H.Dou, O.Takikawa, D.H.Munn, H.E.Gendelman, Y.Persidsky. Inhibition of indoleamine 2,3-dioxygenase (IDO) enhances elimination of virus-infected macrophages in an animal model of HIV-1 encephalitis. Blood 2005; 106:2382-90; PMID:15961516; http://dx.doi.org/10.1182/blood-2005-04-1403
    • (2005) Blood , vol.106 , pp. 2382-2390
    • Potula, R.1    Poluektova, L.2    Knipe, B.3    Chrastil, J.4    Heilman, D.5    Dou, H.6    Takikawa, O.7    Munn, D.H.8    Gendelman, H.E.9    Persidsky, Y.10
  • 18
    • 84907029151 scopus 로고    scopus 로고
    • Noncanonical NF-kappaB activation mediates STAT3-stimulated IDO upregulation in myeloid-derived suppressor cells in breast cancer
    • 25063873
    • J.Yu, Y.Wang, F.Yan, P.Zhang, H.Li, H.Zhao, C.Yan, F.Yan, X.Ren. Noncanonical NF-kappaB activation mediates STAT3-stimulated IDO upregulation in myeloid-derived suppressor cells in breast cancer. J Immunol 2014; 193:2574-86; PMID:25063873; http://dx.doi.org/10.4049/jimmunol.1400833
    • (2014) J Immunol , vol.193 , pp. 2574-2586
    • Yu, J.1    Wang, Y.2    Yan, F.3    Zhang, P.4    Li, H.5    Zhao, H.6    Yan, C.7    Yan, F.8    Ren, X.9
  • 20
    • 84875261622 scopus 로고    scopus 로고
    • Indoleamine 2,3 dioxygenase and metabolic control of immune responses
    • 23103127
    • D.H.Munn, A.L.Mellor. Indoleamine 2,3 dioxygenase and metabolic control of immune responses. Trends Immunol 2013; 34:137-43; PMID:23103127; http://dx.doi.org/10.1016/j.it.2012.10.001
    • (2013) Trends Immunol , vol.34 , pp. 137-143
    • Munn, D.H.1    Mellor, A.L.2
  • 23
    • 0142137237 scopus 로고    scopus 로고
    • Evidence for a tumoral immune resistance mechanism based on tryptophan degradation by indoleamine 2,3-dioxygenase
    • 14502282
    • C.Uyttenhove, L.Pilotte, I.Theate, V.Stroobant, D.Colau, N.Parmentier, T.Boon, B.J.Van den Eynde. Evidence for a tumoral immune resistance mechanism based on tryptophan degradation by indoleamine 2,3-dioxygenase. Nat Med 2003; 9:1269-74; PMID:14502282; http://dx.doi.org/10.1038/nm934
    • (2003) Nat Med , vol.9 , pp. 1269-1274
    • Uyttenhove, C.1    Pilotte, L.2    Theate, I.3    Stroobant, V.4    Colau, D.5    Parmentier, N.6    Boon, T.7    Van den Eynde, B.J.8
  • 26
    • 19344377474 scopus 로고    scopus 로고
    • GCN2 kinase in T cells mediates proliferative arrest and anergy induction in response to indoleamine 2,3-dioxygenase
    • 15894280
    • D.H.Munn, M.D.Sharma, B.Baban, H.P.Harding, Y.Zhang, D.Ron, A.L.Mellor. GCN2 kinase in T cells mediates proliferative arrest and anergy induction in response to indoleamine 2,3-dioxygenase. Immunity 2005; 22:633-42; PMID:15894280; http://dx.doi.org/10.1016/j.immuni.2005.03.013
    • (2005) Immunity , vol.22 , pp. 633-642
    • Munn, D.H.1    Sharma, M.D.2    Baban, B.3    Harding, H.P.4    Zhang, Y.5    Ron, D.6    Mellor, A.L.7
  • 27
    • 84905456971 scopus 로고    scopus 로고
    • Organelle-specific initiation of cell death
    • 25082195
    • L.Galluzzi, J.M.Bravo-San Pedro, G.Kroemer. Organelle-specific initiation of cell death. Nat Cell Biol 2014; 16:728-36; PMID:25082195; http://dx.doi.org/10.1038/ncb3005
    • (2014) Nat Cell Biol , vol.16 , pp. 728-736
    • Galluzzi, L.1    Bravo-San Pedro, J.M.2    Kroemer, G.3
  • 28
    • 70249124641 scopus 로고    scopus 로고
    • + T cells is responsible for indoleamine 2,3-dioxygenase-dependent immune suppression
    • 19564344
    • + T cells is responsible for indoleamine 2,3-dioxygenase-dependent immune suppression. J Immunol 2009; 183:1022-31; PMID:19564344; http://dx.doi.org/10.4049/jimmunol.0900408
    • (2009) J Immunol , vol.183 , pp. 1022-1031
    • Liu, H.1    Liu, L.2    Liu, K.3    Bizargity, P.4    Hancock, W.W.5    Visner, G.A.6
  • 30
    • 0037136328 scopus 로고    scopus 로고
    • Tryptophan-derived catabolites are responsible for inhibition of T and natural killer cell proliferation induced by indoleamine 2,3-dioxygenase
    • 12186838
    • G.Frumento, R.Rotondo, M.Tonetti, G.Damonte, U.Benatti, G.B.Ferrara. Tryptophan-derived catabolites are responsible for inhibition of T and natural killer cell proliferation induced by indoleamine 2,3-dioxygenase. J Exp Med 2002; 196:459-68; PMID:12186838; http://dx.doi.org/10.1084/jem.20020121
    • (2002) J Exp Med , vol.196 , pp. 459-468
    • Frumento, G.1    Rotondo, R.2    Tonetti, M.3    Damonte, G.4    Benatti, U.5    Ferrara, G.B.6
  • 31
    • 33750699056 scopus 로고    scopus 로고
    • The tryptophan catabolite L-kynurenine inhibits the surface expression of NKp46- and NKG2D-activating receptors and regulates NK-cell function
    • 16902152
    • M.Della Chiesa, S.Carlomagno, G.Frumento, M.Balsamo, C.Cantoni, R.Conte, L.Moretta, A.Moretta, M.Vitale. The tryptophan catabolite L-kynurenine inhibits the surface expression of NKp46- and NKG2D-activating receptors and regulates NK-cell function. Blood 2006; 108:4118-25; PMID:16902152; http://dx.doi.org/10.1182/blood-2006-03-006700
    • (2006) Blood , vol.108 , pp. 4118-4125
    • Della Chiesa, M.1    Carlomagno, S.2    Frumento, G.3    Balsamo, M.4    Cantoni, C.5    Conte, R.6    Moretta, L.7    Moretta, A.8    Vitale, M.9
  • 32
    • 84866463547 scopus 로고    scopus 로고
    • Downregulation of indoleamine-2,3-dioxygenase in cervical cancer cells suppresses tumor growth by promoting natural killer cell accumulation
    • 22923135
    • N.Sato, Y.Saga, H.Mizukami, D.Wang, S.Takahashi, H.Nonaka, H.Fujiwara, Y.Takei, S.Machida, O.Takikawa Downregulation of indoleamine-2,3-dioxygenase in cervical cancer cells suppresses tumor growth by promoting natural killer cell accumulation. Oncol Rep 2012; 28:1574-78; PMID:22923135; http://dx.doi.org/10.3892/or.2012.1984
    • (2012) Oncol Rep , vol.28 , pp. 1574-1578
    • Sato, N.1    Saga, Y.2    Mizukami, H.3    Wang, D.4    Takahashi, S.5    Nonaka, H.6    Fujiwara, H.7    Takei, Y.8    Machida, S.9    Takikawa, O.10
  • 33
    • 40649121252 scopus 로고    scopus 로고
    • Modulation of invariant natural killer T cell cytokine responses by indoleamine 2,3-dioxygenase
    • 18272236
    • A.Molano, P.A.Illarionov, G.S.Besra, C.Putterman, S.A.Porcelli. Modulation of invariant natural killer T cell cytokine responses by indoleamine 2,3-dioxygenase. Immunol Lett 2008; 117:81-90; PMID:18272236; http://dx.doi.org/10.1016/j.imlet.2007.12.013
    • (2008) Immunol Lett , vol.117 , pp. 81-90
    • Molano, A.1    Illarionov, P.A.2    Besra, G.S.3    Putterman, C.4    Porcelli, S.A.5
  • 35
    • 78649880396 scopus 로고    scopus 로고
    • An interaction between kynurenine and the aryl hydrocarbon receptor can generate regulatory T cells
    • 20720200
    • J.D.Mezrich, J.H.Fechner, X.Zhang, B.P.Johnson, W.J.Burlingham, C.A.Bradfield. An interaction between kynurenine and the aryl hydrocarbon receptor can generate regulatory T cells. J Immunol 2010; 185:3190-98; PMID:20720200; http://dx.doi.org/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
  • 37
    • 77952977625 scopus 로고    scopus 로고
    • Tryptophan catabolism by indoleamine 2,3-dioxygenase 1 alters the balance of TH17 to regulatory T cells in HIV disease
    • 20484731
    • D.Favre, J.Mold, P.W.Hunt, B.Kanwar, P.Loke, L.Seu, J.D.Barbour, M.M.Lowe, A.Jayawardene, F.Aweeka Tryptophan catabolism by indoleamine 2,3-dioxygenase 1 alters the balance of TH17 to regulatory T cells in HIV disease. Sci Transl Med 2010; 2:32ra6; PMID:20484731; http://dx.doi.org/10.1126/scitranslmed.3000632
    • (2010) Sci Transl Med , vol.2 , pp. 32
    • Favre, D.1    Mold, J.2    Hunt, P.W.3    Kanwar, B.4    Loke, P.5    Seu, L.6    Barbour, J.D.7    Lowe, M.M.8    Jayawardene, A.9    Aweeka, F.10
  • 38
    • 77955859470 scopus 로고    scopus 로고
    • Activation of the aryl hydrocarbon receptor induces human type 1 regulatory T cell-like and Foxp3(+) regulatory T cells
    • 20676092
    • R.Gandhi, D.Kumar, E.J.Burns, M.Nadeau, B.Dake, A.Laroni, D.Kozoriz, H.L.Weiner, F.J.Quintana. Activation of the aryl hydrocarbon receptor induces human type 1 regulatory T cell-like and Foxp3(+) regulatory T cells. Nat Immunol 2010; 11:846-53; PMID:20676092; http://dx.doi.org/10.1038/ni.1915
    • (2010) Nat Immunol , vol.11 , pp. 846-853
    • Gandhi, R.1    Kumar, D.2    Burns, E.J.3    Nadeau, M.4    Dake, B.5    Laroni, A.6    Kozoriz, D.7    Weiner, H.L.8    Quintana, F.J.9
  • 40
    • 70149101645 scopus 로고    scopus 로고
    • IDO activates regulatory T cells and blocks their conversion into Th17-like T cells
    • 19635913
    • B.Baban, P.R.Chandler, M.D.Sharma, J.Pihkala, P.A.Koni, D.H.Munn, A.L.Mellor. IDO activates regulatory T cells and blocks their conversion into Th17-like T cells. J Immunol 2009; 183:2475-83; PMID:19635913; http://dx.doi.org/10.4049/jimmunol.0900986
    • (2009) J Immunol , vol.183 , pp. 2475-2483
    • Baban, B.1    Chandler, P.R.2    Sharma, M.D.3    Pihkala, J.4    Koni, P.A.5    Munn, D.H.6    Mellor, A.L.7
  • 42
    • 78650560167 scopus 로고    scopus 로고
    • Aryl hydrocarbon receptor negatively regulates dendritic cell immunogenicity via a kynurenine-dependent mechanism
    • 21041655
    • N.T.Nguyen, A.Kimura, T.Nakahama, I.Chinen, K.Masuda, K.Nohara, Y.Fujii-Kuriyama, T.Kishimoto. Aryl hydrocarbon receptor negatively regulates dendritic cell immunogenicity via a kynurenine-dependent mechanism. Proc Natl Acad Sci U S A 2010; 107:19961-66; PMID:21041655; http://dx.doi.org/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    Fujii-Kuriyama, Y.7    Kishimoto, T.8
  • 43
    • 84868281887 scopus 로고    scopus 로고
    • A distinct tolerogenic subset of splenic IDO(+)CD11b(+) dendritic cells from orally tolerized mice is responsible for induction of systemic immune tolerance and suppression of collagen-induced arthritis
    • 23121975
    • M.J.Park, K.S.Park, H.S.Park, M.L.Cho, S.Y.Hwang, S.Y.Min, S.Y.Min, M.K.Park, S.H.Park, H.Y.Kim. A distinct tolerogenic subset of splenic IDO(+)CD11b(+) dendritic cells from orally tolerized mice is responsible for induction of systemic immune tolerance and suppression of collagen-induced arthritis. Cell Immunol 2012; 278:45-54; PMID:23121975; http://dx.doi.org/10.1016/j.cellimm.2012.06.009
    • (2012) Cell Immunol , vol.278 , pp. 45-54
    • Park, M.J.1    Park, K.S.2    Park, H.S.3    Cho, M.L.4    Hwang, S.Y.5    Min, S.Y.6    Min, S.Y.7    Park, M.K.8    Park, S.H.9    Kim, H.Y.10
  • 45
    • 33646893538 scopus 로고    scopus 로고
    • The combined effects of tryptophan starvation and tryptophan catabolites down-regulate T cell receptor zeta-chain and induce a regulatory phenotype in naive T cells
    • 16709834
    • F.Fallarino, U.Grohmann, S.You, B.C.McGrath, D.R.Cavener, C.Vacca, C.Orabona, R.Bianchi, M.L.Belladonna, C.Volpi The combined effects of tryptophan starvation and tryptophan catabolites down-regulate T cell receptor zeta-chain and induce a regulatory phenotype in naive T cells. J Immunol 2006; 176:6752-61; PMID:16709834; http://dx.doi.org/10.4049/jimmunol.176.11.6752
    • (2006) J Immunol , vol.176 , pp. 6752-6761
    • Fallarino, F.1    Grohmann, U.2    You, S.3    McGrath, B.C.4    Cavener, D.R.5    Vacca, C.6    Orabona, C.7    Bianchi, R.8    Belladonna, M.L.9    Volpi, C.10
  • 46
    • 54049151564 scopus 로고    scopus 로고
    • The indoleamine 2,3-dioxygenase pathway is essential for human plasmacytoid dendritic cell-induced adaptive T regulatory cell generation
    • 18832696
    • W.Chen, X.Liang, A.J.Peterson, D.H.Munn, B.R.Blazar. The indoleamine 2,3-dioxygenase pathway is essential for human plasmacytoid dendritic cell-induced adaptive T regulatory cell generation. J Immunol 2008; 181:5396-404; PMID:18832696; http://dx.doi.org/10.4049/jimmunol.181.8.5396
    • (2008) J Immunol , vol.181 , pp. 5396-5404
    • Chen, W.1    Liang, X.2    Peterson, A.J.3    Munn, D.H.4    Blazar, B.R.5
  • 47
    • 0042591467 scopus 로고    scopus 로고
    • Cutting edge: induced indoleamine 2,3 dioxygenase expression in dendritic cell subsets suppresses T cell clonal expansion
    • 12902462
    • A.L.Mellor, B.Baban, P.Chandler, B.Marshall, K.Jhaver, A.Hansen, P.A.Koni, M.Iwashima, D.H.Munn. Cutting edge: induced indoleamine 2,3 dioxygenase expression in dendritic cell subsets suppresses T cell clonal expansion. J Immunol 2003; 171:1652-55; PMID:12902462; http://dx.doi.org/10.4049/jimmunol.171.4.1652
    • (2003) J Immunol , vol.171 , pp. 1652-1655
    • Mellor, A.L.1    Baban, B.2    Chandler, P.3    Marshall, B.4    Jhaver, K.5    Hansen, A.6    Koni, P.A.7    Iwashima, M.8    Munn, D.H.9
  • 48
    • 26444489716 scopus 로고    scopus 로고
    • A minor population of splenic dendritic cells expressing CD19 mediates IDO-dependent T cell suppression via type I IFN signaling following B7 ligation
    • 15967784
    • B.Baban, A.M.Hansen, P.R.Chandler, A.Manlapat, A.Bingaman, D.J.Kahler, D.H.Munn, A.L.Mellor. A minor population of splenic dendritic cells expressing CD19 mediates IDO-dependent T cell suppression via type I IFN signaling following B7 ligation. Int Immunol 2005; 17:909-19; PMID:15967784; http://dx.doi.org/10.1093/intimm/dxh271
    • (2005) Int Immunol , vol.17 , pp. 909-919
    • Baban, B.1    Hansen, A.M.2    Chandler, P.R.3    Manlapat, A.4    Bingaman, A.5    Kahler, D.J.6    Munn, D.H.7    Mellor, A.L.8
  • 49
    • 8144224918 scopus 로고    scopus 로고
    • Interferon-gamma-modified dendritic cells suppress B cell function and ameliorate the development of experimental autoimmune myasthenia gravis
    • 15498031
    • S.B.Adikari, H.Lian, H.Link, Y.M.Huang, B.G.Xiao. Interferon-gamma-modified dendritic cells suppress B cell function and ameliorate the development of experimental autoimmune myasthenia gravis. Clin Exp Immunol 2004; 138:230-36; PMID:15498031; http://dx.doi.org/10.1111/j.1365-2249.2004.02585.x
    • (2004) Clin Exp Immunol , vol.138 , pp. 230-236
    • Adikari, S.B.1    Lian, H.2    Link, H.3    Huang, Y.M.4    Xiao, B.G.5
  • 52
    • 4644220112 scopus 로고    scopus 로고
    • Murine plasmacytoid dendritic cells initiate the immunosuppressive pathway of tryptophan catabolism in response to CD200 receptor engagement
    • 15356121
    • F.Fallarino, C.Asselin-Paturel, C.Vacca, R.Bianchi, S.Gizzi, M.C.Fioretti, G.Trinchieri, U.Grohmann, P.Puccetti. Murine plasmacytoid dendritic cells initiate the immunosuppressive pathway of tryptophan catabolism in response to CD200 receptor engagement. J Immunol 2004; 173:3748-54; PMID:15356121; http://dx.doi.org/10.4049/jimmu-nol.173.6.3748
    • (2004) J Immunol , vol.173 , pp. 3748-3754
    • Fallarino, F.1    Asselin-Paturel, C.2    Vacca, C.3    Bianchi, R.4    Gizzi, S.5    Fioretti, M.C.6    Trinchieri, G.7    Grohmann, U.8    Puccetti, P.9
  • 53
    • 34848915783 scopus 로고    scopus 로고
    • Plasmacytoid dendritic cells from mouse tumor-draining lymph nodes directly activate mature Tregs via indoleamine 2,3-dioxygenase
    • 17710230
    • M.D.Sharma, B.Baban, P.Chandler, D.Y.Hou, N.Singh, H.Yagita, M.Azuma, B.R.Blazar, A.L.Mellor, D.H.Munn. Plasmacytoid dendritic cells from mouse tumor-draining lymph nodes directly activate mature Tregs via indoleamine 2,3-dioxygenase. J Clin Invest 2007; 117:2570-82; PMID:17710230; http://dx.doi.org/10.1172/JCI31911
    • (2007) J Clin Invest , vol.117 , pp. 2570-2582
    • Sharma, M.D.1    Baban, B.2    Chandler, P.3    Hou, D.Y.4    Singh, N.5    Yagita, H.6    Azuma, M.7    Blazar, B.R.8    Mellor, A.L.9    Munn, D.H.10
  • 54
    • 35748940007 scopus 로고    scopus 로고
    • Dendritic cell type determines the mechanism of bystander suppression by adaptive T regulatory cells specific for the minor antigen HA-1
    • 17785778
    • R.A.Derks, E.Jankowska-Gan, Q.Xu, W.J.Burlingham. Dendritic cell type determines the mechanism of bystander suppression by adaptive T regulatory cells specific for the minor antigen HA-1. J Immunol 2007; 179:3443-51; PMID:17785778; http://dx.doi.org/10.4049/jimmunol.179.6.3443
    • (2007) J Immunol , vol.179 , pp. 3443-3451
    • Derks, R.A.1    Jankowska-Gan, E.2    Xu, Q.3    Burlingham, W.J.4
  • 56
    • 84886944946 scopus 로고    scopus 로고
    • Plasmacytoid dendritic cells and regulatory T cells in the tumor microenvironment: a dangerous liaison
    • 23762788
    • C.Conrad, M.Gilliet. Plasmacytoid dendritic cells and regulatory T cells in the tumor microenvironment: a dangerous liaison. Oncoimmunology 2013; 2:e23887; PMID:23762788; http://dx.doi.org/10.4161/onci.23887
    • (2013) Oncoimmunology , vol.2 , pp. 23887
    • Conrad, C.1    Gilliet, M.2
  • 57
    • 84882684526 scopus 로고    scopus 로고
    • Plasmacytoid dendritic cells deficient in IFNalpha production promote the amplification of FOXP3 regulatory T cells and are associated with poor prognosis in breast cancer patients
    • 23482834
    • V.Sisirak, J.Faget, N.Vey, J.Y.Blay, C.Menetrier-Caux, C.Caux, N.Bendriss-Vermare. Plasmacytoid dendritic cells deficient in IFNalpha production promote the amplification of FOXP3 regulatory T cells and are associated with poor prognosis in breast cancer patients. Oncoimmunology 2013; 2:e22338; PMID:23482834; http://dx.doi.org/10.4161/onci.22338
    • (2013) Oncoimmunology , vol.2 , pp. 22338
    • Sisirak, V.1    Faget, J.2    Vey, N.3    Blay, J.Y.4    Menetrier-Caux, C.5    Caux, C.6    Bendriss-Vermare, N.7
  • 60
    • 84884491148 scopus 로고    scopus 로고
    • HIV-1 Tat protein induces the production of IDO in human monocyte derived-dendritic cells through a direct mechanism: effect on T cells proliferation
    • 24073214
    • R.Planes, E.Bahraoui. HIV-1 Tat protein induces the production of IDO in human monocyte derived-dendritic cells through a direct mechanism: effect on T cells proliferation. PLoS One 2013; 8:e74551; PMID:24073214; http://dx.doi.org/10.1371/journal.pone.0074551
    • (2013) PLoS One , vol.8 , pp. 74551
    • Planes, R.1    Bahraoui, E.2
  • 61
    • 84865546531 scopus 로고    scopus 로고
    • Activation of the noncanonical NF-kappaB pathway by HIV controls a dendritic cell immunoregulatory phenotype
    • 22879398
    • O.Manches, M.V.Fernandez, J.Plumas, L.Chaperot, N.Bhardwaj. Activation of the noncanonical NF-kappaB pathway by HIV controls a dendritic cell immunoregulatory phenotype. Proc Natl Acad Sci U S A 2012; 109:14122-27; PMID:22879398; http://dx.doi.org/10.1073/pnas.1204032109
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 14122-14127
    • Manches, O.1    Fernandez, M.V.2    Plumas, J.3    Chaperot, L.4    Bhardwaj, N.5
  • 62
    • 0033998033 scopus 로고    scopus 로고
    • Induction of indolamine 2,3-dioxygenase in primary human macrophages by human immunodeficiency virus type 1 is strain dependent
    • 10756023
    • R.S.Grant, H.Naif, S.J.Thuruthyil, N.Nasr, T.Littlejohn, O.Takikawa, V.Kapoor. Induction of indolamine 2,3-dioxygenase in primary human macrophages by human immunodeficiency virus type 1 is strain dependent. J Virol 2000; 74:4110-15; PMID:10756023; http://dx.doi.org/10.1128/JVI.74.9.4110-4115.2000
    • (2000) J Virol , vol.74 , pp. 4110-4115
    • Grant, R.S.1    Naif, H.2    Thuruthyil, S.J.3    Nasr, N.4    Littlejohn, T.5    Takikawa, O.6    Kapoor, V.7
  • 63
    • 0031900585 scopus 로고    scopus 로고
    • Serum kynurenine-to-tryptophan ratio increases with progressive disease in HIV-infected patients
    • 9554499
    • M.Huengsberg, J.B.Winer, M.Gompels, R.Round, J.Ross, M.Shahmanesh. Serum kynurenine-to-tryptophan ratio increases with progressive disease in HIV-infected patients. Clin Chem 1998; 44:858-62; PMID:9554499
    • (1998) Clin Chem , vol.44 , pp. 858-862
    • Huengsberg, M.1    Winer, J.B.2    Gompels, M.3    Round, R.4    Ross, J.5    Shahmanesh, M.6
  • 67
    • 16244408626 scopus 로고    scopus 로고
    • Inhibition of indoleamine 2,3-dioxygenase, an immunoregulatory target of the cancer suppression gene Bin1, potentiates cancer chemotherapy
    • 15711557
    • A.J.Muller, J.B.DuHadaway, P.S.Donover, E.Sutanto-Ward, G.C.Prendergast. Inhibition of indoleamine 2,3-dioxygenase, an immunoregulatory target of the cancer suppression gene Bin1, potentiates cancer chemotherapy. Nat Med 2005; 11:312-19; PMID:15711557; http://dx.doi.org/10.1038/nm1196
    • (2005) Nat Med , vol.11 , pp. 312-319
    • Muller, A.J.1    DuHadaway, J.B.2    Donover, P.S.3    Sutanto-Ward, E.4    Prendergast, G.C.5
  • 68
    • 0041833704 scopus 로고    scopus 로고
    • Expression of a MYCN-interacting isoform of the tumor suppressor BIN1 is reduced in neuroblastomas with unfavorable biological features
    • 12960121
    • T.Tajiri, X.Liu, P.M.Thompson, S.Tanaka, S.Suita, H.Zhao, J.M.Maris, G.C.Prendergast, M.D.Hogarty. Expression of a MYCN-interacting isoform of the tumor suppressor BIN1 is reduced in neuroblastomas with unfavorable biological features. Clin Cancer Res 2003; 9:3345-55; PMID:12960121
    • (2003) Clin Cancer Res , vol.9 , pp. 3345-3355
    • Tajiri, T.1    Liu, X.2    Thompson, P.M.3    Tanaka, S.4    Suita, S.5    Zhao, H.6    Maris, J.M.7    Prendergast, G.C.8    Hogarty, M.D.9
  • 69
    • 0033578314 scopus 로고    scopus 로고
    • Mechanism for elimination of a tumor suppressor: aberrant splicing of a brain-specific exon causes loss of function of Bin1 in melanoma
    • 10449755
    • K.Ge, J.DuHadaway, W.Du, M.Herlyn, U.Rodeck, G.C.Prendergast. Mechanism for elimination of a tumor suppressor: aberrant splicing of a brain-specific exon causes loss of function of Bin1 in melanoma. Proc Natl Acad Sci U S A 1999; 96:9689-94; PMID:10449755; http://dx.doi.org/10.1073/pnas.96.17.9689
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 9689-9694
    • Ge, K.1    DuHadaway, J.2    Du, W.3    Herlyn, M.4    Rodeck, U.5    Prendergast, G.C.6
  • 70
    • 34548016276 scopus 로고    scopus 로고
    • Bin1 ablation increases susceptibility to cancer during aging, particularly lung cancer
    • 17699764
    • M.Y.Chang, J.Boulden, J.B.Katz, L.Wang, T.J.Meyer, A.P.Soler, A.J.Muller, G.C.Prendergast. Bin1 ablation increases susceptibility to cancer during aging, particularly lung cancer. Cancer Res 2007; 67:7605-12; PMID:17699764; http://dx.doi.org/10.1158/0008-5472.CAN-07-1100
    • (2007) Cancer Res , vol.67 , pp. 7605-7612
    • Chang, M.Y.1    Boulden, J.2    Katz, J.B.3    Wang, L.4    Meyer, T.J.5    Soler, A.P.6    Muller, A.J.7    Prendergast, G.C.8
  • 72
    • 33846436452 scopus 로고    scopus 로고
    • Bin1 ablation in mammary gland delays tissue remodeling and drives cancer progression
    • 17210688
    • M.Y.Chang, J.Boulden, E.Sutanto-Ward, J.B.Duhadaway, A.P.Soler, A.J.Muller, G.C.Prendergast. Bin1 ablation in mammary gland delays tissue remodeling and drives cancer progression. Cancer Res 2007; 67:100-07; PMID:17210688; http://dx.doi.org/10.1158/0008-5472.CAN-06-2742
    • (2007) Cancer Res , vol.67 , pp. 100-107
    • Chang, M.Y.1    Boulden, J.2    Sutanto-Ward, E.3    Duhadaway, J.B.4    Soler, A.P.5    Muller, A.J.6    Prendergast, G.C.7
  • 73
    • 0033987640 scopus 로고    scopus 로고
    • Losses of the tumor suppressor BIN1 in breast carcinoma are frequent and reflect deficits in programmed cell death capacity
    • 10652430, <376::AID-IJC14>3.0.CO;2-1
    • K.Ge, J.Duhadaway, D.Sakamuro, R.Wechsler-Reya, C.Reynolds, G.C.Prendergast. Losses of the tumor suppressor BIN1 in breast carcinoma are frequent and reflect deficits in programmed cell death capacity. Int J Cancer 2000; 85:376-83; PMID:10652430; http://dx.doi.org/10.1002/(SICI)1097-0215(20000201)85:3<376::AID-IJC14>3.0.CO;2-1
    • (2000) Int J Cancer , vol.85 , pp. 376-383
    • Ge, K.1    Duhadaway, J.2    Sakamuro, D.3    Wechsler-Reya, R.4    Reynolds, C.5    Prendergast, G.C.6
  • 74
    • 84892157282 scopus 로고    scopus 로고
    • Long-lasting disease stabilization in the absence of toxicity in metastatic lung cancer patients vaccinated with an epitope derived from indoleamine 2,3 dioxygenase
    • 24218513
    • T.Z.Iversen, L.Engell-Noerregaard, E.Ellebaek, R.Andersen, S.K.Larsen, J.Bjoern, C.Zeyher, C.Gouttefangeas, B.M.Thomsen, B.Holm Long-lasting disease stabilization in the absence of toxicity in metastatic lung cancer patients vaccinated with an epitope derived from indoleamine 2,3 dioxygenase. Clin Cancer Res 2014; 20:221-32; PMID:24218513; http://dx.doi.org/10.1158/1078-0432.CCR-13-1560
    • (2014) Clin Cancer Res , vol.20 , pp. 221-232
    • Iversen, T.Z.1    Engell-Noerregaard, L.2    Ellebaek, E.3    Andersen, R.4    Larsen, S.K.5    Bjoern, J.6    Zeyher, C.7    Gouttefangeas, C.8    Thomsen, B.M.9    Holm, B.10
  • 75
    • 84870426822 scopus 로고    scopus 로고
    • Pharmacodynamic assessment of INCB024360, an inhibitor of indoleamine 2,3-dioxygenase 1 (IDO1), in advanced cancer patients
    • R.C.Newton, P.A.Scherle, K.Bowman, X.Liu, Beatty, P.J.G.T.B.J.S.R.L.L.O'DwyerPJ, Gajewski T, Bowman J, Schaub R, Leopold L. Pharmacodynamic assessment of INCB024360, an inhibitor of indoleamine 2,3-dioxygenase 1 (IDO1), in advanced cancer patients. J Clin Oncol 2012; 30:abstr 2500
    • (2012) J Clin Oncol , vol.30 , pp. 2500
    • Newton, R.C.1    Scherle, P.A.2    Bowman, K.3    LiuBeatty, X.4    O’Dwyer, P.J.G.T.B.J.S.R.L.L.5
  • 79
    • 37249048334 scopus 로고    scopus 로고
    • Expression of indoleamine 2,3-dioxygenase in tumor endothelial cells correlates with long-term survival of patients with renal cell carcinoma
    • 18056175
    • R.Riesenberg, C.Weiler, O.Spring, M.Eder, A.Buchner, T.Popp, M.Castro, R.Kammerer, O.Takikawa, R.A.Hatz Expression of indoleamine 2,3-dioxygenase in tumor endothelial cells correlates with long-term survival of patients with renal cell carcinoma. Clin Cancer Res 2007; 13:6993-7002; PMID:18056175; http://dx.doi.org/10.1158/1078-0432.CCR-07-0942
    • (2007) Clin Cancer Res , vol.13 , pp. 6993-7002
    • Riesenberg, R.1    Weiler, C.2    Spring, O.3    Eder, M.4    Buchner, A.5    Popp, T.6    Castro, M.7    Kammerer, R.8    Takikawa, O.9    Hatz, R.A.10
  • 80
    • 84886945280 scopus 로고    scopus 로고
    • Indoleamine 2,3-dioxygenase activity and clinical outcome following induction chemotherapy and concurrent chemoradiation in Stage III non-small cell lung cancer
    • 23802083
    • B.C.Creelan, S.Antonia, G.Bepler, T.J.Garrett, G.R.Simon, H.H.Soliman. Indoleamine 2,3-dioxygenase activity and clinical outcome following induction chemotherapy and concurrent chemoradiation in Stage III non-small cell lung cancer. Oncoimmunology 2013; 2:e23428; PMID:23802083; http://dx.doi.org/10.4161/onci.23428
    • (2013) Oncoimmunology , vol.2 , pp. 23428
    • Creelan, B.C.1    Antonia, S.2    Bepler, G.3    Garrett, T.J.4    Simon, G.R.5    Soliman, H.H.6
  • 81
    • 84875881003 scopus 로고    scopus 로고
    • Metabolites of tryptophan catabolism are elevated in sera of patients with myelodysplastic syndromes and inhibit hematopoietic progenitor amplification
    • 23453284
    • C.Berthon, M.Fontenay, S.Corm, I.Briche, D.Allorge, B.Hennart, M.Lhermitte, B.Quesnel. Metabolites of tryptophan catabolism are elevated in sera of patients with myelodysplastic syndromes and inhibit hematopoietic progenitor amplification. Leuk Res 2013; 37:573-79; PMID:23453284; http://dx.doi.org/10.1016/j.leukres.2013.02.001
    • (2013) Leuk Res , vol.37 , pp. 573-579
    • Berthon, C.1    Fontenay, M.2    Corm, S.3    Briche, I.4    Allorge, D.5    Hennart, B.6    Lhermitte, M.7    Quesnel, B.8
  • 82
    • 77949456437 scopus 로고    scopus 로고
    • Serum concentration of L-kynurenine predicts the clinical outcome of patients with diffuse large B-cell lymphoma treated with R-CHOP
    • 19995374
    • T.Yoshikawa, T.Hara, H.Tsurumi, N.Goto, M.Hoshi, J.Kitagawa, N.Kanemura, S.Kasahara, H.Ito, M.Takemura Serum concentration of L-kynurenine predicts the clinical outcome of patients with diffuse large B-cell lymphoma treated with R-CHOP. Eur J Haematol 2010; 84:304-09; PMID:19995374; http://dx.doi.org/10.1111/j.1600-0609.2009.01393.x
    • (2010) Eur J Haematol , vol.84 , pp. 304-309
    • Yoshikawa, T.1    Hara, T.2    Tsurumi, H.3    Goto, N.4    Hoshi, M.5    Kitagawa, J.6    Kanemura, N.7    Kasahara, S.8    Ito, H.9    Takemura, M.10
  • 83
    • 1542407385 scopus 로고    scopus 로고
    • Immunoactivative role of indoleamine 2,3-dioxygenase in human hepatocellular carcinoma
    • 14748880
    • T.Ishio, S.Goto, K.Tahara, S.Tone, K.Kawano, S.Kitano. Immunoactivative role of indoleamine 2,3-dioxygenase in human hepatocellular carcinoma. J Gastroenterol Hepatol 2004; 19:319-26; PMID:14748880; http://dx.doi.org/10.1111/j.1440-1746.2003.03259.x
    • (2004) J Gastroenterol Hepatol , vol.19 , pp. 319-326
    • Ishio, T.1    Goto, S.2    Tahara, K.3    Tone, S.4    Kawano, K.5    Kitano, S.6
  • 84
    • 27144552597 scopus 로고    scopus 로고
    • + dendritic cells to acquire potent indoleamine 2,3-dioxygenase-dependent T cell regulatory functions via IFN Type 1 signaling
    • 16237046
    • + dendritic cells to acquire potent indoleamine 2,3-dioxygenase-dependent T cell regulatory functions via IFN Type 1 signaling. J Immunol 2005; 175:5601-05; PMID:16237046; http://dx.doi.org/10.4049/jimmunol.175.9.5601
    • (2005) J Immunol , vol.175 , pp. 5601-5605
    • Mellor, A.L.1    Baban, B.2    Chandler, P.R.3    Manlapat, A.4    Kahler, D.J.5    Munn, D.H.6
  • 86
    • 30944437887 scopus 로고    scopus 로고
    • Toll-like receptor 9-mediated induction of the immunosuppressive pathway of tryptophan catabolism
    • 16358364
    • F.Fallarino, P.Puccetti. Toll-like receptor 9-mediated induction of the immunosuppressive pathway of tryptophan catabolism. Eur J Immunol 2006; 36:8-11; PMID:16358364; http://dx.doi.org/10.1002/eji.200535667
    • (2006) Eur J Immunol , vol.36 , pp. 8-11
    • Fallarino, F.1    Puccetti, P.2
  • 90
    • 0023926018 scopus 로고
    • Mechanism of interferon-gamma action. Characterization of indoleamine 2,3-dioxygenase in cultured human cells induced by interferon-gamma and evaluation of the enzyme-mediated tryptophan degradation in its anticellular activity
    • 3123485
    • O.Takikawa, T.Kuroiwa, F.Yamazaki, R.Kido. Mechanism of interferon-gamma action. Characterization of indoleamine 2,3-dioxygenase in cultured human cells induced by interferon-gamma and evaluation of the enzyme-mediated tryptophan degradation in its anticellular activity. J Biol Chem 1988; 263:2041-48; PMID:3123485
    • (1988) J Biol Chem , vol.263 , pp. 2041-2048
    • Takikawa, O.1    Kuroiwa, T.2    Yamazaki, F.3    Kido, R.4
  • 91
    • 0040858936 scopus 로고
    • Induction of indoleamine 2,3-dioxygenase: a mechanism of the antitumor activity of interferon gamma
    • 3124115
    • Y.Ozaki, M.P.Edelstein, D.S.Duch. Induction of indoleamine 2,3-dioxygenase: a mechanism of the antitumor activity of interferon gamma. Proc Natl Acad Sci USA 1988; 85:1242-46; PMID:3124115; http://dx.doi.org/10.1073/pnas.85.4.1242
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 1242-1246
    • Ozaki, Y.1    Edelstein, M.P.2    Duch, D.S.3
  • 92
    • 0023770026 scopus 로고
    • Tryptophan degradation in transplanted tumor cells undergoing rejection
    • 3262668
    • R.Yoshida, S.W.Park, H.Yasui, O.Takikawa. Tryptophan degradation in transplanted tumor cells undergoing rejection. J Immunol 1988; 141:2819-23; PMID:3262668
    • (1988) J Immunol , vol.141 , pp. 2819-2823
    • Yoshida, R.1    Park, S.W.2    Yasui, H.3    Takikawa, O.4
  • 93
    • 77952231121 scopus 로고    scopus 로고
    • Induction of lymphoidlike stroma and immune escape by tumors that express the chemokine CCL21
    • 20339029
    • J.D.Shields, I.C.Kourtis, A.A.Tomei, J.M.Roberts, M.A.Swartz. Induction of lymphoidlike stroma and immune escape by tumors that express the chemokine CCL21. Science 2010; 328:749-52; PMID:20339029; http://dx.doi.org/10.1126/science.1185837
    • (2010) Science , vol.328 , pp. 749-752
    • Shields, J.D.1    Kourtis, I.C.2    Tomei, A.A.3    Roberts, J.M.4    Swartz, M.A.5
  • 95
    • 65249155463 scopus 로고    scopus 로고
    • Transcription factor Foxo3 controls the magnitude of T cell immune responses by modulating the function of dendritic cells
    • 19363483
    • A.S.Dejean, D.R.Beisner, I.L.Ch'en, Y.M.Kerdiles, A.Babour, K.C.Arden, D.H.Castrillon, R.A.DePinho, S.M.Hedrick. Transcription factor Foxo3 controls the magnitude of T cell immune responses by modulating the function of dendritic cells. Nat Immunol 2009; 10:504-13; PMID:19363483; http://dx.doi.org/10.1038/ni.1729
    • (2009) Nat Immunol , vol.10 , pp. 504-513
    • Dejean, A.S.1    Beisner, D.R.2    Ch'en, I.L.3    Kerdiles, Y.M.4    Babour, A.5    Arden, K.C.6    Castrillon, D.H.7    DePinho, R.A.8    Hedrick, S.M.9
  • 96
    • 84906517328 scopus 로고    scopus 로고
    • PD-L1 expression and tumor-infiltrating lymphocytes: revisiting the antitumor immune response potential in breast cancer
    • 25083339
    • K.A.Schalper. PD-L1 expression and tumor-infiltrating lymphocytes: revisiting the antitumor immune response potential in breast cancer. Oncoimmunology 2014; 3:e29288; PMID:25083339; http://dx.doi.org/10.4161/onci.29288
    • (2014) Oncoimmunology , vol.3 , pp. 29288
    • Schalper, K.A.1
  • 97
    • 84904045263 scopus 로고    scopus 로고
    • A novel combinatorial cancer immunotherapy: poly-IC and blockade of the PD-1/PD-L1 pathway
    • 25050210
    • T.Nagato, E.Celis. A novel combinatorial cancer immunotherapy: poly-IC and blockade of the PD-1/PD-L1 pathway. Oncoimmunology 2014; 3:e28440; PMID:25050210; http://dx.doi.org/10.4161/onci.28440
    • (2014) Oncoimmunology , vol.3 , pp. 28440
    • Nagato, T.1    Celis, E.2
  • 98
    • 84904061991 scopus 로고    scopus 로고
    • Durable therapeutic efficacy utilizing combinatorial blockade against IDO, CTLA-4 and PD-L1 in mice with brain tumors
    • 24691018
    • D.A.Wainwright, A.L.Chang, M.Dey, I.V.Balyasnikova, C.Kim, A.L.Tobias, Y.Cheng, J.Kim, L.Zhang, J.Qiao Durable therapeutic efficacy utilizing combinatorial blockade against IDO, CTLA-4 and PD-L1 in mice with brain tumors. Clin Cancer Res 2014; 20:5290-301; PMID:24691018; http://dx.doi.org/10.1158/1078-0432.CCR-14-0514
    • (2014) Clin Cancer Res , vol.20 , pp. 5290-5301
    • Wainwright, D.A.1    Chang, A.L.2    Dey, M.3    Balyasnikova, I.V.4    Kim, C.5    Tobias, A.L.6    Cheng, Y.7    Kim, J.8    Zhang, L.9    Qiao, J.10
  • 99
    • 82155168544 scopus 로고    scopus 로고
    • A prospective phase II trial exploring the association between tumor microenvironment biomarkers and clinical activity of ipilimumab in advanced melanoma
    • 22123319
    • O.Hamid, H.Schmidt, A.Nissan, L.Ridolfi, S.Aamdal, J.Hansson, M.Guida, D.M.Hyams, H.Gómez, L.Bastholt A prospective phase II trial exploring the association between tumor microenvironment biomarkers and clinical activity of ipilimumab in advanced melanoma. J Transl Med 2011; 9:204; PMID:22123319; http://dx.doi.org/10.1186/1479-5876-9-204
    • (2011) J Transl Med , vol.9 , pp. 204
    • Hamid, O.1    Schmidt, H.2    Nissan, A.3    Ridolfi, L.4    Aamdal, S.5    Hansson, J.6    Guida, M.7    Hyams, D.M.8    Gómez, H.9    Bastholt, L.10
  • 104
    • 84880879533 scopus 로고    scopus 로고
    • Tumor growth control with IDO-silencing Salmonella-letter
    • 23832662
    • R.M.Hoffman. Tumor growth control with IDO-silencing Salmonella-letter. Cancer Res 2013; 73:4591; PMID:23832662; http://dx.doi.org/10.1158/0008-5472.CAN-12-4719
    • (2013) Cancer Res , vol.73 , pp. 4591
    • Hoffman, R.M.1
  • 105
    • 84886943979 scopus 로고    scopus 로고
    • A road less traveled paved by IDO silencing: harnessing the antitumor activity of neutrophils
    • 23802075
    • E.R.Manuel, D.J.Diamond. A road less traveled paved by IDO silencing: harnessing the antitumor activity of neutrophils. Oncoimmunology 2013; 2:e23322; PMID:23802075; http://dx.doi.org/10.4161/onci.23322
    • (2013) Oncoimmunology , vol.2 , pp. 23322
    • Manuel, E.R.1    Diamond, D.J.2
  • 106
    • 84871390241 scopus 로고    scopus 로고
    • Silencing IDO in dendritic cells: a novel approach to enhance cancer immunotherapy in a murine breast cancer model
    • 22870862
    • X.Zheng, J.Koropatnick, D.Chen, T.Velenosi, H.Ling, X.Zhang, N.Jiang, B.Navarro, T.E.Ichim, B.Urquhart Silencing IDO in dendritic cells: a novel approach to enhance cancer immunotherapy in a murine breast cancer model. Int J Cancer 2013; 132:967-77; PMID:22870862; http://dx.doi.org/10.1002/ijc.27710
    • (2013) Int J Cancer , vol.132 , pp. 967-977
    • Zheng, X.1    Koropatnick, J.2    Chen, D.3    Velenosi, T.4    Ling, H.5    Zhang, X.6    Jiang, N.7    Navarro, B.8    Ichim, T.E.9    Urquhart, B.10
  • 107
    • 84871232968 scopus 로고    scopus 로고
    • Systemic delivery of Salmonella typhimurium transformed with IDO shRNA enhances intratumoral vector colonization and suppresses tumor growth
    • 23090116
    • C.A.Blache, E.R.Manuel, T.I.Kaltcheva, A.N.Wong, J.D.Ellenhorn, B.R.Blazar, D.J.Diamond. Systemic delivery of Salmonella typhimurium transformed with IDO shRNA enhances intratumoral vector colonization and suppresses tumor growth. Cancer Res 2012; 72:6447-56; PMID:23090116; http://dx.doi.org/10.1158/0008-5472.CAN-12-0193
    • (2012) Cancer Res , vol.72 , pp. 6447-6456
    • Blache, C.A.1    Manuel, E.R.2    Kaltcheva, T.I.3    Wong, A.N.4    Ellenhorn, J.D.5    Blazar, B.R.6    Diamond, D.J.7
  • 108
    • 84863354166 scopus 로고    scopus 로고
    • Indoleamine-2,3-dioxygenase, an immunosuppressive enzyme that inhibits natural killer cell function, as a useful target for ovarian cancer therapy
    • 22179492
    • D.Wang, Y.Saga, H.Mizukami, N.Sato, H.Nonaka, H.Fujiwara, Y.Takei, S.Machida, O.Takikawa, K.Ozawa Indoleamine-2,3-dioxygenase, an immunosuppressive enzyme that inhibits natural killer cell function, as a useful target for ovarian cancer therapy. Int J Oncol 2012; 40:929-34; PMID:22179492
    • (2012) Int J Oncol , vol.40 , pp. 929-934
    • Wang, D.1    Saga, Y.2    Mizukami, H.3    Sato, N.4    Nonaka, H.5    Fujiwara, H.6    Takei, Y.7    Machida, S.8    Takikawa, O.9    Ozawa, K.10
  • 109
    • 33846689594 scopus 로고    scopus 로고
    • Inhibition of indoleamine 2,3-dioxygenase in dendritic cells by stereoisomers of 1-methyl-tryptophan correlates with antitumor responses
    • 17234791
    • D.Y.Hou, A.J.Muller, M.D.Sharma, J.DuHadaway, T.Banerjee, M.Johnson, A.L.Mellor, G.C.Prendergast, D.H.Munn. Inhibition of indoleamine 2,3-dioxygenase in dendritic cells by stereoisomers of 1-methyl-tryptophan correlates with antitumor responses. Cancer Res 2007; 67:792-801; PMID:17234791; http://dx.doi.org/10.1158/0008-5472.CAN-06-2925
    • (2007) Cancer Res , vol.67 , pp. 792-801
    • Hou, D.Y.1    Muller, A.J.2    Sharma, M.D.3    DuHadaway, J.4    Banerjee, T.5    Johnson, M.6    Mellor, A.L.7    Prendergast, G.C.8    Munn, D.H.9
  • 110
    • 84931028590 scopus 로고    scopus 로고
    • NLG919, a novel indoleamine-2,3-dioxygenase (IDO)-pathway inhibitor drug candidate for cancer therapy
    • M.R.Mautino, F.A.Jaipuri, J.Waldo, S.Kumar, J.Adams, C.M.-F.A.M.D.V.N.N.L.C.J.Van AllenC, Marcinowicz-Flick A, Munn D, Vahanian NN, Link CJ. NLG919, a novel indoleamine-2,3-dioxygenase (IDO)-pathway inhibitor drug candidate for cancer therapy. Cancer Res 2013; 73:491; http://dx.doi.org/10.1158/1538-7445.AM2013-491
    • (2013) Cancer Res , vol.73 , pp. 491
    • Mautino, M.R.1    Jaipuri, F.A.2    Waldo, J.3    Kumar, S.4    Adams, J.5    Van Allen, C.M.-F.A.6
  • 111
    • 77951718214 scopus 로고    scopus 로고
    • Selective inhibition of IDO1 effectively regulates mediators of antitumor immunity
    • 20197554
    • X.Liu, N.Shin, H.K.Koblish, G.Yang, Q.Wang, K.Wang, L.Leffet, M.J.Hansbury, B.Thomas, M.Rupar Selective inhibition of IDO1 effectively regulates mediators of antitumor immunity. Blood 2010; 115:3520-30; PMID:20197554; http://dx.doi.org/10.1182/blood-2009-09-246124
    • (2010) Blood , vol.115 , pp. 3520-3530
    • Liu, X.1    Shin, N.2    Koblish, H.K.3    Yang, G.4    Wang, Q.5    Wang, K.6    Leffet, L.7    Hansbury, M.J.8    Thomas, B.9    Rupar, M.10
  • 112
    • 76649088968 scopus 로고    scopus 로고
    • Hydroxyamidine inhibitors of indoleamine-2,3-dioxygenase potently suppress systemic tryptophan catabolism and the growth of IDO-expressing tumors
    • 20124451
    • H.K.Koblish, M.J.Hansbury, K.J.Bowman, G.Yang, C.L.Neilan, P.J.Haley, T.C.Burn, P.Waeltz, R.B.Sparks, E.W.Yue Hydroxyamidine inhibitors of indoleamine-2,3-dioxygenase potently suppress systemic tryptophan catabolism and the growth of IDO-expressing tumors. Mol Cancer Ther 2010; 9:489-98; PMID:20124451; http://dx.doi.org/10.1158/1535-7163.MCT-09-0628
    • (2010) Mol Cancer Ther , vol.9 , pp. 489-498
    • Koblish, H.K.1    Hansbury, M.J.2    Bowman, K.J.3    Yang, G.4    Neilan, C.L.5    Haley, P.J.6    Burn, T.C.7    Waeltz, P.8    Sparks, R.B.9    Yue, E.W.10
  • 113
    • 84977071799 scopus 로고    scopus 로고
    • The indoleamine 2,3-dioxygenase pathway controls complement-dependent enhancement of chemo-radiation therapy against murine glioblastoma
    • 25054064
    • M.Li, A.R.Bolduc, M.N.Hoda, D.N.Gamble, S.B.Dolisca, A.K.Bolduc, K.Hoang, C.Ashley, D.McCall, A.M.Rojiani The indoleamine 2,3-dioxygenase pathway controls complement-dependent enhancement of chemo-radiation therapy against murine glioblastoma. J Immunother Cancer 2014; 2:21; PMID:25054064; http://dx.doi.org/10.1186/2051-1426-2-21
    • (2014) J Immunother Cancer , vol.2 , pp. 21
    • Li, M.1    Bolduc, A.R.2    Hoda, M.N.3    Gamble, D.N.4    Dolisca, S.B.5    Bolduc, A.K.6    Hoang, K.7    Ashley, C.8    McCall, D.9    Rojiani, A.M.10
  • 114
    • 77952051391 scopus 로고    scopus 로고
    • Overcoming tumor antigen anergy in human malignancies using the novel indoleamine 2,3-dioxygenase (IDO) enzyme inhibitor, 1-methyl-D-tryptophan (1MT)
    • H.H.Soliman, S.J.Antonia, D.Sullivan, N.Vanahanian, C.J.Link. Overcoming tumor antigen anergy in human malignancies using the novel indoleamine 2,3-dioxygenase (IDO) enzyme inhibitor, 1-methyl-D-tryptophan (1MT). J Clin Oncol 2009; 27:abstr 3004
    • (2009) J Clin Oncol , vol.27 , pp. 3004
    • Soliman, H.H.1    Antonia, S.J.2    Sullivan, D.3    Vanahanian, N.4    Link, C.J.5
  • 115
    • 84897436132 scopus 로고    scopus 로고
    • A phase I study of indoximod in combination with docetaxel in metastatic solid tumors
    • E.Jackson, E.C.Dees, J.S.Kauh, R.D.Harvey, A.Neuger, R.A.S.J.M.S.E.I.-K.R.H.H.S.LushR, Antonia SJ, Minton SE, Ismail-Khan R, Han HS A phase I study of indoximod in combination with docetaxel in metastatic solid tumors. J Clin Oncol 2013; 31:abstr 3026.
    • (2013) J Clin Oncol , vol.31 , pp. 3026
    • Jackson, E.1    Dees, E.C.2    Kauh, J.S.3    Harvey, R.D.4    Neuger, A.5    Lush, R.A.6
  • 116
  • 117
    • 84918817080 scopus 로고    scopus 로고
    • A phase 2 study of docetaxel in combination with indoximod in metastatic breast cancer
    • H.H.Soliman, S.E.Minton, R.Ismail-Khan, H.S.Han, N.N.Vahanian, W.J.K.E.L.C.J.S.D.A.S.J.RamseyWJ, Kennedy E, Link CJ, Sullivan D, Antonia SJ. A phase 2 study of docetaxel in combination with indoximod in metastatic breast cancer. J Clin Oncol 2014; 32:abstr TPS3124.
    • (2014) J Clin Oncol , vol.32 , pp. 3124
    • Soliman, H.H.1    Minton, S.E.2    Ismail-Khan, R.3    Han, H.S.4    Vahanian, N.N.5    Ramsey, W.J.K.E.6
  • 118
    • 84918768887 scopus 로고    scopus 로고
    • A phase I/II study of the combination of indoximod and temozolomide for adult patients with temozolomide-refractory primary malignant brain tumors
    • Y.Zakharia, T.S.Johnson, H.Colman, N.N.Vahanian, C.J.Link, E.S.R.F.K.F.M.V.J.M.D.KennedyE, Sadek RF, Kong FM, Vender J, Munn D A phase I/II study of the combination of indoximod and temozolomide for adult patients with temozolomide-refractory primary malignant brain tumors. J Clin Oncol 2014; 32:abstr TPS2107.
    • (2014) J Clin Oncol , vol.32 , pp. 2107
    • Zakharia, Y.1    Johnson, T.S.2    Colman, H.3    Vahanian, N.N.4    Link, C.J.5    Kennedy, E.S.6
  • 119
    • 84895900553 scopus 로고    scopus 로고
    • Phase I study of the safety, pharmacokinetics (PK)and pharmacodynamics (PD) of the oral inhibitor of indoleamine 2,3-dioxygenase (IDO1) INCB024360 in patients (pts) with advanced malignancies
    • G.L.Beatty, P.J.O'Dwyer, J.Clark, J.G.Shi, R.C.Newton, R.M.J.L.L.G.T.SchaubR, Maleski J, Leopold L, Gajewski T. Phase I study of the safety, pharmacokinetics (PK)and pharmacodynamics (PD) of the oral inhibitor of indoleamine 2,3-dioxygenase (IDO1) INCB024360 in patients (pts) with advanced malignancies. J Clin Oncol 2013; 31:abstr 3025.
    • (2013) J Clin Oncol , vol.31 , pp. 3025
    • Beatty, G.L.1    O'Dwyer, P.J.2    Clark, J.3    Shi, J.G.4    Newton, R.C.5    Schaub, R.M.J.L.L.G.T.6
  • 120
    • 84920081022 scopus 로고    scopus 로고
    • Preliminary results from a phase 1/2 study of INCB024360 combined with ipilimumab (ipi) in patients (pts) with melanoma
    • G.T.Gibney, O.Hamid, T.C.Gangadhar, J.Lutzky, A.J.Olszanski, T.C.B.B.P.D.Z.Y.N.R.C.GajewskiT, Chmielowski B, Boasberg PD, Zhao Y, Newton RC Preliminary results from a phase 1/2 study of INCB024360 combined with ipilimumab (ipi) in patients (pts) with melanoma. J Clin Oncol 2014; 32:abstr 3010.
    • (2014) J Clin Oncol , vol.32 , pp. 3010
    • Gibney, G.T.1    Hamid, O.2    Gangadhar, T.C.3    Lutzky, J.4    Olszanski, A.J.5    Gajewski, T.6
  • 121
    • 42949141286 scopus 로고    scopus 로고
    • A key in vivo antitumor mechanism of action of natural product-based brassinins is inhibition of indoleamine 2,3-dioxygenase
    • 18026137
    • T.Banerjee, J.B.Duhadaway, P.Gaspari, E.Sutanto-Ward, D.H.Munn, A.L.Mellor, W.P.Malachowski, G.C.Prendergast, A.J.Muller. A key in vivo antitumor mechanism of action of natural product-based brassinins is inhibition of indoleamine 2,3-dioxygenase. Oncogene 2008; 27:2851-57; PMID:18026137; http://dx.doi.org/10.1038/sj.onc.1210939
    • (2008) Oncogene , vol.27 , pp. 2851-2857
    • Banerjee, T.1    Duhadaway, J.B.2    Gaspari, P.3    Sutanto-Ward, E.4    Munn, D.H.5    Mellor, A.L.6    Malachowski, W.P.7    Prendergast, G.C.8    Muller, A.J.9
  • 123
    • 42949087977 scopus 로고    scopus 로고
    • Synthesis of indoleamine 2,3-dioxygenase inhibitory analogues of the sponge alkaloid exiguamine A
    • 18393489
    • G.Carr, M.K.Chung, A.G.Mauk, R.J.Andersen. Synthesis of indoleamine 2,3-dioxygenase inhibitory analogues of the sponge alkaloid exiguamine A. J Med Chem 2008; 51:2634-37; PMID:18393489; http://dx.doi.org/10.1021/jm800143h
    • (2008) J Med Chem , vol.51 , pp. 2634-2637
    • Carr, G.1    Chung, M.K.2    Mauk, A.G.3    Andersen, R.J.4
  • 124
    • 33845591355 scopus 로고    scopus 로고
    • Exiguamine A, an indoleamine-2,3-dioxygenase (IDO) inhibitor isolated from the marine sponge Neopetrosia exigua
    • 17165752
    • H.C.Brastianos, E.Vottero, B.O.Patrick, R.Van Soest, T.Matainaho, A.G.Mauk, R.J.Andersen. Exiguamine A, an indoleamine-2,3-dioxygenase (IDO) inhibitor isolated from the marine sponge Neopetrosia exigua. J Am Chem Soc 2006; 128:16046-47; PMID:17165752; http://dx.doi.org/10.1021/ja067211+
    • (2006) J Am Chem Soc , vol.128 , pp. 16046-16047
    • Brastianos, H.C.1    Vottero, E.2    Patrick, B.O.3    Van Soest, R.4    Matainaho, T.5    Mauk, A.G.6    Andersen, R.J.7
  • 126
    • 33845432326 scopus 로고    scopus 로고
    • Indoleamine 2,3-dioxygenase inhibitors from the Northeastern Pacific Marine Hydroid Garveia annulata
    • 17067170
    • A.Pereira, E.Vottero, M.Roberge, A.G.Mauk, R.J.Andersen. Indoleamine 2,3-dioxygenase inhibitors from the Northeastern Pacific Marine Hydroid Garveia annulata. J Nat Prod 2006; 69:1496-99; PMID:17067170; http://dx.doi.org/10.1021/np060111x
    • (2006) J Nat Prod , vol.69 , pp. 1496-1499
    • Pereira, A.1    Vottero, E.2    Roberge, M.3    Mauk, A.G.4    Andersen, R.J.5
  • 128
    • 79951671971 scopus 로고    scopus 로고
    • Docetaxel and epirubicin compared with docetaxel and prednisone in advanced castrate-resistant prostate cancer: a randomised phase II study
    • 21285986
    • R.Petrioli, A.Pascucci, R.Conca, G.Chiriaco, E.Francini, G.Bargagli, A.I.Fiaschi, A.Manganelli, G.De Rubertis, G.Barbanti Docetaxel and epirubicin compared with docetaxel and prednisone in advanced castrate-resistant prostate cancer: a randomised phase II study. Br J Cancer 2011; 104:613-19; PMID:21285986; http://dx.doi.org/10.1038/bjc.2011.5
    • (2011) Br J Cancer , vol.104 , pp. 613-619
    • Petrioli, R.1    Pascucci, A.2    Conca, R.3    Chiriaco, G.4    Francini, E.5    Bargagli, G.6    Fiaschi, A.I.7    Manganelli, A.8    De Rubertis, G.9    Barbanti, G.10
  • 139
    • 84883461036 scopus 로고    scopus 로고
    • Victories and deceptions in tumor immunology: Stimuvax®
    • 23483762
    • G.Kroemer, L.Zitvogel, L.Galluzzi. Victories and deceptions in tumor immunology: Stimuvax®. Oncoimmunology 2013; 2:e23687; PMID:23483762; http://dx.doi.org/10.4161/onci.23687
    • (2013) Oncoimmunology , vol.2 , pp. 23687
    • Kroemer, G.1    Zitvogel, L.2    Galluzzi, L.3
  • 140
    • 84877896663 scopus 로고    scopus 로고
    • Targeting PD-1/PD-L1 interactions for cancer immunotherapy
    • 23243584
    • L.Zitvogel, G.Kroemer. Targeting PD-1/PD-L1 interactions for cancer immunotherapy. Oncoimmunology 2012; 1:1223-25; PMID:23243584; http://dx.doi.org/10.4161/onci.21335
    • (2012) Oncoimmunology , vol.1 , pp. 1223-1225
    • Zitvogel, L.1    Kroemer, G.2
  • 141
    • 84899075616 scopus 로고    scopus 로고
    • Two is better than one: complementing oncolytic virotherapy with gemcitabine to potentiate antitumor immune responses
    • 24804161
    • S.A.Gujar, D.Clements, P.W.Lee. Two is better than one: complementing oncolytic virotherapy with gemcitabine to potentiate antitumor immune responses. Oncoimmunology 2014; 3:e27622; PMID:24804161; http://dx.doi.org/10.4161/onci.27622
    • (2014) Oncoimmunology , vol.3 , pp. 27622
    • Gujar, S.A.1    Clements, D.2    Lee, P.W.3
  • 143
    • 84857789296 scopus 로고    scopus 로고
    • The secret ally: immunostimulation by anticancer drugs
    • 22301798
    • L.Galluzzi, L.Senovilla, L.Zitvogel, G.Kroemer. The secret ally: immunostimulation by anticancer drugs. Nat Rev Drug Discov 2012; 11:215-33; PMID:22301798; http://dx.doi.org/10.1038/nrd3626
    • (2012) Nat Rev Drug Discov , vol.11 , pp. 215-233
    • Galluzzi, L.1    Senovilla, L.2    Zitvogel, L.3    Kroemer, G.4
  • 144
    • 84880747672 scopus 로고    scopus 로고
    • Mechanism of action of conventional and targeted anticancer therapies: reinstating immunosurveillance
    • 23890065
    • L.Zitvogel, L.Galluzzi, M.J.Smyth, G.Kroemer. Mechanism of action of conventional and targeted anticancer therapies: reinstating immunosurveillance. Immunity 2013; 39:74-88; PMID:23890065; http://dx.doi.org/10.1016/j.immuni.2013.06.014
    • (2013) Immunity , vol.39 , pp. 74-88
    • Zitvogel, L.1    Galluzzi, L.2    Smyth, M.J.3    Kroemer, G.4
  • 145
    • 84877805593 scopus 로고    scopus 로고
    • Phase I study of the CD40 agonist antibody CP-870,893 combined with carboplatin and paclitaxel in patients with advanced solid tumors
    • 23483678
    • R.H.Vonderheide, J.M.Burg, R.Mick, J.A.Trosko, D.Li, M.N.Shaik, A.W.Tolcher, O.Hamid. Phase I study of the CD40 agonist antibody CP-870,893 combined with carboplatin and paclitaxel in patients with advanced solid tumors. Oncoimmunology 2013; 2:e23033; PMID:23483678; http://dx.doi.org/10.4161/onci.23033
    • (2013) Oncoimmunology , vol.2 , pp. 23033
    • Vonderheide, R.H.1    Burg, J.M.2    Mick, R.3    Trosko, J.A.4    Li, D.5    Shaik, M.N.6    Tolcher, A.W.7    Hamid, O.8
  • 147
    • 79960706708 scopus 로고    scopus 로고
    • Randomized multicenter trial of the effects of melanoma-associated helper peptides and cyclophosphamide on the immunogenicity of a multipeptide melanoma vaccine
    • 21690475
    • C.L.Slingluff, Jr., G.R.Petroni, K.A.Chianese-Bullock, M.E.Smolkin, M.I.Ross, N.B.Haas, M.von Mehren, W.W.Grosh. Randomized multicenter trial of the effects of melanoma-associated helper peptides and cyclophosphamide on the immunogenicity of a multipeptide melanoma vaccine. J Clin Oncol 2011; 29:2924-32; PMID:21690475; http://dx.doi.org/10.1200/JCO.2010.33.8053
    • (2011) J Clin Oncol , vol.29 , pp. 2924-2932
    • Slingluff, C.L.1    Petroni, G.R.2    Chianese-Bullock, K.A.3    Smolkin, M.E.4    Ross, M.I.5    Haas, N.B.6    von Mehren, M.7    Grosh, W.W.8
  • 152
    • 84899073975 scopus 로고    scopus 로고
    • Induction of antigen-specific immunity with a vaccine targeting NY-ESO-1 to the dendritic cell receptor DEC-205
    • 24739759
    • M.V.Dhodapkar, M.Sznol, B.Zhao, D.Wang, R.D.Carvajal, M.L.Keohan Induction of antigen-specific immunity with a vaccine targeting NY-ESO-1 to the dendritic cell receptor DEC-205. Sci Transl Med 2014; 6:232ra51; PMID:24739759; http://dx.doi.org/10.1126/scitranslmed.3008068
    • (2014) Sci Transl Med , vol.6 , pp. 232
    • Dhodapkar, M.V.1    Sznol, M.2    Zhao, B.3    Wang, D.4    Carvajal, R.D.5    Keohan, M.L.6
  • 153
    • 84892513912 scopus 로고    scopus 로고
    • CDX-1401 combined with TLR agonist: positive phase 1 results
    • 23980263
    • E.M.Riedmann. CDX-1401 combined with TLR agonist: positive phase 1 results. Hum Vaccin Immunother 2012; 8:1742; PMID:23980263; http://dx.doi.org/10.4161/hv.19658
    • (2012) Hum Vaccin Immunother , vol.8 , pp. 1742
    • Riedmann, E.M.1
  • 156
    • 84906510279 scopus 로고    scopus 로고
    • Distinct immunological mechanisms of CTLA-4 and PD-1 blockade revealed by analyzing TCR usage in blood lymphocytes
    • 25083336
    • L.Robert, C.Harview, R.Emerson, Wang, S.Mok, B.Homet, B.Comin-Anduix, R.C.Koya, H.Robins, P.C.Tumeh Distinct immunological mechanisms of CTLA-4 and PD-1 blockade revealed by analyzing TCR usage in blood lymphocytes. Oncoimmunology 2014; 3:e29244; PMID:25083336; http://dx.doi.org/10.4161/onci.29244
    • (2014) Oncoimmunology , vol.3 , pp. 29244
    • Robert, L.1    Harview, C.2    EmersonWang, R.3    Mok, S.4    Homet, B.5    Comin-Anduix, B.6    Koya, R.C.7    Robins, H.8    Tumeh, P.C.9
  • 157
    • 84908354848 scopus 로고    scopus 로고
    • Anti-programmed-death-receptor-1 treatment with pembrolizumab in ipilimumab-refractory advanced melanoma: a randomised dose-comparison cohort of a phase 1 trial
    • 25034862
    • C.Robert, A.Ribas, J.D.Wolchok, F.S.Hodi, O.Hamid, R.Kefford, J.S.Weber, A.M.Joshua, W.J.Hwu, T.C.Gangadhar Anti-programmed-death-receptor-1 treatment with pembrolizumab in ipilimumab-refractory advanced melanoma: a randomised dose-comparison cohort of a phase 1 trial. Lancet 2014; 384:1109-17 PMID:25034862; http://dx.doi.org/10.1016/S0140-6736(14)60958-2
    • (2014) Lancet , vol.384 , pp. 1109-1117
    • Robert, C.1    Ribas, A.2    Wolchok, J.D.3    Hodi, F.S.4    Hamid, O.5    Kefford, R.6    Weber, J.S.7    Joshua, A.M.8    Hwu, W.J.9    Gangadhar, T.C.10
  • 160
    • 84885736449 scopus 로고    scopus 로고
    • Biological insights into BRAF mutations in melanoma patient: Not mere therapeutic targets
    • 24179707
    • G.Improta, G.Pelosi, E.Tamborini, M.Donia, M.Santinami, F.de Braud, F.Fraggetta. Biological insights into BRAF mutations in melanoma patient: Not mere therapeutic targets. Oncoimmunology 2013; 2:e25594; PMID:24179707; http://dx.doi.org/10.4161/onci.25594
    • (2013) Oncoimmunology , vol.2 , pp. 25594
    • Improta, G.1    Pelosi, G.2    Tamborini, E.3    Donia, M.4    Santinami, M.5    de Braud, F.6    Fraggetta, F.7
  • 163
    • 41349088840 scopus 로고    scopus 로고
    • Levo- but not dextro-1-methyl tryptophan abrogates the IDO activity of human dendritic cells
    • 18045970
    • S.Lob, A.Konigsrainer, R.Schafer, H.G.Rammensee, G.Opelz, P.Terness. Levo- but not dextro-1-methyl tryptophan abrogates the IDO activity of human dendritic cells. Blood 2008; 111:2152-54; PMID:18045970; http://dx.doi.org/10.1182/blood-2007-10-116111
    • (2008) Blood , vol.111 , pp. 2152-2154
    • Lob, S.1    Konigsrainer, A.2    Schafer, R.3    Rammensee, H.G.4    Opelz, G.5    Terness, P.6
  • 164
    • 84870990555 scopus 로고    scopus 로고
    • Effects of 1-methyltryptophan stereoisomers on IDO2 enzyme activity and IDO2-mediated arrest of human T cell proliferation
    • 22527253
    • F.Qian, J.Liao, J.Villella, R.Edwards, P.Kalinski, S.Lele, P.Shrikant, K.Odunsi. Effects of 1-methyltryptophan stereoisomers on IDO2 enzyme activity and IDO2-mediated arrest of human T cell proliferation. Cancer Immunol Immunother 2012; 61:2013-20; PMID:22527253; http://dx.doi.org/10.1007/s00262-012-1265-x
    • (2012) Cancer Immunol Immunother , vol.61 , pp. 2013-2020
    • Qian, F.1    Liao, J.2    Villella, J.3    Edwards, R.4    Kalinski, P.5    Lele, S.6    Shrikant, P.7    Odunsi, K.8
  • 165
    • 77954143054 scopus 로고    scopus 로고
    • 1-L-methyltryptophan is a more effective inhibitor of vertebrate IDO2 enzymes than 1-D-methyltryptophan
    • 20399882
    • H.J.Yuasa, H.J.Ball, C.J.Austin, N.H.Hunt. 1-L-methyltryptophan is a more effective inhibitor of vertebrate IDO2 enzymes than 1-D-methyltryptophan. Comp Biochem Physiol B Biochem Mol Biol 2010; 157:10-15; PMID:20399882; http://dx.doi.org/10.1016/j.cbpb.2010.04.006
    • (2010) Comp Biochem Physiol B Biochem Mol Biol , vol.157 , pp. 10-15
    • Yuasa, H.J.1    Ball, H.J.2    Austin, C.J.3    Hunt, N.H.4
  • 166
    • 0026347919 scopus 로고
    • 1-Methyl-DL-tryptophan, beta-(3-benzofuranyl)-DL-alanine (the oxygen analog of tryptophan), and beta-; 3-benzo(b)thienyl-DL-alanine (the sulfur analog of tryptophan) are competitive inhibitors for indoleamine 2,3-dioxygenase
    • 1952947
    • S.G.Cady, M.Sono. 1-Methyl-DL-tryptophan, beta-(3-benzofuranyl)-DL-alanine (the oxygen analog of tryptophan), and beta-; 3-benzo(b)thienyl-DL-alanine (the sulfur analog of tryptophan) are competitive inhibitors for indoleamine 2,3-dioxygenase. Arch Biochem Biophys 1991; 291:326-33; PMID:1952947; http://dx.doi.org/10.1016/0003-9861(91)90142-6
    • (1991) Arch Biochem Biophys , vol.291 , pp. 326-333
    • Cady, S.G.1    Sono, M.2
  • 170
    • 33747119866 scopus 로고    scopus 로고
    • 4-1BB-mediated amelioration of experimental autoimmune uveoretinitis is caused by indoleamine 2,3-dioxygenase-dependent mechanisms
    • 16899371
    • B.K.Choi, T.Asai, D.S.Vinay, Y.H.Kim, B.S.Kwon. 4-1BB-mediated amelioration of experimental autoimmune uveoretinitis is caused by indoleamine 2,3-dioxygenase-dependent mechanisms. Cytokine 2006; 34:233-42; PMID:16899371; http://dx.doi.org/10.1016/j.cyto.2006.04.008
    • (2006) Cytokine , vol.34 , pp. 233-242
    • Choi, B.K.1    Asai, T.2    Vinay, D.S.3    Kim, Y.H.4    Kwon, B.S.5
  • 173
    • 0031007143 scopus 로고    scopus 로고
    • Monoclonal antibodies against the 4-1BB T-cell activation molecule eradicate established tumors
    • 9176498
    • I.Melero, W.W.Shuford, S.A.Newby, A.Aruffo, J.A.Ledbetter, K.E.Hellstrom, R.S.Mittler, L.Chen. Monoclonal antibodies against the 4-1BB T-cell activation molecule eradicate established tumors. Nat Med 1997; 3:682-85; PMID:9176498; http://dx.doi.org/10.1038/nm0697-682
    • (1997) Nat Med , vol.3 , pp. 682-685
    • Melero, I.1    Shuford, W.W.2    Newby, S.A.3    Aruffo, A.4    Ledbetter, J.A.5    Hellstrom, K.E.6    Mittler, R.S.7    Chen, L.8
  • 175
    • 34547443397 scopus 로고    scopus 로고
    • Transcriptional regulation of indoleamine 2,3-dioxygenase (IDO) by tryptophan and its analogue: down-regulation of the indoleamine 2,3-dioxygenase (IDO) transcription by tryptophan and its analogue
    • 19003025
    • T.Okamoto, S.Tone, H.Kanouchi, C.Miyawaki, S.Ono, Y.Minatogawa. Transcriptional regulation of indoleamine 2,3-dioxygenase (IDO) by tryptophan and its analogue: down-regulation of the indoleamine 2,3-dioxygenase (IDO) transcription by tryptophan and its analogue. Cytotechnology 2007; 54:107-13; PMID:19003025; http://dx.doi.org/10.1007/s10616-007-9081-4
    • (2007) Cytotechnology , vol.54 , pp. 107-113
    • Okamoto, T.1    Tone, S.2    Kanouchi, H.3    Miyawaki, C.4    Ono, S.5    Minatogawa, Y.6
  • 176
    • 79956302084 scopus 로고    scopus 로고
    • The indoleamine-2,3-dioxygenase (IDO) inhibitor 1-methyl-D-tryptophan upregulates IDO1 in human cancer cells
    • 21625531
    • C.A.Opitz, U.M.Litzenburger, U.Opitz, F.Sahm, K.Ochs, C.Lutz, W.Wick, M.Platten. The indoleamine-2,3-dioxygenase (IDO) inhibitor 1-methyl-D-tryptophan upregulates IDO1 in human cancer cells. PLoS One 2011; 6:e19823; PMID:21625531; http://dx.doi.org/10.1371/journal.pone.0019823
    • (2011) PLoS One , vol.6 , pp. 19823
    • Opitz, C.A.1    Litzenburger, U.M.2    Opitz, U.3    Sahm, F.4    Ochs, K.5    Lutz, C.6    Wick, W.7    Platten, M.8
  • 177
    • 0035282223 scopus 로고    scopus 로고
    • Characterisation of L-tryptophan transporters in human placenta: a comparison of brush border and basal membrane vesicles
    • 11230513
    • Y.Kudo, C.A.Boyd. Characterisation of L-tryptophan transporters in human placenta: a comparison of brush border and basal membrane vesicles. J Physiol 2001; 531:405-16; PMID:11230513; http://dx.doi.org/10.1111/j.1469-7793.2001.0405i.x
    • (2001) J Physiol , vol.531 , pp. 405-416
    • Kudo, Y.1    Boyd, C.A.2


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