References
- Lizée G, Overwijk WW, Radvanyi L, et al. Harnessing the power of the immune system to target cancer. Annu Rev Med 2013;64:71–90.
- Topalian SL, Drake CG, Pardoll DM. Immune checkpoint blockade: a common denominator approach to cancer therapy. Cancer Cell 2015;27:450–61.
- Schadendorf D, Hodi FS, Robert C, et al. Pooled analysis of long-term survival data from phase II and phase III trials of ipilimumab in Unresectable or Metastatic Melanoma. J Clin Oncol 2015;33:1889–94.
- Szostak B, Machaj F, Rosik J, et al. CTLA4 antagonists in phase I and phase II clinical trials, current status and future perspectives for cancer therapy. Expert Opin Investig Drugs 2019;28:149–59.
- Alsaab HO, Sau S, Alzhrani R, et al. PD-1 and PD-L1 checkpoint signaling inhibition for cancer immunotherapy: mechanism, combinations, and clinical outcome. Front Pharmacol 2017;8:561
- Majzner RG, Mackall CL. Clinical lessons learned from the first leg of the CAR T cell journey. Nat Med 2019;25:1341–55.
- Kreamer KM. Immune checkpoint blockade: a new paradigm in treating advanced cancer. J Adv Pract Oncol 2014;5:418–31.
- Cervenka I, Agudelo LZ, Ruas JL. Kynurenines: tryptophan’s metabolites in exercise, inflammation, and mental health. Science 2017;357:eaaf9794.
- Munn DH, Mellor AL. Indoleamine 2,3 dioxygenase and metabolic control of immune responses. Trends Immunol 2013;34:137–43.
- Mándi Y, Vécsei L. The kynurenine system and immunoregulation. J Neural Transm (Vienna) 2012;119:197–209.
- Munn DH, Sharma MD, Baban B, et al. GCN2 kinase in T cells mediates proliferative arrest and anergy induction in response to indoleamine 2,3-dioxygenase. Immunity 2005;22:633–42.
- Frumento G, Rotondo R, Tonetti M, et al. 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.
- Mezrich JD, Fechner JH, Zhang X, et al. An interaction between kynurenine and the aryl hydrocarbon receptor can generate regulatory T cells. J Immunol 2010;185:3190–8.
- Okamoto A, Nikaido T, Ochiai K, et al. Indoleamine 2,3-dioxygenase serves as a marker of poor prognosis in gene expression profiles of serous ovarian cancer cells. Clin Cancer Res 2005;11:6030–9.
- Ino K, Yoshida N, Kajiyama H, et al. Indoleamine 2,3-dioxygenase is a novel prognostic indicator for endometrial cancer. Br J Cancer 2006;95:1555–61.
- Pan K, Wang H, Chen MS, et al. Expression and prognosis role of indoleamine 2,3-dioxygenase in hepatocellular carcinoma. J Cancer Res Clin Oncol 2008;134:1247–53.
- Folgiero V, Goffredo BM, Filippini P, et al. Indoleamine 2,3-dioxygenase 1 (IDO1) activity in leukemia blasts correlates with poor outcome in childhood acute myeloid leukemia. Oncotarget 2014;5:2052–64.
- Speeckaert R, Vermaelen K, van Geel N, et al. Indoleamine 2,3-dioxygenase, a new prognostic marker in sentinel lymph nodes of melanoma patients. Eur J Cancer 2012;48:2004–11.
- Liu X, Shin N, Koblish HK, et al. Selective inhibition of IDO1 effectively regulates mediators of antitumor immunity. Blood 2010;115:3520–30.
- Holmgaard RB, Zamarin D, Munn DH, et al. Indoleamine 2,3-dioxygenase is a critical resistance mechanism in antitumor T cell immunotherapy targeting CTLA-4. J Exp Med 2013;210:1389–402.
- Tu W, Yang F, Xu G, et al. Discovery of imidazoisoindole derivatives as highly potent and orally active indoleamine-2,3-dioxygenase inhibitors. ACS Med Chem Lett 2019;10:949–53.
- Gomes B, Driessens G, Bartlett D, et al. Characterization of the selective indoleamine 2,3-dioxygenase-1 (IDO1) catalytic inhibitor EOS200271/PF-06840003 supports IDO1 as a critical resistance mechanism to PD-(L)1 blockade therapy. Mol Cancer Ther 2018;17:2530–42.
- Yue EW, Douty B, Wayland B, et al. Discovery of potent competitive inhibitors of indoleamine 2,3-dioxygenase with in vivo pharmacodynamic activity and efficacy in a mouse melanoma model. J Med Chem 2009;52:7364–7.
- Markwalder JA, Seitz SP, Blat Y, et al. Identification and optimization of a novel series of indoleamine 2,3-dioxygenase inhibitors. Bioorg Med Chem Lett 2017;27:582–5.
- Yue EW, Sparks R, Polam P, et al. INCB24360 (Epacadostat), a highly potent and selective indoleamine-2,3-dioxygenase 1 (IDO1) inhibitor for immuno-oncology. ACS Med Chem Lett 2017;8:486–91.
- Williams DK, Markwalder JA, Balog AJ, et al. Development of a series of novel o-phenylenediamine-based indoleamine 2,3-dioxygenase 1 (IDO1) inhibitors. Bioorg Med Chem Lett 2018;28:732–6.
- Kumar S, Waldo JP, Jaipuri FA, et al. Discovery of clinical candidate (1R,4r)-4-((R)-2-((S)-6-fluoro-5H-imidazo[5,1-a]isoindol-5-yl)-1-hydroxyethyl)cyclohexan-1-ol (Navoximod), a potent and selective inhibitor of indoleamine 2,3-dioxygenase 1. J Med Chem 2019;62:6705–33.
- Brastianos HC, Vottero E, Patrick BO, et al. Exiguamine A, an indoleamine-2,3-dioxygenase (IDO) inhibitor isolated from the marine sponge Neopetrosia exigua. J Am Chem Soc 2006;128:16046–7.
- Yang S, Li X, Hu F, et al. Discovery of tryptanthrin derivatives as potent inhibitors of indoleamine 2,3-dioxygenase with therapeutic activity in Lewis lung cancer (LLC) tumor-bearing mice. J Med Chem 2013;56:8321–31.
- Platten M, Nollen EAA, Röhrig UF, et al. Tryptophan metabolism as a common therapeutic target in cancer, neurodegeneration and beyond. Nat Rev Drug Discov 2019;18:379–401.
- Zou Y, Wang F, Wang Y, et al. Systematic study of imidazoles inhibiting IDO1 via the integration of molecular mechanics and quantum mechanics calculations. Eur J Med Chem 2017;131:152–70.
- Zou Y, Wang Y, Wang F, et al. Discovery of potent IDO1 inhibitors derived from tryptophan using scaffold-hopping and structure-based design approaches. Eur J Med Chem 2017;138:199–211.
- Zou Y, Wang F, Wang Y, et al. Discovery of imidazoleisoindole derivatives as potent IDO1 inhibitors: design, synthesis, biological evaluation and computational studies. Eur J Med Chem 2017;140:293–304.
- Zou Y, Hu Y, Ge S, et al. Effective virtual screening strategy toward heme-containing proteins: identification of novel IDO1 inhibitors. Eur J Med Chem 2019;184:111750
- Gaspari P, Banerjee T, Malachowski WP, et al. Structure-activity study of brassinin derivatives as indoleamine 2,3-dioxygenase inhibitors. J Med Chem 2006;49:684–92.
- Gulçin T, Taslimi P. Sulfonamide inhibitors: a patent review 2013-present. Expert Opin Ther Pat 2018;28:541–9.
- Penning TD, Talley JJ, Bertenshaw SR, et al. Synthesis and biological evaluation of the 1,5-diarylpyrazole class of cyclooxygenase-2 inhibitors: identification of 4-[5-(4-methylphenyl)-3-(trifluoromethyl)-1H-pyrazol-1-yl]benzenesulfonamide (SC-58635, Celecoxib). J Med Chem 1997;40:1347–65.
- Cheng MF, Hung MS, Song JS, et al. Discovery and structure-activity relationships of phenyl benzenesulfonylhydrazides as novel indoleamine 2,3-dioxygenase inhibitors. Bioorg Med Chem Lett 2014;24:3403–6.
- Wang X, Ahn YM, Lentscher AG, et al. Design, synthesis, and evaluation of substituted nicotinamide adenine dinucleotide (NAD+) synthetase inhibitors as potential antitubercular agents. Bioorg Med Chem Lett 2017;27:4426–30.
- Uyttenhove C, Pilotte L, Théate I, et al. Evidence for a tumoral immune resistance mechanism based on tryptophan degradation by indoleamine 2,3-dioxygenase. Nat Med 2003;9:1269–74.
- Negmeldin AT, Knoff JR, Pflum M. The structural requirements of histone deacetylase inhibitors: C4-modified SAHA analogs display dual HDAC6/HDAC8 selectivity. Eur J Med Chem 2018;143:1790–806.
- Lin SY, Yeh TK, Kuo CC, et al. Phenyl benzenesulfonylhydrazides exhibit selective indoleamine 2,3-dioxygenase inhibition with potent in vivo pharmacodynamic activity and Antitumor Efficacy. J Med Chem 2016;59:419–30.
- Jin S, Wang F, Zou Y, et al. Design, synthesis and biological evaluation of phenylsulfonamide-based IDO1 inhibitors. J China Pharm Univ 2018;49:34–8.
- Afonina IS, Cullen SP, Martin SJ. Cytotoxic and non-cytotoxic roles of the CTL/NK protease granzyme B. Immunol Rev 2010;235:105–16.
- Togashi Y, Shitara K, Nishikawa H. Regulatory T cells in cancer immunosuppression – implications for anticancer therapy. Nat Rev Clin Oncol 2019;16:356–71.
- Jafari R, Almqvist H, Axelsson H, et al. The cellular thermal shift assay for evaluating drug target interactions in cells. Nat Protoc 2014;9:2100–22.
- Xu Q, Gu J, Lv Y, et al. Angiogenesis for tumour vascular normalization of Endostar on hepatoma 22 tumour-bearing mice is involved in the immune response. Oncol Lett 2018;15:3437–46.
- Munn DH, Shafizadeh E, Attwood JT, et al. Inhibition of T cell proliferation by macrophage tryptophan catabolism. J Exp Med 1999;189:1363–72.