PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 14632165-3 2003 The objective of this study was to determine the effect of captopril, an angiotensin converting enzyme (ACE) inhibitor, on retinal VEGF, VEGF-R1, and VEGF-R2 expression in a mouse model of oxygen induced retinopathy (OIR). Captopril 59-68 angiotensin I converting enzyme (peptidyl-dipeptidase A) 1 Mus musculus 73-102 14632165-3 2003 The objective of this study was to determine the effect of captopril, an angiotensin converting enzyme (ACE) inhibitor, on retinal VEGF, VEGF-R1, and VEGF-R2 expression in a mouse model of oxygen induced retinopathy (OIR). Captopril 59-68 angiotensin I converting enzyme (peptidyl-dipeptidase A) 1 Mus musculus 104-107 14632165-3 2003 The objective of this study was to determine the effect of captopril, an angiotensin converting enzyme (ACE) inhibitor, on retinal VEGF, VEGF-R1, and VEGF-R2 expression in a mouse model of oxygen induced retinopathy (OIR). Captopril 59-68 vascular endothelial growth factor A Mus musculus 131-135 14632165-3 2003 The objective of this study was to determine the effect of captopril, an angiotensin converting enzyme (ACE) inhibitor, on retinal VEGF, VEGF-R1, and VEGF-R2 expression in a mouse model of oxygen induced retinopathy (OIR). Captopril 59-68 FMS-like tyrosine kinase 1 Mus musculus 137-144 14632165-3 2003 The objective of this study was to determine the effect of captopril, an angiotensin converting enzyme (ACE) inhibitor, on retinal VEGF, VEGF-R1, and VEGF-R2 expression in a mouse model of oxygen induced retinopathy (OIR). Captopril 59-68 kinase insert domain protein receptor Mus musculus 150-157 14632165-6 2003 RESULTS: Captopril plus OIR treated animals had higher levels of retinal VEGF mRNA and protein at P12 (p < 0.05) and lower levels at P17 (p < 0.05) than OIR animals. Captopril 9-18 vascular endothelial growth factor A Mus musculus 73-77 14632165-6 2003 RESULTS: Captopril plus OIR treated animals had higher levels of retinal VEGF mRNA and protein at P12 (p < 0.05) and lower levels at P17 (p < 0.05) than OIR animals. Captopril 9-18 CDK2 (cyclin-dependent kinase 2)-associated protein 1 Mus musculus 98-101 14632165-6 2003 RESULTS: Captopril plus OIR treated animals had higher levels of retinal VEGF mRNA and protein at P12 (p < 0.05) and lower levels at P17 (p < 0.05) than OIR animals. Captopril 9-18 family with sequence similarity 72, member A Mus musculus 136-139 14632165-10 2003 Retinal VEGF-R2 mRNA and protein expression were significantly higher at P12 in OIR plus captopril treated animals than OIR animals (p = 0.01). Captopril 89-98 kinase insert domain protein receptor Mus musculus 8-15 14632165-11 2003 CONCLUSIONS: In summary, captopril maintains VEGF and increases VEGF-R2 expression during the period of hyperoxia when VEGF expression is normally suppressed. Captopril 25-34 vascular endothelial growth factor A Mus musculus 45-49 14632165-11 2003 CONCLUSIONS: In summary, captopril maintains VEGF and increases VEGF-R2 expression during the period of hyperoxia when VEGF expression is normally suppressed. Captopril 25-34 kinase insert domain protein receptor Mus musculus 64-71 14632165-11 2003 CONCLUSIONS: In summary, captopril maintains VEGF and increases VEGF-R2 expression during the period of hyperoxia when VEGF expression is normally suppressed. Captopril 25-34 vascular endothelial growth factor A Mus musculus 64-68 14632165-12 2003 Captopril treatment during oxygen exposure is associated with a reduction in the angiogenic response at day 17 as manifested by decreased VEGF and VEGF-R2 expression in retinal tissue. Captopril 0-9 vascular endothelial growth factor A Mus musculus 138-142 14632165-12 2003 Captopril treatment during oxygen exposure is associated with a reduction in the angiogenic response at day 17 as manifested by decreased VEGF and VEGF-R2 expression in retinal tissue. Captopril 0-9 kinase insert domain protein receptor Mus musculus 147-154 26382631-5 2016 It appears that the host tryptophan catabolic enzyme, indoleamine 2,3-dioxygenase 1 (IDO1) plays a dominant role in the interplay between tryptophan catabolism by microbial communities, the host"s own pathway of metabolite production, and the activation of the aryl hydrocarbon receptor (AhR)/IL-22 axis, eventually impacting on mucosal immune homeostasis and host/fungal symbiosis. Tryptophan 138-148 indoleamine 2,3-dioxygenase 1 Homo sapiens 85-89 26839260-1 2016 Indoleamine 2,3-dioxygenase (IDO) has immunoregulatory roles associated with tryptophan metabolism. Tryptophan 77-87 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 26449488-1 2016 BACKGROUND: Indoleamine 2,3-dioxygenase (IDO), which degrades tryptophan (Trp) to kynurenine (Kyn), has been demonstrated to contribute to modulation of allergic responses. Tryptophan 62-72 indoleamine 2,3-dioxygenase 1 Homo sapiens 12-39 26887418-2 2016 Oxidation of tryptophan, due to immune induction of the enzyme indoleamine 2,3-dioxygenase (IDO), is considered to be the main cause of tryptophan depletion in HIV infection and AIDS. Tryptophan 13-23 indoleamine 2,3-dioxygenase 1 Homo sapiens 92-95 26887418-2 2016 Oxidation of tryptophan, due to immune induction of the enzyme indoleamine 2,3-dioxygenase (IDO), is considered to be the main cause of tryptophan depletion in HIV infection and AIDS. Tryptophan 136-146 indoleamine 2,3-dioxygenase 1 Homo sapiens 92-95 26449488-1 2016 BACKGROUND: Indoleamine 2,3-dioxygenase (IDO), which degrades tryptophan (Trp) to kynurenine (Kyn), has been demonstrated to contribute to modulation of allergic responses. Tryptophan 62-72 indoleamine 2,3-dioxygenase 1 Homo sapiens 41-44 26449488-1 2016 BACKGROUND: Indoleamine 2,3-dioxygenase (IDO), which degrades tryptophan (Trp) to kynurenine (Kyn), has been demonstrated to contribute to modulation of allergic responses. Tryptophan 74-77 indoleamine 2,3-dioxygenase 1 Homo sapiens 12-39 26449488-1 2016 BACKGROUND: Indoleamine 2,3-dioxygenase (IDO), which degrades tryptophan (Trp) to kynurenine (Kyn), has been demonstrated to contribute to modulation of allergic responses. Tryptophan 74-77 indoleamine 2,3-dioxygenase 1 Homo sapiens 41-44 26449488-6 2016 RESULTS: Kyn/Trp (IDO activity) was significantly lower in subjects with food allergy (n = 100) than in aged-matched healthy controls (n = 112) (P = 0.004). Tryptophan 13-16 indoleamine 2,3-dioxygenase 1 Homo sapiens 18-21 25547097-3 2016 By decreasing the availability of tryptophan for serotonin synthesis, such IDO and TDO-driven TRYCATs, also decrease the availability of serotonin for N-acetylserotonin (NAS) and melatonin synthesis. Tryptophan 34-44 indoleamine 2,3-dioxygenase 1 Homo sapiens 75-78 26485560-9 2016 Notably, MSCs express indoleamine-2,3-dioxygenase (IDO), which mediates T-cell suppressive tryptophan catabolism. Tryptophan 91-101 indoleamine 2,3-dioxygenase 1 Homo sapiens 22-49 26485560-9 2016 Notably, MSCs express indoleamine-2,3-dioxygenase (IDO), which mediates T-cell suppressive tryptophan catabolism. Tryptophan 91-101 indoleamine 2,3-dioxygenase 1 Homo sapiens 51-54 26485560-10 2016 Our observations suggest that IDO-induced tryptophan depletion interferes with a tryptophan-sufficiency signal that promotes cellular mTOR activation. Tryptophan 42-52 indoleamine 2,3-dioxygenase 1 Homo sapiens 30-33 26814137-3 2016 Indoleamine 2,3-dioxygenase (IDO), an enzyme that catabolizes tryptophan along the kynurenine pathway, is highly expressed in the placenta and serum during pregnancy. Tryptophan 62-72 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 26814137-3 2016 Indoleamine 2,3-dioxygenase (IDO), an enzyme that catabolizes tryptophan along the kynurenine pathway, is highly expressed in the placenta and serum during pregnancy. Tryptophan 62-72 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 26517244-5 2016 Many tumors have been proven to have a high expression of indoleamine 2, 3-dioxygenase 1 (IDO), which is a rate-limiting enzyme that catalyzes tryptophan to kynurenine, thus causing immune tolerance within the tumor microenvironment. Tryptophan 143-153 indoleamine 2,3-dioxygenase 1 Homo sapiens 58-88 26517244-5 2016 Many tumors have been proven to have a high expression of indoleamine 2, 3-dioxygenase 1 (IDO), which is a rate-limiting enzyme that catalyzes tryptophan to kynurenine, thus causing immune tolerance within the tumor microenvironment. Tryptophan 143-153 indoleamine 2,3-dioxygenase 1 Homo sapiens 90-93 26517538-1 2016 Indoleamine 2,3-dioxygenase (IDO) is a heme-containing oxidoreductase that catalyzes the initial and rate-limiting step in the breakdown of non-dietary tryptophan. Tryptophan 152-162 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 26517538-1 2016 Indoleamine 2,3-dioxygenase (IDO) is a heme-containing oxidoreductase that catalyzes the initial and rate-limiting step in the breakdown of non-dietary tryptophan. Tryptophan 152-162 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 26654772-9 2016 A consequence of increased pro-inflammatory cytokines, is their induction of indoleamine 2,3-dioxygenase (IDO), which takes tryptophan away from serotonin, Nacetylserotonin and melatonin synthesis, driving it to the synthesis of neuroregulatory TRYCATs. Tryptophan 124-134 indoleamine 2,3-dioxygenase 1 Homo sapiens 77-104 26654772-9 2016 A consequence of increased pro-inflammatory cytokines, is their induction of indoleamine 2,3-dioxygenase (IDO), which takes tryptophan away from serotonin, Nacetylserotonin and melatonin synthesis, driving it to the synthesis of neuroregulatory TRYCATs. Tryptophan 124-134 indoleamine 2,3-dioxygenase 1 Homo sapiens 106-109 26458241-0 2016 Indoleamine-2,3-dioxygenase as an effector and an indicator of protective immune responses in patients with acute hepatitis B. UNLABELLED: Indoleamine-2, 3-dioxygenase (IDO), an interferon-gamma-inducible enzyme catalyzing tryptophan into kynurenine, exerts dual functions in infectious diseases, acting as a suppressor of intracellular pathogens and as an immune regulator. Tryptophan 223-233 indoleamine 2,3-dioxygenase 1 Homo sapiens 139-167 26519060-1 2015 Indoleamine 2, 3-dioxygenase 1 (IDO1), IDO2, and tryptophan 2, 3-dioxygenase (TDO) comprise a family of enzymes that catalyze the first- and rate-limiting step associated with the catabolic conversion of tryptophan (Trp) into kynurenine (Kyn). Tryptophan 49-59 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-30 27161289-9 2016 To this regard, the specific interaction of nitric oxide (NO ) with the tryptophan-degrading enzyme IDO-1 could be important, because an enhanced formation of NO has been reported in patients with asthma and allergic rhinitis. Tryptophan 72-82 indoleamine 2,3-dioxygenase 1 Homo sapiens 100-105 27161289-10 2016 Importantly, NO suppresses the activity of the heme enzyme IDO-1, which could explain the higher tryptophan levels. Tryptophan 98-108 indoleamine 2,3-dioxygenase 1 Homo sapiens 60-65 26727596-1 2016 Indoleamine 2,3-dioxygenase (IDO), a tryptophan-catabolizing intracellular enzyme of the L-kynurenine pathway, causes preneoplastic cells and tumor cells to escape the immune system by inducing immune tolerance; this mechanism might be associated with the development and progression of human malignancies. Tryptophan 37-47 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 26727596-1 2016 Indoleamine 2,3-dioxygenase (IDO), a tryptophan-catabolizing intracellular enzyme of the L-kynurenine pathway, causes preneoplastic cells and tumor cells to escape the immune system by inducing immune tolerance; this mechanism might be associated with the development and progression of human malignancies. Tryptophan 37-47 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 25907424-1 2016 The immunomodulatory effects of indoleamine 2,3-dioxygenase (IDO) are ascribed to its ability to catalyze the breakdown of the L-tryptophan along the L-kynurenine pathway. Tryptophan 127-139 indoleamine 2,3-dioxygenase 1 Homo sapiens 32-59 25907424-1 2016 The immunomodulatory effects of indoleamine 2,3-dioxygenase (IDO) are ascribed to its ability to catalyze the breakdown of the L-tryptophan along the L-kynurenine pathway. Tryptophan 127-139 indoleamine 2,3-dioxygenase 1 Homo sapiens 61-64 26647830-1 2016 Indoleamine 2,3-dioxygenase (IDO), through L-tryptophan depletion, activates general control non-derepressible (GCN) 2 kinase and suppresses T-cell proliferation, in addition to suppressing aerobic glycolysis and glutaminolysis, which are required for these rapidly proliferating cells. Tryptophan 43-55 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 26647830-1 2016 Indoleamine 2,3-dioxygenase (IDO), through L-tryptophan depletion, activates general control non-derepressible (GCN) 2 kinase and suppresses T-cell proliferation, in addition to suppressing aerobic glycolysis and glutaminolysis, which are required for these rapidly proliferating cells. Tryptophan 43-55 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 26519060-1 2015 Indoleamine 2, 3-dioxygenase 1 (IDO1), IDO2, and tryptophan 2, 3-dioxygenase (TDO) comprise a family of enzymes that catalyze the first- and rate-limiting step associated with the catabolic conversion of tryptophan (Trp) into kynurenine (Kyn). Tryptophan 49-59 indoleamine 2,3-dioxygenase 1 Homo sapiens 32-36 26519060-1 2015 Indoleamine 2, 3-dioxygenase 1 (IDO1), IDO2, and tryptophan 2, 3-dioxygenase (TDO) comprise a family of enzymes that catalyze the first- and rate-limiting step associated with the catabolic conversion of tryptophan (Trp) into kynurenine (Kyn). Tryptophan 216-219 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-30 26519060-1 2015 Indoleamine 2, 3-dioxygenase 1 (IDO1), IDO2, and tryptophan 2, 3-dioxygenase (TDO) comprise a family of enzymes that catalyze the first- and rate-limiting step associated with the catabolic conversion of tryptophan (Trp) into kynurenine (Kyn). Tryptophan 216-219 indoleamine 2,3-dioxygenase 1 Homo sapiens 32-36 26674411-3 2015 Indoleamine-2,3-dioxygenase (IDO) is an intracellular enzyme, which through the process of tryptophan depletion exerts an immunosuppressive effect, facilitating immune escape of tumors. Tryptophan 91-101 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 26674411-3 2015 Indoleamine-2,3-dioxygenase (IDO) is an intracellular enzyme, which through the process of tryptophan depletion exerts an immunosuppressive effect, facilitating immune escape of tumors. Tryptophan 91-101 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 26489554-2 2015 IDO activity can be measured by the tryptophan (Trp)/kynurenine (Kyn) ratio. Tryptophan 36-46 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 26198597-3 2015 Indoleamine 2,3-dioxygenase (IDO1) is a tryptophan (Trp)-catabolizing enzyme which is assumed to be instrumental in the antibacterial and antiviral defence mechanisms. Tryptophan 40-50 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-33 26198597-3 2015 Indoleamine 2,3-dioxygenase (IDO1) is a tryptophan (Trp)-catabolizing enzyme which is assumed to be instrumental in the antibacterial and antiviral defence mechanisms. Tryptophan 52-55 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-33 26181812-2 2015 One recently explored pathway of HIV pathogenesis involves induction of the enzyme indoleamine 2,3-dioxygenase-1 (IDO), which catabolizes tryptophan into kynurenine and several other immunologically active metabolites that suppress T-cell proliferation. Tryptophan 138-148 indoleamine 2,3-dioxygenase 1 Homo sapiens 83-112 26181812-2 2015 One recently explored pathway of HIV pathogenesis involves induction of the enzyme indoleamine 2,3-dioxygenase-1 (IDO), which catabolizes tryptophan into kynurenine and several other immunologically active metabolites that suppress T-cell proliferation. Tryptophan 138-148 indoleamine 2,3-dioxygenase 1 Homo sapiens 114-117 26181812-5 2015 IDO activity was assessed by the ratio of plasma kynurenine to tryptophan levels (KT ratio), measured by liquid chromatography-tandem mass spectrometry. Tryptophan 63-73 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 26186743-1 2015 IDO1 (indoleamine 2,3-dioxygenase 1) is a member of a unique class of mammalian haem dioxygenases that catalyse the oxidative catabolism of the least-abundant essential amino acid, L-Trp (L-tryptophan), along the kynurenine pathway. Tryptophan 181-186 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-4 26186743-1 2015 IDO1 (indoleamine 2,3-dioxygenase 1) is a member of a unique class of mammalian haem dioxygenases that catalyse the oxidative catabolism of the least-abundant essential amino acid, L-Trp (L-tryptophan), along the kynurenine pathway. Tryptophan 181-186 indoleamine 2,3-dioxygenase 1 Homo sapiens 6-35 26186743-1 2015 IDO1 (indoleamine 2,3-dioxygenase 1) is a member of a unique class of mammalian haem dioxygenases that catalyse the oxidative catabolism of the least-abundant essential amino acid, L-Trp (L-tryptophan), along the kynurenine pathway. Tryptophan 188-200 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-4 26186743-1 2015 IDO1 (indoleamine 2,3-dioxygenase 1) is a member of a unique class of mammalian haem dioxygenases that catalyse the oxidative catabolism of the least-abundant essential amino acid, L-Trp (L-tryptophan), along the kynurenine pathway. Tryptophan 188-200 indoleamine 2,3-dioxygenase 1 Homo sapiens 6-35 26186743-4 2015 IDO1 is recognised as a prominent immune regulatory enzyme capable of modulating immune cell activation status and phenotype via several molecular mechanisms including enzyme-dependent deprivation of L-Trp and its conversion into the aryl hydrocarbon receptor ligand kynurenine and other bioactive kynurenine pathway metabolites, or non-enzymatic cell signalling actions involving tyrosine phosphorylation of IDO1. Tryptophan 200-205 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-4 26279502-6 2015 Given recent observations demonstrating high indoleamine 2,3 dioxygenase 1 (IDO1) expression in GBM, the immunosuppressive impact of IDO1-mediated Trp catabolism, as well as active transport of Trp and the IDO1-downstream Trp catabolite, Kyn, across the blood brain barrier, we hypothesized that peripheral blood analysis of this pathway would provide diagnostic utility. Tryptophan 147-150 indoleamine 2,3-dioxygenase 1 Homo sapiens 133-137 26279502-6 2015 Given recent observations demonstrating high indoleamine 2,3 dioxygenase 1 (IDO1) expression in GBM, the immunosuppressive impact of IDO1-mediated Trp catabolism, as well as active transport of Trp and the IDO1-downstream Trp catabolite, Kyn, across the blood brain barrier, we hypothesized that peripheral blood analysis of this pathway would provide diagnostic utility. Tryptophan 147-150 indoleamine 2,3-dioxygenase 1 Homo sapiens 133-137 26708916-3 2015 The latest researches showed that the abnormal tryptophan metabolism mediated by indoleamine-2, 3-dioxygenase(IDO) is related with the pathogenesis of ITP. Tryptophan 47-57 indoleamine 2,3-dioxygenase 1 Homo sapiens 110-113 26708916-6 2015 Thus, clarifying the abnormal tryptophan metabolism mediated by IDO may provide a new idea for improving the understand of the pathogenesis and treatment of ITP. Tryptophan 30-40 indoleamine 2,3-dioxygenase 1 Homo sapiens 64-67 26708916-7 2015 This review focuses on reasearch progress of the tryptophan metabolism mediated by IDO and ITP. Tryptophan 49-59 indoleamine 2,3-dioxygenase 1 Homo sapiens 83-86 26666715-1 2015 PURPOSE: Indoleamine 2,3-dioxygenase 1 (IDO1: IDO) is an enzyme catabolizing tryptophan (Trp) into the kynurenine (Kyn) pathway, and is an important micro-environmental factor suppressing antitumor immune responses. Tryptophan 77-87 indoleamine 2,3-dioxygenase 1 Homo sapiens 9-38 26666715-1 2015 PURPOSE: Indoleamine 2,3-dioxygenase 1 (IDO1: IDO) is an enzyme catabolizing tryptophan (Trp) into the kynurenine (Kyn) pathway, and is an important micro-environmental factor suppressing antitumor immune responses. Tryptophan 77-87 indoleamine 2,3-dioxygenase 1 Homo sapiens 40-44 26666715-1 2015 PURPOSE: Indoleamine 2,3-dioxygenase 1 (IDO1: IDO) is an enzyme catabolizing tryptophan (Trp) into the kynurenine (Kyn) pathway, and is an important micro-environmental factor suppressing antitumor immune responses. Tryptophan 77-87 indoleamine 2,3-dioxygenase 1 Homo sapiens 40-43 26666715-1 2015 PURPOSE: Indoleamine 2,3-dioxygenase 1 (IDO1: IDO) is an enzyme catabolizing tryptophan (Trp) into the kynurenine (Kyn) pathway, and is an important micro-environmental factor suppressing antitumor immune responses. Tryptophan 89-92 indoleamine 2,3-dioxygenase 1 Homo sapiens 9-38 26666715-1 2015 PURPOSE: Indoleamine 2,3-dioxygenase 1 (IDO1: IDO) is an enzyme catabolizing tryptophan (Trp) into the kynurenine (Kyn) pathway, and is an important micro-environmental factor suppressing antitumor immune responses. Tryptophan 89-92 indoleamine 2,3-dioxygenase 1 Homo sapiens 40-44 26666715-1 2015 PURPOSE: Indoleamine 2,3-dioxygenase 1 (IDO1: IDO) is an enzyme catabolizing tryptophan (Trp) into the kynurenine (Kyn) pathway, and is an important micro-environmental factor suppressing antitumor immune responses. Tryptophan 89-92 indoleamine 2,3-dioxygenase 1 Homo sapiens 40-43 26147366-0 2015 Indoleamine 2,3-dioxygenase depletes tryptophan, activates general control non-derepressible 2 kinase and down-regulates key enzymes involved in fatty acid synthesis in primary human CD4+ T cells. Tryptophan 37-47 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 26489554-2 2015 IDO activity can be measured by the tryptophan (Trp)/kynurenine (Kyn) ratio. Tryptophan 48-51 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 26489565-2 2015 The IDO activity can be measured by the tryptophan (Trp)/kynurenine (Kyn) ratio. Tryptophan 40-50 indoleamine 2,3-dioxygenase 1 Homo sapiens 4-7 26489565-2 2015 The IDO activity can be measured by the tryptophan (Trp)/kynurenine (Kyn) ratio. Tryptophan 52-55 indoleamine 2,3-dioxygenase 1 Homo sapiens 4-7 26378585-2 2015 By cleaving the aromatic indole ring of tryptophan, IDO initiates the production of a variety of tryptophan degradation products called "kynurenines" that are known to exert important immuno-regulatory functions. Tryptophan 40-50 indoleamine 2,3-dioxygenase 1 Homo sapiens 52-55 26378585-2 2015 By cleaving the aromatic indole ring of tryptophan, IDO initiates the production of a variety of tryptophan degradation products called "kynurenines" that are known to exert important immuno-regulatory functions. Tryptophan 97-107 indoleamine 2,3-dioxygenase 1 Homo sapiens 52-55 26378585-5 2015 In this review, we assess how IDO-mediated catabolism of tryptophan can modulate the immune system to arrest inflammation, suppress immunity to cancer and inhibit allergy, autoimmunity and the rejection of transplanted tissues. Tryptophan 57-67 indoleamine 2,3-dioxygenase 1 Homo sapiens 30-33 26285873-3 2015 The inflammation-inducible enzyme indoleamine 2,3 dioxygenase (IDO) is responsible for the first rate-limiting step in the kynurenine pathway, i.e., oxidation of tryptophan to kynurenine. Tryptophan 162-172 indoleamine 2,3-dioxygenase 1 Homo sapiens 34-61 26358342-2 2015 Tryptophan is a substrate of many important proteins, e.g., indolamine 2,3 dioxygenase (IDO). Tryptophan 0-10 indoleamine 2,3-dioxygenase 1 Homo sapiens 60-86 26358342-2 2015 Tryptophan is a substrate of many important proteins, e.g., indolamine 2,3 dioxygenase (IDO). Tryptophan 0-10 indoleamine 2,3-dioxygenase 1 Homo sapiens 88-91 26285873-3 2015 The inflammation-inducible enzyme indoleamine 2,3 dioxygenase (IDO) is responsible for the first rate-limiting step in the kynurenine pathway, i.e., oxidation of tryptophan to kynurenine. Tryptophan 162-172 indoleamine 2,3-dioxygenase 1 Homo sapiens 63-66 26285873-4 2015 Excessive IDO activity in conditions such as HIV/AIDS may lead to tryptophan depletion and accumulation of metabolites downstream from kynurenine. Tryptophan 66-76 indoleamine 2,3-dioxygenase 1 Homo sapiens 10-13 26309411-1 2015 l-Tryptophan (l-Trp) is an essential amino acid that possesses diverse metabolic, neurological, and immunological roles spanning from the synthesis of proteins, neurotransmitter serotonin, and neurohormone melatonin, to its degradation into immunosuppressive catabolites by indoleamine-2, 3-dioxygenase (IDO) in the kynurenine pathway (KP). Tryptophan 0-12 indoleamine 2,3-dioxygenase 1 Homo sapiens 274-302 26309411-1 2015 l-Tryptophan (l-Trp) is an essential amino acid that possesses diverse metabolic, neurological, and immunological roles spanning from the synthesis of proteins, neurotransmitter serotonin, and neurohormone melatonin, to its degradation into immunosuppressive catabolites by indoleamine-2, 3-dioxygenase (IDO) in the kynurenine pathway (KP). Tryptophan 0-12 indoleamine 2,3-dioxygenase 1 Homo sapiens 304-307 26309411-1 2015 l-Tryptophan (l-Trp) is an essential amino acid that possesses diverse metabolic, neurological, and immunological roles spanning from the synthesis of proteins, neurotransmitter serotonin, and neurohormone melatonin, to its degradation into immunosuppressive catabolites by indoleamine-2, 3-dioxygenase (IDO) in the kynurenine pathway (KP). Tryptophan 14-19 indoleamine 2,3-dioxygenase 1 Homo sapiens 274-302 26309411-1 2015 l-Tryptophan (l-Trp) is an essential amino acid that possesses diverse metabolic, neurological, and immunological roles spanning from the synthesis of proteins, neurotransmitter serotonin, and neurohormone melatonin, to its degradation into immunosuppressive catabolites by indoleamine-2, 3-dioxygenase (IDO) in the kynurenine pathway (KP). Tryptophan 14-19 indoleamine 2,3-dioxygenase 1 Homo sapiens 304-307 26309411-3 2015 IDO/AhR acts as a double-edged sword by both depleting l-Trp to starve the invaders and by contributing to the state of immunosuppression with microorganisms that were not cleared during acute infection. Tryptophan 55-60 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 26309411-4 2015 Pathogens experiencing Trp deprivation by IDO-mediated degradation include certain bacteria, parasites, and less likely viruses. Tryptophan 23-26 indoleamine 2,3-dioxygenase 1 Homo sapiens 42-45 25950090-8 2015 Biochemical analyses, using IDO variants with either Ser or Thr substitutions, suggest that the distal-Ser change was crucial for the improvement in affinity for l-Trp in ancient IDO1. Tryptophan 162-167 indoleamine 2,3-dioxygenase 1 Homo sapiens 28-31 25651307-3 2015 Monitoring of tryptophan (trp) metabolism through indoleamine 2.3-dioxygenase (IDO) has been previously proposed to predict acute rejection of human kidney transplants. Tryptophan 14-24 indoleamine 2,3-dioxygenase 1 Homo sapiens 50-77 25651307-3 2015 Monitoring of tryptophan (trp) metabolism through indoleamine 2.3-dioxygenase (IDO) has been previously proposed to predict acute rejection of human kidney transplants. Tryptophan 14-24 indoleamine 2,3-dioxygenase 1 Homo sapiens 79-82 25651307-3 2015 Monitoring of tryptophan (trp) metabolism through indoleamine 2.3-dioxygenase (IDO) has been previously proposed to predict acute rejection of human kidney transplants. Tryptophan 26-29 indoleamine 2,3-dioxygenase 1 Homo sapiens 50-77 25651307-3 2015 Monitoring of tryptophan (trp) metabolism through indoleamine 2.3-dioxygenase (IDO) has been previously proposed to predict acute rejection of human kidney transplants. Tryptophan 26-29 indoleamine 2,3-dioxygenase 1 Homo sapiens 79-82 25728366-4 2015 Induced by inflammatory stimuli, IDO catabolizes tryptophan to kynurenine (KYN), which is subsequently converted into neuroactive metabolites. Tryptophan 49-59 indoleamine 2,3-dioxygenase 1 Homo sapiens 33-36 25950090-1 2015 Indoleamine 2,3-dioxygenase (IDO) is a Trp-degrading enzyme that catalyzes the first step in the kynurenine pathway. Tryptophan 39-42 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 25950090-1 2015 Indoleamine 2,3-dioxygenase (IDO) is a Trp-degrading enzyme that catalyzes the first step in the kynurenine pathway. Tryptophan 39-42 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 25519303-2 2015 Coincidently, most of those malignancies express an inducible tryptophan catabolic enzyme, indoleamine 2,3 dioxygenase 1 (IDO1). Tryptophan 62-72 indoleamine 2,3-dioxygenase 1 Homo sapiens 91-120 25519303-2 2015 Coincidently, most of those malignancies express an inducible tryptophan catabolic enzyme, indoleamine 2,3 dioxygenase 1 (IDO1). Tryptophan 62-72 indoleamine 2,3-dioxygenase 1 Homo sapiens 122-126 25519303-4 2015 The primary function of IDO1 is associated with conversion of the essential amino acid, tryptophan, into downstream catabolites known as kynurenines. Tryptophan 88-98 indoleamine 2,3-dioxygenase 1 Homo sapiens 24-28 25950090-8 2015 Biochemical analyses, using IDO variants with either Ser or Thr substitutions, suggest that the distal-Ser change was crucial for the improvement in affinity for l-Trp in ancient IDO1. Tryptophan 162-167 indoleamine 2,3-dioxygenase 1 Homo sapiens 179-183 25950090-9 2015 The ancestral IDO1 likely had a "moderate" enzymatic efficiency for l-Trp, clearly higher than IDO2 but lower than mammalian IDO1. Tryptophan 68-73 indoleamine 2,3-dioxygenase 1 Homo sapiens 14-18 26110930-1 2015 BACKGROUND: Interferon gamma (IFN-gamma) production induces the transcription of indoleamine 2,3 dioxygenase (IDO) resulting in the reduction of T-cell activation and proliferation through the depletion of tryptophan and the elicitation of Treg lymphocytes. Tryptophan 206-216 indoleamine 2,3-dioxygenase 1 Homo sapiens 81-108 25940712-2 2015 We postulated that the tumor microenvironment suppresses CAR-expressing T cells (CARTs) through the activity of indoleamine 2,3-dioxygenase (IDO), an intracellular enzyme that converts tryptophan into metabolites that inhibit T -: cell activity. Tryptophan 185-195 indoleamine 2,3-dioxygenase 1 Homo sapiens 112-139 25940712-2 2015 We postulated that the tumor microenvironment suppresses CAR-expressing T cells (CARTs) through the activity of indoleamine 2,3-dioxygenase (IDO), an intracellular enzyme that converts tryptophan into metabolites that inhibit T -: cell activity. Tryptophan 185-195 indoleamine 2,3-dioxygenase 1 Homo sapiens 141-144 25788494-1 2015 PURPOSE: Indoleamine 2,3-dioxygenase 1 (IDO1: IDO), an enzyme catabolizing tryptophan (Trp) into the kynurenine (Kyn) pathway, is increasingly being recognized as an important microenvironmental factor suppressing antitumor immune responses. Tryptophan 75-85 indoleamine 2,3-dioxygenase 1 Homo sapiens 9-38 25788494-1 2015 PURPOSE: Indoleamine 2,3-dioxygenase 1 (IDO1: IDO), an enzyme catabolizing tryptophan (Trp) into the kynurenine (Kyn) pathway, is increasingly being recognized as an important microenvironmental factor suppressing antitumor immune responses. Tryptophan 75-85 indoleamine 2,3-dioxygenase 1 Homo sapiens 40-44 25788494-1 2015 PURPOSE: Indoleamine 2,3-dioxygenase 1 (IDO1: IDO), an enzyme catabolizing tryptophan (Trp) into the kynurenine (Kyn) pathway, is increasingly being recognized as an important microenvironmental factor suppressing antitumor immune responses. Tryptophan 75-85 indoleamine 2,3-dioxygenase 1 Homo sapiens 40-43 25788494-1 2015 PURPOSE: Indoleamine 2,3-dioxygenase 1 (IDO1: IDO), an enzyme catabolizing tryptophan (Trp) into the kynurenine (Kyn) pathway, is increasingly being recognized as an important microenvironmental factor suppressing antitumor immune responses. Tryptophan 87-90 indoleamine 2,3-dioxygenase 1 Homo sapiens 9-38 25788494-1 2015 PURPOSE: Indoleamine 2,3-dioxygenase 1 (IDO1: IDO), an enzyme catabolizing tryptophan (Trp) into the kynurenine (Kyn) pathway, is increasingly being recognized as an important microenvironmental factor suppressing antitumor immune responses. Tryptophan 87-90 indoleamine 2,3-dioxygenase 1 Homo sapiens 40-44 25788494-1 2015 PURPOSE: Indoleamine 2,3-dioxygenase 1 (IDO1: IDO), an enzyme catabolizing tryptophan (Trp) into the kynurenine (Kyn) pathway, is increasingly being recognized as an important microenvironmental factor suppressing antitumor immune responses. Tryptophan 87-90 indoleamine 2,3-dioxygenase 1 Homo sapiens 40-43 25605587-2 2015 DCs may express the tryptophan-catabolizing enzyme indolamine2,3-dioxygenase (IDO), which is an inducer of immune tolerance. Tryptophan 20-30 indoleamine 2,3-dioxygenase 1 Homo sapiens 51-76 25605587-2 2015 DCs may express the tryptophan-catabolizing enzyme indolamine2,3-dioxygenase (IDO), which is an inducer of immune tolerance. Tryptophan 20-30 indoleamine 2,3-dioxygenase 1 Homo sapiens 78-81 25605587-6 2015 Up-regulation of IDO1 gene expression was confirmed by the presence of enhanced kynurenine/tryptophan ratios in the plasma from chronic HCV patients. Tryptophan 91-101 indoleamine 2,3-dioxygenase 1 Homo sapiens 17-21 25865484-2 2015 The KP is initiated by the enzyme indoleamine 2,3-dioxygenase (IDO), which degrades tryptophan (TRP) into kynurenine (KYN) en route to neurotoxins. Tryptophan 84-94 indoleamine 2,3-dioxygenase 1 Homo sapiens 34-61 25865484-2 2015 The KP is initiated by the enzyme indoleamine 2,3-dioxygenase (IDO), which degrades tryptophan (TRP) into kynurenine (KYN) en route to neurotoxins. Tryptophan 84-94 indoleamine 2,3-dioxygenase 1 Homo sapiens 63-66 25865484-2 2015 The KP is initiated by the enzyme indoleamine 2,3-dioxygenase (IDO), which degrades tryptophan (TRP) into kynurenine (KYN) en route to neurotoxins. Tryptophan 96-99 indoleamine 2,3-dioxygenase 1 Homo sapiens 34-61 25865484-2 2015 The KP is initiated by the enzyme indoleamine 2,3-dioxygenase (IDO), which degrades tryptophan (TRP) into kynurenine (KYN) en route to neurotoxins. Tryptophan 96-99 indoleamine 2,3-dioxygenase 1 Homo sapiens 63-66 26114426-7 2015 Expression of IDO-1, KMO and QPRT correlated significantly with activation of the kynurenine pathway (kynurenine:tryptophan ratio), quinolinic acid concentration and production of the monocyte derived, pro-inflammatory immune response marker: neopterin. Tryptophan 113-123 indoleamine 2,3-dioxygenase 1 Homo sapiens 14-19 26110930-1 2015 BACKGROUND: Interferon gamma (IFN-gamma) production induces the transcription of indoleamine 2,3 dioxygenase (IDO) resulting in the reduction of T-cell activation and proliferation through the depletion of tryptophan and the elicitation of Treg lymphocytes. Tryptophan 206-216 indoleamine 2,3-dioxygenase 1 Homo sapiens 110-113 25698357-6 2015 In this context, we discuss the immunoregulatory pathway of tryptophan breakdown by enzyme indoleamine 2,3-dioxygenase (IDO), which represents a central regulatory hub for immune, metabolic, and neuroendocrine processes. Tryptophan 60-70 indoleamine 2,3-dioxygenase 1 Homo sapiens 91-118 25698357-6 2015 In this context, we discuss the immunoregulatory pathway of tryptophan breakdown by enzyme indoleamine 2,3-dioxygenase (IDO), which represents a central regulatory hub for immune, metabolic, and neuroendocrine processes. Tryptophan 60-70 indoleamine 2,3-dioxygenase 1 Homo sapiens 120-123 25698357-7 2015 Activation of IDO-mediated tryptophan metabolism is strongly redox-sensitive and is therefore susceptible to modulation by dietary components, phytochemicals, preservatives, and drugs. Tryptophan 27-37 indoleamine 2,3-dioxygenase 1 Homo sapiens 14-17 25639585-1 2015 Acute UVB exposure triggers inflammation leading to the induction of indoleamine 2,3 dioxygenase (IDO1), one of the first enzymes in the kynurenine pathway (KP) for tryptophan degradation. Tryptophan 165-175 indoleamine 2,3-dioxygenase 1 Homo sapiens 98-102 25787773-2 2015 Among many other factors, two regulatory defects that are present in most cancer cells are constitutive activation of Janus kinase (JAK)/signal transducer and activator of transcription (STAT) signaling pathway and the induction of indoleamine 2, 3-dioxygenase (IDO), an enzyme that catalyzes tryptophan degradation, through JAK/STAT signaling. Tryptophan 293-303 indoleamine 2,3-dioxygenase 1 Homo sapiens 232-260 25955018-5 2015 RESULTS: We found that the activity and expression of indoleamine 2,3-dioxygenase 1 (IDO1), which catalyzes the conversion of tryptophan into the immunosuppressive metabolite kynurenine, was higher in all the multidrug resistant cells analyzed and that IDO1 inhibition reduced the growth of drug-resistant tumors in immunocompetent animals. Tryptophan 126-136 indoleamine 2,3-dioxygenase 1 Homo sapiens 54-83 25955018-5 2015 RESULTS: We found that the activity and expression of indoleamine 2,3-dioxygenase 1 (IDO1), which catalyzes the conversion of tryptophan into the immunosuppressive metabolite kynurenine, was higher in all the multidrug resistant cells analyzed and that IDO1 inhibition reduced the growth of drug-resistant tumors in immunocompetent animals. Tryptophan 126-136 indoleamine 2,3-dioxygenase 1 Homo sapiens 85-89 25955018-5 2015 RESULTS: We found that the activity and expression of indoleamine 2,3-dioxygenase 1 (IDO1), which catalyzes the conversion of tryptophan into the immunosuppressive metabolite kynurenine, was higher in all the multidrug resistant cells analyzed and that IDO1 inhibition reduced the growth of drug-resistant tumors in immunocompetent animals. Tryptophan 126-136 indoleamine 2,3-dioxygenase 1 Homo sapiens 253-257 25897671-2 2015 Tryptophan is also needed in the production of kynurenine, a process mediated by the type I interferon (IFN)-regulated rate-limiting enzyme indoleamine 2,3-dioxygenase (IDO). Tryptophan 0-10 indoleamine 2,3-dioxygenase 1 Homo sapiens 169-172 25478733-1 2015 Tryptophan to kynurenine metabolism is controlled by three distinct dioxygenase enzymes: tryptophan 2,3-dioxygenase (TDO), indoleamine 2,3-dioxygenase 1 (IDO1), and indoleamine 2,3-dioxygenase 2 (IDO2). Tryptophan 0-10 indoleamine 2,3-dioxygenase 1 Homo sapiens 123-152 25478733-1 2015 Tryptophan to kynurenine metabolism is controlled by three distinct dioxygenase enzymes: tryptophan 2,3-dioxygenase (TDO), indoleamine 2,3-dioxygenase 1 (IDO1), and indoleamine 2,3-dioxygenase 2 (IDO2). Tryptophan 0-10 indoleamine 2,3-dioxygenase 1 Homo sapiens 154-158 25248875-1 2015 The immunomodulatory effects of indoleamine 2,3-dioxygenase (IDO) are ascribed to its ability to catalyze breakdown of the essential amino acid L-tryptophan. Tryptophan 144-156 indoleamine 2,3-dioxygenase 1 Homo sapiens 32-59 25248875-1 2015 The immunomodulatory effects of indoleamine 2,3-dioxygenase (IDO) are ascribed to its ability to catalyze breakdown of the essential amino acid L-tryptophan. Tryptophan 144-156 indoleamine 2,3-dioxygenase 1 Homo sapiens 61-64 25881064-3 2015 Tryptophan catabolism is initiated by either indoleamine 2,3-dioxygenase (IDO-1/-2) or tryptophan 2,3-dioxygenase 2 (TDO2), resulting in biostatic tryptophan starvation and l-kynurenine production, which participates in shaping the dynamic relationship of the host"s immune system with tumor cells. Tryptophan 0-10 indoleamine 2,3-dioxygenase 1 Homo sapiens 74-82 25667650-3 2015 IDO induces immunosuppression through the depletion of tryptophan and its downstream metabolites. Tryptophan 55-65 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 25949897-5 2015 Tryptophan breakdown confirmed the functional activity of IDO and was linked with increased PD-L1+ cytotoxic T-cells (p = 0.009), relative lymphopenia (p = 0.036), and a higher mDC/pDC ratio (p = 0.002). Tryptophan 0-10 indoleamine 2,3-dioxygenase 1 Homo sapiens 58-61 25712221-3 2015 Here we report on enzyme kinetics and catalytic mechanism of hIDO1, studied at varied levels of dioxygen (O2) and L-tryptophan (L-Trp). Tryptophan 114-126 indoleamine 2,3-dioxygenase 1 Homo sapiens 61-66 25712221-3 2015 Here we report on enzyme kinetics and catalytic mechanism of hIDO1, studied at varied levels of dioxygen (O2) and L-tryptophan (L-Trp). Tryptophan 128-133 indoleamine 2,3-dioxygenase 1 Homo sapiens 61-66 25712221-7 2015 One path, where O2 binds to ferrous hIDO1 first, is faster than the second route, which starts with the binding of L-Trp. Tryptophan 115-120 indoleamine 2,3-dioxygenase 1 Homo sapiens 36-41 25712221-8 2015 However, L-Trp complexation with free ferrous hIDO1 is more rapid than that of O2. Tryptophan 9-14 indoleamine 2,3-dioxygenase 1 Homo sapiens 46-51 25572287-1 2015 Indoleamine 2,3-dioxygenase (IDO) is an enzyme that catalyzes tryptophan degradation and induces immunosuppression. Tryptophan 62-72 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 25702628-1 2015 Indoleamine 2,3-dioxygenase (IDO) and tryptophan 2,3-dioxygenase (TDO) enzymes have independently evolved to catalyze the first step in the catabolism of tryptophan (L-Trp) through the kynurenine pathway. Tryptophan 166-171 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 25702628-1 2015 Indoleamine 2,3-dioxygenase (IDO) and tryptophan 2,3-dioxygenase (TDO) enzymes have independently evolved to catalyze the first step in the catabolism of tryptophan (L-Trp) through the kynurenine pathway. Tryptophan 166-171 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 25702628-6 2015 Interestingly, only mammalian IDO1s and fungal "typical" IDOs have high affinity and catalytic efficiency for L-Trp catabolism, comparable to TDOs. Tryptophan 110-115 indoleamine 2,3-dioxygenase 1 Homo sapiens 30-34 25702628-7 2015 We show that invertebrate IDO enzymes have low affinity and catalytic efficiency for L-Trp catabolism. Tryptophan 85-90 indoleamine 2,3-dioxygenase 1 Homo sapiens 26-29 25702628-8 2015 We suggest that the phylogenetic distribution of "low catalytic-efficiency IDOs" indicates the ancestral IDO also had low affinity and catalytic efficiency for L-Trp catabolism. Tryptophan 160-165 indoleamine 2,3-dioxygenase 1 Homo sapiens 75-78 25596911-6 2015 The rate of synthesis of NAD and niacin from tryptophan oxidation depends on the induction of the enzyme indoleamine 2,3-dioxygenase (IDO) by pro-inflammatory cytokines such as interferon-gamma. Tryptophan 45-55 indoleamine 2,3-dioxygenase 1 Homo sapiens 134-137 25596911-7 2015 Niacin synthesis is not limited by a decrease in tryptophan and excessive IDO activity may therefore lead to a decline in tryptophan levels. Tryptophan 122-132 indoleamine 2,3-dioxygenase 1 Homo sapiens 74-77 25994821-1 2015 In the last years an attention has been paid to the indoleamine 2,3-dioxygenase (IDO), an enzyme catabolising L-tryptophan to kynurenine. Tryptophan 110-122 indoleamine 2,3-dioxygenase 1 Homo sapiens 52-79 25714914-3 2015 Proteomic analysis of vaccine inoculated DCs revealed strong up-regulation of the tryptophan catabolic enzyme indoleamine 2, 3-dioxygenase (IDO1). Tryptophan 82-92 indoleamine 2,3-dioxygenase 1 Homo sapiens 140-144 25714914-6 2015 Determination of IDO1 activity in vaccinated DCs by measurement of tryptophan degradation products (kynurenines) showed increased tryptophan cleavage into N-formyl kynurenine. Tryptophan 67-77 indoleamine 2,3-dioxygenase 1 Homo sapiens 17-21 25714914-6 2015 Determination of IDO1 activity in vaccinated DCs by measurement of tryptophan degradation products (kynurenines) showed increased tryptophan cleavage into N-formyl kynurenine. Tryptophan 130-140 indoleamine 2,3-dioxygenase 1 Homo sapiens 17-21 26155395-1 2015 Tryptophan catabolism by indoleamine 2,3-dioxygenase (IDO1) is a physiological immunoregulatory mechanism often hijacked by tumors. Tryptophan 0-10 indoleamine 2,3-dioxygenase 1 Homo sapiens 54-58 25271151-1 2015 Tryptophan catabolism by indoleamine 2,3-dioxygenase 1 (IDO1) plays a key role in tumoral resistance to immune rejection. Tryptophan 0-10 indoleamine 2,3-dioxygenase 1 Homo sapiens 25-54 25271151-1 2015 Tryptophan catabolism by indoleamine 2,3-dioxygenase 1 (IDO1) plays a key role in tumoral resistance to immune rejection. Tryptophan 0-10 indoleamine 2,3-dioxygenase 1 Homo sapiens 56-60 25973066-1 2015 Indoleamine 2, 3-dioxygenase (IDO) is a rate-limiting enzyme for tryptophan metabolism inducing immune tolerance of tumors. Tryptophan 65-75 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-28 25973066-1 2015 Indoleamine 2, 3-dioxygenase (IDO) is a rate-limiting enzyme for tryptophan metabolism inducing immune tolerance of tumors. Tryptophan 65-75 indoleamine 2,3-dioxygenase 1 Homo sapiens 30-33 25602015-3 2015 Indoleamine 2,3-dioxygenase (IDO), an enzyme that mediates the conversion of tryptophan to kynurenine, has been linked to preeclampsia in humans, and is known to regulate T-cell activity and an endothelial-derived relaxing factor. Tryptophan 77-87 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 25692676-2 2015 IDO1, a catabolic enzyme of tryptophan, represents a critical molecule mediating immunomodulatory functions of MSCs. Tryptophan 28-38 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-4 25534866-1 2015 BACKGROUND AND AIM: Tryptophan (Trp) degradation via indoleamine (2,3)-dioxygenase (IDO), with consequent increased in kynurenine (Kyn) concentrations, has been proposed as marker of immune system activation. Tryptophan 20-30 indoleamine 2,3-dioxygenase 1 Homo sapiens 84-87 25534866-1 2015 BACKGROUND AND AIM: Tryptophan (Trp) degradation via indoleamine (2,3)-dioxygenase (IDO), with consequent increased in kynurenine (Kyn) concentrations, has been proposed as marker of immune system activation. Tryptophan 32-35 indoleamine 2,3-dioxygenase 1 Homo sapiens 84-87 25815143-1 2015 Indoleamine 2,3-dioxygenase (hIDO) is an enzyme that catalyzes the oxidative cleavage of the indole ring of l-tryptophan through the kynurenine pathway, thereby exerting immunosuppressive properties in inflammatory and tumoral tissues. Tryptophan 108-120 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-33 25994821-1 2015 In the last years an attention has been paid to the indoleamine 2,3-dioxygenase (IDO), an enzyme catabolising L-tryptophan to kynurenine. Tryptophan 110-122 indoleamine 2,3-dioxygenase 1 Homo sapiens 81-84 25599530-4 2015 Indoleamine 2,3-dioxygenase (IDO), an enzyme catalyzing the rate-limiting step in the kynurenine pathway of tryptophan degradation, is strongly induced by inflammation in several tissues, including the artery wall. Tryptophan 108-118 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 25599530-4 2015 Indoleamine 2,3-dioxygenase (IDO), an enzyme catalyzing the rate-limiting step in the kynurenine pathway of tryptophan degradation, is strongly induced by inflammation in several tissues, including the artery wall. Tryptophan 108-118 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 25599530-6 2015 This review provides an overview of the emerging field of the kynurenine pathway of tryptophan degradation in CVD, emphasizing the role of IDO-mediated tryptophan metabolism and its metabolites in the modulation of "classical" cardiovascular risk factors, such as hypertension, obesity, lipid metabolism, diabetes mellitus, and in the development of atherosclerotic CVD. Tryptophan 152-162 indoleamine 2,3-dioxygenase 1 Homo sapiens 139-142 26523229-12 2015 AA down-regulates IDO by inhibition of Trp entry into cells. Tryptophan 39-42 indoleamine 2,3-dioxygenase 1 Homo sapiens 18-21 25738401-3 2015 The activation of PBMCs was monitored by the breakdown of tryptophan to kynurenine via enzyme indoleamine 2,3-dioxygenase (IDO) and the production of the immune activation marker neopterin by GTP-cyclohydrolase I (GCH1). Tryptophan 58-68 indoleamine 2,3-dioxygenase 1 Homo sapiens 123-126 24916315-4 2014 Mechanism studies revealed that T cell-derived IFN-gamma and CD40 ligand (CD40L) induced the expression of indoleamine 2,3-dioxygenase (IDO) in OCs, which mediated the immunosuppressive function on T-cell proliferation through depleting tryptophan. Tryptophan 237-247 indoleamine 2,3-dioxygenase 1 Homo sapiens 107-134 24916315-4 2014 Mechanism studies revealed that T cell-derived IFN-gamma and CD40 ligand (CD40L) induced the expression of indoleamine 2,3-dioxygenase (IDO) in OCs, which mediated the immunosuppressive function on T-cell proliferation through depleting tryptophan. Tryptophan 237-247 indoleamine 2,3-dioxygenase 1 Homo sapiens 136-139 25477879-1 2014 IDO2 is a relative of IDO1 implicated in tryptophan catabolism and immune modulation but its specific contributions to normal physiology and pathophysiology are not known. Tryptophan 41-51 indoleamine 2,3-dioxygenase 1 Homo sapiens 22-26 25394548-0 2014 Heme-binding-mediated negative regulation of the tryptophan metabolic enzyme indoleamine 2,3-dioxygenase 1 (IDO1) by IDO2. Tryptophan 49-59 indoleamine 2,3-dioxygenase 1 Homo sapiens 77-106 25394548-0 2014 Heme-binding-mediated negative regulation of the tryptophan metabolic enzyme indoleamine 2,3-dioxygenase 1 (IDO1) by IDO2. Tryptophan 49-59 indoleamine 2,3-dioxygenase 1 Homo sapiens 108-112 25394548-4 2014 Cells co-expressing hIDO1 and hIDO2 showed reduced tryptophan metabolic activity compared with those expressing hIDO1 only. Tryptophan 51-61 indoleamine 2,3-dioxygenase 1 Homo sapiens 20-25 25394548-7 2014 Co-expression of hIDO1 and hIDO2 rescued the cell death induced by tryptophan-depletion through hIDO1 activity. Tryptophan 67-77 indoleamine 2,3-dioxygenase 1 Homo sapiens 17-22 25394548-7 2014 Co-expression of hIDO1 and hIDO2 rescued the cell death induced by tryptophan-depletion through hIDO1 activity. Tryptophan 67-77 indoleamine 2,3-dioxygenase 1 Homo sapiens 96-101 26881062-7 2015 This review provides a comprehensive update of significant biological functions of TRP metabolites along the kynurenine pathway and the complex regulation of LPS-induced IDO activation. Tryptophan 83-86 indoleamine 2,3-dioxygenase 1 Homo sapiens 170-173 26397892-6 2015 The enzyme Indoleamine 2,3 dioxygenase (IDO1) catalyzes the conversion of Trp into Kyn, the first and rate-limiting enzymatic step of the KP. Tryptophan 74-77 indoleamine 2,3-dioxygenase 1 Homo sapiens 40-44 25319657-5 2015 Among the immune inhibitory molecules expressed by DCs is indoleamine 2,3-dioxygenase (IDO), an enzyme that conveys immunosuppressive effects by degrading tryptophan, an essential amino acid required for T-cell proliferation and survival. Tryptophan 155-165 indoleamine 2,3-dioxygenase 1 Homo sapiens 58-85 25319657-5 2015 Among the immune inhibitory molecules expressed by DCs is indoleamine 2,3-dioxygenase (IDO), an enzyme that conveys immunosuppressive effects by degrading tryptophan, an essential amino acid required for T-cell proliferation and survival. Tryptophan 155-165 indoleamine 2,3-dioxygenase 1 Homo sapiens 87-90 25319657-6 2015 Depletion of tryptophan by IDO-positive DCs induces T-cell apoptosis and the conversion of naive CD4+ T cells into regulatory T cells that further suppress antitumor immunity. Tryptophan 13-23 indoleamine 2,3-dioxygenase 1 Homo sapiens 27-30 25540092-17 2014 SUMMARY: Etiological classification of depression expressed by peripheral (TPH1, TDO, IDO) and central (TPH2, KMO)enzymes of tryptophan metabolism may enable depression to be viewed as a clear box, with the inner components available for inspection and treatment. Tryptophan 125-135 indoleamine 2,3-dioxygenase 1 Homo sapiens 86-89 25541686-3 2014 Indoleamine 2,3 dioxygenase-1 (IDO1) is one of the most over-expressed genes in CD and mediates potent anti-inflammatory effects via tryptophan metabolism along the kynurenine pathway. Tryptophan 133-143 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-29 25541686-3 2014 Indoleamine 2,3 dioxygenase-1 (IDO1) is one of the most over-expressed genes in CD and mediates potent anti-inflammatory effects via tryptophan metabolism along the kynurenine pathway. Tryptophan 133-143 indoleamine 2,3-dioxygenase 1 Homo sapiens 31-35 25541686-8 2014 IDO1 enzyme activity was assessed by calculating the serum kynurenine to tryptophan ratio (K/T). Tryptophan 73-83 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-4 25566253-0 2014 Tryptophan Feeding of the IDO1-AhR Axis in Host-Microbial Symbiosis. Tryptophan 0-10 indoleamine 2,3-dioxygenase 1 Homo sapiens 26-30 25941578-1 2014 Indoleamine 2,3-dioxigenase 1 (IDO1) is the main enzyme that catalyzes the first, rate-limiting step of the so-called "kynurenine pathway", i.e., the metabolic cascade that converts the essential amino acid L-tryptophan (Trp) into L-kynurenine (Kyn). Tryptophan 221-224 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-29 25941578-1 2014 Indoleamine 2,3-dioxigenase 1 (IDO1) is the main enzyme that catalyzes the first, rate-limiting step of the so-called "kynurenine pathway", i.e., the metabolic cascade that converts the essential amino acid L-tryptophan (Trp) into L-kynurenine (Kyn). Tryptophan 221-224 indoleamine 2,3-dioxygenase 1 Homo sapiens 31-35 25941578-3 2014 At least in part, this reflects the capacity of IDO1 to restrict the microenvironmental availability of Trp and to favor the accumulation of Kyn and some of its derivatives. Tryptophan 104-107 indoleamine 2,3-dioxygenase 1 Homo sapiens 48-52 23174025-2 2014 Indoleamine-2,3-dioxygenase (IDO) is an enzyme that catabolises tryptophan - an essential amino acid critical for T cell proliferation. Tryptophan 64-74 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 23174025-2 2014 Indoleamine-2,3-dioxygenase (IDO) is an enzyme that catabolises tryptophan - an essential amino acid critical for T cell proliferation. Tryptophan 64-74 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 25400638-4 2014 Induction of IDO and IDO-mediated tryptophan catabolism, together with its downstream products such as kynurenine, is an important immunoregulatory mechanism underlying immunosuppression, tolerance, and immunity. Tryptophan 34-44 indoleamine 2,3-dioxygenase 1 Homo sapiens 21-24 25360135-1 2014 The evolutionary process has conferred a dual - enzymatic and signaling - function on the ancestral metabolic enzyme indoleamine 2,3-dioxygenase 1 (IDO1), which has long been known for converting the essential amino acid tryptophan (TRP) into neuroactive and immunoactive catabolites (kynurenines). Tryptophan 233-236 indoleamine 2,3-dioxygenase 1 Homo sapiens 117-146 25360135-1 2014 The evolutionary process has conferred a dual - enzymatic and signaling - function on the ancestral metabolic enzyme indoleamine 2,3-dioxygenase 1 (IDO1), which has long been known for converting the essential amino acid tryptophan (TRP) into neuroactive and immunoactive catabolites (kynurenines). Tryptophan 233-236 indoleamine 2,3-dioxygenase 1 Homo sapiens 148-152 25360135-2 2014 In addition to TRP catabolic activity, phosphorylated immunoreceptor tyrosine-based inhibitory motifs, present in the IDO1 protein, act as docking sites for different molecular partners, which activate positive (transcriptional) or negative (post-translational) modulation of IDO1 protein. Tryptophan 15-18 indoleamine 2,3-dioxygenase 1 Homo sapiens 118-122 25360135-3 2014 The ligand-operated transcription factor aryl hydrocarbon receptor (AhR) contributes to Ido1 transcription, and it can be operated by both exogenous and endogenous ligands, including l-kynurenine itself, the first byproduct of TRP catabolism. Tryptophan 227-230 indoleamine 2,3-dioxygenase 1 Homo sapiens 88-92 25346733-1 2014 Indoleamine 2,3-dioxygenase (IDO) and tryptophan 2,3-dioxygenase (TDO) are tryptophan-degrading enzymes that have independently evolved to catalyze the first step in tryptophan catabolism via the kynurenine pathway (KP). Tryptophan 75-85 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 25346733-1 2014 Indoleamine 2,3-dioxygenase (IDO) and tryptophan 2,3-dioxygenase (TDO) are tryptophan-degrading enzymes that have independently evolved to catalyze the first step in tryptophan catabolism via the kynurenine pathway (KP). Tryptophan 75-85 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 25346733-9 2014 This review analyzes the evolutionary convergence of IDO and TDO enzymes as tryptophan-catabolizing enzymes and the divergent evolution of IDO homologs to generate an enzyme family with diverse characteristics not possessed by TDO enzymes, with an emphasis on the immune system. Tryptophan 76-86 indoleamine 2,3-dioxygenase 1 Homo sapiens 53-56 24924152-1 2014 CD40/CD40-ligand (CD40L) signalling is a key stimulatory pathway which triggers the tryptophan (Trp) catabolizing enzyme IDO in dendritic cells and is immunosuppressive in cancer. Tryptophan 84-94 indoleamine 2,3-dioxygenase 1 Homo sapiens 121-124 24924152-1 2014 CD40/CD40-ligand (CD40L) signalling is a key stimulatory pathway which triggers the tryptophan (Trp) catabolizing enzyme IDO in dendritic cells and is immunosuppressive in cancer. Tryptophan 96-99 indoleamine 2,3-dioxygenase 1 Homo sapiens 121-124 24924152-2 2014 We reported IDO-induced Trp catabolism results in a T helper type 17 (Th17)/regulatory T cell (Treg ) imbalance, and favours microbial translocation in HIV chronic infection. Tryptophan 24-27 indoleamine 2,3-dioxygenase 1 Homo sapiens 12-15 24924152-13 2014 These results indicate that elevated sCD40L induces immunosuppression in HIV infection by mediating IDO-induced Trp catabolism and Treg expansion. Tryptophan 112-115 indoleamine 2,3-dioxygenase 1 Homo sapiens 100-103 25335725-2 2014 IDO activity can be determined using the tryptophan/kynurenine(Trp/Kyn)ratio. Tryptophan 41-51 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 25335725-2 2014 IDO activity can be determined using the tryptophan/kynurenine(Trp/Kyn)ratio. Tryptophan 63-66 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 24752804-1 2014 Indoleamine-2,3-dioxygenase-1 (IDO1) is a critical immunoregulatory enzyme responsible for the metabolism of tryptophan during inflammation and disease. Tryptophan 109-119 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-29 25091696-9 2014 Kynurenine levels were correlated with the expression of tryptophan-degrading enzyme (IDO1). Tryptophan 57-67 indoleamine 2,3-dioxygenase 1 Homo sapiens 86-90 25075025-1 2014 BACKGROUND/AIM: Indoleamine-2,3-dioxygenase (IDO) is a rate-limiting enzyme for tryptophan metabolism and plays an immunosuppressive role. Tryptophan 80-90 indoleamine 2,3-dioxygenase 1 Homo sapiens 16-43 25075025-1 2014 BACKGROUND/AIM: Indoleamine-2,3-dioxygenase (IDO) is a rate-limiting enzyme for tryptophan metabolism and plays an immunosuppressive role. Tryptophan 80-90 indoleamine 2,3-dioxygenase 1 Homo sapiens 45-48 24989637-1 2014 One of the most significant activities induced by interferon-gamma against intracellular pathogens is the induction of IDO (indoleamine 2,3-dioxygenase) expression, which subsequently results in the depletion of tryptophan. Tryptophan 212-222 indoleamine 2,3-dioxygenase 1 Homo sapiens 119-122 24989637-1 2014 One of the most significant activities induced by interferon-gamma against intracellular pathogens is the induction of IDO (indoleamine 2,3-dioxygenase) expression, which subsequently results in the depletion of tryptophan. Tryptophan 212-222 indoleamine 2,3-dioxygenase 1 Homo sapiens 124-151 24875753-1 2014 Indoleamine 2,3-dioxygenase-2 (IDO2) is one of three enzymes (alongside tryptophan 2,3-dioxygenase and indoleamine 2,3-dioxygenase (IDO1)) that catalyse dioxygenation of L-tryptophan as the first step in the kynurenine pathway. Tryptophan 170-182 indoleamine 2,3-dioxygenase 1 Homo sapiens 132-136 24875753-6 2014 Interestingly, IDO2 demonstrates behaviour distinct from that of IDO1 in terms of substrate specificity and affinity, such that we have identified tryptophan derivatives that are mutually exclusive as substrates for IDO1 and IDO2. Tryptophan 147-157 indoleamine 2,3-dioxygenase 1 Homo sapiens 65-69 24875753-6 2014 Interestingly, IDO2 demonstrates behaviour distinct from that of IDO1 in terms of substrate specificity and affinity, such that we have identified tryptophan derivatives that are mutually exclusive as substrates for IDO1 and IDO2. Tryptophan 147-157 indoleamine 2,3-dioxygenase 1 Homo sapiens 216-220 24768802-1 2014 UNLABELLED: Indoleamine 2,3-dioxygenase (IDO), an enzyme that is ubiquitously distributed in mammalian tissues and cells, converts tryptophan to kynurenine, and is also known as a key molecule that promotes apoptosis in lymphocytes and neurons. Tryptophan 131-141 indoleamine 2,3-dioxygenase 1 Homo sapiens 12-39 24768802-1 2014 UNLABELLED: Indoleamine 2,3-dioxygenase (IDO), an enzyme that is ubiquitously distributed in mammalian tissues and cells, converts tryptophan to kynurenine, and is also known as a key molecule that promotes apoptosis in lymphocytes and neurons. Tryptophan 131-141 indoleamine 2,3-dioxygenase 1 Homo sapiens 41-44 24732701-1 2014 Indoleamine 2,3-dioxygenase (IDO) is a rate-limiting enzyme for tryptophan catabolism that plays an important role in the induction of immune tolerance. Tryptophan 64-74 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 24732701-1 2014 Indoleamine 2,3-dioxygenase (IDO) is a rate-limiting enzyme for tryptophan catabolism that plays an important role in the induction of immune tolerance. Tryptophan 64-74 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 24752804-1 2014 Indoleamine-2,3-dioxygenase-1 (IDO1) is a critical immunoregulatory enzyme responsible for the metabolism of tryptophan during inflammation and disease. Tryptophan 109-119 indoleamine 2,3-dioxygenase 1 Homo sapiens 31-35 24711084-1 2014 Genetic and pharmacological studies of indoleamine 2,3-dioxygenase (IDO) have established this tryptophan catabolic enzyme as a central driver of malignant development and progression. Tryptophan 95-105 indoleamine 2,3-dioxygenase 1 Homo sapiens 39-66 24711084-1 2014 Genetic and pharmacological studies of indoleamine 2,3-dioxygenase (IDO) have established this tryptophan catabolic enzyme as a central driver of malignant development and progression. Tryptophan 95-105 indoleamine 2,3-dioxygenase 1 Homo sapiens 68-71 24807557-0 2014 T cell costimulation molecules CD80/86 inhibit osteoclast differentiation by inducing the IDO/tryptophan pathway. Tryptophan 94-104 indoleamine 2,3-dioxygenase 1 Homo sapiens 90-93 24982234-1 2014 BACKGROUND/AIM: Indoleamine 2, 3-dioxygenase (IDO) induction has been suggested as a mechanism by which immune activation affects tryptophan metabolism and serotonin synthesis in major depressive disorder (MDD). Tryptophan 130-140 indoleamine 2,3-dioxygenase 1 Homo sapiens 16-44 24982234-1 2014 BACKGROUND/AIM: Indoleamine 2, 3-dioxygenase (IDO) induction has been suggested as a mechanism by which immune activation affects tryptophan metabolism and serotonin synthesis in major depressive disorder (MDD). Tryptophan 130-140 indoleamine 2,3-dioxygenase 1 Homo sapiens 46-49 24983463-1 2014 BACKGROUND: Indoleamine 2,3-dioxygenase (IDO), which is mainly expressed in activated dendritic cells, catabolizes tryptophan to kynurenine and other downstream catabolites. Tryptophan 115-125 indoleamine 2,3-dioxygenase 1 Homo sapiens 12-39 24983463-1 2014 BACKGROUND: Indoleamine 2,3-dioxygenase (IDO), which is mainly expressed in activated dendritic cells, catabolizes tryptophan to kynurenine and other downstream catabolites. Tryptophan 115-125 indoleamine 2,3-dioxygenase 1 Homo sapiens 41-44 24983463-4 2014 METHODS: We measured systemic IDO activity (the ratio of plasma kynurenine to tryptophan) in HIV-infected patients before and after highly active antiretroviral therapy (HAART) and its association with a microbial translocation marker, soluble CD14 (sCD14). Tryptophan 78-88 indoleamine 2,3-dioxygenase 1 Homo sapiens 30-33 24845191-1 2014 BACKGROUND: Several studies have suggested that induced tryptophan (TRP) degradation through the kynurenine (KYN) pathway by the enzyme indoleamine 2,3-dioxygenase (IDO) is implicated in the relation between depression and inflammation. Tryptophan 56-66 indoleamine 2,3-dioxygenase 1 Homo sapiens 136-163 24845191-1 2014 BACKGROUND: Several studies have suggested that induced tryptophan (TRP) degradation through the kynurenine (KYN) pathway by the enzyme indoleamine 2,3-dioxygenase (IDO) is implicated in the relation between depression and inflammation. Tryptophan 56-66 indoleamine 2,3-dioxygenase 1 Homo sapiens 165-168 24845191-1 2014 BACKGROUND: Several studies have suggested that induced tryptophan (TRP) degradation through the kynurenine (KYN) pathway by the enzyme indoleamine 2,3-dioxygenase (IDO) is implicated in the relation between depression and inflammation. Tryptophan 68-71 indoleamine 2,3-dioxygenase 1 Homo sapiens 136-163 24845191-1 2014 BACKGROUND: Several studies have suggested that induced tryptophan (TRP) degradation through the kynurenine (KYN) pathway by the enzyme indoleamine 2,3-dioxygenase (IDO) is implicated in the relation between depression and inflammation. Tryptophan 68-71 indoleamine 2,3-dioxygenase 1 Homo sapiens 165-168 24976919-9 2014 During cellular immune response, interferon gamma-dependent pathways are activated such as tryptophan breakdown by the enzyme indoleamine 2,3-dioxygenase (IDO) in monocyte-derived macrophages, fibroblasts, endothelial and epithelial cells. Tryptophan 91-101 indoleamine 2,3-dioxygenase 1 Homo sapiens 126-153 24976919-9 2014 During cellular immune response, interferon gamma-dependent pathways are activated such as tryptophan breakdown by the enzyme indoleamine 2,3-dioxygenase (IDO) in monocyte-derived macrophages, fibroblasts, endothelial and epithelial cells. Tryptophan 91-101 indoleamine 2,3-dioxygenase 1 Homo sapiens 155-158 24798334-4 2014 Kynurenines are tryptophan oxidation products produced from the indoleamine 2,3-dioxygenase (IDO)-mediated kynurenine pathway and are present in the human lens. Tryptophan 16-26 indoleamine 2,3-dioxygenase 1 Homo sapiens 64-91 24798334-4 2014 Kynurenines are tryptophan oxidation products produced from the indoleamine 2,3-dioxygenase (IDO)-mediated kynurenine pathway and are present in the human lens. Tryptophan 16-26 indoleamine 2,3-dioxygenase 1 Homo sapiens 93-96 24911872-2 2014 IDO is an enzyme involved in the catabolism of tryptophan resulting in inhibition of T lymphocyte function. Tryptophan 47-57 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 24528145-2 2014 In cell-mediated immune activation, interferon (IFN)-gamma stimulates macrophage release of neopterin and increases the activity of indoleamine 2,3-dioxygenase (IDO), thereby stimulating tryptophan degradation along the kynurenine pathway. Tryptophan 187-197 indoleamine 2,3-dioxygenase 1 Homo sapiens 132-159 24528145-2 2014 In cell-mediated immune activation, interferon (IFN)-gamma stimulates macrophage release of neopterin and increases the activity of indoleamine 2,3-dioxygenase (IDO), thereby stimulating tryptophan degradation along the kynurenine pathway. Tryptophan 187-197 indoleamine 2,3-dioxygenase 1 Homo sapiens 161-164 24696473-9 2014 Activation of the tryptophan-catabolizing enzyme indoleamine 2,3-dioxygenase (IDO) in cancer tissues facilitates immune escape by the impairment of CTL functions. Tryptophan 18-28 indoleamine 2,3-dioxygenase 1 Homo sapiens 49-76 24696473-9 2014 Activation of the tryptophan-catabolizing enzyme indoleamine 2,3-dioxygenase (IDO) in cancer tissues facilitates immune escape by the impairment of CTL functions. Tryptophan 18-28 indoleamine 2,3-dioxygenase 1 Homo sapiens 78-81 24807557-7 2014 Mechanistically, engagement of CD80/86 by CTLA-4 induced activation of the enzyme indoleamine 2,3-dioxygenase (IDO) in osteoclast precursors, which degraded tryptophan and promoted apoptosis. Tryptophan 157-167 indoleamine 2,3-dioxygenase 1 Homo sapiens 111-114 24145120-4 2014 Microarray data analysis revealed the Trp pathway as the only pathway upregulated significantly in all types of studied TICs, with increased levels of indoleamine-2,3-dioxygenase-1 (IDO1), the rate-limiting enzyme of Trp metabolism along the kynurenine pathway. Tryptophan 38-41 indoleamine 2,3-dioxygenase 1 Homo sapiens 182-186 24530381-1 2014 Indoleamine 2,3-dioxygenase1 (IDO1) is the rate-limiting enzyme in the kynurenine pathway that converts l-tryptophan to l-kynurenine. Tryptophan 104-116 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-28 24530381-1 2014 Indoleamine 2,3-dioxygenase1 (IDO1) is the rate-limiting enzyme in the kynurenine pathway that converts l-tryptophan to l-kynurenine. Tryptophan 104-116 indoleamine 2,3-dioxygenase 1 Homo sapiens 30-34 24710677-3 2014 A dysfunction in the activation of the type 1 immune response is associated with decreased activity of the key enzyme of the tryptophan/kynurenine metabolism, indolamine-2.3-dioxygenase (IDO), results in a higher production of kynurenine acid (KYNA)--an N-methyl-D-aspartate antagonist--in the central nervous system (CNS) and decreased glutamatergic neurotransmission. Tryptophan 125-135 indoleamine 2,3-dioxygenase 1 Homo sapiens 159-185 24710677-3 2014 A dysfunction in the activation of the type 1 immune response is associated with decreased activity of the key enzyme of the tryptophan/kynurenine metabolism, indolamine-2.3-dioxygenase (IDO), results in a higher production of kynurenine acid (KYNA)--an N-methyl-D-aspartate antagonist--in the central nervous system (CNS) and decreased glutamatergic neurotransmission. Tryptophan 125-135 indoleamine 2,3-dioxygenase 1 Homo sapiens 187-190 24220289-9 2014 CONCLUSIONS: Indoleamine 2,3-dioxygenase-1-mediated tryptophan catabolism may contribute to depression symptom severity among HIV-infected individuals, particularly among those with poor dietary protein intake. Tryptophan 52-62 indoleamine 2,3-dioxygenase 1 Homo sapiens 13-42 23877570-2 2014 Here, we hypothesize that the improved healing quality is due to extracellular matrix modulatory effect of IDO-mediated tryptophan metabolites. Tryptophan 120-130 indoleamine 2,3-dioxygenase 1 Homo sapiens 107-110 24587363-1 2014 Indoleamine 2,3-dioxygenase (IDO) is a tryptophan-degrading enzyme known to suppress antitumor CD8(+) T cells (TCD8). Tryptophan 39-49 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 24587363-1 2014 Indoleamine 2,3-dioxygenase (IDO) is a tryptophan-degrading enzyme known to suppress antitumor CD8(+) T cells (TCD8). Tryptophan 39-49 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 25346938-2 2014 Disturbances of tryptophan (TRP) metabolism might contribute to development of IFN-alpha-associated depression due to IFN-alpha-induced activation of indoleamine 2,3-dioxygenase (IDO), a rate-limiting enzyme of TRP-kynurenine (KYN) metabolism. Tryptophan 16-26 indoleamine 2,3-dioxygenase 1 Homo sapiens 150-177 25346938-2 2014 Disturbances of tryptophan (TRP) metabolism might contribute to development of IFN-alpha-associated depression due to IFN-alpha-induced activation of indoleamine 2,3-dioxygenase (IDO), a rate-limiting enzyme of TRP-kynurenine (KYN) metabolism. Tryptophan 28-31 indoleamine 2,3-dioxygenase 1 Homo sapiens 150-177 25346938-2 2014 Disturbances of tryptophan (TRP) metabolism might contribute to development of IFN-alpha-associated depression due to IFN-alpha-induced activation of indoleamine 2,3-dioxygenase (IDO), a rate-limiting enzyme of TRP-kynurenine (KYN) metabolism. Tryptophan 28-31 indoleamine 2,3-dioxygenase 1 Homo sapiens 179-182 25346938-4 2014 The present study assessed KYN/TRP ratio (KTR) as a marker of IDO activity in American Caucasian HCV patients awaiting IFN-alpha treatment. Tryptophan 31-34 indoleamine 2,3-dioxygenase 1 Homo sapiens 62-65 23940074-2 2014 Several mechanisms, such as IDO1-mediated tryptophan (Trp) depletion, but also accumulation of Trp catabolites, have been associated with the antimicrobial effects of IDO(+) cells. Tryptophan 42-52 indoleamine 2,3-dioxygenase 1 Homo sapiens 28-32 23940074-2 2014 Several mechanisms, such as IDO1-mediated tryptophan (Trp) depletion, but also accumulation of Trp catabolites, have been associated with the antimicrobial effects of IDO(+) cells. Tryptophan 54-57 indoleamine 2,3-dioxygenase 1 Homo sapiens 28-32 23940074-8 2014 Surprisingly, the IDO1-mediated antimicrobial effect is less prominent when Trp is depleted, but can be significantly amplified by tryptophan excess, leading to increased accumulation of catabolites that promote enhanced bactericidal activity. Tryptophan 76-79 indoleamine 2,3-dioxygenase 1 Homo sapiens 18-22 23940074-8 2014 Surprisingly, the IDO1-mediated antimicrobial effect is less prominent when Trp is depleted, but can be significantly amplified by tryptophan excess, leading to increased accumulation of catabolites that promote enhanced bactericidal activity. Tryptophan 131-141 indoleamine 2,3-dioxygenase 1 Homo sapiens 18-22 24517146-1 2014 CONTEXT: Indoleamine 2,3-dioxygenase 1 (IDO1) is a single chain oxidoreductase that catalyzes tryptophan degradation to kynurenine. Tryptophan 94-104 indoleamine 2,3-dioxygenase 1 Homo sapiens 9-38 24517146-1 2014 CONTEXT: Indoleamine 2,3-dioxygenase 1 (IDO1) is a single chain oxidoreductase that catalyzes tryptophan degradation to kynurenine. Tryptophan 94-104 indoleamine 2,3-dioxygenase 1 Homo sapiens 40-44 24483723-1 2014 Immune cells utilize the IDO enzymatic conversion of trp to kyn to determine T-cell activation vs. anergy/apoptosis. Tryptophan 53-56 indoleamine 2,3-dioxygenase 1 Homo sapiens 25-28 24483723-5 2014 IDO levels were measured by tandem mass spectrometry and expressed as kyn/trp ratios. Tryptophan 74-77 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 24903009-2 2014 Indoleamine 2,3-dioxygenase 1 (IDO1) is an interferon (IFN)-gamma-inducible enzyme that degrades tryptophan into kynurenine, which, in turn, inhibits effector T cells and promotes regulatory T-cell (Treg) differentiation. Tryptophan 97-107 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-29 24903009-2 2014 Indoleamine 2,3-dioxygenase 1 (IDO1) is an interferon (IFN)-gamma-inducible enzyme that degrades tryptophan into kynurenine, which, in turn, inhibits effector T cells and promotes regulatory T-cell (Treg) differentiation. Tryptophan 97-107 indoleamine 2,3-dioxygenase 1 Homo sapiens 31-35 24145120-4 2014 Microarray data analysis revealed the Trp pathway as the only pathway upregulated significantly in all types of studied TICs, with increased levels of indoleamine-2,3-dioxygenase-1 (IDO1), the rate-limiting enzyme of Trp metabolism along the kynurenine pathway. Tryptophan 217-220 indoleamine 2,3-dioxygenase 1 Homo sapiens 151-180 24145120-4 2014 Microarray data analysis revealed the Trp pathway as the only pathway upregulated significantly in all types of studied TICs, with increased levels of indoleamine-2,3-dioxygenase-1 (IDO1), the rate-limiting enzyme of Trp metabolism along the kynurenine pathway. Tryptophan 217-220 indoleamine 2,3-dioxygenase 1 Homo sapiens 182-186 24184687-2 2014 Inflammatory molecules such as pro-inflammatory cytokines could enhance the activity of the indoleamine 2,3-dioxygenase (IDO) enzyme which is the first rate-limiting enzyme of the tryptophan degradation pathway, the kynurenine pathway. Tryptophan 180-190 indoleamine 2,3-dioxygenase 1 Homo sapiens 92-119 24184687-2 2014 Inflammatory molecules such as pro-inflammatory cytokines could enhance the activity of the indoleamine 2,3-dioxygenase (IDO) enzyme which is the first rate-limiting enzyme of the tryptophan degradation pathway, the kynurenine pathway. Tryptophan 180-190 indoleamine 2,3-dioxygenase 1 Homo sapiens 121-124 24717869-3 2014 Indoleamine 2,3-dioxygenase (IDO) is an enzyme involved in the catabolism of the essential amino acid tryptophan (Trp) to kynurenine (Kyn). Tryptophan 114-117 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 24717869-3 2014 Indoleamine 2,3-dioxygenase (IDO) is an enzyme involved in the catabolism of the essential amino acid tryptophan (Trp) to kynurenine (Kyn). Tryptophan 114-117 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 24717869-9 2014 Serum IDO activity was evaluated by assessing the Kyn/Trp ratio by liquid chromatography. Tryptophan 54-57 indoleamine 2,3-dioxygenase 1 Homo sapiens 6-9 24376420-3 2013 The pro-inflammatory cytokine interferon-gamma (IFN-gamma) and related biochemical pathways like tryptophan breakdown by indoleamine 2,3-dioxygenase (IDO) and neopterin formation are deeply involved in their pathogenesis. Tryptophan 97-107 indoleamine 2,3-dioxygenase 1 Homo sapiens 121-148 25292102-6 2014 In addition, inhibition of IDO activity by the IDO inhibitor 1-MT or tryptophan significantly reduced IFN-gamma-induced apoptosis and death receptor 5 (DR5) expression, which suggests that IDO enzymatic activity plays an important role in the anti-NSCLC cancer effect of IFN-gamma. Tryptophan 69-79 indoleamine 2,3-dioxygenase 1 Homo sapiens 27-30 24782599-1 2014 Human mesenchymal stromal cells (MSC) possess immunosuppressive and antimicrobial effects that are partly mediated by the tryptophan-catabolizing enzyme indoleamine-2,3-dioxygenase (IDO). Tryptophan 122-132 indoleamine 2,3-dioxygenase 1 Homo sapiens 153-180 24782599-1 2014 Human mesenchymal stromal cells (MSC) possess immunosuppressive and antimicrobial effects that are partly mediated by the tryptophan-catabolizing enzyme indoleamine-2,3-dioxygenase (IDO). Tryptophan 122-132 indoleamine 2,3-dioxygenase 1 Homo sapiens 182-185 24697939-12 2014 CONCLUSIONS: Suppressive effect of co-injection of IDO(+)DC and TC is much more effective than administration of IDO(+)DC or TC alone, which suggests that IDO achieved immune suppressive effect through the pathway of tryptophan depletion and accumulation of TC. Tryptophan 217-227 indoleamine 2,3-dioxygenase 1 Homo sapiens 51-54 24697114-2 2014 Indolamine 2,3-dioxygenase, a tryptophan catabolising enzyme, is up-regulated with various inflammatory stimuli. Tryptophan 30-40 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-26 24697114-6 2014 Serum tryptophan and kynurenine levels were determined with HPLC-UV method, and kynurenine/tryptophan ratio was evaluated as IDO activity. Tryptophan 91-101 indoleamine 2,3-dioxygenase 1 Homo sapiens 125-128 24102581-3 2014 Here, we explore the immunomodulatory effects of hAFSCs derived from human amniotic fluid and evaluate the role of IL-10 and the tryptophan-catabolizing enzyme indoleamine 2,3-dioxygenase (IDO) in mediating the immunosuppressive actions of hAFSCs. Tryptophan 129-139 indoleamine 2,3-dioxygenase 1 Homo sapiens 160-187 24988959-2 2014 The enzyme indoleamine 2,3-dioxygenase (IDO) catalyzes the initial step of the kynurenine pathway that converts tryptophan to kynurenine metabolites. Tryptophan 112-122 indoleamine 2,3-dioxygenase 1 Homo sapiens 11-38 24988959-2 2014 The enzyme indoleamine 2,3-dioxygenase (IDO) catalyzes the initial step of the kynurenine pathway that converts tryptophan to kynurenine metabolites. Tryptophan 112-122 indoleamine 2,3-dioxygenase 1 Homo sapiens 40-43 24376420-3 2013 The pro-inflammatory cytokine interferon-gamma (IFN-gamma) and related biochemical pathways like tryptophan breakdown by indoleamine 2,3-dioxygenase (IDO) and neopterin formation are deeply involved in their pathogenesis. Tryptophan 97-107 indoleamine 2,3-dioxygenase 1 Homo sapiens 150-153 24376420-8 2013 The influence of cacao extracts on IDO activity could be of particular relevance for some of the beneficial health effects ascribed to cacao: tryptophan breakdown by IDO is strongly involved in immunoregulation, and the diminished availability of tryptophan limits the biosynthesis of neurotransmitter serotonin. Tryptophan 142-152 indoleamine 2,3-dioxygenase 1 Homo sapiens 35-38 24376420-8 2013 The influence of cacao extracts on IDO activity could be of particular relevance for some of the beneficial health effects ascribed to cacao: tryptophan breakdown by IDO is strongly involved in immunoregulation, and the diminished availability of tryptophan limits the biosynthesis of neurotransmitter serotonin. Tryptophan 142-152 indoleamine 2,3-dioxygenase 1 Homo sapiens 166-169 24376420-8 2013 The influence of cacao extracts on IDO activity could be of particular relevance for some of the beneficial health effects ascribed to cacao: tryptophan breakdown by IDO is strongly involved in immunoregulation, and the diminished availability of tryptophan limits the biosynthesis of neurotransmitter serotonin. Tryptophan 247-257 indoleamine 2,3-dioxygenase 1 Homo sapiens 35-38 24105077-3 2013 Three enzymes are now known to catalyze the first and rate-limiting step in the catabolism of tryptophan along this pathway: tryptophan 2,3-dioxygenase (TDO) and indoleamine 2,3-dioxygenase (IDO, subsequently named IDO1), both of which have been extensively studied, and a third enzyme, indoleamine 2,3-dioxygenase 2 (IDO2), a relative newcomer to the kynurenine pathway field. Tryptophan 94-104 indoleamine 2,3-dioxygenase 1 Homo sapiens 162-189 24105077-3 2013 Three enzymes are now known to catalyze the first and rate-limiting step in the catabolism of tryptophan along this pathway: tryptophan 2,3-dioxygenase (TDO) and indoleamine 2,3-dioxygenase (IDO, subsequently named IDO1), both of which have been extensively studied, and a third enzyme, indoleamine 2,3-dioxygenase 2 (IDO2), a relative newcomer to the kynurenine pathway field. Tryptophan 94-104 indoleamine 2,3-dioxygenase 1 Homo sapiens 191-194 24105077-3 2013 Three enzymes are now known to catalyze the first and rate-limiting step in the catabolism of tryptophan along this pathway: tryptophan 2,3-dioxygenase (TDO) and indoleamine 2,3-dioxygenase (IDO, subsequently named IDO1), both of which have been extensively studied, and a third enzyme, indoleamine 2,3-dioxygenase 2 (IDO2), a relative newcomer to the kynurenine pathway field. Tryptophan 94-104 indoleamine 2,3-dioxygenase 1 Homo sapiens 215-219 24355457-27 2013 Elevated Kyn/Trp ratio is suggested to mirror IDO activity. Tryptophan 13-16 indoleamine 2,3-dioxygenase 1 Homo sapiens 46-49 23942267-1 2013 AIMS: Indoleamine 2,3-dioxygenase (IDO) inhibits T-cell proliferation by catalyzing the conversion of l-tryptophan to l-kynurenine. Tryptophan 102-114 indoleamine 2,3-dioxygenase 1 Homo sapiens 6-33 24393854-2 2013 IDO activity can be determined by the tryptophan( Trp)/kynurenine( Kyn) ratio. Tryptophan 38-48 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 24393854-2 2013 IDO activity can be determined by the tryptophan( Trp)/kynurenine( Kyn) ratio. Tryptophan 50-53 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 24125458-2 2013 The enzyme indoleamine 2,3-dioxygenase (IDO) catalyses tryptophan through the kynurenine pathway, and is considered a crucial immunoregulatory molecule mediating immune tolerance. Tryptophan 55-65 indoleamine 2,3-dioxygenase 1 Homo sapiens 11-38 24125458-2 2013 The enzyme indoleamine 2,3-dioxygenase (IDO) catalyses tryptophan through the kynurenine pathway, and is considered a crucial immunoregulatory molecule mediating immune tolerance. Tryptophan 55-65 indoleamine 2,3-dioxygenase 1 Homo sapiens 40-43 24147117-1 2013 Tryptophan (Trp) catabolism into immunosuppressive kynurenine (Kyn) by indoleamine 2,3-dioxygenase (IDO) was previously linked to Th17/Treg differentiation and immune activation. Tryptophan 0-10 indoleamine 2,3-dioxygenase 1 Homo sapiens 71-98 24147117-1 2013 Tryptophan (Trp) catabolism into immunosuppressive kynurenine (Kyn) by indoleamine 2,3-dioxygenase (IDO) was previously linked to Th17/Treg differentiation and immune activation. Tryptophan 0-10 indoleamine 2,3-dioxygenase 1 Homo sapiens 100-103 24147117-1 2013 Tryptophan (Trp) catabolism into immunosuppressive kynurenine (Kyn) by indoleamine 2,3-dioxygenase (IDO) was previously linked to Th17/Treg differentiation and immune activation. Tryptophan 12-15 indoleamine 2,3-dioxygenase 1 Homo sapiens 71-98 24147117-1 2013 Tryptophan (Trp) catabolism into immunosuppressive kynurenine (Kyn) by indoleamine 2,3-dioxygenase (IDO) was previously linked to Th17/Treg differentiation and immune activation. Tryptophan 12-15 indoleamine 2,3-dioxygenase 1 Homo sapiens 100-103 23488665-1 2013 BACKGROUND AND OBJECTIVE: Indoleamine 2,3-dioxygenase (IDO) is a tryptophan-oxidizing enzyme with immune-inhibitory effects. Tryptophan 65-75 indoleamine 2,3-dioxygenase 1 Homo sapiens 26-53 23488665-1 2013 BACKGROUND AND OBJECTIVE: Indoleamine 2,3-dioxygenase (IDO) is a tryptophan-oxidizing enzyme with immune-inhibitory effects. Tryptophan 65-75 indoleamine 2,3-dioxygenase 1 Homo sapiens 55-58 23882022-2 2013 The antiviral tryptophan-catabolising enzyme indoleamine 2,3-dioxygenase (IDO) is induced by interferon-gamma and suppressed by Th2 mediators interleukin (IL)-4 and IL-13. Tryptophan 14-24 indoleamine 2,3-dioxygenase 1 Homo sapiens 45-72 23882022-2 2013 The antiviral tryptophan-catabolising enzyme indoleamine 2,3-dioxygenase (IDO) is induced by interferon-gamma and suppressed by Th2 mediators interleukin (IL)-4 and IL-13. Tryptophan 14-24 indoleamine 2,3-dioxygenase 1 Homo sapiens 74-77 23942267-1 2013 AIMS: Indoleamine 2,3-dioxygenase (IDO) inhibits T-cell proliferation by catalyzing the conversion of l-tryptophan to l-kynurenine. Tryptophan 102-114 indoleamine 2,3-dioxygenase 1 Homo sapiens 35-38 23879623-1 2013 Indoleamine 2,3-dioxygenase 1 (IDO1), the rate-limiting enzyme of tryptophan catabolism, has been strongly associated with the progression of malignancy and poor survival in melanoma patients. Tryptophan 66-76 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-29 23879623-1 2013 Indoleamine 2,3-dioxygenase 1 (IDO1), the rate-limiting enzyme of tryptophan catabolism, has been strongly associated with the progression of malignancy and poor survival in melanoma patients. Tryptophan 66-76 indoleamine 2,3-dioxygenase 1 Homo sapiens 31-35 23879623-3 2013 Here, in a scenario involving the tryptophan catabolism, we report that melatonin biosynthesis is driven by 1-methyl-tryptophan (1-MT), a competitive inhibitor of IDO1, in human fibroblasts, melanocytes and melanoma cells. Tryptophan 34-44 indoleamine 2,3-dioxygenase 1 Homo sapiens 163-167 23751345-1 2013 The hemoprotein indoleamine 2,3-dioxygenase-1 (IDO1) is the first and rate-limiting enzyme in mammalian tryptophan metabolism. Tryptophan 104-114 indoleamine 2,3-dioxygenase 1 Homo sapiens 16-45 23798565-6 2013 Subsequent depletion of tryptophan by IDO leads to termination of the donor T-cell response prior to development of effector CTL. Tryptophan 24-34 indoleamine 2,3-dioxygenase 1 Homo sapiens 38-41 23823655-4 2013 The indoleamine 2,3-dioxygenase activity was assessed by mass spectrometry assays using the ratio of product L-kynurenine (kyn) to substrate tryptophan (trp). Tryptophan 141-151 indoleamine 2,3-dioxygenase 1 Homo sapiens 4-31 23823655-4 2013 The indoleamine 2,3-dioxygenase activity was assessed by mass spectrometry assays using the ratio of product L-kynurenine (kyn) to substrate tryptophan (trp). Tryptophan 153-156 indoleamine 2,3-dioxygenase 1 Homo sapiens 4-31 23973990-1 2013 Indoleamine 2,3-dioxygenase 1 (IDO1) metabolizes L-tryptophan to kynurenines (KYN), inducing T-cell suppression either directly or by altering antigen-presenting-cell function. Tryptophan 49-61 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-29 23973990-1 2013 Indoleamine 2,3-dioxygenase 1 (IDO1) metabolizes L-tryptophan to kynurenines (KYN), inducing T-cell suppression either directly or by altering antigen-presenting-cell function. Tryptophan 49-61 indoleamine 2,3-dioxygenase 1 Homo sapiens 31-35 23922504-1 2013 Indoleamine 2,3-dioxygenase (IDO) is the first and rate-limiting step along the kynurenine pathway and is thought to play a key role in immune homeostasis through depletion of tryptophan and accumulation of kynurenines. Tryptophan 176-186 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 23922504-1 2013 Indoleamine 2,3-dioxygenase (IDO) is the first and rate-limiting step along the kynurenine pathway and is thought to play a key role in immune homeostasis through depletion of tryptophan and accumulation of kynurenines. Tryptophan 176-186 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 23751345-1 2013 The hemoprotein indoleamine 2,3-dioxygenase-1 (IDO1) is the first and rate-limiting enzyme in mammalian tryptophan metabolism. Tryptophan 104-114 indoleamine 2,3-dioxygenase 1 Homo sapiens 47-51 23548750-1 2013 Indoleamine 2,3-dioxygenase (IDO) is a tryptophan-degrading enzyme and is found in animals, fungi and bacteria. Tryptophan 39-49 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 23754498-1 2013 Indoleamine 2,3-dioxygenase (IDO) is an interferon-gamma (IFN-gamma)-induced tryptophan-degrading enzyme, producing kynurenine (KYN) that participates in the mechanism of tumor immune tolerance. Tryptophan 77-87 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 23754498-1 2013 Indoleamine 2,3-dioxygenase (IDO) is an interferon-gamma (IFN-gamma)-induced tryptophan-degrading enzyme, producing kynurenine (KYN) that participates in the mechanism of tumor immune tolerance. Tryptophan 77-87 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 23754498-3 2013 The aim of this study was to identify whether the metabolites originated from the competitive routes of tryptophan metabolism, such as the serotonergic or N, N-dimethyltryptamine (DMT) pathways, have inhibitory effects on recombinant human IDO (rhIDO) activity. Tryptophan 104-114 indoleamine 2,3-dioxygenase 1 Homo sapiens 240-243 23548750-1 2013 Indoleamine 2,3-dioxygenase (IDO) is a tryptophan-degrading enzyme and is found in animals, fungi and bacteria. Tryptophan 39-49 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 23548750-14 2013 Our study suggests that some fungal IDO enzymes function in tryptophan metabolism and NAD(+) supply. Tryptophan 60-70 indoleamine 2,3-dioxygenase 1 Homo sapiens 36-39 23548750-15 2013 In contrast, other IDO enzymes do not possess sufficient Trp-metabolising capacity to supply NAD(+). Tryptophan 57-60 indoleamine 2,3-dioxygenase 1 Homo sapiens 19-22 23531160-6 2013 These, in turns, would cause the activation of the indoleamine 2,3 dioxygenase (IDO), with subsequent production of tryptophan (TRP) catabolites along the IDO pathway (TRYCATs) and decreased availability of TRP and 5-HT. Tryptophan 116-126 indoleamine 2,3-dioxygenase 1 Homo sapiens 51-78 23620105-3 2013 Among these factors is the tryptophan-degrading enzyme indoleamine 2,3-dioxygenase (IDO). Tryptophan 27-37 indoleamine 2,3-dioxygenase 1 Homo sapiens 55-82 23620105-3 2013 Among these factors is the tryptophan-degrading enzyme indoleamine 2,3-dioxygenase (IDO). Tryptophan 27-37 indoleamine 2,3-dioxygenase 1 Homo sapiens 84-87 23426156-1 2013 BACKGROUND: : Indoleamine 2,3-dioxygenase (IDO) is a tryptophan catabolic enzyme involved in immune tolerance and tumor immune escape processes. Tryptophan 53-63 indoleamine 2,3-dioxygenase 1 Homo sapiens 14-41 23426156-1 2013 BACKGROUND: : Indoleamine 2,3-dioxygenase (IDO) is a tryptophan catabolic enzyme involved in immune tolerance and tumor immune escape processes. Tryptophan 53-63 indoleamine 2,3-dioxygenase 1 Homo sapiens 43-46 23720663-8 2013 Contributing to the poor success of past approaches is the expression of indoleamine 2,3-dioxygenase 1 (IDO), a tryptophan catabolizing enzyme overexpressed in GBM, and critically involved in regulating tumor-infiltrating Treg levels. Tryptophan 112-122 indoleamine 2,3-dioxygenase 1 Homo sapiens 73-102 23720663-8 2013 Contributing to the poor success of past approaches is the expression of indoleamine 2,3-dioxygenase 1 (IDO), a tryptophan catabolizing enzyme overexpressed in GBM, and critically involved in regulating tumor-infiltrating Treg levels. Tryptophan 112-122 indoleamine 2,3-dioxygenase 1 Homo sapiens 104-107 23691219-1 2013 Human fibroblasts provide immunosuppressive functions that are partly mediated by the tryptophan-catabolizing enzyme indoleamine-2,3-dioxygenase (IDO). Tryptophan 86-96 indoleamine 2,3-dioxygenase 1 Homo sapiens 117-144 23691219-1 2013 Human fibroblasts provide immunosuppressive functions that are partly mediated by the tryptophan-catabolizing enzyme indoleamine-2,3-dioxygenase (IDO). Tryptophan 86-96 indoleamine 2,3-dioxygenase 1 Homo sapiens 146-149 23675474-2 2013 In human cells the interferon-gamma (IFN-gamma) inducible enzyme indoleamine 2,3-dioxygenase (IDO) reduces local tryptophan levels and is therefore able to mediate broad-spectrum effector functions: IDO activity restricts the growth of various clinically relevant pathogens such as bacteria, parasites and viruses. Tryptophan 113-123 indoleamine 2,3-dioxygenase 1 Homo sapiens 65-92 23675474-2 2013 In human cells the interferon-gamma (IFN-gamma) inducible enzyme indoleamine 2,3-dioxygenase (IDO) reduces local tryptophan levels and is therefore able to mediate broad-spectrum effector functions: IDO activity restricts the growth of various clinically relevant pathogens such as bacteria, parasites and viruses. Tryptophan 113-123 indoleamine 2,3-dioxygenase 1 Homo sapiens 94-97 23675474-2 2013 In human cells the interferon-gamma (IFN-gamma) inducible enzyme indoleamine 2,3-dioxygenase (IDO) reduces local tryptophan levels and is therefore able to mediate broad-spectrum effector functions: IDO activity restricts the growth of various clinically relevant pathogens such as bacteria, parasites and viruses. Tryptophan 113-123 indoleamine 2,3-dioxygenase 1 Homo sapiens 199-202 23531160-6 2013 These, in turns, would cause the activation of the indoleamine 2,3 dioxygenase (IDO), with subsequent production of tryptophan (TRP) catabolites along the IDO pathway (TRYCATs) and decreased availability of TRP and 5-HT. Tryptophan 116-126 indoleamine 2,3-dioxygenase 1 Homo sapiens 80-83 23531160-6 2013 These, in turns, would cause the activation of the indoleamine 2,3 dioxygenase (IDO), with subsequent production of tryptophan (TRP) catabolites along the IDO pathway (TRYCATs) and decreased availability of TRP and 5-HT. Tryptophan 116-126 indoleamine 2,3-dioxygenase 1 Homo sapiens 155-158 23531160-6 2013 These, in turns, would cause the activation of the indoleamine 2,3 dioxygenase (IDO), with subsequent production of tryptophan (TRP) catabolites along the IDO pathway (TRYCATs) and decreased availability of TRP and 5-HT. Tryptophan 128-131 indoleamine 2,3-dioxygenase 1 Homo sapiens 51-78 23531160-6 2013 These, in turns, would cause the activation of the indoleamine 2,3 dioxygenase (IDO), with subsequent production of tryptophan (TRP) catabolites along the IDO pathway (TRYCATs) and decreased availability of TRP and 5-HT. Tryptophan 128-131 indoleamine 2,3-dioxygenase 1 Homo sapiens 80-83 23531160-6 2013 These, in turns, would cause the activation of the indoleamine 2,3 dioxygenase (IDO), with subsequent production of tryptophan (TRP) catabolites along the IDO pathway (TRYCATs) and decreased availability of TRP and 5-HT. Tryptophan 128-131 indoleamine 2,3-dioxygenase 1 Homo sapiens 155-158 23531160-6 2013 These, in turns, would cause the activation of the indoleamine 2,3 dioxygenase (IDO), with subsequent production of tryptophan (TRP) catabolites along the IDO pathway (TRYCATs) and decreased availability of TRP and 5-HT. Tryptophan 207-210 indoleamine 2,3-dioxygenase 1 Homo sapiens 51-78 23531160-6 2013 These, in turns, would cause the activation of the indoleamine 2,3 dioxygenase (IDO), with subsequent production of tryptophan (TRP) catabolites along the IDO pathway (TRYCATs) and decreased availability of TRP and 5-HT. Tryptophan 207-210 indoleamine 2,3-dioxygenase 1 Homo sapiens 80-83 23531160-6 2013 These, in turns, would cause the activation of the indoleamine 2,3 dioxygenase (IDO), with subsequent production of tryptophan (TRP) catabolites along the IDO pathway (TRYCATs) and decreased availability of TRP and 5-HT. Tryptophan 207-210 indoleamine 2,3-dioxygenase 1 Homo sapiens 155-158 23358471-0 2013 In vivo metabolism of tryptophan in meningiomas is mediated by indoleamine 2,3-dioxygenase 1. Tryptophan 22-32 indoleamine 2,3-dioxygenase 1 Homo sapiens 63-92 22976933-2 2013 A tryptophan-catabolizing enzyme, indoleamine 2,3-dioxygenase (IDO), is reported to be an inducer of immune tolerance. Tryptophan 2-12 indoleamine 2,3-dioxygenase 1 Homo sapiens 63-66 23547116-8 2013 MAPC suppression required licensing and proceeded via IDO-mediated tryptophan catabolism. Tryptophan 67-77 indoleamine 2,3-dioxygenase 1 Homo sapiens 54-57 23453284-1 2013 Tryptophan catabolism, which is mediated by the enzymes indoleamine 2,3-dioxygenase (IDO) and tryptophan 2,3-dioxygenase (TDO), produces kynurenine. Tryptophan 0-10 indoleamine 2,3-dioxygenase 1 Homo sapiens 56-83 23453284-1 2013 Tryptophan catabolism, which is mediated by the enzymes indoleamine 2,3-dioxygenase (IDO) and tryptophan 2,3-dioxygenase (TDO), produces kynurenine. Tryptophan 0-10 indoleamine 2,3-dioxygenase 1 Homo sapiens 85-88 23358471-1 2013 Expression and activity of indoleamine 2,3-dioxygenase (IDO), the first and rate-limiting step of the kynurenine pathway of tryptophan catabolism, can enable tumor cells to effectively evade the host"s immune response. Tryptophan 124-134 indoleamine 2,3-dioxygenase 1 Homo sapiens 27-54 23358471-1 2013 Expression and activity of indoleamine 2,3-dioxygenase (IDO), the first and rate-limiting step of the kynurenine pathway of tryptophan catabolism, can enable tumor cells to effectively evade the host"s immune response. Tryptophan 124-134 indoleamine 2,3-dioxygenase 1 Homo sapiens 56-59 23283180-2 2013 IDO1 initiates tryptophan catabolism along a pathway that generates several bioactive kynurenine-based metabolites. Tryptophan 15-25 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-4 23306541-4 2013 METHODS: We studied the expression of indoleamine 2,3-dioxygenase (IDO), the first enzyme in the kynurenine pathway of tryptophan degradation, in human and murine CF, the impact of IDO on lung inflammation and immunity in murine CF, and the potential role of tryptophan catabolism in pathogenesis and therapy of fungus-associated lung inflammation. Tryptophan 119-129 indoleamine 2,3-dioxygenase 1 Homo sapiens 38-65 23306541-4 2013 METHODS: We studied the expression of indoleamine 2,3-dioxygenase (IDO), the first enzyme in the kynurenine pathway of tryptophan degradation, in human and murine CF, the impact of IDO on lung inflammation and immunity in murine CF, and the potential role of tryptophan catabolism in pathogenesis and therapy of fungus-associated lung inflammation. Tryptophan 119-129 indoleamine 2,3-dioxygenase 1 Homo sapiens 67-70 23314482-1 2013 Indoleamine 2,3-dioxygenase 1 (IDO1) is a tryptophan-catabolizing enzyme whose expression by a broad range of clinical tumors is associated with immunosuppression and poor patient outcome. Tryptophan 42-52 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-29 23314482-1 2013 Indoleamine 2,3-dioxygenase 1 (IDO1) is a tryptophan-catabolizing enzyme whose expression by a broad range of clinical tumors is associated with immunosuppression and poor patient outcome. Tryptophan 42-52 indoleamine 2,3-dioxygenase 1 Homo sapiens 31-35 23178757-2 2013 Meanwhile, interferon (IFN)-gamma is a crucial factor for eliminating chlamydiae from infected cells through indoleamine 2,3-dioxygenase (IDO) expression, resulting in depletion of tryptophan. Tryptophan 181-191 indoleamine 2,3-dioxygenase 1 Homo sapiens 138-141 23212959-4 2013 In the second approach, DCs were transduced to express the tryptophan-catabolising enzyme IDO. Tryptophan 59-69 indoleamine 2,3-dioxygenase 1 Homo sapiens 90-93 23683418-15 2013 (2)IFN-gamma-induced expression of IDO on MSCs involved in tryptophan catabolism. Tryptophan 59-69 indoleamine 2,3-dioxygenase 1 Homo sapiens 35-38 23802083-1 2013 Indoleamine 2,3-dioxygenase (IDO) has recently been proposed to account for tumor-induced immunosuppression by influencing the conversion of tryptophan (Trp) into kynurenine (Kyn). Tryptophan 141-151 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 23802083-1 2013 Indoleamine 2,3-dioxygenase (IDO) has recently been proposed to account for tumor-induced immunosuppression by influencing the conversion of tryptophan (Trp) into kynurenine (Kyn). Tryptophan 141-151 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 23802083-1 2013 Indoleamine 2,3-dioxygenase (IDO) has recently been proposed to account for tumor-induced immunosuppression by influencing the conversion of tryptophan (Trp) into kynurenine (Kyn). Tryptophan 153-156 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 23802083-1 2013 Indoleamine 2,3-dioxygenase (IDO) has recently been proposed to account for tumor-induced immunosuppression by influencing the conversion of tryptophan (Trp) into kynurenine (Kyn). Tryptophan 153-156 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 23128419-1 2013 PURPOSE OF REVIEW: Indoleamine 2,3 dioxygenase (IDO), the key metabolic enzyme implicated in tryptophan catabolism has been studied extensively during the past years in cancer, infections and autoimmunity. Tryptophan 93-103 indoleamine 2,3-dioxygenase 1 Homo sapiens 19-46 23089565-1 2013 Indoleamine 2,3-dioxygenase (IDO) is a rate-limiting enzyme for the tryptophan catabolism that plays an important role in the induction of immune tolerance. Tryptophan 68-78 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 23089565-1 2013 Indoleamine 2,3-dioxygenase (IDO) is a rate-limiting enzyme for the tryptophan catabolism that plays an important role in the induction of immune tolerance. Tryptophan 68-78 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 23319400-6 2013 Indoleamine 2,3-dioxygenase (IDO) is the initial and rate-limiting enzyme of tryptophan catabolism in human placental trophoblasts. Tryptophan 77-87 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 23319400-6 2013 Indoleamine 2,3-dioxygenase (IDO) is the initial and rate-limiting enzyme of tryptophan catabolism in human placental trophoblasts. Tryptophan 77-87 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 23476103-1 2013 Indoleamine 2,3-dioxygenase 1 (IDO1), the L-tryptophan-degrading enzyme, plays a key role in the immunomodulatory effects on several types of immune cells. Tryptophan 42-54 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-29 23476103-1 2013 Indoleamine 2,3-dioxygenase 1 (IDO1), the L-tryptophan-degrading enzyme, plays a key role in the immunomodulatory effects on several types of immune cells. Tryptophan 42-54 indoleamine 2,3-dioxygenase 1 Homo sapiens 31-35 24553013-2 2013 These factors couple to the induction of neuroregulatory tryptophan catabolites via the activation of indoleamine 2,3-dioxygenase (IDO) and tryptophan 2,3-dioxygenase (TDO). Tryptophan 57-67 indoleamine 2,3-dioxygenase 1 Homo sapiens 102-129 24553013-2 2013 These factors couple to the induction of neuroregulatory tryptophan catabolites via the activation of indoleamine 2,3-dioxygenase (IDO) and tryptophan 2,3-dioxygenase (TDO). Tryptophan 57-67 indoleamine 2,3-dioxygenase 1 Homo sapiens 131-134 24553013-9 2013 Second, the more systemic regulation of tryptophan availability occurs via the IL-6 induction of IDO. Tryptophan 40-50 indoleamine 2,3-dioxygenase 1 Homo sapiens 97-100 23232072-2 2012 Indoleamine 2,3-dioxygenase 1 (IDO1) degrades tryptophan into kynurenine (KYN), which inhibits effector T cells and promote regulatory T-cell (Treg) differentiation. Tryptophan 46-56 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-29 23232072-2 2012 Indoleamine 2,3-dioxygenase 1 (IDO1) degrades tryptophan into kynurenine (KYN), which inhibits effector T cells and promote regulatory T-cell (Treg) differentiation. Tryptophan 46-56 indoleamine 2,3-dioxygenase 1 Homo sapiens 31-35 23232072-5 2012 IDO1-driven tryptophan breakdown was correlated with the release of hepatocyte growth factor (HGF) and with the frequency of Treg cells and NY-ESO-1-specific CD8(+) T cells. Tryptophan 12-22 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-4 23264892-1 2012 Tryptophan catabolism by indoleamine 2,3-dioxygenase (IDO) alters inflammation and favors T-cell tolerance in cancer, but the underlying molecular mechanisms remain poorly understood. Tryptophan 0-10 indoleamine 2,3-dioxygenase 1 Homo sapiens 25-52 23264892-1 2012 Tryptophan catabolism by indoleamine 2,3-dioxygenase (IDO) alters inflammation and favors T-cell tolerance in cancer, but the underlying molecular mechanisms remain poorly understood. Tryptophan 0-10 indoleamine 2,3-dioxygenase 1 Homo sapiens 54-57 23264892-4 2012 Addressing this gap in knowledge, we report that the IDO-mediated catabolism of tryptophan also inhibits the immunoregulatory kinases mTOR and PKC-Theta, along with the induction of autophagy. Tryptophan 80-90 indoleamine 2,3-dioxygenase 1 Homo sapiens 53-56 23264892-5 2012 These effects were relieved specifically by tryptophan but also by the experimental agent 1-methyl-D-tryptophan (D-1MT, also known as NLG8189), the latter of which reversed the inhibitory signals generated by IDO with higher potency. Tryptophan 44-54 indoleamine 2,3-dioxygenase 1 Homo sapiens 209-212 23209301-1 2013 The heme enzyme indoleamine 2,3-dioxygenase (IDO) is a key regulator of immune responses through catalyzing l-tryptophan (l-Trp) oxidation. Tryptophan 108-120 indoleamine 2,3-dioxygenase 1 Homo sapiens 16-43 23209301-1 2013 The heme enzyme indoleamine 2,3-dioxygenase (IDO) is a key regulator of immune responses through catalyzing l-tryptophan (l-Trp) oxidation. Tryptophan 108-120 indoleamine 2,3-dioxygenase 1 Homo sapiens 45-48 23209301-1 2013 The heme enzyme indoleamine 2,3-dioxygenase (IDO) is a key regulator of immune responses through catalyzing l-tryptophan (l-Trp) oxidation. Tryptophan 122-127 indoleamine 2,3-dioxygenase 1 Homo sapiens 16-43 23209301-1 2013 The heme enzyme indoleamine 2,3-dioxygenase (IDO) is a key regulator of immune responses through catalyzing l-tryptophan (l-Trp) oxidation. Tryptophan 122-127 indoleamine 2,3-dioxygenase 1 Homo sapiens 45-48 23209301-3 2013 Exposure of IDO-expressing cells or recombinant human IDO (rIDO) to H(2)O(2) inhibited dioxygenase activity in a manner abrogated by l-Trp. Tryptophan 133-138 indoleamine 2,3-dioxygenase 1 Homo sapiens 12-15 23209301-3 2013 Exposure of IDO-expressing cells or recombinant human IDO (rIDO) to H(2)O(2) inhibited dioxygenase activity in a manner abrogated by l-Trp. Tryptophan 133-138 indoleamine 2,3-dioxygenase 1 Homo sapiens 54-57 23209301-8 2013 The promotion of H(2)O(2) consumption by peroxidase substrates, NO consumption, and IDO nitration was inhibited by l-Trp. Tryptophan 115-120 indoleamine 2,3-dioxygenase 1 Homo sapiens 84-87 23209301-11 2013 Peroxidase-mediated dioxygenase inactivation, NO consumption, or protein nitration may modulate the biological actions of IDO expressed in inflammatory tissues where the levels of H(2)O(2) and NO are elevated and l-Trp is low. Tryptophan 213-218 indoleamine 2,3-dioxygenase 1 Homo sapiens 122-125 23063682-1 2012 Indoleamine dioxygenase (IDO) is a heme- containing enzyme that catalyzes the oxidation of tryptophan to N-formylkynurenine, kynurenine and the downstream quinolinic acid. Tryptophan 91-101 indoleamine 2,3-dioxygenase 1 Homo sapiens 25-28 23128419-1 2013 PURPOSE OF REVIEW: Indoleamine 2,3 dioxygenase (IDO), the key metabolic enzyme implicated in tryptophan catabolism has been studied extensively during the past years in cancer, infections and autoimmunity. Tryptophan 93-103 indoleamine 2,3-dioxygenase 1 Homo sapiens 48-51 23243629-1 2012 Indoleamine 2,3-dioxygenase (IDO) is the rate-limiting enzyme in the tryptophan-catabolizing pathway and a key regulator of peripheral immune tolerance. Tryptophan 69-79 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 23243629-1 2012 Indoleamine 2,3-dioxygenase (IDO) is the rate-limiting enzyme in the tryptophan-catabolizing pathway and a key regulator of peripheral immune tolerance. Tryptophan 69-79 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 23267883-2 2012 IDO activity can be measured by the tryptophan(Trp)/kynurenine(Kyn) ratio. Tryptophan 36-46 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 22527253-2 2012 IDO1 catalyzes the initial and rate-limiting step in the degradation of tryptophan and is a key enzyme in mediating tumor immune tolerance via arrest of T cell proliferation. Tryptophan 72-82 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-4 22527253-4 2012 Here, we demonstrate that similar to IDO1, IDO2 also degrades tryptophan into kynurenine and is inhibited more efficiently by Levo-1-methyl tryptophan (L-1MT), an IDO1 competitive inhibitor, than by dextro-methyl tryptophan (D-1MT). Tryptophan 62-72 indoleamine 2,3-dioxygenase 1 Homo sapiens 37-41 22527253-4 2012 Here, we demonstrate that similar to IDO1, IDO2 also degrades tryptophan into kynurenine and is inhibited more efficiently by Levo-1-methyl tryptophan (L-1MT), an IDO1 competitive inhibitor, than by dextro-methyl tryptophan (D-1MT). Tryptophan 62-72 indoleamine 2,3-dioxygenase 1 Homo sapiens 163-167 23267883-2 2012 IDO activity can be measured by the tryptophan(Trp)/kynurenine(Kyn) ratio. Tryptophan 47-50 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 23267888-2 2012 IDO activity can be measured by the tryptophan(Trp)/kynurenine(Kyn) ratio. Tryptophan 36-46 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 23267888-2 2012 IDO activity can be measured by the tryptophan(Trp)/kynurenine(Kyn) ratio. Tryptophan 47-50 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 22981691-5 2012 BACKGROUND: Indoleamine 2,3-dioxygenase (IDO) is an enzyme involved in the catabolism of tryptophan, suppressing T-cell activity. Tryptophan 89-99 indoleamine 2,3-dioxygenase 1 Homo sapiens 12-39 22722711-1 2012 PURPOSE: Indoleamine 2,3-dioxygenase (IDO) is a tryptophan-catabolizing enzyme with immunoregulatory properties in cancer. Tryptophan 48-58 indoleamine 2,3-dioxygenase 1 Homo sapiens 9-36 22722711-1 2012 PURPOSE: Indoleamine 2,3-dioxygenase (IDO) is a tryptophan-catabolizing enzyme with immunoregulatory properties in cancer. Tryptophan 48-58 indoleamine 2,3-dioxygenase 1 Homo sapiens 38-41 22722711-4 2012 IDO expression was correlated with induction of apoptosis in myeloma cells and coupled with tryptophan depletion as well as rescue using IDO inhibitors. Tryptophan 92-102 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 22722711-9 2012 However, cytokine stimulation of MSCs specifically induced IDO, which mediated a marked sensitivity of proximal myeloma cells to tryptophan depletion in the microenvironment, suggesting that selective measures to regulate its availability could be a useful strategy to achieve myeloma growth inhibition and apoptosis. Tryptophan 129-139 indoleamine 2,3-dioxygenase 1 Homo sapiens 59-62 22526360-2 2012 Impaired IDO-mediated tryptophan catabolism has been observed in autoimmune diseases. Tryptophan 22-32 indoleamine 2,3-dioxygenase 1 Homo sapiens 9-12 22526360-3 2012 In order to investigate the effects of IDO-mediated tryptophan catabolism and IDO-expressing DCs in immune thrombocytopenia, the concentrations of kynurenine were detected by high-pressure liquid chromatography. Tryptophan 52-62 indoleamine 2,3-dioxygenase 1 Homo sapiens 39-42 22981691-5 2012 BACKGROUND: Indoleamine 2,3-dioxygenase (IDO) is an enzyme involved in the catabolism of tryptophan, suppressing T-cell activity. Tryptophan 89-99 indoleamine 2,3-dioxygenase 1 Homo sapiens 41-44 22981691-11 2012 RESULTS: In patients with CLL, the serum kyn-trp ratio--reflecting increased IDO activity--was significantly higher compared with controls, but in peripheral blood mononuclear cells (PBMCs)--mainly representing malignant B cells--the expression of genes encoding IDO and IDO2 enzymes was reduced. Tryptophan 45-48 indoleamine 2,3-dioxygenase 1 Homo sapiens 77-80 22564706-1 2012 Indoleamine 2,3-dioxygenase (IDO) is a tryptophan-degrading enzyme and known as a mammalian immunosuppressive molecule. Tryptophan 39-49 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 25054303-2 2012 The current concept suggests that in the tumor microenvironment, tryptophan is metabolized by specialized dioxygenases, chiefly indoleamine-2,3-dioxygenase (IDO), which is expressed by tumor cells and antigen-presenting cells. Tryptophan 65-75 indoleamine 2,3-dioxygenase 1 Homo sapiens 128-155 25054303-2 2012 The current concept suggests that in the tumor microenvironment, tryptophan is metabolized by specialized dioxygenases, chiefly indoleamine-2,3-dioxygenase (IDO), which is expressed by tumor cells and antigen-presenting cells. Tryptophan 65-75 indoleamine 2,3-dioxygenase 1 Homo sapiens 157-160 25054303-3 2012 High IDO activity leads to the depletion of tryptophan from the local microenvironment, while immediate tryptophan metabolites, particularly kynurenine, accumulate to high micromolar levels. Tryptophan 44-54 indoleamine 2,3-dioxygenase 1 Homo sapiens 5-8 22512584-2 2012 Among the enzymes involved, indoleamine 2,3-dioxygenase (IDO), an intracellular enzyme that initiates the first and rate-limiting step of tryptophan breakdown along the kynurenine pathway, has emerged as a promising molecular target for the development of new immunotherapeutic anticancer agents. Tryptophan 138-148 indoleamine 2,3-dioxygenase 1 Homo sapiens 28-55 22512584-2 2012 Among the enzymes involved, indoleamine 2,3-dioxygenase (IDO), an intracellular enzyme that initiates the first and rate-limiting step of tryptophan breakdown along the kynurenine pathway, has emerged as a promising molecular target for the development of new immunotherapeutic anticancer agents. Tryptophan 138-148 indoleamine 2,3-dioxygenase 1 Homo sapiens 57-60 23741252-2 2012 Indoleamine 2,3-dioxygenase (IDO), the tryptophan catabolic enzyme, plays a significant role in regulating the immune response and provides tumor cells with a potent tool to evade the immune system. Tryptophan 39-49 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 23741252-2 2012 Indoleamine 2,3-dioxygenase (IDO), the tryptophan catabolic enzyme, plays a significant role in regulating the immune response and provides tumor cells with a potent tool to evade the immune system. Tryptophan 39-49 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 22683764-1 2012 The kynurenine pathway (KP) and its rate-limiting tryptophan degrading enzyme indolamine 2,3-dioxygenase (IDO) have been implicated in the pathogenesis of depression. Tryptophan 50-60 indoleamine 2,3-dioxygenase 1 Homo sapiens 78-104 22683764-1 2012 The kynurenine pathway (KP) and its rate-limiting tryptophan degrading enzyme indolamine 2,3-dioxygenase (IDO) have been implicated in the pathogenesis of depression. Tryptophan 50-60 indoleamine 2,3-dioxygenase 1 Homo sapiens 106-109 22564706-1 2012 Indoleamine 2,3-dioxygenase (IDO) is a tryptophan-degrading enzyme and known as a mammalian immunosuppressive molecule. Tryptophan 39-49 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 22592557-2 2012 The potential induction of indoleamine 2,3-dioxygenase-1 (IDO1), the rate-limiting enzyme in tryptophan/kynurenine degradation pathway, by proinflammatory cytokines, could be associated with these disorders but has remained unexplored in obesity. Tryptophan 93-103 indoleamine 2,3-dioxygenase 1 Homo sapiens 27-56 22481272-1 2012 Indoleamine 2,3-dioxygenase (IDO), a metabolic enzyme that catalyzes tryptophan conversion into kynurenines, is a crucial regulator of immunity. Tryptophan 69-79 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 22481272-1 2012 Indoleamine 2,3-dioxygenase (IDO), a metabolic enzyme that catalyzes tryptophan conversion into kynurenines, is a crucial regulator of immunity. Tryptophan 69-79 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 22481272-3 2012 IDO is highly expressed in dendritic cells (DCs) that exploit the enzyme"s activity and the production of tryptophan catabolites to regulate immune responses by acting on several cell types, including T lymphocytes, of which they promote a regulatory phenotype. Tryptophan 106-116 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 22592557-2 2012 The potential induction of indoleamine 2,3-dioxygenase-1 (IDO1), the rate-limiting enzyme in tryptophan/kynurenine degradation pathway, by proinflammatory cytokines, could be associated with these disorders but has remained unexplored in obesity. Tryptophan 93-103 indoleamine 2,3-dioxygenase 1 Homo sapiens 58-62 22592557-7 2012 In obese subjects, the ratio of kynurenine to tryptophan, which reflects IDO1 activation, is higher than in lean subjects. Tryptophan 46-56 indoleamine 2,3-dioxygenase 1 Homo sapiens 73-77 22707953-4 2012 Indoleamine 2,3-dioxygenase (IDO), a rate-limiting enzyme in the tryptophan catabolism, plays a key role in induction of tolerance against fungi. Tryptophan 65-75 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 21823214-1 2012 BACKGROUND: Indoleamine 2,3 dioxygenase-1 (IDO1) is a tryptophan catabolizing enzyme with immunotolerance-promoting functions. Tryptophan 54-64 indoleamine 2,3-dioxygenase 1 Homo sapiens 12-41 21823214-1 2012 BACKGROUND: Indoleamine 2,3 dioxygenase-1 (IDO1) is a tryptophan catabolizing enzyme with immunotolerance-promoting functions. Tryptophan 54-64 indoleamine 2,3-dioxygenase 1 Homo sapiens 43-47 21823214-2 2012 We sought to determine if increased gut expression of IDO1 in Crohn"s disease (CD) would result in detectable changes in serum levels of tryptophan and the initial IDO1 pathway catabolite, kynurenine. Tryptophan 137-147 indoleamine 2,3-dioxygenase 1 Homo sapiens 54-58 21823214-14 2012 CONCLUSIONS: IDO1 expression in CD is associated with lower serum tryptophan and an elevated K/T ratio. Tryptophan 66-76 indoleamine 2,3-dioxygenase 1 Homo sapiens 13-17 22707953-4 2012 Indoleamine 2,3-dioxygenase (IDO), a rate-limiting enzyme in the tryptophan catabolism, plays a key role in induction of tolerance against fungi. Tryptophan 65-75 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 22519427-1 2012 A series of recent studies have demonstrated that the immunoregulatory pathway of tryptophan catabolism, initiated by the enzyme indoleamine 2,3-dioxygenase (IDO), is a critical participant in allergic inflammation. Tryptophan 82-92 indoleamine 2,3-dioxygenase 1 Homo sapiens 129-156 22519427-1 2012 A series of recent studies have demonstrated that the immunoregulatory pathway of tryptophan catabolism, initiated by the enzyme indoleamine 2,3-dioxygenase (IDO), is a critical participant in allergic inflammation. Tryptophan 82-92 indoleamine 2,3-dioxygenase 1 Homo sapiens 158-161 22460077-7 2012 We have used an automated two-dimensional liquid chromatography (LC) system coupled with electrospray ionization quadrupole ion-trap MS to identify PTMs for indoleamine 2,3-dioxygenase 1 (IDO1), one of the tryptophan catabolic enzymes. Tryptophan 206-216 indoleamine 2,3-dioxygenase 1 Homo sapiens 157-186 22460077-7 2012 We have used an automated two-dimensional liquid chromatography (LC) system coupled with electrospray ionization quadrupole ion-trap MS to identify PTMs for indoleamine 2,3-dioxygenase 1 (IDO1), one of the tryptophan catabolic enzymes. Tryptophan 206-216 indoleamine 2,3-dioxygenase 1 Homo sapiens 188-192 22458995-2 2012 These lower levels may be regarded as a biochemical marker for cellular immune activation, which may lead to increased catabolism of tryptophan into kynurenine via stimulation of the enzyme indoleamine 2,3-dioxygenase (IDO) by interferon-gamma. Tryptophan 133-143 indoleamine 2,3-dioxygenase 1 Homo sapiens 219-222 22249100-7 2012 Here, the authors reviewed and discussed how the expression of IDO by the primary cells of our skin substitute can serve as a source of IDO enzyme activity and generate a tryptophan-deficient environment. Tryptophan 171-181 indoleamine 2,3-dioxygenase 1 Homo sapiens 63-66 22717876-1 2012 This review focuses on the placental expression of the tryptophan-degrading enzyme indoleamine 2,3-dioxygenase-1 (IDO1) and its potential roles, which may not only encompass immunosuppression and antimicrobial activity, but also vasodilation based on the endothelial expression on both sides of the feto-maternal interface. Tryptophan 55-65 indoleamine 2,3-dioxygenase 1 Homo sapiens 83-112 22717876-1 2012 This review focuses on the placental expression of the tryptophan-degrading enzyme indoleamine 2,3-dioxygenase-1 (IDO1) and its potential roles, which may not only encompass immunosuppression and antimicrobial activity, but also vasodilation based on the endothelial expression on both sides of the feto-maternal interface. Tryptophan 55-65 indoleamine 2,3-dioxygenase 1 Homo sapiens 114-118 22301793-4 2012 with a decline in titer after 48 h. Concomitant with viral control was the robust induction of indoleamine 2,3-dioxygenase (IDO) and resultant metabolism of L-tryptophan (L-Trp) to kynurenine. Tryptophan 157-169 indoleamine 2,3-dioxygenase 1 Homo sapiens 95-122 22301793-4 2012 with a decline in titer after 48 h. Concomitant with viral control was the robust induction of indoleamine 2,3-dioxygenase (IDO) and resultant metabolism of L-tryptophan (L-Trp) to kynurenine. Tryptophan 157-169 indoleamine 2,3-dioxygenase 1 Homo sapiens 124-127 22301793-4 2012 with a decline in titer after 48 h. Concomitant with viral control was the robust induction of indoleamine 2,3-dioxygenase (IDO) and resultant metabolism of L-tryptophan (L-Trp) to kynurenine. Tryptophan 171-176 indoleamine 2,3-dioxygenase 1 Homo sapiens 95-122 22301793-4 2012 with a decline in titer after 48 h. Concomitant with viral control was the robust induction of indoleamine 2,3-dioxygenase (IDO) and resultant metabolism of L-tryptophan (L-Trp) to kynurenine. Tryptophan 171-176 indoleamine 2,3-dioxygenase 1 Homo sapiens 124-127 22301793-9 2012 Whereas IDO-mediated L-Trp metabolism can exhibit antiviral properties, inhibition of IDO activity in MDM with L-1-MT or the addition of excess L-Trp did not affect viral control. Tryptophan 21-26 indoleamine 2,3-dioxygenase 1 Homo sapiens 8-11 22301793-10 2012 However, culturing MDM in L-Trp-deficient medium or overexpression of IDO in cells prior to infection significantly attenuated WNV replication, which was reversed by adding excess L-Trp. Tryptophan 180-185 indoleamine 2,3-dioxygenase 1 Homo sapiens 70-73 22112538-1 2012 Indoleamine 2,3-dioxygenase-1 (IDO-1) is a heme containing enzyme that catalyses the initial step in the major pathway of l-tryptophan catabolism; the kynurenine pathway. Tryptophan 122-134 indoleamine 2,3-dioxygenase 1 Homo sapiens 31-36 22071871-5 2012 Moreover, treatment with IL-1beta resulted in an increase in kynurenine, the catabolic product of IDO-induced tryptophan metabolism. Tryptophan 110-120 indoleamine 2,3-dioxygenase 1 Homo sapiens 98-101 22196056-1 2012 Indoleamine 2,3-dioxygenase (IDO) and tryptophan dioxygenase (TDO) are two heme proteins that catalyze the oxidation reaction of tryptophan (Trp) to N-formylkynurenine (NFK). Tryptophan 141-144 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 22196056-1 2012 Indoleamine 2,3-dioxygenase (IDO) and tryptophan dioxygenase (TDO) are two heme proteins that catalyze the oxidation reaction of tryptophan (Trp) to N-formylkynurenine (NFK). Tryptophan 141-144 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 22196056-3 2012 Our recent studies revealed that the dioxygenase reaction catalyzed by hIDO and TDO is initiated by addition of the ferric iron-bound superoxide to the C(2) C(3) bond of Trp to form a ferryl and Trp-epoxide intermediate, via a 2-indolenylperoxo radical transition state. Tryptophan 170-173 indoleamine 2,3-dioxygenase 1 Homo sapiens 71-75 22196056-9 2012 The results underscore the importance of the NH(3)(+) group of Trp in the two-step ferryl-based mechanism of hIDO and xcTDO, by acting as an acid catalyst to facilitate the epoxide ring-opening reaction and ferryl oxygen addition to the indole ring. Tryptophan 63-66 indoleamine 2,3-dioxygenase 1 Homo sapiens 109-113 22112538-1 2012 Indoleamine 2,3-dioxygenase-1 (IDO-1) is a heme containing enzyme that catalyses the initial step in the major pathway of l-tryptophan catabolism; the kynurenine pathway. Tryptophan 122-134 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-29 22184722-7 2012 Moreover, we found that conditioned medium from IDO(+) MPhis effectively suppressed T cell responses in vitro, an effect that could be reversed by adding extrinsic IDO substrate tryptophan or by pretreating MPhis with an IDO inhibitor 1-methyl-DL-tryptophan. Tryptophan 178-188 indoleamine 2,3-dioxygenase 1 Homo sapiens 164-167 22184722-7 2012 Moreover, we found that conditioned medium from IDO(+) MPhis effectively suppressed T cell responses in vitro, an effect that could be reversed by adding extrinsic IDO substrate tryptophan or by pretreating MPhis with an IDO inhibitor 1-methyl-DL-tryptophan. Tryptophan 178-188 indoleamine 2,3-dioxygenase 1 Homo sapiens 164-167 22369947-3 2012 Indeed, several small molecule inhibitors of indoleamine 2,3-dioxygenase (IDO), a rate-limiting enzyme in the catabolism of Trp to Kyn, exert antitumor effects in animal models. Tryptophan 124-127 indoleamine 2,3-dioxygenase 1 Homo sapiens 45-72 22369947-3 2012 Indeed, several small molecule inhibitors of indoleamine 2,3-dioxygenase (IDO), a rate-limiting enzyme in the catabolism of Trp to Kyn, exert antitumor effects in animal models. Tryptophan 124-127 indoleamine 2,3-dioxygenase 1 Homo sapiens 74-77 22219312-2 2012 Indoleamine 2,3-dioxygenase (IDO), a potent immunoregulatory molecule, catalyzes the rate-limiting step of tryptophan (Trp) degradation in the kynurenine (Kyn) pathway. Tryptophan 107-117 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 22219312-2 2012 Indoleamine 2,3-dioxygenase (IDO), a potent immunoregulatory molecule, catalyzes the rate-limiting step of tryptophan (Trp) degradation in the kynurenine (Kyn) pathway. Tryptophan 107-117 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 22219312-2 2012 Indoleamine 2,3-dioxygenase (IDO), a potent immunoregulatory molecule, catalyzes the rate-limiting step of tryptophan (Trp) degradation in the kynurenine (Kyn) pathway. Tryptophan 119-122 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 22219312-2 2012 Indoleamine 2,3-dioxygenase (IDO), a potent immunoregulatory molecule, catalyzes the rate-limiting step of tryptophan (Trp) degradation in the kynurenine (Kyn) pathway. Tryptophan 119-122 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 22219312-3 2012 An increase in IDO activity determined by the serum Trp/Kyn ratio has been shown to be associated with poor prognosis in cancers and bacteremia. Tryptophan 52-55 indoleamine 2,3-dioxygenase 1 Homo sapiens 15-18 22219312-6 2012 IDO activity was estimated by calculating the serum Kyn-to-Trp ratio. Tryptophan 59-62 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 22282879-3 2012 The presence of additional IDO directs more tryptophan down the kynurenine pathway, leaving less available for synthesis of serotonin and its metabolites. Tryptophan 44-54 indoleamine 2,3-dioxygenase 1 Homo sapiens 27-30 22258797-1 2012 Tryptophan is one of the essential amino acids, 80% of which is catabolised in the extrahepatic tissues by indoleamine-2,3-dioxygenase (IDO), the rate-limiting enzyme of the kynurenine pathway. Tryptophan 0-10 indoleamine 2,3-dioxygenase 1 Homo sapiens 107-134 22258797-1 2012 Tryptophan is one of the essential amino acids, 80% of which is catabolised in the extrahepatic tissues by indoleamine-2,3-dioxygenase (IDO), the rate-limiting enzyme of the kynurenine pathway. Tryptophan 0-10 indoleamine 2,3-dioxygenase 1 Homo sapiens 136-139 22108515-1 2012 BACKGROUND: Indoleamine 2,3-dioxygenase 1 (IDO1) is a tryptophan-catabolising enzyme that induces immune tolerance by modulating T-cell responses. Tryptophan 54-64 indoleamine 2,3-dioxygenase 1 Homo sapiens 12-41 22108515-1 2012 BACKGROUND: Indoleamine 2,3-dioxygenase 1 (IDO1) is a tryptophan-catabolising enzyme that induces immune tolerance by modulating T-cell responses. Tryptophan 54-64 indoleamine 2,3-dioxygenase 1 Homo sapiens 43-47 22814706-4 2012 A dysfunction in the activation of the type-1 immune response seems to be associated with decreased activity of the key enzyme of the tryptophan/kynurenine metabolism, indoleamine 2,3-dioxygenase (IDO). Tryptophan 134-144 indoleamine 2,3-dioxygenase 1 Homo sapiens 168-195 22814706-4 2012 A dysfunction in the activation of the type-1 immune response seems to be associated with decreased activity of the key enzyme of the tryptophan/kynurenine metabolism, indoleamine 2,3-dioxygenase (IDO). Tryptophan 134-144 indoleamine 2,3-dioxygenase 1 Homo sapiens 197-200 23028625-0 2012 Influence of tryptophan contained in 1-Methyl-Tryptophan on antimicrobial and immunoregulatory functions of indoleamine 2,3-dioxygenase. Tryptophan 13-23 indoleamine 2,3-dioxygenase 1 Homo sapiens 108-135 22184722-7 2012 Moreover, we found that conditioned medium from IDO(+) MPhis effectively suppressed T cell responses in vitro, an effect that could be reversed by adding extrinsic IDO substrate tryptophan or by pretreating MPhis with an IDO inhibitor 1-methyl-DL-tryptophan. Tryptophan 178-188 indoleamine 2,3-dioxygenase 1 Homo sapiens 48-51 22072376-4 2012 The active form of Stat3 was detected by flow-cytometry, and IDO enzyme activity following IFN-gamma stimulation of keratocytes was measured by tryptophan to kynurenine conversion with photometric determination of kynurenine concentration in the supernatant. Tryptophan 144-154 indoleamine 2,3-dioxygenase 1 Homo sapiens 61-64 22064648-10 2012 Finally, the expression of the tryptophan-catabolizing enzyme indoleamine 2,3-dioxygenase (IDO) after the exposure of MIC-1 to maturing DCs was analysed by western blot. Tryptophan 31-41 indoleamine 2,3-dioxygenase 1 Homo sapiens 62-89 22064648-10 2012 Finally, the expression of the tryptophan-catabolizing enzyme indoleamine 2,3-dioxygenase (IDO) after the exposure of MIC-1 to maturing DCs was analysed by western blot. Tryptophan 31-41 indoleamine 2,3-dioxygenase 1 Homo sapiens 91-94 22594922-2 2012 It is known that IDO induces T-cell differentiation to regulatory T-cells (Treg) through tryptophan depletion and/or kynurenine pathway products. Tryptophan 89-99 indoleamine 2,3-dioxygenase 1 Homo sapiens 17-20 21990421-1 2012 Recent studies have underscored physiological and pathophysiological roles for the tryptophan-degrading enzyme indolamine 2,3-dioxygenase (IDO) in immune counterregulation. Tryptophan 83-93 indoleamine 2,3-dioxygenase 1 Homo sapiens 111-137 21990421-1 2012 Recent studies have underscored physiological and pathophysiological roles for the tryptophan-degrading enzyme indolamine 2,3-dioxygenase (IDO) in immune counterregulation. Tryptophan 83-93 indoleamine 2,3-dioxygenase 1 Homo sapiens 139-142 22557874-3 2012 Indoleamine 2, 3-dioxygenase (IDO), the first rate-limiting enzyme in the tryptophan catabolism, is up regulated by interferon-gamma (IFN-g) which harbors single nucleotide polymorphisms (SNPs). Tryptophan 74-84 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-28 22557874-3 2012 Indoleamine 2, 3-dioxygenase (IDO), the first rate-limiting enzyme in the tryptophan catabolism, is up regulated by interferon-gamma (IFN-g) which harbors single nucleotide polymorphisms (SNPs). Tryptophan 74-84 indoleamine 2,3-dioxygenase 1 Homo sapiens 30-33 22860140-1 2012 BACKGROUND: Our earlier genome-wide expression study revealed up-regulation of a tryptophan-catabolizing enzyme, indoleamine 2,3-dioxygenase (IDO1), in patients with scrub typhus. Tryptophan 81-91 indoleamine 2,3-dioxygenase 1 Homo sapiens 142-146 22860140-7 2012 Inhibition of IDO1 activity in IFN-gamma treated cultures by 1-methyl-L-tryptophan, a competitive inhibitor of IDO1, resulted in partial restoration of infection index; while excessive supplementation of L-tryptophan in IFN-gamma treated cultures raised the index to an even higher level than that of the untreated ones. Tryptophan 70-82 indoleamine 2,3-dioxygenase 1 Homo sapiens 14-18 22860140-7 2012 Inhibition of IDO1 activity in IFN-gamma treated cultures by 1-methyl-L-tryptophan, a competitive inhibitor of IDO1, resulted in partial restoration of infection index; while excessive supplementation of L-tryptophan in IFN-gamma treated cultures raised the index to an even higher level than that of the untreated ones. Tryptophan 70-82 indoleamine 2,3-dioxygenase 1 Homo sapiens 111-115 22860140-8 2012 Altogether, these data implied that IDO1 was partly involved in restriction of OT growth caused by IFN-gamma through deprivation of tryptophan. Tryptophan 132-142 indoleamine 2,3-dioxygenase 1 Homo sapiens 36-40 22860140-9 2012 CONCLUSIONS/SIGNIFICANCE: Activation of IDO1 appeared to be a defensive mechanism downstream of IFN-gamma that limited intracellular expansion of OT via tryptophan depletion. Tryptophan 153-163 indoleamine 2,3-dioxygenase 1 Homo sapiens 40-44 23028625-1 2012 Indoleamine 2,3-dioxygenase (IDO) has been identified as an important antimicrobial and immunoregulatory effector molecule essential for the establishment of tolerance by regulating local tryptophan (Trp) concentrations. Tryptophan 188-198 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 23028625-1 2012 Indoleamine 2,3-dioxygenase (IDO) has been identified as an important antimicrobial and immunoregulatory effector molecule essential for the establishment of tolerance by regulating local tryptophan (Trp) concentrations. Tryptophan 188-198 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 23028625-1 2012 Indoleamine 2,3-dioxygenase (IDO) has been identified as an important antimicrobial and immunoregulatory effector molecule essential for the establishment of tolerance by regulating local tryptophan (Trp) concentrations. Tryptophan 200-203 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 23028625-1 2012 Indoleamine 2,3-dioxygenase (IDO) has been identified as an important antimicrobial and immunoregulatory effector molecule essential for the establishment of tolerance by regulating local tryptophan (Trp) concentrations. Tryptophan 200-203 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 23028625-5 2012 While IDO enzyme activity is more efficiently inhibited by 1-L-MT in cell-free or in vitro settings, 1-D-MT is superior to 1-L-MT in the enhancement of anti-tumor responses in vivo.Here, we present new data showing that commercially available 1-L-MT lots contain tryptophan in amounts sufficient to compensate for the IDO-mediated tryptophan depletion in vitro. Tryptophan 263-273 indoleamine 2,3-dioxygenase 1 Homo sapiens 6-9 23028625-5 2012 While IDO enzyme activity is more efficiently inhibited by 1-L-MT in cell-free or in vitro settings, 1-D-MT is superior to 1-L-MT in the enhancement of anti-tumor responses in vivo.Here, we present new data showing that commercially available 1-L-MT lots contain tryptophan in amounts sufficient to compensate for the IDO-mediated tryptophan depletion in vitro. Tryptophan 331-341 indoleamine 2,3-dioxygenase 1 Homo sapiens 6-9 23028625-7 2012 Consistent with this, the tryptophan within 1-L-MT lots was sufficient to antagonize IDO-mediated inhibition of T cell responses. Tryptophan 26-36 indoleamine 2,3-dioxygenase 1 Homo sapiens 85-88 23028625-9 2012 In summary, these data reveal that tryptophan within 1-L-MT can affect the results of in vitro studies in an L-stereospecific and IDO-independent way. Tryptophan 35-45 indoleamine 2,3-dioxygenase 1 Homo sapiens 130-133 22693634-4 2012 Recently, Indoleamine-pyrrole 2,3- dioxygenase (IDO)-derived tryptophan metabolites, including L-kynurenine, were also shown to be involved in several counter-regulatory mechanisms. Tryptophan 61-71 indoleamine 2,3-dioxygenase 1 Homo sapiens 10-46 22693634-4 2012 Recently, Indoleamine-pyrrole 2,3- dioxygenase (IDO)-derived tryptophan metabolites, including L-kynurenine, were also shown to be involved in several counter-regulatory mechanisms. Tryptophan 61-71 indoleamine 2,3-dioxygenase 1 Homo sapiens 48-51 22897519-2 2012 Indoleamine 2,3-dioxygenase (IDO) and arginase type I (ARG) catabolize tryptophane and arginine, respectively, and exert proapoptotic and antiproliferative effects on T-cells. Tryptophan 71-82 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 22897519-2 2012 Indoleamine 2,3-dioxygenase (IDO) and arginase type I (ARG) catabolize tryptophane and arginine, respectively, and exert proapoptotic and antiproliferative effects on T-cells. Tryptophan 71-82 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 22039265-0 2011 Tryptophan catabolism is associated with acute GVHD after human allogeneic stem cell transplantation and indicates activation of indoleamine 2,3-dioxygenase. Tryptophan 0-10 indoleamine 2,3-dioxygenase 1 Homo sapiens 129-156 22039265-1 2011 Induction of indoleamine 2,3-dioxygenase (IDO), the rate-limiting enzyme in tryptophan degradation along the kynurenine pathway, acts as a potent immunoregulatory loop. Tryptophan 76-86 indoleamine 2,3-dioxygenase 1 Homo sapiens 13-40 22039265-1 2011 Induction of indoleamine 2,3-dioxygenase (IDO), the rate-limiting enzyme in tryptophan degradation along the kynurenine pathway, acts as a potent immunoregulatory loop. Tryptophan 76-86 indoleamine 2,3-dioxygenase 1 Homo sapiens 42-45 22082147-1 2011 Tryptophan dioxygenase (TDO) and indoleamine 2,3-dioxygenase (IDO) are the only two heme proteins that catalyze the oxidation reaction of tryptophan (Trp) to N-formylkynurenine. Tryptophan 138-148 indoleamine 2,3-dioxygenase 1 Homo sapiens 33-60 22082147-1 2011 Tryptophan dioxygenase (TDO) and indoleamine 2,3-dioxygenase (IDO) are the only two heme proteins that catalyze the oxidation reaction of tryptophan (Trp) to N-formylkynurenine. Tryptophan 138-148 indoleamine 2,3-dioxygenase 1 Homo sapiens 62-65 22082147-1 2011 Tryptophan dioxygenase (TDO) and indoleamine 2,3-dioxygenase (IDO) are the only two heme proteins that catalyze the oxidation reaction of tryptophan (Trp) to N-formylkynurenine. Tryptophan 150-153 indoleamine 2,3-dioxygenase 1 Homo sapiens 33-60 22082147-1 2011 Tryptophan dioxygenase (TDO) and indoleamine 2,3-dioxygenase (IDO) are the only two heme proteins that catalyze the oxidation reaction of tryptophan (Trp) to N-formylkynurenine. Tryptophan 150-153 indoleamine 2,3-dioxygenase 1 Homo sapiens 62-65 22082147-2 2011 While human IDO is able to oxidize both L- and D-Trp, human TDO (hTDO) displays major specificity for L-Trp. Tryptophan 48-52 indoleamine 2,3-dioxygenase 1 Homo sapiens 12-15 22410120-1 2011 BACKGROUND: Indoleamine 2,3-dioxygenase (IDO) is a tryptophan catalyzing enzyme. Tryptophan 51-61 indoleamine 2,3-dioxygenase 1 Homo sapiens 12-39 22410120-1 2011 BACKGROUND: Indoleamine 2,3-dioxygenase (IDO) is a tryptophan catalyzing enzyme. Tryptophan 51-61 indoleamine 2,3-dioxygenase 1 Homo sapiens 41-44 22396896-2 2011 The key Th-1 type, pro-inflammatory cytokine, interferon-gamma (IFNG), transcriptionally induces the rate-limiting enzyme of tryptophan (TRY) - kynurenine (KYN) pathway, indoleamine 2,3- dioxygenase (IDO). Tryptophan 125-135 indoleamine 2,3-dioxygenase 1 Homo sapiens 200-203 22068654-3 2011 However, the exact role of tryptophan catabolism by IDO in human cancers remains poorly understood. Tryptophan 27-37 indoleamine 2,3-dioxygenase 1 Homo sapiens 52-55 22034910-2 2011 The involvement of indoleamine 2, 3-dioxygenase (IDO) and kynurenines, the products of tryptophan degradation in various pathological conditions was well documented. Tryptophan 87-97 indoleamine 2,3-dioxygenase 1 Homo sapiens 19-47 22034910-2 2011 The involvement of indoleamine 2, 3-dioxygenase (IDO) and kynurenines, the products of tryptophan degradation in various pathological conditions was well documented. Tryptophan 87-97 indoleamine 2,3-dioxygenase 1 Homo sapiens 49-52 21835273-1 2011 Indoleamine 2,3-dioxygenase (IDO1) catalyzes the first step in tryptophan breakdown along the kynurenine pathway. Tryptophan 63-73 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-33 21835273-5 2011 We found that the K(m) of human IDO2 for l-tryptophan is much higher than that of IDO1. Tryptophan 41-53 indoleamine 2,3-dioxygenase 1 Homo sapiens 82-86 21765346-2 2011 BACKGROUND: Indoleamine 2,3-dioxygenase 1 is an inducible enzyme that converts tryptophan to kynurenine and shares functional similarities with inducible nitric oxide synthase. Tryptophan 79-89 indoleamine 2,3-dioxygenase 1 Homo sapiens 12-41 21952237-1 2011 Indoleamine 2,3-dioxygenase (IDO) is an enzyme that degrades an essential amino acid, tryptophan, and plays a role in inhibiting the proliferation of T cells and intracellular pathogens. Tryptophan 86-96 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 21952237-1 2011 Indoleamine 2,3-dioxygenase (IDO) is an enzyme that degrades an essential amino acid, tryptophan, and plays a role in inhibiting the proliferation of T cells and intracellular pathogens. Tryptophan 86-96 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 22338916-1 2011 Indoleamine 2,3-dioxygenase (IDO) catalyses tryptophan degradation in the kynurenine pathway, and plays an important role in immune tolerance by regulating antigen-presenting cells. Tryptophan 44-54 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 22338916-1 2011 Indoleamine 2,3-dioxygenase (IDO) catalyses tryptophan degradation in the kynurenine pathway, and plays an important role in immune tolerance by regulating antigen-presenting cells. Tryptophan 44-54 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 22068654-1 2011 Indoleamine 2,3-dioxygenase (IDO) is a tryptophan-catabolizing enzyme with immune-regulating activities in many contexts, such as fetal protection, allograft protection, and cancer progression. Tryptophan 39-49 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 21917155-9 2011 RESULTS: IDO transgenic CHO cells yielded high levels of IDO enzymatic activity, resulting in complete depletion of tryptophan from the culture medium. Tryptophan 116-126 indoleamine 2,3-dioxygenase 1 Homo sapiens 9-12 22202242-2 2011 IDO activity can be measured by kynurenine( Kyn)/tryptophan (Trp) ratio. Tryptophan 49-59 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 22202242-2 2011 IDO activity can be measured by kynurenine( Kyn)/tryptophan (Trp) ratio. Tryptophan 61-64 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 21911470-1 2011 Gamma interferon (IFN-gamma) induces expression of the tryptophan-catabolizing enzyme indoleamine 2,3-dioxygenase (IDO1) in human epithelial cells, the permissive cells for the obligate intracellular bacterium Chlamydia trachomatis. Tryptophan 55-65 indoleamine 2,3-dioxygenase 1 Homo sapiens 115-119 21911470-2 2011 IDO1 depletes tryptophan by catabolizing it to kynurenine with consequences for C. trachomatis, which is a tryptophan auxotroph. Tryptophan 14-24 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-4 21911470-2 2011 IDO1 depletes tryptophan by catabolizing it to kynurenine with consequences for C. trachomatis, which is a tryptophan auxotroph. Tryptophan 107-117 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-4 21937116-2 2011 The enzyme indoleamine 2,3-dioxygenase (IDO) can exert necessary regulating effects by catabolizing tryptophan, leading to the suppression of immune responses in different settings, such as pregnancy and tumor growth. Tryptophan 100-110 indoleamine 2,3-dioxygenase 1 Homo sapiens 11-38 21937116-2 2011 The enzyme indoleamine 2,3-dioxygenase (IDO) can exert necessary regulating effects by catabolizing tryptophan, leading to the suppression of immune responses in different settings, such as pregnancy and tumor growth. Tryptophan 100-110 indoleamine 2,3-dioxygenase 1 Homo sapiens 40-43 21937116-3 2011 IDO"s immuno-suppressive actions are mediated by tryptophan starvation and the accumulation of toxic tryptophan metabolites, resulting in T cell anergy, inhibition of clonal expansion or apoptosis. Tryptophan 49-59 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 21937116-3 2011 IDO"s immuno-suppressive actions are mediated by tryptophan starvation and the accumulation of toxic tryptophan metabolites, resulting in T cell anergy, inhibition of clonal expansion or apoptosis. Tryptophan 101-111 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 21937116-10 2011 We, however, report weak or absent enzymatic activity from these IDO-expressing cells, as assessed by tryptophan consumption. Tryptophan 102-112 indoleamine 2,3-dioxygenase 1 Homo sapiens 65-68 22068654-1 2011 Indoleamine 2,3-dioxygenase (IDO) is a tryptophan-catabolizing enzyme with immune-regulating activities in many contexts, such as fetal protection, allograft protection, and cancer progression. Tryptophan 39-49 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 21366559-1 2011 BACKGROUND: Indoleamine 2,3-dioxygenase (IDO) is a tryptophan-degrading enzyme which suppresses T lymphocyte activity and induces Foxp3+ CD4+ regulatory T cells (Tregs) polarisation. Tryptophan 51-61 indoleamine 2,3-dioxygenase 1 Homo sapiens 12-39 21366559-1 2011 BACKGROUND: Indoleamine 2,3-dioxygenase (IDO) is a tryptophan-degrading enzyme which suppresses T lymphocyte activity and induces Foxp3+ CD4+ regulatory T cells (Tregs) polarisation. Tryptophan 51-61 indoleamine 2,3-dioxygenase 1 Homo sapiens 41-44 21689736-1 2011 Indoleamine 2,3-dioxygenase (IDO) and tryptophan 2,3-dioxygenase (TDO) are tryptophan-degrading enzymes that catalyze the first step in L-Trp catabolism via the kynurenine pathway. Tryptophan 136-141 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 21720257-0 2011 Serum tryptophan and kynurenine concentrations as parameters for indoleamine 2,3-dioxygenase activity in patients with endometrial, ovarian, and vulvar cancer. Tryptophan 6-16 indoleamine 2,3-dioxygenase 1 Homo sapiens 65-92 21720257-7 2011 Indoleamine 2,3-dioxygenase activity was estimated by calculating the kyn/trp ratio. Tryptophan 74-77 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 21917155-9 2011 RESULTS: IDO transgenic CHO cells yielded high levels of IDO enzymatic activity, resulting in complete depletion of tryptophan from the culture medium. Tryptophan 116-126 indoleamine 2,3-dioxygenase 1 Homo sapiens 57-60 21784100-1 2011 OBJECTIVES: Indoleamine 2,3-dioxygenase (IDO) catalyzes the rate-limiting step of tryptophan (Trp) degradation in the kynurenine (Kyn) pathway. Tryptophan 82-92 indoleamine 2,3-dioxygenase 1 Homo sapiens 12-39 21784100-1 2011 OBJECTIVES: Indoleamine 2,3-dioxygenase (IDO) catalyzes the rate-limiting step of tryptophan (Trp) degradation in the kynurenine (Kyn) pathway. Tryptophan 82-92 indoleamine 2,3-dioxygenase 1 Homo sapiens 41-44 21784100-1 2011 OBJECTIVES: Indoleamine 2,3-dioxygenase (IDO) catalyzes the rate-limiting step of tryptophan (Trp) degradation in the kynurenine (Kyn) pathway. Tryptophan 94-97 indoleamine 2,3-dioxygenase 1 Homo sapiens 12-39 21784100-1 2011 OBJECTIVES: Indoleamine 2,3-dioxygenase (IDO) catalyzes the rate-limiting step of tryptophan (Trp) degradation in the kynurenine (Kyn) pathway. Tryptophan 94-97 indoleamine 2,3-dioxygenase 1 Homo sapiens 41-44 21784100-2 2011 By depleting Trp, IDO plays a critical role in inducing immune suppression and tolerance. Tryptophan 13-16 indoleamine 2,3-dioxygenase 1 Homo sapiens 18-21 21784100-3 2011 The aim of present study was to investigate serum IDO activity, determined by Kyn-to-Trp ratio (Kyn/Trp ratio), in community-acquired pneumonia (CAP) and to examine its clinical significance. Tryptophan 85-88 indoleamine 2,3-dioxygenase 1 Homo sapiens 50-53 21784100-3 2011 The aim of present study was to investigate serum IDO activity, determined by Kyn-to-Trp ratio (Kyn/Trp ratio), in community-acquired pneumonia (CAP) and to examine its clinical significance. Tryptophan 100-103 indoleamine 2,3-dioxygenase 1 Homo sapiens 50-53 21690092-2 2011 This reaction led to the formation of the dioxygen adduct of IDO and supported the oxidation of Trp to N-formylkynurenine. Tryptophan 96-99 indoleamine 2,3-dioxygenase 1 Homo sapiens 61-64 21742032-3 2011 IDO activity is estimated by calculating the kynurenine to tryptophan ratio (Kyn/Trp). Tryptophan 59-69 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 21742032-3 2011 IDO activity is estimated by calculating the kynurenine to tryptophan ratio (Kyn/Trp). Tryptophan 81-84 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 21742973-1 2011 IDO is the rate-limiting enzyme in the kynurenine pathway, catabolizing tryptophan to kynurenine. Tryptophan 72-82 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 21742973-2 2011 Tryptophan depletion by IDO-expressing tumors is a common mechanism of immune evasion inducing regulatory T cells and inhibiting effector T cells. Tryptophan 0-10 indoleamine 2,3-dioxygenase 1 Homo sapiens 24-27 21742973-4 2011 We demonstrate that IDO(+) tumor cells express a novel amino acid transporter, which accounts for ~50% of the tryptophan uptake. Tryptophan 110-120 indoleamine 2,3-dioxygenase 1 Homo sapiens 20-23 21742973-6 2011 Under conditions of low extracellular tryptophan, expression of this novel transporter significantly increases tryptophan entry into IDO(+) tumors relative to tryptophan uptake through the low-affinity System L alone, and further decreases tryptophan levels in the microenvironment. Tryptophan 38-48 indoleamine 2,3-dioxygenase 1 Homo sapiens 133-136 21742973-6 2011 Under conditions of low extracellular tryptophan, expression of this novel transporter significantly increases tryptophan entry into IDO(+) tumors relative to tryptophan uptake through the low-affinity System L alone, and further decreases tryptophan levels in the microenvironment. Tryptophan 111-121 indoleamine 2,3-dioxygenase 1 Homo sapiens 133-136 21742973-6 2011 Under conditions of low extracellular tryptophan, expression of this novel transporter significantly increases tryptophan entry into IDO(+) tumors relative to tryptophan uptake through the low-affinity System L alone, and further decreases tryptophan levels in the microenvironment. Tryptophan 111-121 indoleamine 2,3-dioxygenase 1 Homo sapiens 133-136 21742973-6 2011 Under conditions of low extracellular tryptophan, expression of this novel transporter significantly increases tryptophan entry into IDO(+) tumors relative to tryptophan uptake through the low-affinity System L alone, and further decreases tryptophan levels in the microenvironment. Tryptophan 111-121 indoleamine 2,3-dioxygenase 1 Homo sapiens 133-136 21742973-8 2011 These findings highlight the ability of IDO-expressing tumor cells to thrive in a tryptophan-depleted microenvironment by expressing a novel, highly tryptophan-specific transporter, which is resistant to inhibition by most other amino acids. Tryptophan 82-92 indoleamine 2,3-dioxygenase 1 Homo sapiens 40-43 21742973-8 2011 These findings highlight the ability of IDO-expressing tumor cells to thrive in a tryptophan-depleted microenvironment by expressing a novel, highly tryptophan-specific transporter, which is resistant to inhibition by most other amino acids. Tryptophan 149-159 indoleamine 2,3-dioxygenase 1 Homo sapiens 40-43 21810259-1 2011 BACKGROUND: We have established that activation of the tryptophan degrading enzyme indoleamine 2,3 dioxygenase (IDO) mediates the switch from cytokine-induced sickness behavior to depressive-like behavior. Tryptophan 55-65 indoleamine 2,3-dioxygenase 1 Homo sapiens 112-115 21726069-2 2011 Tryptophan catabolism mediated by indoleamine 2,3-dioxygenase (IDO) is an important mechanism of peripheral immune tolerance contributing to tumoral immune resistance. Tryptophan 0-10 indoleamine 2,3-dioxygenase 1 Homo sapiens 34-61 21726069-2 2011 Tryptophan catabolism mediated by indoleamine 2,3-dioxygenase (IDO) is an important mechanism of peripheral immune tolerance contributing to tumoral immune resistance. Tryptophan 0-10 indoleamine 2,3-dioxygenase 1 Homo sapiens 63-66 21487895-1 2011 INTRODUCTION: Indoleamine 2,3-dioxygenase (IDO) can promote peripheral immune tolerance and control autoimmune responses through tryptophan catabolism. Tryptophan 129-139 indoleamine 2,3-dioxygenase 1 Homo sapiens 14-41 21778315-0 2011 Systemic changes of tryptophan catabolites via the indoleamine-2,3-dioxygenase pathway in primary cervical cancer. Tryptophan 20-30 indoleamine 2,3-dioxygenase 1 Homo sapiens 51-78 21778315-1 2011 BACKGROUND/AIM: Induction of tryptophan catabolism is mediated by inflammatory mechanisms including up-regulation of the immunoregulatory enzyme indoleamine-2,3-dioxygenase (IDO). Tryptophan 29-39 indoleamine 2,3-dioxygenase 1 Homo sapiens 145-172 21778315-1 2011 BACKGROUND/AIM: Induction of tryptophan catabolism is mediated by inflammatory mechanisms including up-regulation of the immunoregulatory enzyme indoleamine-2,3-dioxygenase (IDO). Tryptophan 29-39 indoleamine 2,3-dioxygenase 1 Homo sapiens 174-177 21487895-1 2011 INTRODUCTION: Indoleamine 2,3-dioxygenase (IDO) can promote peripheral immune tolerance and control autoimmune responses through tryptophan catabolism. Tryptophan 129-139 indoleamine 2,3-dioxygenase 1 Homo sapiens 43-46 21487895-3 2011 Impaired IDO-mediated tryptophan catabolism has been observed in some autoimmune diseases. Tryptophan 22-32 indoleamine 2,3-dioxygenase 1 Homo sapiens 9-12 21277567-8 2011 Increased inflammation was related to reduced tryptophan concentrations and increased kynurenine levels, suggestive of IDO-induced increased tryptophan catabolism. Tryptophan 141-151 indoleamine 2,3-dioxygenase 1 Homo sapiens 119-122 21718232-1 2011 Indoleamine 2,3-dioxygenase (IDO) is the rate limiting enzyme of the kynurenine pathway that degrades L-tryptophan, but a wider range of functions have now been proposed for this enzyme, including antioxidant activity. Tryptophan 102-114 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 21718232-1 2011 Indoleamine 2,3-dioxygenase (IDO) is the rate limiting enzyme of the kynurenine pathway that degrades L-tryptophan, but a wider range of functions have now been proposed for this enzyme, including antioxidant activity. Tryptophan 102-114 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 21076293-7 2011 Recent data also indicate strongly, that immune-mediated tryptophan degradation is crucially involved in the development of depression: IDO activation leads to the accumulation of neurotoxic metabolites, which are supposed to induce depressive-like behaviour. Tryptophan 57-67 indoleamine 2,3-dioxygenase 1 Homo sapiens 136-139 21434757-2 2011 Furthermore, accelerated tryptophan (Trp) degradation by the enzyme indoleamine 2,3-dioxygenase (IDO) is detectable in blood samples of patients by an increased kynurenine (Kyn) to Trp ratio (Kyn/Trp). Tryptophan 25-35 indoleamine 2,3-dioxygenase 1 Homo sapiens 68-95 21434757-2 2011 Furthermore, accelerated tryptophan (Trp) degradation by the enzyme indoleamine 2,3-dioxygenase (IDO) is detectable in blood samples of patients by an increased kynurenine (Kyn) to Trp ratio (Kyn/Trp). Tryptophan 25-35 indoleamine 2,3-dioxygenase 1 Homo sapiens 97-100 21434757-2 2011 Furthermore, accelerated tryptophan (Trp) degradation by the enzyme indoleamine 2,3-dioxygenase (IDO) is detectable in blood samples of patients by an increased kynurenine (Kyn) to Trp ratio (Kyn/Trp). Tryptophan 37-40 indoleamine 2,3-dioxygenase 1 Homo sapiens 68-95 21434757-2 2011 Furthermore, accelerated tryptophan (Trp) degradation by the enzyme indoleamine 2,3-dioxygenase (IDO) is detectable in blood samples of patients by an increased kynurenine (Kyn) to Trp ratio (Kyn/Trp). Tryptophan 37-40 indoleamine 2,3-dioxygenase 1 Homo sapiens 97-100 21434757-2 2011 Furthermore, accelerated tryptophan (Trp) degradation by the enzyme indoleamine 2,3-dioxygenase (IDO) is detectable in blood samples of patients by an increased kynurenine (Kyn) to Trp ratio (Kyn/Trp). Tryptophan 181-184 indoleamine 2,3-dioxygenase 1 Homo sapiens 68-95 21434757-2 2011 Furthermore, accelerated tryptophan (Trp) degradation by the enzyme indoleamine 2,3-dioxygenase (IDO) is detectable in blood samples of patients by an increased kynurenine (Kyn) to Trp ratio (Kyn/Trp). Tryptophan 181-184 indoleamine 2,3-dioxygenase 1 Homo sapiens 97-100 21434757-2 2011 Furthermore, accelerated tryptophan (Trp) degradation by the enzyme indoleamine 2,3-dioxygenase (IDO) is detectable in blood samples of patients by an increased kynurenine (Kyn) to Trp ratio (Kyn/Trp). Tryptophan 181-184 indoleamine 2,3-dioxygenase 1 Homo sapiens 68-95 21434757-2 2011 Furthermore, accelerated tryptophan (Trp) degradation by the enzyme indoleamine 2,3-dioxygenase (IDO) is detectable in blood samples of patients by an increased kynurenine (Kyn) to Trp ratio (Kyn/Trp). Tryptophan 181-184 indoleamine 2,3-dioxygenase 1 Homo sapiens 97-100 21377330-1 2011 PURPOSE: Indoleamine 2,3-dioxygenase (IDO) is a cytokine-inducible enzyme that participates in tryptophan (trp) and serotonin metabolism with an ability to modulate neuroinflammation. Tryptophan 95-105 indoleamine 2,3-dioxygenase 1 Homo sapiens 9-36 21377330-1 2011 PURPOSE: Indoleamine 2,3-dioxygenase (IDO) is a cytokine-inducible enzyme that participates in tryptophan (trp) and serotonin metabolism with an ability to modulate neuroinflammation. Tryptophan 95-105 indoleamine 2,3-dioxygenase 1 Homo sapiens 38-41 21377330-1 2011 PURPOSE: Indoleamine 2,3-dioxygenase (IDO) is a cytokine-inducible enzyme that participates in tryptophan (trp) and serotonin metabolism with an ability to modulate neuroinflammation. Tryptophan 107-110 indoleamine 2,3-dioxygenase 1 Homo sapiens 9-36 21377330-1 2011 PURPOSE: Indoleamine 2,3-dioxygenase (IDO) is a cytokine-inducible enzyme that participates in tryptophan (trp) and serotonin metabolism with an ability to modulate neuroinflammation. Tryptophan 107-110 indoleamine 2,3-dioxygenase 1 Homo sapiens 38-41 21492353-4 2011 The IDO enzyme pathway was assessed by MS assays using the ratio of product l-kyn to substrate trp. Tryptophan 95-98 indoleamine 2,3-dioxygenase 1 Homo sapiens 4-7 20822828-1 2011 Tryptophan-degrading enzyme indoleamine 2,3-dioxygenase (IDO) represents an antimicrobial and antitumoral immune effector mechanism, but IDO also suppresses T-cell responses and thus can cause immune system failure. Tryptophan 0-10 indoleamine 2,3-dioxygenase 1 Homo sapiens 28-55 20822828-1 2011 Tryptophan-degrading enzyme indoleamine 2,3-dioxygenase (IDO) represents an antimicrobial and antitumoral immune effector mechanism, but IDO also suppresses T-cell responses and thus can cause immune system failure. Tryptophan 0-10 indoleamine 2,3-dioxygenase 1 Homo sapiens 57-60 20822828-1 2011 Tryptophan-degrading enzyme indoleamine 2,3-dioxygenase (IDO) represents an antimicrobial and antitumoral immune effector mechanism, but IDO also suppresses T-cell responses and thus can cause immune system failure. Tryptophan 0-10 indoleamine 2,3-dioxygenase 1 Homo sapiens 137-140 20822828-3 2011 Compared to healthy controls, accelerated tryptophan degradation was observed in the blood of 20 patients with ovarian carcinoma as is reflected by an increased kynurenine to tryptophan ratio (kyn/trp) which allows an estimate of IDO activity. Tryptophan 42-52 indoleamine 2,3-dioxygenase 1 Homo sapiens 230-233 20822828-3 2011 Compared to healthy controls, accelerated tryptophan degradation was observed in the blood of 20 patients with ovarian carcinoma as is reflected by an increased kynurenine to tryptophan ratio (kyn/trp) which allows an estimate of IDO activity. Tryptophan 175-185 indoleamine 2,3-dioxygenase 1 Homo sapiens 230-233 20822828-3 2011 Compared to healthy controls, accelerated tryptophan degradation was observed in the blood of 20 patients with ovarian carcinoma as is reflected by an increased kynurenine to tryptophan ratio (kyn/trp) which allows an estimate of IDO activity. Tryptophan 197-200 indoleamine 2,3-dioxygenase 1 Homo sapiens 230-233 21445845-1 2011 Human indoleamine 2,3-dioxygenase (hIDO), a monomeric heme enzyme, catalyzes the oxidative degradation of L-tryptophan (L-Trp) and other indoleamine derivatives. Tryptophan 106-118 indoleamine 2,3-dioxygenase 1 Homo sapiens 35-39 21445845-1 2011 Human indoleamine 2,3-dioxygenase (hIDO), a monomeric heme enzyme, catalyzes the oxidative degradation of L-tryptophan (L-Trp) and other indoleamine derivatives. Tryptophan 120-125 indoleamine 2,3-dioxygenase 1 Homo sapiens 35-39 21445845-3 2011 This substrate inhibition of hIDO is a result of the binding of a second L-Trp molecule in an inhibitory substrate binding site of the enzyme. Tryptophan 73-78 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-33 20300979-1 2011 Indoleamine 2,3-dioxygenase (IDO), a catabolizing enzyme of tryptophan, is a novel immunosuppressive agent blocking T-cell activation in neoplastic cells, including acute myeloid leukemia (AML) cells. Tryptophan 60-70 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 20300979-1 2011 Indoleamine 2,3-dioxygenase (IDO), a catabolizing enzyme of tryptophan, is a novel immunosuppressive agent blocking T-cell activation in neoplastic cells, including acute myeloid leukemia (AML) cells. Tryptophan 60-70 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 21502325-6 2011 The unfavorable entropic factor for the peroxide reaction highlights the scenario that the structure of hIDO is not optimized for utilizing H(2)O(2) as a co-substrate for oxidizing L-Trp. Tryptophan 181-186 indoleamine 2,3-dioxygenase 1 Homo sapiens 104-108 21185346-0 2011 The new "5-HT" hypothesis of depression: cell-mediated immune activation induces indoleamine 2,3-dioxygenase, which leads to lower plasma tryptophan and an increased synthesis of detrimental tryptophan catabolites (TRYCATs), both of which contribute to the onset of depression. Tryptophan 138-148 indoleamine 2,3-dioxygenase 1 Homo sapiens 81-108 21185346-5 2011 There is evidence that activation of IDO reduces plasma tryptophan and increases TRYCAT synthesis in depressive states and that TDO activation may play a role as well. Tryptophan 56-66 indoleamine 2,3-dioxygenase 1 Homo sapiens 37-40 21185346-11 2011 It is concluded that activation of the TRYCAT pathway by IDO and TDO may be associated with the development of depressive symptoms through tryptophan depletion and the detrimental effects of TRYCATs. Tryptophan 139-149 indoleamine 2,3-dioxygenase 1 Homo sapiens 57-60 20938662-1 2011 Indoleamine 2,3-dioxygenase (IDO) exerts immunomodulatory effects due to enzymatic activities catalyzing the essential amino acid L-tryptophan. Tryptophan 130-142 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 20938662-1 2011 Indoleamine 2,3-dioxygenase (IDO) exerts immunomodulatory effects due to enzymatic activities catalyzing the essential amino acid L-tryptophan. Tryptophan 130-142 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 21328391-6 2011 The kynurenine to tryptophan (kyn/trp) ratio reflecting IDO activity was calculated. Tryptophan 18-28 indoleamine 2,3-dioxygenase 1 Homo sapiens 56-59 21328391-8 2011 A maximum kyn/trp ratio >202 micromol/mmol (high IDO level) was also associated with other parameters reflecting the severity of the disease and renal impairment. Tryptophan 14-17 indoleamine 2,3-dioxygenase 1 Homo sapiens 52-55 21328391-9 2011 Patients with high IDO levels had higher maximum serum creatinine (379 vs. 102 micromol/L, P<0.001), plasma C-reactive protein (104.1 vs. 72.1 mg/L, P=0.029), and blood leukocyte values (11.9 vs. 9.0 x 10(9) /L, P<0.001) compared to patients with kyn/trp ratio <= 202 micromol/mmol. Tryptophan 257-260 indoleamine 2,3-dioxygenase 1 Homo sapiens 19-22 21242993-5 2011 Moreover, we identify the tryptophan catabolizing enzyme indoleamine 2,3-dioxygenase (IDO) as the underlying molecular mechanism. Tryptophan 26-36 indoleamine 2,3-dioxygenase 1 Homo sapiens 57-84 21242993-5 2011 Moreover, we identify the tryptophan catabolizing enzyme indoleamine 2,3-dioxygenase (IDO) as the underlying molecular mechanism. Tryptophan 26-36 indoleamine 2,3-dioxygenase 1 Homo sapiens 86-89 21189261-1 2011 Indoleamine 2,3-dioxygenase (IDO) is the first and rate-limiting enzyme of tryptophan catabolism through the kynurenine pathway. Tryptophan 75-85 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 21189261-1 2011 Indoleamine 2,3-dioxygenase (IDO) is the first and rate-limiting enzyme of tryptophan catabolism through the kynurenine pathway. Tryptophan 75-85 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 21189261-6 2011 The absence of IDO also increased the tryptophan content of the caput epididymis and generated a parallel increase in caput epididymal protein content as a consequence of deficient proteasomal activity. Tryptophan 38-48 indoleamine 2,3-dioxygenase 1 Homo sapiens 15-18 21292009-2 2011 Indoleamine 2,3-dioxygenase (IDO) is inducible by inflammation and through tryptophan depletion and generation of kynurenine pathway products suppresses adaptive immune response. Tryptophan 75-85 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 21292009-2 2011 Indoleamine 2,3-dioxygenase (IDO) is inducible by inflammation and through tryptophan depletion and generation of kynurenine pathway products suppresses adaptive immune response. Tryptophan 75-85 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 21161299-8 2011 IFNG and IFN-alpha transcriptionally induce indoleamine-2,3-dioxygenase (IDO), the rate-limiting enzyme of the kynurenine (KYN) pathway of tryptophan (TRY) metabolism. Tryptophan 139-149 indoleamine 2,3-dioxygenase 1 Homo sapiens 44-71 21161299-8 2011 IFNG and IFN-alpha transcriptionally induce indoleamine-2,3-dioxygenase (IDO), the rate-limiting enzyme of the kynurenine (KYN) pathway of tryptophan (TRY) metabolism. Tryptophan 139-149 indoleamine 2,3-dioxygenase 1 Homo sapiens 73-76 20658274-4 2011 Differences in the activation of the enzyme indoleamine 2,3-dioxygenase (IDO) and in the tryptophan-kynurenine metabolism resulting in an increased tryptophan and serotonin degradation and probably in an increased production of quinolinic acid might play a key role in major depression (MD). Tryptophan 148-158 indoleamine 2,3-dioxygenase 1 Homo sapiens 73-76 21092022-1 2011 Immunomodulatory properties of IDO1 relate to tryptophan catabolism. Tryptophan 46-56 indoleamine 2,3-dioxygenase 1 Homo sapiens 31-35 21092022-2 2011 The degradation of tryptophan by IDO1 leads to suppression of T cell responses. Tryptophan 19-29 indoleamine 2,3-dioxygenase 1 Homo sapiens 33-37 21517756-1 2011 Indoleamine 2,3-dioxygenase (IDO) is an intracellular heme-containing enzyme that catalyzes the initial rate-limiting step in tryptophan degradation along the kynurenine pathway. Tryptophan 126-136 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 21517756-1 2011 Indoleamine 2,3-dioxygenase (IDO) is an intracellular heme-containing enzyme that catalyzes the initial rate-limiting step in tryptophan degradation along the kynurenine pathway. Tryptophan 126-136 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 21517758-4 2011 IDO can both deplete tryptophan in local tissue microenvironments and generate immunoregulatory catabolites, known as kynurenines. Tryptophan 21-31 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 21517758-6 2011 In turn, T(reg) cells induce IDO in dendritic cells (DCs) and convert inflammatory into regulatory DCs, which can further expand the T(reg) cell compartment by tryptophan catabolism. Tryptophan 160-170 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 21517758-8 2011 Thus, in the periphery, tolerogenic immune responses mediated by T(reg) cells can be induced and amplified by IDO, a tryptophan catabolizing enzyme that also contributes to the plasticity of the T(reg) cell lineage. Tryptophan 117-127 indoleamine 2,3-dioxygenase 1 Homo sapiens 110-113 21517759-1 2011 The enzyme indoleamine 2,3-dioxygenase (IDO, EC 1.13.11.42) belongs to the family of heme-containing oxidoreductases and catalyzes the first and rate-limiting step in the kynurenine pathway, the major pathway of tryptophan metabolism. Tryptophan 212-222 indoleamine 2,3-dioxygenase 1 Homo sapiens 11-38 21517759-1 2011 The enzyme indoleamine 2,3-dioxygenase (IDO, EC 1.13.11.42) belongs to the family of heme-containing oxidoreductases and catalyzes the first and rate-limiting step in the kynurenine pathway, the major pathway of tryptophan metabolism. Tryptophan 212-222 indoleamine 2,3-dioxygenase 1 Homo sapiens 40-43 21517759-4 2011 The active IDO conformer exists only in the presence of reducing cofactors (such as cytochrome b(5)), requiring the single electron reduction of ferric-to-ferrous iron (Fe(3+) Fe(2+)), which facilitates binding of L-Trp and O(2) to the enzyme active site. Tryptophan 214-219 indoleamine 2,3-dioxygenase 1 Homo sapiens 11-14 20691158-2 2010 In parallel, IFN-gamma induces the tryptophan-(trp)-degrading enzyme indoleamine 2,3-dioxygenase (IDO) and triggers the formation of reactive oxygen species (ROS). Tryptophan 35-45 indoleamine 2,3-dioxygenase 1 Homo sapiens 69-96 21322487-4 2011 The Fe-O2 and the O-O stretching frequencies of the IDO-Trp-O2 ternary complex at Trp concentrations of 50 microM and 8 mM are essentially identical. Tryptophan 56-59 indoleamine 2,3-dioxygenase 1 Homo sapiens 52-55 21461581-4 2011 The enzymatic activity of IDO was estimated by determining tryptophan and kynurenine concentrations in the cell culture medium by an amino acid analyzer. Tryptophan 59-69 indoleamine 2,3-dioxygenase 1 Homo sapiens 26-29 21084050-1 2010 BACKGROUND: Hemodialysis patients often present with increased concentrations of tryptophan catabolites perhaps related to an enhanced activity of tryptophan-degrading enzyme indoleamine 2,3-dioxygenase (IDO) that is inducible by pro-inflammatory stimuli. Tryptophan 81-91 indoleamine 2,3-dioxygenase 1 Homo sapiens 175-202 21084050-1 2010 BACKGROUND: Hemodialysis patients often present with increased concentrations of tryptophan catabolites perhaps related to an enhanced activity of tryptophan-degrading enzyme indoleamine 2,3-dioxygenase (IDO) that is inducible by pro-inflammatory stimuli. Tryptophan 81-91 indoleamine 2,3-dioxygenase 1 Homo sapiens 204-207 21084050-1 2010 BACKGROUND: Hemodialysis patients often present with increased concentrations of tryptophan catabolites perhaps related to an enhanced activity of tryptophan-degrading enzyme indoleamine 2,3-dioxygenase (IDO) that is inducible by pro-inflammatory stimuli. Tryptophan 147-157 indoleamine 2,3-dioxygenase 1 Homo sapiens 175-202 21084050-1 2010 BACKGROUND: Hemodialysis patients often present with increased concentrations of tryptophan catabolites perhaps related to an enhanced activity of tryptophan-degrading enzyme indoleamine 2,3-dioxygenase (IDO) that is inducible by pro-inflammatory stimuli. Tryptophan 147-157 indoleamine 2,3-dioxygenase 1 Homo sapiens 204-207 21028817-0 2010 A specific interaction of L-tryptophan with CO of CO-bound indoleamine 2,3-dioxygenase identified by resonance Raman spectroscopy. Tryptophan 26-38 indoleamine 2,3-dioxygenase 1 Homo sapiens 59-86 21028817-1 2010 Indoleamine 2,3-dioxygenase (IDO) is a heme enzyme which catalyzes dioxygenation of l-Trp (tryptophan), yielding N-formylkynurenine. Tryptophan 84-89 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 21028817-1 2010 Indoleamine 2,3-dioxygenase (IDO) is a heme enzyme which catalyzes dioxygenation of l-Trp (tryptophan), yielding N-formylkynurenine. Tryptophan 84-89 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 21028817-1 2010 Indoleamine 2,3-dioxygenase (IDO) is a heme enzyme which catalyzes dioxygenation of l-Trp (tryptophan), yielding N-formylkynurenine. Tryptophan 91-101 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 21028817-1 2010 Indoleamine 2,3-dioxygenase (IDO) is a heme enzyme which catalyzes dioxygenation of l-Trp (tryptophan), yielding N-formylkynurenine. Tryptophan 91-101 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 21028817-2 2010 IDO thus plays a key role in l-Trp catabolism in mammals. Tryptophan 29-34 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 21028817-4 2010 Binding of CO to l-Trp-bound IDO causes a significant change in the electronic and RR spectra of the heme, indicating that the pi* orbitals of the carbon atom of CO interact with pi orbitals of Fe and the porphyrin. Tryptophan 19-22 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 19857540-6 2010 Tryptophan depletion or "deletion" by induction of indoleamine-2,3-dioxygenase (IDO), the first step in oxidative tryptophan metabolism, is a known mechanism for immune suppression that is of critical importance in cancer and pregnancy, and, potentially, in HIV/AIDS. Tryptophan 0-10 indoleamine 2,3-dioxygenase 1 Homo sapiens 51-78 19857540-6 2010 Tryptophan depletion or "deletion" by induction of indoleamine-2,3-dioxygenase (IDO), the first step in oxidative tryptophan metabolism, is a known mechanism for immune suppression that is of critical importance in cancer and pregnancy, and, potentially, in HIV/AIDS. Tryptophan 0-10 indoleamine 2,3-dioxygenase 1 Homo sapiens 80-83 19857540-6 2010 Tryptophan depletion or "deletion" by induction of indoleamine-2,3-dioxygenase (IDO), the first step in oxidative tryptophan metabolism, is a known mechanism for immune suppression that is of critical importance in cancer and pregnancy, and, potentially, in HIV/AIDS. Tryptophan 114-124 indoleamine 2,3-dioxygenase 1 Homo sapiens 51-78 19857540-6 2010 Tryptophan depletion or "deletion" by induction of indoleamine-2,3-dioxygenase (IDO), the first step in oxidative tryptophan metabolism, is a known mechanism for immune suppression that is of critical importance in cancer and pregnancy, and, potentially, in HIV/AIDS. Tryptophan 114-124 indoleamine 2,3-dioxygenase 1 Homo sapiens 80-83 19857540-9 2010 This model is directly supported by evidence that antioxidants can counteract indoleamine-2,3-dioxygenase (IDO), providing the critical link between oxidative stress and tryptophan metabolism proposed here. Tryptophan 170-180 indoleamine 2,3-dioxygenase 1 Homo sapiens 78-105 19857540-9 2010 This model is directly supported by evidence that antioxidants can counteract indoleamine-2,3-dioxygenase (IDO), providing the critical link between oxidative stress and tryptophan metabolism proposed here. Tryptophan 170-180 indoleamine 2,3-dioxygenase 1 Homo sapiens 107-110 21041655-3 2010 Furthermore, we found that Ahr is required to induce indoleamine 2,3-dioxygenase (IDO) expression, an immunosuppressive enzyme that catabolizes tryptophan into kynurenine (Kyn) and other metabolites in DC. Tryptophan 144-154 indoleamine 2,3-dioxygenase 1 Homo sapiens 53-80 21041655-3 2010 Furthermore, we found that Ahr is required to induce indoleamine 2,3-dioxygenase (IDO) expression, an immunosuppressive enzyme that catabolizes tryptophan into kynurenine (Kyn) and other metabolites in DC. Tryptophan 144-154 indoleamine 2,3-dioxygenase 1 Homo sapiens 82-85 20732369-1 2010 Indoleamine 2,3-dioxygenase (IDO), an enzyme expressed in many cell types, catalyses degradation of tryptophan (Trp) to kynurenine (Kyn) and may exert immunosuppressive functions, mediated mainly by kynurenines. Tryptophan 100-110 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 20732369-1 2010 Indoleamine 2,3-dioxygenase (IDO), an enzyme expressed in many cell types, catalyses degradation of tryptophan (Trp) to kynurenine (Kyn) and may exert immunosuppressive functions, mediated mainly by kynurenines. Tryptophan 100-110 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 20732369-1 2010 Indoleamine 2,3-dioxygenase (IDO), an enzyme expressed in many cell types, catalyses degradation of tryptophan (Trp) to kynurenine (Kyn) and may exert immunosuppressive functions, mediated mainly by kynurenines. Tryptophan 112-115 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 20732369-1 2010 Indoleamine 2,3-dioxygenase (IDO), an enzyme expressed in many cell types, catalyses degradation of tryptophan (Trp) to kynurenine (Kyn) and may exert immunosuppressive functions, mediated mainly by kynurenines. Tryptophan 112-115 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 21094802-1 2010 BACKGROUND: Indoleamine 2,3-dioxygenase (IDO) is a tryptophan-degrading enzyme that suppresses T-lymphocyte activity. Tryptophan 51-61 indoleamine 2,3-dioxygenase 1 Homo sapiens 12-39 21094802-1 2010 BACKGROUND: Indoleamine 2,3-dioxygenase (IDO) is a tryptophan-degrading enzyme that suppresses T-lymphocyte activity. Tryptophan 51-61 indoleamine 2,3-dioxygenase 1 Homo sapiens 41-44 20570568-3 2010 The tryptophan catabolizing enzyme indoleamine 2,3-dioxygenase (IDO) is considered critical for regulating immune responses and suppression of inflammation. Tryptophan 4-14 indoleamine 2,3-dioxygenase 1 Homo sapiens 64-67 21084489-3 2011 One ISG candidate, indoleamine 2,3-dioxygenase (IDO), an IFN-gamma-induced enzyme catalyzing tryptophan degradation, efficiently reduced the level of intracellular HBV DNA without altering the steady-state level of viral RNA. Tryptophan 93-103 indoleamine 2,3-dioxygenase 1 Homo sapiens 48-51 21084489-4 2011 Furthermore, expression of an enzymatically inactive IDO mutant did not inhibit HBV replication, and tryptophan supplementation in culture completely restored HBV replication in IDO-expressing cells, indicating that the antiviral effect elicited by IDO is mediated by tryptophan deprivation. Tryptophan 101-111 indoleamine 2,3-dioxygenase 1 Homo sapiens 178-181 21084489-4 2011 Furthermore, expression of an enzymatically inactive IDO mutant did not inhibit HBV replication, and tryptophan supplementation in culture completely restored HBV replication in IDO-expressing cells, indicating that the antiviral effect elicited by IDO is mediated by tryptophan deprivation. Tryptophan 101-111 indoleamine 2,3-dioxygenase 1 Homo sapiens 178-181 21084489-5 2011 Interestingly, IDO-mediated tryptophan deprivation preferentially inhibited viral protein translation and genome replication but did not significantly alter global cellular protein synthesis. Tryptophan 28-38 indoleamine 2,3-dioxygenase 1 Homo sapiens 15-18 21084489-6 2011 Finally, tryptophan supplementation was able to completely restore HBV replication in IFN-gamma- but not IFN-alpha-treated cells, which strongly argues that IDO is the primary mediator of IFN-gamma-elicited antiviral response against HBV in human hepatocyte-derived cells. Tryptophan 9-19 indoleamine 2,3-dioxygenase 1 Homo sapiens 157-160 20941617-0 2011 Indoleamine 2,3-dioxygenase and regulatory function: tryptophan starvation and beyond. Tryptophan 53-63 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 20941617-1 2011 Indoleamine 2,3-dioxygenase (IDO) is an ancestral enzyme that, initially confined to the regulation of tryptophan availability in local tissue microenvironments, is now considered to play a wider role that extends to homeostasis and plasticity of the immune system. Tryptophan 103-113 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 20941617-1 2011 Indoleamine 2,3-dioxygenase (IDO) is an ancestral enzyme that, initially confined to the regulation of tryptophan availability in local tissue microenvironments, is now considered to play a wider role that extends to homeostasis and plasticity of the immune system. Tryptophan 103-113 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 21617756-1 2011 PURPOSE: To screen for sequence variations in the IDO gene that encodes indoleamine 2, 3- dioxygenase (IDO), the first rate limiting enzyme involved in the tryptophan catabolism which results in the production of UV filters playing a role in the maintenance of lens transparency. Tryptophan 156-166 indoleamine 2,3-dioxygenase 1 Homo sapiens 50-53 21617756-1 2011 PURPOSE: To screen for sequence variations in the IDO gene that encodes indoleamine 2, 3- dioxygenase (IDO), the first rate limiting enzyme involved in the tryptophan catabolism which results in the production of UV filters playing a role in the maintenance of lens transparency. Tryptophan 156-166 indoleamine 2,3-dioxygenase 1 Homo sapiens 103-106 21712776-2 2011 Induction of indoleamine 2,3-dioxygenase (IDO) with consequent synthesis of tryptophan catabolites (TRYCATs) and lowered tryptophan are associated with the onset of depression in the puerperium and during interferon-alpha treatment. Tryptophan 76-86 indoleamine 2,3-dioxygenase 1 Homo sapiens 13-40 21712776-2 2011 Induction of indoleamine 2,3-dioxygenase (IDO) with consequent synthesis of tryptophan catabolites (TRYCATs) and lowered tryptophan are associated with the onset of depression in the puerperium and during interferon-alpha treatment. Tryptophan 76-86 indoleamine 2,3-dioxygenase 1 Homo sapiens 42-45 21712776-2 2011 Induction of indoleamine 2,3-dioxygenase (IDO) with consequent synthesis of tryptophan catabolites (TRYCATs) and lowered tryptophan are associated with the onset of depression in the puerperium and during interferon-alpha treatment. Tryptophan 121-131 indoleamine 2,3-dioxygenase 1 Homo sapiens 13-40 21712776-2 2011 Induction of indoleamine 2,3-dioxygenase (IDO) with consequent synthesis of tryptophan catabolites (TRYCATs) and lowered tryptophan are associated with the onset of depression in the puerperium and during interferon-alpha treatment. Tryptophan 121-131 indoleamine 2,3-dioxygenase 1 Homo sapiens 42-45 20940053-7 2011 On the contrary, the time course of Kyn markedly arose during treatment, paralleled by a significant increase of [Kyn/Trp]x10(3) ratio, an index used to measure IDO activity. Tryptophan 118-121 indoleamine 2,3-dioxygenase 1 Homo sapiens 161-164 20940053-10 2011 Our results support the hypothesis that the increased IDO-mediated tryptophan metabolism along the Kyn pathway, leading to plasma Trp depletion and a decline of serotonin pathway, concurs to the development of depressive symptoms observed in HCV patients undergoing IFN-alpha therapy. Tryptophan 67-77 indoleamine 2,3-dioxygenase 1 Homo sapiens 54-57 20940053-10 2011 Our results support the hypothesis that the increased IDO-mediated tryptophan metabolism along the Kyn pathway, leading to plasma Trp depletion and a decline of serotonin pathway, concurs to the development of depressive symptoms observed in HCV patients undergoing IFN-alpha therapy. Tryptophan 130-133 indoleamine 2,3-dioxygenase 1 Homo sapiens 54-57 21980470-4 2011 METHODOLOGY/PRINCIPAL FINDINGS: A PCR-sequencing strategy, applied to DNA samples from healthy Caucasians, allowed us to identify a VNTR polymorphism in the IDO1 promoter, which correlates significantly with serum tryptophan concentration, controlled partially by IDO activity, in female subjects, but not in males. Tryptophan 214-224 indoleamine 2,3-dioxygenase 1 Homo sapiens 157-161 21980470-4 2011 METHODOLOGY/PRINCIPAL FINDINGS: A PCR-sequencing strategy, applied to DNA samples from healthy Caucasians, allowed us to identify a VNTR polymorphism in the IDO1 promoter, which correlates significantly with serum tryptophan concentration, controlled partially by IDO activity, in female subjects, but not in males. Tryptophan 214-224 indoleamine 2,3-dioxygenase 1 Homo sapiens 157-160 21731667-4 2011 Increased IDO activity (measured by the kynurenine to tryptophan [KT] ratio in plasma) causes T-cell apoptosis, vasodilation and nitric oxide synthase inhibition. Tryptophan 54-64 indoleamine 2,3-dioxygenase 1 Homo sapiens 10-13 21731667-10 2011 IDO-mediated tryptophan catabolism is associated with dysregulated immune responses and impaired microvascular reactivity in sepsis and may link these two fundamental processes in sepsis pathophysiology. Tryptophan 13-23 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 21625531-2 2011 IDO is expressed in tumors and tumor-draining lymph nodes and degrades tryptophan (trp) to create an immunsuppressive micromilieu both by depleting trp and by accumulating immunosuppressive metabolites of the kynurenine (kyn) pathway. Tryptophan 71-81 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 21625531-2 2011 IDO is expressed in tumors and tumor-draining lymph nodes and degrades tryptophan (trp) to create an immunsuppressive micromilieu both by depleting trp and by accumulating immunosuppressive metabolites of the kynurenine (kyn) pathway. Tryptophan 83-86 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 21625531-2 2011 IDO is expressed in tumors and tumor-draining lymph nodes and degrades tryptophan (trp) to create an immunsuppressive micromilieu both by depleting trp and by accumulating immunosuppressive metabolites of the kynurenine (kyn) pathway. Tryptophan 148-151 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 21042238-3 2010 Recent research demonstrated that MSCs express the tryptophan-catabolizing enzyme indoleamine 2,3-dioxygenase (IDO), known to suppress T-cell responses. Tryptophan 51-61 indoleamine 2,3-dioxygenase 1 Homo sapiens 82-109 21042238-3 2010 Recent research demonstrated that MSCs express the tryptophan-catabolizing enzyme indoleamine 2,3-dioxygenase (IDO), known to suppress T-cell responses. Tryptophan 51-61 indoleamine 2,3-dioxygenase 1 Homo sapiens 111-114 21224538-2 2010 IDO activity can be measured by tryptophan (Trp)/kynurenine (Kyn) ratio. Tryptophan 32-42 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 21224538-2 2010 IDO activity can be measured by tryptophan (Trp)/kynurenine (Kyn) ratio. Tryptophan 44-47 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 20715188-1 2010 The first and rate-limiting step of the kynurenine pathway, in which tryptophan (Trp) is converted to N-formylkynurenine is catalyzed by two heme-containing proteins, Indoleamine 2,3-dioxygenase (IDO), and Tryptophan 2,3-dioxygenase (TDO). Tryptophan 69-79 indoleamine 2,3-dioxygenase 1 Homo sapiens 167-194 20715188-1 2010 The first and rate-limiting step of the kynurenine pathway, in which tryptophan (Trp) is converted to N-formylkynurenine is catalyzed by two heme-containing proteins, Indoleamine 2,3-dioxygenase (IDO), and Tryptophan 2,3-dioxygenase (TDO). Tryptophan 69-79 indoleamine 2,3-dioxygenase 1 Homo sapiens 196-199 20715188-1 2010 The first and rate-limiting step of the kynurenine pathway, in which tryptophan (Trp) is converted to N-formylkynurenine is catalyzed by two heme-containing proteins, Indoleamine 2,3-dioxygenase (IDO), and Tryptophan 2,3-dioxygenase (TDO). Tryptophan 81-84 indoleamine 2,3-dioxygenase 1 Homo sapiens 167-194 20715188-1 2010 The first and rate-limiting step of the kynurenine pathway, in which tryptophan (Trp) is converted to N-formylkynurenine is catalyzed by two heme-containing proteins, Indoleamine 2,3-dioxygenase (IDO), and Tryptophan 2,3-dioxygenase (TDO). Tryptophan 81-84 indoleamine 2,3-dioxygenase 1 Homo sapiens 196-199 20648630-1 2010 Indoleamine 2,3-dioxygenase (IDO), a tryptophan degrading enzyme, is a potent immunomodulatory factor. Tryptophan 37-47 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 20648630-1 2010 Indoleamine 2,3-dioxygenase (IDO), a tryptophan degrading enzyme, is a potent immunomodulatory factor. Tryptophan 37-47 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 20648630-3 2010 However, the mechanism(s) of this selective effect of IDO-induced low tryptophan environment is not elucidated. Tryptophan 70-80 indoleamine 2,3-dioxygenase 1 Homo sapiens 54-57 20648630-4 2010 The aim of present study was to investigate whether the activity of general control non-derepressible-2(GCN2) kinase stress-responsive pathway and its known inhibitor, protein IMPACT homolog, in immune and skin cells are differentially regulated in response to IDO-induced low tryptophan environment. Tryptophan 277-287 indoleamine 2,3-dioxygenase 1 Homo sapiens 261-264 20648630-10 2010 This may be due to the ability of IMPACT to recover the effects of IDO-mediated tryptophan depletion (GCN2 dependent) but not the effects of IDO-generated cytotoxic metabolites. Tryptophan 80-90 indoleamine 2,3-dioxygenase 1 Homo sapiens 67-70 20691158-2 2010 In parallel, IFN-gamma induces the tryptophan-(trp)-degrading enzyme indoleamine 2,3-dioxygenase (IDO) and triggers the formation of reactive oxygen species (ROS). Tryptophan 35-45 indoleamine 2,3-dioxygenase 1 Homo sapiens 98-101 20691158-2 2010 In parallel, IFN-gamma induces the tryptophan-(trp)-degrading enzyme indoleamine 2,3-dioxygenase (IDO) and triggers the formation of reactive oxygen species (ROS). Tryptophan 47-50 indoleamine 2,3-dioxygenase 1 Homo sapiens 69-96 20691158-2 2010 In parallel, IFN-gamma induces the tryptophan-(trp)-degrading enzyme indoleamine 2,3-dioxygenase (IDO) and triggers the formation of reactive oxygen species (ROS). Tryptophan 47-50 indoleamine 2,3-dioxygenase 1 Homo sapiens 98-101 20691158-7 2010 The increase of the kyn to trp quotient indicates accelerated IDO activity. Tryptophan 27-30 indoleamine 2,3-dioxygenase 1 Homo sapiens 62-65 20435158-2 2010 IFN-gamma induces the expression of indoleamine 2,3-dioxygenase (IDO) and thereby enhances the production of kynurenines from l-tryptophan. Tryptophan 126-138 indoleamine 2,3-dioxygenase 1 Homo sapiens 36-63 20081878-8 2010 Exposure to vitamin D resulted in increased expression of IDO, an enzyme responsible for tryptophan metabolism that is upregulated in tolerizing DCs. Tryptophan 89-99 indoleamine 2,3-dioxygenase 1 Homo sapiens 58-61 20435158-2 2010 IFN-gamma induces the expression of indoleamine 2,3-dioxygenase (IDO) and thereby enhances the production of kynurenines from l-tryptophan. Tryptophan 126-138 indoleamine 2,3-dioxygenase 1 Homo sapiens 65-68 20424892-1 2010 Indoleamine 2,3-dioxygenase (IDO) is an enzyme that suppresses adaptive T-cell immunity by catabolizing tryptophan from the cellular microenvironment. Tryptophan 104-114 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 20424892-1 2010 Indoleamine 2,3-dioxygenase (IDO) is an enzyme that suppresses adaptive T-cell immunity by catabolizing tryptophan from the cellular microenvironment. Tryptophan 104-114 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 27713369-3 2010 The suppressive effect of both cannabinoids on mitogen-induced tryptophan degradation mediated by indoleamine-2,3-dioxygenase (IDO), suggests an additional mechanism by which antidepressive effects of cannabinoids might be linked to the serotonergic system. Tryptophan 63-73 indoleamine 2,3-dioxygenase 1 Homo sapiens 98-125 27713369-3 2010 The suppressive effect of both cannabinoids on mitogen-induced tryptophan degradation mediated by indoleamine-2,3-dioxygenase (IDO), suggests an additional mechanism by which antidepressive effects of cannabinoids might be linked to the serotonergic system. Tryptophan 63-73 indoleamine 2,3-dioxygenase 1 Homo sapiens 127-130 20361220-1 2010 Tryptophan dioxygenase (TDO) and indoleamine 2,3-dioxygenase (IDO) are two heme-containing enzymes which catalyze the conversion of L: -tryptophan to N-formylkynurenine (NFK). Tryptophan 132-146 indoleamine 2,3-dioxygenase 1 Homo sapiens 33-60 20361220-1 2010 Tryptophan dioxygenase (TDO) and indoleamine 2,3-dioxygenase (IDO) are two heme-containing enzymes which catalyze the conversion of L: -tryptophan to N-formylkynurenine (NFK). Tryptophan 132-146 indoleamine 2,3-dioxygenase 1 Homo sapiens 62-65 20406333-3 2010 The KP is initiated by pro-inflammatory cytokines via induction of the enzyme indoleamine 2,3-dioxygenase (IDO), which degrades tryptophan (TRP) into kynurenine (KYN). Tryptophan 128-138 indoleamine 2,3-dioxygenase 1 Homo sapiens 107-110 20406333-3 2010 The KP is initiated by pro-inflammatory cytokines via induction of the enzyme indoleamine 2,3-dioxygenase (IDO), which degrades tryptophan (TRP) into kynurenine (KYN). Tryptophan 140-143 indoleamine 2,3-dioxygenase 1 Homo sapiens 107-110 20484729-1 2010 New data from Favre and colleagues strengthen the link between activation of the tryptophan oxidation (TOx) pathway--via the indoleamine 2,3-dioxygenase enzymes IDO1 and IDO2--and chronic inflammation in progressive HIV disease. Tryptophan 81-91 indoleamine 2,3-dioxygenase 1 Homo sapiens 161-165 20350764-1 2010 OBJECTIVE: Indoleamine 2,3-dioxygenase (IDO) is a tryptophan-catabolizing enzyme that induces tolerance to host immune surveillance within the tumor microenvironment. Tryptophan 50-60 indoleamine 2,3-dioxygenase 1 Homo sapiens 11-38 20350764-1 2010 OBJECTIVE: Indoleamine 2,3-dioxygenase (IDO) is a tryptophan-catabolizing enzyme that induces tolerance to host immune surveillance within the tumor microenvironment. Tryptophan 50-60 indoleamine 2,3-dioxygenase 1 Homo sapiens 40-43 20689575-13 2010 Since patients showed Trp catabolism already prior to surgery, IDO is also a possible target enzyme for humans modulating immune homeostasis and mood. Tryptophan 22-25 indoleamine 2,3-dioxygenase 1 Homo sapiens 63-66 20693847-3 2010 IDO is an inducible enzyme that catalyzes the rate-limiting first step in tryptophan catabolism. Tryptophan 74-84 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 20693847-5 2010 IDO causes immunosuppression through breakdown of tryptophan in the tumor microenvironment and tumor-draining lymph nodes. Tryptophan 50-60 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 20476772-1 2010 Human indoleamine 2,3-dioxygenase (hIDO) is an intracellular heme-containing enzyme, which catalyzes the initial and rate-determining step of l-tryptophan (l-Trp) metabolism via the kynurenine pathway in nonhepatic tissues. Tryptophan 142-154 indoleamine 2,3-dioxygenase 1 Homo sapiens 35-39 20476772-1 2010 Human indoleamine 2,3-dioxygenase (hIDO) is an intracellular heme-containing enzyme, which catalyzes the initial and rate-determining step of l-tryptophan (l-Trp) metabolism via the kynurenine pathway in nonhepatic tissues. Tryptophan 156-161 indoleamine 2,3-dioxygenase 1 Homo sapiens 35-39 20633104-4 2010 One of the mechanisms by which chronic inflammation might trigger and/or maintain the development of MetS/AAND is transcriptional induction of indoleamine 2,3-dioxygenase (IDO), rate-limiting enzyme of tryptophan (TRY)-kynurenine (KYN) pathway, by pro-inflammatory cytokines (PIC). Tryptophan 202-212 indoleamine 2,3-dioxygenase 1 Homo sapiens 143-170 20633104-4 2010 One of the mechanisms by which chronic inflammation might trigger and/or maintain the development of MetS/AAND is transcriptional induction of indoleamine 2,3-dioxygenase (IDO), rate-limiting enzyme of tryptophan (TRY)-kynurenine (KYN) pathway, by pro-inflammatory cytokines (PIC). Tryptophan 202-212 indoleamine 2,3-dioxygenase 1 Homo sapiens 172-175 19765856-3 2010 IFN-gamma induces several biochemical pathways in human monocytes, among them neopterin formation by GTP-cyclohydrolase I (GTP-CH I) and tryptophan degradation by the enzyme indoleamine 2,3-dioxygenase (IDO). Tryptophan 137-147 indoleamine 2,3-dioxygenase 1 Homo sapiens 174-201 19765856-4 2010 IDO-mediated tryptophan deprivation efficiently inhibits the growth of proliferating cells and microbes, thus we wanted to examine whether enhanced tryptophan degradation by monocytic precursor cells also suppresses erythropoiesis. Tryptophan 13-23 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 20428785-2 2010 Mechanistically, since IDO is a rate-limiting enzyme of the kynurenine pathway responsible for tryptophan catabolism, the prevailing explanation for its immunosuppressive action is based on the assumption that the presence of IDO in selected cell populations would consume local tryptophan and subsequently starve adjacent maternal T-cells of this essential amino acid. Tryptophan 95-105 indoleamine 2,3-dioxygenase 1 Homo sapiens 23-26 20428785-2 2010 Mechanistically, since IDO is a rate-limiting enzyme of the kynurenine pathway responsible for tryptophan catabolism, the prevailing explanation for its immunosuppressive action is based on the assumption that the presence of IDO in selected cell populations would consume local tryptophan and subsequently starve adjacent maternal T-cells of this essential amino acid. Tryptophan 95-105 indoleamine 2,3-dioxygenase 1 Homo sapiens 226-229 20428785-2 2010 Mechanistically, since IDO is a rate-limiting enzyme of the kynurenine pathway responsible for tryptophan catabolism, the prevailing explanation for its immunosuppressive action is based on the assumption that the presence of IDO in selected cell populations would consume local tryptophan and subsequently starve adjacent maternal T-cells of this essential amino acid. Tryptophan 279-289 indoleamine 2,3-dioxygenase 1 Homo sapiens 23-26 20428785-3 2010 In this review, an alternative hypothesis is discussed, which suggests that IDO is mainly expressed in various types of antigen-presenting cells (such as placental syncytiotrophoblasts during pregnancy), and that its main function is to produce biologically-active tryptophan catabolites that will mediate immunosuppression. Tryptophan 265-275 indoleamine 2,3-dioxygenase 1 Homo sapiens 76-79 20428785-4 2010 Mechanistically, because these tryptophan catabolites are concentrated in a microenvironment surrounding the IDO-expressing dendritic cells, they will selectively suppress the proliferation of a sub-population of T-cells that are activated by the allogeneic antigen-presenting cells and ultimately wipe out this T-cell sub-population. Tryptophan 31-41 indoleamine 2,3-dioxygenase 1 Homo sapiens 109-112 20484731-0 2010 Tryptophan catabolism by indoleamine 2,3-dioxygenase 1 alters the balance of TH17 to regulatory T cells in HIV disease. Tryptophan 0-10 indoleamine 2,3-dioxygenase 1 Homo sapiens 25-54 20207585-3 2010 Pro-inflammatory cytokines, e.g. interferon-gamma (IFN-gamma), are the primary inducers of tryptophan-degrading enzyme indoleamine 2,3-dioxygenase (IDO) and of neopterin biosynthesis by GTP-cyclohydrolase I. Tryptophan 91-101 indoleamine 2,3-dioxygenase 1 Homo sapiens 119-146 20427394-2 2010 Indoleamine 2,3-dioxygenase (IDO) is an enzyme involved in tryptophan catabolism that is expressed by DCs isolated from tumour-draining lymph nodes. Tryptophan 59-69 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 20427394-2 2010 Indoleamine 2,3-dioxygenase (IDO) is an enzyme involved in tryptophan catabolism that is expressed by DCs isolated from tumour-draining lymph nodes. Tryptophan 59-69 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 20207585-3 2010 Pro-inflammatory cytokines, e.g. interferon-gamma (IFN-gamma), are the primary inducers of tryptophan-degrading enzyme indoleamine 2,3-dioxygenase (IDO) and of neopterin biosynthesis by GTP-cyclohydrolase I. Tryptophan 91-101 indoleamine 2,3-dioxygenase 1 Homo sapiens 148-151 20197554-1 2010 Indoleamine 2,3-dioxygenase-1 (IDO1; IDO) mediates oxidative cleavage of tryptophan, an amino acid essential for cell proliferation and survival. Tryptophan 73-83 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-29 20197554-1 2010 Indoleamine 2,3-dioxygenase-1 (IDO1; IDO) mediates oxidative cleavage of tryptophan, an amino acid essential for cell proliferation and survival. Tryptophan 73-83 indoleamine 2,3-dioxygenase 1 Homo sapiens 31-35 20197554-1 2010 Indoleamine 2,3-dioxygenase-1 (IDO1; IDO) mediates oxidative cleavage of tryptophan, an amino acid essential for cell proliferation and survival. Tryptophan 73-83 indoleamine 2,3-dioxygenase 1 Homo sapiens 31-34 20197554-9 2010 Analysis of plasma kynurenine/tryptophan levels in patients with cancer affirms that the IDO pathway is activated in multiple tumor types. Tryptophan 30-40 indoleamine 2,3-dioxygenase 1 Homo sapiens 89-92 19995374-3 2010 Indoleamine 2,3-dioxygenase (IDO) exerts intense immunomodulatory effects because of enzymatic activities that catalyze the breakdown of the essential amino acid L-tryptophan. Tryptophan 162-174 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 19995374-3 2010 Indoleamine 2,3-dioxygenase (IDO) exerts intense immunomodulatory effects because of enzymatic activities that catalyze the breakdown of the essential amino acid L-tryptophan. Tryptophan 162-174 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 21051918-2 2010 A recent study revealed that indoleamine 2,3-dioxygenase (IDO)-mediated tryptophan depletion was able to affect local tumor-infiltrating lymphocytes. Tryptophan 72-82 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-56 19918244-1 2010 Cytokine-induced activation of indoleamine 2,3-dioxygenase (IDO) catabolizes L-tryptophan (TRP) into L-kynurenine (KYN), which is metabolized to quinolinic acid (QUIN) and kynurenic acid (KA). Tryptophan 77-89 indoleamine 2,3-dioxygenase 1 Homo sapiens 31-58 19918244-1 2010 Cytokine-induced activation of indoleamine 2,3-dioxygenase (IDO) catabolizes L-tryptophan (TRP) into L-kynurenine (KYN), which is metabolized to quinolinic acid (QUIN) and kynurenic acid (KA). Tryptophan 77-89 indoleamine 2,3-dioxygenase 1 Homo sapiens 60-63 19918244-1 2010 Cytokine-induced activation of indoleamine 2,3-dioxygenase (IDO) catabolizes L-tryptophan (TRP) into L-kynurenine (KYN), which is metabolized to quinolinic acid (QUIN) and kynurenic acid (KA). Tryptophan 91-94 indoleamine 2,3-dioxygenase 1 Homo sapiens 31-58 19918244-1 2010 Cytokine-induced activation of indoleamine 2,3-dioxygenase (IDO) catabolizes L-tryptophan (TRP) into L-kynurenine (KYN), which is metabolized to quinolinic acid (QUIN) and kynurenic acid (KA). Tryptophan 91-94 indoleamine 2,3-dioxygenase 1 Homo sapiens 60-63 20178337-5 2010 In this study we show that NADPH-cytochrome P450 reductase (CPR) is capable of supporting IDO activity in vitro and that oxidation of l-Trp follows substrate inhibition kinetics (k(cat) = 0.89 +/- 0.04 s(-1), K(m) = 0.72 +/- 0.15 microM, and K(i) = 9.4 +/- 2.0 microM). Tryptophan 134-139 indoleamine 2,3-dioxygenase 1 Homo sapiens 90-93 20178337-9 2010 Our data indicate that CPR is capable of supporting IDO activity in vitro and oxidation of tryptophan by IDO displays substrate stereochemistry dependent atypical kinetics which can be modulated by the addition of cytochrome b(5). Tryptophan 91-101 indoleamine 2,3-dioxygenase 1 Homo sapiens 105-108 20151841-2 2010 Indoleamine 2,3-dioxygenase (IDO), the rate-limiting enzyme of tryptophan catabolism, plays a pivotal role in immune tolerance and is induced during various inflammatory conditions. Tryptophan 63-73 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 20151841-2 2010 Indoleamine 2,3-dioxygenase (IDO), the rate-limiting enzyme of tryptophan catabolism, plays a pivotal role in immune tolerance and is induced during various inflammatory conditions. Tryptophan 63-73 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 19487045-1 2010 BACKGROUND: Indoleamine 2,3-dioxygenase (IDO) catalyzes the rate-limiting step of tryptophan (Trp) degradation along the kynurenine (Kyn) pathway. Tryptophan 82-92 indoleamine 2,3-dioxygenase 1 Homo sapiens 12-39 19487045-1 2010 BACKGROUND: Indoleamine 2,3-dioxygenase (IDO) catalyzes the rate-limiting step of tryptophan (Trp) degradation along the kynurenine (Kyn) pathway. Tryptophan 82-92 indoleamine 2,3-dioxygenase 1 Homo sapiens 41-44 19487045-1 2010 BACKGROUND: Indoleamine 2,3-dioxygenase (IDO) catalyzes the rate-limiting step of tryptophan (Trp) degradation along the kynurenine (Kyn) pathway. Tryptophan 94-97 indoleamine 2,3-dioxygenase 1 Homo sapiens 12-39 19487045-1 2010 BACKGROUND: Indoleamine 2,3-dioxygenase (IDO) catalyzes the rate-limiting step of tryptophan (Trp) degradation along the kynurenine (Kyn) pathway. Tryptophan 94-97 indoleamine 2,3-dioxygenase 1 Homo sapiens 41-44 19487045-2 2010 By depleting tryptophan, IDO is considered to be a fundamental immune escape mechanism for tumor cells. Tryptophan 13-23 indoleamine 2,3-dioxygenase 1 Homo sapiens 25-28 19487045-4 2010 Thus, the present study investigated IDO activity determined by serum Trp and Kyn concentrations in lung cancer and the correlation between the IDO activity and clinical parameters. Tryptophan 70-73 indoleamine 2,3-dioxygenase 1 Homo sapiens 37-40 19487045-6 2010 The IDO activity was estimated by calculating the serum Kyn-to-Trp ratio (Kyn/Trp ratio). Tryptophan 63-66 indoleamine 2,3-dioxygenase 1 Homo sapiens 4-7 19487045-6 2010 The IDO activity was estimated by calculating the serum Kyn-to-Trp ratio (Kyn/Trp ratio). Tryptophan 78-81 indoleamine 2,3-dioxygenase 1 Homo sapiens 4-7 19487045-8 2010 The IDO activity determined by the Kyn/Trp ratio was significantly higher in the patients than in the controls (47.1+/-21.3 vs. 32.9+/-9.10, respectively; p<0.0001). Tryptophan 39-42 indoleamine 2,3-dioxygenase 1 Homo sapiens 4-7 19958238-1 2010 The immunoregulatory enzyme indoleamine 2,3-dioxygenase (IDO) controls tryptophan metabolism and is induced by pro-inflammatory stimuli. Tryptophan 71-81 indoleamine 2,3-dioxygenase 1 Homo sapiens 28-55 19958238-1 2010 The immunoregulatory enzyme indoleamine 2,3-dioxygenase (IDO) controls tryptophan metabolism and is induced by pro-inflammatory stimuli. Tryptophan 71-81 indoleamine 2,3-dioxygenase 1 Homo sapiens 57-60 20100004-4 2010 AREAS COVERED IN THIS REVIEW: Advances in the biochemistry of IDO and our understanding of the biological relevance of IDO-mediated tryptophan consumption to the establishment of immune tolerance are summarised and discussed. Tryptophan 132-142 indoleamine 2,3-dioxygenase 1 Homo sapiens 119-122 19778568-2 2010 IDO metabolizes tryptophan (TRP) into kynurenine (KYN), thereby decreasing TRP availability to the brain. Tryptophan 16-26 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 19778568-2 2010 IDO metabolizes tryptophan (TRP) into kynurenine (KYN), thereby decreasing TRP availability to the brain. Tryptophan 28-31 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 19778568-2 2010 IDO metabolizes tryptophan (TRP) into kynurenine (KYN), thereby decreasing TRP availability to the brain. Tryptophan 75-78 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 19928918-4 2010 By locally degrading tryptophan, IDO inhibits the proliferation of T lymphocytes and induces T cell apoptosis, leading to suppression of T cell response. Tryptophan 21-31 indoleamine 2,3-dioxygenase 1 Homo sapiens 33-36 20000778-1 2010 The heme enzyme indoleamine 2,3-dioxygenase (IDO) plays an important immune regulatory role by catalyzing the oxidative degradation of l-tryptophan. Tryptophan 135-147 indoleamine 2,3-dioxygenase 1 Homo sapiens 16-43 20000778-1 2010 The heme enzyme indoleamine 2,3-dioxygenase (IDO) plays an important immune regulatory role by catalyzing the oxidative degradation of l-tryptophan. Tryptophan 135-147 indoleamine 2,3-dioxygenase 1 Homo sapiens 45-48 19941414-0 2010 Activation of indoleamine 2,3-dioxygenase-induced tryptophan degradation in advanced atherosclerotic plaques: Tampere vascular study. Tryptophan 50-60 indoleamine 2,3-dioxygenase 1 Homo sapiens 14-41 19941414-1 2010 OBJECTIVE: We aimed to characterize the expression of indoleamine 2,3-dioxygenase (IDO) or IDO-induced tryptophan degradation-dependent pathways, which may lead to suppression of T cells and possible protection against atherosclerosis. Tryptophan 103-113 indoleamine 2,3-dioxygenase 1 Homo sapiens 54-81 19941414-1 2010 OBJECTIVE: We aimed to characterize the expression of indoleamine 2,3-dioxygenase (IDO) or IDO-induced tryptophan degradation-dependent pathways, which may lead to suppression of T cells and possible protection against atherosclerosis. Tryptophan 103-113 indoleamine 2,3-dioxygenase 1 Homo sapiens 83-86 19941414-1 2010 OBJECTIVE: We aimed to characterize the expression of indoleamine 2,3-dioxygenase (IDO) or IDO-induced tryptophan degradation-dependent pathways, which may lead to suppression of T cells and possible protection against atherosclerosis. Tryptophan 103-113 indoleamine 2,3-dioxygenase 1 Homo sapiens 91-94 19249120-1 2010 High Mphi:T cell ratios suppress the immune response to the retroviral superantigen Mls by IFNgamma-triggered production of the arg- and trp-consuming enzymes iNOS and IDO. Tryptophan 137-140 indoleamine 2,3-dioxygenase 1 Homo sapiens 168-171 22084593-0 2010 IDO-Mediated Tryptophan Degradation in the Pathogenesis of Malignant Tumor Disease. Tryptophan 13-23 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 22084593-2 2010 Among other tumoricidal biochemical pathways, IFN-gamma induces the tryptophan-degrading enzyme indoleamine 2,3-dioxygenase (IDO) in a variety of cells including macrophages, dendritic cells (DCs) and tumor cells. Tryptophan 68-78 indoleamine 2,3-dioxygenase 1 Homo sapiens 96-123 22084593-2 2010 Among other tumoricidal biochemical pathways, IFN-gamma induces the tryptophan-degrading enzyme indoleamine 2,3-dioxygenase (IDO) in a variety of cells including macrophages, dendritic cells (DCs) and tumor cells. Tryptophan 68-78 indoleamine 2,3-dioxygenase 1 Homo sapiens 125-128 22084593-4 2010 Furthermore IDO activity during malignant tumor diseases seems to be part of the tumoricidal immune defense strategy, which in the long run is detrimental to the host, when tryptophan deprivation and production of pro-apoptotic tryptophan catabolites counteract T-cell responsiveness. Tryptophan 173-183 indoleamine 2,3-dioxygenase 1 Homo sapiens 12-15 22084593-4 2010 Furthermore IDO activity during malignant tumor diseases seems to be part of the tumoricidal immune defense strategy, which in the long run is detrimental to the host, when tryptophan deprivation and production of pro-apoptotic tryptophan catabolites counteract T-cell responsiveness. Tryptophan 228-238 indoleamine 2,3-dioxygenase 1 Homo sapiens 12-15 19487973-1 2010 Indoleamine 2,3-dioxygenase (IDO), which is the rate-limiting enzyme for tryptophan (trp) catabolism, may play a critical role in various inflammatory disorders. Tryptophan 73-83 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 19487973-1 2010 Indoleamine 2,3-dioxygenase (IDO), which is the rate-limiting enzyme for tryptophan (trp) catabolism, may play a critical role in various inflammatory disorders. Tryptophan 73-83 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 19487973-1 2010 Indoleamine 2,3-dioxygenase (IDO), which is the rate-limiting enzyme for tryptophan (trp) catabolism, may play a critical role in various inflammatory disorders. Tryptophan 85-88 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 19487973-1 2010 Indoleamine 2,3-dioxygenase (IDO), which is the rate-limiting enzyme for tryptophan (trp) catabolism, may play a critical role in various inflammatory disorders. Tryptophan 85-88 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 19487973-6 2010 The kyn-to-trp ratio (kyn/trp), reflecting the activity of the IDO enzyme, was calculated. Tryptophan 11-14 indoleamine 2,3-dioxygenase 1 Homo sapiens 63-66 19487973-6 2010 The kyn-to-trp ratio (kyn/trp), reflecting the activity of the IDO enzyme, was calculated. Tryptophan 26-29 indoleamine 2,3-dioxygenase 1 Homo sapiens 63-66 20204824-0 2010 Design of novel hypoxia-targeting IDO hybrid inhibitors conjugated with an unsubstituted L-TRP as an IDO affinity moiety. Tryptophan 89-94 indoleamine 2,3-dioxygenase 1 Homo sapiens 34-37 20204824-0 2010 Design of novel hypoxia-targeting IDO hybrid inhibitors conjugated with an unsubstituted L-TRP as an IDO affinity moiety. Tryptophan 89-94 indoleamine 2,3-dioxygenase 1 Homo sapiens 101-104 20204824-1 2010 We presented here design, syntheses and inhibitory activities of novel hypoxia-targeting IDO hybrid inhibitors conjugated with an unsubstituted L-Trp as an IDO affinity moiety without inhibitor 1MT, such as L-Trp-TPZ hybrids 1 (TX-2274), 2 (UTX-3), 3 (UTX-4), and 4 (UTX-2). Tryptophan 144-149 indoleamine 2,3-dioxygenase 1 Homo sapiens 89-92 20204824-1 2010 We presented here design, syntheses and inhibitory activities of novel hypoxia-targeting IDO hybrid inhibitors conjugated with an unsubstituted L-Trp as an IDO affinity moiety without inhibitor 1MT, such as L-Trp-TPZ hybrids 1 (TX-2274), 2 (UTX-3), 3 (UTX-4), and 4 (UTX-2). Tryptophan 144-149 indoleamine 2,3-dioxygenase 1 Homo sapiens 156-159 20204824-1 2010 We presented here design, syntheses and inhibitory activities of novel hypoxia-targeting IDO hybrid inhibitors conjugated with an unsubstituted L-Trp as an IDO affinity moiety without inhibitor 1MT, such as L-Trp-TPZ hybrids 1 (TX-2274), 2 (UTX-3), 3 (UTX-4), and 4 (UTX-2). Tryptophan 146-149 indoleamine 2,3-dioxygenase 1 Homo sapiens 89-92 20204824-1 2010 We presented here design, syntheses and inhibitory activities of novel hypoxia-targeting IDO hybrid inhibitors conjugated with an unsubstituted L-Trp as an IDO affinity moiety without inhibitor 1MT, such as L-Trp-TPZ hybrids 1 (TX-2274), 2 (UTX-3), 3 (UTX-4), and 4 (UTX-2). Tryptophan 146-149 indoleamine 2,3-dioxygenase 1 Homo sapiens 156-159 22084588-3 2010 According to recent data, degradation of L-tryptophan (TRP) via the kynurenine (KYN) pathway by the cytokine-inducible enzyme indoleamine 2,3-dioxygenase (IDO) could represent an important contributor to the deficient responsiveness of immunocompetent cells. Tryptophan 41-53 indoleamine 2,3-dioxygenase 1 Homo sapiens 155-158 22084588-3 2010 According to recent data, degradation of L-tryptophan (TRP) via the kynurenine (KYN) pathway by the cytokine-inducible enzyme indoleamine 2,3-dioxygenase (IDO) could represent an important contributor to the deficient responsiveness of immunocompetent cells. Tryptophan 55-58 indoleamine 2,3-dioxygenase 1 Homo sapiens 155-158 22084588-10 2010 Cytokines released during the pro-inflammatory response may induce the activity of IDO and thus accelerate TRP degradation. Tryptophan 107-110 indoleamine 2,3-dioxygenase 1 Homo sapiens 83-86 22084590-1 2010 In recent years tryptophan metabolism and its rate limiting enzyme indoleamine 2,3-dioxygenase (IDO) have attracted increasing attention for their potential to modulate immune responses including the regulation of transplantation tolerance. Tryptophan 16-26 indoleamine 2,3-dioxygenase 1 Homo sapiens 96-99 20379874-3 2010 Indoleamine 2,3 dioxygenase (IDO) is an enzyme that metabolises tryptophan and is known to be central in the regulation of immune responses. Tryptophan 64-74 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 20379874-3 2010 Indoleamine 2,3 dioxygenase (IDO) is an enzyme that metabolises tryptophan and is known to be central in the regulation of immune responses. Tryptophan 64-74 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 21051918-2 2010 A recent study revealed that indoleamine 2,3-dioxygenase (IDO)-mediated tryptophan depletion was able to affect local tumor-infiltrating lymphocytes. Tryptophan 72-82 indoleamine 2,3-dioxygenase 1 Homo sapiens 58-61 19828695-0 2009 Inducing the tryptophan catabolic pathway, indoleamine 2,3-dioxygenase (IDO), for suppression of graft-versus-host disease (GVHD) lethality. Tryptophan 13-23 indoleamine 2,3-dioxygenase 1 Homo sapiens 43-70 19828695-0 2009 Inducing the tryptophan catabolic pathway, indoleamine 2,3-dioxygenase (IDO), for suppression of graft-versus-host disease (GVHD) lethality. Tryptophan 13-23 indoleamine 2,3-dioxygenase 1 Homo sapiens 72-75 20037301-2 2009 IDO activity can be measured by tryptophan (Trp)/kynurenine (Kyn) ratio. Tryptophan 32-42 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 20037301-2 2009 IDO activity can be measured by tryptophan (Trp)/kynurenine (Kyn) ratio. Tryptophan 44-47 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 19783182-1 2009 BACKGROUND: Indoleamine 2,3-dioxygenase (IDO), an enzyme involved in the degradation of tryptophan (Try) to kynurenine (Kyn), is thought to suppress T-cell activity. Tryptophan 88-98 indoleamine 2,3-dioxygenase 1 Homo sapiens 12-39 19783182-1 2009 BACKGROUND: Indoleamine 2,3-dioxygenase (IDO), an enzyme involved in the degradation of tryptophan (Try) to kynurenine (Kyn), is thought to suppress T-cell activity. Tryptophan 88-98 indoleamine 2,3-dioxygenase 1 Homo sapiens 41-44 19434461-1 2009 BACKGROUND: Tryptophan catabolism via the kynurenine pathway, mediated by indoleamine 2,3-dioxygenase (IDO), is a mechanism involved in tumor immunoresistance. Tryptophan 12-22 indoleamine 2,3-dioxygenase 1 Homo sapiens 74-101 19434461-1 2009 BACKGROUND: Tryptophan catabolism via the kynurenine pathway, mediated by indoleamine 2,3-dioxygenase (IDO), is a mechanism involved in tumor immunoresistance. Tryptophan 12-22 indoleamine 2,3-dioxygenase 1 Homo sapiens 103-106 19434461-3 2009 In the present study, we investigated whether increased tryptophan metabolism in brain tumors measured by PET is related to expression of IDO in resected brain tumor specimens. Tryptophan 56-66 indoleamine 2,3-dioxygenase 1 Homo sapiens 138-141 19540675-1 2009 An increase in immune-stimulated synthesis of kynurenine from tryptophan by indoleamine 2,3-dioxygenase (IDO) has been observed in patients with coronary artery disease (CAD). Tryptophan 62-72 indoleamine 2,3-dioxygenase 1 Homo sapiens 76-103 19828629-1 2009 Catabolism of tryptophan by IDO1 plays an important role in the control of immune responses. Tryptophan 14-24 indoleamine 2,3-dioxygenase 1 Homo sapiens 28-32 19828629-6 2009 Indeed, in human monocytes BLIMP-1 mRNA and protein are up-regulated in response to both a pharmacological activator of GCN2 and tryptophan-depletion generated by IDO1-transfected cells. Tryptophan 129-139 indoleamine 2,3-dioxygenase 1 Homo sapiens 163-167 19540675-1 2009 An increase in immune-stimulated synthesis of kynurenine from tryptophan by indoleamine 2,3-dioxygenase (IDO) has been observed in patients with coronary artery disease (CAD). Tryptophan 62-72 indoleamine 2,3-dioxygenase 1 Homo sapiens 105-108 19540675-3 2009 We hypothesize that IDO activation, as measured by the kynurenine to tryptophan (K/T) ratio, is associated with depressive symptoms in those with CAD. Tryptophan 69-79 indoleamine 2,3-dioxygenase 1 Homo sapiens 20-23 19805032-2 2009 hTDO and hIDO catalyze the same oxidative ring cleavage reaction of L-tryptophan to N-formyl kynurenine, the initial and rate-limiting step of the kynurenine pathway. Tryptophan 68-80 indoleamine 2,3-dioxygenase 1 Homo sapiens 9-13 19844741-2 2009 Recently, the tryptophan-catabolizing enzyme indoleamine 2,3-dioxygenase (IDO) derived from both the tumor cells and surrounding nontumor cells was found to function as a critical immunosuppressive factor. Tryptophan 14-24 indoleamine 2,3-dioxygenase 1 Homo sapiens 45-72 19844741-2 2009 Recently, the tryptophan-catabolizing enzyme indoleamine 2,3-dioxygenase (IDO) derived from both the tumor cells and surrounding nontumor cells was found to function as a critical immunosuppressive factor. Tryptophan 14-24 indoleamine 2,3-dioxygenase 1 Homo sapiens 74-77 19693771-1 2009 Indoleamine 2,3-dioxygenase (IDO) is the rate-limiting enzyme in the kynurenine (Kyn) pathway of tryptophan (Trp) metabolism. Tryptophan 97-107 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 19693771-1 2009 Indoleamine 2,3-dioxygenase (IDO) is the rate-limiting enzyme in the kynurenine (Kyn) pathway of tryptophan (Trp) metabolism. Tryptophan 97-107 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 19693771-1 2009 Indoleamine 2,3-dioxygenase (IDO) is the rate-limiting enzyme in the kynurenine (Kyn) pathway of tryptophan (Trp) metabolism. Tryptophan 109-112 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 19693771-1 2009 Indoleamine 2,3-dioxygenase (IDO) is the rate-limiting enzyme in the kynurenine (Kyn) pathway of tryptophan (Trp) metabolism. Tryptophan 109-112 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 19935463-4 2009 METHODS: Tryptophan degradation was measured to estimate IDO activity in patient sera and cell culture supernatants with high performance liquid chromatography. Tryptophan 9-19 indoleamine 2,3-dioxygenase 1 Homo sapiens 57-60 19491279-5 2009 Although D-1MT inhibited kynurenine production at high concentrations, L-1MT was more effective in abrogating kynurenine generation and tryptophan depletion, whereas tryptophan was completely depleted by IDO even in the presence of high amounts of D-1MT. Tryptophan 166-176 indoleamine 2,3-dioxygenase 1 Homo sapiens 204-207 19625705-1 2009 The role of the tryptophan-metabolizing enzyme indoleamine 2,3-dioxygenase (IDO) in down-regulating human alloresponses has recently been controversially debated. Tryptophan 16-26 indoleamine 2,3-dioxygenase 1 Homo sapiens 47-74 19625705-1 2009 The role of the tryptophan-metabolizing enzyme indoleamine 2,3-dioxygenase (IDO) in down-regulating human alloresponses has recently been controversially debated. Tryptophan 16-26 indoleamine 2,3-dioxygenase 1 Homo sapiens 76-79 19637229-1 2009 In mammals, the regulation of local tryptophan concentrations by the IFN-gamma-i inducible enzyme IDO is a prominent antimicrobial and immunoregulatory effector mechanism. Tryptophan 36-46 indoleamine 2,3-dioxygenase 1 Homo sapiens 98-101 19656212-5 2009 HIV and viral proteins can activate IDO in immune cells leading to an increase catabolism of tryptophan through the KP; the consequence being the production of immuno-modulative and neuroactive metabolites. Tryptophan 93-103 indoleamine 2,3-dioxygenase 1 Homo sapiens 36-39 19737010-1 2009 Human indoleamine 2,3-dioxygenase (hIDO) is an intracellular heme-containing enzyme, which catalyzes the initial and rate-determining step of L-tryptophan (L-Trp) metabolism via the kynurenine pathway. Tryptophan 142-154 indoleamine 2,3-dioxygenase 1 Homo sapiens 35-39 19737010-1 2009 Human indoleamine 2,3-dioxygenase (hIDO) is an intracellular heme-containing enzyme, which catalyzes the initial and rate-determining step of L-tryptophan (L-Trp) metabolism via the kynurenine pathway. Tryptophan 156-161 indoleamine 2,3-dioxygenase 1 Homo sapiens 35-39 19737010-3 2009 Here we report evidence supporting the presence of an inhibitory substrate binding site (S(i)) in hIDO that is capable of binding molecules with a wide variety of structures, including substrates (L-Trp and 1-methyl-L-tryptophan), an effector (3-indole ethanol), and an uncompetitive inhibitor (Mitomycin C). Tryptophan 197-202 indoleamine 2,3-dioxygenase 1 Homo sapiens 98-102 19322906-1 2009 Indoleamine 2,3-dioxygenase (IDO) is a tryptophan catabolizing enzyme that has a number of immunoregulatory effects. Tryptophan 39-49 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 19322906-1 2009 Indoleamine 2,3-dioxygenase (IDO) is a tryptophan catabolizing enzyme that has a number of immunoregulatory effects. Tryptophan 39-49 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 19363598-1 2009 Indoleamine 2,3-dioxygenase (IDO)-expression in antigen-presenting cells (APCs) may control autoimmune responses by depleting the available tryptophan, whereas tryptophanyl-tRNA synthetase (TTS) may counteract this effect. Tryptophan 140-150 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 19363598-1 2009 Indoleamine 2,3-dioxygenase (IDO)-expression in antigen-presenting cells (APCs) may control autoimmune responses by depleting the available tryptophan, whereas tryptophanyl-tRNA synthetase (TTS) may counteract this effect. Tryptophan 140-150 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 19199463-2 2009 OBJECT: Indoleamine 2,3-dioxygenase (IDO), a kynurenine pathway (KP) enzyme catalyzing oxidation of the essential amino acid tryptophan (Trp), is thought to be involved in the immune resistance of malignant tumors through T-cell inactivation caused by Trp depletion and metabolite accumulation. Tryptophan 137-140 indoleamine 2,3-dioxygenase 1 Homo sapiens 8-35 19199463-2 2009 OBJECT: Indoleamine 2,3-dioxygenase (IDO), a kynurenine pathway (KP) enzyme catalyzing oxidation of the essential amino acid tryptophan (Trp), is thought to be involved in the immune resistance of malignant tumors through T-cell inactivation caused by Trp depletion and metabolite accumulation. Tryptophan 137-140 indoleamine 2,3-dioxygenase 1 Homo sapiens 37-40 19199463-2 2009 OBJECT: Indoleamine 2,3-dioxygenase (IDO), a kynurenine pathway (KP) enzyme catalyzing oxidation of the essential amino acid tryptophan (Trp), is thought to be involved in the immune resistance of malignant tumors through T-cell inactivation caused by Trp depletion and metabolite accumulation. Tryptophan 252-255 indoleamine 2,3-dioxygenase 1 Homo sapiens 8-35 19199463-2 2009 OBJECT: Indoleamine 2,3-dioxygenase (IDO), a kynurenine pathway (KP) enzyme catalyzing oxidation of the essential amino acid tryptophan (Trp), is thought to be involved in the immune resistance of malignant tumors through T-cell inactivation caused by Trp depletion and metabolite accumulation. Tryptophan 252-255 indoleamine 2,3-dioxygenase 1 Homo sapiens 37-40 19199463-4 2009 The object of this study was to investigate the possibility of IDO-dependent Trp depletion by malignant gliomas and the practicability of using an IDO inhibitor together with anticancer drugs to reserve Trp without decreasing the cytotoxicity of the drugs. Tryptophan 77-80 indoleamine 2,3-dioxygenase 1 Homo sapiens 63-66 19199463-4 2009 The object of this study was to investigate the possibility of IDO-dependent Trp depletion by malignant gliomas and the practicability of using an IDO inhibitor together with anticancer drugs to reserve Trp without decreasing the cytotoxicity of the drugs. Tryptophan 203-206 indoleamine 2,3-dioxygenase 1 Homo sapiens 147-150 19199463-5 2009 METHODS: The authors studied expression of IDO and other KP enzymes and the effects of an IDO inhibitor, 1-methyl L-tryptophan (1MT), on Trp metabolism and cytotoxicity of anticancer drugs, together with direct measurement of KP metabolites, in cultured human malignant glioma cells. Tryptophan 137-140 indoleamine 2,3-dioxygenase 1 Homo sapiens 90-93 19199463-7 2009 The IDO inhibitor 1MT successfully prevented Trp consumption by the stimulated glioma cells. Tryptophan 45-48 indoleamine 2,3-dioxygenase 1 Homo sapiens 4-7 19199463-9 2009 CONCLUSIONS: These findings suggest that the robust IDO expression with rapid consumption of Trp in human glioma cells induced by IFN-gamma could lead to immune resistance in glioma cells. Tryptophan 93-96 indoleamine 2,3-dioxygenase 1 Homo sapiens 52-55 19199463-10 2009 Indoleamine 2,3-dioxygenase inhibitors that prevent Trp depletion could be used with anticancer drugs to improve therapeutic effects. Tryptophan 52-55 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 19457071-1 2009 Indoleamine 2,3-dioxygenase (IDO) is the rate-limiting enzyme of the kynurenine pathway of tryptophan metabolism, ultimately leading to production of the excitotoxin quinolinic acid (QUIN) by monocytic cells. Tryptophan 91-101 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 19457071-1 2009 Indoleamine 2,3-dioxygenase (IDO) is the rate-limiting enzyme of the kynurenine pathway of tryptophan metabolism, ultimately leading to production of the excitotoxin quinolinic acid (QUIN) by monocytic cells. Tryptophan 91-101 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 18612775-0 2009 Highlights at the gate of tryptophan catabolism: a review on the mechanisms of activation and regulation of indoleamine 2,3-dioxygenase (IDO), a novel target in cancer disease. Tryptophan 26-36 indoleamine 2,3-dioxygenase 1 Homo sapiens 108-135 18612775-0 2009 Highlights at the gate of tryptophan catabolism: a review on the mechanisms of activation and regulation of indoleamine 2,3-dioxygenase (IDO), a novel target in cancer disease. Tryptophan 26-36 indoleamine 2,3-dioxygenase 1 Homo sapiens 137-140 19491279-6 2009 Together, the results indicate that, whereas the generation of tryptophan metabolites (kynurenines) by IDO is important in mediating suppression of T-cell proliferation, the degree to which tryptophan depletion is restored by 1MT is also critical in overcoming IDO-induced arrest of T-cell proliferation. Tryptophan 63-73 indoleamine 2,3-dioxygenase 1 Homo sapiens 103-106 19597340-1 2009 PURPOSE: Indoleamine 2,3-dioxygenase (IDO), a tryptophan catabolic enzyme, plays an important role in immune escape through suppressing T-cell function. Tryptophan 46-56 indoleamine 2,3-dioxygenase 1 Homo sapiens 38-41 19535644-1 2009 Tryptophan catabolism through IDO activity can cause nonresponsiveness and tolerance acting on T cells. Tryptophan 0-10 indoleamine 2,3-dioxygenase 1 Homo sapiens 30-33 19494274-2 2009 As with a variety of autoimmune disorders, evidence of elevated tryptophan catabolism has been detected in RA patients indicative of activation of the immunomodulatory enzyme IDO. Tryptophan 64-74 indoleamine 2,3-dioxygenase 1 Homo sapiens 175-178 19602041-1 2009 The interferon (IFN)-gamma-inducible tryptophan degrading enzyme indoleamine 2,3-dioxygenase (IDO) has not only been recognized as a potent antimicrobial effector molecule for the last 25 years but was recently found also to have potent immunoregulatory properties. Tryptophan 37-47 indoleamine 2,3-dioxygenase 1 Homo sapiens 65-92 19514129-1 2009 OBJECTIVES: Indoleamine 2,3-dioxygenase (IDO), a rate-limiting enzyme in tryptophan catabolism, is a key regulator of immune tolerance. Tryptophan 73-83 indoleamine 2,3-dioxygenase 1 Homo sapiens 12-39 19514129-1 2009 OBJECTIVES: Indoleamine 2,3-dioxygenase (IDO), a rate-limiting enzyme in tryptophan catabolism, is a key regulator of immune tolerance. Tryptophan 73-83 indoleamine 2,3-dioxygenase 1 Homo sapiens 41-44 19534572-2 2009 IDO is an IFN-inducible, intracellular enzyme that catalyzes the initial and rate-limiting step in the degradation of the essential amino acid, tryptophan. Tryptophan 144-154 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 19534572-3 2009 It has been suggested that IDO has the capacity to regulate the immune system via two discrete mechanisms; firstly the deprivation of tryptophan, which is essential for T cell proliferation and via the cytotoxic effects of tryptophan metabolites on T(H)1 cell survival. Tryptophan 134-144 indoleamine 2,3-dioxygenase 1 Homo sapiens 27-30 19534572-3 2009 It has been suggested that IDO has the capacity to regulate the immune system via two discrete mechanisms; firstly the deprivation of tryptophan, which is essential for T cell proliferation and via the cytotoxic effects of tryptophan metabolites on T(H)1 cell survival. Tryptophan 223-233 indoleamine 2,3-dioxygenase 1 Homo sapiens 27-30 19519465-3 2009 Recent advances in the biochemistry of IDO and in our understanding of the biological relevance of IDO-mediated tryptophan consumption to the establishment of dominant immune tolerance to cancer will be summarised and discussed. Tryptophan 112-122 indoleamine 2,3-dioxygenase 1 Homo sapiens 99-102 19602041-2 2009 In this study, we provide evidence that both tryptophan starvation and production of toxic tryptophan metabolites are involved in the immunoregulation mediated by IDO, whereas tryptophan starvation seems to be the only antibacterial effector mechanism. Tryptophan 91-101 indoleamine 2,3-dioxygenase 1 Homo sapiens 163-166 19602041-2 2009 In this study, we provide evidence that both tryptophan starvation and production of toxic tryptophan metabolites are involved in the immunoregulation mediated by IDO, whereas tryptophan starvation seems to be the only antibacterial effector mechanism. Tryptophan 91-101 indoleamine 2,3-dioxygenase 1 Homo sapiens 163-166 19602041-7 2009 Therefore, we suggest that during the first phase of infection the IDO-mediated tryptophan depletion has a predominantly antimicrobial effect whereas in the next stage, and with ongoing tryptophan degradation, the minimum threshold concentration of tryptophan for T-cell activation is undercut, resulting in an inhibition of T-cell growth and subsequent IDO activation. Tryptophan 80-90 indoleamine 2,3-dioxygenase 1 Homo sapiens 67-70 19602041-7 2009 Therefore, we suggest that during the first phase of infection the IDO-mediated tryptophan depletion has a predominantly antimicrobial effect whereas in the next stage, and with ongoing tryptophan degradation, the minimum threshold concentration of tryptophan for T-cell activation is undercut, resulting in an inhibition of T-cell growth and subsequent IDO activation. Tryptophan 80-90 indoleamine 2,3-dioxygenase 1 Homo sapiens 354-357 19602041-7 2009 Therefore, we suggest that during the first phase of infection the IDO-mediated tryptophan depletion has a predominantly antimicrobial effect whereas in the next stage, and with ongoing tryptophan degradation, the minimum threshold concentration of tryptophan for T-cell activation is undercut, resulting in an inhibition of T-cell growth and subsequent IDO activation. Tryptophan 186-196 indoleamine 2,3-dioxygenase 1 Homo sapiens 67-70 19602041-7 2009 Therefore, we suggest that during the first phase of infection the IDO-mediated tryptophan depletion has a predominantly antimicrobial effect whereas in the next stage, and with ongoing tryptophan degradation, the minimum threshold concentration of tryptophan for T-cell activation is undercut, resulting in an inhibition of T-cell growth and subsequent IDO activation. Tryptophan 186-196 indoleamine 2,3-dioxygenase 1 Homo sapiens 67-70 19155537-1 2009 BACKGROUND: Tryptophan (Trp) is catabolized by indoleamine 2,3-dioxygenase (IDO). Tryptophan 12-22 indoleamine 2,3-dioxygenase 1 Homo sapiens 47-74 19155537-1 2009 BACKGROUND: Tryptophan (Trp) is catabolized by indoleamine 2,3-dioxygenase (IDO). Tryptophan 12-22 indoleamine 2,3-dioxygenase 1 Homo sapiens 76-79 19155537-1 2009 BACKGROUND: Tryptophan (Trp) is catabolized by indoleamine 2,3-dioxygenase (IDO). Tryptophan 24-27 indoleamine 2,3-dioxygenase 1 Homo sapiens 47-74 19155537-1 2009 BACKGROUND: Tryptophan (Trp) is catabolized by indoleamine 2,3-dioxygenase (IDO). Tryptophan 24-27 indoleamine 2,3-dioxygenase 1 Homo sapiens 76-79 19602041-1 2009 The interferon (IFN)-gamma-inducible tryptophan degrading enzyme indoleamine 2,3-dioxygenase (IDO) has not only been recognized as a potent antimicrobial effector molecule for the last 25 years but was recently found also to have potent immunoregulatory properties. Tryptophan 37-47 indoleamine 2,3-dioxygenase 1 Homo sapiens 94-97 19602041-2 2009 In this study, we provide evidence that both tryptophan starvation and production of toxic tryptophan metabolites are involved in the immunoregulation mediated by IDO, whereas tryptophan starvation seems to be the only antibacterial effector mechanism. Tryptophan 45-55 indoleamine 2,3-dioxygenase 1 Homo sapiens 163-166 19276371-1 2009 Human mesenchymal stem cells (MSC) strongly repress activated T-cell proliferation through the production of a complex set of soluble factors, including the tryptophan-catabolizing enzyme indoleamine 2,3-dioxygenase (IDO), which is induced by IFN-gamma. Tryptophan 157-167 indoleamine 2,3-dioxygenase 1 Homo sapiens 188-215 19290871-0 2009 Oxidation of L-tryptophan in biology: a comparison between tryptophan 2,3-dioxygenase and indoleamine 2,3-dioxygenase. Tryptophan 13-25 indoleamine 2,3-dioxygenase 1 Homo sapiens 90-117 19276371-1 2009 Human mesenchymal stem cells (MSC) strongly repress activated T-cell proliferation through the production of a complex set of soluble factors, including the tryptophan-catabolizing enzyme indoleamine 2,3-dioxygenase (IDO), which is induced by IFN-gamma. Tryptophan 157-167 indoleamine 2,3-dioxygenase 1 Homo sapiens 217-220 19067144-8 2009 Recently, the role of certain pro-inflammatory cytokines that could enhance the activity of the enzyme, indoleamine 2-3, dioxygenase (IDO) which in turn would increase tryptophan degradation into kynurenine and decrease tryptophan availability of tryptophan in the brain to synthesize serotonin, a neurotransmitter which is necessary for the normal mood state became of interest in pathophysiology of psychiatric disorders. Tryptophan 168-178 indoleamine 2,3-dioxygenase 1 Homo sapiens 104-132 19275153-1 2009 Indoleamine 2,3-dioxygenase (IDO) and tryptophan 2,3-dioxygenase (TDO) are heme enzymes that catalyze the O(2)-dependent oxidation of L-tryptophan to N-formyl-kynurenine. Tryptophan 134-146 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 19275153-1 2009 Indoleamine 2,3-dioxygenase (IDO) and tryptophan 2,3-dioxygenase (TDO) are heme enzymes that catalyze the O(2)-dependent oxidation of L-tryptophan to N-formyl-kynurenine. Tryptophan 134-146 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 18945560-3 2009 IFN-gamma induces expression of the enzyme indoleamine 2,3-dioxygenase (IDO), resulting in the degradation of intracellular pools of tryptophan, thereby depriving the organism of this essential growth nutrient. Tryptophan 133-143 indoleamine 2,3-dioxygenase 1 Homo sapiens 43-70 18945560-3 2009 IFN-gamma induces expression of the enzyme indoleamine 2,3-dioxygenase (IDO), resulting in the degradation of intracellular pools of tryptophan, thereby depriving the organism of this essential growth nutrient. Tryptophan 133-143 indoleamine 2,3-dioxygenase 1 Homo sapiens 72-75 19023117-4 2009 The tryptophan catabolic enzyme, indoleamine 2,3-dioxygenase (IDO), is one of the key players involved in the inhibition of cell proliferation, including that of activated T cells. Tryptophan 4-14 indoleamine 2,3-dioxygenase 1 Homo sapiens 33-60 19023117-4 2009 The tryptophan catabolic enzyme, indoleamine 2,3-dioxygenase (IDO), is one of the key players involved in the inhibition of cell proliferation, including that of activated T cells. Tryptophan 4-14 indoleamine 2,3-dioxygenase 1 Homo sapiens 62-65 18986303-3 2009 Activated IDO is indicated by an increased kyn/trp (kynurenine/tryptophan) ratio. Tryptophan 47-50 indoleamine 2,3-dioxygenase 1 Homo sapiens 10-13 18986303-3 2009 Activated IDO is indicated by an increased kyn/trp (kynurenine/tryptophan) ratio. Tryptophan 63-73 indoleamine 2,3-dioxygenase 1 Homo sapiens 10-13 18986303-12 2009 In conclusion, these results imply that increased tryptophan degradation in patients is due to activated IDO, which most probably is a consequence of a host defence response. Tryptophan 50-60 indoleamine 2,3-dioxygenase 1 Homo sapiens 105-108 19353519-5 2009 Immunosuppression mediated by TLR was dependent on the production of immunosuppressive kynurenines by the tryptophan-degrading enzyme indoleamine-2,3-dioxygenase-1 (IDO1). Tryptophan 106-116 indoleamine 2,3-dioxygenase 1 Homo sapiens 134-163 19353519-5 2009 Immunosuppression mediated by TLR was dependent on the production of immunosuppressive kynurenines by the tryptophan-degrading enzyme indoleamine-2,3-dioxygenase-1 (IDO1). Tryptophan 106-116 indoleamine 2,3-dioxygenase 1 Homo sapiens 165-169 19327051-4 2009 Activation of indoleamine-2,3-dioxygenase (IDO), the rate-limiting enzyme of the kynurenine pathway, leads to increased tryptophan catabolism and the generation of neurotoxins such as kynurenine (KYN). Tryptophan 120-130 indoleamine 2,3-dioxygenase 1 Homo sapiens 14-41 19327051-4 2009 Activation of indoleamine-2,3-dioxygenase (IDO), the rate-limiting enzyme of the kynurenine pathway, leads to increased tryptophan catabolism and the generation of neurotoxins such as kynurenine (KYN). Tryptophan 120-130 indoleamine 2,3-dioxygenase 1 Homo sapiens 43-46 18639339-1 2009 The enzyme indoleamine 2,3-dioxygenase (IDO) converts tryptophan to kynurenine, blocking T-cell activation and inducing immunosuppression. Tryptophan 54-64 indoleamine 2,3-dioxygenase 1 Homo sapiens 40-43 18639339-2 2009 In patients with acute myeloid leukemia (AML), the serum kynurenine/tryptophan ratio (Kyn/Trp) was raised, suggesting a higher IDO activity than in healthy people. Tryptophan 68-78 indoleamine 2,3-dioxygenase 1 Homo sapiens 127-130 18639339-2 2009 In patients with acute myeloid leukemia (AML), the serum kynurenine/tryptophan ratio (Kyn/Trp) was raised, suggesting a higher IDO activity than in healthy people. Tryptophan 90-93 indoleamine 2,3-dioxygenase 1 Homo sapiens 127-130 18639339-4 2009 IDO activity was also detected in AML cells after exposure to IFN-gammain vitro, suggesting that the higher Kyn/Trp ratio in serum of AML patients might have resulted from stimulated leukemic blast cells. Tryptophan 112-115 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 19067144-8 2009 Recently, the role of certain pro-inflammatory cytokines that could enhance the activity of the enzyme, indoleamine 2-3, dioxygenase (IDO) which in turn would increase tryptophan degradation into kynurenine and decrease tryptophan availability of tryptophan in the brain to synthesize serotonin, a neurotransmitter which is necessary for the normal mood state became of interest in pathophysiology of psychiatric disorders. Tryptophan 168-178 indoleamine 2,3-dioxygenase 1 Homo sapiens 134-137 19067144-8 2009 Recently, the role of certain pro-inflammatory cytokines that could enhance the activity of the enzyme, indoleamine 2-3, dioxygenase (IDO) which in turn would increase tryptophan degradation into kynurenine and decrease tryptophan availability of tryptophan in the brain to synthesize serotonin, a neurotransmitter which is necessary for the normal mood state became of interest in pathophysiology of psychiatric disorders. Tryptophan 220-230 indoleamine 2,3-dioxygenase 1 Homo sapiens 104-132 19067144-8 2009 Recently, the role of certain pro-inflammatory cytokines that could enhance the activity of the enzyme, indoleamine 2-3, dioxygenase (IDO) which in turn would increase tryptophan degradation into kynurenine and decrease tryptophan availability of tryptophan in the brain to synthesize serotonin, a neurotransmitter which is necessary for the normal mood state became of interest in pathophysiology of psychiatric disorders. Tryptophan 220-230 indoleamine 2,3-dioxygenase 1 Homo sapiens 134-137 19067144-8 2009 Recently, the role of certain pro-inflammatory cytokines that could enhance the activity of the enzyme, indoleamine 2-3, dioxygenase (IDO) which in turn would increase tryptophan degradation into kynurenine and decrease tryptophan availability of tryptophan in the brain to synthesize serotonin, a neurotransmitter which is necessary for the normal mood state became of interest in pathophysiology of psychiatric disorders. Tryptophan 220-230 indoleamine 2,3-dioxygenase 1 Homo sapiens 104-132 19067144-8 2009 Recently, the role of certain pro-inflammatory cytokines that could enhance the activity of the enzyme, indoleamine 2-3, dioxygenase (IDO) which in turn would increase tryptophan degradation into kynurenine and decrease tryptophan availability of tryptophan in the brain to synthesize serotonin, a neurotransmitter which is necessary for the normal mood state became of interest in pathophysiology of psychiatric disorders. Tryptophan 220-230 indoleamine 2,3-dioxygenase 1 Homo sapiens 134-137 18397228-1 2009 BACKGROUND/AIMS: Indoleamine-2,3-dioxygenase (IDO) is a tryptophan-catabolizing enzyme inducing suppression of T-cell function and immune tolerance. Tryptophan 56-66 indoleamine 2,3-dioxygenase 1 Homo sapiens 17-44 18397228-1 2009 BACKGROUND/AIMS: Indoleamine-2,3-dioxygenase (IDO) is a tryptophan-catabolizing enzyme inducing suppression of T-cell function and immune tolerance. Tryptophan 56-66 indoleamine 2,3-dioxygenase 1 Homo sapiens 46-49 19154614-0 2009 Tryptophan degradation in irritable bowel syndrome: evidence of indoleamine 2,3-dioxygenase activation in a male cohort. Tryptophan 0-10 indoleamine 2,3-dioxygenase 1 Homo sapiens 64-91 19162548-4 2009 In these cells, autocrine, paracrine and T-cell-derived TGF-beta activates the tolerogenic pathway of tryptophan catabolism - mediated by indoleamine 2,3-dioxygenase (IDO) - resulting in a burst of regulatory kynurenines that contribute to establishing a state of "infectious tolerance". Tryptophan 102-112 indoleamine 2,3-dioxygenase 1 Homo sapiens 138-165 19162548-4 2009 In these cells, autocrine, paracrine and T-cell-derived TGF-beta activates the tolerogenic pathway of tryptophan catabolism - mediated by indoleamine 2,3-dioxygenase (IDO) - resulting in a burst of regulatory kynurenines that contribute to establishing a state of "infectious tolerance". Tryptophan 102-112 indoleamine 2,3-dioxygenase 1 Homo sapiens 167-170 19154614-11 2009 CONCLUSION: These findings suggest that the activity of IDO, the immunoresponsive enzyme which is responsible for the degradation of tryptophan along this pathway, is enhanced in IBS patients relative to controls. Tryptophan 133-143 indoleamine 2,3-dioxygenase 1 Homo sapiens 56-59 18418598-8 2009 IDO1 activity of Hela cells was blocked by transfection with IDO1-specific siRNA and analysed for tryptophan degradation by RP-HPLC. Tryptophan 98-108 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-4 18274832-1 2009 The hemoprotein indoleamine 2,3-dioxygenase (IDO) is the first and rate-limiting enzyme in the most significant pathway for mammalian tryptophan metabolism. Tryptophan 134-144 indoleamine 2,3-dioxygenase 1 Homo sapiens 16-43 18274832-1 2009 The hemoprotein indoleamine 2,3-dioxygenase (IDO) is the first and rate-limiting enzyme in the most significant pathway for mammalian tryptophan metabolism. Tryptophan 134-144 indoleamine 2,3-dioxygenase 1 Homo sapiens 45-48 18418598-11 2009 Treatment of Hela cells with IDO1-specific siRNA resulted in complete abrogation of tryptophan degradation. Tryptophan 84-94 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-33 18418598-13 2009 CONCLUSIONS: Although IDO2 is expressed in human tumors, tryptophan degradation is entirely provided by IDO1. Tryptophan 57-67 indoleamine 2,3-dioxygenase 1 Homo sapiens 104-108 19802733-1 2009 Indoleamine 2,3-dioxygenase (IDO) is a tryptophan-catabolising enzyme inducing immune tolerance. Tryptophan 39-49 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 19802733-1 2009 Indoleamine 2,3-dioxygenase (IDO) is a tryptophan-catabolising enzyme inducing immune tolerance. Tryptophan 39-49 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 19929471-6 2009 IDO enzyme activity was determined by high-performance liquid chromatography (HPLC) measurement of kynurenine (K) and tryptophan (T) concentrations in culture supernatants. Tryptophan 118-128 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 19167991-4 2009 In PBMC treated with mitogen phytohaemagglutinin, neopterin production and tryptophan degradation by enzyme indoleamine 2,3-dioxygenase (IDO) as well as release of cytokines was significantly enhanced and upon treatment with propolis extracts all these effects were dose-dependently suppressed. Tryptophan 75-85 indoleamine 2,3-dioxygenase 1 Homo sapiens 108-135 19167991-4 2009 In PBMC treated with mitogen phytohaemagglutinin, neopterin production and tryptophan degradation by enzyme indoleamine 2,3-dioxygenase (IDO) as well as release of cytokines was significantly enhanced and upon treatment with propolis extracts all these effects were dose-dependently suppressed. Tryptophan 75-85 indoleamine 2,3-dioxygenase 1 Homo sapiens 137-140 19811321-2 2009 Recently, Indoleamine-2,3 Dioxygenase (IDO)--a tryptophan degrading enzyme--has been shown to be implicated in one of nature"s most impressive examples of tolerance, which is maternal acceptance of the semi-allogeneic foetus. Tryptophan 47-57 indoleamine 2,3-dioxygenase 1 Homo sapiens 10-37 19811321-2 2009 Recently, Indoleamine-2,3 Dioxygenase (IDO)--a tryptophan degrading enzyme--has been shown to be implicated in one of nature"s most impressive examples of tolerance, which is maternal acceptance of the semi-allogeneic foetus. Tryptophan 47-57 indoleamine 2,3-dioxygenase 1 Homo sapiens 39-42 19228097-1 2009 BACKGROUND: Indoleamine 2,3-dioxygenase (IDO) is an intracellular tryptophan-oxidizing enzyme with immunosuppressive characteristics. Tryptophan 66-76 indoleamine 2,3-dioxygenase 1 Homo sapiens 12-39 19058839-1 2009 BACKGROUND: Indoleamine 2, 3-dioxygenase (IDO), a tryptophan-degrading enzyme in dendritic cells (DCs), mediates an immunosuppressive effect on activated T lymphocytes. Tryptophan 50-60 indoleamine 2,3-dioxygenase 1 Homo sapiens 12-40 19058839-1 2009 BACKGROUND: Indoleamine 2, 3-dioxygenase (IDO), a tryptophan-degrading enzyme in dendritic cells (DCs), mediates an immunosuppressive effect on activated T lymphocytes. Tryptophan 50-60 indoleamine 2,3-dioxygenase 1 Homo sapiens 42-45 19228097-1 2009 BACKGROUND: Indoleamine 2,3-dioxygenase (IDO) is an intracellular tryptophan-oxidizing enzyme with immunosuppressive characteristics. Tryptophan 66-76 indoleamine 2,3-dioxygenase 1 Homo sapiens 41-44 18676626-1 2008 PURPOSE: Indolemine 2,3-dioxygenase (IDO)-mediated oxidation of tryptophan produces kynurenines (KYNs), which may play a role in cataract formation. Tryptophan 64-74 indoleamine 2,3-dioxygenase 1 Homo sapiens 9-35 19233480-2 2009 Among several mechanisms involved in pregnancy maintenance, progesterone-induced immunomodulation, asymmetric antibody (AAb) production, indoleamine 2,3-dioxygenase (IDO)-mediated tryptophan catabolism and Th1- to Th2-type cytokine balance have been particularly well studied. Tryptophan 180-190 indoleamine 2,3-dioxygenase 1 Homo sapiens 137-164 19233480-2 2009 Among several mechanisms involved in pregnancy maintenance, progesterone-induced immunomodulation, asymmetric antibody (AAb) production, indoleamine 2,3-dioxygenase (IDO)-mediated tryptophan catabolism and Th1- to Th2-type cytokine balance have been particularly well studied. Tryptophan 180-190 indoleamine 2,3-dioxygenase 1 Homo sapiens 166-169 18639341-0 2009 Indoleamine 2,3-dioxygenase is highly expressed in human adult T-cell leukemia/lymphoma and chemotherapy changes tryptophan catabolism in serum and reduced activity. Tryptophan 113-123 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 18639341-2 2009 Indoleamine 2,3-dioxygenase (IDO), the l-tryptophan (l-TRP)-degrading enzyme, plays a key role in the powerful immunomodulatory effects of several different types of immune cells. Tryptophan 39-51 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 18639341-2 2009 Indoleamine 2,3-dioxygenase (IDO), the l-tryptophan (l-TRP)-degrading enzyme, plays a key role in the powerful immunomodulatory effects of several different types of immune cells. Tryptophan 39-51 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 18639341-2 2009 Indoleamine 2,3-dioxygenase (IDO), the l-tryptophan (l-TRP)-degrading enzyme, plays a key role in the powerful immunomodulatory effects of several different types of immune cells. Tryptophan 53-58 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 18639341-2 2009 Indoleamine 2,3-dioxygenase (IDO), the l-tryptophan (l-TRP)-degrading enzyme, plays a key role in the powerful immunomodulatory effects of several different types of immune cells. Tryptophan 53-58 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 18639341-3 2009 In this study, we investigated the IDO expression in ATLL cells and the effect of chemotherapy on IDO-initiating l-TRP catabolism in patients with ATLL. Tryptophan 113-118 indoleamine 2,3-dioxygenase 1 Homo sapiens 98-101 18639341-8 2009 These data provide evidence that IDO is highly expressed in ATLL cells, and that IDO-initiating l-TRP catabolism changes with chemotherapy. Tryptophan 96-101 indoleamine 2,3-dioxygenase 1 Homo sapiens 33-36 18639341-8 2009 These data provide evidence that IDO is highly expressed in ATLL cells, and that IDO-initiating l-TRP catabolism changes with chemotherapy. Tryptophan 96-101 indoleamine 2,3-dioxygenase 1 Homo sapiens 81-84 19007906-1 2009 Initially recognized in infection because of antimicrobial activity ("tryptophan starvation"), indoleamine 2,3-dioxygenase (IDO) is widely involved in host immune homeostasis and even immune evasion by microbes that establish commensalism or chronic infection. Tryptophan 70-80 indoleamine 2,3-dioxygenase 1 Homo sapiens 95-122 19007906-1 2009 Initially recognized in infection because of antimicrobial activity ("tryptophan starvation"), indoleamine 2,3-dioxygenase (IDO) is widely involved in host immune homeostasis and even immune evasion by microbes that establish commensalism or chronic infection. Tryptophan 70-80 indoleamine 2,3-dioxygenase 1 Homo sapiens 124-127 19021508-1 2008 The haem proteins TDO (tryptophan 2,3-dioxygenase) and IDO (indoleamine 2,3-dioxygenase) are specific and powerful oxidation catalysts that insert one molecule of dioxygen into L-tryptophan in the first and rate-limiting step in the kynurenine pathway. Tryptophan 177-189 indoleamine 2,3-dioxygenase 1 Homo sapiens 55-58 19021508-1 2008 The haem proteins TDO (tryptophan 2,3-dioxygenase) and IDO (indoleamine 2,3-dioxygenase) are specific and powerful oxidation catalysts that insert one molecule of dioxygen into L-tryptophan in the first and rate-limiting step in the kynurenine pathway. Tryptophan 177-189 indoleamine 2,3-dioxygenase 1 Homo sapiens 60-87 19021508-2 2008 Recent crystallographic and biochemical analyses of TDO and IDO have greatly aided our understanding of the mechanisms employed by these enzymes in the binding and activation of dioxygen and tryptophan. Tryptophan 191-201 indoleamine 2,3-dioxygenase 1 Homo sapiens 60-63 18676626-1 2008 PURPOSE: Indolemine 2,3-dioxygenase (IDO)-mediated oxidation of tryptophan produces kynurenines (KYNs), which may play a role in cataract formation. Tryptophan 64-74 indoleamine 2,3-dioxygenase 1 Homo sapiens 37-40 19106591-2 2008 IDO activity can be measured by tryptophan (Trp)/kynurenine (Kyn) ratio. Tryptophan 32-42 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 18847306-2 2008 IDO is an IFN-gamma-inducible, intracellular enzyme that catalyzes the initial and rate-limiting step in the degradation of tryptophan. Tryptophan 124-134 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 18847306-3 2008 It has been suggested that IDO can regulate the immune system either through deprivation of tryptophan that is essential for T cell proliferation or via cytotoxic effects of kynurenine pathway metabolites on T cell survival. Tryptophan 92-102 indoleamine 2,3-dioxygenase 1 Homo sapiens 27-30 19106591-2 2008 IDO activity can be measured by tryptophan (Trp)/kynurenine (Kyn) ratio. Tryptophan 44-47 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 18064486-5 2008 OBJECTIVE: This overview article focuses on IDO-mediated tryptophan catabolism with special regard to its role in cancer and transplantation immunology. Tryptophan 57-67 indoleamine 2,3-dioxygenase 1 Homo sapiens 44-47 18712870-1 2008 Indoleamine 2,3-dioxygenase (IDO) and tryptophan 2,3-dioxygenase (TDO) are heme-containing dioxygenases and catalyze oxidative cleavage of the pyrrole ring of L-tryptophan. Tryptophan 159-171 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 18832696-3 2008 In this study, we show that human PDCs express high levels of IDO, an intracellular enzyme that catabolizes tryptophan degradation. Tryptophan 108-118 indoleamine 2,3-dioxygenase 1 Homo sapiens 62-65 18619832-9 2008 In these patients, IDO gene expression correlated with kynurenine/tryptophan ratio in sera. Tryptophan 66-76 indoleamine 2,3-dioxygenase 1 Homo sapiens 19-22 18712870-1 2008 Indoleamine 2,3-dioxygenase (IDO) and tryptophan 2,3-dioxygenase (TDO) are heme-containing dioxygenases and catalyze oxidative cleavage of the pyrrole ring of L-tryptophan. Tryptophan 159-171 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 18712654-3 2008 Indoleamine 2,3-dioxygenase (IDO) is the principle enzyme in the degradation of the essential amino acid L-tryptophan to L-kynurenine. Tryptophan 105-117 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 18671950-2 2008 Indoleamine 2,3-dioxygenase (IDO), an enzyme catalyzing the catabolism of L-tryptophan along the kynurenine pathway, is inducible in APC and represents one of the main endogenous mechanisms of T cell homeostasis, peripheral tolerance and immunosuppression. Tryptophan 74-86 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 18671950-2 2008 Indoleamine 2,3-dioxygenase (IDO), an enzyme catalyzing the catabolism of L-tryptophan along the kynurenine pathway, is inducible in APC and represents one of the main endogenous mechanisms of T cell homeostasis, peripheral tolerance and immunosuppression. Tryptophan 74-86 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 18712654-3 2008 Indoleamine 2,3-dioxygenase (IDO) is the principle enzyme in the degradation of the essential amino acid L-tryptophan to L-kynurenine. Tryptophan 105-117 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 18501338-1 2008 Indoleamine 2,3-dioxygenase (IDO) is the rate-limiting enzyme in the kynurenine pathway that converts L-tryptophan to L-kynurenine. Tryptophan 102-114 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 18490060-1 2008 Indoleamine 2,3-dioxygenase (IDO) catalyzes the initial and rate-limiting step of tryptophan degradation along the kynurenine pathway, and is hypothesized to limit tryptophan availability at embryo implantation and prevent maternal T cell activation at the maternal-fetal interface. Tryptophan 82-92 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 18490060-1 2008 Indoleamine 2,3-dioxygenase (IDO) catalyzes the initial and rate-limiting step of tryptophan degradation along the kynurenine pathway, and is hypothesized to limit tryptophan availability at embryo implantation and prevent maternal T cell activation at the maternal-fetal interface. Tryptophan 164-174 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 18501338-1 2008 Indoleamine 2,3-dioxygenase (IDO) is the rate-limiting enzyme in the kynurenine pathway that converts L-tryptophan to L-kynurenine. Tryptophan 102-114 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 18221253-1 2008 Indoleamine 2,3-dioxygenase (IDO) is an interferon-gamma-inducible intracellular enzyme which catalyses the catabolism of tryptophan. Tryptophan 122-132 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 18221253-1 2008 Indoleamine 2,3-dioxygenase (IDO) is an interferon-gamma-inducible intracellular enzyme which catalyses the catabolism of tryptophan. Tryptophan 122-132 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 18471709-2 2008 One possible mechanism by which PDA cells can escape immune detection is through upregulation of indoleamine 2,3-dioxygenase (IDO), an enzyme that can starve T lymphocytes of tryptophan. Tryptophan 175-185 indoleamine 2,3-dioxygenase 1 Homo sapiens 126-129 18299324-1 2008 The heme protein indoleamine 2,3-dioxygenase (IDO) initiates oxidative metabolism of tryptophan along the kynurenine pathway, and this requires reductive activation of Fe(3+)-IDO. Tryptophan 85-95 indoleamine 2,3-dioxygenase 1 Homo sapiens 17-44 18299324-1 2008 The heme protein indoleamine 2,3-dioxygenase (IDO) initiates oxidative metabolism of tryptophan along the kynurenine pathway, and this requires reductive activation of Fe(3+)-IDO. Tryptophan 85-95 indoleamine 2,3-dioxygenase 1 Homo sapiens 46-49 18299324-1 2008 The heme protein indoleamine 2,3-dioxygenase (IDO) initiates oxidative metabolism of tryptophan along the kynurenine pathway, and this requires reductive activation of Fe(3+)-IDO. Tryptophan 85-95 indoleamine 2,3-dioxygenase 1 Homo sapiens 175-178 17945348-3 2008 Because tryptophan is a precursor of the neurotransmitter 5-hydroxytryptamine (serotonin), tryptophan depletion by IDO can cause mood disturbances in patients with chronic immune activation. Tryptophan 91-101 indoleamine 2,3-dioxygenase 1 Homo sapiens 115-118 18370410-1 2008 The initial step in the l-kynurenine pathway is oxidation of l-tryptophan to N-formylkynurenine and is catalyzed by one of two heme enzymes, tryptophan 2,3-dioxygenase (TDO) or indoleamine 2,3-dioxygenase (IDO). Tryptophan 61-73 indoleamine 2,3-dioxygenase 1 Homo sapiens 177-204 18471256-1 2008 We have previously demonstrated that indoleamine 2, 3-dioxygenase (IDO) expressed by dermal fibroblasts generated a tryptophan deficient environment in which immune cells, but not skin cells, undergo apoptosis. Tryptophan 116-126 indoleamine 2,3-dioxygenase 1 Homo sapiens 37-65 18471256-1 2008 We have previously demonstrated that indoleamine 2, 3-dioxygenase (IDO) expressed by dermal fibroblasts generated a tryptophan deficient environment in which immune cells, but not skin cells, undergo apoptosis. Tryptophan 116-126 indoleamine 2,3-dioxygenase 1 Homo sapiens 67-70 18471256-3 2008 Here, we asked the question of whether the activity of the general control nondepressing-2 (GCN2) kinase pathway in primary immune and skin cells is differently regulated in response to IDO-induced tryptophan deficient environment. Tryptophan 198-208 indoleamine 2,3-dioxygenase 1 Homo sapiens 186-189 18471256-6 2008 Evaluating the mechanism by which skin cells, but not T cells, are resistant to IDO induced low tryptophan environment, we then co-cultured IDO-expressing fibroblasts with bystander human T cells, the fibroblasts, or keratinocytes for 3 days. Tryptophan 96-106 indoleamine 2,3-dioxygenase 1 Homo sapiens 80-83 18465467-2 2008 The kynurenine (KYN) pathway, which is initiated by indoleamine 2,3-dioxygenase (IDO), is the main TRP metabolic pathway. Tryptophan 99-102 indoleamine 2,3-dioxygenase 1 Homo sapiens 52-79 18465467-2 2008 The kynurenine (KYN) pathway, which is initiated by indoleamine 2,3-dioxygenase (IDO), is the main TRP metabolic pathway. Tryptophan 99-102 indoleamine 2,3-dioxygenase 1 Homo sapiens 81-84 18370410-1 2008 The initial step in the l-kynurenine pathway is oxidation of l-tryptophan to N-formylkynurenine and is catalyzed by one of two heme enzymes, tryptophan 2,3-dioxygenase (TDO) or indoleamine 2,3-dioxygenase (IDO). Tryptophan 61-73 indoleamine 2,3-dioxygenase 1 Homo sapiens 206-209 18272236-2 2008 Although the immunoregulatory effects of IDO may be in part due to generalized suppression of cell proliferation caused by tryptophan starvation, there is also evidence that tryptophan catabolites could be directly responsible for some of the observed effects. Tryptophan 123-133 indoleamine 2,3-dioxygenase 1 Homo sapiens 41-44 18547472-2 2008 During inflammation IDO can be induced in different cell types resulting in local tryptophan depletion. Tryptophan 82-92 indoleamine 2,3-dioxygenase 1 Homo sapiens 20-23 17942160-3 2008 The tryptophan catabolism enzyme indoleamine 2,3-dioxygenase (IDO) is interferon-gamma (IFN-gamma)-inducible and has recently become a focus for maternal-fetal tolerance for successful pregnancy. Tryptophan 4-14 indoleamine 2,3-dioxygenase 1 Homo sapiens 33-60 17942160-3 2008 The tryptophan catabolism enzyme indoleamine 2,3-dioxygenase (IDO) is interferon-gamma (IFN-gamma)-inducible and has recently become a focus for maternal-fetal tolerance for successful pregnancy. Tryptophan 4-14 indoleamine 2,3-dioxygenase 1 Homo sapiens 62-65 18547472-11 2008 Since bacterial invasion is more pronounced in erosions and in crypt abscesses and since IDO activity and the resulting local tryptophan depletion can cause growth arrest of several tryptophan-dependent microorganisms, IDO expression in the vicinity of interruptions of the epithelial barrier may point to a role for IDO as a local anti-infectious agent. Tryptophan 182-192 indoleamine 2,3-dioxygenase 1 Homo sapiens 89-92 18447640-9 2008 oMSCs also demonstrated the ability to suppress allogeneic T cell proliferation, which was associated with the expression of the tryptophan-degrading enzyme indoleamine 2,3-dioxygenase (IDO). Tryptophan 129-139 indoleamine 2,3-dioxygenase 1 Homo sapiens 157-184 18447640-9 2008 oMSCs also demonstrated the ability to suppress allogeneic T cell proliferation, which was associated with the expression of the tryptophan-degrading enzyme indoleamine 2,3-dioxygenase (IDO). Tryptophan 129-139 indoleamine 2,3-dioxygenase 1 Homo sapiens 186-189 18205804-6 2008 Furthermore, the IFN-gamma-dependent antimicrobial effects of HBE4-E6/E7 (human lung bronchus epithelial cells) and A549 (human type II alveolar cells) correlated with the activation of the tryptophan-degrading enzyme indoleamine 2,3-dioxygenase (IDO). Tryptophan 190-200 indoleamine 2,3-dioxygenase 1 Homo sapiens 218-245 18205804-6 2008 Furthermore, the IFN-gamma-dependent antimicrobial effects of HBE4-E6/E7 (human lung bronchus epithelial cells) and A549 (human type II alveolar cells) correlated with the activation of the tryptophan-degrading enzyme indoleamine 2,3-dioxygenase (IDO). Tryptophan 190-200 indoleamine 2,3-dioxygenase 1 Homo sapiens 247-250 18205804-7 2008 It was found that both the abrogation of IDO activity by the specific IDO-inhibitor 1-L-methyltryptophan and the supplementation of cultures with tryptophan result in an inhibition of IFN-gamma-induced antimicrobial effects mediated by lung cells. Tryptophan 94-104 indoleamine 2,3-dioxygenase 1 Homo sapiens 41-44 18205804-7 2008 It was found that both the abrogation of IDO activity by the specific IDO-inhibitor 1-L-methyltryptophan and the supplementation of cultures with tryptophan result in an inhibition of IFN-gamma-induced antimicrobial effects mediated by lung cells. Tryptophan 94-104 indoleamine 2,3-dioxygenase 1 Homo sapiens 70-73 18045970-2 2008 Here we show that human dendritic cells (DCs) express both IDO-1 and IDO-2, but that only IDO1 mediates tryptophan catabolism; furthermore, its activity is blocked by levo-1MT, whereas D-1MT is inefficient. Tryptophan 104-114 indoleamine 2,3-dioxygenase 1 Homo sapiens 90-94 18176870-1 2008 The immunomodulatory effects of the tryptophan-catabolizing enzyme indoleamine 2,3-dioxygenase (IDO) have been elucidated at a cellular level and implicated in the pathogenesis of several complex diseases. Tryptophan 36-46 indoleamine 2,3-dioxygenase 1 Homo sapiens 67-94 18176870-1 2008 The immunomodulatory effects of the tryptophan-catabolizing enzyme indoleamine 2,3-dioxygenase (IDO) have been elucidated at a cellular level and implicated in the pathogenesis of several complex diseases. Tryptophan 36-46 indoleamine 2,3-dioxygenase 1 Homo sapiens 96-99 18660700-1 2008 PURPOSE OF REVIEW: The immunomodulatory enzyme indoleamine 2,3-dioxygenase (IDO) is activated by interferon-gamma and via tryptophan depletion and the production of proapoptotic downstream metabolites IDO suppresses adaptive T-cell-mediated immunity in inflammation, host immune defence and maternal tolerance. Tryptophan 122-132 indoleamine 2,3-dioxygenase 1 Homo sapiens 47-74 18547472-1 2008 Indoleamine 2,3-dioxygenase (IDO) catalyzes the first step in the degradation of tryptophan, an essential amino acid. Tryptophan 81-91 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 18547472-1 2008 Indoleamine 2,3-dioxygenase (IDO) catalyzes the first step in the degradation of tryptophan, an essential amino acid. Tryptophan 81-91 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 18660700-1 2008 PURPOSE OF REVIEW: The immunomodulatory enzyme indoleamine 2,3-dioxygenase (IDO) is activated by interferon-gamma and via tryptophan depletion and the production of proapoptotic downstream metabolites IDO suppresses adaptive T-cell-mediated immunity in inflammation, host immune defence and maternal tolerance. Tryptophan 122-132 indoleamine 2,3-dioxygenase 1 Homo sapiens 76-79 18660700-1 2008 PURPOSE OF REVIEW: The immunomodulatory enzyme indoleamine 2,3-dioxygenase (IDO) is activated by interferon-gamma and via tryptophan depletion and the production of proapoptotic downstream metabolites IDO suppresses adaptive T-cell-mediated immunity in inflammation, host immune defence and maternal tolerance. Tryptophan 122-132 indoleamine 2,3-dioxygenase 1 Homo sapiens 201-204 18660700-2 2008 In addition, IDO-mediated tryptophan catabolism occurring in dendritic cells is an emerging potent mechanism of peripheral tolerance. Tryptophan 26-36 indoleamine 2,3-dioxygenase 1 Homo sapiens 13-16 18660704-1 2008 PURPOSE OF REVIEW: Indoleamine 2,3-dioxygenase (IDO) catalyzes tryptophan and suppresses adaptive immunity by inhibiting T-cell proliferation and promoting their apoptosis. Tryptophan 63-73 indoleamine 2,3-dioxygenase 1 Homo sapiens 19-46 18660704-1 2008 PURPOSE OF REVIEW: Indoleamine 2,3-dioxygenase (IDO) catalyzes tryptophan and suppresses adaptive immunity by inhibiting T-cell proliferation and promoting their apoptosis. Tryptophan 63-73 indoleamine 2,3-dioxygenase 1 Homo sapiens 48-51 18660704-3 2008 RECENT FINDINGS: IDO catalyzes tryptophan and suppresses T-cell proliferation while tryptophan metabolites induce T-cell apoptosis. Tryptophan 31-41 indoleamine 2,3-dioxygenase 1 Homo sapiens 17-20 17870068-1 2007 The enzyme indoleamine 2,3-dioxygenase (IDO) catalyzes degradation of tryptophan, an essential amino acid required for lymphocyte activation and proliferation. Tryptophan 70-80 indoleamine 2,3-dioxygenase 1 Homo sapiens 40-43 17876564-6 2008 We focus here on recent findings establishing the tryptophan catabolizing enzyme indoleamine-pyrrole 2,3 dioxygenase (IDO) as a central feature of DC with regulatory function both in cancer and chronic infection. Tryptophan 50-60 indoleamine 2,3-dioxygenase 1 Homo sapiens 81-116 17876564-6 2008 We focus here on recent findings establishing the tryptophan catabolizing enzyme indoleamine-pyrrole 2,3 dioxygenase (IDO) as a central feature of DC with regulatory function both in cancer and chronic infection. Tryptophan 50-60 indoleamine 2,3-dioxygenase 1 Homo sapiens 118-121 18226121-1 2008 AIM: We have previously demonstrated that mRNA expression and enzyme activity levels of placental indoleamine 2,3-dioxygenase (IDO), which degrades L-tryptophan and blocks the proliferation of T cells, are significantly low in patients with severe pre-eclampsia. Tryptophan 148-160 indoleamine 2,3-dioxygenase 1 Homo sapiens 98-125 18226121-1 2008 AIM: We have previously demonstrated that mRNA expression and enzyme activity levels of placental indoleamine 2,3-dioxygenase (IDO), which degrades L-tryptophan and blocks the proliferation of T cells, are significantly low in patients with severe pre-eclampsia. Tryptophan 148-160 indoleamine 2,3-dioxygenase 1 Homo sapiens 127-130 18008147-1 2008 We have previously demonstrated that indoleamine 2,3-dioxygenase (IDO) expression by skin cells generates a tryptophan deficient environment in which THP-1, Jurkat cells as well as human PBMC are unable to survive. Tryptophan 108-118 indoleamine 2,3-dioxygenase 1 Homo sapiens 37-64 18008147-1 2008 We have previously demonstrated that indoleamine 2,3-dioxygenase (IDO) expression by skin cells generates a tryptophan deficient environment in which THP-1, Jurkat cells as well as human PBMC are unable to survive. Tryptophan 108-118 indoleamine 2,3-dioxygenase 1 Homo sapiens 66-69 18008147-4 2008 To address these questions, we co-cultured IDO-expressing fibroblasts with bystander human CD4+ and CD8+ T cells for 4 days and then the survival and proliferation rates as well as downstream metabolic pathway of tryptophan degradation in these cells were evaluated. Tryptophan 213-223 indoleamine 2,3-dioxygenase 1 Homo sapiens 43-46 18008147-8 2008 In conclusion, the finding of this study revealed that the proliferation of CD8+ and CD4+ T cells are suppressed in response to tryptophan deficient environment caused by IDO expression and it is more so for CD8+ T than CD4+ T cells. Tryptophan 128-138 indoleamine 2,3-dioxygenase 1 Homo sapiens 171-174 18365624-3 2008 RESULTS: IDO played an immunoregulatory role by locally depleting tryptophan in tissue microenvironment which resulted in immunosuppression of allogeneic T-cell proliferation. Tryptophan 66-76 indoleamine 2,3-dioxygenase 1 Homo sapiens 9-12 17933973-1 2007 Cells that express indoleamine 2,3-dioxygenase (IDO), the rate-limiting enzyme in the catabolism of tryptophan, suppress T cell responses and promote immunological tolerance. Tryptophan 100-110 indoleamine 2,3-dioxygenase 1 Homo sapiens 19-46 17933973-1 2007 Cells that express indoleamine 2,3-dioxygenase (IDO), the rate-limiting enzyme in the catabolism of tryptophan, suppress T cell responses and promote immunological tolerance. Tryptophan 100-110 indoleamine 2,3-dioxygenase 1 Homo sapiens 48-51 17933973-12 2007 Regulation of tryptophan catabolism by means of IDO overexpression may be a useful approach in heart transplantation. Tryptophan 14-24 indoleamine 2,3-dioxygenase 1 Homo sapiens 48-51 18094439-1 2007 Indolemine 2, 3-dioxygenase (IDO) is a cytosolic monomeric hemoprotein enzyme that catalyses tryptophan, the least available essential amino acid in the human body, to N-formylkynurenine, which in turn rapidly degrades to give kynurenine. Tryptophan 93-103 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 18094439-1 2007 Indolemine 2, 3-dioxygenase (IDO) is a cytosolic monomeric hemoprotein enzyme that catalyses tryptophan, the least available essential amino acid in the human body, to N-formylkynurenine, which in turn rapidly degrades to give kynurenine. Tryptophan 93-103 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 18094439-3 2007 Expression of IDO by certain dendritic cells, monocytes and macrophages has a regulatory effect on T cells probably by providing a tryptophan-deficient microenvironment and/or accumulation of toxic metabolites of tryptophan. Tryptophan 131-141 indoleamine 2,3-dioxygenase 1 Homo sapiens 14-17 18094439-3 2007 Expression of IDO by certain dendritic cells, monocytes and macrophages has a regulatory effect on T cells probably by providing a tryptophan-deficient microenvironment and/or accumulation of toxic metabolites of tryptophan. Tryptophan 213-223 indoleamine 2,3-dioxygenase 1 Homo sapiens 14-17 18026683-1 2007 Indoleamine 2,3-dioxygenase (IDO) and tryptophan 2,3-dioxygenase (TDO) are tryptophan-degrading enzymes that catalyze the same reaction, the first step in tryptophan catabolism via the kynurenine pathway. Tryptophan 38-48 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 18026683-1 2007 Indoleamine 2,3-dioxygenase (IDO) and tryptophan 2,3-dioxygenase (TDO) are tryptophan-degrading enzymes that catalyze the same reaction, the first step in tryptophan catabolism via the kynurenine pathway. Tryptophan 75-85 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 18026683-1 2007 Indoleamine 2,3-dioxygenase (IDO) and tryptophan 2,3-dioxygenase (TDO) are tryptophan-degrading enzymes that catalyze the same reaction, the first step in tryptophan catabolism via the kynurenine pathway. Tryptophan 75-85 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 18205804-8 2008 Therefore it is suggested that tryptophan depletion via IFN-gamma-mediated IDO induction is a major antibacterial, antiparasitic, antiviral and immunoregulatory mechanism in human lung cells. Tryptophan 31-41 indoleamine 2,3-dioxygenase 1 Homo sapiens 75-78 18453754-15 2008 CONCLUSIONS: Trophoblasts inhibit T lymphocyte through IDO-mediated tryptophan depletion and placenta-derived immunoregulatory factors. Tryptophan 68-78 indoleamine 2,3-dioxygenase 1 Homo sapiens 55-58 18036645-1 2008 BACKGROUND: Indoleamine-2, 3-dioxygenase (IDO), a tryptophan-degrading enzyme, plays a key role in the regulation of T-lymphocyte function. Tryptophan 50-60 indoleamine 2,3-dioxygenase 1 Homo sapiens 12-40 18036645-1 2008 BACKGROUND: Indoleamine-2, 3-dioxygenase (IDO), a tryptophan-degrading enzyme, plays a key role in the regulation of T-lymphocyte function. Tryptophan 50-60 indoleamine 2,3-dioxygenase 1 Homo sapiens 42-45 18055547-4 2007 Indoleamine 2,3-dioxygenase (IDO), which degrades tryptophan and suppresses T-cell proliferation, is induced by IFNs and other inflammatory cytokines. Tryptophan 50-60 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 18055547-4 2007 Indoleamine 2,3-dioxygenase (IDO), which degrades tryptophan and suppresses T-cell proliferation, is induced by IFNs and other inflammatory cytokines. Tryptophan 50-60 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 18077563-6 2007 The effect of IFN-gamma on iNOS might be mediated by kynurenine derivatives of tryptophan because (1) IFN-gamma stimulates the rate-determining enzyme of the Try-kynurenine pathway, indoleamine-2,3-dioxygenase (IDO) and (2) some kynurenines (e.g., quinolinic and picolinic acids) can stimulate iNOS. Tryptophan 79-89 indoleamine 2,3-dioxygenase 1 Homo sapiens 182-209 18077563-6 2007 The effect of IFN-gamma on iNOS might be mediated by kynurenine derivatives of tryptophan because (1) IFN-gamma stimulates the rate-determining enzyme of the Try-kynurenine pathway, indoleamine-2,3-dioxygenase (IDO) and (2) some kynurenines (e.g., quinolinic and picolinic acids) can stimulate iNOS. Tryptophan 79-89 indoleamine 2,3-dioxygenase 1 Homo sapiens 211-214 18056175-10 2007 CONCLUSIONS: IDO in endothelial cells might limit the influx of tryptophan from the blood to the tumor or generate tumor-toxic metabolites, thus restricting tumor growth and contributing to survival. Tryptophan 64-74 indoleamine 2,3-dioxygenase 1 Homo sapiens 13-16 17594069-1 2007 The tryptophan-catabolizing enzyme indoleamine-2,3-dioxygenase (IDO) initiates the first and rate-limiting step of the kynurenine pathway. Tryptophan 4-14 indoleamine 2,3-dioxygenase 1 Homo sapiens 35-62 17594069-1 2007 The tryptophan-catabolizing enzyme indoleamine-2,3-dioxygenase (IDO) initiates the first and rate-limiting step of the kynurenine pathway. Tryptophan 4-14 indoleamine 2,3-dioxygenase 1 Homo sapiens 64-67 18063923-0 2007 The immune effects of TRYCATs (tryptophan catabolites along the IDO pathway): relevance for depression - and other conditions characterized by tryptophan depletion induced by inflammation. Tryptophan 31-41 indoleamine 2,3-dioxygenase 1 Homo sapiens 64-67 18063923-0 2007 The immune effects of TRYCATs (tryptophan catabolites along the IDO pathway): relevance for depression - and other conditions characterized by tryptophan depletion induced by inflammation. Tryptophan 143-153 indoleamine 2,3-dioxygenase 1 Homo sapiens 64-67 18063923-1 2007 Immune activation is accompanied by induction of indoleamine (2,3)-dioxygenase (IDO), an enzyme which degrades tryptophan, a phenomenon which plays a role in the pathophysiology of major depression and post-natal depression and anxiety states. Tryptophan 111-121 indoleamine 2,3-dioxygenase 1 Homo sapiens 80-83 18063923-2 2007 TRYCATs - tryptophan catabolites along the IDO pathway - such as kynurenine, kynurenic acid, xanthurenic acid, and quinolinic acid, have multiple effects, e.g. apoptotic, anti- versus pro-oxidant, neurotoxic versus neuroprotective, and anxiolytic versus anxiogenic effects. Tryptophan 8-20 indoleamine 2,3-dioxygenase 1 Homo sapiens 43-46 17711489-1 2007 Indoleamine 2,3-dioxygenase (IDO) is a tryptophan-degrading enzyme which suppresses T lymphocyte activity. Tryptophan 39-49 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 17711489-1 2007 Indoleamine 2,3-dioxygenase (IDO) is a tryptophan-degrading enzyme which suppresses T lymphocyte activity. Tryptophan 39-49 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 17711489-2 2007 IDO activity can be determined by relating kynurenine, the main metabolite of tryptophan, to tryptophan (kyn/trp). Tryptophan 78-88 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 17711489-2 2007 IDO activity can be determined by relating kynurenine, the main metabolite of tryptophan, to tryptophan (kyn/trp). Tryptophan 93-103 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 17711489-2 2007 IDO activity can be determined by relating kynurenine, the main metabolite of tryptophan, to tryptophan (kyn/trp). Tryptophan 109-112 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 17870068-7 2007 IDO catalytic activity was assessed by measuring the presence of kynurenine, a product generated by tryptophan degradation, in uveal melanoma culture supernatants. Tryptophan 100-110 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 17999277-3 2007 Indoleamine 2,3-dioxygenase (IDO) is the first and regulatory enzyme in the major route of l-tryptophan catabolism, which induces immunosuppression of T lymphocytes. Tryptophan 91-103 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 17999277-3 2007 Indoleamine 2,3-dioxygenase (IDO) is the first and regulatory enzyme in the major route of l-tryptophan catabolism, which induces immunosuppression of T lymphocytes. Tryptophan 91-103 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 17715231-7 2007 Accordingly, plasma kynurenine/tryptophan, a marker for IDO enzymatic activity, was significantly higher in SIV(HI) compared to SIV(LO) and correlated with plasma viral levels. Tryptophan 31-41 indoleamine 2,3-dioxygenase 1 Homo sapiens 56-59 17457312-5 2007 Proinflammatory cytokines such as interleukin-2, interferon-gamma, or tumor necrosis factor-alpha activate the tryptophan- and serotonin-degrading enzyme indoleamine 2,3-dioxygenase (IDO). Tryptophan 111-121 indoleamine 2,3-dioxygenase 1 Homo sapiens 183-186 17457312-6 2007 Depressive states during inflammatory somatic disorders are also associated with increased proinflammatory cytokines and increased consumption of tryptophan via activation of IDO. Tryptophan 146-156 indoleamine 2,3-dioxygenase 1 Homo sapiens 175-178 17457312-7 2007 An enhanced consumption of serotonin and its precursor tryptophan through IDO activation could well explain the reduced availability of serotonergic neurotransmission in MD. Tryptophan 55-65 indoleamine 2,3-dioxygenase 1 Homo sapiens 74-77 17457312-9 2007 In inflammatory states of the central nervous system, IDO is mainly activated in microglial cells, which preferentially metabolize tryptophan to the NMDA receptor agonist quinolinic acid, whereas astrocytes - counteracting this metabolism due to the lack of an enzyme of this metabolism - have been observed to be reduced in MD. Tryptophan 131-141 indoleamine 2,3-dioxygenase 1 Homo sapiens 54-57 17928982-5 2007 Immune activation with increased production of proinflammatory cytokines activate the tryptophan- and serotonin-degradating enzyme indolamine-2,3-dioxygenase (IDO). Tryptophan 86-96 indoleamine 2,3-dioxygenase 1 Homo sapiens 131-157 17928982-5 2007 Immune activation with increased production of proinflammatory cytokines activate the tryptophan- and serotonin-degradating enzyme indolamine-2,3-dioxygenase (IDO). Tryptophan 86-96 indoleamine 2,3-dioxygenase 1 Homo sapiens 159-162 17928982-6 2007 The increased consumption of serotonin and its precursor tryptophan due to IDO activation may explain the reduced availability of serotonin in depression. Tryptophan 57-67 indoleamine 2,3-dioxygenase 1 Homo sapiens 75-78 17714779-2 2007 The objectives of this study were to investigate the phenotype and differentiation characteristics of MSC derived from human placenta and evaluate the role of the tryptophan degrading enzyme, indoleamine 2,3 dioxygenase (IDO), in mediating their immunosuppressive affect. Tryptophan 163-173 indoleamine 2,3-dioxygenase 1 Homo sapiens 192-219 17661345-1 2007 Indoleamine 2,3-dioxygenase (IDO), a tryptophan catabolizing enzyme, has been implicated in the pathogenesis of various neurological disorders. Tryptophan 37-47 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 17661345-1 2007 Indoleamine 2,3-dioxygenase (IDO), a tryptophan catabolizing enzyme, has been implicated in the pathogenesis of various neurological disorders. Tryptophan 37-47 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 17896864-2 2007 Tryptophan sequestration by up-regulation of the key enzyme for tryptophan degradation, indoleamine 2,3-dioxygenase (IDO), e.g., in cancer and inflammation, is thought to suppress the immune response via T cell starvation. Tryptophan 0-10 indoleamine 2,3-dioxygenase 1 Homo sapiens 88-115 17896864-2 2007 Tryptophan sequestration by up-regulation of the key enzyme for tryptophan degradation, indoleamine 2,3-dioxygenase (IDO), e.g., in cancer and inflammation, is thought to suppress the immune response via T cell starvation. Tryptophan 0-10 indoleamine 2,3-dioxygenase 1 Homo sapiens 117-120 17896864-2 2007 Tryptophan sequestration by up-regulation of the key enzyme for tryptophan degradation, indoleamine 2,3-dioxygenase (IDO), e.g., in cancer and inflammation, is thought to suppress the immune response via T cell starvation. Tryptophan 64-74 indoleamine 2,3-dioxygenase 1 Homo sapiens 88-115 17896864-2 2007 Tryptophan sequestration by up-regulation of the key enzyme for tryptophan degradation, indoleamine 2,3-dioxygenase (IDO), e.g., in cancer and inflammation, is thought to suppress the immune response via T cell starvation. Tryptophan 64-74 indoleamine 2,3-dioxygenase 1 Homo sapiens 117-120 17522338-2 2007 The molecular mechanism is widely thought to imply tryptophan degradation by the interferon-gamma (IFNgamma)-induced expression of indoleamine 2,3-dioxygenase (IDO). Tryptophan 51-61 indoleamine 2,3-dioxygenase 1 Homo sapiens 131-158 17522338-2 2007 The molecular mechanism is widely thought to imply tryptophan degradation by the interferon-gamma (IFNgamma)-induced expression of indoleamine 2,3-dioxygenase (IDO). Tryptophan 51-61 indoleamine 2,3-dioxygenase 1 Homo sapiens 160-163 17609291-2 2007 Indoleamine 2,3-dioxygenase (IDO) converts tryptophan to N-formyl-kynurenine and contributes to immune privilege in tissues by increasing Fas-mediated T cell apoptosis. Tryptophan 43-53 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 17609291-2 2007 Indoleamine 2,3-dioxygenase (IDO) converts tryptophan to N-formyl-kynurenine and contributes to immune privilege in tissues by increasing Fas-mediated T cell apoptosis. Tryptophan 43-53 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 17195079-6 2007 IDO was strongly upregulated in human DCs on RNA and on protein level upon in vitro maturation by Interleukin-1beta (IL-1beta), tumour necrosis factor-alpha (TNF-alpha), Interleukin-6 (IL-6) and Prostaglandin E2 (PGE2) over a time course of 24 h. The enzymatic activity of induced IDO was demonstrated by measuring tryptophan degradation. Tryptophan 315-325 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 17626075-1 2007 Indoleamine 2,3-dioxygenase (IDO) is the first and rate-limiting enzyme in the kynurenine pathway of tryptophan catabolism and has been implicated in neurotoxicity and suppression of the antiviral T-cell response in HIV encephalitis (HIVE). Tryptophan 101-111 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 17626075-1 2007 Indoleamine 2,3-dioxygenase (IDO) is the first and rate-limiting enzyme in the kynurenine pathway of tryptophan catabolism and has been implicated in neurotoxicity and suppression of the antiviral T-cell response in HIV encephalitis (HIVE). Tryptophan 101-111 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 17626075-8 2007 The involvement of IDO was demonstrated by partial but significant reversal of the PIC-mediated antiviral effect by IDO RNA interference and/or tryptophan supplementation. Tryptophan 144-154 indoleamine 2,3-dioxygenase 1 Homo sapiens 19-22 17535808-1 2007 The heme protein indoleamine 2,3-dioxygenase (IDO) is induced by the proinflammatory cytokine interferon-gamma (IFNgamma) and plays an important role in the immune response by catalyzing the oxidative degradation of L-tryptophan (Trp) that contributes to immune suppression and tolerance. Tryptophan 230-233 indoleamine 2,3-dioxygenase 1 Homo sapiens 17-44 17535808-1 2007 The heme protein indoleamine 2,3-dioxygenase (IDO) is induced by the proinflammatory cytokine interferon-gamma (IFNgamma) and plays an important role in the immune response by catalyzing the oxidative degradation of L-tryptophan (Trp) that contributes to immune suppression and tolerance. Tryptophan 230-233 indoleamine 2,3-dioxygenase 1 Homo sapiens 46-49 17671174-3 2007 Here, we report the discovery of a novel IDO-related tryptophan catabolic enzyme termed IDO2 that is preferentially inhibited by D-1MT. Tryptophan 53-63 indoleamine 2,3-dioxygenase 1 Homo sapiens 41-44 17671174-4 2007 IDO2 is not as widely expressed as IDO but like its relative is also expressed in antigen-presenting dendritic cells where tryptophan catabolism drives immune tolerance. Tryptophan 123-133 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 17521318-7 2007 IFN-gamma also induced expression of indoleamine 2,3, dioxygenase (IDO), involved in tryptophan catabolism. Tryptophan 85-95 indoleamine 2,3-dioxygenase 1 Homo sapiens 37-65 17521318-7 2007 IFN-gamma also induced expression of indoleamine 2,3, dioxygenase (IDO), involved in tryptophan catabolism. Tryptophan 85-95 indoleamine 2,3-dioxygenase 1 Homo sapiens 67-70 17521318-10 2007 These findings support a model where IDO exerts its effect through the local accumulation of tryptophan metabolites rather than through tryptophan depletion. Tryptophan 93-103 indoleamine 2,3-dioxygenase 1 Homo sapiens 37-40 17521318-10 2007 These findings support a model where IDO exerts its effect through the local accumulation of tryptophan metabolites rather than through tryptophan depletion. Tryptophan 136-146 indoleamine 2,3-dioxygenase 1 Homo sapiens 37-40 17617580-3 2007 The enzyme IDO degrades the indole moiety of tryptophan, not only depleting tryptophan but also producing immunomodulatory metabolites called kynurenines, which have apoptosis-inducing capabilities. Tryptophan 45-55 indoleamine 2,3-dioxygenase 1 Homo sapiens 11-14 17617580-3 2007 The enzyme IDO degrades the indole moiety of tryptophan, not only depleting tryptophan but also producing immunomodulatory metabolites called kynurenines, which have apoptosis-inducing capabilities. Tryptophan 76-86 indoleamine 2,3-dioxygenase 1 Homo sapiens 11-14 17535808-1 2007 The heme protein indoleamine 2,3-dioxygenase (IDO) is induced by the proinflammatory cytokine interferon-gamma (IFNgamma) and plays an important role in the immune response by catalyzing the oxidative degradation of L-tryptophan (Trp) that contributes to immune suppression and tolerance. Tryptophan 216-228 indoleamine 2,3-dioxygenase 1 Homo sapiens 17-44 17535808-1 2007 The heme protein indoleamine 2,3-dioxygenase (IDO) is induced by the proinflammatory cytokine interferon-gamma (IFNgamma) and plays an important role in the immune response by catalyzing the oxidative degradation of L-tryptophan (Trp) that contributes to immune suppression and tolerance. Tryptophan 216-228 indoleamine 2,3-dioxygenase 1 Homo sapiens 46-49 17644189-2 2007 By catabolizing tryptophan to N-formyl-kynurenine, IDO starves T cells from this important amino acid rendering them incapable of mounting appropriate immune responses. Tryptophan 16-26 indoleamine 2,3-dioxygenase 1 Homo sapiens 51-54 17644189-6 2007 IDO-induced tryptophan depletion from the tumor microenvironment could be the result of either elevated levels of the enzyme or augmented tryptophan consumption by both tumor cells and antigen presenting cells of the host. Tryptophan 12-22 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 17644189-6 2007 IDO-induced tryptophan depletion from the tumor microenvironment could be the result of either elevated levels of the enzyme or augmented tryptophan consumption by both tumor cells and antigen presenting cells of the host. Tryptophan 138-148 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 17158233-3 2007 Indoleamine 2,3-dioxygenase (IDO) is an immunosuppressive enzyme that inhibits T-cell proliferation by catabolizing the essential amino acid tryptophan (Trp) into the kynurenine (kyn) pathway. Tryptophan 153-156 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 17671174-6 2007 Like IDO, IDO2 catabolizes tryptophan, triggers phosphorylation of the translation initiation factor eIF2alpha, and (reported here for the first time) mobilizes translation of LIP, an inhibitory isoform of the immune regulatory transcription factor NF-IL6. Tryptophan 27-37 indoleamine 2,3-dioxygenase 1 Homo sapiens 5-8 17671174-7 2007 Tryptophan restoration switches off this signaling pathway when activated by IDO, but not IDO2, arguing that IDO2 has a distinct signaling role. Tryptophan 0-10 indoleamine 2,3-dioxygenase 1 Homo sapiens 77-80 17158233-3 2007 Indoleamine 2,3-dioxygenase (IDO) is an immunosuppressive enzyme that inhibits T-cell proliferation by catabolizing the essential amino acid tryptophan (Trp) into the kynurenine (kyn) pathway. Tryptophan 153-156 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 17349013-1 2007 Indoleamine 2,3 dioxygenase (IDO), an enzyme involved in the catabolism of tryptophan, suppresses T cell activity and is up-regulated by various inflammatory stimuli. Tryptophan 75-85 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 17349013-1 2007 Indoleamine 2,3 dioxygenase (IDO), an enzyme involved in the catabolism of tryptophan, suppresses T cell activity and is up-regulated by various inflammatory stimuli. Tryptophan 75-85 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 17349013-2 2007 The ratio of kynurenine, the main metabolite of tryptophan, to tryptophan (kyn/trp) reflects IDO activity. Tryptophan 48-58 indoleamine 2,3-dioxygenase 1 Homo sapiens 93-96 17349013-2 2007 The ratio of kynurenine, the main metabolite of tryptophan, to tryptophan (kyn/trp) reflects IDO activity. Tryptophan 63-73 indoleamine 2,3-dioxygenase 1 Homo sapiens 93-96 17349013-2 2007 The ratio of kynurenine, the main metabolite of tryptophan, to tryptophan (kyn/trp) reflects IDO activity. Tryptophan 79-82 indoleamine 2,3-dioxygenase 1 Homo sapiens 93-96 17393386-1 2007 A series of recent studies, including an article in this issue of the European Journal of Immunology, have demonstrated that the immunoregulatory pathway of tryptophan catabolism, initiated by the enzyme indoleamine 2,3-dioxygenase (IDO), not only represents an effector mechanism of peripheral tolerance, but is also a critical participant in the promotion of an optimally protective immune response balanced between inflammation and tolerance. Tryptophan 157-167 indoleamine 2,3-dioxygenase 1 Homo sapiens 233-236 17430108-2 2007 The tryptophan-degrading enzyme indoleamine 2,3-dioxygenase (IDO) is reported to be critically implicated. Tryptophan 4-14 indoleamine 2,3-dioxygenase 1 Homo sapiens 32-59 17430108-2 2007 The tryptophan-degrading enzyme indoleamine 2,3-dioxygenase (IDO) is reported to be critically implicated. Tryptophan 4-14 indoleamine 2,3-dioxygenase 1 Homo sapiens 61-64 17430109-0 2007 Tryptophan catabolism in IDO+ plasmacytoid dendritic cells. Tryptophan 0-10 indoleamine 2,3-dioxygenase 1 Homo sapiens 25-28 17430110-2 2007 HIV infection is associated with increased tryptophan (trp) catabolism by the cytokine-inducible enzyme indoleamine 2,3-dioxygenase (IDO). Tryptophan 43-53 indoleamine 2,3-dioxygenase 1 Homo sapiens 104-131 17430110-2 2007 HIV infection is associated with increased tryptophan (trp) catabolism by the cytokine-inducible enzyme indoleamine 2,3-dioxygenase (IDO). Tryptophan 43-53 indoleamine 2,3-dioxygenase 1 Homo sapiens 133-136 17430110-2 2007 HIV infection is associated with increased tryptophan (trp) catabolism by the cytokine-inducible enzyme indoleamine 2,3-dioxygenase (IDO). Tryptophan 55-58 indoleamine 2,3-dioxygenase 1 Homo sapiens 104-131 17430110-2 2007 HIV infection is associated with increased tryptophan (trp) catabolism by the cytokine-inducible enzyme indoleamine 2,3-dioxygenase (IDO). Tryptophan 55-58 indoleamine 2,3-dioxygenase 1 Homo sapiens 133-136 17430110-6 2007 HIV-induced, IDO-mediated trp catabolism may contribute to the perpetuation of HIV infection into its chronic phase by dampening efficient immune anti-viral responses. Tryptophan 26-29 indoleamine 2,3-dioxygenase 1 Homo sapiens 13-16 17430111-3 2007 Enhanced tryptophan degradation by the enzyme indoleamine-2, 3-dioxygenase (IDO) contributes importantly to disease progression and "complications" of HIV infection: By a subsequent impairment of protein metabolism and serotonin formation, the development of neuropsychiatric disorders and weight loss in HIV infected patients can be enforced. Tryptophan 9-19 indoleamine 2,3-dioxygenase 1 Homo sapiens 46-74 17430111-3 2007 Enhanced tryptophan degradation by the enzyme indoleamine-2, 3-dioxygenase (IDO) contributes importantly to disease progression and "complications" of HIV infection: By a subsequent impairment of protein metabolism and serotonin formation, the development of neuropsychiatric disorders and weight loss in HIV infected patients can be enforced. Tryptophan 9-19 indoleamine 2,3-dioxygenase 1 Homo sapiens 76-79 17430112-0 2007 Role of indoleamine 2,3-dioxygenase in antimicrobial defence and immuno-regulation: tryptophan depletion versus production of toxic kynurenines. Tryptophan 84-94 indoleamine 2,3-dioxygenase 1 Homo sapiens 8-35 17430112-1 2007 Tryptophan metabolism occurs via the protohemoprotein enzymes tryptophan 2,3-dioxygenase (TDO) and indoleamine 2,3-dioxygenase (IDO), the latter action of which has a number of effects in the body including both antimicrobial defence and immune regulation. Tryptophan 0-10 indoleamine 2,3-dioxygenase 1 Homo sapiens 99-126 17430112-1 2007 Tryptophan metabolism occurs via the protohemoprotein enzymes tryptophan 2,3-dioxygenase (TDO) and indoleamine 2,3-dioxygenase (IDO), the latter action of which has a number of effects in the body including both antimicrobial defence and immune regulation. Tryptophan 0-10 indoleamine 2,3-dioxygenase 1 Homo sapiens 128-131 17430112-3 2007 The list of pathogens that are "sensitive" to IDO-mediated tryptophan degradation covers intra-cellular parasites such as toxoplasma and possibly plasmodia, viruses (herpes viruses) to intra-cellular bacteria (chlamydia and rickettsia) and extra-cellular bacteria such as streptococci, enterococci and staphylococci. Tryptophan 59-69 indoleamine 2,3-dioxygenase 1 Homo sapiens 46-49 17430113-1 2007 Cells at the maternal-fetal interface express indoleamine 2,3 dioxygenase (IDO) to consume all local tryptophan for the express purpose of starving adjacent maternal T cells of this most limiting and essential amino acid. Tryptophan 101-111 indoleamine 2,3-dioxygenase 1 Homo sapiens 46-73 17430113-1 2007 Cells at the maternal-fetal interface express indoleamine 2,3 dioxygenase (IDO) to consume all local tryptophan for the express purpose of starving adjacent maternal T cells of this most limiting and essential amino acid. Tryptophan 101-111 indoleamine 2,3-dioxygenase 1 Homo sapiens 75-78 17430113-6 2007 Approaches to cell specific therapeutic IDO induction with NAD precursor supplementation to prevent the collateral non-T cell pathogenesis due to chronic TNFalpha-IDO activated tryptophan depletion in autoimmune diseases are reviewed. Tryptophan 177-187 indoleamine 2,3-dioxygenase 1 Homo sapiens 40-43 17430113-6 2007 Approaches to cell specific therapeutic IDO induction with NAD precursor supplementation to prevent the collateral non-T cell pathogenesis due to chronic TNFalpha-IDO activated tryptophan depletion in autoimmune diseases are reviewed. Tryptophan 177-187 indoleamine 2,3-dioxygenase 1 Homo sapiens 163-166 17430113-10 2007 Loss of function leads to psychotic symptoms rapidly progressing to presenile dementia likely due to unchecked increases in microglial IDO expression, which depletes neurons of tryptophan causing neurodegeneration. Tryptophan 177-187 indoleamine 2,3-dioxygenase 1 Homo sapiens 135-138 17355802-1 2007 BACKGROUND & OBJECTIVE: Indoleamine 2,3-dioxygenase (IDO), a cytosolic hemoprotein, catalyzes the rate-limiting step in tryptophan catabolism along the kynurenine pathway in mammals, arrests the growth of pathogens, and suppresses T-cell responses, therefore, leads to IDO-dependent tumor immune tolerance. Tryptophan 124-134 indoleamine 2,3-dioxygenase 1 Homo sapiens 28-55 17371982-1 2007 Dendritic cell-derived indoleamine 2,3-dioxygenase (IDO) suppresses naive T cell proliferation and induces their apoptosis by catalyzing tryptophan, and hence is essential for the maintenance of peripheral tolerance. Tryptophan 137-147 indoleamine 2,3-dioxygenase 1 Homo sapiens 23-50 17371982-1 2007 Dendritic cell-derived indoleamine 2,3-dioxygenase (IDO) suppresses naive T cell proliferation and induces their apoptosis by catalyzing tryptophan, and hence is essential for the maintenance of peripheral tolerance. Tryptophan 137-147 indoleamine 2,3-dioxygenase 1 Homo sapiens 52-55 17371982-2 2007 However, it is not known whether memory T cells are subject to the regulation by IDO-mediated tryptophan catabolism, as memory T cells respond more rapidly and vigorously than their naive counterparts and are resistant to conventional costimulatory blockade. Tryptophan 94-104 indoleamine 2,3-dioxygenase 1 Homo sapiens 81-84 17371982-3 2007 In this study, we present the evidence that memory CD8+ T cells are susceptible to tryptophan catabolism mediated by IDO. Tryptophan 83-93 indoleamine 2,3-dioxygenase 1 Homo sapiens 117-120 17355802-1 2007 BACKGROUND & OBJECTIVE: Indoleamine 2,3-dioxygenase (IDO), a cytosolic hemoprotein, catalyzes the rate-limiting step in tryptophan catabolism along the kynurenine pathway in mammals, arrests the growth of pathogens, and suppresses T-cell responses, therefore, leads to IDO-dependent tumor immune tolerance. Tryptophan 124-134 indoleamine 2,3-dioxygenase 1 Homo sapiens 57-60 17355802-1 2007 BACKGROUND & OBJECTIVE: Indoleamine 2,3-dioxygenase (IDO), a cytosolic hemoprotein, catalyzes the rate-limiting step in tryptophan catabolism along the kynurenine pathway in mammals, arrests the growth of pathogens, and suppresses T-cell responses, therefore, leads to IDO-dependent tumor immune tolerance. Tryptophan 124-134 indoleamine 2,3-dioxygenase 1 Homo sapiens 273-276 17305476-1 2007 The extrahepatic enzyme indoleamine 2,3-dioxygenase (IDO) catalyzes tryptophan degradation in the first and rate-limiting step towards biosynthesis of the central metabolic co-factor nicotinamide adenine dinucleotide (NAD). Tryptophan 68-78 indoleamine 2,3-dioxygenase 1 Homo sapiens 53-56 17227442-3 2007 Activation of indoleamine-2,3-dioxygenase (IDO), the first and rate-limiting enzyme of the kynurenine pathway by IFNs, leads to an increase in tryptophan (Trp) catabolism. Tryptophan 143-153 indoleamine 2,3-dioxygenase 1 Homo sapiens 14-41 17227442-3 2007 Activation of indoleamine-2,3-dioxygenase (IDO), the first and rate-limiting enzyme of the kynurenine pathway by IFNs, leads to an increase in tryptophan (Trp) catabolism. Tryptophan 143-153 indoleamine 2,3-dioxygenase 1 Homo sapiens 43-46 17227442-3 2007 Activation of indoleamine-2,3-dioxygenase (IDO), the first and rate-limiting enzyme of the kynurenine pathway by IFNs, leads to an increase in tryptophan (Trp) catabolism. Tryptophan 155-158 indoleamine 2,3-dioxygenase 1 Homo sapiens 14-41 17227442-3 2007 Activation of indoleamine-2,3-dioxygenase (IDO), the first and rate-limiting enzyme of the kynurenine pathway by IFNs, leads to an increase in tryptophan (Trp) catabolism. Tryptophan 155-158 indoleamine 2,3-dioxygenase 1 Homo sapiens 43-46 17191041-2 2007 Via tryptophan deprivation, IDO activity suppresses T cell proliferation and differentiation and is thought to be a fundamental immune escape mechanism for tumor cells. Tryptophan 4-14 indoleamine 2,3-dioxygenase 1 Homo sapiens 28-31 17430114-3 2007 Negative-feedback mechanisms to counteract inflammation involve the induction of the immunoregulatory enzyme indoleamine 2,3-dioxygenase (IDO), which mediates anti-inflammatory activities and T-cell inhibition via tryptophan catabolism. Tryptophan 214-224 indoleamine 2,3-dioxygenase 1 Homo sapiens 109-136 17430114-3 2007 Negative-feedback mechanisms to counteract inflammation involve the induction of the immunoregulatory enzyme indoleamine 2,3-dioxygenase (IDO), which mediates anti-inflammatory activities and T-cell inhibition via tryptophan catabolism. Tryptophan 214-224 indoleamine 2,3-dioxygenase 1 Homo sapiens 138-141 17430116-2 2007 The synthesis of serotonin is dependent on the availability of tryptophan--an amino acid that is linked to the immune system by its catabolism via the enzyme indoleamine-2,3-dioxygenase (IDO). Tryptophan 63-73 indoleamine 2,3-dioxygenase 1 Homo sapiens 158-185 17430116-2 2007 The synthesis of serotonin is dependent on the availability of tryptophan--an amino acid that is linked to the immune system by its catabolism via the enzyme indoleamine-2,3-dioxygenase (IDO). Tryptophan 63-73 indoleamine 2,3-dioxygenase 1 Homo sapiens 187-190 17430117-7 2007 In addition, we previously demonstrated that IDO mediated tryptophan catabolism due to chronic immune activation is the cause for such reduced tryptophan plasma levels in morbidly obese patients compared to lean individuals. Tryptophan 58-68 indoleamine 2,3-dioxygenase 1 Homo sapiens 45-48 17430117-7 2007 In addition, we previously demonstrated that IDO mediated tryptophan catabolism due to chronic immune activation is the cause for such reduced tryptophan plasma levels in morbidly obese patients compared to lean individuals. Tryptophan 143-153 indoleamine 2,3-dioxygenase 1 Homo sapiens 45-48 17430117-9 2007 IDO-mediated tryptophan degradation due to chronic immune activation can therefore be considered as the driving force for food intake. Tryptophan 13-23 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 17430117-10 2007 We here review the potential pathogenic links between chronic immune activation and decreased IDO mediated tryptophan and serotonin levels in morbid obesity. Tryptophan 107-117 indoleamine 2,3-dioxygenase 1 Homo sapiens 94-97 17239019-1 2007 Indoleamine 2,3-dioxygenase (IDO), by enzymatic tryptophan degradation, has recently been proposed to have profound immunoregulatory activity. Tryptophan 48-58 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 17239019-1 2007 Indoleamine 2,3-dioxygenase (IDO), by enzymatic tryptophan degradation, has recently been proposed to have profound immunoregulatory activity. Tryptophan 48-58 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 17192467-1 2007 Indoleamine 2,3-dioxygenase (IDO) catalyzes the initial, rate-limiting step of tryptophan (Trp) catabolism along the kynurenine (KYN) pathway, and its induction in cells of the immune system in response to cytokines has been implicated in the regulation of antigen presentation and responses to cell-mediated immune attack. Tryptophan 79-89 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 17320464-1 2007 Indoleamine 2,3-dioxygenase (IDO) is a heme enzyme that initiates the oxidative degradation of the least abundant, essential amino acid, l-tryptophan, along the kynurenine pathway. Tryptophan 137-149 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 17192467-1 2007 Indoleamine 2,3-dioxygenase (IDO) catalyzes the initial, rate-limiting step of tryptophan (Trp) catabolism along the kynurenine (KYN) pathway, and its induction in cells of the immune system in response to cytokines has been implicated in the regulation of antigen presentation and responses to cell-mediated immune attack. Tryptophan 79-89 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 17192467-1 2007 Indoleamine 2,3-dioxygenase (IDO) catalyzes the initial, rate-limiting step of tryptophan (Trp) catabolism along the kynurenine (KYN) pathway, and its induction in cells of the immune system in response to cytokines has been implicated in the regulation of antigen presentation and responses to cell-mediated immune attack. Tryptophan 91-94 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 17192467-1 2007 Indoleamine 2,3-dioxygenase (IDO) catalyzes the initial, rate-limiting step of tryptophan (Trp) catabolism along the kynurenine (KYN) pathway, and its induction in cells of the immune system in response to cytokines has been implicated in the regulation of antigen presentation and responses to cell-mediated immune attack. Tryptophan 91-94 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 17320464-1 2007 Indoleamine 2,3-dioxygenase (IDO) is a heme enzyme that initiates the oxidative degradation of the least abundant, essential amino acid, l-tryptophan, along the kynurenine pathway. Tryptophan 137-149 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 16902152-1 2006 Tryptophan (Trp) catabolism mediated by indoleamine 2,3-dioxygenase (IDO) plays a central role in the regulation of T-cell-mediated immune responses. Tryptophan 0-10 indoleamine 2,3-dioxygenase 1 Homo sapiens 40-67 17982903-10 2007 Due to the inhibition of IDO, tryptophan is predominantly metabolized by tryptophan 2,3-dioxygenase (TDO), which is located in astrocytes, but not in microglia cells. Tryptophan 30-40 indoleamine 2,3-dioxygenase 1 Homo sapiens 25-28 17136028-1 2007 The immunomodulatory enzyme indoleamine 2,3-dioxygenase (IDO) is activated by interferon-gamma (IFN-gamma) and via tryptophan depletion, suppresses adaptive T cell-mediated immunity in inflammation, host immune defense, and maternal tolerance. Tryptophan 115-125 indoleamine 2,3-dioxygenase 1 Homo sapiens 28-55 17136028-1 2007 The immunomodulatory enzyme indoleamine 2,3-dioxygenase (IDO) is activated by interferon-gamma (IFN-gamma) and via tryptophan depletion, suppresses adaptive T cell-mediated immunity in inflammation, host immune defense, and maternal tolerance. Tryptophan 115-125 indoleamine 2,3-dioxygenase 1 Homo sapiens 57-60 17136028-3 2007 Therefore, we investigated the usefulness of IDO-mediated tryptophan catabolism in the evaluation of kidney allograft rejection. Tryptophan 58-68 indoleamine 2,3-dioxygenase 1 Homo sapiens 45-48 17136028-12 2007 Kyn/trp correlated significantly with neopterin suggesting an IFN-gamma-induced increase in IDO activity. Tryptophan 4-7 indoleamine 2,3-dioxygenase 1 Homo sapiens 92-95 16902152-1 2006 Tryptophan (Trp) catabolism mediated by indoleamine 2,3-dioxygenase (IDO) plays a central role in the regulation of T-cell-mediated immune responses. Tryptophan 0-10 indoleamine 2,3-dioxygenase 1 Homo sapiens 69-72 16902152-1 2006 Tryptophan (Trp) catabolism mediated by indoleamine 2,3-dioxygenase (IDO) plays a central role in the regulation of T-cell-mediated immune responses. Tryptophan 12-15 indoleamine 2,3-dioxygenase 1 Homo sapiens 40-67 16902152-1 2006 Tryptophan (Trp) catabolism mediated by indoleamine 2,3-dioxygenase (IDO) plays a central role in the regulation of T-cell-mediated immune responses. Tryptophan 12-15 indoleamine 2,3-dioxygenase 1 Homo sapiens 69-72 16902152-3 2006 Indeed, l-kynurenine, a Trp-derived catabolite resulting from IDO activity, was found to prevent the cytokine-mediated up-regulation of the expression and function of specific triggering receptors responsible for the induction of NK-cell-mediated killing. Tryptophan 24-27 indoleamine 2,3-dioxygenase 1 Homo sapiens 62-65 17117179-1 2006 Indoleamine 2,3-dioxygenase (IDO) is a tryptophan-catabolising enzyme inducing immune tolerance. Tryptophan 39-49 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 16522817-6 2006 As a consequence, T-cell proliferation and cytokine production were significantly inhibited, which was mediated mainly by IDO-induced tryptophan depletion. Tryptophan 134-144 indoleamine 2,3-dioxygenase 1 Homo sapiens 122-125 16997853-1 2006 Tryptophan catabolism via the enzyme indoleamine 2,3-dioxygenase (IDO) allows human monocyte-derived macrophages (MDM) and other APC to suppress T cell proliferation. Tryptophan 0-10 indoleamine 2,3-dioxygenase 1 Homo sapiens 66-69 16997853-3 2006 For tryptophan to be catabolized by IDO, it must first enter the APC via transmembrane transport. Tryptophan 4-14 indoleamine 2,3-dioxygenase 1 Homo sapiens 36-39 16997853-4 2006 It has been shown that MDM in vitro readily deplete tryptophan present in the extracellular medium to nanomolar levels via IDO activity; yet, no currently known amino acid transport system displays high affinity and specificity sufficiently to permit efficient uptake of tryptophan at these low concentrations. Tryptophan 52-62 indoleamine 2,3-dioxygenase 1 Homo sapiens 123-126 16997853-9 2006 In contrast, resting human T cells expressed only the conventional system L. We speculate that the high-affinity, tryptophan-specific transport system allows MDM to take up tryptophan efficiently under conditions of low substrate concentration, such as may occur during interaction between T cells and IDO-expressing APC. Tryptophan 114-124 indoleamine 2,3-dioxygenase 1 Homo sapiens 302-305 16997853-9 2006 In contrast, resting human T cells expressed only the conventional system L. We speculate that the high-affinity, tryptophan-specific transport system allows MDM to take up tryptophan efficiently under conditions of low substrate concentration, such as may occur during interaction between T cells and IDO-expressing APC. Tryptophan 173-183 indoleamine 2,3-dioxygenase 1 Homo sapiens 302-305 16907915-1 2006 Indoleamine 2,3-dioxygenase (IDO), an enzyme involved in the degradation of the essential amino acid tryptophan (trp) to its main metabolite kynurenine (kyn), suppresses T cell activity. Tryptophan 113-116 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 16907915-1 2006 Indoleamine 2,3-dioxygenase (IDO), an enzyme involved in the degradation of the essential amino acid tryptophan (trp) to its main metabolite kynurenine (kyn), suppresses T cell activity. Tryptophan 113-116 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 16896154-7 2006 CTLA-4 blockade decreased expression of the tryptophan-depleting enzyme IDO and the level of the suppressive cytokine transforming growth factor-beta (TGF-beta) in tissues. Tryptophan 44-54 indoleamine 2,3-dioxygenase 1 Homo sapiens 72-75 17030574-1 2006 Gamma interferon (IFN-gamma)-induced indoleamine dioxygenase (IDO), which inhibits chlamydial replication by reducing the availability of tryptophan, is up-regulated by interleukin-1beta (IL-1beta) and tumor necrosis factor alpha (TNF-alpha). Tryptophan 138-148 indoleamine 2,3-dioxygenase 1 Homo sapiens 62-65 17114500-6 2006 Furthermore, we found that functionally active tryptophanyl-tRNA-synthetase (TTS) was significantly elevated in T cells derived from the SF of RA patients, leading to enhanced storage of tryptophan in T cells and to subsequent resistance to IDO-mediated deprivation of tryptophan. Tryptophan 47-57 indoleamine 2,3-dioxygenase 1 Homo sapiens 241-244 17114500-8 2006 These results suggest that the resistance of T cells to IDO-mediated deprivation of tryptophan represents a mechanism by which autoreactive T cells are sustained in vivo in RA patients. Tryptophan 84-94 indoleamine 2,3-dioxygenase 1 Homo sapiens 56-59 17062375-12 2006 IDO catalyzes the first step in tryptophan metabolism, the degradation from tryptophan to kynurenine, as does tryptophan 2,3-dioxygenase (TDO). Tryptophan 32-42 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 17062375-12 2006 IDO catalyzes the first step in tryptophan metabolism, the degradation from tryptophan to kynurenine, as does tryptophan 2,3-dioxygenase (TDO). Tryptophan 76-86 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 17062375-13 2006 Due to the inhibition of IDO, tryptophan-kynurenine is predominantly metabolized by TDO, which is located in astrocytes, not in microglial or other CNS cells. Tryptophan 30-40 indoleamine 2,3-dioxygenase 1 Homo sapiens 25-28 16797727-1 2006 Indoleamine 2,3-dioxygenase (IDO) is an enzyme that depletes l-tryptophan, which provokes a decreased T cell response. Tryptophan 61-73 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 16797727-1 2006 Indoleamine 2,3-dioxygenase (IDO) is an enzyme that depletes l-tryptophan, which provokes a decreased T cell response. Tryptophan 61-73 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 16834326-1 2006 Indoleamine 2,3-dioxygenase (IDO) is a heme-containing enzyme, which catalyzes the initial and rate-determining step of L-tryptophan (L-Trp) metabolism via the kynurenine pathway in nonhepatic tissues. Tryptophan 120-132 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 16834326-1 2006 Indoleamine 2,3-dioxygenase (IDO) is a heme-containing enzyme, which catalyzes the initial and rate-determining step of L-tryptophan (L-Trp) metabolism via the kynurenine pathway in nonhepatic tissues. Tryptophan 120-132 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 16834326-1 2006 Indoleamine 2,3-dioxygenase (IDO) is a heme-containing enzyme, which catalyzes the initial and rate-determining step of L-tryptophan (L-Trp) metabolism via the kynurenine pathway in nonhepatic tissues. Tryptophan 134-139 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 16834326-1 2006 Indoleamine 2,3-dioxygenase (IDO) is a heme-containing enzyme, which catalyzes the initial and rate-determining step of L-tryptophan (L-Trp) metabolism via the kynurenine pathway in nonhepatic tissues. Tryptophan 134-139 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 16834326-5 2006 Resonance Raman data show that the heme prosthetic group in the NO-bound hIDO is situated in a unique protein environment and adopts an out-of-plane deformed geometry that is sensitive to L-Trp binding. Tryptophan 188-193 indoleamine 2,3-dioxygenase 1 Homo sapiens 73-77 16834326-9 2006 The spectroscopic data presented here not only provide the first glimpse of the possible regulatory mechanism of hIDO by NO in the cell at the molecular level, but they also suggest that the NO-dependent regulation can be modulated by cellular factors, such as the NO abundance, pH, redox environment, and L-Trp availability. Tryptophan 306-311 indoleamine 2,3-dioxygenase 1 Homo sapiens 113-117 16931033-1 2006 Interferon (IFN)-gamma-induced expression of indoleamine 2,3-dioxygenase (IDO), an enzyme that inhibits some pathogens by limiting tryptophan availability, is transcriptionally enhanced by tumor necrosis factor (TNF)-alpha. Tryptophan 131-141 indoleamine 2,3-dioxygenase 1 Homo sapiens 45-72 16931033-1 2006 Interferon (IFN)-gamma-induced expression of indoleamine 2,3-dioxygenase (IDO), an enzyme that inhibits some pathogens by limiting tryptophan availability, is transcriptionally enhanced by tumor necrosis factor (TNF)-alpha. Tryptophan 131-141 indoleamine 2,3-dioxygenase 1 Homo sapiens 74-77 16490253-3 2006 IDO degrades Trp to kynurenine, which is further metabolized to 3-hydroxyanthranilic acid. Tryptophan 13-16 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 16687019-1 2006 BACKGROUND: Increased activity of the immuno-modulatory enzyme indoleamine-2,3-dioxygenase (IDO) during immune activation, results in tryptophan depletion. Tryptophan 134-144 indoleamine 2,3-dioxygenase 1 Homo sapiens 63-90 16842443-1 2006 Indoleamine 2,3-dioxygenase (IDO), a key enzyme of tryptophan (TRP) metabolism, is induced in various tissues of patients with bacterial and viral infection or with neoplastic diseases. Tryptophan 51-61 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 16842443-1 2006 Indoleamine 2,3-dioxygenase (IDO), a key enzyme of tryptophan (TRP) metabolism, is induced in various tissues of patients with bacterial and viral infection or with neoplastic diseases. Tryptophan 51-61 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 16842443-1 2006 Indoleamine 2,3-dioxygenase (IDO), a key enzyme of tryptophan (TRP) metabolism, is induced in various tissues of patients with bacterial and viral infection or with neoplastic diseases. Tryptophan 63-66 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 16842443-1 2006 Indoleamine 2,3-dioxygenase (IDO), a key enzyme of tryptophan (TRP) metabolism, is induced in various tissues of patients with bacterial and viral infection or with neoplastic diseases. Tryptophan 63-66 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 16261283-2 2006 The proinflammatory cytokine interferon-gamma in various cells, including monocytes, induces the enzyme indoleamine (2,3)-dioxygenase (IDO), which converts tryptophan to kynurenine. Tryptophan 156-166 indoleamine 2,3-dioxygenase 1 Homo sapiens 135-138 16513157-1 2006 Indoleamine 2,3-dioxygenase (IDO), an enzyme degrading tryptophan (trp) to kynurenine (kyn), suppresses T cell activity. Tryptophan 55-65 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 16513157-1 2006 Indoleamine 2,3-dioxygenase (IDO), an enzyme degrading tryptophan (trp) to kynurenine (kyn), suppresses T cell activity. Tryptophan 55-65 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 16513157-1 2006 Indoleamine 2,3-dioxygenase (IDO), an enzyme degrading tryptophan (trp) to kynurenine (kyn), suppresses T cell activity. Tryptophan 67-70 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 16513157-1 2006 Indoleamine 2,3-dioxygenase (IDO), an enzyme degrading tryptophan (trp) to kynurenine (kyn), suppresses T cell activity. Tryptophan 67-70 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 16687019-1 2006 BACKGROUND: Increased activity of the immuno-modulatory enzyme indoleamine-2,3-dioxygenase (IDO) during immune activation, results in tryptophan depletion. Tryptophan 134-144 indoleamine 2,3-dioxygenase 1 Homo sapiens 92-95 16687019-4 2006 We examined IDO-mediated tryptophan-catabolism in morbidly obese patients compared to lean individuals. Tryptophan 25-35 indoleamine 2,3-dioxygenase 1 Homo sapiens 12-15 16897708-1 2006 Indoleamine 2,3-dioxygenase (IDO) is a tryptophan degradation enzyme that is emerging as an important drug target. Tryptophan 39-49 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 16897708-4 2006 We show that expression of human IDO in a Saccharomyces cerevisiae tryptophan auxotroph restricts yeast growth in the presence of low tryptophan concentrations and that inhibition of IDO activity can restore growth. Tryptophan 67-77 indoleamine 2,3-dioxygenase 1 Homo sapiens 33-36 16897708-4 2006 We show that expression of human IDO in a Saccharomyces cerevisiae tryptophan auxotroph restricts yeast growth in the presence of low tryptophan concentrations and that inhibition of IDO activity can restore growth. Tryptophan 134-144 indoleamine 2,3-dioxygenase 1 Homo sapiens 33-36 16482510-1 2006 Indoleamine 2,3-dioxygenase (IDO) suppresses T cell responses by its action in catabolising tryptophan. Tryptophan 92-102 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 16482510-1 2006 Indoleamine 2,3-dioxygenase (IDO) suppresses T cell responses by its action in catabolising tryptophan. Tryptophan 92-102 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 16489067-11 2006 CONCLUSION: IDO-high expression by colorectal tumor cells enables certain cancer subsets to initially avoid immune attack and defeat the invasion of T cells via local tryptophan depletion and the production of proapoptotic tryptophan catabolites. Tryptophan 167-177 indoleamine 2,3-dioxygenase 1 Homo sapiens 12-15 16477023-1 2006 Human indoleamine 2,3-dioxygenase (IDO) catalyzes the cleavage of the pyrrol ring of L-Trp and incorporates both atoms of a molecule of oxygen (O2). Tryptophan 85-90 indoleamine 2,3-dioxygenase 1 Homo sapiens 6-33 16477023-1 2006 Human indoleamine 2,3-dioxygenase (IDO) catalyzes the cleavage of the pyrrol ring of L-Trp and incorporates both atoms of a molecule of oxygen (O2). Tryptophan 85-90 indoleamine 2,3-dioxygenase 1 Homo sapiens 35-38 16489067-11 2006 CONCLUSION: IDO-high expression by colorectal tumor cells enables certain cancer subsets to initially avoid immune attack and defeat the invasion of T cells via local tryptophan depletion and the production of proapoptotic tryptophan catabolites. Tryptophan 223-233 indoleamine 2,3-dioxygenase 1 Homo sapiens 12-15 16368976-7 2006 Induction of IDO in human cell lines inhibited growth of L2 and mouse pneumonitis agent, now referred to as Chlamydia muridarum MoPn equally in all but two lines, and inhibition was completely reversible by the addition of tryptophan. Tryptophan 223-233 indoleamine 2,3-dioxygenase 1 Homo sapiens 13-16 16321356-4 2006 Measured activities of IDO, including in the presence of tryptophan-based inhibitors, were in statistical agreement with the absorbance and HPLC assay methods. Tryptophan 57-67 indoleamine 2,3-dioxygenase 1 Homo sapiens 23-26 16476191-2 2006 Indoleamine-2,3-dioxygenase (IDO), an enzyme classically known for its role in the tryptophan degradation pathway, has recently emerged as an important immunomodulator of T-cell function and inducer of tolerance. Tryptophan 83-93 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 16476191-2 2006 Indoleamine-2,3-dioxygenase (IDO), an enzyme classically known for its role in the tryptophan degradation pathway, has recently emerged as an important immunomodulator of T-cell function and inducer of tolerance. Tryptophan 83-93 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 16476191-3 2006 The induced expression of IDO by dendritic cells may suppress T-cell responses and promote tolerance either through direct effects on T cells (mediated by tryptophan depletion or tryptophan metabolites) or through effects of IDO on the dendritic cell. Tryptophan 155-165 indoleamine 2,3-dioxygenase 1 Homo sapiens 26-29 16476191-3 2006 The induced expression of IDO by dendritic cells may suppress T-cell responses and promote tolerance either through direct effects on T cells (mediated by tryptophan depletion or tryptophan metabolites) or through effects of IDO on the dendritic cell. Tryptophan 179-189 indoleamine 2,3-dioxygenase 1 Homo sapiens 26-29 16139256-4 2006 Tryptophan depletion via IDO is part of the cytostatic and antiproliferative activity mediated by interferon-gamma in cells. Tryptophan 0-10 indoleamine 2,3-dioxygenase 1 Homo sapiens 25-28 16139256-6 2006 IDO activity is characterized best by the kynurenine to tryptophan ratio which correlates with concentrations of immune activation markers such as neopterin. Tryptophan 56-66 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 16139256-10 2006 As such, monitoring tryptophan metabolism in chronic immunopathology provides a better understanding of the association between immune activation and IDO and its role in the development of immunodeficiency, anemia and mood disorders. Tryptophan 20-30 indoleamine 2,3-dioxygenase 1 Homo sapiens 150-153 16385630-1 2006 Production of indoleamine 2,3-dioxygenase (IDO) by tumor cells, leading to tryptophan depletion and production of immunosuppressive metabolites, may facilitate immune tolerance of cancer. Tryptophan 75-85 indoleamine 2,3-dioxygenase 1 Homo sapiens 14-41 16385630-1 2006 Production of indoleamine 2,3-dioxygenase (IDO) by tumor cells, leading to tryptophan depletion and production of immunosuppressive metabolites, may facilitate immune tolerance of cancer. Tryptophan 75-85 indoleamine 2,3-dioxygenase 1 Homo sapiens 43-46 16417228-1 2006 The expression of indoleamine 2,3-dioxygenase (IDO), which metabolizes tryptophan, an essential amino acid, into kynurenine, has been identified as having a key role in the prevention of the immune rejection of the semi-allogeneic fetus during pregnancy. Tryptophan 71-81 indoleamine 2,3-dioxygenase 1 Homo sapiens 18-45 16365430-1 2006 IDO induction can deplete L-tryptophan in target cells, an effect partially responsible for the antimicrobial activities and antiallogeneic T cell responses of IFN-gamma in human macrophages, dendritic cells, and bone marrow cells. Tryptophan 26-38 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 16417228-1 2006 The expression of indoleamine 2,3-dioxygenase (IDO), which metabolizes tryptophan, an essential amino acid, into kynurenine, has been identified as having a key role in the prevention of the immune rejection of the semi-allogeneic fetus during pregnancy. Tryptophan 71-81 indoleamine 2,3-dioxygenase 1 Homo sapiens 47-50 16417228-6 2006 Using a co-culture system, we further confirm that IDO can induce angiogenesis through the depletion of tryptophan. Tryptophan 104-114 indoleamine 2,3-dioxygenase 1 Homo sapiens 51-54 16166276-1 2005 Activation of the tryptophan catabolizing enzyme indoleamine 2,3-dioxygenase (IDO) in cancer cells facilitates immune escape. Tryptophan 18-28 indoleamine 2,3-dioxygenase 1 Homo sapiens 78-81 16236119-3 2005 IDO is an enzyme that acts by depleting the surrounding microenvironment of the essential amino acid, tryptophan, thereby inhibiting T-cell proliferation. Tryptophan 102-112 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 15961516-1 2005 Indoleamine 2,3-dioxygenase (IDO) is the rate-limiting enzyme in the kynurenine pathway of tryptophan metabolism. Tryptophan 91-101 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 15961516-1 2005 Indoleamine 2,3-dioxygenase (IDO) is the rate-limiting enzyme in the kynurenine pathway of tryptophan metabolism. Tryptophan 91-101 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 16166276-1 2005 Activation of the tryptophan catabolizing enzyme indoleamine 2,3-dioxygenase (IDO) in cancer cells facilitates immune escape. Tryptophan 18-28 indoleamine 2,3-dioxygenase 1 Homo sapiens 49-76 16083346-2 2005 Elevated tryptophan catabolism mediated by IDO is associated with a wide variety of human cancers and has historically been thought to be a tumoricidal consequence of IFN-gamma exposure. Tryptophan 9-19 indoleamine 2,3-dioxygenase 1 Homo sapiens 43-46 16113824-6 2005 This antiviral effect was completely blocked in the presence of L-tryptophan, indicating the induction of the tryptophan degrading enzyme indoleamine 2,3-dioxygenase (IDO) to be responsible for the observed antiviral effect. Tryptophan 64-76 indoleamine 2,3-dioxygenase 1 Homo sapiens 138-165 16113824-6 2005 This antiviral effect was completely blocked in the presence of L-tryptophan, indicating the induction of the tryptophan degrading enzyme indoleamine 2,3-dioxygenase (IDO) to be responsible for the observed antiviral effect. Tryptophan 64-76 indoleamine 2,3-dioxygenase 1 Homo sapiens 167-170 16113824-6 2005 This antiviral effect was completely blocked in the presence of L-tryptophan, indicating the induction of the tryptophan degrading enzyme indoleamine 2,3-dioxygenase (IDO) to be responsible for the observed antiviral effect. Tryptophan 66-76 indoleamine 2,3-dioxygenase 1 Homo sapiens 138-165 16113824-6 2005 This antiviral effect was completely blocked in the presence of L-tryptophan, indicating the induction of the tryptophan degrading enzyme indoleamine 2,3-dioxygenase (IDO) to be responsible for the observed antiviral effect. Tryptophan 66-76 indoleamine 2,3-dioxygenase 1 Homo sapiens 167-170 16157293-3 2005 A growing body of evidence supports the hypothesis that specialized subsets of dendritic cells expressing indoleamine 2,3 dioxygenase (IDO), which catalyzes oxidative catabolism of tryptophan, play critical roles in regulation of T cell-mediated immune responses. Tryptophan 181-191 indoleamine 2,3-dioxygenase 1 Homo sapiens 106-133 16157293-3 2005 A growing body of evidence supports the hypothesis that specialized subsets of dendritic cells expressing indoleamine 2,3 dioxygenase (IDO), which catalyzes oxidative catabolism of tryptophan, play critical roles in regulation of T cell-mediated immune responses. Tryptophan 181-191 indoleamine 2,3-dioxygenase 1 Homo sapiens 135-138 16157293-4 2005 IDO-dependent T cell suppression by dendritic cells suggests that biochemical changes due to tryptophan catabolism have profound effects on T cell proliferation, differentiation, effector functions, and viability. Tryptophan 93-103 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 16394644-1 2005 Indoleamine 2,3-dioxygenase (IDO), one of the enzymes of tryptophan catabolism, has been shown to play an essential role for successful pregnancy through the inhibition of allogenic fetus-induced T-cell proliferation, and interferon-gamma (IFN-gamma) induces the expression of IDO in CD14-positive (CD14(+)) cells. Tryptophan 57-67 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 16394644-1 2005 Indoleamine 2,3-dioxygenase (IDO), one of the enzymes of tryptophan catabolism, has been shown to play an essential role for successful pregnancy through the inhibition of allogenic fetus-induced T-cell proliferation, and interferon-gamma (IFN-gamma) induces the expression of IDO in CD14-positive (CD14(+)) cells. Tryptophan 57-67 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 16394644-1 2005 Indoleamine 2,3-dioxygenase (IDO), one of the enzymes of tryptophan catabolism, has been shown to play an essential role for successful pregnancy through the inhibition of allogenic fetus-induced T-cell proliferation, and interferon-gamma (IFN-gamma) induces the expression of IDO in CD14-positive (CD14(+)) cells. Tryptophan 57-67 indoleamine 2,3-dioxygenase 1 Homo sapiens 277-280 16178870-2 2005 The kynurenine per tryptophan ratio (kyn/trp), which reflects the activity of the indoleamine-pyrrole 2,3-dioxygenase (IDO) enzyme involved in tryptophan catabolism, was calculated. Tryptophan 19-29 indoleamine 2,3-dioxygenase 1 Homo sapiens 119-122 16178870-2 2005 The kynurenine per tryptophan ratio (kyn/trp), which reflects the activity of the indoleamine-pyrrole 2,3-dioxygenase (IDO) enzyme involved in tryptophan catabolism, was calculated. Tryptophan 41-44 indoleamine 2,3-dioxygenase 1 Homo sapiens 119-122 16178870-2 2005 The kynurenine per tryptophan ratio (kyn/trp), which reflects the activity of the indoleamine-pyrrole 2,3-dioxygenase (IDO) enzyme involved in tryptophan catabolism, was calculated. Tryptophan 143-153 indoleamine 2,3-dioxygenase 1 Homo sapiens 82-117 16178870-2 2005 The kynurenine per tryptophan ratio (kyn/trp), which reflects the activity of the indoleamine-pyrrole 2,3-dioxygenase (IDO) enzyme involved in tryptophan catabolism, was calculated. Tryptophan 143-153 indoleamine 2,3-dioxygenase 1 Homo sapiens 119-122 16178870-6 2005 Female pSS patients with high IDO activity (kyn/trp x 1000 > or = 34.0) had significantly higher ESR, serum C-reactive protein, serum IgA and serum beta-2 microglobulin concentrations as well as higher serum creatinine levels, and they had positive antinuclear antibodies more frequently and presented with more American-European consensus group criteria than those with low IDO activity (kyn/trp x 1000 < 34.0). Tryptophan 48-51 indoleamine 2,3-dioxygenase 1 Homo sapiens 30-33 16178870-6 2005 Female pSS patients with high IDO activity (kyn/trp x 1000 > or = 34.0) had significantly higher ESR, serum C-reactive protein, serum IgA and serum beta-2 microglobulin concentrations as well as higher serum creatinine levels, and they had positive antinuclear antibodies more frequently and presented with more American-European consensus group criteria than those with low IDO activity (kyn/trp x 1000 < 34.0). Tryptophan 396-399 indoleamine 2,3-dioxygenase 1 Homo sapiens 30-33 15896467-1 2005 Tryptophan degradation by the enzyme indoleamine-(2,3)-dioxy genase (IDO) and neopterin production are induced within cellular immune activation by stimulation of monocyte-derived macrophages and dendritic cells with cytokine interferon-gamma. Tryptophan 0-10 indoleamine 2,3-dioxygenase 1 Homo sapiens 37-67 15896467-1 2005 Tryptophan degradation by the enzyme indoleamine-(2,3)-dioxy genase (IDO) and neopterin production are induced within cellular immune activation by stimulation of monocyte-derived macrophages and dendritic cells with cytokine interferon-gamma. Tryptophan 0-10 indoleamine 2,3-dioxygenase 1 Homo sapiens 69-72 15494706-0 2005 IDO and interferon-alpha-induced depressive symptoms: a shift in hypothesis from tryptophan depletion to neurotoxicity. Tryptophan 81-91 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 15919929-4 2005 The antiviral activity induced by IFN-gamma correlates with the induction of indoleamine 2,3-dioxygenase (IDO), an enzyme of the tryptophan degradation pathway known to mediate antiviral as well as antibacterial and antiparasitic effects. Tryptophan 129-139 indoleamine 2,3-dioxygenase 1 Homo sapiens 77-104 15919929-4 2005 The antiviral activity induced by IFN-gamma correlates with the induction of indoleamine 2,3-dioxygenase (IDO), an enzyme of the tryptophan degradation pathway known to mediate antiviral as well as antibacterial and antiparasitic effects. Tryptophan 129-139 indoleamine 2,3-dioxygenase 1 Homo sapiens 106-109 15919929-5 2005 The IFN-gamma-induced antiviral activity can be overcome by the addition of excess amounts of l-tryptophan, which indicates a specific role of IDO in the anti-MV activity. Tryptophan 94-106 indoleamine 2,3-dioxygenase 1 Homo sapiens 143-146 15494706-2 2005 The enzyme indoleamine 2,3-dioxygenase (IDO), which converts tryptophan (TRP) into kynurenine (KYN) and which is stimulated by proinflammatory cytokines, may be implicated in the development of IFN-alpha-induced depressive symptoms, first by decreasing the TRP availability to the brain and second by the induction of the KYN pathway resulting in the production of neurotoxic metabolites. Tryptophan 73-76 indoleamine 2,3-dioxygenase 1 Homo sapiens 40-43 15494706-2 2005 The enzyme indoleamine 2,3-dioxygenase (IDO), which converts tryptophan (TRP) into kynurenine (KYN) and which is stimulated by proinflammatory cytokines, may be implicated in the development of IFN-alpha-induced depressive symptoms, first by decreasing the TRP availability to the brain and second by the induction of the KYN pathway resulting in the production of neurotoxic metabolites. Tryptophan 257-260 indoleamine 2,3-dioxygenase 1 Homo sapiens 11-38 15494706-2 2005 The enzyme indoleamine 2,3-dioxygenase (IDO), which converts tryptophan (TRP) into kynurenine (KYN) and which is stimulated by proinflammatory cytokines, may be implicated in the development of IFN-alpha-induced depressive symptoms, first by decreasing the TRP availability to the brain and second by the induction of the KYN pathway resulting in the production of neurotoxic metabolites. Tryptophan 61-71 indoleamine 2,3-dioxygenase 1 Homo sapiens 11-38 15494706-2 2005 The enzyme indoleamine 2,3-dioxygenase (IDO), which converts tryptophan (TRP) into kynurenine (KYN) and which is stimulated by proinflammatory cytokines, may be implicated in the development of IFN-alpha-induced depressive symptoms, first by decreasing the TRP availability to the brain and second by the induction of the KYN pathway resulting in the production of neurotoxic metabolites. Tryptophan 257-260 indoleamine 2,3-dioxygenase 1 Homo sapiens 40-43 15494706-2 2005 The enzyme indoleamine 2,3-dioxygenase (IDO), which converts tryptophan (TRP) into kynurenine (KYN) and which is stimulated by proinflammatory cytokines, may be implicated in the development of IFN-alpha-induced depressive symptoms, first by decreasing the TRP availability to the brain and second by the induction of the KYN pathway resulting in the production of neurotoxic metabolites. Tryptophan 61-71 indoleamine 2,3-dioxygenase 1 Homo sapiens 40-43 15494706-2 2005 The enzyme indoleamine 2,3-dioxygenase (IDO), which converts tryptophan (TRP) into kynurenine (KYN) and which is stimulated by proinflammatory cytokines, may be implicated in the development of IFN-alpha-induced depressive symptoms, first by decreasing the TRP availability to the brain and second by the induction of the KYN pathway resulting in the production of neurotoxic metabolites. Tryptophan 73-76 indoleamine 2,3-dioxygenase 1 Homo sapiens 11-38 15762873-3 2005 Within activation of the cellular immune system, Th1-type cytokine interferon (IFN)-gamma induces enzyme indoleamine-2,3-dioxygenase (IDO) which converts tryptophan to kynurenine. Tryptophan 154-164 indoleamine 2,3-dioxygenase 1 Homo sapiens 105-132 15762873-3 2005 Within activation of the cellular immune system, Th1-type cytokine interferon (IFN)-gamma induces enzyme indoleamine-2,3-dioxygenase (IDO) which converts tryptophan to kynurenine. Tryptophan 154-164 indoleamine 2,3-dioxygenase 1 Homo sapiens 134-137 15853924-2 2005 The key enzyme is indoleamine-pyrrole 2,3-dioxygenase (EC 1.13.11.42) (IDO) which converts trp to kynurenine (kyn), the main toxic metabolite. Tryptophan 91-94 indoleamine 2,3-dioxygenase 1 Homo sapiens 18-53 15967116-1 2005 Indoleamine 2,3-dioxygenase (IDO), a catabolizing enzyme of tryptophan, is supposed to play a role in tumor immune escape. Tryptophan 60-70 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 15967116-1 2005 Indoleamine 2,3-dioxygenase (IDO), a catabolizing enzyme of tryptophan, is supposed to play a role in tumor immune escape. Tryptophan 60-70 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 15853924-2 2005 The key enzyme is indoleamine-pyrrole 2,3-dioxygenase (EC 1.13.11.42) (IDO) which converts trp to kynurenine (kyn), the main toxic metabolite. Tryptophan 91-94 indoleamine 2,3-dioxygenase 1 Homo sapiens 71-74 15466932-3 2005 A concomitant increase of TTS has been postulated to protect the IDO-expressing cells from tryptophan catabolism. Tryptophan 91-101 indoleamine 2,3-dioxygenase 1 Homo sapiens 65-68 15466932-10 2005 This is the first report of IDO and TTS regulation by the CTLA-4-B7 system in human CD4(+) and CD8(+) T cells, and raises the possibility that these 2 tryptophan-modulating enzymes provide an important mechanism for regulating immune responses. Tryptophan 151-161 indoleamine 2,3-dioxygenase 1 Homo sapiens 28-31 15684619-1 2005 Indoleamine 2,3-dioxygenase (IDO), which enzymatically depletes tryptophan, is an important antimicrobial defense mechanism against susceptible pathogens. Tryptophan 64-74 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 15684619-1 2005 Indoleamine 2,3-dioxygenase (IDO), which enzymatically depletes tryptophan, is an important antimicrobial defense mechanism against susceptible pathogens. Tryptophan 64-74 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 14624357-2 2005 We have found that the IFN-gamma-mediated activation of the tryptophan-degrading enzyme indoleamine 2,3-dioxygenase (IDO) is, at least in part, responsible for this antimicrobial activity. Tryptophan 60-70 indoleamine 2,3-dioxygenase 1 Homo sapiens 88-115 14624357-2 2005 We have found that the IFN-gamma-mediated activation of the tryptophan-degrading enzyme indoleamine 2,3-dioxygenase (IDO) is, at least in part, responsible for this antimicrobial activity. Tryptophan 60-70 indoleamine 2,3-dioxygenase 1 Homo sapiens 117-120 14624357-9 2005 The enhanced antimicrobial effect of IFN-gamma in the presence of glucocorticoids is due to the enhancement of the IDO-mediated tryptophan degradation, demonstrated by the complete abrogation of this antimicrobial effect by tryptophan resupplementation. Tryptophan 128-138 indoleamine 2,3-dioxygenase 1 Homo sapiens 115-118 14624357-9 2005 The enhanced antimicrobial effect of IFN-gamma in the presence of glucocorticoids is due to the enhancement of the IDO-mediated tryptophan degradation, demonstrated by the complete abrogation of this antimicrobial effect by tryptophan resupplementation. Tryptophan 224-234 indoleamine 2,3-dioxygenase 1 Homo sapiens 115-118 16359238-5 2005 L-tryptophan, an inhibitor of IDO, completely blocked the antiviral activity of IFN-gamma against vaccinia virus in 143B cells, an human osteosarcoma cell line, whereas N(G)-methyl-L-arginine, a NOS2 inhibitor, did not. Tryptophan 0-12 indoleamine 2,3-dioxygenase 1 Homo sapiens 30-33 15718917-0 2005 Enhanced enzymatic degradation of tryptophan by indoleamine 2,3-dioxygenase contributes to the tryptophan-deficient state seen after major trauma. Tryptophan 34-44 indoleamine 2,3-dioxygenase 1 Homo sapiens 48-75 15718917-0 2005 Enhanced enzymatic degradation of tryptophan by indoleamine 2,3-dioxygenase contributes to the tryptophan-deficient state seen after major trauma. Tryptophan 95-105 indoleamine 2,3-dioxygenase 1 Homo sapiens 48-75 15718917-4 2005 Tryptophan is enzymatically degraded by indoleamine 2,3-dioxygenase (IDO), whose activity is solely dependent on expression of interferon-gamma (IFN-gamma). Tryptophan 0-10 indoleamine 2,3-dioxygenase 1 Homo sapiens 40-67 15718917-4 2005 Tryptophan is enzymatically degraded by indoleamine 2,3-dioxygenase (IDO), whose activity is solely dependent on expression of interferon-gamma (IFN-gamma). Tryptophan 0-10 indoleamine 2,3-dioxygenase 1 Homo sapiens 69-72 15718917-5 2005 Because increased expression of IFN-gamma has been reported in trauma patients, we investigated whether enhanced IDO-mediated tryptophan degradation is associated with lymphopenia and poor outcomes after major trauma. Tryptophan 126-136 indoleamine 2,3-dioxygenase 1 Homo sapiens 113-116 15718917-12 2005 A concomitant increase in kynurenine suggests that the observed tryptophan deficiency is caused, in part, by IDO-mediated tryptophan degradation. Tryptophan 64-74 indoleamine 2,3-dioxygenase 1 Homo sapiens 109-112 15541637-6 2004 RESULTS: Levels of mRNA for IDO (indoleamine 2,3-dioxygenase) and kynureninase, enzymes constituting the tryptophan degradation pathway, were found to be upregulated in the skin lesions as compared to the uninvolved skin of patients with AD or psoriasis. Tryptophan 105-115 indoleamine 2,3-dioxygenase 1 Homo sapiens 28-31 15541637-6 2004 RESULTS: Levels of mRNA for IDO (indoleamine 2,3-dioxygenase) and kynureninase, enzymes constituting the tryptophan degradation pathway, were found to be upregulated in the skin lesions as compared to the uninvolved skin of patients with AD or psoriasis. Tryptophan 105-115 indoleamine 2,3-dioxygenase 1 Homo sapiens 33-60 15380529-2 2004 The tryptophan-metabolizing enzyme indoleamine 2,3-dioxygenase (IDO) regulates T-cell proliferation and survival. Tryptophan 4-14 indoleamine 2,3-dioxygenase 1 Homo sapiens 35-62 15528322-2 2004 Indoleamine 2,3-dioxygenase (IDO)-catalyzed conversion of tryptophan to kynurenines (KYN) regulates T cell function. Tryptophan 58-68 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 15528322-2 2004 Indoleamine 2,3-dioxygenase (IDO)-catalyzed conversion of tryptophan to kynurenines (KYN) regulates T cell function. Tryptophan 58-68 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 15380529-2 2004 The tryptophan-metabolizing enzyme indoleamine 2,3-dioxygenase (IDO) regulates T-cell proliferation and survival. Tryptophan 4-14 indoleamine 2,3-dioxygenase 1 Homo sapiens 64-67 15380529-6 2004 Upregulation of IDO is of functional significance, as we detected an increase of kynurenine and of the kynurenine/tryptophan ratio in supernatants from colonic explant cultures (CECs) of CD patients. Tryptophan 114-124 indoleamine 2,3-dioxygenase 1 Homo sapiens 16-19 15459668-0 2004 IDO expression by dendritic cells: tolerance and tryptophan catabolism. Tryptophan 49-59 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 15281097-1 2004 Indoleamine 2,3-dioxygenase (IDO) is an intracellular tryptophan-catabolizing enzyme possessing various immunosuppressive properties. Tryptophan 54-64 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 15281097-1 2004 Indoleamine 2,3-dioxygenase (IDO) is an intracellular tryptophan-catabolizing enzyme possessing various immunosuppressive properties. Tryptophan 54-64 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 15302611-2 2004 Th1-type cytokine interferon-gamma (IFN-gamma) induces neopterin production as well as tryptophan degradation via indoleamine (2,3)-dioxygenase (IDO), and quantification of these biochemical alterations allows one to monitor immune system activation. Tryptophan 87-97 indoleamine 2,3-dioxygenase 1 Homo sapiens 145-148 15358362-1 2004 The hemoprotein indoleamine 2,3-dioxygenase (IDO) is the first and rate-limiting enzyme in mammalian tryptophan metabolism. Tryptophan 101-111 indoleamine 2,3-dioxygenase 1 Homo sapiens 16-43 15358362-1 2004 The hemoprotein indoleamine 2,3-dioxygenase (IDO) is the first and rate-limiting enzyme in mammalian tryptophan metabolism. Tryptophan 101-111 indoleamine 2,3-dioxygenase 1 Homo sapiens 45-48 15302611-5 2004 The ratio of the concentration of the product of IDO, kynurenine, versus the substrate tryptophan (kyn/trp) was calculated to estimate IDO activity. Tryptophan 87-97 indoleamine 2,3-dioxygenase 1 Homo sapiens 135-138 15302611-5 2004 The ratio of the concentration of the product of IDO, kynurenine, versus the substrate tryptophan (kyn/trp) was calculated to estimate IDO activity. Tryptophan 103-106 indoleamine 2,3-dioxygenase 1 Homo sapiens 135-138 15374002-6 2004 We found that IFN-gamma induces a strong activation of the tryptophan-degrading enzyme indoleamine 2,3-dioxygenase (IDO) and in addition, that the IFN-gamma-induced IDO activity was enhanced in the presence of TNF-alpha. Tryptophan 59-69 indoleamine 2,3-dioxygenase 1 Homo sapiens 87-114 15248850-1 2004 BACKGROUND: Indoleamine 2,3-dioxygenase (IDO) is a tryptophan (TRP)-catabolizing enzyme with regulatory effects on T cells. Tryptophan 51-61 indoleamine 2,3-dioxygenase 1 Homo sapiens 12-39 15248850-1 2004 BACKGROUND: Indoleamine 2,3-dioxygenase (IDO) is a tryptophan (TRP)-catabolizing enzyme with regulatory effects on T cells. Tryptophan 51-61 indoleamine 2,3-dioxygenase 1 Homo sapiens 41-44 15248850-1 2004 BACKGROUND: Indoleamine 2,3-dioxygenase (IDO) is a tryptophan (TRP)-catabolizing enzyme with regulatory effects on T cells. Tryptophan 63-66 indoleamine 2,3-dioxygenase 1 Homo sapiens 12-39 15248850-1 2004 BACKGROUND: Indoleamine 2,3-dioxygenase (IDO) is a tryptophan (TRP)-catabolizing enzyme with regulatory effects on T cells. Tryptophan 63-66 indoleamine 2,3-dioxygenase 1 Homo sapiens 41-44 15254594-3 2004 Here we report that the administration of certain toll-like receptor (TLR) ligands, via the activation of innate immunity, induces high levels of indoleamine 2,3-dioxygenase (IDO), the rate-limiting enzyme of tryptophan catabolism in various organs. Tryptophan 209-219 indoleamine 2,3-dioxygenase 1 Homo sapiens 146-173 15254594-3 2004 Here we report that the administration of certain toll-like receptor (TLR) ligands, via the activation of innate immunity, induces high levels of indoleamine 2,3-dioxygenase (IDO), the rate-limiting enzyme of tryptophan catabolism in various organs. Tryptophan 209-219 indoleamine 2,3-dioxygenase 1 Homo sapiens 175-178 15374002-6 2004 We found that IFN-gamma induces a strong activation of the tryptophan-degrading enzyme indoleamine 2,3-dioxygenase (IDO) and in addition, that the IFN-gamma-induced IDO activity was enhanced in the presence of TNF-alpha. Tryptophan 59-69 indoleamine 2,3-dioxygenase 1 Homo sapiens 116-119 15374002-6 2004 We found that IFN-gamma induces a strong activation of the tryptophan-degrading enzyme indoleamine 2,3-dioxygenase (IDO) and in addition, that the IFN-gamma-induced IDO activity was enhanced in the presence of TNF-alpha. Tryptophan 59-69 indoleamine 2,3-dioxygenase 1 Homo sapiens 165-168 15374002-7 2004 Furthermore, we found that the induction of IDO activity is responsible for the inhibition of herpes simplex virus replication, since the presence of excess amounts of l-tryptophan abrogates the antiviral effect induced by IFN-gamma and the combination of IFN-gamma and TNF-alpha. Tryptophan 168-180 indoleamine 2,3-dioxygenase 1 Homo sapiens 44-47 15102086-6 2004 IDO-mediated damage of immune cells was restored by an addition of tryptophan and IDO inhibitor. Tryptophan 67-77 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 15001472-0 2004 Human bone marrow stromal cells inhibit allogeneic T-cell responses by indoleamine 2,3-dioxygenase-mediated tryptophan degradation. Tryptophan 108-118 indoleamine 2,3-dioxygenase 1 Homo sapiens 71-98 15001472-2 2004 Recently, expression of indoleamine 2,3-dioxygenase (IDO), which is induced by interferon-gamma (IFN-gamma) and catalyzes the conversion from tryptophan to kynurenine, has been identified as a T-cell inhibitory effector pathway in professional antigen-presenting cells. Tryptophan 142-152 indoleamine 2,3-dioxygenase 1 Homo sapiens 24-51 15001472-2 2004 Recently, expression of indoleamine 2,3-dioxygenase (IDO), which is induced by interferon-gamma (IFN-gamma) and catalyzes the conversion from tryptophan to kynurenine, has been identified as a T-cell inhibitory effector pathway in professional antigen-presenting cells. Tryptophan 142-152 indoleamine 2,3-dioxygenase 1 Homo sapiens 53-56 15001472-5 2004 Concomitantly, IDO activity resulting in tryptophan depletion and kynurenine production is detected in MSC/MLR coculture supernatants. Tryptophan 41-51 indoleamine 2,3-dioxygenase 1 Homo sapiens 15-18 15001472-6 2004 Addition of tryptophan significantly restores allogeneic T-cell proliferation, thus identifying IDO-mediated tryptophan catabolism as a novel T-cell inhibitory effector mechanism in human MSCs. Tryptophan 12-22 indoleamine 2,3-dioxygenase 1 Homo sapiens 96-99 15001472-6 2004 Addition of tryptophan significantly restores allogeneic T-cell proliferation, thus identifying IDO-mediated tryptophan catabolism as a novel T-cell inhibitory effector mechanism in human MSCs. Tryptophan 109-119 indoleamine 2,3-dioxygenase 1 Homo sapiens 96-99 15102781-1 2004 Tryptophan depletion resulting from indoleamine 2,3-dioxygenase (IDO) activity within the kynurenine pathway is one of the most prominent gamma interferon (IFN-gamma)-inducible antimicrobial effector mechanisms in human cells. Tryptophan 0-10 indoleamine 2,3-dioxygenase 1 Homo sapiens 36-63 15102781-1 2004 Tryptophan depletion resulting from indoleamine 2,3-dioxygenase (IDO) activity within the kynurenine pathway is one of the most prominent gamma interferon (IFN-gamma)-inducible antimicrobial effector mechanisms in human cells. Tryptophan 0-10 indoleamine 2,3-dioxygenase 1 Homo sapiens 65-68 15034022-1 2004 Human monocyte-derived dendritic cells (DCs) are capable of expressing the tryptophan-degrading enzyme indoleamine 2,3-dioxygenase (IDO), which allows them to suppress Ag-driven proliferation of T cells in vitro. Tryptophan 75-85 indoleamine 2,3-dioxygenase 1 Homo sapiens 103-130 15034022-1 2004 Human monocyte-derived dendritic cells (DCs) are capable of expressing the tryptophan-degrading enzyme indoleamine 2,3-dioxygenase (IDO), which allows them to suppress Ag-driven proliferation of T cells in vitro. Tryptophan 75-85 indoleamine 2,3-dioxygenase 1 Homo sapiens 132-135 14748880-1 2004 BACKGROUND: Indoleamine 2,3-dioxygenase (IDO) is a tryptophan catabolic enzyme. Tryptophan 51-61 indoleamine 2,3-dioxygenase 1 Homo sapiens 12-39 14748880-1 2004 BACKGROUND: Indoleamine 2,3-dioxygenase (IDO) is a tryptophan catabolic enzyme. Tryptophan 51-61 indoleamine 2,3-dioxygenase 1 Homo sapiens 41-44 13678429-1 2003 Interferon-gamma (IFN-gamma)-induced indoleamine 2,3-dioxygenase (IDO) activity inhibits the growth of susceptible intracellular pathogens by catalyzing the oxidative cleavage of the indole ring of L-tryptophan and depleting pools of the essential amino acid. Tryptophan 198-210 indoleamine 2,3-dioxygenase 1 Homo sapiens 37-64 14871294-1 2004 Indoleamine 2,3-dioxygenase (IDO) is a tryptophan catabolic enzyme that is widely distributed in various tissues. Tryptophan 39-49 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 14871294-1 2004 Indoleamine 2,3-dioxygenase (IDO) is a tryptophan catabolic enzyme that is widely distributed in various tissues. Tryptophan 39-49 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 14563947-3 2003 APCs that express the tryptophan-degrading enzyme indoleamine 2,3-dioxygenase (IDO) have been found to inhibit T-cell responses both in vitro and in vivo. Tryptophan 22-32 indoleamine 2,3-dioxygenase 1 Homo sapiens 50-77 14563947-3 2003 APCs that express the tryptophan-degrading enzyme indoleamine 2,3-dioxygenase (IDO) have been found to inhibit T-cell responses both in vitro and in vivo. Tryptophan 22-32 indoleamine 2,3-dioxygenase 1 Homo sapiens 79-82 12963490-3 2003 As a rate-limiting enzyme, IDO regulates tryptophan catabolism via the kynurenine pathway producing a series of metabolic precursors (some of which are neurotoxic) before complete oxidation to the essential pyridine nucleotide NAD. Tryptophan 41-51 indoleamine 2,3-dioxygenase 1 Homo sapiens 27-30 12963490-9 2003 These results support the hypothesis that one important consequence of increasing IDO activity in astroglial cells during inflammation is to maintain NAD levels through de novo synthesis from tryptophan. Tryptophan 192-202 indoleamine 2,3-dioxygenase 1 Homo sapiens 82-85 12966593-1 2003 OBJECTIVE: Activation of the enzyme indoleamine-(2,3)-dioxygenase (IDO) by interferon (IFN)-g leads to enhanced tryptophan conversion to kynurenine. Tryptophan 112-122 indoleamine 2,3-dioxygenase 1 Homo sapiens 36-65 12966593-1 2003 OBJECTIVE: Activation of the enzyme indoleamine-(2,3)-dioxygenase (IDO) by interferon (IFN)-g leads to enhanced tryptophan conversion to kynurenine. Tryptophan 112-122 indoleamine 2,3-dioxygenase 1 Homo sapiens 67-70 12950637-1 2003 Indoleamine 2,3-dioxygenase (IDO) is an intracellular tryptophan-oxidizing enzyme possessing various immunosuppressive characteristics. Tryptophan 54-64 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 12950637-1 2003 Indoleamine 2,3-dioxygenase (IDO) is an intracellular tryptophan-oxidizing enzyme possessing various immunosuppressive characteristics. Tryptophan 54-64 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 12766158-2 2003 Indoleamine 2,3-dioxgyenase (IDO) is a cytosolic heme protein which, together with the hepatic enzyme tryptophan 2,3-dioxygenase, catalyzes the first and rate-limiting step in the major pathway of tryptophan metabolism, the kynurenine pathway. Tryptophan 102-112 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 12766158-2 2003 Indoleamine 2,3-dioxgyenase (IDO) is a cytosolic heme protein which, together with the hepatic enzyme tryptophan 2,3-dioxygenase, catalyzes the first and rate-limiting step in the major pathway of tryptophan metabolism, the kynurenine pathway. Tryptophan 102-112 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 12766158-3 2003 The physiological role of IDO is not fully understood but is of great interest, because IDO is widely distributed in human tissues, can be up-regulated via cytokines such as interferon-gamma, and can thereby modulate the levels of tryptophan, which is vital for cell growth. Tryptophan 231-241 indoleamine 2,3-dioxygenase 1 Homo sapiens 26-29 12766158-3 2003 The physiological role of IDO is not fully understood but is of great interest, because IDO is widely distributed in human tissues, can be up-regulated via cytokines such as interferon-gamma, and can thereby modulate the levels of tryptophan, which is vital for cell growth. Tryptophan 231-241 indoleamine 2,3-dioxygenase 1 Homo sapiens 88-91 14719046-3 2004 In addition, the enzyme indoleamine 2,3-dioxygenase (IDO), which converts tryptophan into kynurenine, may play an important role, first, because IDO activation leads to reduced levels of tryptophan, the precursor of serotonin (5-HT), and thus to reduced central 5-HT synthesis. Tryptophan 74-84 indoleamine 2,3-dioxygenase 1 Homo sapiens 24-51 14719046-3 2004 In addition, the enzyme indoleamine 2,3-dioxygenase (IDO), which converts tryptophan into kynurenine, may play an important role, first, because IDO activation leads to reduced levels of tryptophan, the precursor of serotonin (5-HT), and thus to reduced central 5-HT synthesis. Tryptophan 74-84 indoleamine 2,3-dioxygenase 1 Homo sapiens 53-56 14719046-3 2004 In addition, the enzyme indoleamine 2,3-dioxygenase (IDO), which converts tryptophan into kynurenine, may play an important role, first, because IDO activation leads to reduced levels of tryptophan, the precursor of serotonin (5-HT), and thus to reduced central 5-HT synthesis. Tryptophan 74-84 indoleamine 2,3-dioxygenase 1 Homo sapiens 145-148 14719046-3 2004 In addition, the enzyme indoleamine 2,3-dioxygenase (IDO), which converts tryptophan into kynurenine, may play an important role, first, because IDO activation leads to reduced levels of tryptophan, the precursor of serotonin (5-HT), and thus to reduced central 5-HT synthesis. Tryptophan 187-197 indoleamine 2,3-dioxygenase 1 Homo sapiens 24-51 14719046-3 2004 In addition, the enzyme indoleamine 2,3-dioxygenase (IDO), which converts tryptophan into kynurenine, may play an important role, first, because IDO activation leads to reduced levels of tryptophan, the precursor of serotonin (5-HT), and thus to reduced central 5-HT synthesis. Tryptophan 187-197 indoleamine 2,3-dioxygenase 1 Homo sapiens 53-56 14719046-3 2004 In addition, the enzyme indoleamine 2,3-dioxygenase (IDO), which converts tryptophan into kynurenine, may play an important role, first, because IDO activation leads to reduced levels of tryptophan, the precursor of serotonin (5-HT), and thus to reduced central 5-HT synthesis. Tryptophan 187-197 indoleamine 2,3-dioxygenase 1 Homo sapiens 145-148 14592780-4 2003 Recently, pro-inflammatory cytokines have been found to have profound effects on the metabolism of brain serotonin through the enzyme indoleamine-2,3-dioxygenase (IDO) that metabolizes the tryptophan, the precursor of 5-HT to neurodegenerative quinolinate and neuroprotective kynurenate. Tryptophan 189-199 indoleamine 2,3-dioxygenase 1 Homo sapiens 134-161 14592780-4 2003 Recently, pro-inflammatory cytokines have been found to have profound effects on the metabolism of brain serotonin through the enzyme indoleamine-2,3-dioxygenase (IDO) that metabolizes the tryptophan, the precursor of 5-HT to neurodegenerative quinolinate and neuroprotective kynurenate. Tryptophan 189-199 indoleamine 2,3-dioxygenase 1 Homo sapiens 163-166 12848846-5 2003 It has recently been found that inhibition of IDO can result in the rejection of allogenic fetuses, suggesting that tryptophan breakdown is necessary for maintaining aspects of immune tolerance. Tryptophan 116-126 indoleamine 2,3-dioxygenase 1 Homo sapiens 46-49 13678429-1 2003 Interferon-gamma (IFN-gamma)-induced indoleamine 2,3-dioxygenase (IDO) activity inhibits the growth of susceptible intracellular pathogens by catalyzing the oxidative cleavage of the indole ring of L-tryptophan and depleting pools of the essential amino acid. Tryptophan 198-210 indoleamine 2,3-dioxygenase 1 Homo sapiens 66-69 12814390-2 2003 Cytokine interferon-gamma, which is released during cell-mediated immune responses, induces indoleamine (2,3)-dioxygenase (IDO), an enzyme degrading tryptophan to kynurenine. Tryptophan 149-159 indoleamine 2,3-dioxygenase 1 Homo sapiens 123-126 12883120-5 2003 RESULTS: The catabolism of tryptophan is stimulated under the influence of stress, hormones and inflammation by the induction of the enzymes tryptophan pyrrolase (in the liver) and IDO (ubiquitous). Tryptophan 27-37 indoleamine 2,3-dioxygenase 1 Homo sapiens 181-184 12711393-3 2003 Amino acid sequences clearly show that Sulculus and Turbo myoglobins evolved not from the globin gene but from the gene for indoleamine dioxygenase (IDO), a tryptophan-degrading enzyme. Tryptophan 157-167 indoleamine 2,3-dioxygenase 1 Homo sapiens 124-147 12738417-0 2003 Tolerance, DCs and tryptophan: much ado about IDO. Tryptophan 19-29 indoleamine 2,3-dioxygenase 1 Homo sapiens 46-49 12711393-3 2003 Amino acid sequences clearly show that Sulculus and Turbo myoglobins evolved not from the globin gene but from the gene for indoleamine dioxygenase (IDO), a tryptophan-degrading enzyme. Tryptophan 157-167 indoleamine 2,3-dioxygenase 1 Homo sapiens 149-152 12479977-7 2003 The data point to an involvement of cytokine-induced IDO activation in the degradation of tryptophan observed during pregnancy. Tryptophan 90-100 indoleamine 2,3-dioxygenase 1 Homo sapiens 53-56 15206713-2 2003 In this report we discuss our working model, the tryptophan depletion hypothesis, to explain links between IDO expression and inhibition of T cell responses. Tryptophan 49-59 indoleamine 2,3-dioxygenase 1 Homo sapiens 107-110 15206718-8 2003 The data point to an involvement of cytokine-induced IDO activation in the degradation of tryptophan observed during pregnancy. Tryptophan 90-100 indoleamine 2,3-dioxygenase 1 Homo sapiens 53-56 15206713-3 2003 We posit that IDO+ cells, particularly professional antigen presenting cells (APCs) promote T cell entry but block cell cycle progression due to tryptophan catabolism. Tryptophan 145-155 indoleamine 2,3-dioxygenase 1 Homo sapiens 14-17 15206720-4 2003 Taken together, these findings together with previous data on the immunosuppressive impact of tryptophan depletion suggest IDO-induced suppression of antitumoral immune response in both adenocarcinoma and squamous cell carcinoma of endometrium and cervix. Tryptophan 94-104 indoleamine 2,3-dioxygenase 1 Homo sapiens 123-126 15206741-0 2003 Age-related nuclear cataract and indoleamine 2,3-dioxygenase-initiated tryptophan metabolism in the human lens. Tryptophan 71-81 indoleamine 2,3-dioxygenase 1 Homo sapiens 33-60 15206720-5 2003 On the other hand, IDO as also known to inhibit tumor cell proliferation by tryptophan depletion. Tryptophan 76-86 indoleamine 2,3-dioxygenase 1 Homo sapiens 19-22 15206723-6 2003 By catabolizing extracellular tryptophan IDO inhibits local T cell proliferation thereby preventing placental rejection. Tryptophan 30-40 indoleamine 2,3-dioxygenase 1 Homo sapiens 41-44 15206745-1 2003 Activation of indoleamine-(2,3)-dioxygenase (IDO), an enzyme converting tryptophan to N-formyl-kynurenine, was found to be critical for induction of T-cell tolerance. Tryptophan 72-82 indoleamine 2,3-dioxygenase 1 Homo sapiens 14-43 15206745-1 2003 Activation of indoleamine-(2,3)-dioxygenase (IDO), an enzyme converting tryptophan to N-formyl-kynurenine, was found to be critical for induction of T-cell tolerance. Tryptophan 72-82 indoleamine 2,3-dioxygenase 1 Homo sapiens 45-48 12401473-3 2002 In various cells interferon-gamma induces indoleamine 2,3-dioxygenase (IDO) which degrades tryptophan via the kynurenine pathway. Tryptophan 91-101 indoleamine 2,3-dioxygenase 1 Homo sapiens 42-69 12488496-10 2002 Simultaneously, tryptophan degradation by induction of indoleamine (2,3)-dioxygenase (IDO) was tested in stimulated cells. Tryptophan 16-26 indoleamine 2,3-dioxygenase 1 Homo sapiens 86-89 12414962-2 2002 Indoleamine 2,3-dioxygenase (IDO), the first and rate-limiting enzyme in tryptophan catabolism in extrahepatic tissues, can lead to neurotoxicity through the generation of quinolinic acid and immunosuppression and can alter brain chemistry via depletion of tryptophan. Tryptophan 73-83 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 12414962-2 2002 Indoleamine 2,3-dioxygenase (IDO), the first and rate-limiting enzyme in tryptophan catabolism in extrahepatic tissues, can lead to neurotoxicity through the generation of quinolinic acid and immunosuppression and can alter brain chemistry via depletion of tryptophan. Tryptophan 73-83 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 12414962-2 2002 Indoleamine 2,3-dioxygenase (IDO), the first and rate-limiting enzyme in tryptophan catabolism in extrahepatic tissues, can lead to neurotoxicity through the generation of quinolinic acid and immunosuppression and can alter brain chemistry via depletion of tryptophan. Tryptophan 257-267 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 12414962-2 2002 Indoleamine 2,3-dioxygenase (IDO), the first and rate-limiting enzyme in tryptophan catabolism in extrahepatic tissues, can lead to neurotoxicity through the generation of quinolinic acid and immunosuppression and can alter brain chemistry via depletion of tryptophan. Tryptophan 257-267 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 12401473-3 2002 In various cells interferon-gamma induces indoleamine 2,3-dioxygenase (IDO) which degrades tryptophan via the kynurenine pathway. Tryptophan 91-101 indoleamine 2,3-dioxygenase 1 Homo sapiens 71-74 11934353-1 2002 BACKGROUND: Xanthurenic acid is an endogenous product of tryptophan degradation by indoleamine 2,3-dioxygenase (IDO). Tryptophan 57-67 indoleamine 2,3-dioxygenase 1 Homo sapiens 83-110 11912287-10 2002 IDO is secreted, as determined by analysis of cervical mucus by high pressure liquid chromatography for the presence of the tryptophan metabolite L-kynurenine, indicating IDO activity. Tryptophan 124-134 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 12186837-0 2002 Inhibition of allogeneic T cell proliferation by indoleamine 2,3-dioxygenase-expressing dendritic cells: mediation of suppression by tryptophan metabolites. Tryptophan 133-143 indoleamine 2,3-dioxygenase 1 Homo sapiens 49-76 12186837-1 2002 Indoleamine 2,3-dioxygenase (IDO), an enzyme involved in the catabolism of tryptophan, is expressed in certain cells and tissues, particularly in antigen-presenting cells of lymphoid organs and in the placenta. Tryptophan 75-85 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 12186837-1 2002 Indoleamine 2,3-dioxygenase (IDO), an enzyme involved in the catabolism of tryptophan, is expressed in certain cells and tissues, particularly in antigen-presenting cells of lymphoid organs and in the placenta. Tryptophan 75-85 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 12186837-3 2002 Degradation of tryptophan, an essential amino acid required for cell proliferation, was reported to be the mechanism of IDO-induced T cell suppression. Tryptophan 15-25 indoleamine 2,3-dioxygenase 1 Homo sapiens 120-123 12186838-0 2002 Tryptophan-derived catabolites are responsible for inhibition of T and natural killer cell proliferation induced by indoleamine 2,3-dioxygenase. Tryptophan 0-10 indoleamine 2,3-dioxygenase 1 Homo sapiens 116-143 12186838-1 2002 Macrophages exposed to macrophage colony-stimulating factor acquire the capacity to suppress T cell proliferation; this effect is associated with de novo expression of the tryptophan-catabolizing enzyme indoleamine 2,3-dioxygenase (IDO). Tryptophan 172-182 indoleamine 2,3-dioxygenase 1 Homo sapiens 203-230 12186838-1 2002 Macrophages exposed to macrophage colony-stimulating factor acquire the capacity to suppress T cell proliferation; this effect is associated with de novo expression of the tryptophan-catabolizing enzyme indoleamine 2,3-dioxygenase (IDO). Tryptophan 172-182 indoleamine 2,3-dioxygenase 1 Homo sapiens 232-235 12186838-8 2002 Inhibition of cell proliferation induced by the tryptophan catabolites resulting from IDO activity was selective, applying only to cells undergoing activation. Tryptophan 48-58 indoleamine 2,3-dioxygenase 1 Homo sapiens 86-89 12186838-10 2002 We suggest that IDO exerts its effect on cell proliferation by (i) starting the cascade of biochemical reactions that produce the three catabolites and by (ii) enhancing their inhibitory potential by depriving the extracellular microenvironment of tryptophan. Tryptophan 248-258 indoleamine 2,3-dioxygenase 1 Homo sapiens 16-19 11867636-10 2002 Using CO as a structural probe for the distal environment of Fe(2+) hIDO revealed that binding of L-Trp in the distal pocket converted IDO to a peroxidase-like enzyme. Tryptophan 98-103 indoleamine 2,3-dioxygenase 1 Homo sapiens 69-72 11934353-1 2002 BACKGROUND: Xanthurenic acid is an endogenous product of tryptophan degradation by indoleamine 2,3-dioxygenase (IDO). Tryptophan 57-67 indoleamine 2,3-dioxygenase 1 Homo sapiens 112-115 11985668-3 2002 This immuno-inhibitory phenotype was further shown to result from induction of the tryptophan-catabolizing enzyme, indoleamine 2,3-dioxygenase (IDO), by interferon-gamma (IFN-gamma) secreted from cocultured allo-reactive PBL. Tryptophan 83-93 indoleamine 2,3-dioxygenase 1 Homo sapiens 115-142 11985668-3 2002 This immuno-inhibitory phenotype was further shown to result from induction of the tryptophan-catabolizing enzyme, indoleamine 2,3-dioxygenase (IDO), by interferon-gamma (IFN-gamma) secreted from cocultured allo-reactive PBL. Tryptophan 83-93 indoleamine 2,3-dioxygenase 1 Homo sapiens 144-147 11375052-1 2001 BACKGROUND: The tryptophan catabolizing enzyme, indoleamine 2,3, dioxygenase (IDO) is one of two mammalian enzymes, which can catabolize the rarest essential amino acid, tryptophan. Tryptophan 16-26 indoleamine 2,3-dioxygenase 1 Homo sapiens 48-76 11440641-1 2001 Indoleamine 2,3-dioxygenase (IDO) is the rate-limiting enzyme in the catabolism of tryptophan. Tryptophan 83-93 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 11440641-1 2001 Indoleamine 2,3-dioxygenase (IDO) is the rate-limiting enzyme in the catabolism of tryptophan. Tryptophan 83-93 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 11440641-2 2001 By creating a local microenvironment in which levels of tryptophan are low, IDO-expressing antigen-presenting cells (APC) could regulate T cell activation. Tryptophan 56-66 indoleamine 2,3-dioxygenase 1 Homo sapiens 76-79 11375052-1 2001 BACKGROUND: The tryptophan catabolizing enzyme, indoleamine 2,3, dioxygenase (IDO) is one of two mammalian enzymes, which can catabolize the rarest essential amino acid, tryptophan. Tryptophan 16-26 indoleamine 2,3-dioxygenase 1 Homo sapiens 78-81 11375052-1 2001 BACKGROUND: The tryptophan catabolizing enzyme, indoleamine 2,3, dioxygenase (IDO) is one of two mammalian enzymes, which can catabolize the rarest essential amino acid, tryptophan. Tryptophan 170-180 indoleamine 2,3-dioxygenase 1 Homo sapiens 48-76 11375052-1 2001 BACKGROUND: The tryptophan catabolizing enzyme, indoleamine 2,3, dioxygenase (IDO) is one of two mammalian enzymes, which can catabolize the rarest essential amino acid, tryptophan. Tryptophan 170-180 indoleamine 2,3-dioxygenase 1 Homo sapiens 78-81 11465083-1 2000 Tryptophan is a constituent of proteins and in parallel it represents a source for mainly two pivotal biochemical pathways: the generation of 5-hydroxytryptamine (serotonin), and the formation of kynurenine by the enzymes tryptophan pyrrolase (TP) and indoleamine 2,3-dioxygenase (IDO). Tryptophan 0-10 indoleamine 2,3-dioxygenase 1 Homo sapiens 252-279 11465083-1 2000 Tryptophan is a constituent of proteins and in parallel it represents a source for mainly two pivotal biochemical pathways: the generation of 5-hydroxytryptamine (serotonin), and the formation of kynurenine by the enzymes tryptophan pyrrolase (TP) and indoleamine 2,3-dioxygenase (IDO). Tryptophan 0-10 indoleamine 2,3-dioxygenase 1 Homo sapiens 281-284 9731757-0 1998 Modulation of cellular tryptophan metabolism in human fibroblasts by transforming growth factor-beta: selective inhibition of indoleamine 2,3-dioxygenase and tryptophanyl-tRNA synthetase gene expression. Tryptophan 23-33 indoleamine 2,3-dioxygenase 1 Homo sapiens 126-153 10834318-3 2000 IFN-gamma stimulates the enzyme indoleamine (2,3)-dioxygenase (IDO) converting tryptophan to the metabolite kynurenine which in macrophages is subsequently degraded to other, partly neurotoxic compounds like quinolinic acid, and finally to nicrotinamides. Tryptophan 79-89 indoleamine 2,3-dioxygenase 1 Homo sapiens 63-66 10725715-2 2000 Production of indoleamine 2, 3-dioxygenase (IDO) by macrophages has recently been described to result in inhibition of T cell proliferation through tryptophan degradation. Tryptophan 148-158 indoleamine 2,3-dioxygenase 1 Homo sapiens 14-42 10725715-2 2000 Production of indoleamine 2, 3-dioxygenase (IDO) by macrophages has recently been described to result in inhibition of T cell proliferation through tryptophan degradation. Tryptophan 148-158 indoleamine 2,3-dioxygenase 1 Homo sapiens 44-47 10725715-5 2000 IDO produced from activated DCs was functionally active and capable of metabolizing tryptophan to kynurenine. Tryptophan 84-94 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 10725715-8 2000 These results suggest that activation of DCs induces the production of functional IDO, which causes depletion of tryptophan and subsequent inhibition of T cell proliferation. Tryptophan 113-123 indoleamine 2,3-dioxygenase 1 Homo sapiens 82-85 10805371-4 2000 Furthermore, excess tryptophan reversed the effect of combined cytokine treatment, indicating that IDO alone was responsible for chlamydial inhibition. Tryptophan 20-30 indoleamine 2,3-dioxygenase 1 Homo sapiens 99-102 10540337-5 1999 Here we describe experiments in which the L-tryptophan analog, 6-chloro-DL-tryptophan (CDLT) caused a dose-dependent inhibition in the IFN-gamma-induced IDO-mediated L-tryptophan degradation in monocyte-derived macrophages and glioblastoma cells. Tryptophan 42-54 indoleamine 2,3-dioxygenase 1 Homo sapiens 153-156 10540337-5 1999 Here we describe experiments in which the L-tryptophan analog, 6-chloro-DL-tryptophan (CDLT) caused a dose-dependent inhibition in the IFN-gamma-induced IDO-mediated L-tryptophan degradation in monocyte-derived macrophages and glioblastoma cells. Tryptophan 73-85 indoleamine 2,3-dioxygenase 1 Homo sapiens 153-156 10500295-1 1999 Some macrophages inhibit microbial infections by producing indoleamine 2,3 dioxygenase (IDO), which catabolizes tryptophan. Tryptophan 112-122 indoleamine 2,3-dioxygenase 1 Homo sapiens 59-86 10500295-1 1999 Some macrophages inhibit microbial infections by producing indoleamine 2,3 dioxygenase (IDO), which catabolizes tryptophan. Tryptophan 112-122 indoleamine 2,3-dioxygenase 1 Homo sapiens 88-91 10510970-4 1999 This study describes the IFN-gamma-induced expression of IDO -- shown at a transcriptional level by Northern blot analysis, at translational level by Western blot and also at a functional level by L-tryptophan degradation to L-kynurenine -- in the uro-epithelial cell line RT4. Tryptophan 197-209 indoleamine 2,3-dioxygenase 1 Homo sapiens 57-60 10206145-2 1999 In contrast the induction of the tryptophan degrading enzyme indolamine 2,3-dioxygenase (IDO) has been described to be the most effective anti-parasitic mechanism in most human cells. Tryptophan 33-43 indoleamine 2,3-dioxygenase 1 Homo sapiens 61-87 10206145-2 1999 In contrast the induction of the tryptophan degrading enzyme indolamine 2,3-dioxygenase (IDO) has been described to be the most effective anti-parasitic mechanism in most human cells. Tryptophan 33-43 indoleamine 2,3-dioxygenase 1 Homo sapiens 89-92 10206145-5 1999 This was due to an activation of IDO, and the anti-parasitic effect mediated by RT4 cells was abrogated by the addition of L-tryptophan. Tryptophan 123-135 indoleamine 2,3-dioxygenase 1 Homo sapiens 33-36 9916720-3 1999 Inhibition by IFN-gamma, and to a lesser extent IFN-beta, was almost completely reversed by addition of L-tryptophan to the culture medium, strongly implicating the indoleamine 2,3 dioxygenase (IDO) pathway. Tryptophan 104-116 indoleamine 2,3-dioxygenase 1 Homo sapiens 165-192 9916720-3 1999 Inhibition by IFN-gamma, and to a lesser extent IFN-beta, was almost completely reversed by addition of L-tryptophan to the culture medium, strongly implicating the indoleamine 2,3 dioxygenase (IDO) pathway. Tryptophan 104-116 indoleamine 2,3-dioxygenase 1 Homo sapiens 194-197 10821443-2 2000 During immune response, interferon-gamma stimulates indoleamine 2,3-dioxygenase (IDO) converting tryptophan to N-formylkynurenine followed by kynurenine in an ensuing step. Tryptophan 97-107 indoleamine 2,3-dioxygenase 1 Homo sapiens 52-79 10821443-2 2000 During immune response, interferon-gamma stimulates indoleamine 2,3-dioxygenase (IDO) converting tryptophan to N-formylkynurenine followed by kynurenine in an ensuing step. Tryptophan 97-107 indoleamine 2,3-dioxygenase 1 Homo sapiens 81-84 10821443-3 2000 Thus, IDO activity is estimated by the kynurenine per tryptophan quotient (Kyn/Trp). Tryptophan 54-64 indoleamine 2,3-dioxygenase 1 Homo sapiens 6-9 10821443-3 2000 Thus, IDO activity is estimated by the kynurenine per tryptophan quotient (Kyn/Trp). Tryptophan 79-82 indoleamine 2,3-dioxygenase 1 Homo sapiens 6-9 10721097-1 1999 Stimulation of human monocyte-derived-macrophages (MDM) with interferon gamma induces the L-tryptophan degrading enzyme indoleamine 2,3-dioxygenase (IDO). Tryptophan 90-102 indoleamine 2,3-dioxygenase 1 Homo sapiens 120-147 10721097-1 1999 Stimulation of human monocyte-derived-macrophages (MDM) with interferon gamma induces the L-tryptophan degrading enzyme indoleamine 2,3-dioxygenase (IDO). Tryptophan 90-102 indoleamine 2,3-dioxygenase 1 Homo sapiens 149-152 10721097-2 1999 It has been well documented that the growth of some intra-cellular parasites such as Chlamydia and Toxoplasma in human fibroblasts and glioblastoma cells is inhibited by IDO mediated L-tryptophan depletion. Tryptophan 183-195 indoleamine 2,3-dioxygenase 1 Homo sapiens 170-173 10721098-4 1999 Indoleamine 2,3-dioxygenase activity (IDO) is the initial and rate limiting enzyme of Trp degradation along the kynurenine pathway. Tryptophan 86-89 indoleamine 2,3-dioxygenase 1 Homo sapiens 38-41 10721101-5 1999 In addition, IDO activity seems to be related with the decrease in Trp, as demonstrated by the inverse correlation found between these two substances in the SF of all patients. Tryptophan 67-70 indoleamine 2,3-dioxygenase 1 Homo sapiens 13-16 10786059-2 1999 The role of indoleamine 2.3-dioxygenase (IDO)--the first enzyme of the tryptophan degradation--is also described. Tryptophan 71-81 indoleamine 2,3-dioxygenase 1 Homo sapiens 12-39 10786059-2 1999 The role of indoleamine 2.3-dioxygenase (IDO)--the first enzyme of the tryptophan degradation--is also described. Tryptophan 71-81 indoleamine 2,3-dioxygenase 1 Homo sapiens 41-44 10731095-1 1999 The heme enzyme indoleamine 2,3-dioxygenase (IDO) oxidizes the pyrrole moiety of L-tryptophan (Trp) and other indoleamines and represents the initial and rate-limiting enzyme of the kynurenine (Kyn) pathway. Tryptophan 81-93 indoleamine 2,3-dioxygenase 1 Homo sapiens 16-43 10731095-1 1999 The heme enzyme indoleamine 2,3-dioxygenase (IDO) oxidizes the pyrrole moiety of L-tryptophan (Trp) and other indoleamines and represents the initial and rate-limiting enzyme of the kynurenine (Kyn) pathway. Tryptophan 81-93 indoleamine 2,3-dioxygenase 1 Homo sapiens 45-48 10731095-1 1999 The heme enzyme indoleamine 2,3-dioxygenase (IDO) oxidizes the pyrrole moiety of L-tryptophan (Trp) and other indoleamines and represents the initial and rate-limiting enzyme of the kynurenine (Kyn) pathway. Tryptophan 95-98 indoleamine 2,3-dioxygenase 1 Homo sapiens 16-43 10731095-1 1999 The heme enzyme indoleamine 2,3-dioxygenase (IDO) oxidizes the pyrrole moiety of L-tryptophan (Trp) and other indoleamines and represents the initial and rate-limiting enzyme of the kynurenine (Kyn) pathway. Tryptophan 95-98 indoleamine 2,3-dioxygenase 1 Homo sapiens 45-48 10731095-5 1999 Induction of IDO and metabolism of Trp along the Kyn pathway is implicated in a variety of physiological and pathophysiological processes, including anti-microbial and anti-tumor defense, neuropathology, immunoregulation and antioxidant activity. Tryptophan 35-38 indoleamine 2,3-dioxygenase 1 Homo sapiens 13-16 7537250-1 1995 One mechanism by which interferons (IFNs) can inhibit chlamydial infection is by the induction of the enzyme indoleamine 2,3-dioxygenase (IDO), which restricts the availability of tryptophan, which is required for chlamydial growth. Tryptophan 180-190 indoleamine 2,3-dioxygenase 1 Homo sapiens 138-141 9879957-6 1998 The activity of the tryptophan-degrading enzyme indoleamine 2,3-dioxygenase (IDO) was not detected in untreated or in IFN-gamma-treated or chlamydiae-infected or mock-infected U937 cells. Tryptophan 20-30 indoleamine 2,3-dioxygenase 1 Homo sapiens 48-75 9879957-6 1998 The activity of the tryptophan-degrading enzyme indoleamine 2,3-dioxygenase (IDO) was not detected in untreated or in IFN-gamma-treated or chlamydiae-infected or mock-infected U937 cells. Tryptophan 20-30 indoleamine 2,3-dioxygenase 1 Homo sapiens 77-80 9284972-4 1997 IFN-gamma induces a high level of indoleamine dioxygenase (IDO), a tryptophan degrading enzyme, and high cortisol levels induce high tryptophan oxygenase activity, which in turn increases metabolism along the tryptophan-nicotinic acid pathway. Tryptophan 67-77 indoleamine 2,3-dioxygenase 1 Homo sapiens 34-57 9284972-4 1997 IFN-gamma induces a high level of indoleamine dioxygenase (IDO), a tryptophan degrading enzyme, and high cortisol levels induce high tryptophan oxygenase activity, which in turn increases metabolism along the tryptophan-nicotinic acid pathway. Tryptophan 67-77 indoleamine 2,3-dioxygenase 1 Homo sapiens 59-62 9284972-4 1997 IFN-gamma induces a high level of indoleamine dioxygenase (IDO), a tryptophan degrading enzyme, and high cortisol levels induce high tryptophan oxygenase activity, which in turn increases metabolism along the tryptophan-nicotinic acid pathway. Tryptophan 133-143 indoleamine 2,3-dioxygenase 1 Homo sapiens 34-57 9032125-6 1997 In responsive HMCLs, r-hu-IFN-gamma induced strong indoleamine-2,3-dioxygenase (IDO) activity, which causes rapid degradation of tryptophan; however, the correlation between r-hu-IFN-gamma-mediated growth arrest and IDO induction was not absolute. Tryptophan 129-139 indoleamine 2,3-dioxygenase 1 Homo sapiens 51-78 9032125-6 1997 In responsive HMCLs, r-hu-IFN-gamma induced strong indoleamine-2,3-dioxygenase (IDO) activity, which causes rapid degradation of tryptophan; however, the correlation between r-hu-IFN-gamma-mediated growth arrest and IDO induction was not absolute. Tryptophan 129-139 indoleamine 2,3-dioxygenase 1 Homo sapiens 80-83 8765749-5 1996 The cDNA-derived amino acid sequence showed no significant homology with those of any other invertebrate myoglobins and hemoglobins, but surprisingly showed 35% homology with a vertebrate tryptophan-degrading enzyme, indoleamine dioxygenase (IDO). Tryptophan 188-198 indoleamine 2,3-dioxygenase 1 Homo sapiens 217-240 8817290-1 1996 BACKGROUND: Indoleamine 2,3-dioxygenase (IDO) is the first enzyme of the tryptophan degradation pathway. Tryptophan 73-83 indoleamine 2,3-dioxygenase 1 Homo sapiens 12-39 8817290-1 1996 BACKGROUND: Indoleamine 2,3-dioxygenase (IDO) is the first enzyme of the tryptophan degradation pathway. Tryptophan 73-83 indoleamine 2,3-dioxygenase 1 Homo sapiens 41-44 8906279-6 1996 We therefore tentatively conclude that tryptophan is degraded by IDO and depleted, whereby the growth of viruses, bacteria and certain parasites is inhibited, because tryptophan is the least available and therefore most important essential amino acid for their growth. Tryptophan 39-49 indoleamine 2,3-dioxygenase 1 Homo sapiens 65-68 8906279-6 1996 We therefore tentatively conclude that tryptophan is degraded by IDO and depleted, whereby the growth of viruses, bacteria and certain parasites is inhibited, because tryptophan is the least available and therefore most important essential amino acid for their growth. Tryptophan 167-177 indoleamine 2,3-dioxygenase 1 Homo sapiens 65-68 7490512-1 1995 Induction of indoleamine 2,3-dioxygenase (IDO), an enzyme expressed by mononuclear phagocytes and some fibroblast cell lines in response to interferon-gamma, leads to enhanced degradation of tryptophan to kynurenine. Tryptophan 191-201 indoleamine 2,3-dioxygenase 1 Homo sapiens 13-40 7490512-1 1995 Induction of indoleamine 2,3-dioxygenase (IDO), an enzyme expressed by mononuclear phagocytes and some fibroblast cell lines in response to interferon-gamma, leads to enhanced degradation of tryptophan to kynurenine. Tryptophan 191-201 indoleamine 2,3-dioxygenase 1 Homo sapiens 42-45 7665918-2 1995 In addition, IFN-gamma also exerts potent effects on cellular tryptophan levels by inducing the expression of indoleamine 2,3-dioxygenase (IDO) and tryptophanyl-tRNA synthetase. Tryptophan 62-72 indoleamine 2,3-dioxygenase 1 Homo sapiens 110-137 7665918-2 1995 In addition, IFN-gamma also exerts potent effects on cellular tryptophan levels by inducing the expression of indoleamine 2,3-dioxygenase (IDO) and tryptophanyl-tRNA synthetase. Tryptophan 62-72 indoleamine 2,3-dioxygenase 1 Homo sapiens 139-142 7665918-3 1995 Because recent evidence indicates that IDO-mediated oxidative tryptophan catabolism is important in cellular responses to IFN-gamma, we investigated the role of IDO in the IFN-gamma-induced modulation of type I collagen gene expression. Tryptophan 62-72 indoleamine 2,3-dioxygenase 1 Homo sapiens 39-42 7665918-4 1995 IFN-gamma ( > or = 50 U/ml) stimulated IDO expression in human dermal fibroblasts in vitro, resulting in a > 90% depletion of tryptophan in the culture media following incubation for 48 h. Higher concentrations of IFN-gamma ( > or = 500 U/ml) caused a marked decrease in type I collagen mRNA levels. Tryptophan 132-142 indoleamine 2,3-dioxygenase 1 Homo sapiens 42-45 7615820-5 1995 In addition, incubation of fibroblasts with IFN-gamma resulted in a marked increase in cellular indoleamine 2,3-dioxygenase (IDO) mRNA, a > 90% depletion of tryptophan, and a corresponding > 30-fold increase in the tryptophan metabolite kynurenine in the culture media. Tryptophan 160-170 indoleamine 2,3-dioxygenase 1 Homo sapiens 125-128 7615820-5 1995 In addition, incubation of fibroblasts with IFN-gamma resulted in a marked increase in cellular indoleamine 2,3-dioxygenase (IDO) mRNA, a > 90% depletion of tryptophan, and a corresponding > 30-fold increase in the tryptophan metabolite kynurenine in the culture media. Tryptophan 221-231 indoleamine 2,3-dioxygenase 1 Homo sapiens 125-128 7537250-7 1995 The addition of exogenous tryptophan reversed the effect of combined IFN and IL-1 treatment, indicating that IDO activity induced by combined cytokine treatment was responsible for chlamydial inhibition. Tryptophan 26-36 indoleamine 2,3-dioxygenase 1 Homo sapiens 109-112 7720088-1 1995 The tryptophan decyclizing enzyme indoleamine 2,3-dioxygenase (IDO) was induced in human monocyte-derived macrophages (MDM) treated with human recombinant interferon-beta (IFN-beta) or interferon-gamma (IFN-gamma). Tryptophan 4-14 indoleamine 2,3-dioxygenase 1 Homo sapiens 34-61 7542758-3 1995 The structure of 7-NI resembles that of tryptophan which can be metabolized by the enzyme indolamine 2,3-dioxygenase (IDO). Tryptophan 40-50 indoleamine 2,3-dioxygenase 1 Homo sapiens 90-116 7542758-3 1995 The structure of 7-NI resembles that of tryptophan which can be metabolized by the enzyme indolamine 2,3-dioxygenase (IDO). Tryptophan 40-50 indoleamine 2,3-dioxygenase 1 Homo sapiens 118-121 7790043-4 1995 The negative correlation of NPT and Trp concentrations indicates activity of indoleamine 2,3-dioxygenase (IDO), a Trp degradating enzyme, in cancer-burden patients. Tryptophan 36-39 indoleamine 2,3-dioxygenase 1 Homo sapiens 77-104 7790043-4 1995 The negative correlation of NPT and Trp concentrations indicates activity of indoleamine 2,3-dioxygenase (IDO), a Trp degradating enzyme, in cancer-burden patients. Tryptophan 36-39 indoleamine 2,3-dioxygenase 1 Homo sapiens 106-109 7790043-4 1995 The negative correlation of NPT and Trp concentrations indicates activity of indoleamine 2,3-dioxygenase (IDO), a Trp degradating enzyme, in cancer-burden patients. Tryptophan 114-117 indoleamine 2,3-dioxygenase 1 Homo sapiens 77-104 7790043-4 1995 The negative correlation of NPT and Trp concentrations indicates activity of indoleamine 2,3-dioxygenase (IDO), a Trp degradating enzyme, in cancer-burden patients. Tryptophan 114-117 indoleamine 2,3-dioxygenase 1 Homo sapiens 106-109 7790043-5 1995 The activity of IDO can be induced by cytokines such as IFN-gamma, and therefore low Trp levels may result from endogenous IFN-gamma production due to immune activation against tumors. Tryptophan 85-88 indoleamine 2,3-dioxygenase 1 Homo sapiens 16-19 7720088-1 1995 The tryptophan decyclizing enzyme indoleamine 2,3-dioxygenase (IDO) was induced in human monocyte-derived macrophages (MDM) treated with human recombinant interferon-beta (IFN-beta) or interferon-gamma (IFN-gamma). Tryptophan 4-14 indoleamine 2,3-dioxygenase 1 Homo sapiens 63-66 7814143-6 1995 These results show that induction of IDO by IFN-gamma in vivo can metabolize L-tryptophan rapidly enough for it to become depleted, despite a continued supply of L-tryptophan from the host. Tryptophan 77-89 indoleamine 2,3-dioxygenase 1 Homo sapiens 37-40 7814143-6 1995 These results show that induction of IDO by IFN-gamma in vivo can metabolize L-tryptophan rapidly enough for it to become depleted, despite a continued supply of L-tryptophan from the host. Tryptophan 162-174 indoleamine 2,3-dioxygenase 1 Homo sapiens 37-40 7814143-7 1995 The IDO mRNA and protein remained induced after the L-tryptophan levels had returned to normal, suggesting that the gene may be post-transcriptionally regulated and/or the IDO co-factor supply may be limited. Tryptophan 52-64 indoleamine 2,3-dioxygenase 1 Homo sapiens 4-7 8118042-1 1994 Indoleamine 2,3-dioxygenase (IDO), a flavin-dependent enzyme that catalyzes the conversion of tryptophan to kynurenine, is induced in peripheral blood mononuclear cells by interferon-gamma (IFN gamma). Tryptophan 94-104 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 7897249-3 1994 Destruction of L-tryptophan is due to an increased activity of indoleamine 2,3-dioxygenase (IDO), which is transcriptionally activated by IFN-gamma. Tryptophan 15-27 indoleamine 2,3-dioxygenase 1 Homo sapiens 92-95 7523670-2 1994 Interferon gamma (IFN-gamma) has antitumor cell activity related to stimulation of 2,3 indoleamine dioxygenase (IDO), a widely distributed tryptophan catabolizing enzyme. Tryptophan 139-149 indoleamine 2,3-dioxygenase 1 Homo sapiens 112-115 8118042-1 1994 Indoleamine 2,3-dioxygenase (IDO), a flavin-dependent enzyme that catalyzes the conversion of tryptophan to kynurenine, is induced in peripheral blood mononuclear cells by interferon-gamma (IFN gamma). Tryptophan 94-104 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 8288893-1 1994 IFN-gamma induces the production of N-formyl-kynurenine from L-tryptophan in various cell types by the induction of the enzyme indoleamine 2,3-dioxygenase (IDO). Tryptophan 61-73 indoleamine 2,3-dioxygenase 1 Homo sapiens 156-159 1591013-2 1992 Indoleamine 2,3-dioxygenase (IDO), an inducible cellular enzyme, metabolizes tryptophan to N-formyl-L-kynurenine. Tryptophan 77-87 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 8293279-3 1993 These increases were attributed to the induction of indoleamine-2,3-dioxygenase (IDO), the enzyme that converts L-tryptophan into L-KYN. Tryptophan 112-124 indoleamine 2,3-dioxygenase 1 Homo sapiens 52-79 8293279-3 1993 These increases were attributed to the induction of indoleamine-2,3-dioxygenase (IDO), the enzyme that converts L-tryptophan into L-KYN. Tryptophan 112-124 indoleamine 2,3-dioxygenase 1 Homo sapiens 81-84 1591013-2 1992 Indoleamine 2,3-dioxygenase (IDO), an inducible cellular enzyme, metabolizes tryptophan to N-formyl-L-kynurenine. Tryptophan 77-87 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 1917395-2 1991 The treatment resulted in the induction of the tryptophan decyclizing enzyme indolamine 2,3-deoxygenase (IDO) in a dose-dependent manner as determined by assaying the conversion of tryptophan to its metabolites using reversed-phase high-performance liquid chromatography. Tryptophan 47-57 indoleamine 2,3-dioxygenase 1 Homo sapiens 77-103 1532618-7 1992 Our data suggest that indoleamine-2,3-dioxygenase (IDO), the rate limiting enzyme of the kynurenine pathway of L-tryptophan metabolism, was activated in both syndromes by cytokines including IFN-gamma, and that perhaps products of tryptophan metabolism played a role in the pathogenesis of EMS and TOS. Tryptophan 111-123 indoleamine 2,3-dioxygenase 1 Homo sapiens 22-49 1532618-7 1992 Our data suggest that indoleamine-2,3-dioxygenase (IDO), the rate limiting enzyme of the kynurenine pathway of L-tryptophan metabolism, was activated in both syndromes by cytokines including IFN-gamma, and that perhaps products of tryptophan metabolism played a role in the pathogenesis of EMS and TOS. Tryptophan 111-123 indoleamine 2,3-dioxygenase 1 Homo sapiens 51-54 1532618-7 1992 Our data suggest that indoleamine-2,3-dioxygenase (IDO), the rate limiting enzyme of the kynurenine pathway of L-tryptophan metabolism, was activated in both syndromes by cytokines including IFN-gamma, and that perhaps products of tryptophan metabolism played a role in the pathogenesis of EMS and TOS. Tryptophan 113-123 indoleamine 2,3-dioxygenase 1 Homo sapiens 22-49 1532618-7 1992 Our data suggest that indoleamine-2,3-dioxygenase (IDO), the rate limiting enzyme of the kynurenine pathway of L-tryptophan metabolism, was activated in both syndromes by cytokines including IFN-gamma, and that perhaps products of tryptophan metabolism played a role in the pathogenesis of EMS and TOS. Tryptophan 113-123 indoleamine 2,3-dioxygenase 1 Homo sapiens 51-54 1917395-2 1991 The treatment resulted in the induction of the tryptophan decyclizing enzyme indolamine 2,3-deoxygenase (IDO) in a dose-dependent manner as determined by assaying the conversion of tryptophan to its metabolites using reversed-phase high-performance liquid chromatography. Tryptophan 47-57 indoleamine 2,3-dioxygenase 1 Homo sapiens 105-108 1917395-2 1991 The treatment resulted in the induction of the tryptophan decyclizing enzyme indolamine 2,3-deoxygenase (IDO) in a dose-dependent manner as determined by assaying the conversion of tryptophan to its metabolites using reversed-phase high-performance liquid chromatography. Tryptophan 181-191 indoleamine 2,3-dioxygenase 1 Homo sapiens 77-103 1917395-2 1991 The treatment resulted in the induction of the tryptophan decyclizing enzyme indolamine 2,3-deoxygenase (IDO) in a dose-dependent manner as determined by assaying the conversion of tryptophan to its metabolites using reversed-phase high-performance liquid chromatography. Tryptophan 181-191 indoleamine 2,3-dioxygenase 1 Homo sapiens 105-108 1917395-6 1991 Reversal by the addition of exogenous tryptophan substantiated that IFN-gamma-mediated induction of IDO and catabolism of tryptophan were responsible for inhibition of intracellular growth of C. trachomatis. Tryptophan 38-48 indoleamine 2,3-dioxygenase 1 Homo sapiens 100-103 1722946-2 1991 Indoleamine 2,3-dioxygenase (IDO) is induced by infections, viruses, lipopolysaccharides, or interferons (IFNs) and this results in significant catabolism of Trp along the kynurenine (Kyn) pathway. Tryptophan 158-161 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 1907934-3 1991 In particular, interferon-gamma (IFN-gamma) induces an enzyme of tryptophan catabolism, indoleamine 2,3-dioxygenase (IDO), which is responsible for conversion of tryptophan and other indole derivatives to kynurenine. Tryptophan 65-75 indoleamine 2,3-dioxygenase 1 Homo sapiens 88-115 1907934-3 1991 In particular, interferon-gamma (IFN-gamma) induces an enzyme of tryptophan catabolism, indoleamine 2,3-dioxygenase (IDO), which is responsible for conversion of tryptophan and other indole derivatives to kynurenine. Tryptophan 65-75 indoleamine 2,3-dioxygenase 1 Homo sapiens 117-120 1907934-3 1991 In particular, interferon-gamma (IFN-gamma) induces an enzyme of tryptophan catabolism, indoleamine 2,3-dioxygenase (IDO), which is responsible for conversion of tryptophan and other indole derivatives to kynurenine. Tryptophan 162-172 indoleamine 2,3-dioxygenase 1 Homo sapiens 88-115 1907934-3 1991 In particular, interferon-gamma (IFN-gamma) induces an enzyme of tryptophan catabolism, indoleamine 2,3-dioxygenase (IDO), which is responsible for conversion of tryptophan and other indole derivatives to kynurenine. Tryptophan 162-172 indoleamine 2,3-dioxygenase 1 Homo sapiens 117-120 1909303-7 1991 Highest degree of correlation was found between neopterin, IFN-gamma and the kynurenine per tryptophan quotient which is the ratio between the product and the substrate concentration of IDO. Tryptophan 92-102 indoleamine 2,3-dioxygenase 1 Homo sapiens 186-189 1909303-8 1991 The data indicate that decreased tryptophan in HIV-1 seropositives may result from chronic immune activation and can be referred to increased activation of IDO. Tryptophan 33-43 indoleamine 2,3-dioxygenase 1 Homo sapiens 156-159 1722946-2 1991 Indoleamine 2,3-dioxygenase (IDO) is induced by infections, viruses, lipopolysaccharides, or interferons (IFNs) and this results in significant catabolism of Trp along the kynurenine (Kyn) pathway. Tryptophan 158-161 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 1722946-6 1991 We find that cancer patients given Type I or Type II IFNs can induce IDO which results in decreased serum Trp levels (20-50% of pretreatment) and increased urinary metabolites of the Kyn pathway (5 to 500 fold of pretreatment). Tryptophan 106-109 indoleamine 2,3-dioxygenase 1 Homo sapiens 69-72 1722946-11 1991 We propose that IDO is induced chronically by HIV infection, is further increased by opportunistic infections, and that this chronic loss of Trp initiates mechanisms responsible for the cachexia, dementia, diarrhea and possibly immunosuppression of AIDS patients. Tryptophan 141-144 indoleamine 2,3-dioxygenase 1 Homo sapiens 16-19 2116480-1 1990 The depletion of an essential amino acid, tryptophan, caused by induction of indoleamine 2,3-dioxygenase (IDO), has been shown to be a mechanism involving self-defense against inhaled microorganisms and tumor growth. Tryptophan 42-52 indoleamine 2,3-dioxygenase 1 Homo sapiens 77-104 2174056-2 1990 The interferon (IFN)-gamma-mediated induction of indoleamine 2,3-dioxygenase (IDO) enzyme, which converts tryptophan into N-formylkynurenine, has been implicated in the inhibition of intracellular pathogens, e.g. Toxoplasma gondii and Chlamydia psittaci, and in the antiproliferative effect of IFN-gamma on tumor cells. Tryptophan 106-116 indoleamine 2,3-dioxygenase 1 Homo sapiens 49-76 2174056-2 1990 The interferon (IFN)-gamma-mediated induction of indoleamine 2,3-dioxygenase (IDO) enzyme, which converts tryptophan into N-formylkynurenine, has been implicated in the inhibition of intracellular pathogens, e.g. Toxoplasma gondii and Chlamydia psittaci, and in the antiproliferative effect of IFN-gamma on tumor cells. Tryptophan 106-116 indoleamine 2,3-dioxygenase 1 Homo sapiens 78-81 2116480-1 1990 The depletion of an essential amino acid, tryptophan, caused by induction of indoleamine 2,3-dioxygenase (IDO), has been shown to be a mechanism involving self-defense against inhaled microorganisms and tumor growth. Tryptophan 42-52 indoleamine 2,3-dioxygenase 1 Homo sapiens 106-109 33813026-0 2021 Tryptophan metabolism in brain tumors - IDO and beyond. Tryptophan 0-10 indoleamine 2,3-dioxygenase 1 Homo sapiens 40-43 2166783-4 1990 The negative correlation of tryptophan with kynurenine and neopterin concentrations indicates activity of indoleamine 2,3-dioxygenase (IDO) in patients. Tryptophan 28-38 indoleamine 2,3-dioxygenase 1 Homo sapiens 106-133 2166783-4 1990 The negative correlation of tryptophan with kynurenine and neopterin concentrations indicates activity of indoleamine 2,3-dioxygenase (IDO) in patients. Tryptophan 28-38 indoleamine 2,3-dioxygenase 1 Homo sapiens 135-138 2166783-5 1990 IDO can be induced by cytokines such as interferon-gamma and therefore low tryptophan levels may result from chronic immune stimulation in HIV-1 seropositives. Tryptophan 75-85 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 33813026-3 2021 In recent years, improved understanding of the regulation and downstream function of tryptophan metabolism has been significantly expanded beyond the initial in vitro observation that the enzyme indoleamine-2,3-dioxygenase 1 (IDO1) promotes the depletion of intracellular tryptophan. Tryptophan 85-95 indoleamine 2,3-dioxygenase 1 Homo sapiens 195-224 33813026-3 2021 In recent years, improved understanding of the regulation and downstream function of tryptophan metabolism has been significantly expanded beyond the initial in vitro observation that the enzyme indoleamine-2,3-dioxygenase 1 (IDO1) promotes the depletion of intracellular tryptophan. Tryptophan 85-95 indoleamine 2,3-dioxygenase 1 Homo sapiens 226-230 33813026-3 2021 In recent years, improved understanding of the regulation and downstream function of tryptophan metabolism has been significantly expanded beyond the initial in vitro observation that the enzyme indoleamine-2,3-dioxygenase 1 (IDO1) promotes the depletion of intracellular tryptophan. Tryptophan 272-282 indoleamine 2,3-dioxygenase 1 Homo sapiens 195-224 33813026-3 2021 In recent years, improved understanding of the regulation and downstream function of tryptophan metabolism has been significantly expanded beyond the initial in vitro observation that the enzyme indoleamine-2,3-dioxygenase 1 (IDO1) promotes the depletion of intracellular tryptophan. Tryptophan 272-282 indoleamine 2,3-dioxygenase 1 Homo sapiens 226-230 33777052-1 2021 Background: The immunomodulatory enzyme, indoleamine 2,3-dioxygenase (IDO) facilitates tryptophan catabolism at the rate-limiting step of the kynurenine (Kyn) pathway. Tryptophan 87-97 indoleamine 2,3-dioxygenase 1 Homo sapiens 41-68 33777052-1 2021 Background: The immunomodulatory enzyme, indoleamine 2,3-dioxygenase (IDO) facilitates tryptophan catabolism at the rate-limiting step of the kynurenine (Kyn) pathway. Tryptophan 87-97 indoleamine 2,3-dioxygenase 1 Homo sapiens 70-73 34943977-6 2021 Bearing in mind the complexity of the tumoral terrain and the existence of different cancers with IDO1/TDO2 expressing and non-expressing tumoral cells, here we present a comprehensive analysis of the TRP global metabolic hub and the driving potential of the process of oncogenesis with the main focus on liver cancers. Tryptophan 201-204 indoleamine 2,3-dioxygenase 1 Homo sapiens 98-102 34948292-3 2021 Microarray and mRNAseq profiles from multiple experiments confirmed that enzymes responsible for Trp degradation via the kynurenine pathway (IDO1, KYNU, IL4I1, KMO, and TDO2), receptor of Trp metabolites (HCAR3), and enzymes catalyzing NAD+ turnover (NAMPT, NNMT, PARP9, CD38) were synchronously coregulated in IBD, but not in intestinal malignancies. Tryptophan 97-100 indoleamine 2,3-dioxygenase 1 Homo sapiens 141-145 34949925-0 2021 Temporary Intermediates of L-Trp Along the Reaction Pathway of Human Indoleamine 2,3-Dioxygenase 1 and Identification of an Exo Site. Tryptophan 27-32 indoleamine 2,3-dioxygenase 1 Homo sapiens 69-98 34498786-1 2021 Indoleamine 2, 3-dioxygenase (IDO) catabolizes tryptophan, mediates immunomodulatory functions and is released by stromal cells such as mesenchymal stem cells. Tryptophan 47-57 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-28 34859884-3 2022 This was not related to the expression of the tryptophan-catabolizing indoleamine 2,3-dioxygenase (IDO)-1, but rather to that of its isoform IDO-2, which otherwise is expressed rarely. Tryptophan 46-56 indoleamine 2,3-dioxygenase 1 Homo sapiens 70-105 34498786-1 2021 Indoleamine 2, 3-dioxygenase (IDO) catabolizes tryptophan, mediates immunomodulatory functions and is released by stromal cells such as mesenchymal stem cells. Tryptophan 47-57 indoleamine 2,3-dioxygenase 1 Homo sapiens 30-33 34479957-2 2021 Greater than 90% of GBM expresses the tryptophan (Trp) metabolic enzyme, indoleamine 2,3-dioxygenase 1 (IDO). Tryptophan 38-48 indoleamine 2,3-dioxygenase 1 Homo sapiens 73-102 34479957-2 2021 Greater than 90% of GBM expresses the tryptophan (Trp) metabolic enzyme, indoleamine 2,3-dioxygenase 1 (IDO). Tryptophan 38-48 indoleamine 2,3-dioxygenase 1 Homo sapiens 104-107 34479957-2 2021 Greater than 90% of GBM expresses the tryptophan (Trp) metabolic enzyme, indoleamine 2,3-dioxygenase 1 (IDO). Tryptophan 50-53 indoleamine 2,3-dioxygenase 1 Homo sapiens 73-102 34479957-2 2021 Greater than 90% of GBM expresses the tryptophan (Trp) metabolic enzyme, indoleamine 2,3-dioxygenase 1 (IDO). Tryptophan 50-53 indoleamine 2,3-dioxygenase 1 Homo sapiens 104-107 34479957-3 2021 This observation supported the historical hypothesis that IDO suppresses the antitumor immune response solely through a mechanism that requires intratumoral Trp depletion. Tryptophan 157-160 indoleamine 2,3-dioxygenase 1 Homo sapiens 58-61 34648231-5 2021 Decreased IDO-1 activity was hypothesized due to altered plasma levels of tryptophan and its metabolites in IgE-FA children. Tryptophan 74-84 indoleamine 2,3-dioxygenase 1 Homo sapiens 10-15 34752953-1 2022 Indoleamine 2,3-dioxygenase 1 (IDO1), a known immunosuppressive enzyme that catalyzes the rate-limiting step in the oxidation of tryptophan (Trp) to kynurenine (Kyn), has received increasing attention as an attractive immunotherapeutic target for cancer therapy. Tryptophan 129-139 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-29 34752953-1 2022 Indoleamine 2,3-dioxygenase 1 (IDO1), a known immunosuppressive enzyme that catalyzes the rate-limiting step in the oxidation of tryptophan (Trp) to kynurenine (Kyn), has received increasing attention as an attractive immunotherapeutic target for cancer therapy. Tryptophan 129-139 indoleamine 2,3-dioxygenase 1 Homo sapiens 31-35 34752953-1 2022 Indoleamine 2,3-dioxygenase 1 (IDO1), a known immunosuppressive enzyme that catalyzes the rate-limiting step in the oxidation of tryptophan (Trp) to kynurenine (Kyn), has received increasing attention as an attractive immunotherapeutic target for cancer therapy. Tryptophan 141-144 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-29 34752953-1 2022 Indoleamine 2,3-dioxygenase 1 (IDO1), a known immunosuppressive enzyme that catalyzes the rate-limiting step in the oxidation of tryptophan (Trp) to kynurenine (Kyn), has received increasing attention as an attractive immunotherapeutic target for cancer therapy. Tryptophan 141-144 indoleamine 2,3-dioxygenase 1 Homo sapiens 31-35 34619429-3 2021 The kynurenine pathway, which accounts for ~90% of tryptophan breakdown, is mediated by indoleamine 2,3 dioxygenase 1 (IDO1) in the placenta. Tryptophan 51-61 indoleamine 2,3-dioxygenase 1 Homo sapiens 88-117 34718362-2 2021 Herein, we demonstrated a targeted photo- and immune-active nanoplatform termed NLG919@HA-Ce6 to simultaneously elicit efficient immunogenic cell death (ICD) using the photosensitizer Ce6 and modulate the tryptophan metabolic pathway using an indoleamine 2,3-dioxygenase (IDO) inhibitor NLG919 for the combined photodynamic therapy (PDT) and checkpoint blockade immunotherapy. Tryptophan 205-215 indoleamine 2,3-dioxygenase 1 Homo sapiens 243-270 34718362-2 2021 Herein, we demonstrated a targeted photo- and immune-active nanoplatform termed NLG919@HA-Ce6 to simultaneously elicit efficient immunogenic cell death (ICD) using the photosensitizer Ce6 and modulate the tryptophan metabolic pathway using an indoleamine 2,3-dioxygenase (IDO) inhibitor NLG919 for the combined photodynamic therapy (PDT) and checkpoint blockade immunotherapy. Tryptophan 205-215 indoleamine 2,3-dioxygenase 1 Homo sapiens 272-275 34802039-1 2021 The indoleamine 2,3-dioxygenase (IDO) enzyme is the first rate-limiting enzyme of the tryptophan degradation pathway in which dysfunction of neuroactive metabolites has been implicated in the pathophysiology of schizophrenia. Tryptophan 86-96 indoleamine 2,3-dioxygenase 1 Homo sapiens 4-31 34802039-1 2021 The indoleamine 2,3-dioxygenase (IDO) enzyme is the first rate-limiting enzyme of the tryptophan degradation pathway in which dysfunction of neuroactive metabolites has been implicated in the pathophysiology of schizophrenia. Tryptophan 86-96 indoleamine 2,3-dioxygenase 1 Homo sapiens 33-36 34619429-3 2021 The kynurenine pathway, which accounts for ~90% of tryptophan breakdown, is mediated by indoleamine 2,3 dioxygenase 1 (IDO1) in the placenta. Tryptophan 51-61 indoleamine 2,3-dioxygenase 1 Homo sapiens 119-123 34867973-3 2021 Herein, we report a novel role for Indoleamine 2, 3- dioxygenase (IDO), a metabolic enzyme that degrades tryptophan (Trp) and the Trp metabolite L-kynurenine (L-Kyn) in the regulation of Breg differentiation in the lung TME. Tryptophan 105-115 indoleamine 2,3-dioxygenase 1 Homo sapiens 66-69 34867973-3 2021 Herein, we report a novel role for Indoleamine 2, 3- dioxygenase (IDO), a metabolic enzyme that degrades tryptophan (Trp) and the Trp metabolite L-kynurenine (L-Kyn) in the regulation of Breg differentiation in the lung TME. Tryptophan 117-120 indoleamine 2,3-dioxygenase 1 Homo sapiens 66-69 34867973-3 2021 Herein, we report a novel role for Indoleamine 2, 3- dioxygenase (IDO), a metabolic enzyme that degrades tryptophan (Trp) and the Trp metabolite L-kynurenine (L-Kyn) in the regulation of Breg differentiation in the lung TME. Tryptophan 130-133 indoleamine 2,3-dioxygenase 1 Homo sapiens 66-69 34785665-1 2021 During systemic inflammation, indoleamine 2,3-dioxygenase 1 (IDO1) becomes expressed in endothelial cells where it uses hydrogen peroxide (H2O2) to oxidize L-tryptophan to the tricyclic hydroperoxide, cis-WOOH, that then relaxes arteries via oxidation of protein kinase G 1alpha. Tryptophan 156-168 indoleamine 2,3-dioxygenase 1 Homo sapiens 30-59 34785665-1 2021 During systemic inflammation, indoleamine 2,3-dioxygenase 1 (IDO1) becomes expressed in endothelial cells where it uses hydrogen peroxide (H2O2) to oxidize L-tryptophan to the tricyclic hydroperoxide, cis-WOOH, that then relaxes arteries via oxidation of protein kinase G 1alpha. Tryptophan 156-168 indoleamine 2,3-dioxygenase 1 Homo sapiens 61-65 34869307-2 2021 Tryptophan degrading enzymes indoleamine 2,3 dioxygenase (IDO) and tryptophan 2,3 dioxygenase (TDO) also induce T cell immune tolerance. Tryptophan 0-10 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-56 34869307-2 2021 Tryptophan degrading enzymes indoleamine 2,3 dioxygenase (IDO) and tryptophan 2,3 dioxygenase (TDO) also induce T cell immune tolerance. Tryptophan 0-10 indoleamine 2,3-dioxygenase 1 Homo sapiens 58-61 34829665-2 2021 Tryptophan breakdown via indoleamine 2,3-dioxygenase-1 (IDO-1) along the kynurenine axis concomitant with a pro-inflammatory state was found to be more active in BD, and associated with overweight/obesity. Tryptophan 0-10 indoleamine 2,3-dioxygenase 1 Homo sapiens 25-54 34829665-2 2021 Tryptophan breakdown via indoleamine 2,3-dioxygenase-1 (IDO-1) along the kynurenine axis concomitant with a pro-inflammatory state was found to be more active in BD, and associated with overweight/obesity. Tryptophan 0-10 indoleamine 2,3-dioxygenase 1 Homo sapiens 56-61 34819875-1 2021 Indoleamine-2,3-dioxygenase (IDO) is the "rate-limiting" enzyme in the kynurenine (Kyn) pathway of the tryptophan (Trp) catabolism. Tryptophan 103-113 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 34819875-1 2021 Indoleamine-2,3-dioxygenase (IDO) is the "rate-limiting" enzyme in the kynurenine (Kyn) pathway of the tryptophan (Trp) catabolism. Tryptophan 103-113 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 34819875-1 2021 Indoleamine-2,3-dioxygenase (IDO) is the "rate-limiting" enzyme in the kynurenine (Kyn) pathway of the tryptophan (Trp) catabolism. Tryptophan 115-118 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 34819875-1 2021 Indoleamine-2,3-dioxygenase (IDO) is the "rate-limiting" enzyme in the kynurenine (Kyn) pathway of the tryptophan (Trp) catabolism. Tryptophan 115-118 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 34819931-2 2021 A key protein in human intracellular antichlamydial defense is the tryptophan-degrading enzyme indoleamine 2,3-dioxygenase (IDO) which limits the growth of the tryptophan auxotroph Chlamydia. Tryptophan 67-77 indoleamine 2,3-dioxygenase 1 Homo sapiens 95-122 34819931-2 2021 A key protein in human intracellular antichlamydial defense is the tryptophan-degrading enzyme indoleamine 2,3-dioxygenase (IDO) which limits the growth of the tryptophan auxotroph Chlamydia. Tryptophan 67-77 indoleamine 2,3-dioxygenase 1 Homo sapiens 124-127 34819931-2 2021 A key protein in human intracellular antichlamydial defense is the tryptophan-degrading enzyme indoleamine 2,3-dioxygenase (IDO) which limits the growth of the tryptophan auxotroph Chlamydia. Tryptophan 160-170 indoleamine 2,3-dioxygenase 1 Homo sapiens 95-122 34819931-2 2021 A key protein in human intracellular antichlamydial defense is the tryptophan-degrading enzyme indoleamine 2,3-dioxygenase (IDO) which limits the growth of the tryptophan auxotroph Chlamydia. Tryptophan 160-170 indoleamine 2,3-dioxygenase 1 Homo sapiens 124-127 34535975-3 2021 Inhibition of indoleamine-2,3-dioxygenase (IDO) decreases tryptophan elimination to induce T cells activation for tumor immunosuppression relief. Tryptophan 58-68 indoleamine 2,3-dioxygenase 1 Homo sapiens 14-41 34535975-3 2021 Inhibition of indoleamine-2,3-dioxygenase (IDO) decreases tryptophan elimination to induce T cells activation for tumor immunosuppression relief. Tryptophan 58-68 indoleamine 2,3-dioxygenase 1 Homo sapiens 43-46 34535975-8 2021 NLG919 inhibits IDO to reduce tryptophan metabolism, so immunity in tumors is aroused to anti-tumor. Tryptophan 30-40 indoleamine 2,3-dioxygenase 1 Homo sapiens 16-19 34482001-1 2021 Indoleamine 2, 3-dioxygenase (IDO), a tryptophan-catabolizing enzyme, is essential in physiological immunoregulation. Tryptophan 38-48 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-28 34482001-1 2021 Indoleamine 2, 3-dioxygenase (IDO), a tryptophan-catabolizing enzyme, is essential in physiological immunoregulation. Tryptophan 38-48 indoleamine 2,3-dioxygenase 1 Homo sapiens 30-33 34670590-5 2021 At the molecular level, the tryptophan metabolites, kynurenine or kynurenic acid, produced by indoleamine 2,3-dioxygenase (IDO), augment the expression of TNF-stimulated gene 6 (TSG6) through the activation of the aryl hydrocarbon receptor (AHR). Tryptophan 28-38 indoleamine 2,3-dioxygenase 1 Homo sapiens 94-121 34670590-5 2021 At the molecular level, the tryptophan metabolites, kynurenine or kynurenic acid, produced by indoleamine 2,3-dioxygenase (IDO), augment the expression of TNF-stimulated gene 6 (TSG6) through the activation of the aryl hydrocarbon receptor (AHR). Tryptophan 28-38 indoleamine 2,3-dioxygenase 1 Homo sapiens 123-126 34657635-1 2021 BACKGROUND: Increased tryptophan (Trp) metabolism by indoleamine 2,3-dioxygenase (IDO)/tryptophan 2,3-dioxygenase (TDO) represents one of the most studied pathways for immunosuppression in tumor tissues. Tryptophan 22-32 indoleamine 2,3-dioxygenase 1 Homo sapiens 53-80 34687129-5 2021 For example, increased expression of the enzyme IDO1, which converts Trp into Kyn, leads to an increase in Kyn levels in numerous cancers. Tryptophan 69-72 indoleamine 2,3-dioxygenase 1 Homo sapiens 48-52 34657635-1 2021 BACKGROUND: Increased tryptophan (Trp) metabolism by indoleamine 2,3-dioxygenase (IDO)/tryptophan 2,3-dioxygenase (TDO) represents one of the most studied pathways for immunosuppression in tumor tissues. Tryptophan 22-32 indoleamine 2,3-dioxygenase 1 Homo sapiens 82-85 34657635-1 2021 BACKGROUND: Increased tryptophan (Trp) metabolism by indoleamine 2,3-dioxygenase (IDO)/tryptophan 2,3-dioxygenase (TDO) represents one of the most studied pathways for immunosuppression in tumor tissues. Tryptophan 34-37 indoleamine 2,3-dioxygenase 1 Homo sapiens 53-80 34657635-1 2021 BACKGROUND: Increased tryptophan (Trp) metabolism by indoleamine 2,3-dioxygenase (IDO)/tryptophan 2,3-dioxygenase (TDO) represents one of the most studied pathways for immunosuppression in tumor tissues. Tryptophan 34-37 indoleamine 2,3-dioxygenase 1 Homo sapiens 82-85 34680153-12 2021 IDO depletes tryptophan and activates GCN2K. Tryptophan 13-23 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 34614413-3 2021 Pharmacologic inhibition of Bruton"s tyrosine kinase (BTK) and the tryptophan-degrading enzyme indoleamine 2,3-dioxygenase (IDO) or deletion of Btk or Ido1 allowed robust differentiation of inflammatory Ly6c+CD103+ DCs during chemotherapy, promoting antitumor T cell responses and inhibiting tumor growth. Tryptophan 67-77 indoleamine 2,3-dioxygenase 1 Homo sapiens 95-122 34174026-2 2021 Metabolism of tryptophan to N -formyl-kynurenine by hIDO1 leads to immune suppression to result in cancer cell immune escape. Tryptophan 14-24 indoleamine 2,3-dioxygenase 1 Homo sapiens 52-57 34614413-3 2021 Pharmacologic inhibition of Bruton"s tyrosine kinase (BTK) and the tryptophan-degrading enzyme indoleamine 2,3-dioxygenase (IDO) or deletion of Btk or Ido1 allowed robust differentiation of inflammatory Ly6c+CD103+ DCs during chemotherapy, promoting antitumor T cell responses and inhibiting tumor growth. Tryptophan 67-77 indoleamine 2,3-dioxygenase 1 Homo sapiens 124-127 34440060-3 2021 To illustrate, catabolism of tryptophan by indoleamine 2,3-dioxygenase (IDO) gives rise to numerous biologically active metabolites implicated in CKD progression. Tryptophan 29-39 indoleamine 2,3-dioxygenase 1 Homo sapiens 72-75 34137184-2 2021 As a consequence, enzymes catalyzing rate limiting steps along l -Trp catabolic pathways - including IDO1, TDO, TPH1 and TPH2 - have turned interesting drug targets for the design and development of novel therapeutic agents for different disorders such as carcinoid syndrome, cancer and autoimmune diseases. Tryptophan 63-69 indoleamine 2,3-dioxygenase 1 Homo sapiens 101-105 34576067-5 2021 Here, we provide an overview of the fundamental aspects of Trp metabolism and the interplay between the dysregulation of the main actors involved in Trp metabolism such as indoleamine 2, 3-dioxygenase 1 (IDO) and CVD, including atherosclerosis and myocardial infarction. Tryptophan 59-62 indoleamine 2,3-dioxygenase 1 Homo sapiens 204-207 34576067-5 2021 Here, we provide an overview of the fundamental aspects of Trp metabolism and the interplay between the dysregulation of the main actors involved in Trp metabolism such as indoleamine 2, 3-dioxygenase 1 (IDO) and CVD, including atherosclerosis and myocardial infarction. Tryptophan 149-152 indoleamine 2,3-dioxygenase 1 Homo sapiens 172-202 34576067-5 2021 Here, we provide an overview of the fundamental aspects of Trp metabolism and the interplay between the dysregulation of the main actors involved in Trp metabolism such as indoleamine 2, 3-dioxygenase 1 (IDO) and CVD, including atherosclerosis and myocardial infarction. Tryptophan 149-152 indoleamine 2,3-dioxygenase 1 Homo sapiens 204-207 34900804-6 2021 IDO activity was estimated using kynurenine/tryptophan ratio (KTR). Tryptophan 44-54 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 34284200-1 2021 Indoleamine 2,3-dioxygenase (IDO) as a principle enzyme in tryptophan (Trp) catabolism, modulates immune responses and promotes cancer progression. Tryptophan 59-69 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 34284200-1 2021 Indoleamine 2,3-dioxygenase (IDO) as a principle enzyme in tryptophan (Trp) catabolism, modulates immune responses and promotes cancer progression. Tryptophan 59-69 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 34284200-1 2021 Indoleamine 2,3-dioxygenase (IDO) as a principle enzyme in tryptophan (Trp) catabolism, modulates immune responses and promotes cancer progression. Tryptophan 71-74 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 34284200-1 2021 Indoleamine 2,3-dioxygenase (IDO) as a principle enzyme in tryptophan (Trp) catabolism, modulates immune responses and promotes cancer progression. Tryptophan 71-74 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 34365162-6 2021 The aim of this review is to summarize the most important information concerning the immune regulation in pregnancy, focusing on the role of tryptophan (Trp) catabolism performed by indoleamine 2,3-dioxygenase (IDO) and tryptophan 2,3-dioxygenase (TDO) in the placenta. Tryptophan 141-151 indoleamine 2,3-dioxygenase 1 Homo sapiens 182-209 34365162-6 2021 The aim of this review is to summarize the most important information concerning the immune regulation in pregnancy, focusing on the role of tryptophan (Trp) catabolism performed by indoleamine 2,3-dioxygenase (IDO) and tryptophan 2,3-dioxygenase (TDO) in the placenta. Tryptophan 141-151 indoleamine 2,3-dioxygenase 1 Homo sapiens 211-214 34365162-6 2021 The aim of this review is to summarize the most important information concerning the immune regulation in pregnancy, focusing on the role of tryptophan (Trp) catabolism performed by indoleamine 2,3-dioxygenase (IDO) and tryptophan 2,3-dioxygenase (TDO) in the placenta. Tryptophan 153-156 indoleamine 2,3-dioxygenase 1 Homo sapiens 182-209 34365162-6 2021 The aim of this review is to summarize the most important information concerning the immune regulation in pregnancy, focusing on the role of tryptophan (Trp) catabolism performed by indoleamine 2,3-dioxygenase (IDO) and tryptophan 2,3-dioxygenase (TDO) in the placenta. Tryptophan 153-156 indoleamine 2,3-dioxygenase 1 Homo sapiens 211-214 34440798-2 2021 The enzyme indoleamine-2,3-dioxygenase (IDO), which participates in the rate-limiting step of tryptophan catabolism through the kynurenine pathway (KP), is associated with poor prognosis in patients with GBM. Tryptophan 94-104 indoleamine 2,3-dioxygenase 1 Homo sapiens 11-38 34440798-2 2021 The enzyme indoleamine-2,3-dioxygenase (IDO), which participates in the rate-limiting step of tryptophan catabolism through the kynurenine pathway (KP), is associated with poor prognosis in patients with GBM. Tryptophan 94-104 indoleamine 2,3-dioxygenase 1 Homo sapiens 40-43 34311709-1 2021 BACKGROUND: Indoleamine 2,3 dioxygenase (IDO), the rate-limiting enzyme in the kynurenine (Kyn) pathway of tryptophan (Trp) degradation, is modulated by inflammation, and is regarded as a key molecule driving immunotolerance and immunosuppressive mechanisms. Tryptophan 107-117 indoleamine 2,3-dioxygenase 1 Homo sapiens 12-39 34311709-1 2021 BACKGROUND: Indoleamine 2,3 dioxygenase (IDO), the rate-limiting enzyme in the kynurenine (Kyn) pathway of tryptophan (Trp) degradation, is modulated by inflammation, and is regarded as a key molecule driving immunotolerance and immunosuppressive mechanisms. Tryptophan 107-117 indoleamine 2,3-dioxygenase 1 Homo sapiens 41-44 34311709-1 2021 BACKGROUND: Indoleamine 2,3 dioxygenase (IDO), the rate-limiting enzyme in the kynurenine (Kyn) pathway of tryptophan (Trp) degradation, is modulated by inflammation, and is regarded as a key molecule driving immunotolerance and immunosuppressive mechanisms. Tryptophan 119-122 indoleamine 2,3-dioxygenase 1 Homo sapiens 12-39 34311709-1 2021 BACKGROUND: Indoleamine 2,3 dioxygenase (IDO), the rate-limiting enzyme in the kynurenine (Kyn) pathway of tryptophan (Trp) degradation, is modulated by inflammation, and is regarded as a key molecule driving immunotolerance and immunosuppressive mechanisms. Tryptophan 119-122 indoleamine 2,3-dioxygenase 1 Homo sapiens 41-44 34977580-0 2021 Design, synthesis and evaluation of tryptophan analogues as tool compounds to study IDO1 activity. Tryptophan 36-46 indoleamine 2,3-dioxygenase 1 Homo sapiens 84-88 34977580-1 2021 The metabolism of l-tryptophan to N-formyl-l-kynurenine by indoleamine-2,3-dioxygenase 1 (IDO1) is thought to play a critical role in tumour-mediated immune suppression. Tryptophan 18-30 indoleamine 2,3-dioxygenase 1 Homo sapiens 59-88 34977580-1 2021 The metabolism of l-tryptophan to N-formyl-l-kynurenine by indoleamine-2,3-dioxygenase 1 (IDO1) is thought to play a critical role in tumour-mediated immune suppression. Tryptophan 18-30 indoleamine 2,3-dioxygenase 1 Homo sapiens 90-94 34977580-3 2021 Here we report the design, synthesis and biological evaluation of a series of tryptophan analogues which have the potential to intercept putative intermediates in the metabolism of 1 by IDO1. Tryptophan 78-88 indoleamine 2,3-dioxygenase 1 Homo sapiens 186-190 34977580-6 2021 These findings provide a start-point for development of further mechanistic probes and more potent tryptophan-based IDO1 inhibitors. Tryptophan 99-109 indoleamine 2,3-dioxygenase 1 Homo sapiens 116-120 34396771-11 2021 The IDO1 inhibitor reversed the ITM by suppressing IDO1-mediated Trp degradation and exhaustion of cytotoxic T cells. Tryptophan 65-68 indoleamine 2,3-dioxygenase 1 Homo sapiens 4-8 34396771-11 2021 The IDO1 inhibitor reversed the ITM by suppressing IDO1-mediated Trp degradation and exhaustion of cytotoxic T cells. Tryptophan 65-68 indoleamine 2,3-dioxygenase 1 Homo sapiens 51-55 34522439-3 2021 Respiratory viral infections are believed to affect the expression of indoleamine 2,3-dioxygenase (IDO), a limiting enzyme in tryptophan catabolism, which is presumed to alter asthmatic airway inflammation. Tryptophan 126-136 indoleamine 2,3-dioxygenase 1 Homo sapiens 99-102 34292726-1 2021 Indoleamine 2,3-dioxygenase 1 (IDO1), a heme-containing enzyme that mediates the rate-limiting step in the metabolism of l-tryptophan to kynurenine, has been widely explored as a potential immunotherapeutic target in oncology. Tryptophan 121-133 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-29 34292726-1 2021 Indoleamine 2,3-dioxygenase 1 (IDO1), a heme-containing enzyme that mediates the rate-limiting step in the metabolism of l-tryptophan to kynurenine, has been widely explored as a potential immunotherapeutic target in oncology. Tryptophan 121-133 indoleamine 2,3-dioxygenase 1 Homo sapiens 31-35 34336787-1 2021 Indoleamine-2,3-dioxygenase (IDO1) and tryptophan dioxygenases are two heme based metalloenzymes that catalyze the tryptophan oxidation reaction by inserting molecular dioxygen to cleave the pyrrole ring. Tryptophan 115-125 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-33 35582948-14 2022 CONCLUSIONS: Kynurenine, an IDO1-mediated tryptophan metabolism main product, promotes RUNX2 ubiquitination and subsequently leads to its proteasomal degradation via an aryl hydrocarbon receptor-dependent nongenomic pathway. Tryptophan 42-52 indoleamine 2,3-dioxygenase 1 Homo sapiens 28-32 34065885-2 2021 Here, we attempted to produce kynurenine, a health-promoting metabolite, in plants of Nicotiana tabacum (tobacco) transformed by Agrobacterium tumefaciens with the gene, coding for human indoleamine 2,3-dioxygenase 1 (IDO1), an enzyme responsible for the kynurenine production because of tryptophan degradation. Tryptophan 288-298 indoleamine 2,3-dioxygenase 1 Homo sapiens 187-216 34065885-2 2021 Here, we attempted to produce kynurenine, a health-promoting metabolite, in plants of Nicotiana tabacum (tobacco) transformed by Agrobacterium tumefaciens with the gene, coding for human indoleamine 2,3-dioxygenase 1 (IDO1), an enzyme responsible for the kynurenine production because of tryptophan degradation. Tryptophan 288-298 indoleamine 2,3-dioxygenase 1 Homo sapiens 218-222 34223158-4 2021 One prominent endogenous ligand of AHR is the oncometabolite kynurenine, a product of tryptophan metabolism catalyzed by the dioxygenases IDO1 and TDO that are often aberrantly activated in cancer. Tryptophan 86-96 indoleamine 2,3-dioxygenase 1 Homo sapiens 138-142 34326168-8 2021 Tryptophan and IDO inhibitors administration, both increased intracellular tryptophan, and tryptophanyl-tRNA synthetase (WARS) overexpression decreased Jurkat and mice CD8+ T cell surface PD-1. Tryptophan 75-85 indoleamine 2,3-dioxygenase 1 Homo sapiens 15-18 34249475-6 2021 Of note, we discovered that the PrPC-ILK signaling axis controls the expression and activity of the tryptophan metabolizing enzyme indoleamine 2,3 dioxygenase IDO1, a key player in immune tolerance. Tryptophan 100-110 indoleamine 2,3-dioxygenase 1 Homo sapiens 159-163 34145969-2 2021 When discovered more than 50 years ago, IDO1 was thought to be an effector molecule capable of mediating a survival strategy based on the deprivation of bacteria and tumor cells of the essential amino acid tryptophan. Tryptophan 206-216 indoleamine 2,3-dioxygenase 1 Homo sapiens 40-44 34145969-1 2021 Indoleamine 2,3-dioxygenase 1 (IDO1) catalyzes the initial rate-limiting step in the degradation of the essential amino acid tryptophan along the kynurenine pathway. Tryptophan 125-135 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-29 34145969-1 2021 Indoleamine 2,3-dioxygenase 1 (IDO1) catalyzes the initial rate-limiting step in the degradation of the essential amino acid tryptophan along the kynurenine pathway. Tryptophan 125-135 indoleamine 2,3-dioxygenase 1 Homo sapiens 31-35 34145969-3 2021 Since 1998, when tryptophan catabolism was discovered to be crucially involved in the maintenance of maternal T cell tolerance, IDO1 has become the focus of several laboratories around the world. Tryptophan 17-27 indoleamine 2,3-dioxygenase 1 Homo sapiens 128-132 34127024-4 2021 The tryptophan-kynurenine metabolic pathway degrades more than 90% of tryptophan (TRP) throughout the body, with indoleamine 2,3-dioxygenase (IDO), the key metabolic enzyme, being activated in the inflammatory environment. Tryptophan 4-14 indoleamine 2,3-dioxygenase 1 Homo sapiens 113-140 34127024-4 2021 The tryptophan-kynurenine metabolic pathway degrades more than 90% of tryptophan (TRP) throughout the body, with indoleamine 2,3-dioxygenase (IDO), the key metabolic enzyme, being activated in the inflammatory environment. Tryptophan 4-14 indoleamine 2,3-dioxygenase 1 Homo sapiens 142-145 34127024-4 2021 The tryptophan-kynurenine metabolic pathway degrades more than 90% of tryptophan (TRP) throughout the body, with indoleamine 2,3-dioxygenase (IDO), the key metabolic enzyme, being activated in the inflammatory environment. Tryptophan 70-80 indoleamine 2,3-dioxygenase 1 Homo sapiens 113-140 34127024-4 2021 The tryptophan-kynurenine metabolic pathway degrades more than 90% of tryptophan (TRP) throughout the body, with indoleamine 2,3-dioxygenase (IDO), the key metabolic enzyme, being activated in the inflammatory environment. Tryptophan 70-80 indoleamine 2,3-dioxygenase 1 Homo sapiens 142-145 34195299-11 2021 Genes associated with tryptophan metabolism (IDO1 and KYNU) and metalloproteinases were among the most differentially expressed between the high- and low-risk groups. Tryptophan 22-32 indoleamine 2,3-dioxygenase 1 Homo sapiens 45-49 34087175-1 2021 We talk to Alice Clare Newman, new mother, postdoc, and first author of "Immune-regulated IDO1-dependent tryptophan metabolism is source of one-carbon units for pancreatic cancer and stellate cells," about her paper, juggling family and career, and life-changing moments that led to the realization that life doesn"t wait for science. Tryptophan 105-115 indoleamine 2,3-dioxygenase 1 Homo sapiens 90-94 34117113-2 2021 Indoximod is a small-molecule IDO pathway inhibitor that reverses the immunosuppressive effects of low tryptophan (Trp) and high kynurenine (Kyn) that result from IDO activity. Tryptophan 103-113 indoleamine 2,3-dioxygenase 1 Homo sapiens 30-33 34117113-2 2021 Indoximod is a small-molecule IDO pathway inhibitor that reverses the immunosuppressive effects of low tryptophan (Trp) and high kynurenine (Kyn) that result from IDO activity. Tryptophan 103-113 indoleamine 2,3-dioxygenase 1 Homo sapiens 163-166 34117113-2 2021 Indoximod is a small-molecule IDO pathway inhibitor that reverses the immunosuppressive effects of low tryptophan (Trp) and high kynurenine (Kyn) that result from IDO activity. Tryptophan 115-118 indoleamine 2,3-dioxygenase 1 Homo sapiens 30-33 34117113-2 2021 Indoximod is a small-molecule IDO pathway inhibitor that reverses the immunosuppressive effects of low tryptophan (Trp) and high kynurenine (Kyn) that result from IDO activity. Tryptophan 115-118 indoleamine 2,3-dioxygenase 1 Homo sapiens 163-166 35466092-5 2022 One of the most important of these genes is indoleamine-pyrrole 2,3-dioxygenase (IDO), which plays a major role in tryptophan catabolism. Tryptophan 115-125 indoleamine 2,3-dioxygenase 1 Homo sapiens 44-79 35244712-1 2022 Tryptophan 2,3-dioxygenase (TDO) and indoleamine 2,3-dioxygenase (IDO) catalyze the same reaction, oxidative cleavage of L-tryptophan (L-Trp) to N-formyl-kynurenine. Tryptophan 121-133 indoleamine 2,3-dioxygenase 1 Homo sapiens 37-64 35244712-1 2022 Tryptophan 2,3-dioxygenase (TDO) and indoleamine 2,3-dioxygenase (IDO) catalyze the same reaction, oxidative cleavage of L-tryptophan (L-Trp) to N-formyl-kynurenine. Tryptophan 121-133 indoleamine 2,3-dioxygenase 1 Homo sapiens 66-69 35244712-1 2022 Tryptophan 2,3-dioxygenase (TDO) and indoleamine 2,3-dioxygenase (IDO) catalyze the same reaction, oxidative cleavage of L-tryptophan (L-Trp) to N-formyl-kynurenine. Tryptophan 135-140 indoleamine 2,3-dioxygenase 1 Homo sapiens 37-64 35244712-1 2022 Tryptophan 2,3-dioxygenase (TDO) and indoleamine 2,3-dioxygenase (IDO) catalyze the same reaction, oxidative cleavage of L-tryptophan (L-Trp) to N-formyl-kynurenine. Tryptophan 135-140 indoleamine 2,3-dioxygenase 1 Homo sapiens 66-69 35604497-3 2022 Indoleamine 2,3-dioxygenase 1 (IDO1) is activated in chronic inflammatory states and catalyzes the first and rate-limiting step of tryptophan (TRP) metabolism along the kynurenine pathway (KP). Tryptophan 131-141 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-29 35604497-3 2022 Indoleamine 2,3-dioxygenase 1 (IDO1) is activated in chronic inflammatory states and catalyzes the first and rate-limiting step of tryptophan (TRP) metabolism along the kynurenine pathway (KP). Tryptophan 131-141 indoleamine 2,3-dioxygenase 1 Homo sapiens 31-35 35604497-3 2022 Indoleamine 2,3-dioxygenase 1 (IDO1) is activated in chronic inflammatory states and catalyzes the first and rate-limiting step of tryptophan (TRP) metabolism along the kynurenine pathway (KP). Tryptophan 143-146 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-29 35604497-3 2022 Indoleamine 2,3-dioxygenase 1 (IDO1) is activated in chronic inflammatory states and catalyzes the first and rate-limiting step of tryptophan (TRP) metabolism along the kynurenine pathway (KP). Tryptophan 143-146 indoleamine 2,3-dioxygenase 1 Homo sapiens 31-35 35466092-5 2022 One of the most important of these genes is indoleamine-pyrrole 2,3-dioxygenase (IDO), which plays a major role in tryptophan catabolism. Tryptophan 115-125 indoleamine 2,3-dioxygenase 1 Homo sapiens 81-84 35466092-6 2022 IDO is an intracellular monomeric enzyme that is also responsible for breaking down and consuming tryptophan in the Kynurenine pathway. Tryptophan 98-108 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 35358772-1 2022 Indoleamine 2, 3-dioxygenase 1 (IDO1) and tryptophan 2, 3-dioxygenase (TDO), catalyzing the first and rate-limiting step of tryptophan-kynurenine (Trp-Kyn) metabolism pathway, are the appealing targets for cancer immunotherapy. Tryptophan 124-134 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-30 35545044-4 2022 In contrast, the tryptophan catabolism rate-limiting enzymes IDO1 and TDO2 are highly overexpressed in stroma, raising the hypothesis that kynurenine-mediated suppression of antitumor immunity may be predominantly constrained by the stroma. Tryptophan 17-27 indoleamine 2,3-dioxygenase 1 Homo sapiens 61-65 35358772-1 2022 Indoleamine 2, 3-dioxygenase 1 (IDO1) and tryptophan 2, 3-dioxygenase (TDO), catalyzing the first and rate-limiting step of tryptophan-kynurenine (Trp-Kyn) metabolism pathway, are the appealing targets for cancer immunotherapy. Tryptophan 124-134 indoleamine 2,3-dioxygenase 1 Homo sapiens 32-36 35358772-1 2022 Indoleamine 2, 3-dioxygenase 1 (IDO1) and tryptophan 2, 3-dioxygenase (TDO), catalyzing the first and rate-limiting step of tryptophan-kynurenine (Trp-Kyn) metabolism pathway, are the appealing targets for cancer immunotherapy. Tryptophan 147-150 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-30 35358772-1 2022 Indoleamine 2, 3-dioxygenase 1 (IDO1) and tryptophan 2, 3-dioxygenase (TDO), catalyzing the first and rate-limiting step of tryptophan-kynurenine (Trp-Kyn) metabolism pathway, are the appealing targets for cancer immunotherapy. Tryptophan 147-150 indoleamine 2,3-dioxygenase 1 Homo sapiens 32-36 35510301-11 2022 Moreover, eATP increased kynurenine which is the active metabolite of tryptophan breakdown catalyzed by the IDO enzyme and significantly induced IFNgamma protein expression. Tryptophan 70-80 indoleamine 2,3-dioxygenase 1 Homo sapiens 108-111 35435494-8 2022 In addition, dietary supplemented with 0.18% Trp reduced the levels of serum DA, Adr, noradrenaline (NA), CRH, TDO, IDO, kynurenic acid, IL-1beta, and hypothalamic 5-HIAA/5-HT (P < 0.05), increased the levels of serum Trp, 5-HT, and IL-22, and upregulated the concentrations of hypothalamic Trp and 5-HT in heat-stressed broilers (P < 0.05). Tryptophan 45-48 indoleamine 2,3-dioxygenase 1 Homo sapiens 116-119 35502977-2 2022 Tumor cells enlisted an alternative pathway to break down tryptophan, the target of IDO1, and increased the activity of pathways that generate NAD+. Tryptophan 58-68 indoleamine 2,3-dioxygenase 1 Homo sapiens 84-88 35422466-1 2022 The tryptophan catabolite (TRYCAT) pathway is implicated in the pathophysiology of schizophrenia (SCZ) since the rate-limiting enzyme indoleamine-dioxygenase (IDO) may be induced by inflammatory and oxidative stress mediators. Tryptophan 4-14 indoleamine 2,3-dioxygenase 1 Homo sapiens 134-157 35456119-2 2022 Indoleamine2,3-dioxygenase 1 (IDO-1) is an enzyme that initiates the tryptophan degradation that is important in initial host innate immune defense against infectious pathogens. Tryptophan 69-79 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-28 35456119-2 2022 Indoleamine2,3-dioxygenase 1 (IDO-1) is an enzyme that initiates the tryptophan degradation that is important in initial host innate immune defense against infectious pathogens. Tryptophan 69-79 indoleamine 2,3-dioxygenase 1 Homo sapiens 30-35 35456119-5 2022 Higher IDO-1 (Kyn/Trp ratio) activation was observed during the early acute phase of CHIKV infection and declined in the chronic phase. Tryptophan 18-21 indoleamine 2,3-dioxygenase 1 Homo sapiens 7-12 35493480-1 2022 Indoleamine-2,3-dioxygenase (IDO)1 and IDO2 are closely related tryptophan catabolizing enzymes that have immunomodulatory properties. Tryptophan 64-74 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-34 35458704-7 2022 Although LPS increased AhR and its target gene CYP1B1, curcumin further enhanced LPS-induced CYP1B1 and indoleamine 2,3-dioxygenase (IDO), which metabolizes tryptophan to AhR ligands kynurenine (KYN) and kynurenic acid (KYNA). Tryptophan 157-167 indoleamine 2,3-dioxygenase 1 Homo sapiens 104-131 35458704-7 2022 Although LPS increased AhR and its target gene CYP1B1, curcumin further enhanced LPS-induced CYP1B1 and indoleamine 2,3-dioxygenase (IDO), which metabolizes tryptophan to AhR ligands kynurenine (KYN) and kynurenic acid (KYNA). Tryptophan 157-167 indoleamine 2,3-dioxygenase 1 Homo sapiens 133-136 35413710-1 2022 BACKGROUND: The enzyme indolamine-2,3-dioxygenase 1 (IDO1) is the rate-limiting enzyme of the kynurenine (KYN) pathway and metabolizes the essential amino acid tryptophan to KYNs. Tryptophan 160-170 indoleamine 2,3-dioxygenase 1 Homo sapiens 23-51 35413710-1 2022 BACKGROUND: The enzyme indolamine-2,3-dioxygenase 1 (IDO1) is the rate-limiting enzyme of the kynurenine (KYN) pathway and metabolizes the essential amino acid tryptophan to KYNs. Tryptophan 160-170 indoleamine 2,3-dioxygenase 1 Homo sapiens 53-57 35422466-1 2022 The tryptophan catabolite (TRYCAT) pathway is implicated in the pathophysiology of schizophrenia (SCZ) since the rate-limiting enzyme indoleamine-dioxygenase (IDO) may be induced by inflammatory and oxidative stress mediators. Tryptophan 4-14 indoleamine 2,3-dioxygenase 1 Homo sapiens 159-162 35294258-3 2022 IDO1 inhibition resulted in efficient blockade of the kynurenine pathway of tryptophan degradation and was accompanied by a metabolic adaptation that shunted tryptophan catabolism toward the serotonin pathway. Tryptophan 76-86 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-4 35371054-1 2022 The indoleamine 2,3-dioxygenase 1 (IDO1) metabolic circuitry, comprising the first tryptophan (Trp) catabolite L-kynurenine (Kyn) and the aryl hydrocarbon receptor (AHR), has emerged as a mechanism of cancer immune evasion. Tryptophan 83-93 indoleamine 2,3-dioxygenase 1 Homo sapiens 4-33 35371054-1 2022 The indoleamine 2,3-dioxygenase 1 (IDO1) metabolic circuitry, comprising the first tryptophan (Trp) catabolite L-kynurenine (Kyn) and the aryl hydrocarbon receptor (AHR), has emerged as a mechanism of cancer immune evasion. Tryptophan 83-93 indoleamine 2,3-dioxygenase 1 Homo sapiens 35-39 35371054-1 2022 The indoleamine 2,3-dioxygenase 1 (IDO1) metabolic circuitry, comprising the first tryptophan (Trp) catabolite L-kynurenine (Kyn) and the aryl hydrocarbon receptor (AHR), has emerged as a mechanism of cancer immune evasion. Tryptophan 95-98 indoleamine 2,3-dioxygenase 1 Homo sapiens 4-33 35371054-1 2022 The indoleamine 2,3-dioxygenase 1 (IDO1) metabolic circuitry, comprising the first tryptophan (Trp) catabolite L-kynurenine (Kyn) and the aryl hydrocarbon receptor (AHR), has emerged as a mechanism of cancer immune evasion. Tryptophan 95-98 indoleamine 2,3-dioxygenase 1 Homo sapiens 35-39 35294258-3 2022 IDO1 inhibition resulted in efficient blockade of the kynurenine pathway of tryptophan degradation and was accompanied by a metabolic adaptation that shunted tryptophan catabolism toward the serotonin pathway. Tryptophan 158-168 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-4 35245456-1 2022 IDO1 oxidizes tryptophan (TRP) to generate kynurenine (KYN), the substrate for 1-carbon and NAD metabolism, and is implicated in pro-cancer pathophysiology and infection biology. Tryptophan 14-24 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-4 35245456-1 2022 IDO1 oxidizes tryptophan (TRP) to generate kynurenine (KYN), the substrate for 1-carbon and NAD metabolism, and is implicated in pro-cancer pathophysiology and infection biology. Tryptophan 26-29 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-4 35085834-2 2022 IDO1 enzyme catabolizes L-tryptophan (L-Trp) into kynurenine (KYN) thus stimulating the KYN pathway. Tryptophan 24-36 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-4 35085834-2 2022 IDO1 enzyme catabolizes L-tryptophan (L-Trp) into kynurenine (KYN) thus stimulating the KYN pathway. Tryptophan 38-43 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-4 35150740-3 2022 We found that IDO1 was necessary and sufficient for production of kynurenine, a downstream tryptophan metabolite, in cancer cells. Tryptophan 91-101 indoleamine 2,3-dioxygenase 1 Homo sapiens 14-18 35264796-1 2022 Activated T cells secrete interferon-gamma, which triggers intracellular tryptophan shortage by upregulating the indoleamine 2,3-dioxygenase 1 (IDO1) enzyme1-4. Tryptophan 73-83 indoleamine 2,3-dioxygenase 1 Homo sapiens 113-142 35226872-6 2022 In addition, mf significantly induced the frequency of interferon (IFN)-gamma+ human monocytes and at the same time induced the mRNA expression of indoleamine 2,3-dioxygenase (IDO) through an IFN-gamma-dependent mechanism; significantly enhanced tryptophan degradation (an indicator of IDO activity; P < 0.005). Tryptophan 246-256 indoleamine 2,3-dioxygenase 1 Homo sapiens 147-174 35226872-6 2022 In addition, mf significantly induced the frequency of interferon (IFN)-gamma+ human monocytes and at the same time induced the mRNA expression of indoleamine 2,3-dioxygenase (IDO) through an IFN-gamma-dependent mechanism; significantly enhanced tryptophan degradation (an indicator of IDO activity; P < 0.005). Tryptophan 246-256 indoleamine 2,3-dioxygenase 1 Homo sapiens 176-179 35051612-1 2022 Indoleamine-2, 3-dioxygenase (IDO1) and Tryptophan-2, 3-dioxygense (TDO) are heme-containing dioxygenases that catalyze the conversion of tryptophan to N-formyl-kynurenine and thus enable generation of l-kynurenine and related metabolites that govern the immune response and broadly impact human biology. Tryptophan 138-148 indoleamine 2,3-dioxygenase 1 Homo sapiens 30-34 35203299-4 2022 It induces Indolamine 2,3 dioxygenase (IDO-1), the enzyme which, starting from Tryptophan (Trp), produces Kynurenine (Kyn, Beta-Anthraniloyl-L-Alanine). Tryptophan 79-89 indoleamine 2,3-dioxygenase 1 Homo sapiens 11-37 35203299-4 2022 It induces Indolamine 2,3 dioxygenase (IDO-1), the enzyme which, starting from Tryptophan (Trp), produces Kynurenine (Kyn, Beta-Anthraniloyl-L-Alanine). Tryptophan 79-89 indoleamine 2,3-dioxygenase 1 Homo sapiens 39-44 35203299-4 2022 It induces Indolamine 2,3 dioxygenase (IDO-1), the enzyme which, starting from Tryptophan (Trp), produces Kynurenine (Kyn, Beta-Anthraniloyl-L-Alanine). Tryptophan 91-94 indoleamine 2,3-dioxygenase 1 Homo sapiens 11-37 35203299-4 2022 It induces Indolamine 2,3 dioxygenase (IDO-1), the enzyme which, starting from Tryptophan (Trp), produces Kynurenine (Kyn, Beta-Anthraniloyl-L-Alanine). Tryptophan 91-94 indoleamine 2,3-dioxygenase 1 Homo sapiens 39-44 35187162-1 2022 Background: Indoleamine 2,3-dioxygenase 1 (IDO1) catalyzes the first step of tryptophan catabolism in the kynurenine (Kyn) pathway. Tryptophan 77-87 indoleamine 2,3-dioxygenase 1 Homo sapiens 12-41 35187162-1 2022 Background: Indoleamine 2,3-dioxygenase 1 (IDO1) catalyzes the first step of tryptophan catabolism in the kynurenine (Kyn) pathway. Tryptophan 77-87 indoleamine 2,3-dioxygenase 1 Homo sapiens 43-47 35264796-1 2022 Activated T cells secrete interferon-gamma, which triggers intracellular tryptophan shortage by upregulating the indoleamine 2,3-dioxygenase 1 (IDO1) enzyme1-4. Tryptophan 73-83 indoleamine 2,3-dioxygenase 1 Homo sapiens 144-148 35173722-2 2022 Three cytosolic enzymes, namely indoleamine 2,3-dioxygenase 1 (IDO1), IDO2 and tryptophan 2,3-dioxygenase (TDO2), catalyzes the first-rate limiting step of the degradation of Trp to kynurenine (Kyn) and modulates immunity toward immunosuppression mainly through the aryl hydrocarbon receptor (AhR) activation in numerous types of cancer. Tryptophan 175-178 indoleamine 2,3-dioxygenase 1 Homo sapiens 32-61 35173722-2 2022 Three cytosolic enzymes, namely indoleamine 2,3-dioxygenase 1 (IDO1), IDO2 and tryptophan 2,3-dioxygenase (TDO2), catalyzes the first-rate limiting step of the degradation of Trp to kynurenine (Kyn) and modulates immunity toward immunosuppression mainly through the aryl hydrocarbon receptor (AhR) activation in numerous types of cancer. Tryptophan 175-178 indoleamine 2,3-dioxygenase 1 Homo sapiens 63-67 2553814-1 1989 Indoleamine 2,3-dioxygenase (IDO) is a flavin-dependent enzyme which uses superoxide anion as a cosubstrate to catalyze the decyclization of the pyrrole ring of L-tryptophan to form formylkynurenine. Tryptophan 161-173 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 35057467-3 2022 An association between the induction of the tryptophan catabolic pathway via indoleamine 2,3-dioxygenase (IDO) activity and obesity-related inflammation has been observed. Tryptophan 44-54 indoleamine 2,3-dioxygenase 1 Homo sapiens 77-104 35057467-3 2022 An association between the induction of the tryptophan catabolic pathway via indoleamine 2,3-dioxygenase (IDO) activity and obesity-related inflammation has been observed. Tryptophan 44-54 indoleamine 2,3-dioxygenase 1 Homo sapiens 106-109 35057467-5 2022 In this prospective cohort study, plasma kynurenine, tryptophan, and serotonin levels were measured by ELISA, and IDO activity was estimated by calculating the kynurenine/tryptophan ratio in a clinically characterized population with severe obesity (BMI >= 97th percentile) aged 9 to 19 (n = 125). Tryptophan 171-181 indoleamine 2,3-dioxygenase 1 Homo sapiens 114-117 34269660-7 2022 IFN-gamma upregulates the enzyme indoleamine 2,3-dioxygenase (IDO), decreasing serum levels of the Trp and increasing metabolite levels of kynurenine. Tryptophan 99-102 indoleamine 2,3-dioxygenase 1 Homo sapiens 33-60 34269660-7 2022 IFN-gamma upregulates the enzyme indoleamine 2,3-dioxygenase (IDO), decreasing serum levels of the Trp and increasing metabolite levels of kynurenine. Tryptophan 99-102 indoleamine 2,3-dioxygenase 1 Homo sapiens 62-65 35045867-3 2022 The serum levels of tryptophan (Trp) and its metabolites, IDO1 and IDO2 mRNA levels, and the relationship of IDO1 and IDO2 SNPs with the serum Kyn/Trp ratio in TB patients and healthy controls were examined by LC/ESI-MS/MS analysis. Tryptophan 147-150 indoleamine 2,3-dioxygenase 1 Homo sapiens 109-113 35045867-5 2022 RESULTS: In Chinese Han participants, only IDO2 had SNPs R248W and Y359X that affected IDO activity, as determined by the serum Kyn/Trp ratio. Tryptophan 132-135 indoleamine 2,3-dioxygenase 1 Homo sapiens 87-90 2553814-1 1989 Indoleamine 2,3-dioxygenase (IDO) is a flavin-dependent enzyme which uses superoxide anion as a cosubstrate to catalyze the decyclization of the pyrrole ring of L-tryptophan to form formylkynurenine. Tryptophan 161-173 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 2472288-1 1989 Indoleamine 2,3-dioxygenase (IDO) is an interferon (IFN)-induced protein that initiates the metabolism of tryptophan along the kynurenine pathway. Tryptophan 106-116 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 2472288-1 1989 Indoleamine 2,3-dioxygenase (IDO) is an interferon (IFN)-induced protein that initiates the metabolism of tryptophan along the kynurenine pathway. Tryptophan 106-116 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 2443564-1 1987 Degradation of tryptophan to kynurenine, catalyzed by indoleamine 2,3-dioxygenase (IDO), has been augmented in human epithelial cell lines treated with human interferon-gamma (HuIFN-gamma). Tryptophan 15-25 indoleamine 2,3-dioxygenase 1 Homo sapiens 54-81 2463322-1 1989 Interferon (IFN)-induced tryptophan degradation, catalyzed by indoleamine 2,3-dioxygenase (IDO), has been shown to mediate antimicrobial activity in epithelial cells. Tryptophan 25-35 indoleamine 2,3-dioxygenase 1 Homo sapiens 62-89 2463322-1 1989 Interferon (IFN)-induced tryptophan degradation, catalyzed by indoleamine 2,3-dioxygenase (IDO), has been shown to mediate antimicrobial activity in epithelial cells. Tryptophan 25-35 indoleamine 2,3-dioxygenase 1 Homo sapiens 91-94 2785576-1 1989 Degradation of tryptophan to kynurenine, catalyzed by indoleamine 2,3-dioxygenase (IDO), has been shown previously to be augmented in human peripheral blood mononuclear cells (PBMCs) treated in vitro with interferons-alpha, -beta, and -gamma (IFNs), and in human epithelial cells treated with IFN-gamma. Tryptophan 15-25 indoleamine 2,3-dioxygenase 1 Homo sapiens 54-81 2785576-1 1989 Degradation of tryptophan to kynurenine, catalyzed by indoleamine 2,3-dioxygenase (IDO), has been shown previously to be augmented in human peripheral blood mononuclear cells (PBMCs) treated in vitro with interferons-alpha, -beta, and -gamma (IFNs), and in human epithelial cells treated with IFN-gamma. Tryptophan 15-25 indoleamine 2,3-dioxygenase 1 Homo sapiens 83-86 2443564-1 1987 Degradation of tryptophan to kynurenine, catalyzed by indoleamine 2,3-dioxygenase (IDO), has been augmented in human epithelial cell lines treated with human interferon-gamma (HuIFN-gamma). Tryptophan 15-25 indoleamine 2,3-dioxygenase 1 Homo sapiens 83-86 2443564-8 1987 Furthermore, T24 bladder carcinoma cells, in which IDO was induced by HuIFN-gamma but not by the other biologic response modifiers, were induced to degrade tryptophan by supernatants of HuIL-2-stimulated PMC cultures, but not by HuIFN-beta-stimulated PMC culture supernatants. Tryptophan 156-166 indoleamine 2,3-dioxygenase 1 Homo sapiens 51-54 2428037-0 1986 Interferon enhances tryptophan metabolism by inducing pulmonary indoleamine 2,3-dioxygenase: its possible occurrence in cancer patients. Tryptophan 20-30 indoleamine 2,3-dioxygenase 1 Homo sapiens 64-91 2428037-5 1986 IDO thus induced in slices avidly metabolized tryptophan in situ: Upon a 24-hr incubation of lung slices pretreated with varied doses of IFN-gamma (10-10(3) units/ml), up to 96% of the tryptophan in the slices was depleted and up to 70% of the tryptophan in the medium was converted, mainly to formylkynurenine, kynurenine, or both. Tryptophan 46-56 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 2428037-5 1986 IDO thus induced in slices avidly metabolized tryptophan in situ: Upon a 24-hr incubation of lung slices pretreated with varied doses of IFN-gamma (10-10(3) units/ml), up to 96% of the tryptophan in the slices was depleted and up to 70% of the tryptophan in the medium was converted, mainly to formylkynurenine, kynurenine, or both. Tryptophan 185-195 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 2428037-5 1986 IDO thus induced in slices avidly metabolized tryptophan in situ: Upon a 24-hr incubation of lung slices pretreated with varied doses of IFN-gamma (10-10(3) units/ml), up to 96% of the tryptophan in the slices was depleted and up to 70% of the tryptophan in the medium was converted, mainly to formylkynurenine, kynurenine, or both. Tryptophan 185-195 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 2428037-6 1986 The foregoing results suggest that an IFN-mediated induction of IDO also takes place in vivo in human lungs as a response to cancer, leading to metabolic consequences such as depletion of tryptophan and accumulation of (formyl)kynurenine, which may provide a unique host defense mechanism. Tryptophan 188-198 indoleamine 2,3-dioxygenase 1 Homo sapiens 64-67 33711443-1 2021 Indoleamine 2,3-dioxygenase (IDO1) and tryptophane 2,3-dioxygenase (TDO) are two heme-containing enzymes which catalyze the conversion of tryptophan to N-formylkynurenine. Tryptophan 39-49 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-33 33901770-1 2021 The expression of tryptophan catabolising enzyme indoleamine 2,3-dioxygenase 1 (IDO1) or tryptophan 2,3-dioxygenase 2 (TDO2) in cancers is associated with suppressed immunity and poor patient prognosis. Tryptophan 18-28 indoleamine 2,3-dioxygenase 1 Homo sapiens 49-78 33901770-1 2021 The expression of tryptophan catabolising enzyme indoleamine 2,3-dioxygenase 1 (IDO1) or tryptophan 2,3-dioxygenase 2 (TDO2) in cancers is associated with suppressed immunity and poor patient prognosis. Tryptophan 18-28 indoleamine 2,3-dioxygenase 1 Homo sapiens 80-84 34053179-2 2021 The intracellular enzyme indoleamine 2,3-dioxygenase (IDO) is a critical regulator of the tumour microenvironment (TME) via tryptophan metabolism. Tryptophan 124-134 indoleamine 2,3-dioxygenase 1 Homo sapiens 54-57 33741464-1 2021 Human indoleamine 2,3-dioxygenase 1 (hIDO1) and tryptophan dioxygenase (hTDO) are rate-limiting enzymes in the kynurenine pathway (KP) of L-tryptophan (L-Trp) metabolism and are becoming key drug targets in the combination therapy of checkpoint inhibitors in immunoncology. Tryptophan 138-150 indoleamine 2,3-dioxygenase 1 Homo sapiens 6-35 33741464-1 2021 Human indoleamine 2,3-dioxygenase 1 (hIDO1) and tryptophan dioxygenase (hTDO) are rate-limiting enzymes in the kynurenine pathway (KP) of L-tryptophan (L-Trp) metabolism and are becoming key drug targets in the combination therapy of checkpoint inhibitors in immunoncology. Tryptophan 138-150 indoleamine 2,3-dioxygenase 1 Homo sapiens 37-42 33741464-1 2021 Human indoleamine 2,3-dioxygenase 1 (hIDO1) and tryptophan dioxygenase (hTDO) are rate-limiting enzymes in the kynurenine pathway (KP) of L-tryptophan (L-Trp) metabolism and are becoming key drug targets in the combination therapy of checkpoint inhibitors in immunoncology. Tryptophan 152-157 indoleamine 2,3-dioxygenase 1 Homo sapiens 6-35 33741464-1 2021 Human indoleamine 2,3-dioxygenase 1 (hIDO1) and tryptophan dioxygenase (hTDO) are rate-limiting enzymes in the kynurenine pathway (KP) of L-tryptophan (L-Trp) metabolism and are becoming key drug targets in the combination therapy of checkpoint inhibitors in immunoncology. Tryptophan 152-157 indoleamine 2,3-dioxygenase 1 Homo sapiens 37-42 33243840-0 2021 Decreased IDO1 Dependent Tryptophan Metabolism in Aged Lung during Influenza. Tryptophan 25-35 indoleamine 2,3-dioxygenase 1 Homo sapiens 10-14 33831358-0 2021 Immune-regulated IDO1-dependent tryptophan metabolism is source of one-carbon units for pancreatic cancer and stellate cells. Tryptophan 32-42 indoleamine 2,3-dioxygenase 1 Homo sapiens 17-21 33984619-1 2021 Indoleamine 2,3-deoxygenase (IDO) produced by cancer cells catabolizes tryptophan (TRP) to kynurenine (KYN) in the environment, resulting induction of cancer immune escape through induction of T cell anergy and enhancement of regulatory T cells. Tryptophan 71-81 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 33984619-1 2021 Indoleamine 2,3-deoxygenase (IDO) produced by cancer cells catabolizes tryptophan (TRP) to kynurenine (KYN) in the environment, resulting induction of cancer immune escape through induction of T cell anergy and enhancement of regulatory T cells. Tryptophan 83-86 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 33984619-10 2021 The ratio of KYN/TRP, widely considered to represent IDO activity, was also significantly elevated. Tryptophan 17-20 indoleamine 2,3-dioxygenase 1 Homo sapiens 53-56 33984619-11 2021 Moreover, treatment with an IDO inhibitor L-1-methyl-tryptophan (L-1MT) clearly diminished the elevation of KYN/TRP ratio induced by the incubation with canine MCT cells. Tryptophan 112-115 indoleamine 2,3-dioxygenase 1 Homo sapiens 28-31 33984619-12 2021 Our results indicate that canine MCT cells could directly regulate the concentrations of TRP and KYN through expressing IDO, suggesting that canine MCT have an immune escape ability. Tryptophan 89-92 indoleamine 2,3-dioxygenase 1 Homo sapiens 120-123 33922388-1 2021 The enzyme indoleamine 2,3-dioxygenase 1 (IDO1) degrade tryptophan (Trp) into kynurenine (Kyn) at the initial step of an enzymatic pathway affecting T cell proliferation. Tryptophan 56-66 indoleamine 2,3-dioxygenase 1 Homo sapiens 11-40 33922388-1 2021 The enzyme indoleamine 2,3-dioxygenase 1 (IDO1) degrade tryptophan (Trp) into kynurenine (Kyn) at the initial step of an enzymatic pathway affecting T cell proliferation. Tryptophan 56-66 indoleamine 2,3-dioxygenase 1 Homo sapiens 42-46 33922388-1 2021 The enzyme indoleamine 2,3-dioxygenase 1 (IDO1) degrade tryptophan (Trp) into kynurenine (Kyn) at the initial step of an enzymatic pathway affecting T cell proliferation. Tryptophan 68-71 indoleamine 2,3-dioxygenase 1 Homo sapiens 11-40 33922388-1 2021 The enzyme indoleamine 2,3-dioxygenase 1 (IDO1) degrade tryptophan (Trp) into kynurenine (Kyn) at the initial step of an enzymatic pathway affecting T cell proliferation. Tryptophan 68-71 indoleamine 2,3-dioxygenase 1 Homo sapiens 42-46 33883013-1 2021 Indoleamine 2,3-dioxygenase 1 (IDO1) is a heme enzyme that catalyzes the oxidation of L-tryptophan. Tryptophan 86-98 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-29 33883013-1 2021 Indoleamine 2,3-dioxygenase 1 (IDO1) is a heme enzyme that catalyzes the oxidation of L-tryptophan. Tryptophan 86-98 indoleamine 2,3-dioxygenase 1 Homo sapiens 31-35 33622713-2 2021 The tryptophan catabolizing enzyme IDO1 (indoleamine 2,3-dioxygenase) has been implicated in promoting neovascularization through its positioning as a key regulatory node between the inflammatory cytokines IFNgamma and IL6. Tryptophan 4-14 indoleamine 2,3-dioxygenase 1 Homo sapiens 35-39 33905074-1 2021 Indoleamine 2,3-dioxygenase 1 (IDO1) is a heme-containing enzyme that catalyzes the first and rate-limiting step in catabolism of tryptophan via the kynurenine pathway, which plays a pivotal role in the proliferation and differentiation of T cells. Tryptophan 130-140 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-29 33905074-1 2021 Indoleamine 2,3-dioxygenase 1 (IDO1) is a heme-containing enzyme that catalyzes the first and rate-limiting step in catabolism of tryptophan via the kynurenine pathway, which plays a pivotal role in the proliferation and differentiation of T cells. Tryptophan 130-140 indoleamine 2,3-dioxygenase 1 Homo sapiens 31-35 33968089-6 2021 Accumulating evidence indicates that IDO2 is much less effective than IDO1 in metabolizing Trp and its functions are rather the consequence of interaction with other, still undefined proteins that may vary in distinct inflammatory and neoplastic contexts. Tryptophan 91-94 indoleamine 2,3-dioxygenase 1 Homo sapiens 70-74 33346015-9 2021 Thus, a depletion of TRP via an ICCGs-inflammatory IDO activation is not likely in MDD. Tryptophan 21-24 indoleamine 2,3-dioxygenase 1 Homo sapiens 51-54 33875612-2 2021 Indoleamine 2,3 dioxygenase (IDO) catabolizes tryptophan (T) to kynurenine (K), regulating immune activity, and IDO activity increases with age. Tryptophan 46-56 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 33875612-2 2021 Indoleamine 2,3 dioxygenase (IDO) catabolizes tryptophan (T) to kynurenine (K), regulating immune activity, and IDO activity increases with age. Tryptophan 46-56 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 33831358-4 2021 Tryptophan is a theoretical source of one-carbon units through metabolism by IDO1, an enzyme intensively investigated in the context of tumor immune evasion. Tryptophan 0-10 indoleamine 2,3-dioxygenase 1 Homo sapiens 77-81 33831358-6 2021 In IDO1-expressing cancer cells, tryptophan is a bona fide one-carbon donor for purine nucleotide synthesis in vitro and in vivo. Tryptophan 33-43 indoleamine 2,3-dioxygenase 1 Homo sapiens 3-7 32794357-5 2021 RESULTS: We established for the first time that plasma TRP level was significantly decreased while both plasma and urinary KYN/TRP ratios were significantly higher in bladder cancer patients and expression level of IDO1 but not TDO2 was increased in human bladder tumor. Tryptophan 55-58 indoleamine 2,3-dioxygenase 1 Homo sapiens 215-219 32794357-5 2021 RESULTS: We established for the first time that plasma TRP level was significantly decreased while both plasma and urinary KYN/TRP ratios were significantly higher in bladder cancer patients and expression level of IDO1 but not TDO2 was increased in human bladder tumor. Tryptophan 127-130 indoleamine 2,3-dioxygenase 1 Homo sapiens 215-219 33557523-1 2021 The heme enzyme indoleamine 2,3-dioxygenase 1 (IDO1) plays an essential role in immunity, neuronal function, and aging through catalysis of the rate-limiting step in the kynurenine pathway of tryptophan metabolism. Tryptophan 192-202 indoleamine 2,3-dioxygenase 1 Homo sapiens 16-45 33707952-1 2021 Purpose: Indolamine 2,3-dioxygenase (IDO) is the rate limiting enzyme of tryptophan degradation and is a negative prognostic factor in oral squamous cell carcinoma (OSCC) patients, while the underlying molecular mechanism remains unclear. Tryptophan 73-83 indoleamine 2,3-dioxygenase 1 Homo sapiens 9-35 33707952-1 2021 Purpose: Indolamine 2,3-dioxygenase (IDO) is the rate limiting enzyme of tryptophan degradation and is a negative prognostic factor in oral squamous cell carcinoma (OSCC) patients, while the underlying molecular mechanism remains unclear. Tryptophan 73-83 indoleamine 2,3-dioxygenase 1 Homo sapiens 37-40 33460767-2 2021 The majority of free Trp is broken down through the kynurenine (Kyn) pathway (KP), in which indoleamine-2,3-dioxygenase (IDO) and tryptophan-2,3-dioxygenase (TDO) catalyze the rate-limiting step. Tryptophan 21-24 indoleamine 2,3-dioxygenase 1 Homo sapiens 92-119 33460767-2 2021 The majority of free Trp is broken down through the kynurenine (Kyn) pathway (KP), in which indoleamine-2,3-dioxygenase (IDO) and tryptophan-2,3-dioxygenase (TDO) catalyze the rate-limiting step. Tryptophan 21-24 indoleamine 2,3-dioxygenase 1 Homo sapiens 121-124 33460767-5 2021 Various signaling molecules control IDO expression, initiating the immunoregulatory pathway of Trp catabolism. Tryptophan 95-98 indoleamine 2,3-dioxygenase 1 Homo sapiens 36-39 33410234-1 2021 Indoleamine 2,3-dioxygenase 1 (IDO1) is a key enzyme associated with immunomodulation through its regulation of the tryptophan-kynurenine (Kyn) pathway in advanced cancers, including metastatic renal cell carcinoma (mRCC). Tryptophan 116-126 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-29 33410234-1 2021 Indoleamine 2,3-dioxygenase 1 (IDO1) is a key enzyme associated with immunomodulation through its regulation of the tryptophan-kynurenine (Kyn) pathway in advanced cancers, including metastatic renal cell carcinoma (mRCC). Tryptophan 116-126 indoleamine 2,3-dioxygenase 1 Homo sapiens 31-35 33427761-4 2021 We recently showed that in systemic inflammation and oxidative stress associated with models of inflammation including sepsis, the tryptophan catabolizing enzyme indoleamine 2,3-dioxygenase-1 (Ido1) contributes to hypotension and decreased blood pressure through production of singlet molecular oxygen (1O2). Tryptophan 131-141 indoleamine 2,3-dioxygenase 1 Homo sapiens 162-191 33427761-4 2021 We recently showed that in systemic inflammation and oxidative stress associated with models of inflammation including sepsis, the tryptophan catabolizing enzyme indoleamine 2,3-dioxygenase-1 (Ido1) contributes to hypotension and decreased blood pressure through production of singlet molecular oxygen (1O2). Tryptophan 131-141 indoleamine 2,3-dioxygenase 1 Homo sapiens 193-197 33427761-5 2021 Once formed, 1O2 converts tryptophan bound to Ido1 to a vasoactive hydroperoxide which decreases arterial tone and blood pressure via oxidation of a specific cysteine residue of protein kinase G1alpha. Tryptophan 26-36 indoleamine 2,3-dioxygenase 1 Homo sapiens 46-50 33427761-6 2021 SUMMARY: These works show, for the first time, that 1O2 contributes to arterial redox signalling and that Ido1 contributes to the regulation of blood pressure through production of a novel tryptophan-derived hydroperoxide, thus presenting a new signalling pathway as novel target in the treatment of blood pressure disorders such as sepsis. Tryptophan 189-199 indoleamine 2,3-dioxygenase 1 Homo sapiens 106-110 33737337-8 2021 We demonstrate that Indoleamine-pyrrole 2,3-dioxygenase1 (IDO1), due to its ability to convert tryptophan into kynurenines, is involved in NB resistance to activity of immune cells. Tryptophan 95-105 indoleamine 2,3-dioxygenase 1 Homo sapiens 20-56 33737337-8 2021 We demonstrate that Indoleamine-pyrrole 2,3-dioxygenase1 (IDO1), due to its ability to convert tryptophan into kynurenines, is involved in NB resistance to activity of immune cells. Tryptophan 95-105 indoleamine 2,3-dioxygenase 1 Homo sapiens 58-62 33718949-2 2021 Plasma indoleamine 2,3-dioxygenase (IDO) activity, measured by kynurenine-to-tryptophan (K/T) ratio has been proposed as a blood-based TB biomarker. Tryptophan 77-87 indoleamine 2,3-dioxygenase 1 Homo sapiens 7-34 33718949-2 2021 Plasma indoleamine 2,3-dioxygenase (IDO) activity, measured by kynurenine-to-tryptophan (K/T) ratio has been proposed as a blood-based TB biomarker. Tryptophan 77-87 indoleamine 2,3-dioxygenase 1 Homo sapiens 36-39 33686747-3 2021 IDO1 is a high-affinity Trp-degrading enzyme involved in several physiological processes. Tryptophan 24-27 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-4 33686747-10 2021 Our results shed new light in the enzymatic activity of IDO2 and they support the view that this isoform of IDO also participates in the metabolism of Trp in vivo. Tryptophan 151-154 indoleamine 2,3-dioxygenase 1 Homo sapiens 56-59 33675038-2 2021 Regulation of T cell induction by DCs may occur via the intracellular enzyme indoleamine 2,3-dioxygenase 1 (IDO), which catalyzes conversion of the essential amino acid tryptophan into kynurenine. Tryptophan 169-179 indoleamine 2,3-dioxygenase 1 Homo sapiens 77-106 33675038-2 2021 Regulation of T cell induction by DCs may occur via the intracellular enzyme indoleamine 2,3-dioxygenase 1 (IDO), which catalyzes conversion of the essential amino acid tryptophan into kynurenine. Tryptophan 169-179 indoleamine 2,3-dioxygenase 1 Homo sapiens 108-111 33557523-1 2021 The heme enzyme indoleamine 2,3-dioxygenase 1 (IDO1) plays an essential role in immunity, neuronal function, and aging through catalysis of the rate-limiting step in the kynurenine pathway of tryptophan metabolism. Tryptophan 192-202 indoleamine 2,3-dioxygenase 1 Homo sapiens 47-51 33708223-0 2021 Tryptophan: A Rheostat of Cancer Immune Escape Mediated by Immunosuppressive Enzymes IDO1 and TDO. Tryptophan 0-10 indoleamine 2,3-dioxygenase 1 Homo sapiens 85-89 33708223-1 2021 Blockade of the immunosuppressive tryptophan catabolism mediated by indoleamine 2,3-dioxygenase 1 (IDO1) and tryptophan 2,3-dioxygenase (TDO) holds enormous promise for sensitising cancer patients to immune checkpoint blockade. Tryptophan 34-44 indoleamine 2,3-dioxygenase 1 Homo sapiens 68-97 33708223-1 2021 Blockade of the immunosuppressive tryptophan catabolism mediated by indoleamine 2,3-dioxygenase 1 (IDO1) and tryptophan 2,3-dioxygenase (TDO) holds enormous promise for sensitising cancer patients to immune checkpoint blockade. Tryptophan 34-44 indoleamine 2,3-dioxygenase 1 Homo sapiens 99-103 33557876-2 2021 Indoleamine 2,3-dioxygenase 1 (IDO1), a monomeric heme-containing enzyme, catalyzes the first and rate-limiting step in the kynurenine pathway of tryptophan metabolism, which plays an important role in immunity and neuronal function. Tryptophan 146-156 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-29 33557876-2 2021 Indoleamine 2,3-dioxygenase 1 (IDO1), a monomeric heme-containing enzyme, catalyzes the first and rate-limiting step in the kynurenine pathway of tryptophan metabolism, which plays an important role in immunity and neuronal function. Tryptophan 146-156 indoleamine 2,3-dioxygenase 1 Homo sapiens 31-35 33422134-14 2021 Mechanistically, the tryptophan metabolites, kynurenine (KYN) or kynurenic acid (KYNA) produced by IDO, augmented the expression of TSG-6 through activating their common receptor aryl hydrocarbon receptor (AHR). Tryptophan 21-31 indoleamine 2,3-dioxygenase 1 Homo sapiens 99-102 33373218-1 2021 Human indoleamine 2,3-dioxygenase 1 (hIDO1) and human tryptophan dioxygenase (hTDO) are two important heme proteins that degrade the essential amino acid, l-tryptophan (Trp), along the kynurenine pathway. Tryptophan 155-167 indoleamine 2,3-dioxygenase 1 Homo sapiens 6-35 33373218-1 2021 Human indoleamine 2,3-dioxygenase 1 (hIDO1) and human tryptophan dioxygenase (hTDO) are two important heme proteins that degrade the essential amino acid, l-tryptophan (Trp), along the kynurenine pathway. Tryptophan 155-167 indoleamine 2,3-dioxygenase 1 Homo sapiens 37-42 33373218-1 2021 Human indoleamine 2,3-dioxygenase 1 (hIDO1) and human tryptophan dioxygenase (hTDO) are two important heme proteins that degrade the essential amino acid, l-tryptophan (Trp), along the kynurenine pathway. Tryptophan 169-172 indoleamine 2,3-dioxygenase 1 Homo sapiens 6-35 33373218-1 2021 Human indoleamine 2,3-dioxygenase 1 (hIDO1) and human tryptophan dioxygenase (hTDO) are two important heme proteins that degrade the essential amino acid, l-tryptophan (Trp), along the kynurenine pathway. Tryptophan 169-172 indoleamine 2,3-dioxygenase 1 Homo sapiens 37-42 32974990-1 2021 Indoleamine-2,3-dioxygenase 1 (IDO1) is a heme-containing enzyme that catalyzes the rate-limiting step in the kynurenine pathway of tryptophan (TRP) metabolism. Tryptophan 132-142 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-29 32974990-1 2021 Indoleamine-2,3-dioxygenase 1 (IDO1) is a heme-containing enzyme that catalyzes the rate-limiting step in the kynurenine pathway of tryptophan (TRP) metabolism. Tryptophan 132-142 indoleamine 2,3-dioxygenase 1 Homo sapiens 31-35 32974990-1 2021 Indoleamine-2,3-dioxygenase 1 (IDO1) is a heme-containing enzyme that catalyzes the rate-limiting step in the kynurenine pathway of tryptophan (TRP) metabolism. Tryptophan 144-147 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-29 32974990-1 2021 Indoleamine-2,3-dioxygenase 1 (IDO1) is a heme-containing enzyme that catalyzes the rate-limiting step in the kynurenine pathway of tryptophan (TRP) metabolism. Tryptophan 144-147 indoleamine 2,3-dioxygenase 1 Homo sapiens 31-35 33333163-2 2021 Drug candidates targeting IDO1, a key enzyme in tryptophan metabolism, are currently under clinical investigation in combination with PD-1/PD-L1 agents as well as with other established anti-tumor therapeutics. Tryptophan 48-58 indoleamine 2,3-dioxygenase 1 Homo sapiens 26-30 33542896-2 2020 Kyn, the main product of Trp metabolism pathway catalyzed by TDO2 and indoleamine 2,3-dioxygenase (IDO) in tumor cells, was also demonstrated to activate aryl hydrocarbon receptor (AhR), which may regulate cancer growth and invasion in some malignancies. Tryptophan 25-28 indoleamine 2,3-dioxygenase 1 Homo sapiens 70-97 33542896-2 2020 Kyn, the main product of Trp metabolism pathway catalyzed by TDO2 and indoleamine 2,3-dioxygenase (IDO) in tumor cells, was also demonstrated to activate aryl hydrocarbon receptor (AhR), which may regulate cancer growth and invasion in some malignancies. Tryptophan 25-28 indoleamine 2,3-dioxygenase 1 Homo sapiens 99-102 33422142-12 2021 A significant increase in the kynurenine/tryptophan ratio suggests that this may be a result of a shift to the kynurenine metabolic route due to increased IDO activity, potentially as a result of systemic inflammation. Tryptophan 41-51 indoleamine 2,3-dioxygenase 1 Homo sapiens 155-158 33418116-4 2021 IDO1 regulates immune cell function through the kynurenine pathway but also by depleting tryptophan in microenvironments, and especially in tumors, which led to the development of IDO1 inhibitors for cancer therapy. Tryptophan 89-99 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-4 33418116-4 2021 IDO1 regulates immune cell function through the kynurenine pathway but also by depleting tryptophan in microenvironments, and especially in tumors, which led to the development of IDO1 inhibitors for cancer therapy. Tryptophan 89-99 indoleamine 2,3-dioxygenase 1 Homo sapiens 180-184 33539022-3 2021 In contrast, IDO is constitutively expressed by various tumors and creates an immunosuppressive microenvironment around the tumor tissue both by depletion of the essential amino acid Trp and by formation of Kyn, which is immunosuppressive metabolite of Trp. Tryptophan 183-186 indoleamine 2,3-dioxygenase 1 Homo sapiens 13-16 33539022-3 2021 In contrast, IDO is constitutively expressed by various tumors and creates an immunosuppressive microenvironment around the tumor tissue both by depletion of the essential amino acid Trp and by formation of Kyn, which is immunosuppressive metabolite of Trp. Tryptophan 253-256 indoleamine 2,3-dioxygenase 1 Homo sapiens 13-16 33539025-1 2021 The tryptophan catabolizing enzyme indoleamine 2,3-dioxygenase (IDO-1) has gained major attention due the immunoregulatory nature of this pathway. Tryptophan 4-14 indoleamine 2,3-dioxygenase 1 Homo sapiens 64-69 33390854-8 2021 IFN-gamma treatment and IDO1 overexpression promoted tryptophan depletion and kynurenine accumulation in cervical cancer cells. Tryptophan 53-63 indoleamine 2,3-dioxygenase 1 Homo sapiens 24-28 32707579-8 2021 Supervised resistance exercise might positively regulate the Kynurenine pathway and downregulate the kynurenine/tryptophan (indicative of IDO/TDO enzyme) levels, hence modulating the immune system. Tryptophan 112-122 indoleamine 2,3-dioxygenase 1 Homo sapiens 138-141 33298590-2 2021 Activated IDO1 metabolizes tryptophan into immunosuppressive kynurenine, leading to suppressed effector T-cell (Teff) proliferation, allowing for tumor escape from host immune surveillance. Tryptophan 27-37 indoleamine 2,3-dioxygenase 1 Homo sapiens 10-14 33328638-3 2021 One such mechanism is the production of tryptophan metabolites along the kynurenine pathway by the enzyme indoleamine 2,3-dioxygenase 1 (IDO1), which is induced by IFNgamma3-5. Tryptophan 40-50 indoleamine 2,3-dioxygenase 1 Homo sapiens 106-135 33328638-3 2021 One such mechanism is the production of tryptophan metabolites along the kynurenine pathway by the enzyme indoleamine 2,3-dioxygenase 1 (IDO1), which is induced by IFNgamma3-5. Tryptophan 40-50 indoleamine 2,3-dioxygenase 1 Homo sapiens 137-141 33328638-11 2021 Together, our results suggest that IDO1-mediated depletion of tryptophan, which is induced by IFNgamma, has a role in the immune recognition of melanoma cells by contributing to diversification of the peptidome landscape. Tryptophan 62-72 indoleamine 2,3-dioxygenase 1 Homo sapiens 35-39 33584686-1 2020 Indoleamine 2,3-dioxygenase (IDO1) is a key regulator of immune suppression by catalyzing the oxidation of L-tryptophan. Tryptophan 107-119 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-33 33552055-10 2020 Tryptophan is catabolized through 2,3-dioxygenase (TDO) and indoleamine 2,3-dioxygenase (IDO) 1 and IDO2 enzymes, while three other enzymes catabolize Arg: inducible nitric oxide synthetase (iNOS), and two arginase isoforms (ARG1, ARG2). Tryptophan 0-10 indoleamine 2,3-dioxygenase 1 Homo sapiens 60-95 33447047-1 2020 Immunohistochemical localization of indoleamine 2,3-dioxygenase-1 and indoleamine 2,3-dioxygenase-2, the first and rate-limiting enzyme in tryptophan metabolism along the kynurenine pathway, has been studied in order to better understand the physiological significance of these enzymes at the maternal-fetal interface of human pregnancy with a gestational age of 7 weeks (n = 1) and term placentas (37-40 weeks of gestation, n = 5). Tryptophan 139-149 indoleamine 2,3-dioxygenase 1 Homo sapiens 36-65 33025106-6 2021 Moreover, immunosuppressive cells suppress the function of effector immune cells by catabolizing L-arginine and tryptophan through the activation of arginase 1 (ARG1) and indoleamine 2,3-dioxygenase (IDO), respectively. Tryptophan 112-122 indoleamine 2,3-dioxygenase 1 Homo sapiens 171-198 33025106-6 2021 Moreover, immunosuppressive cells suppress the function of effector immune cells by catabolizing L-arginine and tryptophan through the activation of arginase 1 (ARG1) and indoleamine 2,3-dioxygenase (IDO), respectively. Tryptophan 112-122 indoleamine 2,3-dioxygenase 1 Homo sapiens 200-203 33569314-10 2021 Deregulated IDO activity was validated by additional HPLC measurements, which revealed that baseline Trp levels were predictive for CI response. Tryptophan 101-104 indoleamine 2,3-dioxygenase 1 Homo sapiens 12-15 33569314-15 2021 Trp as a surrogate parameter of IDO activity is a promising biomarker in patients undergoing treatment with CIs and might be a future marker in trials investigating IDO inhibitors. Tryptophan 0-3 indoleamine 2,3-dioxygenase 1 Homo sapiens 32-35 33569314-15 2021 Trp as a surrogate parameter of IDO activity is a promising biomarker in patients undergoing treatment with CIs and might be a future marker in trials investigating IDO inhibitors. Tryptophan 0-3 indoleamine 2,3-dioxygenase 1 Homo sapiens 165-168 33362375-14 2020 IDO1 mRNA levels were positively associated with the KYN/Trp ratio (r = 0.327, P = 0.003). Tryptophan 57-60 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-4 33159421-2 2020 Indoleamine 2,3-dioxygenase 1 (IDO1) is a cytosolic enzyme that controls immune responses via tryptophan metabolism, mainly through its enzymic activity. Tryptophan 94-104 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-29 33159421-2 2020 Indoleamine 2,3-dioxygenase 1 (IDO1) is a cytosolic enzyme that controls immune responses via tryptophan metabolism, mainly through its enzymic activity. Tryptophan 94-104 indoleamine 2,3-dioxygenase 1 Homo sapiens 31-35 33055013-4 2020 IDO1 converts l-tryptophan into metabolites, collectively known as kynurenines, endowed with several immunoregulatory effects via activation of the arylhydrocarbon receptor (AhR). Tryptophan 14-26 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-4 33539022-2 2021 IDO-mediated degradation of tryptophan (Trp) along the kynurenine (Kyn) pathway by immune cells is associated with the anti-microbial, and anti-tumor defense mechanisms. Tryptophan 28-38 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 33539022-2 2021 IDO-mediated degradation of tryptophan (Trp) along the kynurenine (Kyn) pathway by immune cells is associated with the anti-microbial, and anti-tumor defense mechanisms. Tryptophan 40-43 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 32976029-2 2020 IDO is the rate-limiting step in tryptophan metabolism catabolism into its byproducts - kynurenines. Tryptophan 33-43 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 32940915-1 2020 The enzyme, indoleamine 2,3-dioxygenase 1 (IDO), catabolizes tryptophan (Trp) in the kynurenine (Kyn) pathway, and is important in suppressing antitumor immune responses in the tumor microenvironment. Tryptophan 61-71 indoleamine 2,3-dioxygenase 1 Homo sapiens 12-41 32940915-1 2020 The enzyme, indoleamine 2,3-dioxygenase 1 (IDO), catabolizes tryptophan (Trp) in the kynurenine (Kyn) pathway, and is important in suppressing antitumor immune responses in the tumor microenvironment. Tryptophan 61-71 indoleamine 2,3-dioxygenase 1 Homo sapiens 43-46 32940915-1 2020 The enzyme, indoleamine 2,3-dioxygenase 1 (IDO), catabolizes tryptophan (Trp) in the kynurenine (Kyn) pathway, and is important in suppressing antitumor immune responses in the tumor microenvironment. Tryptophan 73-76 indoleamine 2,3-dioxygenase 1 Homo sapiens 12-41 32940915-1 2020 The enzyme, indoleamine 2,3-dioxygenase 1 (IDO), catabolizes tryptophan (Trp) in the kynurenine (Kyn) pathway, and is important in suppressing antitumor immune responses in the tumor microenvironment. Tryptophan 73-76 indoleamine 2,3-dioxygenase 1 Homo sapiens 43-46 32605792-1 2020 Indoleamine 2,3-dioxygenase 1 (IDO1) - the enzyme catalyzing the rate-limiting step of tryptophan catabolism along the kynurenine pathway - belongs to the class of inhibitory immune checkpoint molecules. Tryptophan 87-97 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-29 32605792-1 2020 Indoleamine 2,3-dioxygenase 1 (IDO1) - the enzyme catalyzing the rate-limiting step of tryptophan catabolism along the kynurenine pathway - belongs to the class of inhibitory immune checkpoint molecules. Tryptophan 87-97 indoleamine 2,3-dioxygenase 1 Homo sapiens 31-35 32776284-1 2020 PURPOSE: Indoleamine 2,3-dioxygenase-1 (IDO1) and more recently, tryptophan 2,3-dioxygenase (TDO), are tryptophan-catabolizing enzymes with immunoregulatory properties in cancer. Tryptophan 65-75 indoleamine 2,3-dioxygenase 1 Homo sapiens 9-38 32776284-1 2020 PURPOSE: Indoleamine 2,3-dioxygenase-1 (IDO1) and more recently, tryptophan 2,3-dioxygenase (TDO), are tryptophan-catabolizing enzymes with immunoregulatory properties in cancer. Tryptophan 65-75 indoleamine 2,3-dioxygenase 1 Homo sapiens 40-44 32466694-1 2020 Indoleamine 2,3-dioxygenase 1 (IDO1) as a key rate-limiting enzyme in the kynurenine pathway of tryptophan metabolism plays an important role in tumour immune escape. Tryptophan 96-106 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-29 32466694-1 2020 Indoleamine 2,3-dioxygenase 1 (IDO1) as a key rate-limiting enzyme in the kynurenine pathway of tryptophan metabolism plays an important role in tumour immune escape. Tryptophan 96-106 indoleamine 2,3-dioxygenase 1 Homo sapiens 31-35 33261077-1 2020 The novel high-affinity tryptophan (Trp)-selective transport system is present at elevated levels in human interferon-gamma (IFN-gamma)-treated and indoleamine 2,3-dioxygenase 1 (IDO1)-expressing cells. Tryptophan 24-34 indoleamine 2,3-dioxygenase 1 Homo sapiens 148-177 33261077-1 2020 The novel high-affinity tryptophan (Trp)-selective transport system is present at elevated levels in human interferon-gamma (IFN-gamma)-treated and indoleamine 2,3-dioxygenase 1 (IDO1)-expressing cells. Tryptophan 24-34 indoleamine 2,3-dioxygenase 1 Homo sapiens 179-183 33261077-1 2020 The novel high-affinity tryptophan (Trp)-selective transport system is present at elevated levels in human interferon-gamma (IFN-gamma)-treated and indoleamine 2,3-dioxygenase 1 (IDO1)-expressing cells. Tryptophan 36-39 indoleamine 2,3-dioxygenase 1 Homo sapiens 148-177 33261077-1 2020 The novel high-affinity tryptophan (Trp)-selective transport system is present at elevated levels in human interferon-gamma (IFN-gamma)-treated and indoleamine 2,3-dioxygenase 1 (IDO1)-expressing cells. Tryptophan 36-39 indoleamine 2,3-dioxygenase 1 Homo sapiens 179-183 33261077-4 2020 Here, we aimed to elucidate the relationship between TrpRS and IDO1 in high-affinity Trp uptake. Tryptophan 53-56 indoleamine 2,3-dioxygenase 1 Homo sapiens 63-67 33261077-5 2020 We demonstrated that overexpression of IDO1 in HeLa cells drastically enhances high-affinity Trp uptake upon addition of purified TrpRS protein to uptake assay buffer. Tryptophan 93-96 indoleamine 2,3-dioxygenase 1 Homo sapiens 39-43 33222028-2 2021 Tryptophan (Trp) is oxidized with tryptophan 2,3-dioxygenase and indolamine 2,3-dioxygenase (IDO). Tryptophan 0-10 indoleamine 2,3-dioxygenase 1 Homo sapiens 65-91 33222028-2 2021 Tryptophan (Trp) is oxidized with tryptophan 2,3-dioxygenase and indolamine 2,3-dioxygenase (IDO). Tryptophan 0-10 indoleamine 2,3-dioxygenase 1 Homo sapiens 93-96 33222028-2 2021 Tryptophan (Trp) is oxidized with tryptophan 2,3-dioxygenase and indolamine 2,3-dioxygenase (IDO). Tryptophan 12-15 indoleamine 2,3-dioxygenase 1 Homo sapiens 65-91 33222028-2 2021 Tryptophan (Trp) is oxidized with tryptophan 2,3-dioxygenase and indolamine 2,3-dioxygenase (IDO). Tryptophan 12-15 indoleamine 2,3-dioxygenase 1 Homo sapiens 93-96 33222028-4 2021 The ratio of Kyn to Trp can be used as an indicator to assess IDO activity. Tryptophan 20-23 indoleamine 2,3-dioxygenase 1 Homo sapiens 62-65 32987253-6 2020 Notably, indoleamine 2,3-dioxygenase 1 (IDO1) expression in tumour cells inversely correlated with circulating tryptophan levels but directly correlated with the level of eMDSCs. Tryptophan 111-121 indoleamine 2,3-dioxygenase 1 Homo sapiens 9-38 32987253-6 2020 Notably, indoleamine 2,3-dioxygenase 1 (IDO1) expression in tumour cells inversely correlated with circulating tryptophan levels but directly correlated with the level of eMDSCs. Tryptophan 111-121 indoleamine 2,3-dioxygenase 1 Homo sapiens 40-44 33118843-1 2020 Indoleamine 2, 3-dioxygenase (IDO) as an intracellular cytosolic enzyme converts tryptophan (Trp) to N-formyl kynurenine which leads to proinflammatory T-cell apoptosis and prevention of immune cells maturation via decreasing the level of cellular energy. Tryptophan 81-91 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-28 33118843-1 2020 Indoleamine 2, 3-dioxygenase (IDO) as an intracellular cytosolic enzyme converts tryptophan (Trp) to N-formyl kynurenine which leads to proinflammatory T-cell apoptosis and prevention of immune cells maturation via decreasing the level of cellular energy. Tryptophan 81-91 indoleamine 2,3-dioxygenase 1 Homo sapiens 30-33 33118843-1 2020 Indoleamine 2, 3-dioxygenase (IDO) as an intracellular cytosolic enzyme converts tryptophan (Trp) to N-formyl kynurenine which leads to proinflammatory T-cell apoptosis and prevention of immune cells maturation via decreasing the level of cellular energy. Tryptophan 93-96 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-28 33118843-1 2020 Indoleamine 2, 3-dioxygenase (IDO) as an intracellular cytosolic enzyme converts tryptophan (Trp) to N-formyl kynurenine which leads to proinflammatory T-cell apoptosis and prevention of immune cells maturation via decreasing the level of cellular energy. Tryptophan 93-96 indoleamine 2,3-dioxygenase 1 Homo sapiens 30-33 33040382-1 2021 The enzyme IDO-1 is involved in the first stage of tryptophan catabolism and has been described in both microbicidal and tolerogenic microenvironments. Tryptophan 51-61 indoleamine 2,3-dioxygenase 1 Homo sapiens 11-16 32435912-1 2020 Previous studies have pointed out that indoleamine 2,3-dioxygenase (IDO), the rate-limiting enzyme initiating tryptophan metabolism, plays a role in the regulation of the immune system. Tryptophan 110-120 indoleamine 2,3-dioxygenase 1 Homo sapiens 39-66 33037467-0 2020 Tryptophan conjugated magnetic nanoparticles for targeting tumors overexpressing indoleamine 2,3 dioxygenase (IDO) and L-type amino acid transporter. Tryptophan 0-10 indoleamine 2,3-dioxygenase 1 Homo sapiens 81-108 33037467-0 2020 Tryptophan conjugated magnetic nanoparticles for targeting tumors overexpressing indoleamine 2,3 dioxygenase (IDO) and L-type amino acid transporter. Tryptophan 0-10 indoleamine 2,3-dioxygenase 1 Homo sapiens 110-113 32435912-1 2020 Previous studies have pointed out that indoleamine 2,3-dioxygenase (IDO), the rate-limiting enzyme initiating tryptophan metabolism, plays a role in the regulation of the immune system. Tryptophan 110-120 indoleamine 2,3-dioxygenase 1 Homo sapiens 68-71 33061415-1 2020 Type 1 diabetes (T1D) is characterized by anomalous functioning of the immuno regulatory, tryptophan-catabolic enzyme indoleamine 2,3 dioxygenase 1 (IDO1). Tryptophan 90-100 indoleamine 2,3-dioxygenase 1 Homo sapiens 118-147 33061415-1 2020 Type 1 diabetes (T1D) is characterized by anomalous functioning of the immuno regulatory, tryptophan-catabolic enzyme indoleamine 2,3 dioxygenase 1 (IDO1). Tryptophan 90-100 indoleamine 2,3-dioxygenase 1 Homo sapiens 149-153 33072086-1 2020 Indoleamine 2,3-dioxygenase 1 (IDO1) is a cytosolic haem-containing enzyme involved in the degradation of tryptophan to kynurenine. Tryptophan 106-116 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-29 33072086-1 2020 Indoleamine 2,3-dioxygenase 1 (IDO1) is a cytosolic haem-containing enzyme involved in the degradation of tryptophan to kynurenine. Tryptophan 106-116 indoleamine 2,3-dioxygenase 1 Homo sapiens 31-35 32781018-5 2020 When stromal cells are treated with tryptophan, tryptophan hydroxylase-1 remains unchanged, but indoleamine 2,3-dioxygenase 1 is significantly increased, suggesting tryptophan is mainly metabolized through kynurenine pathway. Tryptophan 36-46 indoleamine 2,3-dioxygenase 1 Homo sapiens 96-125 33241018-1 2020 Background: Indoleamine 2,3-dioxygenase (IDO), a limiting enzyme in the IDO/kynurenine (Kyn) pathway, converts tryptophan (Trp) into Kyn, and plays a significant role in immune suppression and tumor immune evasion. Tryptophan 111-121 indoleamine 2,3-dioxygenase 1 Homo sapiens 12-39 33241018-1 2020 Background: Indoleamine 2,3-dioxygenase (IDO), a limiting enzyme in the IDO/kynurenine (Kyn) pathway, converts tryptophan (Trp) into Kyn, and plays a significant role in immune suppression and tumor immune evasion. Tryptophan 111-121 indoleamine 2,3-dioxygenase 1 Homo sapiens 41-44 33241018-1 2020 Background: Indoleamine 2,3-dioxygenase (IDO), a limiting enzyme in the IDO/kynurenine (Kyn) pathway, converts tryptophan (Trp) into Kyn, and plays a significant role in immune suppression and tumor immune evasion. Tryptophan 111-121 indoleamine 2,3-dioxygenase 1 Homo sapiens 72-75 33241018-1 2020 Background: Indoleamine 2,3-dioxygenase (IDO), a limiting enzyme in the IDO/kynurenine (Kyn) pathway, converts tryptophan (Trp) into Kyn, and plays a significant role in immune suppression and tumor immune evasion. Tryptophan 123-126 indoleamine 2,3-dioxygenase 1 Homo sapiens 12-39 33241018-1 2020 Background: Indoleamine 2,3-dioxygenase (IDO), a limiting enzyme in the IDO/kynurenine (Kyn) pathway, converts tryptophan (Trp) into Kyn, and plays a significant role in immune suppression and tumor immune evasion. Tryptophan 123-126 indoleamine 2,3-dioxygenase 1 Homo sapiens 41-44 33241018-1 2020 Background: Indoleamine 2,3-dioxygenase (IDO), a limiting enzyme in the IDO/kynurenine (Kyn) pathway, converts tryptophan (Trp) into Kyn, and plays a significant role in immune suppression and tumor immune evasion. Tryptophan 123-126 indoleamine 2,3-dioxygenase 1 Homo sapiens 72-75 33241018-4 2020 The correlation between IDO activity, as computed by Kyn: Trp ratios and survival was estimated using Kaplan-Meier curves. Tryptophan 58-61 indoleamine 2,3-dioxygenase 1 Homo sapiens 24-27 32590336-5 2020 In addition, because of its potential influence on the response to ICIs, major interest has been shown in the tryptophan-degrading enzymes indoleamine 2,3-dioxygenase (IDO) and tryptophan 2,3-dioxygenase (TDO). Tryptophan 110-120 indoleamine 2,3-dioxygenase 1 Homo sapiens 139-166 32590336-5 2020 In addition, because of its potential influence on the response to ICIs, major interest has been shown in the tryptophan-degrading enzymes indoleamine 2,3-dioxygenase (IDO) and tryptophan 2,3-dioxygenase (TDO). Tryptophan 110-120 indoleamine 2,3-dioxygenase 1 Homo sapiens 168-171 32590336-7 2020 IDO and TDO are especially of interest in NETs since some tumours produce serotonin but the majority do not, which potentially deplete the precursor tryptophan. Tryptophan 149-159 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 32842609-1 2020 Tryptophan (TRP) is an essential, aromatic amino acid catabolized by indoleamine 2,3-dioxygenase (IDO) and tryptophan 2,3-dioxygenase (TDO) enzymes into kynurenine. Tryptophan 0-10 indoleamine 2,3-dioxygenase 1 Homo sapiens 69-96 32842609-1 2020 Tryptophan (TRP) is an essential, aromatic amino acid catabolized by indoleamine 2,3-dioxygenase (IDO) and tryptophan 2,3-dioxygenase (TDO) enzymes into kynurenine. Tryptophan 0-10 indoleamine 2,3-dioxygenase 1 Homo sapiens 98-101 32842609-1 2020 Tryptophan (TRP) is an essential, aromatic amino acid catabolized by indoleamine 2,3-dioxygenase (IDO) and tryptophan 2,3-dioxygenase (TDO) enzymes into kynurenine. Tryptophan 12-15 indoleamine 2,3-dioxygenase 1 Homo sapiens 69-96 32842609-1 2020 Tryptophan (TRP) is an essential, aromatic amino acid catabolized by indoleamine 2,3-dioxygenase (IDO) and tryptophan 2,3-dioxygenase (TDO) enzymes into kynurenine. Tryptophan 12-15 indoleamine 2,3-dioxygenase 1 Homo sapiens 98-101 32907554-2 2020 IDO1 breaks-down tryptophan to generate kynurenine derivatives, which may activate the aryl hydrocarbon receptor (AHR). Tryptophan 17-27 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-4 32899743-4 2020 We found that l-tryptophan (Trp) metabolism and, in particular, the kynurenine pathway would exert protective effects in all experimental models and in some, but not all, RA patients, possibly due to single nucleotide polymorphisms in the gene coding for indoleamine 2,3-dioxygenase 1 (IDO1; the enzyme catalyzing the rate-limiting step of the kynurenine pathway). Tryptophan 14-26 indoleamine 2,3-dioxygenase 1 Homo sapiens 255-284 32899743-4 2020 We found that l-tryptophan (Trp) metabolism and, in particular, the kynurenine pathway would exert protective effects in all experimental models and in some, but not all, RA patients, possibly due to single nucleotide polymorphisms in the gene coding for indoleamine 2,3-dioxygenase 1 (IDO1; the enzyme catalyzing the rate-limiting step of the kynurenine pathway). Tryptophan 14-26 indoleamine 2,3-dioxygenase 1 Homo sapiens 286-290 32899743-4 2020 We found that l-tryptophan (Trp) metabolism and, in particular, the kynurenine pathway would exert protective effects in all experimental models and in some, but not all, RA patients, possibly due to single nucleotide polymorphisms in the gene coding for indoleamine 2,3-dioxygenase 1 (IDO1; the enzyme catalyzing the rate-limiting step of the kynurenine pathway). Tryptophan 28-31 indoleamine 2,3-dioxygenase 1 Homo sapiens 255-284 32899743-4 2020 We found that l-tryptophan (Trp) metabolism and, in particular, the kynurenine pathway would exert protective effects in all experimental models and in some, but not all, RA patients, possibly due to single nucleotide polymorphisms in the gene coding for indoleamine 2,3-dioxygenase 1 (IDO1; the enzyme catalyzing the rate-limiting step of the kynurenine pathway). Tryptophan 28-31 indoleamine 2,3-dioxygenase 1 Homo sapiens 286-290 33014820-2 2020 B7 family molecules provide both co-stimulatory and co-inhibitory signals to T cells while tryptophan degrading enzymes like Indoleamine 2,3 dioxygenase (IDO) and Tryptophan 2,3 Dioxygenase (TDO) mediate tumor immune tolerance. Tryptophan 91-101 indoleamine 2,3-dioxygenase 1 Homo sapiens 125-152 33014820-2 2020 B7 family molecules provide both co-stimulatory and co-inhibitory signals to T cells while tryptophan degrading enzymes like Indoleamine 2,3 dioxygenase (IDO) and Tryptophan 2,3 Dioxygenase (TDO) mediate tumor immune tolerance. Tryptophan 91-101 indoleamine 2,3-dioxygenase 1 Homo sapiens 154-157 32387857-1 2020 As a rate-limiting enzyme in the major pathway of l-tryptophan catabolism, indoleamine 2, 3-dioxygenase 1 (IDO1) has been regarded as a potential target for the treatment of a variety of diseases. Tryptophan 50-62 indoleamine 2,3-dioxygenase 1 Homo sapiens 75-105 32387857-1 2020 As a rate-limiting enzyme in the major pathway of l-tryptophan catabolism, indoleamine 2, 3-dioxygenase 1 (IDO1) has been regarded as a potential target for the treatment of a variety of diseases. Tryptophan 50-62 indoleamine 2,3-dioxygenase 1 Homo sapiens 107-111 32430712-1 2020 Indoleamine 2, 3-dioxygenase (IDO), an immunosuppressive enzyme that mediates the conversion of tryptophan to kynurenine, was shown to play a key role in placental development during normal pregnancy. Tryptophan 96-106 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-28 32350858-7 2020 In vitro experiments confirmed tryptophan catabolism and depletion of CD8+ T cells in IDO-1+ MDS, suggesting that IDO-1 expression induces an immunosuppressive microenvironment in MDS, thereby leading to treatment failure under AZA treatment. Tryptophan 31-41 indoleamine 2,3-dioxygenase 1 Homo sapiens 114-119 32430712-1 2020 Indoleamine 2, 3-dioxygenase (IDO), an immunosuppressive enzyme that mediates the conversion of tryptophan to kynurenine, was shown to play a key role in placental development during normal pregnancy. Tryptophan 96-106 indoleamine 2,3-dioxygenase 1 Homo sapiens 30-33 34008371-1 2020 Indoleamine 2, 3-dioxygenase (IDO) is an important immunoregulatory enzyme, which mediates immune effects by depleting tryptophan and producing multiple metabolites. Tryptophan 119-129 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-28 34008371-1 2020 Indoleamine 2, 3-dioxygenase (IDO) is an important immunoregulatory enzyme, which mediates immune effects by depleting tryptophan and producing multiple metabolites. Tryptophan 119-129 indoleamine 2,3-dioxygenase 1 Homo sapiens 30-33 32456621-1 2020 BACKGROUND: Indoleamine 2,3-dioxygenase (IDO) is a rate-limiting enzyme in the metabolism of tryptophan into kynurenine. Tryptophan 93-103 indoleamine 2,3-dioxygenase 1 Homo sapiens 12-39 32475317-1 2020 l-tryptophan induces IDO (indoleamine 2,3-dioxygenase) 1-dependent vasodilation. Tryptophan 0-12 indoleamine 2,3-dioxygenase 1 Homo sapiens 21-24 32475317-1 2020 l-tryptophan induces IDO (indoleamine 2,3-dioxygenase) 1-dependent vasodilation. Tryptophan 0-12 indoleamine 2,3-dioxygenase 1 Homo sapiens 26-56 32475317-9 2020 After in vitro incubation of placental arteries with IDO1-upregulating cytokines interferon-gamma and tumor necrosis factor-alpha, l-tryptophan induced vasodilation. Tryptophan 131-143 indoleamine 2,3-dioxygenase 1 Homo sapiens 53-57 32475317-13 2020 Vasodilation to the lipophilic, transporter independent ethyl ester of l-tryptophan was reduced in preeclamptic versus healthy placental arteries, in agreement with reduced IDO1 expression. Tryptophan 71-83 indoleamine 2,3-dioxygenase 1 Homo sapiens 173-177 32475317-14 2020 In conclusion, l-tryptophan induces IDO1- and NO-dependent relaxation in placental arteries, which is determined by l-tryptophan uptake rather than IDO1 expression. Tryptophan 15-27 indoleamine 2,3-dioxygenase 1 Homo sapiens 36-40 32475317-14 2020 In conclusion, l-tryptophan induces IDO1- and NO-dependent relaxation in placental arteries, which is determined by l-tryptophan uptake rather than IDO1 expression. Tryptophan 116-128 indoleamine 2,3-dioxygenase 1 Homo sapiens 36-40 32475317-15 2020 Increased l-tryptophan uptake might compensate for reduced IDO1 expression in preeclamptic placentas. Tryptophan 10-22 indoleamine 2,3-dioxygenase 1 Homo sapiens 59-63 31609478-8 2020 Gene expression analysis in PDAC tumors (n = 63) showed a positive correlation between the expression of NOS2 and the tryptophan/kynurenine pathway genes, including indoleamine-2,3-dioxygenase 1 (IDO1) and several aryl hydrocarbon receptor (AHR)-target genes including NFE2L2 (NRF2), SERPINB2, IL1b, IL6 and IL8, which are implicated in pancreatic cancer. Tryptophan 118-128 indoleamine 2,3-dioxygenase 1 Homo sapiens 165-194 31609478-8 2020 Gene expression analysis in PDAC tumors (n = 63) showed a positive correlation between the expression of NOS2 and the tryptophan/kynurenine pathway genes, including indoleamine-2,3-dioxygenase 1 (IDO1) and several aryl hydrocarbon receptor (AHR)-target genes including NFE2L2 (NRF2), SERPINB2, IL1b, IL6 and IL8, which are implicated in pancreatic cancer. Tryptophan 118-128 indoleamine 2,3-dioxygenase 1 Homo sapiens 196-200 32314169-1 2020 Kynurenine pathway of tryptophan metabolism is involved in the pathophysiology of chronic kidney disease (CKD) and diabetes mellitus, mainly through the inflammation-induced activity of indoleamine 2,3-dioxygenase (IDO), and few studies have investigated its potential link with proteinuria. Tryptophan 22-32 indoleamine 2,3-dioxygenase 1 Homo sapiens 215-218 32536910-1 2020 Indoleamine 2,3-dioxygenase 2 (IDO2) is an analog of the tryptophan degrading and immunomodulating enzyme indoleamine 2,3-dioxygenase 1 (IDO1). Tryptophan 57-67 indoleamine 2,3-dioxygenase 1 Homo sapiens 106-135 32536910-1 2020 Indoleamine 2,3-dioxygenase 2 (IDO2) is an analog of the tryptophan degrading and immunomodulating enzyme indoleamine 2,3-dioxygenase 1 (IDO1). Tryptophan 57-67 indoleamine 2,3-dioxygenase 1 Homo sapiens 137-141 32568737-1 2020 Indoleamine 2,3-Dioxygenase (IDO), is a speed limiting enzyme that catalyzes the decomposition and metabolism of Tryptophan along Tryptophan-IDO-Kynurenine pathway [1]. Tryptophan 113-123 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 32568737-1 2020 Indoleamine 2,3-Dioxygenase (IDO), is a speed limiting enzyme that catalyzes the decomposition and metabolism of Tryptophan along Tryptophan-IDO-Kynurenine pathway [1]. Tryptophan 113-123 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 32568737-1 2020 Indoleamine 2,3-Dioxygenase (IDO), is a speed limiting enzyme that catalyzes the decomposition and metabolism of Tryptophan along Tryptophan-IDO-Kynurenine pathway [1]. Tryptophan 113-123 indoleamine 2,3-dioxygenase 1 Homo sapiens 141-144 32568737-1 2020 Indoleamine 2,3-Dioxygenase (IDO), is a speed limiting enzyme that catalyzes the decomposition and metabolism of Tryptophan along Tryptophan-IDO-Kynurenine pathway [1]. Tryptophan 130-140 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 32568737-1 2020 Indoleamine 2,3-Dioxygenase (IDO), is a speed limiting enzyme that catalyzes the decomposition and metabolism of Tryptophan along Tryptophan-IDO-Kynurenine pathway [1]. Tryptophan 130-140 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 32568737-1 2020 Indoleamine 2,3-Dioxygenase (IDO), is a speed limiting enzyme that catalyzes the decomposition and metabolism of Tryptophan along Tryptophan-IDO-Kynurenine pathway [1]. Tryptophan 130-140 indoleamine 2,3-dioxygenase 1 Homo sapiens 141-144 32612606-1 2020 Indoleamine 2, 3-dioxygenase 1 (IDO; IDO1; INDO) is a rate-limiting enzyme that metabolizes the essential amino acid, tryptophan, into downstream kynurenines. Tryptophan 118-128 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-30 32612606-1 2020 Indoleamine 2, 3-dioxygenase 1 (IDO; IDO1; INDO) is a rate-limiting enzyme that metabolizes the essential amino acid, tryptophan, into downstream kynurenines. Tryptophan 118-128 indoleamine 2,3-dioxygenase 1 Homo sapiens 32-35 32612606-1 2020 Indoleamine 2, 3-dioxygenase 1 (IDO; IDO1; INDO) is a rate-limiting enzyme that metabolizes the essential amino acid, tryptophan, into downstream kynurenines. Tryptophan 118-128 indoleamine 2,3-dioxygenase 1 Homo sapiens 37-41 32612606-2 2020 Canonically, the metabolic depletion of tryptophan and/or the accumulation of kynurenine is the mechanism that defines how immunosuppressive IDO inhibits immune cell effector functions and/or facilitates T cell death. Tryptophan 40-50 indoleamine 2,3-dioxygenase 1 Homo sapiens 141-144 32934882-1 2020 Indoleamine 2,3-dioxygenase 1 (IDO1) catalyzes the first, rate-limiting step of the so-called "kynurenine pathway", which converts the essential amino acid L-tryptophan (Trp) into the immunosuppressive metabolite L-kynurenine (Kyn). Tryptophan 156-168 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-29 32934882-1 2020 Indoleamine 2,3-dioxygenase 1 (IDO1) catalyzes the first, rate-limiting step of the so-called "kynurenine pathway", which converts the essential amino acid L-tryptophan (Trp) into the immunosuppressive metabolite L-kynurenine (Kyn). Tryptophan 156-168 indoleamine 2,3-dioxygenase 1 Homo sapiens 31-35 32934882-1 2020 Indoleamine 2,3-dioxygenase 1 (IDO1) catalyzes the first, rate-limiting step of the so-called "kynurenine pathway", which converts the essential amino acid L-tryptophan (Trp) into the immunosuppressive metabolite L-kynurenine (Kyn). Tryptophan 170-173 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-29 32934882-1 2020 Indoleamine 2,3-dioxygenase 1 (IDO1) catalyzes the first, rate-limiting step of the so-called "kynurenine pathway", which converts the essential amino acid L-tryptophan (Trp) into the immunosuppressive metabolite L-kynurenine (Kyn). Tryptophan 170-173 indoleamine 2,3-dioxygenase 1 Homo sapiens 31-35 32934882-3 2020 At least in part, the immunomodulatory functions of IDO1 can be explained by depletion of Trp and accumulation of Kyn and its derivatives. Tryptophan 90-93 indoleamine 2,3-dioxygenase 1 Homo sapiens 52-56 32545442-3 2020 Indoleamine 2,3-dioxygenase 1 (IDO1) mediates tryptophan metabolism and T cell suppression, but the immune-independent function of IDO1 in cancer behavior is not fully understood. Tryptophan 46-56 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-29 32545442-3 2020 Indoleamine 2,3-dioxygenase 1 (IDO1) mediates tryptophan metabolism and T cell suppression, but the immune-independent function of IDO1 in cancer behavior is not fully understood. Tryptophan 46-56 indoleamine 2,3-dioxygenase 1 Homo sapiens 31-35 32545442-6 2020 With the treatment of kynurenine, the first breakdown product of the IDO1-mediated tryptophan metabolism, the radiosensitivity of HeLa and SiHa cells decreased. Tryptophan 83-93 indoleamine 2,3-dioxygenase 1 Homo sapiens 69-73 32370297-1 2020 Indolamine-2,3-dioxygenase (IDO) is an intracellular enzyme that catalyzes amino acid tryptophan to L-kynurenine. Tryptophan 86-96 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-26 32370297-1 2020 Indolamine-2,3-dioxygenase (IDO) is an intracellular enzyme that catalyzes amino acid tryptophan to L-kynurenine. Tryptophan 86-96 indoleamine 2,3-dioxygenase 1 Homo sapiens 28-31 32369456-5 2020 Persons with active TB and LTBI also exhibit increased expression of indoleamine 2,3-dioxygenase-1 (IDO-1), suggesting IDO-1 mediates observed increases in tryptophan catabolism. Tryptophan 156-166 indoleamine 2,3-dioxygenase 1 Homo sapiens 69-98 32369456-5 2020 Persons with active TB and LTBI also exhibit increased expression of indoleamine 2,3-dioxygenase-1 (IDO-1), suggesting IDO-1 mediates observed increases in tryptophan catabolism. Tryptophan 156-166 indoleamine 2,3-dioxygenase 1 Homo sapiens 100-105 32369456-5 2020 Persons with active TB and LTBI also exhibit increased expression of indoleamine 2,3-dioxygenase-1 (IDO-1), suggesting IDO-1 mediates observed increases in tryptophan catabolism. Tryptophan 156-166 indoleamine 2,3-dioxygenase 1 Homo sapiens 119-124 32369456-6 2020 Together, these data indicate IDO-1-mediated tryptophan catabolism is highly preserved in the human response to Mycobacterium tuberculosis and could be a target for biomarker development as well as host-directed therapies. Tryptophan 45-55 indoleamine 2,3-dioxygenase 1 Homo sapiens 30-35 32301149-1 2020 Indoleamine 2,3-dioxygenase (IDO) is the rate-limiting enzyme in conversion of tryptophan to kynurenines, feeding de novo nicotinamide synthesis. Tryptophan 79-89 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 32301149-3 2020 IDO mediates immune suppression through depletion of tryptophan required by T lymphocytes and other mechanisms. Tryptophan 53-63 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 32456621-1 2020 BACKGROUND: Indoleamine 2,3-dioxygenase (IDO) is a rate-limiting enzyme in the metabolism of tryptophan into kynurenine. Tryptophan 93-103 indoleamine 2,3-dioxygenase 1 Homo sapiens 41-44 32035622-2 2020 IDO1, an enzyme involved in tryptophan metabolism, is now proposed as a new target in GBM treatment, since several reports have demonstrated that IDO1 expression is related to GBM malignancy. Tryptophan 28-38 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-4 32035622-2 2020 IDO1, an enzyme involved in tryptophan metabolism, is now proposed as a new target in GBM treatment, since several reports have demonstrated that IDO1 expression is related to GBM malignancy. Tryptophan 28-38 indoleamine 2,3-dioxygenase 1 Homo sapiens 146-150 32153576-3 2020 In the course of anti-tumor immune response, the pro-inflammatory cytokine interferon gamma (IFN-gamma) induces both, the enzyme indoleamine 2,3-dioxygenase (IDO) to degrade tryptophan and the enzyme GTP-cyclohydrolase I to form neopterin. Tryptophan 174-184 indoleamine 2,3-dioxygenase 1 Homo sapiens 158-161 31057090-1 2020 Indoleamine-2,3-dioxygenase 1 (IDO1) is an extrahepatic, heme-containing and tryptophan-catalyzing enzyme responsible for causing blockade of T-cell proliferation and differentiation by depleting tryptophan level in cancerous cells. Tryptophan 77-87 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-29 31057090-1 2020 Indoleamine-2,3-dioxygenase 1 (IDO1) is an extrahepatic, heme-containing and tryptophan-catalyzing enzyme responsible for causing blockade of T-cell proliferation and differentiation by depleting tryptophan level in cancerous cells. Tryptophan 77-87 indoleamine 2,3-dioxygenase 1 Homo sapiens 31-35 31057090-1 2020 Indoleamine-2,3-dioxygenase 1 (IDO1) is an extrahepatic, heme-containing and tryptophan-catalyzing enzyme responsible for causing blockade of T-cell proliferation and differentiation by depleting tryptophan level in cancerous cells. Tryptophan 196-206 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-29 31057090-1 2020 Indoleamine-2,3-dioxygenase 1 (IDO1) is an extrahepatic, heme-containing and tryptophan-catalyzing enzyme responsible for causing blockade of T-cell proliferation and differentiation by depleting tryptophan level in cancerous cells. Tryptophan 196-206 indoleamine 2,3-dioxygenase 1 Homo sapiens 31-35 31964747-3 2020 IFNgamma activates human cells to produce the tryptophan (trp) catabolizing enzyme, IDO. Tryptophan 46-56 indoleamine 2,3-dioxygenase 1 Homo sapiens 84-87 31964747-3 2020 IFNgamma activates human cells to produce the tryptophan (trp) catabolizing enzyme, IDO. Tryptophan 58-61 indoleamine 2,3-dioxygenase 1 Homo sapiens 84-87 32194552-11 2020 IDO1 inhibition using GDC-0919 resulted in (i) a significant decrease of plasmatic Kynurenine to Tryptophan ratio and in (ii) a decrease of tumoral Kynurenine. Tryptophan 97-107 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-4 31197246-1 2020 Indoleamine 2,3-dioxygenase 1 (IDO1) is emerging as a promising therapeutic target for the treatment of malignant tumors characterized by dysregulated tryptophan metabolism. Tryptophan 151-161 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-29 31197246-1 2020 Indoleamine 2,3-dioxygenase 1 (IDO1) is emerging as a promising therapeutic target for the treatment of malignant tumors characterized by dysregulated tryptophan metabolism. Tryptophan 151-161 indoleamine 2,3-dioxygenase 1 Homo sapiens 31-35 31799743-2 2020 Tryptophan (TRP), an essential amino acid, is catabolized into tolerogenic metabolites, kynurenines (KYN), by indoleamine 2,3-dioxygenase 1 (IDO1), which can induce Foxp3+ T regulatory cells (Tregs). Tryptophan 0-10 indoleamine 2,3-dioxygenase 1 Homo sapiens 110-139 31799743-2 2020 Tryptophan (TRP), an essential amino acid, is catabolized into tolerogenic metabolites, kynurenines (KYN), by indoleamine 2,3-dioxygenase 1 (IDO1), which can induce Foxp3+ T regulatory cells (Tregs). Tryptophan 0-10 indoleamine 2,3-dioxygenase 1 Homo sapiens 141-145 31799743-2 2020 Tryptophan (TRP), an essential amino acid, is catabolized into tolerogenic metabolites, kynurenines (KYN), by indoleamine 2,3-dioxygenase 1 (IDO1), which can induce Foxp3+ T regulatory cells (Tregs). Tryptophan 12-15 indoleamine 2,3-dioxygenase 1 Homo sapiens 110-139 31799743-2 2020 Tryptophan (TRP), an essential amino acid, is catabolized into tolerogenic metabolites, kynurenines (KYN), by indoleamine 2,3-dioxygenase 1 (IDO1), which can induce Foxp3+ T regulatory cells (Tregs). Tryptophan 12-15 indoleamine 2,3-dioxygenase 1 Homo sapiens 141-145 31846032-0 2020 Hypoxia decreases the T helper cell-suppressive capacity of synovial fibroblasts by downregulating IDO1-mediated tryptophan metabolism. Tryptophan 113-123 indoleamine 2,3-dioxygenase 1 Homo sapiens 99-103 31846032-2 2020 Synovial fibroblasts possess the capacity to suppress T cell responses through indoleamine 2, 3-dioxygenase 1 (IDO1)-mediated tryptophan metabolism. Tryptophan 126-136 indoleamine 2,3-dioxygenase 1 Homo sapiens 79-109 31846032-2 2020 Synovial fibroblasts possess the capacity to suppress T cell responses through indoleamine 2, 3-dioxygenase 1 (IDO1)-mediated tryptophan metabolism. Tryptophan 126-136 indoleamine 2,3-dioxygenase 1 Homo sapiens 111-115 32346606-7 2020 TDO2 expression was correlated with immune infiltrates and tryptophan metabolism-related genes (IDO1 and kynureninase [KYNU]). Tryptophan 59-69 indoleamine 2,3-dioxygenase 1 Homo sapiens 96-100 32346606-9 2020 Additionally, we established the concept that tryptophan-catabolizing enzymes (IDO1, IDO2, TDO2, and KYNU) may function through co-regulating the immunological microenvironment, and thus immunotherapy targeting IDO1 alone might be insufficient. Tryptophan 46-56 indoleamine 2,3-dioxygenase 1 Homo sapiens 79-83 32346606-9 2020 Additionally, we established the concept that tryptophan-catabolizing enzymes (IDO1, IDO2, TDO2, and KYNU) may function through co-regulating the immunological microenvironment, and thus immunotherapy targeting IDO1 alone might be insufficient. Tryptophan 46-56 indoleamine 2,3-dioxygenase 1 Homo sapiens 211-215 32226425-4 2020 IDO1 degrades L-tryptophan to L-kynurenine-an activating ligand for AhR-thus establishing a feed-forward loop. Tryptophan 14-26 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-4 31981851-1 2020 Indoleamine 2,3-dioxygenase 1 (IDO1) is the enzyme catalyzing the oxidative metabolism of tryptophan, which accounts for cancer immunosuppression in tumor microenvironment. Tryptophan 90-100 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-29 31981851-1 2020 Indoleamine 2,3-dioxygenase 1 (IDO1) is the enzyme catalyzing the oxidative metabolism of tryptophan, which accounts for cancer immunosuppression in tumor microenvironment. Tryptophan 90-100 indoleamine 2,3-dioxygenase 1 Homo sapiens 31-35 32296044-1 2020 Indoleamine 2,3-dioxygenase 1 (IDO1), indoleamine 2,3-dioxygenase 2 (IDO2), and tryptophan 2,3-dioxygenase (TDO) initiate the first step of the kynurenine pathway (KP), leading to the transformation of L-tryptophan (Trp) into L-kynurenine (Kyn) and other downstream metabolites. Tryptophan 202-214 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-29 32296044-1 2020 Indoleamine 2,3-dioxygenase 1 (IDO1), indoleamine 2,3-dioxygenase 2 (IDO2), and tryptophan 2,3-dioxygenase (TDO) initiate the first step of the kynurenine pathway (KP), leading to the transformation of L-tryptophan (Trp) into L-kynurenine (Kyn) and other downstream metabolites. Tryptophan 202-214 indoleamine 2,3-dioxygenase 1 Homo sapiens 31-35 32296044-1 2020 Indoleamine 2,3-dioxygenase 1 (IDO1), indoleamine 2,3-dioxygenase 2 (IDO2), and tryptophan 2,3-dioxygenase (TDO) initiate the first step of the kynurenine pathway (KP), leading to the transformation of L-tryptophan (Trp) into L-kynurenine (Kyn) and other downstream metabolites. Tryptophan 216-219 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-29 32296044-1 2020 Indoleamine 2,3-dioxygenase 1 (IDO1), indoleamine 2,3-dioxygenase 2 (IDO2), and tryptophan 2,3-dioxygenase (TDO) initiate the first step of the kynurenine pathway (KP), leading to the transformation of L-tryptophan (Trp) into L-kynurenine (Kyn) and other downstream metabolites. Tryptophan 216-219 indoleamine 2,3-dioxygenase 1 Homo sapiens 31-35 32117235-1 2020 Indoleamine 2,3-dioxygenase (IDO) and tryptophan 2,3-dioxygenase (TDO2) are the key enzymes of tryptophan (TRP) metabolism in the kynurenine pathway (KP). Tryptophan 107-110 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 32117235-1 2020 Indoleamine 2,3-dioxygenase (IDO) and tryptophan 2,3-dioxygenase (TDO2) are the key enzymes of tryptophan (TRP) metabolism in the kynurenine pathway (KP). Tryptophan 107-110 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 32117235-7 2020 Our results show a heterogeneous and inversely correlated expression profile of TRP-metabolizing genes among GBM and HNSCC cells, with low, but inducible IDO1 expression upon IFNgamma treatment. Tryptophan 80-83 indoleamine 2,3-dioxygenase 1 Homo sapiens 154-158 32117223-12 2020 Tryptophan depletion and kynurenine accumulation were found in the supernatants of PBMC-DENV cultures, which presented enhanced detection of indoleamine 2,3-dioxygenase 1 and 2 transcripts as compared to controls. Tryptophan 0-10 indoleamine 2,3-dioxygenase 1 Homo sapiens 141-176 32050636-5 2020 Both TDO and indoleamine 2,3-dioxygenase (IDO) catalyze tryptophan and produce kynurenine, which could cause inhibition of T cell immune responses. Tryptophan 56-66 indoleamine 2,3-dioxygenase 1 Homo sapiens 13-40 32050636-5 2020 Both TDO and indoleamine 2,3-dioxygenase (IDO) catalyze tryptophan and produce kynurenine, which could cause inhibition of T cell immune responses. Tryptophan 56-66 indoleamine 2,3-dioxygenase 1 Homo sapiens 42-45 31753057-2 2020 It is modelled by administration of lipopolysaccharides (LPS) to induce expression of pro-inflammatory cytokines that then activate indoleamine 2,3 dioxygenase (IDO1), the rate-limiting enzyme in the kynurenine pathway of tryptophan metabolism. Tryptophan 222-232 indoleamine 2,3-dioxygenase 1 Homo sapiens 161-165 31765740-2 2020 The major metabolic pathway of tryptophan, an essential amino acid in humans, is the kynurenine pathway (KP) in which indoleamine 2,3-dioxygenase (IDO) and tryptophan 2,3-dioxygenase (TDO) catalyze the conversion of tryptophan into kynurenine. Tryptophan 31-41 indoleamine 2,3-dioxygenase 1 Homo sapiens 118-145 31765740-2 2020 The major metabolic pathway of tryptophan, an essential amino acid in humans, is the kynurenine pathway (KP) in which indoleamine 2,3-dioxygenase (IDO) and tryptophan 2,3-dioxygenase (TDO) catalyze the conversion of tryptophan into kynurenine. Tryptophan 31-41 indoleamine 2,3-dioxygenase 1 Homo sapiens 147-150 31786316-4 2020 Furthermore, kynurenine activation of Ahr is observed to stimulate expression of the enzyme IDO1, which generates kynurenine by degrading tryptophan, representing a positive feedback loop that may link inflammation with ROS production. Tryptophan 138-148 indoleamine 2,3-dioxygenase 1 Homo sapiens 92-96 31821895-1 2020 OBJECTIVES: During dengue fever, a pronounced gamma interferon immune response produces neopterin and promotes tryptophan degradation by the enzyme Indoleamine 2,3 Dioxygenase-1 (IDO-1). Tryptophan 111-121 indoleamine 2,3-dioxygenase 1 Homo sapiens 148-177 31821895-1 2020 OBJECTIVES: During dengue fever, a pronounced gamma interferon immune response produces neopterin and promotes tryptophan degradation by the enzyme Indoleamine 2,3 Dioxygenase-1 (IDO-1). Tryptophan 111-121 indoleamine 2,3-dioxygenase 1 Homo sapiens 179-184 31821895-2 2020 Activated IDO-1 is indicated by increased kynurenine to tryptophan ratio (Kyn/Trp) in patients. Tryptophan 56-66 indoleamine 2,3-dioxygenase 1 Homo sapiens 10-15 31267172-4 2019 Upon microbial infection, interferon gamma (IFN-gamma), a major cytokine of the adaptive immune response, induces a broad spectrum of effector molecules, such as the tryptophan-degrading enzyme indoleamine 2,3-dioxygenase-1 (IDO1). Tryptophan 166-176 indoleamine 2,3-dioxygenase 1 Homo sapiens 194-223 31870154-2 2020 This 2,3-dioxygenative cleavage of the indole ring of tryptophan with dioxygen is mediated by two heme enzymes, tryptophan 2,3-dioxygenase (TDO) and indoleamine 2,3-dioxygenase (IDO), during its conversion to N-formylkynurenine in the first and rate-limiting step of kynurenine pathway. Tryptophan 54-64 indoleamine 2,3-dioxygenase 1 Homo sapiens 149-176 31870154-2 2020 This 2,3-dioxygenative cleavage of the indole ring of tryptophan with dioxygen is mediated by two heme enzymes, tryptophan 2,3-dioxygenase (TDO) and indoleamine 2,3-dioxygenase (IDO), during its conversion to N-formylkynurenine in the first and rate-limiting step of kynurenine pathway. Tryptophan 54-64 indoleamine 2,3-dioxygenase 1 Homo sapiens 178-181 32047753-2 2019 Indoleamine 2, 3-dioxygenase 1 (IDO1) catalyzes the conversion of tryptophan to kynurenine causing lysine depletion, which is an important target in the research and development of anticancer drugs. Tryptophan 66-76 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-30 32047753-2 2019 Indoleamine 2, 3-dioxygenase 1 (IDO1) catalyzes the conversion of tryptophan to kynurenine causing lysine depletion, which is an important target in the research and development of anticancer drugs. Tryptophan 66-76 indoleamine 2,3-dioxygenase 1 Homo sapiens 32-36 31819194-2 2020 Three enzymes, indoleamine-2,3-dioxygenase 1 and 2 (IDO1/2) and tryptophan-2,3-dioxygenase (TDO2), catalyse the first step of the degradation of the essential amino acid tryptophan (Trp) to kynurenine (Kyn). Tryptophan 64-74 indoleamine 2,3-dioxygenase 1 Homo sapiens 15-50 31819194-2 2020 Three enzymes, indoleamine-2,3-dioxygenase 1 and 2 (IDO1/2) and tryptophan-2,3-dioxygenase (TDO2), catalyse the first step of the degradation of the essential amino acid tryptophan (Trp) to kynurenine (Kyn). Tryptophan 64-74 indoleamine 2,3-dioxygenase 1 Homo sapiens 52-58 31819194-2 2020 Three enzymes, indoleamine-2,3-dioxygenase 1 and 2 (IDO1/2) and tryptophan-2,3-dioxygenase (TDO2), catalyse the first step of the degradation of the essential amino acid tryptophan (Trp) to kynurenine (Kyn). Tryptophan 182-185 indoleamine 2,3-dioxygenase 1 Homo sapiens 15-50 31819194-2 2020 Three enzymes, indoleamine-2,3-dioxygenase 1 and 2 (IDO1/2) and tryptophan-2,3-dioxygenase (TDO2), catalyse the first step of the degradation of the essential amino acid tryptophan (Trp) to kynurenine (Kyn). Tryptophan 182-185 indoleamine 2,3-dioxygenase 1 Homo sapiens 52-58 31802183-0 2020 A highly efficient modality to block the degradation of tryptophan for cancer immunotherapy: locked nucleic acid-modified antisense oligonucleotides to inhibit human indoleamine 2,3-dioxygenase 1/tryptophan 2,3-dioxygenase expression. Tryptophan 56-66 indoleamine 2,3-dioxygenase 1 Homo sapiens 166-222 31802183-5 2020 We, therefore, sought to add an alternative, highly efficient approach to block the degradation of tryptophan by inhibiting the expression of IDO1 and TDO2 using locked nucleic acid (LNA)-modified antisense oligonucleotides (ASOs). Tryptophan 99-109 indoleamine 2,3-dioxygenase 1 Homo sapiens 142-146 32125093-8 2020 RESULTS: The expression level of IDO1 in PSCC cells was positively correlated with serum Kyn concentration and Kyn/Trp radio (KTR; both P < 0.001) but negatively correlated with serum Trp concentration (P = 0.001). Tryptophan 115-118 indoleamine 2,3-dioxygenase 1 Homo sapiens 33-37 32125093-8 2020 RESULTS: The expression level of IDO1 in PSCC cells was positively correlated with serum Kyn concentration and Kyn/Trp radio (KTR; both P < 0.001) but negatively correlated with serum Trp concentration (P = 0.001). Tryptophan 184-187 indoleamine 2,3-dioxygenase 1 Homo sapiens 33-37 31724832-0 2019 Tracking Hidden Binding Pockets Along the Molecular Recognition Path of l-Trp to Indoleamine 2,3-Dioxygenase 1. Tryptophan 72-77 indoleamine 2,3-dioxygenase 1 Homo sapiens 81-110 31724832-1 2019 Indoleamine 2,3-dioxygenase 1 (IDO1) catalyzes the oxidative cleavage of l-Tryptophan (l-Trp) to yield N-formyl-kynurenine in the first and rate limiting step of the kynurenine pathway. Tryptophan 73-85 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-29 31724832-1 2019 Indoleamine 2,3-dioxygenase 1 (IDO1) catalyzes the oxidative cleavage of l-Tryptophan (l-Trp) to yield N-formyl-kynurenine in the first and rate limiting step of the kynurenine pathway. Tryptophan 73-85 indoleamine 2,3-dioxygenase 1 Homo sapiens 31-35 31724832-1 2019 Indoleamine 2,3-dioxygenase 1 (IDO1) catalyzes the oxidative cleavage of l-Tryptophan (l-Trp) to yield N-formyl-kynurenine in the first and rate limiting step of the kynurenine pathway. Tryptophan 87-92 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-29 31724832-1 2019 Indoleamine 2,3-dioxygenase 1 (IDO1) catalyzes the oxidative cleavage of l-Tryptophan (l-Trp) to yield N-formyl-kynurenine in the first and rate limiting step of the kynurenine pathway. Tryptophan 87-92 indoleamine 2,3-dioxygenase 1 Homo sapiens 31-35 31724832-4 2019 In this work, we investigated the molecular recognition path of l-Trp to IDO1, integrating biophysical methods with supervised molecular dynamics (suMD) and mutagenesis experiments. Tryptophan 64-69 indoleamine 2,3-dioxygenase 1 Homo sapiens 73-77 31724832-5 2019 Results allowed disclosing for the first time high and low dissociation constants of l-Trp to IDO1, and the presence of a metastable interaction site located at the upper part of a channel whose borders are defined by the EF-loop and the C-terminal part of the JK-loop. Tryptophan 85-90 indoleamine 2,3-dioxygenase 1 Homo sapiens 94-98 32496990-1 2020 BACKGROUND AND OBJECTIVE: Indoleamine-2,3-dioxygenase 1 (IDO1) which catalyzes degradation of L-tryptophan (L-Trp) to N-formyl kynurenine (NFK) in the first and rate-limiting step of Kynurenine (KYN) pathway has been identified as a promising therapeutic target for cancer immunotherapy. Tryptophan 94-106 indoleamine 2,3-dioxygenase 1 Homo sapiens 26-55 32496990-1 2020 BACKGROUND AND OBJECTIVE: Indoleamine-2,3-dioxygenase 1 (IDO1) which catalyzes degradation of L-tryptophan (L-Trp) to N-formyl kynurenine (NFK) in the first and rate-limiting step of Kynurenine (KYN) pathway has been identified as a promising therapeutic target for cancer immunotherapy. Tryptophan 94-106 indoleamine 2,3-dioxygenase 1 Homo sapiens 57-61 32496990-1 2020 BACKGROUND AND OBJECTIVE: Indoleamine-2,3-dioxygenase 1 (IDO1) which catalyzes degradation of L-tryptophan (L-Trp) to N-formyl kynurenine (NFK) in the first and rate-limiting step of Kynurenine (KYN) pathway has been identified as a promising therapeutic target for cancer immunotherapy. Tryptophan 108-113 indoleamine 2,3-dioxygenase 1 Homo sapiens 26-55 32496990-1 2020 BACKGROUND AND OBJECTIVE: Indoleamine-2,3-dioxygenase 1 (IDO1) which catalyzes degradation of L-tryptophan (L-Trp) to N-formyl kynurenine (NFK) in the first and rate-limiting step of Kynurenine (KYN) pathway has been identified as a promising therapeutic target for cancer immunotherapy. Tryptophan 108-113 indoleamine 2,3-dioxygenase 1 Homo sapiens 57-61 31276825-5 2020 Meanwhile, two IDO isoforms from scallop (IDO-I and -III) and sponge IDOs show high L-Trp catalytic activity, which is comparable to vertebrate IDO1. Tryptophan 84-89 indoleamine 2,3-dioxygenase 1 Homo sapiens 15-18 31276825-5 2020 Meanwhile, two IDO isoforms from scallop (IDO-I and -III) and sponge IDOs show high L-Trp catalytic activity, which is comparable to vertebrate IDO1. Tryptophan 84-89 indoleamine 2,3-dioxygenase 1 Homo sapiens 42-45 31276825-5 2020 Meanwhile, two IDO isoforms from scallop (IDO-I and -III) and sponge IDOs show high L-Trp catalytic activity, which is comparable to vertebrate IDO1. Tryptophan 84-89 indoleamine 2,3-dioxygenase 1 Homo sapiens 144-148 31276825-10 2020 However, this may be specific for human IDO1 because G9th/His was demonstrated to be very effective in increasing the L-Trp affinity even in vertebrate IDOs. Tryptophan 118-123 indoleamine 2,3-dioxygenase 1 Homo sapiens 40-44 31844921-1 2020 BACKGROUND: Indoleamine 2,3-dioxygenase (IDO) catalyses degradation of the essential amino acid tryptophan leading to the production of immunosuppressive kynurenine and tryptophan exhausting. Tryptophan 96-106 indoleamine 2,3-dioxygenase 1 Homo sapiens 12-39 31844921-1 2020 BACKGROUND: Indoleamine 2,3-dioxygenase (IDO) catalyses degradation of the essential amino acid tryptophan leading to the production of immunosuppressive kynurenine and tryptophan exhausting. Tryptophan 96-106 indoleamine 2,3-dioxygenase 1 Homo sapiens 41-44 32452326-1 2020 Indoleamine 2, 3-dioxygenase 1 (IDO1) is the only rate-limiting enzyme outside the liver that catalyzes the oxidation and cracking of indole rings in the tryptophan along the kynurenine pathway (KP). Tryptophan 154-164 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-30 32452326-1 2020 Indoleamine 2, 3-dioxygenase 1 (IDO1) is the only rate-limiting enzyme outside the liver that catalyzes the oxidation and cracking of indole rings in the tryptophan along the kynurenine pathway (KP). Tryptophan 154-164 indoleamine 2,3-dioxygenase 1 Homo sapiens 32-36 31714063-1 2019 We show how the macrocyclic host cucurbit[8]uril (CB[8]) and a fluorescent dye form a biosensing ensemble while its cavity simultaneously traps tryptophan, the upstream substrate of IDO1 enzymes, therefore providing a label-free method to monitor the activity of IDO1 in real time. Tryptophan 144-154 indoleamine 2,3-dioxygenase 1 Homo sapiens 182-186 31714063-1 2019 We show how the macrocyclic host cucurbit[8]uril (CB[8]) and a fluorescent dye form a biosensing ensemble while its cavity simultaneously traps tryptophan, the upstream substrate of IDO1 enzymes, therefore providing a label-free method to monitor the activity of IDO1 in real time. Tryptophan 144-154 indoleamine 2,3-dioxygenase 1 Homo sapiens 263-267 31714063-2 2019 Incubation of malignant HeLa and HepG2 cells over-expressing IDO1 with the associative biosensor resulted in its spontaneous uptake and a fluorescence switch-on response in situ, which can be traced to the displacement of tryptophan from CB[8] upon IDO1-catalyzed oxidation. Tryptophan 222-232 indoleamine 2,3-dioxygenase 1 Homo sapiens 61-65 31714063-2 2019 Incubation of malignant HeLa and HepG2 cells over-expressing IDO1 with the associative biosensor resulted in its spontaneous uptake and a fluorescence switch-on response in situ, which can be traced to the displacement of tryptophan from CB[8] upon IDO1-catalyzed oxidation. Tryptophan 222-232 indoleamine 2,3-dioxygenase 1 Homo sapiens 249-253 31267172-4 2019 Upon microbial infection, interferon gamma (IFN-gamma), a major cytokine of the adaptive immune response, induces a broad spectrum of effector molecules, such as the tryptophan-degrading enzyme indoleamine 2,3-dioxygenase-1 (IDO1). Tryptophan 166-176 indoleamine 2,3-dioxygenase 1 Homo sapiens 225-229 31267172-12 2019 Instead, iNOS activity inhibited IDO1-mediated tryptophan degradation and bacteriostasis. Tryptophan 47-57 indoleamine 2,3-dioxygenase 1 Homo sapiens 33-37 31253481-1 2019 PURPOSES: Indoleamine-2,3-dioxygenase-1 (IDO1) is a key enzyme of tryptophan metabolism which regulates T cell function in immune cells and little is known about the role of IDO1 expression in bladder cancer cells. Tryptophan 66-76 indoleamine 2,3-dioxygenase 1 Homo sapiens 10-39 31795096-1 2019 Cancers express tryptophan catabolising enzymes indoleamine 2,3-dioxygenase 1 (IDO1) and tryptophan 2,3-dioxygenase (TDO2) to produce immunosuppressive tryptophan metabolites that undermine patients" immune systems, leading to poor disease outcomes. Tryptophan 16-26 indoleamine 2,3-dioxygenase 1 Homo sapiens 48-77 31795096-1 2019 Cancers express tryptophan catabolising enzymes indoleamine 2,3-dioxygenase 1 (IDO1) and tryptophan 2,3-dioxygenase (TDO2) to produce immunosuppressive tryptophan metabolites that undermine patients" immune systems, leading to poor disease outcomes. Tryptophan 16-26 indoleamine 2,3-dioxygenase 1 Homo sapiens 79-83 31729973-8 2019 RESULTS: Hemodialysis kynurenine and kynurenine/L - tryptophan blood ratio levels were significantly higher, when compared to the control group, indicating an increased indoleamine 2,3-dioxygenase-1 activity in hemodialysis patients. Tryptophan 52-62 indoleamine 2,3-dioxygenase 1 Homo sapiens 169-198 31489989-2 2019 Immune activation after stimulation with interferon-gamma leads to increased production of neopterin but also results in increased tryptophan catabolism through indoleamine 2,3-dioxygenase (IDO). Tryptophan 131-141 indoleamine 2,3-dioxygenase 1 Homo sapiens 161-188 31489989-2 2019 Immune activation after stimulation with interferon-gamma leads to increased production of neopterin but also results in increased tryptophan catabolism through indoleamine 2,3-dioxygenase (IDO). Tryptophan 131-141 indoleamine 2,3-dioxygenase 1 Homo sapiens 190-193 31253481-1 2019 PURPOSES: Indoleamine-2,3-dioxygenase-1 (IDO1) is a key enzyme of tryptophan metabolism which regulates T cell function in immune cells and little is known about the role of IDO1 expression in bladder cancer cells. Tryptophan 66-76 indoleamine 2,3-dioxygenase 1 Homo sapiens 41-45 29683396-3 2019 However, a clear biological framework linking dysfunctions in Trp metabolism via 5-HT and Kyn, cortisol, and the activities of tryptophan and indoleamino 2,3-dioxygenase (TDO, IDO) enzymes has not been yet clarified in MDD with or without suicidal behaviours.Methods: We analysed peripheral markers of Trp via 5-HT and Kyn pathways, Kyn/Trp ratio as a measure of TDO/IDO activities, cortisol, and psychopathology in 73 non-suicidal and 56 suicidal MDD patients, and in 40 healthy controls.Results: Plasma Trp levels were lower and the ratio Kyn/Trp higher in suicidal MDD than in non-suicidal MDD patients and controls. Tryptophan 62-65 indoleamine 2,3-dioxygenase 1 Homo sapiens 367-370 29683396-3 2019 However, a clear biological framework linking dysfunctions in Trp metabolism via 5-HT and Kyn, cortisol, and the activities of tryptophan and indoleamino 2,3-dioxygenase (TDO, IDO) enzymes has not been yet clarified in MDD with or without suicidal behaviours.Methods: We analysed peripheral markers of Trp via 5-HT and Kyn pathways, Kyn/Trp ratio as a measure of TDO/IDO activities, cortisol, and psychopathology in 73 non-suicidal and 56 suicidal MDD patients, and in 40 healthy controls.Results: Plasma Trp levels were lower and the ratio Kyn/Trp higher in suicidal MDD than in non-suicidal MDD patients and controls. Tryptophan 302-305 indoleamine 2,3-dioxygenase 1 Homo sapiens 176-179 29683396-3 2019 However, a clear biological framework linking dysfunctions in Trp metabolism via 5-HT and Kyn, cortisol, and the activities of tryptophan and indoleamino 2,3-dioxygenase (TDO, IDO) enzymes has not been yet clarified in MDD with or without suicidal behaviours.Methods: We analysed peripheral markers of Trp via 5-HT and Kyn pathways, Kyn/Trp ratio as a measure of TDO/IDO activities, cortisol, and psychopathology in 73 non-suicidal and 56 suicidal MDD patients, and in 40 healthy controls.Results: Plasma Trp levels were lower and the ratio Kyn/Trp higher in suicidal MDD than in non-suicidal MDD patients and controls. Tryptophan 302-305 indoleamine 2,3-dioxygenase 1 Homo sapiens 176-179 29683396-3 2019 However, a clear biological framework linking dysfunctions in Trp metabolism via 5-HT and Kyn, cortisol, and the activities of tryptophan and indoleamino 2,3-dioxygenase (TDO, IDO) enzymes has not been yet clarified in MDD with or without suicidal behaviours.Methods: We analysed peripheral markers of Trp via 5-HT and Kyn pathways, Kyn/Trp ratio as a measure of TDO/IDO activities, cortisol, and psychopathology in 73 non-suicidal and 56 suicidal MDD patients, and in 40 healthy controls.Results: Plasma Trp levels were lower and the ratio Kyn/Trp higher in suicidal MDD than in non-suicidal MDD patients and controls. Tryptophan 302-305 indoleamine 2,3-dioxygenase 1 Homo sapiens 176-179 29683396-3 2019 However, a clear biological framework linking dysfunctions in Trp metabolism via 5-HT and Kyn, cortisol, and the activities of tryptophan and indoleamino 2,3-dioxygenase (TDO, IDO) enzymes has not been yet clarified in MDD with or without suicidal behaviours.Methods: We analysed peripheral markers of Trp via 5-HT and Kyn pathways, Kyn/Trp ratio as a measure of TDO/IDO activities, cortisol, and psychopathology in 73 non-suicidal and 56 suicidal MDD patients, and in 40 healthy controls.Results: Plasma Trp levels were lower and the ratio Kyn/Trp higher in suicidal MDD than in non-suicidal MDD patients and controls. Tryptophan 302-305 indoleamine 2,3-dioxygenase 1 Homo sapiens 176-179 31737575-4 2019 IDO is the rate-limiting enzyme converting tryptophan to kynurenine. Tryptophan 43-53 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 31737575-8 2019 In this review, we explore the link between IDO-mediated tryptophan catabolism and the presence of active TB disease in HIV-infected patients. Tryptophan 57-67 indoleamine 2,3-dioxygenase 1 Homo sapiens 44-47 31681271-9 2019 Remarkably, in contrast to the prevention of sepsis death of animal model by IDO1 inhibition before sepsis initiation, we demonstrated that the combination therapy of IDO1 inhibition by 1-methyl-D-tryptophan (1-MT) and tryptophan supplementation rather than 1-MT administration alone after sepsis onset rescued sepsis animals, highlighting the translational significance of tryptophan restoration in IDO1 targeting therapy of severe inflammatory diseases like sepsis. Tryptophan 197-207 indoleamine 2,3-dioxygenase 1 Homo sapiens 167-171 31681271-9 2019 Remarkably, in contrast to the prevention of sepsis death of animal model by IDO1 inhibition before sepsis initiation, we demonstrated that the combination therapy of IDO1 inhibition by 1-methyl-D-tryptophan (1-MT) and tryptophan supplementation rather than 1-MT administration alone after sepsis onset rescued sepsis animals, highlighting the translational significance of tryptophan restoration in IDO1 targeting therapy of severe inflammatory diseases like sepsis. Tryptophan 197-207 indoleamine 2,3-dioxygenase 1 Homo sapiens 167-171 31681271-9 2019 Remarkably, in contrast to the prevention of sepsis death of animal model by IDO1 inhibition before sepsis initiation, we demonstrated that the combination therapy of IDO1 inhibition by 1-methyl-D-tryptophan (1-MT) and tryptophan supplementation rather than 1-MT administration alone after sepsis onset rescued sepsis animals, highlighting the translational significance of tryptophan restoration in IDO1 targeting therapy of severe inflammatory diseases like sepsis. Tryptophan 219-229 indoleamine 2,3-dioxygenase 1 Homo sapiens 167-171 31681271-9 2019 Remarkably, in contrast to the prevention of sepsis death of animal model by IDO1 inhibition before sepsis initiation, we demonstrated that the combination therapy of IDO1 inhibition by 1-methyl-D-tryptophan (1-MT) and tryptophan supplementation rather than 1-MT administration alone after sepsis onset rescued sepsis animals, highlighting the translational significance of tryptophan restoration in IDO1 targeting therapy of severe inflammatory diseases like sepsis. Tryptophan 219-229 indoleamine 2,3-dioxygenase 1 Homo sapiens 167-171 31525930-1 2019 Indoleamine 2,3-dioxygenase 1 (IDO1) catalyzes the rate-limiting step in the kynurenine pathway of tryptophan metabolism, which is involved in immunity, neuronal function, and aging. Tryptophan 99-109 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-29 31525930-1 2019 Indoleamine 2,3-dioxygenase 1 (IDO1) catalyzes the rate-limiting step in the kynurenine pathway of tryptophan metabolism, which is involved in immunity, neuronal function, and aging. Tryptophan 99-109 indoleamine 2,3-dioxygenase 1 Homo sapiens 31-35 31461509-0 2019 Host cell depletion of tryptophan by IFNgamma-induced Indoleamine 2,3-dioxygenase 1 (IDO1) inhibits lysosomal replication of Coxiella burnetii. Tryptophan 23-33 indoleamine 2,3-dioxygenase 1 Homo sapiens 85-89 31436417-1 2019 Indoleamine 2,3-dioxygenase (IDO1) is a heme enzyme that catalyzes the oxygenation of the indole ring of tryptophan to afford N-formylkynurenine. Tryptophan 105-115 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-33 31436417-10 2019 Tryptophan significantly enhanced the relatively lower-affinity binding of hydrogen sulfide to IDO1, inspiring the use of the small molecule 3-mercaptoindole (3MI), which selectively binds to and activates ferric IDO1. Tryptophan 0-10 indoleamine 2,3-dioxygenase 1 Homo sapiens 95-99 31436417-10 2019 Tryptophan significantly enhanced the relatively lower-affinity binding of hydrogen sulfide to IDO1, inspiring the use of the small molecule 3-mercaptoindole (3MI), which selectively binds to and activates ferric IDO1. Tryptophan 0-10 indoleamine 2,3-dioxygenase 1 Homo sapiens 213-217 31788580-1 2019 Indoleamine 2,3-dioxygenase (IDO), an intracellular enzyme responsible for catalyzing the rate limiting step of tryptophan catabolism, plays a critical role in immune cell suppression and tolerance. Tryptophan 112-122 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 31788580-1 2019 Indoleamine 2,3-dioxygenase (IDO), an intracellular enzyme responsible for catalyzing the rate limiting step of tryptophan catabolism, plays a critical role in immune cell suppression and tolerance. Tryptophan 112-122 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 31431359-1 2019 Indoleamine 2,3-dioxygenase 1 (IDO1) is a heme-containing enzyme that acts on the first and rate-limiting step of the tryptophan/kynurenine pathway. Tryptophan 118-128 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-29 31431359-1 2019 Indoleamine 2,3-dioxygenase 1 (IDO1) is a heme-containing enzyme that acts on the first and rate-limiting step of the tryptophan/kynurenine pathway. Tryptophan 118-128 indoleamine 2,3-dioxygenase 1 Homo sapiens 31-35 31233921-1 2019 Indoleamine 2, 3-dioxygenase 1 (IDO1) plays a key role in tryptophan catabolism which is an important mechanism in immune tolerance. Tryptophan 58-68 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-30 31233921-1 2019 Indoleamine 2, 3-dioxygenase 1 (IDO1) plays a key role in tryptophan catabolism which is an important mechanism in immune tolerance. Tryptophan 58-68 indoleamine 2,3-dioxygenase 1 Homo sapiens 32-36 31091352-1 2019 IDO is an enzyme that participates in the degradation of tryptophan (Trp), which is an essential amino acid necessary for vital cellular processes. Tryptophan 57-67 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 31091352-1 2019 IDO is an enzyme that participates in the degradation of tryptophan (Trp), which is an essential amino acid necessary for vital cellular processes. Tryptophan 69-72 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 31091352-2 2019 The degradation of Trp and the metabolites generated by the enzymatic activity of IDO can have immunomodulating effects, notably over T cells, which are particularly sensitive to the absence of Trp and leads to the inhibition of T cell activation, cell death, and the suppression of T cell effector functions. Tryptophan 19-22 indoleamine 2,3-dioxygenase 1 Homo sapiens 82-85 31091352-2 2019 The degradation of Trp and the metabolites generated by the enzymatic activity of IDO can have immunomodulating effects, notably over T cells, which are particularly sensitive to the absence of Trp and leads to the inhibition of T cell activation, cell death, and the suppression of T cell effector functions. Tryptophan 194-197 indoleamine 2,3-dioxygenase 1 Homo sapiens 82-85 31412167-9 2019 CONCLUSIONS: The upregulation of IDO expression in leukocytes and squamous cells in HPV-associated SIL and SCC suggests that immunosuppressive mechanisms involving tryptophan metabolism may have a role in cervical carcinogenesis. Tryptophan 164-174 indoleamine 2,3-dioxygenase 1 Homo sapiens 33-36 31461509-8 2019 IDO1 is an enzyme that catabolizes cellular tryptophan to kynurenine metabolites thereby reducing tryptophan availability in cells. Tryptophan 44-54 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-4 31461509-8 2019 IDO1 is an enzyme that catabolizes cellular tryptophan to kynurenine metabolites thereby reducing tryptophan availability in cells. Tryptophan 98-108 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-4 31488951-1 2019 The plasma kynurenine to tryptophan ([Kyn]/[Trp]) ratio is frequently used to express or reflect the activity of the extrahepatic Trp-degrading enzyme indoleamine 2,3-dioxygenase (IDO). Tryptophan 25-35 indoleamine 2,3-dioxygenase 1 Homo sapiens 180-183 31488951-1 2019 The plasma kynurenine to tryptophan ([Kyn]/[Trp]) ratio is frequently used to express or reflect the activity of the extrahepatic Trp-degrading enzyme indoleamine 2,3-dioxygenase (IDO). Tryptophan 130-133 indoleamine 2,3-dioxygenase 1 Homo sapiens 180-183 31405517-1 2019 Human indoleamine 2,3-dioxygenase 1 (IDO) is a heme enzyme that catalyzes the first reaction of the main metabolic pathway of L-tryptophan (Trp) to produce N-formylkynurenin. Tryptophan 126-138 indoleamine 2,3-dioxygenase 1 Homo sapiens 6-35 31405517-1 2019 Human indoleamine 2,3-dioxygenase 1 (IDO) is a heme enzyme that catalyzes the first reaction of the main metabolic pathway of L-tryptophan (Trp) to produce N-formylkynurenin. Tryptophan 126-138 indoleamine 2,3-dioxygenase 1 Homo sapiens 37-40 31405517-1 2019 Human indoleamine 2,3-dioxygenase 1 (IDO) is a heme enzyme that catalyzes the first reaction of the main metabolic pathway of L-tryptophan (Trp) to produce N-formylkynurenin. Tryptophan 140-143 indoleamine 2,3-dioxygenase 1 Homo sapiens 6-35 31405517-1 2019 Human indoleamine 2,3-dioxygenase 1 (IDO) is a heme enzyme that catalyzes the first reaction of the main metabolic pathway of L-tryptophan (Trp) to produce N-formylkynurenin. Tryptophan 140-143 indoleamine 2,3-dioxygenase 1 Homo sapiens 37-40 31405517-3 2019 For establishment of the chemical mechanism of this unique enzymatic reaction, it is necessary to determine the conformation and electronic state of the substrate Trp bound to IDO. Tryptophan 163-166 indoleamine 2,3-dioxygenase 1 Homo sapiens 176-179 31405517-4 2019 In this study, we measured the ultraviolet resonance Raman spectra of IDO in the presence of Trp to detect the vibrational modes of the substrate Trp. Tryptophan 93-96 indoleamine 2,3-dioxygenase 1 Homo sapiens 70-73 31405517-4 2019 In this study, we measured the ultraviolet resonance Raman spectra of IDO in the presence of Trp to detect the vibrational modes of the substrate Trp. Tryptophan 146-149 indoleamine 2,3-dioxygenase 1 Homo sapiens 70-73 31481962-1 2019 Indoleamine 2,3-dioxygenase 1 (IDO1) catalyzes the first step in the kynurenine pathway of tryptophan (Trp) degradation that produces several biologically active Trp metabolites. Tryptophan 91-101 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-29 31481962-1 2019 Indoleamine 2,3-dioxygenase 1 (IDO1) catalyzes the first step in the kynurenine pathway of tryptophan (Trp) degradation that produces several biologically active Trp metabolites. Tryptophan 91-101 indoleamine 2,3-dioxygenase 1 Homo sapiens 31-35 31481962-1 2019 Indoleamine 2,3-dioxygenase 1 (IDO1) catalyzes the first step in the kynurenine pathway of tryptophan (Trp) degradation that produces several biologically active Trp metabolites. Tryptophan 103-106 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-29 31481962-1 2019 Indoleamine 2,3-dioxygenase 1 (IDO1) catalyzes the first step in the kynurenine pathway of tryptophan (Trp) degradation that produces several biologically active Trp metabolites. Tryptophan 103-106 indoleamine 2,3-dioxygenase 1 Homo sapiens 31-35 31481962-1 2019 Indoleamine 2,3-dioxygenase 1 (IDO1) catalyzes the first step in the kynurenine pathway of tryptophan (Trp) degradation that produces several biologically active Trp metabolites. Tryptophan 162-165 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-29 31481962-1 2019 Indoleamine 2,3-dioxygenase 1 (IDO1) catalyzes the first step in the kynurenine pathway of tryptophan (Trp) degradation that produces several biologically active Trp metabolites. Tryptophan 162-165 indoleamine 2,3-dioxygenase 1 Homo sapiens 31-35 32055299-1 2019 Indoleamine 2,3-dioxygenase 1 (IDO1), an important immunoregulatory enzyme ubiquitously expressed in various tissues and cells, plays a key role in tryptophan metabolism via the kynurenine pathway and has emerged as an attractive therapeutic target for the treatment of cancer and other diseases, such as Alzheimer"s disease and arthritis. Tryptophan 148-158 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-29 32055299-1 2019 Indoleamine 2,3-dioxygenase 1 (IDO1), an important immunoregulatory enzyme ubiquitously expressed in various tissues and cells, plays a key role in tryptophan metabolism via the kynurenine pathway and has emerged as an attractive therapeutic target for the treatment of cancer and other diseases, such as Alzheimer"s disease and arthritis. Tryptophan 148-158 indoleamine 2,3-dioxygenase 1 Homo sapiens 31-35 32055299-2 2019 IDO1 has diverse biological roles in immune suppression and tumor progression by tryptophan catabolism. Tryptophan 81-91 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-4 32055299-5 2019 In this review, IDO1 inhibitors are grouped as tryptophan derivatives, inhibitors with an imidazole, 1,2,3-triazole or tetrazole scaffold, inhibitors with quinone or iminoquinone, N-hydroxyamidines and other derivatives, and their enzymatic inhibitory activity, selectivity and other biological activities are also introduced and summarized. Tryptophan 47-57 indoleamine 2,3-dioxygenase 1 Homo sapiens 16-20 31286779-3 2019 Indoleamine 2,3-dioxygenase-1 (IDO1), a tryptophan catabolic enzyme overexpressed in tumor-draining lymph nodes (TDLNs) and tumor tissues, plays a pivotal role in the generation of the immunosuppressive microenvironment. Tryptophan 40-50 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-29 31286779-3 2019 Indoleamine 2,3-dioxygenase-1 (IDO1), a tryptophan catabolic enzyme overexpressed in tumor-draining lymph nodes (TDLNs) and tumor tissues, plays a pivotal role in the generation of the immunosuppressive microenvironment. Tryptophan 40-50 indoleamine 2,3-dioxygenase 1 Homo sapiens 31-35 30679801-4 2019 MSCs use tryptophan-depleting IDO to suppress T-cells. Tryptophan 9-19 indoleamine 2,3-dioxygenase 1 Homo sapiens 30-33 31306164-3 2019 Indoleamine-2,3-dioxygenase (IDO) enzyme activity is the first and rate-limiting step in tryptophan catabolism and is measured by the kynurenine to tryptophan ratio (KTR). Tryptophan 89-99 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 31306164-3 2019 Indoleamine-2,3-dioxygenase (IDO) enzyme activity is the first and rate-limiting step in tryptophan catabolism and is measured by the kynurenine to tryptophan ratio (KTR). Tryptophan 148-158 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 31006829-7 2019 IFN-gamma significantly inhibited hCM proliferation, and IFN-gamma-induced IDO expression caused cell cycle arrest in G0/G1 through tryptophan depletion. Tryptophan 132-142 indoleamine 2,3-dioxygenase 1 Homo sapiens 75-78 31324754-2 2019 Indoleamine 2,3-dioxygenase 1 (IDO1) is an enzyme that participates in tumor immune escape primarily by catalyzing tryptophan to L-kynurenine. Tryptophan 115-125 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-29 31324754-2 2019 Indoleamine 2,3-dioxygenase 1 (IDO1) is an enzyme that participates in tumor immune escape primarily by catalyzing tryptophan to L-kynurenine. Tryptophan 115-125 indoleamine 2,3-dioxygenase 1 Homo sapiens 31-35 31315643-1 2019 BACKGROUND: IDO1 (Indoleamine 2,3-dioxygenase 1) inhibits host anti-tumor immune response by exhausting tryptophan in tumor microenvironment, but the pathogenic mechanisms of IDO1 in gastric cancer (GC) cells need to be further explored. Tryptophan 104-114 indoleamine 2,3-dioxygenase 1 Homo sapiens 12-16 31315643-1 2019 BACKGROUND: IDO1 (Indoleamine 2,3-dioxygenase 1) inhibits host anti-tumor immune response by exhausting tryptophan in tumor microenvironment, but the pathogenic mechanisms of IDO1 in gastric cancer (GC) cells need to be further explored. Tryptophan 104-114 indoleamine 2,3-dioxygenase 1 Homo sapiens 18-47 31417567-4 2019 Particularly, a multitude of IDO1 inhibiting tryptophan analogs are widely applied in several clinical trials. Tryptophan 45-55 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-33 31417567-7 2019 In this review we provide a deeper insight into the physiological consequences of an IDO1 inhibiting therapy based on TRP related molecules. Tryptophan 118-121 indoleamine 2,3-dioxygenase 1 Homo sapiens 85-89 31357483-6 2019 Non-functional IDO2, combined with well-established substrate inhibition of IDO1 and kinetic asymmetry of the large neutral amino acid transporter, LAT1, yielded a mathematical model of tryptophan metabolism that displays both physiological and pathological steady-states. Tryptophan 186-196 indoleamine 2,3-dioxygenase 1 Homo sapiens 76-80 30990966-0 2019 Capping Silica Nanoparticles with Tryptophan-Mediated Cucurbit[8]uril Complex for Targeted Intracellular Drug Delivery Triggered by Tumor-Overexpressed IDO1 Enzyme. Tryptophan 34-44 indoleamine 2,3-dioxygenase 1 Homo sapiens 152-156 30990966-3 2019 The supramolecular interaction between tryptophan and cucurbit[8]uril is disrupted in the presence of indoleamine 2,3-dioxygenase 1 (IDO1) enzyme (abundant in the tumor intracellular microenvironment), which catalyzes the metabolism of tryptophan into N-formylkynurenine, resulting in the disassembly of the "gate-keeper" of the nanocarriers and intracellular release of therapeutics exclusively in tumor cells. Tryptophan 39-49 indoleamine 2,3-dioxygenase 1 Homo sapiens 102-131 30990966-3 2019 The supramolecular interaction between tryptophan and cucurbit[8]uril is disrupted in the presence of indoleamine 2,3-dioxygenase 1 (IDO1) enzyme (abundant in the tumor intracellular microenvironment), which catalyzes the metabolism of tryptophan into N-formylkynurenine, resulting in the disassembly of the "gate-keeper" of the nanocarriers and intracellular release of therapeutics exclusively in tumor cells. Tryptophan 39-49 indoleamine 2,3-dioxygenase 1 Homo sapiens 133-137 30990966-3 2019 The supramolecular interaction between tryptophan and cucurbit[8]uril is disrupted in the presence of indoleamine 2,3-dioxygenase 1 (IDO1) enzyme (abundant in the tumor intracellular microenvironment), which catalyzes the metabolism of tryptophan into N-formylkynurenine, resulting in the disassembly of the "gate-keeper" of the nanocarriers and intracellular release of therapeutics exclusively in tumor cells. Tryptophan 236-246 indoleamine 2,3-dioxygenase 1 Homo sapiens 102-131 30990966-3 2019 The supramolecular interaction between tryptophan and cucurbit[8]uril is disrupted in the presence of indoleamine 2,3-dioxygenase 1 (IDO1) enzyme (abundant in the tumor intracellular microenvironment), which catalyzes the metabolism of tryptophan into N-formylkynurenine, resulting in the disassembly of the "gate-keeper" of the nanocarriers and intracellular release of therapeutics exclusively in tumor cells. Tryptophan 236-246 indoleamine 2,3-dioxygenase 1 Homo sapiens 133-137 30847484-4 2019 Indoleamine 2,3-dioxygenase (IDO), the rate-limiting enzyme in the kynurenine pathway of tryptophan (Trp) degradation, is modulated by inflammation and regarded as a key molecule driving immunotolerance and immunosuppressive mechanisms. Tryptophan 89-99 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 30847484-4 2019 Indoleamine 2,3-dioxygenase (IDO), the rate-limiting enzyme in the kynurenine pathway of tryptophan (Trp) degradation, is modulated by inflammation and regarded as a key molecule driving immunotolerance and immunosuppressive mechanisms. Tryptophan 89-99 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 30847484-4 2019 Indoleamine 2,3-dioxygenase (IDO), the rate-limiting enzyme in the kynurenine pathway of tryptophan (Trp) degradation, is modulated by inflammation and regarded as a key molecule driving immunotolerance and immunosuppressive mechanisms. Tryptophan 101-104 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 30847484-4 2019 Indoleamine 2,3-dioxygenase (IDO), the rate-limiting enzyme in the kynurenine pathway of tryptophan (Trp) degradation, is modulated by inflammation and regarded as a key molecule driving immunotolerance and immunosuppressive mechanisms. Tryptophan 101-104 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 30847484-5 2019 A large body of evidence indicates that IDO-mediated Trp metabolism is involved directly or indirectly in atherogenesis. Tryptophan 53-56 indoleamine 2,3-dioxygenase 1 Homo sapiens 40-43 31239324-1 2019 Kynurenine, which is generated from tryptophan by indoleamine 2,3-dioxygenase 1 (IDO1), binds to the aryl hydrocarbon receptor (AhR). Tryptophan 36-46 indoleamine 2,3-dioxygenase 1 Homo sapiens 50-79 31239324-1 2019 Kynurenine, which is generated from tryptophan by indoleamine 2,3-dioxygenase 1 (IDO1), binds to the aryl hydrocarbon receptor (AhR). Tryptophan 36-46 indoleamine 2,3-dioxygenase 1 Homo sapiens 81-85 31186442-2 2019 Indoleamine 2,3-dioxygenase (IDO), the rate-limiting enzyme in the tryptophan-kynurenine pathway, is positively associated with cardiac events, and may be relevant to cancer. Tryptophan 67-77 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 31186442-2 2019 Indoleamine 2,3-dioxygenase (IDO), the rate-limiting enzyme in the tryptophan-kynurenine pathway, is positively associated with cardiac events, and may be relevant to cancer. Tryptophan 67-77 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 31181125-2 2019 Indoleamine-pyrrole 2,3-dioxygenase-1 (IDO-1) expression is associated with low serum tryptophan concentrations and is increased in the gastrointestinal tract of humans with inflammatory bowel disease (IBD). Tryptophan 86-96 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-37 31181125-2 2019 Indoleamine-pyrrole 2,3-dioxygenase-1 (IDO-1) expression is associated with low serum tryptophan concentrations and is increased in the gastrointestinal tract of humans with inflammatory bowel disease (IBD). Tryptophan 86-96 indoleamine 2,3-dioxygenase 1 Homo sapiens 39-44 31231617-3 2019 In human cells, the interferon-gamma inducible indoleamine 2,3-dioxygenase 1 (IDO1) is an antimicrobial effector mechanism that degrades tryptophan to kynurenine and thus limits pathogen proliferation in vitro. Tryptophan 137-147 indoleamine 2,3-dioxygenase 1 Homo sapiens 78-82 31119110-3 2019 IFN-gamma-inducible indole-2,3-dioxygenase 1 (IDO1), which mediates tryptophan degradation, has a major role in anti-T. gondii immune responses in various human cells. Tryptophan 68-78 indoleamine 2,3-dioxygenase 1 Homo sapiens 20-44 31082908-2 2019 SUMMARY BACKGROUND DATA: IDO1 is a primary enzyme that generates immunosuppressive metabolites such as tryptophan and kynurenine. Tryptophan 103-113 indoleamine 2,3-dioxygenase 1 Homo sapiens 25-29 30770348-1 2019 PURPOSE: IDO1 induces immune suppression in T cells through l-tryptophan (Trp) depletion and kynurenine (Kyn) accumulation in the local tumor microenvironment, suppressing effector T cells and hyperactivating regulatory T cells (Treg). Tryptophan 60-72 indoleamine 2,3-dioxygenase 1 Homo sapiens 9-13 30770348-1 2019 PURPOSE: IDO1 induces immune suppression in T cells through l-tryptophan (Trp) depletion and kynurenine (Kyn) accumulation in the local tumor microenvironment, suppressing effector T cells and hyperactivating regulatory T cells (Treg). Tryptophan 74-77 indoleamine 2,3-dioxygenase 1 Homo sapiens 9-13 30959226-1 2019 Abnormalities in the kynurenine pathway (KP) have been implicated in the cognitive deficits of psychiatry disorders, possibly through cytokines that increase the activity of indoleamine-2,3 dioxygenase (IDO), a key enzyme for tryptophan-to-kynurenine conversion. Tryptophan 226-236 indoleamine 2,3-dioxygenase 1 Homo sapiens 174-201 30959226-1 2019 Abnormalities in the kynurenine pathway (KP) have been implicated in the cognitive deficits of psychiatry disorders, possibly through cytokines that increase the activity of indoleamine-2,3 dioxygenase (IDO), a key enzyme for tryptophan-to-kynurenine conversion. Tryptophan 226-236 indoleamine 2,3-dioxygenase 1 Homo sapiens 203-206 31096672-1 2019 IDO1, a key dioxygenase in tryptophan-kynurenine metabolism, appeared in the last 10 years at the vanguard of druggable targets in cancer therapy due to its well-established role both in immune escape and inflammatory neovascularization. Tryptophan 27-37 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-4 31075929-2 2019 IDO suppresses T cell immunity by catabolizing tryptophan into kynurenine (KYN), which induces apoptosis in T effector cells and enhances T regulatory cells, providing a powerful immunosuppressive mechanism in tumors. Tryptophan 47-57 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 31134053-3 2019 The role played by the enzyme indoleamine 2,3-dioxygenase 1 (IDO1), which catalyzes the first and rate-limiting step of tryptophan catabolism along the kynurenine pathway, is increasingly being recognized, but whether and how genetic variation of IDO1 influences the risk of aspergillosis in susceptible patients is incompletely understood. Tryptophan 120-130 indoleamine 2,3-dioxygenase 1 Homo sapiens 30-59 31134053-3 2019 The role played by the enzyme indoleamine 2,3-dioxygenase 1 (IDO1), which catalyzes the first and rate-limiting step of tryptophan catabolism along the kynurenine pathway, is increasingly being recognized, but whether and how genetic variation of IDO1 influences the risk of aspergillosis in susceptible patients is incompletely understood. Tryptophan 120-130 indoleamine 2,3-dioxygenase 1 Homo sapiens 61-65 31134053-3 2019 The role played by the enzyme indoleamine 2,3-dioxygenase 1 (IDO1), which catalyzes the first and rate-limiting step of tryptophan catabolism along the kynurenine pathway, is increasingly being recognized, but whether and how genetic variation of IDO1 influences the risk of aspergillosis in susceptible patients is incompletely understood. Tryptophan 120-130 indoleamine 2,3-dioxygenase 1 Homo sapiens 247-251 30623620-7 2019 IDO-1 enzyme activity was calculated using tryptophan and kynurenine levels. Tryptophan 43-53 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-5 31119110-3 2019 IFN-gamma-inducible indole-2,3-dioxygenase 1 (IDO1), which mediates tryptophan degradation, has a major role in anti-T. gondii immune responses in various human cells. Tryptophan 68-78 indoleamine 2,3-dioxygenase 1 Homo sapiens 46-50 31191872-0 2019 Synthesis and initial evaluation of radioactive 5-I-alpha-methyl-tryptophan: a Trp based agent targeting IDO-1. Tryptophan 79-82 indoleamine 2,3-dioxygenase 1 Homo sapiens 105-110 31190914-3 2019 Patients and methods: Plasma indoleamine 2,3-dioxygenase (IDO) was measured by the ratio of kynurenine (Kyn) to tryptophan (Trp) concentrations, using high performance liquid chromatography-mass spectrometry (LC-MS/MS). Tryptophan 112-122 indoleamine 2,3-dioxygenase 1 Homo sapiens 58-61 31190914-3 2019 Patients and methods: Plasma indoleamine 2,3-dioxygenase (IDO) was measured by the ratio of kynurenine (Kyn) to tryptophan (Trp) concentrations, using high performance liquid chromatography-mass spectrometry (LC-MS/MS). Tryptophan 124-127 indoleamine 2,3-dioxygenase 1 Homo sapiens 58-61 30983018-4 2019 To understand the mechanism of this endotoxin tolerance (ET) phenomenon in buffalo GCs, we have further studied the genome-wide transcriptomic analyses in buffalo GCs (unpublished data) and identified indoleamine 2,3-dioxygenase 1 (IDO1) gene, known to be involved in tryptophan catabolism, was found to be highly upregulated in endotoxin-tolerant GCs. Tryptophan 268-278 indoleamine 2,3-dioxygenase 1 Homo sapiens 201-230 30983018-4 2019 To understand the mechanism of this endotoxin tolerance (ET) phenomenon in buffalo GCs, we have further studied the genome-wide transcriptomic analyses in buffalo GCs (unpublished data) and identified indoleamine 2,3-dioxygenase 1 (IDO1) gene, known to be involved in tryptophan catabolism, was found to be highly upregulated in endotoxin-tolerant GCs. Tryptophan 268-278 indoleamine 2,3-dioxygenase 1 Homo sapiens 232-236 30107503-1 2019 BACKGROUND: Indoleamine 2,3-dioxygenase (IDO) is an immunoregulatory enzyme that metabolizes tryptophan to immunosuppressive kynurenines. Tryptophan 93-103 indoleamine 2,3-dioxygenase 1 Homo sapiens 41-44 30797943-4 2019 We examined here current knowledge of indoleamine 2,3-dioxygenase 1 (IDO1) and arginase 1 (ARG1), the main enzymes catabolizing tryptophan and arginine, respectively, in organ-specific and systemic autoimmune diseases as well as in the development of autoantibodies to therapeutic proteins. Tryptophan 128-138 indoleamine 2,3-dioxygenase 1 Homo sapiens 38-67 30797943-4 2019 We examined here current knowledge of indoleamine 2,3-dioxygenase 1 (IDO1) and arginase 1 (ARG1), the main enzymes catabolizing tryptophan and arginine, respectively, in organ-specific and systemic autoimmune diseases as well as in the development of autoantibodies to therapeutic proteins. Tryptophan 128-138 indoleamine 2,3-dioxygenase 1 Homo sapiens 69-73 30714436-3 2019 Indoleamine 2,3-dioxygenase (IDO) that initiates the degradation of trp and tryptophanyl-tRNA synthetase (TTS) essential for tryptophan synthesis, regulate trp bioavailability. Tryptophan 68-71 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 30910218-4 2019 Mass spectrometer analysis of human DCs treated with CTB-INS suggest that upregulation of the tryptophan catabolic enzyme indoleamine 2, 3-dioxygenase (IDO1) is responsible for inhibiting DC activation thereby resulting in a state of immunological tolerance within the DC. Tryptophan 94-104 indoleamine 2,3-dioxygenase 1 Homo sapiens 152-156 30910218-7 2019 LPS stimulation of increased levels of IDO1 in the DC resulted in increased secretion of kynurenines, tryptophan degradation products known to suppress DC mediated pro-inflammatory T cell differentiation and to stimulate the proliferation of regulatory T cells (Tregs). Tryptophan 102-112 indoleamine 2,3-dioxygenase 1 Homo sapiens 39-43 30714436-3 2019 Indoleamine 2,3-dioxygenase (IDO) that initiates the degradation of trp and tryptophanyl-tRNA synthetase (TTS) essential for tryptophan synthesis, regulate trp bioavailability. Tryptophan 68-71 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 30714436-3 2019 Indoleamine 2,3-dioxygenase (IDO) that initiates the degradation of trp and tryptophanyl-tRNA synthetase (TTS) essential for tryptophan synthesis, regulate trp bioavailability. Tryptophan 76-86 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 30714436-3 2019 Indoleamine 2,3-dioxygenase (IDO) that initiates the degradation of trp and tryptophanyl-tRNA synthetase (TTS) essential for tryptophan synthesis, regulate trp bioavailability. Tryptophan 76-86 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 30714436-3 2019 Indoleamine 2,3-dioxygenase (IDO) that initiates the degradation of trp and tryptophanyl-tRNA synthetase (TTS) essential for tryptophan synthesis, regulate trp bioavailability. Tryptophan 156-159 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 30714436-3 2019 Indoleamine 2,3-dioxygenase (IDO) that initiates the degradation of trp and tryptophanyl-tRNA synthetase (TTS) essential for tryptophan synthesis, regulate trp bioavailability. Tryptophan 156-159 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 30377198-0 2019 Reimagining IDO Pathway Inhibition in Cancer Immunotherapy via Downstream Focus on the Tryptophan-Kynurenine-Aryl Hydrocarbon Axis. Tryptophan 87-97 indoleamine 2,3-dioxygenase 1 Homo sapiens 12-15 30870462-5 2019 In this study, we demonstrate that IDO-mediated tryptophan starvation triggered by human MSCs inhibits T-cell activation and proliferation through induction of cellular stress. Tryptophan 48-58 indoleamine 2,3-dioxygenase 1 Homo sapiens 35-38 30832593-4 2019 IDO1 catalyzes the degradation of tryptophan, which can eliminate C. trachomatis infection in vitro. Tryptophan 34-44 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-4 30832615-1 2019 BACKGROUND: Indoleamine 2, 3-dioxygenase (IDO) is a key enzyme in the degradation of tryptophan (Trp) to kynurenine (Kyn). Tryptophan 85-95 indoleamine 2,3-dioxygenase 1 Homo sapiens 12-40 30832615-1 2019 BACKGROUND: Indoleamine 2, 3-dioxygenase (IDO) is a key enzyme in the degradation of tryptophan (Trp) to kynurenine (Kyn). Tryptophan 85-95 indoleamine 2,3-dioxygenase 1 Homo sapiens 42-45 30832615-1 2019 BACKGROUND: Indoleamine 2, 3-dioxygenase (IDO) is a key enzyme in the degradation of tryptophan (Trp) to kynurenine (Kyn). Tryptophan 97-100 indoleamine 2,3-dioxygenase 1 Homo sapiens 12-40 30832615-1 2019 BACKGROUND: Indoleamine 2, 3-dioxygenase (IDO) is a key enzyme in the degradation of tryptophan (Trp) to kynurenine (Kyn). Tryptophan 97-100 indoleamine 2,3-dioxygenase 1 Homo sapiens 42-45 30377198-5 2019 Indoleamine 2,3-dioxygenase 1 (IDO1), a principle enzyme in Trp catabolism, is the target of small-molecule inhibitors in clinical development in combination with PD-1 checkpoint inhibitors. Tryptophan 60-63 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-29 30377198-5 2019 Indoleamine 2,3-dioxygenase 1 (IDO1), a principle enzyme in Trp catabolism, is the target of small-molecule inhibitors in clinical development in combination with PD-1 checkpoint inhibitors. Tryptophan 60-63 indoleamine 2,3-dioxygenase 1 Homo sapiens 31-35 30713125-1 2019 BACKGROUND: INCB024360 is an oral inhibitor of the enzyme indoleamine 2,3-dioxygenase (IDO), which catalyzes the degradation of tryptophan to kynurenine. Tryptophan 128-138 indoleamine 2,3-dioxygenase 1 Homo sapiens 58-85 30713125-1 2019 BACKGROUND: INCB024360 is an oral inhibitor of the enzyme indoleamine 2,3-dioxygenase (IDO), which catalyzes the degradation of tryptophan to kynurenine. Tryptophan 128-138 indoleamine 2,3-dioxygenase 1 Homo sapiens 87-90 30594037-1 2019 Indoleamine 2,3-dioxygenase 1 (IDO1) is a key enzyme in tryptophan metabolism and plays an important role in tumor cell immunosuppression and angiogenesis. Tryptophan 56-66 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-29 30696923-6 2019 Indoleamine 2,3 dioxygenase (IDO) and arginase 1 (ARG1), which catabolize Trp and Arg, respectively, respond to inflammatory cues including interferons and transforming growth factor-beta (TGFbeta) cytokines. Tryptophan 74-77 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 30696923-6 2019 Indoleamine 2,3 dioxygenase (IDO) and arginase 1 (ARG1), which catabolize Trp and Arg, respectively, respond to inflammatory cues including interferons and transforming growth factor-beta (TGFbeta) cytokines. Tryptophan 74-77 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 30594037-1 2019 Indoleamine 2,3-dioxygenase 1 (IDO1) is a key enzyme in tryptophan metabolism and plays an important role in tumor cell immunosuppression and angiogenesis. Tryptophan 56-66 indoleamine 2,3-dioxygenase 1 Homo sapiens 31-35 30585477-1 2019 The heme enzyme indoleamine 2,3-dioxygenase-1 (IDO1) catalyzes the first reaction of l-tryptophan oxidation along the kynurenine pathway. Tryptophan 85-97 indoleamine 2,3-dioxygenase 1 Homo sapiens 47-51 30585477-4 2019 Ultraviolet-visible absorption and resonance Raman spectroscopy showed that incubation of dithionite-reduced, ferrous-IDO1 protein (FeII-IDO1) with nitrite under anaerobic conditions resulted in the time-dependent formation of an FeII-nitrosyl IDO1 species, which was inhibited by substrate l-tryptophan, dependent on the concentration of nitrite or IDO1, and independent of the concentration of the reductant, dithionite. Tryptophan 291-303 indoleamine 2,3-dioxygenase 1 Homo sapiens 118-122 30585477-4 2019 Ultraviolet-visible absorption and resonance Raman spectroscopy showed that incubation of dithionite-reduced, ferrous-IDO1 protein (FeII-IDO1) with nitrite under anaerobic conditions resulted in the time-dependent formation of an FeII-nitrosyl IDO1 species, which was inhibited by substrate l-tryptophan, dependent on the concentration of nitrite or IDO1, and independent of the concentration of the reductant, dithionite. Tryptophan 291-303 indoleamine 2,3-dioxygenase 1 Homo sapiens 137-141 30585477-4 2019 Ultraviolet-visible absorption and resonance Raman spectroscopy showed that incubation of dithionite-reduced, ferrous-IDO1 protein (FeII-IDO1) with nitrite under anaerobic conditions resulted in the time-dependent formation of an FeII-nitrosyl IDO1 species, which was inhibited by substrate l-tryptophan, dependent on the concentration of nitrite or IDO1, and independent of the concentration of the reductant, dithionite. Tryptophan 291-303 indoleamine 2,3-dioxygenase 1 Homo sapiens 137-141 30585477-4 2019 Ultraviolet-visible absorption and resonance Raman spectroscopy showed that incubation of dithionite-reduced, ferrous-IDO1 protein (FeII-IDO1) with nitrite under anaerobic conditions resulted in the time-dependent formation of an FeII-nitrosyl IDO1 species, which was inhibited by substrate l-tryptophan, dependent on the concentration of nitrite or IDO1, and independent of the concentration of the reductant, dithionite. Tryptophan 291-303 indoleamine 2,3-dioxygenase 1 Homo sapiens 137-141 30585477-7 2019 Electron paramagnetic resonance studies measuring NO production showed that the conventional IDO1 dioxygenase reducing cofactors, ascorbate and methylene blue, enhanced IDO1"s nitrite reductase activity and the time- and IDO1 concentration-dependent release of NO in a manner inhibited by l-tryptophan or the IDO inhibitor 1-methyl-l-tryptophan. Tryptophan 289-301 indoleamine 2,3-dioxygenase 1 Homo sapiens 93-97 30585477-7 2019 Electron paramagnetic resonance studies measuring NO production showed that the conventional IDO1 dioxygenase reducing cofactors, ascorbate and methylene blue, enhanced IDO1"s nitrite reductase activity and the time- and IDO1 concentration-dependent release of NO in a manner inhibited by l-tryptophan or the IDO inhibitor 1-methyl-l-tryptophan. Tryptophan 289-301 indoleamine 2,3-dioxygenase 1 Homo sapiens 169-173 30585477-7 2019 Electron paramagnetic resonance studies measuring NO production showed that the conventional IDO1 dioxygenase reducing cofactors, ascorbate and methylene blue, enhanced IDO1"s nitrite reductase activity and the time- and IDO1 concentration-dependent release of NO in a manner inhibited by l-tryptophan or the IDO inhibitor 1-methyl-l-tryptophan. Tryptophan 289-301 indoleamine 2,3-dioxygenase 1 Homo sapiens 169-173 30987575-1 2019 BACKGROUND: L-kynurenine, derivate of L-tryptophan, is synthetized by indoleamine 2,3-dioxygenase (IDO). Tryptophan 38-50 indoleamine 2,3-dioxygenase 1 Homo sapiens 70-97 30240768-2 2019 Indoleamine 2,3-dioxygenase 1 (IDO1) and tryptophan 2,3-dioxygenase 2 (TDO2) are the key rate-limiting enzymes of the tryptophan-to-kynurenine metabolic pathway. Tryptophan 41-51 indoleamine 2,3-dioxygenase 1 Homo sapiens 31-35 29611873-1 2019 Indoleamine-2,3-dioxygenase (IDO) is an enzyme that catalyzes tryptophan to kynurenine and studies have revealed that IDO play a vital role in regulation of liver immunity and inflammation activities. Tryptophan 62-72 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 29611873-1 2019 Indoleamine-2,3-dioxygenase (IDO) is an enzyme that catalyzes tryptophan to kynurenine and studies have revealed that IDO play a vital role in regulation of liver immunity and inflammation activities. Tryptophan 62-72 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 29611873-1 2019 Indoleamine-2,3-dioxygenase (IDO) is an enzyme that catalyzes tryptophan to kynurenine and studies have revealed that IDO play a vital role in regulation of liver immunity and inflammation activities. Tryptophan 62-72 indoleamine 2,3-dioxygenase 1 Homo sapiens 118-121 30669473-7 2019 The activation of indolamine 2,3-dioxygenase (IDO), the rate-limiting step of the kynurenine pathway of tryptophan (Trp) metabolism, plays crucial immunomodulatory roles. Tryptophan 104-114 indoleamine 2,3-dioxygenase 1 Homo sapiens 18-44 30669473-7 2019 The activation of indolamine 2,3-dioxygenase (IDO), the rate-limiting step of the kynurenine pathway of tryptophan (Trp) metabolism, plays crucial immunomodulatory roles. Tryptophan 104-114 indoleamine 2,3-dioxygenase 1 Homo sapiens 46-49 30669473-7 2019 The activation of indolamine 2,3-dioxygenase (IDO), the rate-limiting step of the kynurenine pathway of tryptophan (Trp) metabolism, plays crucial immunomodulatory roles. Tryptophan 116-119 indoleamine 2,3-dioxygenase 1 Homo sapiens 18-44 30669473-7 2019 The activation of indolamine 2,3-dioxygenase (IDO), the rate-limiting step of the kynurenine pathway of tryptophan (Trp) metabolism, plays crucial immunomodulatory roles. Tryptophan 116-119 indoleamine 2,3-dioxygenase 1 Homo sapiens 46-49 30659394-2 2019 RECENT FINDINGS: IDO-1 alters tryptophan metabolism in a manner enhancing T-regulatory cell activity, but pre-clinical data show that its role in tumorigenesis is context-dependent on host and tumor interaction, highlighting some challenges in understanding the molecular oncology of this enzymatic drug target. Tryptophan 30-40 indoleamine 2,3-dioxygenase 1 Homo sapiens 17-22 30832549-1 2019 Indoleamine 2, 3-dioxygenase (IDO), an immunosuppressive enzyme that mediates the conversion of tryptophan to kynurenine, was shown to play a key role in placental development during normal pregnancy. Tryptophan 96-106 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-28 30832549-1 2019 Indoleamine 2, 3-dioxygenase (IDO), an immunosuppressive enzyme that mediates the conversion of tryptophan to kynurenine, was shown to play a key role in placental development during normal pregnancy. Tryptophan 96-106 indoleamine 2,3-dioxygenase 1 Homo sapiens 30-33 30666511-1 2019 The impairment of regulatory T cells (Tregs) is a characteristic feature of autoimmune hepatitis (AIH), and the degradation of tryptophan (Trp) to kynurenine (Kyn), by gamma interferon-induced indoleamine-2,3-dioxygenase-1 (IDO-1), is a central metabolomics check point in the differentiation of Tregs. Tryptophan 139-142 indoleamine 2,3-dioxygenase 1 Homo sapiens 193-222 30666511-1 2019 The impairment of regulatory T cells (Tregs) is a characteristic feature of autoimmune hepatitis (AIH), and the degradation of tryptophan (Trp) to kynurenine (Kyn), by gamma interferon-induced indoleamine-2,3-dioxygenase-1 (IDO-1), is a central metabolomics check point in the differentiation of Tregs. Tryptophan 139-142 indoleamine 2,3-dioxygenase 1 Homo sapiens 224-229 30987575-1 2019 BACKGROUND: L-kynurenine, derivate of L-tryptophan, is synthetized by indoleamine 2,3-dioxygenase (IDO). Tryptophan 38-50 indoleamine 2,3-dioxygenase 1 Homo sapiens 99-102 30788254-2 2019 In the TME, cancer cells exploit indoleamine 2, 3-dioxygenase (IDO), as a cytosolic enzyme that catalyzes the L-tryptophan (Trp) through the kynurenine (Kyn) pathway, which could negatively regulate the activity of T cells. Tryptophan 110-122 indoleamine 2,3-dioxygenase 1 Homo sapiens 33-61 30788254-2 2019 In the TME, cancer cells exploit indoleamine 2, 3-dioxygenase (IDO), as a cytosolic enzyme that catalyzes the L-tryptophan (Trp) through the kynurenine (Kyn) pathway, which could negatively regulate the activity of T cells. Tryptophan 110-122 indoleamine 2,3-dioxygenase 1 Homo sapiens 63-66 30788254-2 2019 In the TME, cancer cells exploit indoleamine 2, 3-dioxygenase (IDO), as a cytosolic enzyme that catalyzes the L-tryptophan (Trp) through the kynurenine (Kyn) pathway, which could negatively regulate the activity of T cells. Tryptophan 124-127 indoleamine 2,3-dioxygenase 1 Homo sapiens 33-61 30788254-2 2019 In the TME, cancer cells exploit indoleamine 2, 3-dioxygenase (IDO), as a cytosolic enzyme that catalyzes the L-tryptophan (Trp) through the kynurenine (Kyn) pathway, which could negatively regulate the activity of T cells. Tryptophan 124-127 indoleamine 2,3-dioxygenase 1 Homo sapiens 63-66 30788254-3 2019 Thus, Trp/Kyn pathway, can be targeted with novel treatment modalities such as IDO1 inhibitor to benefit patients with aggressive solid tumors. Tryptophan 6-9 indoleamine 2,3-dioxygenase 1 Homo sapiens 79-83 30662547-1 2019 Background: Indoleamine 2,3-dioxygenase (IDO), an enzyme involved in tryptophan (Trp) metabolism, is generally considered to be an immunosuppressive molecule. Tryptophan 69-79 indoleamine 2,3-dioxygenase 1 Homo sapiens 12-39 30662547-1 2019 Background: Indoleamine 2,3-dioxygenase (IDO), an enzyme involved in tryptophan (Trp) metabolism, is generally considered to be an immunosuppressive molecule. Tryptophan 69-79 indoleamine 2,3-dioxygenase 1 Homo sapiens 41-44 30662547-1 2019 Background: Indoleamine 2,3-dioxygenase (IDO), an enzyme involved in tryptophan (Trp) metabolism, is generally considered to be an immunosuppressive molecule. Tryptophan 81-84 indoleamine 2,3-dioxygenase 1 Homo sapiens 12-39 30662547-1 2019 Background: Indoleamine 2,3-dioxygenase (IDO), an enzyme involved in tryptophan (Trp) metabolism, is generally considered to be an immunosuppressive molecule. Tryptophan 81-84 indoleamine 2,3-dioxygenase 1 Homo sapiens 41-44 30415456-3 2019 We have identified a pathogenic mechanism that contributes to the tumor-induced immunosuppression in the form of increased indoleamine 2,3 dioxygenase 1 (IDO1) expression; an enzyme that metabolizes the essential amino acid, tryptophan (Trp), into kynurenine (Kyn). Tryptophan 225-235 indoleamine 2,3-dioxygenase 1 Homo sapiens 123-152 30415456-3 2019 We have identified a pathogenic mechanism that contributes to the tumor-induced immunosuppression in the form of increased indoleamine 2,3 dioxygenase 1 (IDO1) expression; an enzyme that metabolizes the essential amino acid, tryptophan (Trp), into kynurenine (Kyn). Tryptophan 225-235 indoleamine 2,3-dioxygenase 1 Homo sapiens 154-158 30415456-3 2019 We have identified a pathogenic mechanism that contributes to the tumor-induced immunosuppression in the form of increased indoleamine 2,3 dioxygenase 1 (IDO1) expression; an enzyme that metabolizes the essential amino acid, tryptophan (Trp), into kynurenine (Kyn). Tryptophan 237-240 indoleamine 2,3-dioxygenase 1 Homo sapiens 123-152 30415456-3 2019 We have identified a pathogenic mechanism that contributes to the tumor-induced immunosuppression in the form of increased indoleamine 2,3 dioxygenase 1 (IDO1) expression; an enzyme that metabolizes the essential amino acid, tryptophan (Trp), into kynurenine (Kyn). Tryptophan 237-240 indoleamine 2,3-dioxygenase 1 Homo sapiens 154-158 30415456-8 2019 CONCLUSIONS: Here, we have validated the ability to use PET of the Trp probe, AMT, for use in visualizing and quantifying intratumoral Trp uptake in GBM patients treated with an IDO1 pathway inhibitor. Tryptophan 67-70 indoleamine 2,3-dioxygenase 1 Homo sapiens 178-182 30415456-8 2019 CONCLUSIONS: Here, we have validated the ability to use PET of the Trp probe, AMT, for use in visualizing and quantifying intratumoral Trp uptake in GBM patients treated with an IDO1 pathway inhibitor. Tryptophan 135-138 indoleamine 2,3-dioxygenase 1 Homo sapiens 178-182 31727243-1 2019 Indoleamine 2,3-dioxygenase 1 (IDO1) catalyzes the first and rate-limiting reaction of l-tryptophan (Trp) conversion into l-kynurenine (Kyn). Tryptophan 87-99 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-29 31727243-1 2019 Indoleamine 2,3-dioxygenase 1 (IDO1) catalyzes the first and rate-limiting reaction of l-tryptophan (Trp) conversion into l-kynurenine (Kyn). Tryptophan 87-99 indoleamine 2,3-dioxygenase 1 Homo sapiens 31-35 31727243-1 2019 Indoleamine 2,3-dioxygenase 1 (IDO1) catalyzes the first and rate-limiting reaction of l-tryptophan (Trp) conversion into l-kynurenine (Kyn). Tryptophan 101-104 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-29 31727243-1 2019 Indoleamine 2,3-dioxygenase 1 (IDO1) catalyzes the first and rate-limiting reaction of l-tryptophan (Trp) conversion into l-kynurenine (Kyn). Tryptophan 101-104 indoleamine 2,3-dioxygenase 1 Homo sapiens 31-35 30137504-6 2018 Microarray analysis revealed that the gene encoding indoleamine 2,3-dioxygenase 1 (IDO1), a major enzyme involved in the tryptophan metabolic process, was highly induced by LMP1. Tryptophan 121-131 indoleamine 2,3-dioxygenase 1 Homo sapiens 52-81 30264546-1 2018 Indoleamine 2,3-dioxygenase 1 (IDO1) is a tryptophan-metabolizing enzyme that is widely distributed in normal or malignant tissues and contributes to immunologic tolerance and immune escape. Tryptophan 42-52 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-29 30264546-1 2018 Indoleamine 2,3-dioxygenase 1 (IDO1) is a tryptophan-metabolizing enzyme that is widely distributed in normal or malignant tissues and contributes to immunologic tolerance and immune escape. Tryptophan 42-52 indoleamine 2,3-dioxygenase 1 Homo sapiens 31-35 30175442-4 2018 The KYN:TRP ratio reflected IDO activity. Tryptophan 8-11 indoleamine 2,3-dioxygenase 1 Homo sapiens 28-31 30306723-2 2018 MSCs can act as immuosuppressive cells, partially due to the expression of the enzyme indoleamine dioxygenase (IDO) which converts tryptophan to kynurenine. Tryptophan 131-141 indoleamine 2,3-dioxygenase 1 Homo sapiens 86-109 30306723-2 2018 MSCs can act as immuosuppressive cells, partially due to the expression of the enzyme indoleamine dioxygenase (IDO) which converts tryptophan to kynurenine. Tryptophan 131-141 indoleamine 2,3-dioxygenase 1 Homo sapiens 111-114 30006478-2 2018 Changes in indoleamine 2,3 dioxygenase (IDO) activity, which catabolizes the degradation of tryptophan to kynurenine, may predict rejection. Tryptophan 92-102 indoleamine 2,3-dioxygenase 1 Homo sapiens 11-38 30006478-2 2018 Changes in indoleamine 2,3 dioxygenase (IDO) activity, which catabolizes the degradation of tryptophan to kynurenine, may predict rejection. Tryptophan 92-102 indoleamine 2,3-dioxygenase 1 Homo sapiens 40-43 31736606-4 2019 Here we review the potential role of two rate-limiting enzymes that evolved separately to catabolize tryptophan, indoleamine 2,3-dioxygenase (IDO) and tryptophan 2,3-dioxygenase 2 (TDO2), that may be active in ovarian cancers and result in the production of immune suppressive catabolites. Tryptophan 101-111 indoleamine 2,3-dioxygenase 1 Homo sapiens 113-140 31736606-4 2019 Here we review the potential role of two rate-limiting enzymes that evolved separately to catabolize tryptophan, indoleamine 2,3-dioxygenase (IDO) and tryptophan 2,3-dioxygenase 2 (TDO2), that may be active in ovarian cancers and result in the production of immune suppressive catabolites. Tryptophan 101-111 indoleamine 2,3-dioxygenase 1 Homo sapiens 142-145 30574192-1 2018 Indoleamine 2,3-dioxygenase (IDO) has the most important role in modulation of tryptophan-dependent effects in the gastrointestinal tract, including modulation of intestinal immune response. Tryptophan 79-89 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 30574192-1 2018 Indoleamine 2,3-dioxygenase (IDO) has the most important role in modulation of tryptophan-dependent effects in the gastrointestinal tract, including modulation of intestinal immune response. Tryptophan 79-89 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 30232146-3 2018 IDO1 is induced in response to inflammatory stimuli such as IFNgamma and promotes immune tolerance by depleting tryptophan and producing tryptophan catabolites, including kynurenine, in the tumor microenvironment. Tryptophan 112-122 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-4 30232146-3 2018 IDO1 is induced in response to inflammatory stimuli such as IFNgamma and promotes immune tolerance by depleting tryptophan and producing tryptophan catabolites, including kynurenine, in the tumor microenvironment. Tryptophan 137-147 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-4 30137504-6 2018 Microarray analysis revealed that the gene encoding indoleamine 2,3-dioxygenase 1 (IDO1), a major enzyme involved in the tryptophan metabolic process, was highly induced by LMP1. Tryptophan 121-131 indoleamine 2,3-dioxygenase 1 Homo sapiens 83-87 30137504-8 2018 IDO1-induced tryptophan consumption and production of tryptophan metabolites appeared to be responsible for inhibition of B-cell function. Tryptophan 13-23 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-4 30137504-8 2018 IDO1-induced tryptophan consumption and production of tryptophan metabolites appeared to be responsible for inhibition of B-cell function. Tryptophan 54-64 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-4 30387777-5 2018 One of these crystal forms diffracted to 1.5 A resolution and can be readily used for soaking experiments to determine high-resolution structures of IDO1 in complex with the substrate tryptophan or inhibitors that coordinate the heme. Tryptophan 184-194 indoleamine 2,3-dioxygenase 1 Homo sapiens 149-153 30254983-1 2018 Exploding interest in immunometabolism as a source of new cancer therapeutics has been driven in large part by studies of tryptophan catabolism mediated by IDO/TDO enzymes. Tryptophan 122-132 indoleamine 2,3-dioxygenase 1 Homo sapiens 156-159 30402507-2 2018 Indoleamine 2,3-dioxygenase (IDO) promotes the effector T cell apoptosis by catalyzing the rate-limiting first step in tryptophan catabolism, and its high expression in H. pylori-infected human gastric mucosa attenuates Th1 and Th17 immune response. Tryptophan 119-129 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 30283439-6 2018 Instead, IFN-gamma-induced tryptophan degradation by indole-2,3-dioxygenase (IDO) is important for the anti-T. gondii human response. Tryptophan 27-37 indoleamine 2,3-dioxygenase 1 Homo sapiens 53-75 30283439-6 2018 Instead, IFN-gamma-induced tryptophan degradation by indole-2,3-dioxygenase (IDO) is important for the anti-T. gondii human response. Tryptophan 27-37 indoleamine 2,3-dioxygenase 1 Homo sapiens 77-80 30055888-1 2018 Kynurenine is biosynthesised from tryptophan catalysed by indoleamine 2,3-dioxygenase (IDO). Tryptophan 34-44 indoleamine 2,3-dioxygenase 1 Homo sapiens 58-85 30055888-1 2018 Kynurenine is biosynthesised from tryptophan catalysed by indoleamine 2,3-dioxygenase (IDO). Tryptophan 34-44 indoleamine 2,3-dioxygenase 1 Homo sapiens 87-90 30524887-5 2018 In human cancers expression of the Trp-degrading enzymes indoleamine-2,3-dioxygenase-1 (IDO1) and tryptophan-2,3-dioxygenase (TDO2) was positively associated with the expression of the tryptophanyl-tRNA synthestase WARS. Tryptophan 35-38 indoleamine 2,3-dioxygenase 1 Homo sapiens 57-86 30524887-5 2018 In human cancers expression of the Trp-degrading enzymes indoleamine-2,3-dioxygenase-1 (IDO1) and tryptophan-2,3-dioxygenase (TDO2) was positively associated with the expression of the tryptophanyl-tRNA synthestase WARS. Tryptophan 35-38 indoleamine 2,3-dioxygenase 1 Homo sapiens 88-92 30524887-7 2018 Moreover, we show here that IDO1- and TDO2-mediated Trp deprivation upregulates WARS expression by activating the general control non-derepressible-2 (GCN2) kinase, leading to phosphorylation of the eukaryotic translation initiation factor 2alpha (eIF2alpha) and induction of activating transcription factor 4 (ATF4). Tryptophan 52-55 indoleamine 2,3-dioxygenase 1 Homo sapiens 28-32 29746927-1 2018 Indoleamine 2,3-dioxygenase 1 (IDO1), involved in the catabolism of tryptophan (Trp) to kynurenine (Kyn) is an important regulator of tumor-mediated immunosuppression implicated in resistance to anti-PD1 immunotherapy. Tryptophan 68-78 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-29 29746927-1 2018 Indoleamine 2,3-dioxygenase 1 (IDO1), involved in the catabolism of tryptophan (Trp) to kynurenine (Kyn) is an important regulator of tumor-mediated immunosuppression implicated in resistance to anti-PD1 immunotherapy. Tryptophan 68-78 indoleamine 2,3-dioxygenase 1 Homo sapiens 31-35 29746927-1 2018 Indoleamine 2,3-dioxygenase 1 (IDO1), involved in the catabolism of tryptophan (Trp) to kynurenine (Kyn) is an important regulator of tumor-mediated immunosuppression implicated in resistance to anti-PD1 immunotherapy. Tryptophan 80-83 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-29 29746927-1 2018 Indoleamine 2,3-dioxygenase 1 (IDO1), involved in the catabolism of tryptophan (Trp) to kynurenine (Kyn) is an important regulator of tumor-mediated immunosuppression implicated in resistance to anti-PD1 immunotherapy. Tryptophan 80-83 indoleamine 2,3-dioxygenase 1 Homo sapiens 31-35 30010674-1 2018 Increased tryptophan (Trp) catabolism in the tumor microenvironment (TME) can mediate immune suppression by upregulation of interferon (IFN)-gamma-inducible indoleamine 2,3-dioxygenase (IDO1) and/or ectopic expression of the predominantly liver-restricted enzyme tryptophan 2,3-dioxygenase (TDO). Tryptophan 10-20 indoleamine 2,3-dioxygenase 1 Homo sapiens 186-190 30010674-1 2018 Increased tryptophan (Trp) catabolism in the tumor microenvironment (TME) can mediate immune suppression by upregulation of interferon (IFN)-gamma-inducible indoleamine 2,3-dioxygenase (IDO1) and/or ectopic expression of the predominantly liver-restricted enzyme tryptophan 2,3-dioxygenase (TDO). Tryptophan 22-25 indoleamine 2,3-dioxygenase 1 Homo sapiens 186-190 29787958-2 2018 The kynurenine pathway (KP) and its rate-limiting tryptophan degrading enzyme, indolamine 2,3 dioxygenase (IDO), have been implicated in the pathogenesis of depression. Tryptophan 50-60 indoleamine 2,3-dioxygenase 1 Homo sapiens 79-105 29787958-2 2018 The kynurenine pathway (KP) and its rate-limiting tryptophan degrading enzyme, indolamine 2,3 dioxygenase (IDO), have been implicated in the pathogenesis of depression. Tryptophan 50-60 indoleamine 2,3-dioxygenase 1 Homo sapiens 107-110 29967604-10 2018 Finally, hsa-miR-99b/let-7e/miR-125a cluster regulates generation of the suppressive tryptophan (Trp) metabolite kynurenine by targeting the tryptophanyl-tRNA synthetase WARS, the direct competitor of IDO in terms of availability of Trp. Tryptophan 85-95 indoleamine 2,3-dioxygenase 1 Homo sapiens 201-204 30081936-5 2018 The IDO activity was expressed with kyn/trp ratio. Tryptophan 40-43 indoleamine 2,3-dioxygenase 1 Homo sapiens 4-7 30081936-11 2018 CONCLUSION: IDO activity, expressed as kyn/trp ratio, is associated with response to immunotherapy; in particular, higher kyn/trp ratio could predict resistance to anti-PD-1 treatment. Tryptophan 43-46 indoleamine 2,3-dioxygenase 1 Homo sapiens 12-15 30081936-11 2018 CONCLUSION: IDO activity, expressed as kyn/trp ratio, is associated with response to immunotherapy; in particular, higher kyn/trp ratio could predict resistance to anti-PD-1 treatment. Tryptophan 126-129 indoleamine 2,3-dioxygenase 1 Homo sapiens 12-15 30081936-12 2018 These preliminary results suggest the possibility of using anti-PD-1 plus IDO inhibitor in those patients with high level of kyn/trp ratio. Tryptophan 129-132 indoleamine 2,3-dioxygenase 1 Homo sapiens 74-77 30275755-4 2018 The indoleamine 2,3-dioxygenase 1 (IDO) catalyzes conversion of tryptophan to kynurenine to induce immune evasion in tumor microenvironment. Tryptophan 64-74 indoleamine 2,3-dioxygenase 1 Homo sapiens 4-33 30275755-4 2018 The indoleamine 2,3-dioxygenase 1 (IDO) catalyzes conversion of tryptophan to kynurenine to induce immune evasion in tumor microenvironment. Tryptophan 64-74 indoleamine 2,3-dioxygenase 1 Homo sapiens 35-38 30068361-1 2018 Indoleamine 2, 3-dioxygenases (IDO1 and IDO2) and tryptophan 2, 3-dioxygenase (TDO) are tryptophan catabolic enzymes that catalyze the conversion of tryptophan into kynurenine. Tryptophan 50-60 indoleamine 2,3-dioxygenase 1 Homo sapiens 31-35 30068361-1 2018 Indoleamine 2, 3-dioxygenases (IDO1 and IDO2) and tryptophan 2, 3-dioxygenase (TDO) are tryptophan catabolic enzymes that catalyze the conversion of tryptophan into kynurenine. Tryptophan 88-98 indoleamine 2,3-dioxygenase 1 Homo sapiens 31-35 29980987-1 2018 Indoleamine 2,3-dioxygenase (IDO) is an enzyme of interest in immuno-oncology because of the immunosuppressive effects that result from its role in tryptophan catabolism. Tryptophan 148-158 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 29980987-1 2018 Indoleamine 2,3-dioxygenase (IDO) is an enzyme of interest in immuno-oncology because of the immunosuppressive effects that result from its role in tryptophan catabolism. Tryptophan 148-158 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 30141341-2 2018 Accurate measurement of tryptophan and kynurenine is critical for monitoring the activity of IDO/TDO. Tryptophan 24-34 indoleamine 2,3-dioxygenase 1 Homo sapiens 93-96 29897749-1 2018 Human indoleamine 2,3-dioxygenase 1 (hIDO1) and tryptophan dioxygenase (hTDO) catalyze the same dioxygenation reaction of Trp to generate N-formyl kynurenine (NFK). Tryptophan 122-125 indoleamine 2,3-dioxygenase 1 Homo sapiens 37-42 29897749-4 2018 In addition, in hIDO1, the indoleamine group of the substrate Trp is H-bonded to S167 through a bridging water, while that in hTDO is directly H-bonded to H76. Tryptophan 62-65 indoleamine 2,3-dioxygenase 1 Homo sapiens 16-21 29693118-1 2018 It is generally hypothesized in the literature that indoleamine 2,3-dioxygenase (IDO), by degrading L-tryptophan along the kynurenine pathway, suppresses CD4+ T-cell function by inducing apoptosis, inhibiting proliferation and promoting differentiation towards a regulatory phenotype. Tryptophan 100-112 indoleamine 2,3-dioxygenase 1 Homo sapiens 52-79 29693118-1 2018 It is generally hypothesized in the literature that indoleamine 2,3-dioxygenase (IDO), by degrading L-tryptophan along the kynurenine pathway, suppresses CD4+ T-cell function by inducing apoptosis, inhibiting proliferation and promoting differentiation towards a regulatory phenotype. Tryptophan 100-112 indoleamine 2,3-dioxygenase 1 Homo sapiens 81-84 29921320-1 2018 BACKGROUND: Indoleamine-2,3-dioxygenase 1 (IDO1) catalyzes the oxidation of tryptophan into kynurenine and is partially responsible for acquired immune tolerance associated with cancer. Tryptophan 76-86 indoleamine 2,3-dioxygenase 1 Homo sapiens 12-41 29921320-1 2018 BACKGROUND: Indoleamine-2,3-dioxygenase 1 (IDO1) catalyzes the oxidation of tryptophan into kynurenine and is partially responsible for acquired immune tolerance associated with cancer. Tryptophan 76-86 indoleamine 2,3-dioxygenase 1 Homo sapiens 43-47 30349892-10 2018 The IDO1 inhibitor epacadostat significantly reduced the Kyn/Trp ratio, TF expression and activity, as well as NF-kappaB (p65) binding activity in activated macrophages. Tryptophan 61-64 indoleamine 2,3-dioxygenase 1 Homo sapiens 4-8 30050535-1 2018 The indoleamine 2,3-dioxygenase (IDO) enzyme can act as an immunoregulator by inhibiting T cell function via the degradation of the essential amino acid tryptophan (trp) into kynurenine (kyn) and its derivates. Tryptophan 165-168 indoleamine 2,3-dioxygenase 1 Homo sapiens 33-36 30050535-5 2018 Here, we demonstrate that patchy tumor IDO expression is associated with an increased systemic kyn/trp ratio in cervical cancer (P = 0.009), whereas marginal tumor expression at the interface with the stroma is linked to improved disease-free (DFS) (P = 0.017) and disease-specific survival (P = 0.043). Tryptophan 99-102 indoleamine 2,3-dioxygenase 1 Homo sapiens 39-42 29896251-1 2018 Indoleamine 2, 3-dioxygenase (IDO) catalyzes the degradation of trytophan, which serves a key role in immune suppression via regulating the production of several metabolites. Tryptophan 64-73 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-28 29896251-1 2018 Indoleamine 2, 3-dioxygenase (IDO) catalyzes the degradation of trytophan, which serves a key role in immune suppression via regulating the production of several metabolites. Tryptophan 64-73 indoleamine 2,3-dioxygenase 1 Homo sapiens 30-33 29520060-2 2018 One plausible mechanism involves dysregulation of various pro-inflammatory cytokines associated with the disease, which affect indoleamine-2,3-dioxygenase (IDO), a key enzyme for tryptophan to kynurenine conversion. Tryptophan 179-189 indoleamine 2,3-dioxygenase 1 Homo sapiens 127-154 29520060-2 2018 One plausible mechanism involves dysregulation of various pro-inflammatory cytokines associated with the disease, which affect indoleamine-2,3-dioxygenase (IDO), a key enzyme for tryptophan to kynurenine conversion. Tryptophan 179-189 indoleamine 2,3-dioxygenase 1 Homo sapiens 156-159 29967604-10 2018 Finally, hsa-miR-99b/let-7e/miR-125a cluster regulates generation of the suppressive tryptophan (Trp) metabolite kynurenine by targeting the tryptophanyl-tRNA synthetase WARS, the direct competitor of IDO in terms of availability of Trp. Tryptophan 97-100 indoleamine 2,3-dioxygenase 1 Homo sapiens 201-204 29967604-10 2018 Finally, hsa-miR-99b/let-7e/miR-125a cluster regulates generation of the suppressive tryptophan (Trp) metabolite kynurenine by targeting the tryptophanyl-tRNA synthetase WARS, the direct competitor of IDO in terms of availability of Trp. Tryptophan 233-236 indoleamine 2,3-dioxygenase 1 Homo sapiens 201-204 29679555-1 2018 BACKGROUND: Indoleamine-2,3-dioxygenase (IDO) catalyzes the first step of tryptophan (Trp) catabolism, yielding kynurenine (Kyn) metabolites. Tryptophan 74-84 indoleamine 2,3-dioxygenase 1 Homo sapiens 41-44 29679555-1 2018 BACKGROUND: Indoleamine-2,3-dioxygenase (IDO) catalyzes the first step of tryptophan (Trp) catabolism, yielding kynurenine (Kyn) metabolites. Tryptophan 86-89 indoleamine 2,3-dioxygenase 1 Homo sapiens 12-39 29679555-1 2018 BACKGROUND: Indoleamine-2,3-dioxygenase (IDO) catalyzes the first step of tryptophan (Trp) catabolism, yielding kynurenine (Kyn) metabolites. Tryptophan 86-89 indoleamine 2,3-dioxygenase 1 Homo sapiens 41-44 29679555-2 2018 The kynurenine-to-tryptophan (K/T) ratio is used as a surrogate for biological IDO enzyme activity. Tryptophan 18-28 indoleamine 2,3-dioxygenase 1 Homo sapiens 79-82 29141444-6 2018 Neopterin was correlated with KYN/TRP, suggesting that the indoleamine 2,3-dioxygenase-1 (IDO-1) enzyme was activated. Tryptophan 34-37 indoleamine 2,3-dioxygenase 1 Homo sapiens 59-88 29868176-9 2018 Results: The kynurenine/tryptophan ratio, as a measure of indoleamine 2,3-dioxygenase (IDO) activity, was increased in patients with SLE. Tryptophan 24-34 indoleamine 2,3-dioxygenase 1 Homo sapiens 58-85 29868176-9 2018 Results: The kynurenine/tryptophan ratio, as a measure of indoleamine 2,3-dioxygenase (IDO) activity, was increased in patients with SLE. Tryptophan 24-34 indoleamine 2,3-dioxygenase 1 Homo sapiens 87-90 29746559-3 2018 Messenger RNA expression analysis suggested most genes were present at similar levels across all undifferentiated cells, though notably, IDO1, which encodes for indoleamine 2,3-dioxygenase and catabolises tryptophan to kynureninase (shown to be elevated in serum from diabetic patients), was not expressed in any PMA-treated MCLC, but present in GM-CSF-treated PBMCs. Tryptophan 205-215 indoleamine 2,3-dioxygenase 1 Homo sapiens 137-141 29141444-6 2018 Neopterin was correlated with KYN/TRP, suggesting that the indoleamine 2,3-dioxygenase-1 (IDO-1) enzyme was activated. Tryptophan 34-37 indoleamine 2,3-dioxygenase 1 Homo sapiens 90-95 29141444-11 2018 CONCLUSION: The pro-inflammatory state of obesity in pregnancy may drive activation of IDO-1, resulting in diversion of TRP away from serotonin and melatonin production and toward KYN metabolites. Tryptophan 120-123 indoleamine 2,3-dioxygenase 1 Homo sapiens 87-92 29375124-1 2018 Indoleamine 2, 3-dioxygenase 1 (IDO1) is a rate-limiting metabolic enzyme that converts the essential amino acid tryptophan (Trp) into downstream catabolites known as kynurenines. Tryptophan 125-128 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-30 29375124-1 2018 Indoleamine 2, 3-dioxygenase 1 (IDO1) is a rate-limiting metabolic enzyme that converts the essential amino acid tryptophan (Trp) into downstream catabolites known as kynurenines. Tryptophan 125-128 indoleamine 2,3-dioxygenase 1 Homo sapiens 32-36 29375124-5 2018 Similar to the dual faces of the astrological Gemini, we highlight the multiple roles of IDO1 and review its canonical association with IDO1-dependent tryptophan metabolism, as well as documented evidence confirming the dispensability of enzyme activity for its immunosuppressive effects. Tryptophan 151-161 indoleamine 2,3-dioxygenase 1 Homo sapiens 136-140 29271486-3 2018 Experimental evidence suggests a potential additional mechanism for CTLA-4 Ig compounds through binding to B7 molecules expressed on antigen-presenting cells (APCs) and up-regulation of indoleamine 2,3-dioxygenase (IDO), an immunomodulating enzyme that catalyzes the degradation of tryptophan to kynurenine and that down-regulates T cell immunity. Tryptophan 282-292 indoleamine 2,3-dioxygenase 1 Homo sapiens 186-213 29271486-3 2018 Experimental evidence suggests a potential additional mechanism for CTLA-4 Ig compounds through binding to B7 molecules expressed on antigen-presenting cells (APCs) and up-regulation of indoleamine 2,3-dioxygenase (IDO), an immunomodulating enzyme that catalyzes the degradation of tryptophan to kynurenine and that down-regulates T cell immunity. Tryptophan 282-292 indoleamine 2,3-dioxygenase 1 Homo sapiens 215-218 29473428-2 2018 Activation of IDO1 depletes tryptophan and produces kynurenine, which induces T cell anergy and suppresses tumor control by the immune system. Tryptophan 28-38 indoleamine 2,3-dioxygenase 1 Homo sapiens 14-18 29679555-1 2018 BACKGROUND: Indoleamine-2,3-dioxygenase (IDO) catalyzes the first step of tryptophan (Trp) catabolism, yielding kynurenine (Kyn) metabolites. Tryptophan 74-84 indoleamine 2,3-dioxygenase 1 Homo sapiens 12-39 29685162-1 2018 BACKGROUND: Indoleamine 2,3-dioxygenase 1 (IDO1) catalyzes the first and rate-limiting step in converting tryptophan to kynurenine. Tryptophan 106-116 indoleamine 2,3-dioxygenase 1 Homo sapiens 12-41 29685162-1 2018 BACKGROUND: Indoleamine 2,3-dioxygenase 1 (IDO1) catalyzes the first and rate-limiting step in converting tryptophan to kynurenine. Tryptophan 106-116 indoleamine 2,3-dioxygenase 1 Homo sapiens 43-47 29719533-11 2018 The ratio of Kyn and trp (kyn/trp) was calculated to estimate IDO-enzyme activity. Tryptophan 21-24 indoleamine 2,3-dioxygenase 1 Homo sapiens 62-65 29719533-11 2018 The ratio of Kyn and trp (kyn/trp) was calculated to estimate IDO-enzyme activity. Tryptophan 30-33 indoleamine 2,3-dioxygenase 1 Homo sapiens 62-65 29615752-1 2018 Indoleamine 2,3-dioxygenase-1 (IDO1) mediates the degradation of L-tryptophan (L-Trp) and is constitutively expressed in the chorionic vascular endothelium of the human placenta with highest levels in the microvasculature. Tryptophan 65-77 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-29 29615752-1 2018 Indoleamine 2,3-dioxygenase-1 (IDO1) mediates the degradation of L-tryptophan (L-Trp) and is constitutively expressed in the chorionic vascular endothelium of the human placenta with highest levels in the microvasculature. Tryptophan 65-77 indoleamine 2,3-dioxygenase 1 Homo sapiens 31-35 29615752-1 2018 Indoleamine 2,3-dioxygenase-1 (IDO1) mediates the degradation of L-tryptophan (L-Trp) and is constitutively expressed in the chorionic vascular endothelium of the human placenta with highest levels in the microvasculature. Tryptophan 79-84 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-29 29615752-1 2018 Indoleamine 2,3-dioxygenase-1 (IDO1) mediates the degradation of L-tryptophan (L-Trp) and is constitutively expressed in the chorionic vascular endothelium of the human placenta with highest levels in the microvasculature. Tryptophan 79-84 indoleamine 2,3-dioxygenase 1 Homo sapiens 31-35 29615752-3 2018 In the large arteries of the chorionic plate L-Trp induced relaxation only after upregulation of IDO1 using interferon gamma and tumor necrosis factor alpha. Tryptophan 45-50 indoleamine 2,3-dioxygenase 1 Homo sapiens 97-101 29154462-3 2018 Indoleamine-2,3-dioxygenase (IDO) is the first and rate-limiting enzyme of tryptophan catabolism. Tryptophan 75-85 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 29154462-3 2018 Indoleamine-2,3-dioxygenase (IDO) is the first and rate-limiting enzyme of tryptophan catabolism. Tryptophan 75-85 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 29543650-0 2018 Tryptophan catabolites along the indoleamine 2,3-dioxygenase pathway as a biological link between depression and cancer. Tryptophan 0-10 indoleamine 2,3-dioxygenase 1 Homo sapiens 33-60 29543650-6 2018 IDO catabolizes tryptophan, the amino acid precursor of serotonin and melatonin, to the metabolites collectively called TRYCATs. Tryptophan 16-26 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 29393500-4 2018 The present review evaluates the recent progress in elucidating how catabolism of tryptophan regulated by IDO modulates the immune response to inflammatory and immunological signals. Tryptophan 82-92 indoleamine 2,3-dioxygenase 1 Homo sapiens 106-109 29436668-4 2018 The goblet cell differentiation in DMEM was inhibited by 1-methyl-tryptophan (1-MT), an inhibitor of indoleamine 2,3 dioxygenase-1 which is the initial enzyme in tryptophan metabolism along the kynurenine (KN) pathway, whereas tryptophan and KN induced goblet cell differentiation in RPMI. Tryptophan 66-76 indoleamine 2,3-dioxygenase 1 Homo sapiens 101-130 29436668-4 2018 The goblet cell differentiation in DMEM was inhibited by 1-methyl-tryptophan (1-MT), an inhibitor of indoleamine 2,3 dioxygenase-1 which is the initial enzyme in tryptophan metabolism along the kynurenine (KN) pathway, whereas tryptophan and KN induced goblet cell differentiation in RPMI. Tryptophan 162-172 indoleamine 2,3-dioxygenase 1 Homo sapiens 101-130 29651242-1 2018 Indoleamine 2,3-dioxygenase 1 (IDO1) is an intracellular monomeric heme-containing enzyme that catalyzes the first and the rate limiting step in catabolism of tryptophan via the kynurenine (KYN) pathway, which plays a significant role in the proliferation and differentiation of T cells. Tryptophan 159-169 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-29 29651242-1 2018 Indoleamine 2,3-dioxygenase 1 (IDO1) is an intracellular monomeric heme-containing enzyme that catalyzes the first and the rate limiting step in catabolism of tryptophan via the kynurenine (KYN) pathway, which plays a significant role in the proliferation and differentiation of T cells. Tryptophan 159-169 indoleamine 2,3-dioxygenase 1 Homo sapiens 31-35 29531094-2 2018 One mechanism by which this is accomplished is through immune suppression effected by up-regulation of indoleamine 2,3-dioxygenase (IDO1), a heme enzyme that catalyzes the oxidation of tryptophan to N-formylkynurenine. Tryptophan 185-195 indoleamine 2,3-dioxygenase 1 Homo sapiens 132-136 29563329-9 2018 Thus, functional SNPs of IDO1 are associated with defective tryptophan catabolism in human T1D, and maneuvers aimed at restoring IDO1 function would be therapeutically effective in at least a subgroup of T1D pediatric patients. Tryptophan 60-70 indoleamine 2,3-dioxygenase 1 Homo sapiens 25-29 29515027-6 2018 RNA sequencing analysis of PCs, gamma-PCs, ECs, and gamma-ECs reveal induction of indoleamine 2,3-dioxygenase 1 (IDO1) in gamma-PCs to significantly higher levels than in gamma-ECs that correlates with tryptophan depletion in vitro. Tryptophan 202-212 indoleamine 2,3-dioxygenase 1 Homo sapiens 82-111 29515027-6 2018 RNA sequencing analysis of PCs, gamma-PCs, ECs, and gamma-ECs reveal induction of indoleamine 2,3-dioxygenase 1 (IDO1) in gamma-PCs to significantly higher levels than in gamma-ECs that correlates with tryptophan depletion in vitro. Tryptophan 202-212 indoleamine 2,3-dioxygenase 1 Homo sapiens 113-117 29515027-9 2018 We conclude that immunosuppressive properties of human PCs are not intrinsic but instead result from IFN-gamma-induced IDO1-mediated tryptophan depletion. Tryptophan 133-143 indoleamine 2,3-dioxygenase 1 Homo sapiens 119-123 29576845-3 2018 When screening for immunomodulatory compounds, the two interferon gamma- (IFN-gamma-) dependent immunometabolic pathways of tryptophan breakdown via indoleamine 2,3-dioxygenase-1 (IDO-1) and neopterin formation by GTP-cyclohydrolase 1 (GTP-CH-I) represent prominent targets, as IFN-gamma-related signaling is strongly sensitive to oxidative triggers. Tryptophan 124-134 indoleamine 2,3-dioxygenase 1 Homo sapiens 149-178 29512370-0 2018 Indoleamine 2, 3-dioxygenase Up-regulates Hypoxia-inducible Factor-1alpha Expression by Degrading L-tryptophan but Not Its Activity in Human Alloreactive T-cells. Tryptophan 98-110 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-28 29254698-2 2018 Traditionally the immunosuppressive effect of IDO1 has been attributed mainly to reduced levels of tryptophan, which activates the kinase general control nonderepressible 2 (GCN2). Tryptophan 99-109 indoleamine 2,3-dioxygenase 1 Homo sapiens 46-50 29576845-3 2018 When screening for immunomodulatory compounds, the two interferon gamma- (IFN-gamma-) dependent immunometabolic pathways of tryptophan breakdown via indoleamine 2,3-dioxygenase-1 (IDO-1) and neopterin formation by GTP-cyclohydrolase 1 (GTP-CH-I) represent prominent targets, as IFN-gamma-related signaling is strongly sensitive to oxidative triggers. Tryptophan 124-134 indoleamine 2,3-dioxygenase 1 Homo sapiens 180-185 28595944-5 2018 CMI cytokines, including IFN-gamma, TNFalpha and IL-1beta, induce the catabolism of tryptophan (TRY) by stimulating indoleamine 2,3-dioxygenase (IDO) resulting in the synthesis of kynurenine (KYN) and other tryptophan catabolites (TRYCATs). Tryptophan 84-94 indoleamine 2,3-dioxygenase 1 Homo sapiens 116-143 28595944-5 2018 CMI cytokines, including IFN-gamma, TNFalpha and IL-1beta, induce the catabolism of tryptophan (TRY) by stimulating indoleamine 2,3-dioxygenase (IDO) resulting in the synthesis of kynurenine (KYN) and other tryptophan catabolites (TRYCATs). Tryptophan 84-94 indoleamine 2,3-dioxygenase 1 Homo sapiens 145-148 28595944-5 2018 CMI cytokines, including IFN-gamma, TNFalpha and IL-1beta, induce the catabolism of tryptophan (TRY) by stimulating indoleamine 2,3-dioxygenase (IDO) resulting in the synthesis of kynurenine (KYN) and other tryptophan catabolites (TRYCATs). Tryptophan 207-217 indoleamine 2,3-dioxygenase 1 Homo sapiens 116-143 28595944-5 2018 CMI cytokines, including IFN-gamma, TNFalpha and IL-1beta, induce the catabolism of tryptophan (TRY) by stimulating indoleamine 2,3-dioxygenase (IDO) resulting in the synthesis of kynurenine (KYN) and other tryptophan catabolites (TRYCATs). Tryptophan 207-217 indoleamine 2,3-dioxygenase 1 Homo sapiens 145-148 30068874-6 2018 Western blot analysis revealed that expression of indoleamine 2,3-dioxygenase (IDO), the enzyme catalyzing Trp to generate Kyn, was dramatically inhibited in colon cancer cells after celastrol treatment, with a dose-dependent manner. Tryptophan 107-110 indoleamine 2,3-dioxygenase 1 Homo sapiens 50-77 29354636-1 2017 The human heme enzymes tryptophan 2,3-dioxygenase (hTDO) and indoleamine 2,3 dioxygenase (hIDO) catalyze the initial step in L-tryptophan (L-Trp) catabolism, the insertion of dioxygen into L-Trp. Tryptophan 125-137 indoleamine 2,3-dioxygenase 1 Homo sapiens 90-94 29354636-1 2017 The human heme enzymes tryptophan 2,3-dioxygenase (hTDO) and indoleamine 2,3 dioxygenase (hIDO) catalyze the initial step in L-tryptophan (L-Trp) catabolism, the insertion of dioxygen into L-Trp. Tryptophan 139-144 indoleamine 2,3-dioxygenase 1 Homo sapiens 90-94 29354636-1 2017 The human heme enzymes tryptophan 2,3-dioxygenase (hTDO) and indoleamine 2,3 dioxygenase (hIDO) catalyze the initial step in L-tryptophan (L-Trp) catabolism, the insertion of dioxygen into L-Trp. Tryptophan 189-194 indoleamine 2,3-dioxygenase 1 Homo sapiens 90-94 30068874-6 2018 Western blot analysis revealed that expression of indoleamine 2,3-dioxygenase (IDO), the enzyme catalyzing Trp to generate Kyn, was dramatically inhibited in colon cancer cells after celastrol treatment, with a dose-dependent manner. Tryptophan 107-110 indoleamine 2,3-dioxygenase 1 Homo sapiens 79-82 29080383-1 2018 Indoleamine 2,3-dioxygenase 1 (IDO) is an enzyme catabolizing tryptophan (Trp) into the kynurenine (Kyn) pathway. Tryptophan 62-72 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-29 29080383-1 2018 Indoleamine 2,3-dioxygenase 1 (IDO) is an enzyme catabolizing tryptophan (Trp) into the kynurenine (Kyn) pathway. Tryptophan 62-72 indoleamine 2,3-dioxygenase 1 Homo sapiens 31-34 29080383-1 2018 Indoleamine 2,3-dioxygenase 1 (IDO) is an enzyme catabolizing tryptophan (Trp) into the kynurenine (Kyn) pathway. Tryptophan 74-77 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-29 29080383-1 2018 Indoleamine 2,3-dioxygenase 1 (IDO) is an enzyme catabolizing tryptophan (Trp) into the kynurenine (Kyn) pathway. Tryptophan 74-77 indoleamine 2,3-dioxygenase 1 Homo sapiens 31-34 30134237-2 2018 Upregulation of IDO1 decreases tryptophan levels and increases the accumulation of kynurenine and its metabolites. Tryptophan 31-41 indoleamine 2,3-dioxygenase 1 Homo sapiens 16-20 29111717-1 2017 Tumors use tryptophan-catabolizing enzymes such as indoleamine 2,3-dioxygenase (IDO-1) to induce an immunosuppressive environment. Tryptophan 11-21 indoleamine 2,3-dioxygenase 1 Homo sapiens 80-85 30134237-1 2018 BACKGROUND/AIMS: Indoleamine 2,3-dioxygenase 1 (IDO1) is a heme-containing enzyme catalyzing the initial and rate-limiting steps in the kynurenine pathway, which converts tryptophan into kynurenine. Tryptophan 171-181 indoleamine 2,3-dioxygenase 1 Homo sapiens 17-46 30134237-1 2018 BACKGROUND/AIMS: Indoleamine 2,3-dioxygenase 1 (IDO1) is a heme-containing enzyme catalyzing the initial and rate-limiting steps in the kynurenine pathway, which converts tryptophan into kynurenine. Tryptophan 171-181 indoleamine 2,3-dioxygenase 1 Homo sapiens 48-52 29413890-1 2018 The tryptophan catabolic enzyme indoleamine 2,3-dioxygenase-1 (IDO1) has attracted enormous attention in driving cancer immunosuppression, neovascularization, and metastasis. Tryptophan 4-14 indoleamine 2,3-dioxygenase 1 Homo sapiens 63-67 29413890-10 2018 Indoximod, a tryptophan mimetic compound with a different mechanism of action in the IDO pathway has also advanced in multiple Phase II trials. Tryptophan 13-23 indoleamine 2,3-dioxygenase 1 Homo sapiens 85-88 29413421-1 2018 We discuss how small-molecule inhibitors of the tryptophan (Trp) catabolic enzyme indoleamine 2,3-dioxygenase (IDO) represent a vanguard of new immunometabolic adjuvants to safely enhance the efficacy of cancer immunotherapy, radiotherapy, or "immunogenic" chemotherapy by leveraging responses to tumor neoantigens. Tryptophan 48-58 indoleamine 2,3-dioxygenase 1 Homo sapiens 82-109 29413421-1 2018 We discuss how small-molecule inhibitors of the tryptophan (Trp) catabolic enzyme indoleamine 2,3-dioxygenase (IDO) represent a vanguard of new immunometabolic adjuvants to safely enhance the efficacy of cancer immunotherapy, radiotherapy, or "immunogenic" chemotherapy by leveraging responses to tumor neoantigens. Tryptophan 48-58 indoleamine 2,3-dioxygenase 1 Homo sapiens 111-114 29413421-1 2018 We discuss how small-molecule inhibitors of the tryptophan (Trp) catabolic enzyme indoleamine 2,3-dioxygenase (IDO) represent a vanguard of new immunometabolic adjuvants to safely enhance the efficacy of cancer immunotherapy, radiotherapy, or "immunogenic" chemotherapy by leveraging responses to tumor neoantigens. Tryptophan 60-63 indoleamine 2,3-dioxygenase 1 Homo sapiens 82-109 29413421-1 2018 We discuss how small-molecule inhibitors of the tryptophan (Trp) catabolic enzyme indoleamine 2,3-dioxygenase (IDO) represent a vanguard of new immunometabolic adjuvants to safely enhance the efficacy of cancer immunotherapy, radiotherapy, or "immunogenic" chemotherapy by leveraging responses to tumor neoantigens. Tryptophan 60-63 indoleamine 2,3-dioxygenase 1 Homo sapiens 111-114 29099929-5 2017 The IFN-inducible genes included 3 transcripts involved in tryptophan catabolism (IDO1, KMO, KYNU) that play a pivotal role in immune evasion by certain other microbial pathogens by driving the differentiation of regulatory T cells. Tryptophan 59-69 indoleamine 2,3-dioxygenase 1 Homo sapiens 82-86 28801236-4 2017 METHODS: Biomarkers involved in indoleamine 2,3-dioxygenase 1 and guanosine triphosphate cyclohydrolase I enzymatic pathways (namely neopterin, tryptophan, kynurenine, phenylalanine, tyrosine, and nitrite) were analyzed in a population of Spanish older adults aged 65 years and above, and their relationships with frailty status were evaluated. Tryptophan 144-154 indoleamine 2,3-dioxygenase 1 Homo sapiens 32-61 28557618-2 2017 By converting tryptophan (Trp) into kynurenine (Kyn), IDO1 is involved in the immune response homeostasis, and its dysregulated expression is described in immune-related pathologies, as tumors that hijack it to evade immune destruction. Tryptophan 14-24 indoleamine 2,3-dioxygenase 1 Homo sapiens 54-58 29278387-2 2017 Dendritic cells (DCs) play a key role in T-cell activation and regulation by promoting a tolerogenic environment through the expression of the immunosuppressive enzyme indoleamine 2,3-dioxygenase (IDO), an intracellular enzyme involved in tryptophan catabolism. Tryptophan 239-249 indoleamine 2,3-dioxygenase 1 Homo sapiens 168-195 29278387-2 2017 Dendritic cells (DCs) play a key role in T-cell activation and regulation by promoting a tolerogenic environment through the expression of the immunosuppressive enzyme indoleamine 2,3-dioxygenase (IDO), an intracellular enzyme involved in tryptophan catabolism. Tryptophan 239-249 indoleamine 2,3-dioxygenase 1 Homo sapiens 197-200 28705908-4 2017 Laser-dissected pulmonary arteries from IPAH and control lungs were tested for the expression of indoleamine-2, 3-dioxygenase (IDO), the rate-limiting enzyme for the conversion from tryptophan to kynurenine. Tryptophan 182-192 indoleamine 2,3-dioxygenase 1 Homo sapiens 97-125 28705908-4 2017 Laser-dissected pulmonary arteries from IPAH and control lungs were tested for the expression of indoleamine-2, 3-dioxygenase (IDO), the rate-limiting enzyme for the conversion from tryptophan to kynurenine. Tryptophan 182-192 indoleamine 2,3-dioxygenase 1 Homo sapiens 127-130 29150070-1 2017 BACKGROUND: The tryptophan metabolic pathway mediated by indolamine 2,3-dioxygenase (IDO), a tryptophan-degrading enzyme, plays an important role in controlling the development of allergic inflammation. Tryptophan 16-26 indoleamine 2,3-dioxygenase 1 Homo sapiens 57-83 29150070-1 2017 BACKGROUND: The tryptophan metabolic pathway mediated by indolamine 2,3-dioxygenase (IDO), a tryptophan-degrading enzyme, plays an important role in controlling the development of allergic inflammation. Tryptophan 16-26 indoleamine 2,3-dioxygenase 1 Homo sapiens 85-88 29150070-1 2017 BACKGROUND: The tryptophan metabolic pathway mediated by indolamine 2,3-dioxygenase (IDO), a tryptophan-degrading enzyme, plays an important role in controlling the development of allergic inflammation. Tryptophan 93-103 indoleamine 2,3-dioxygenase 1 Homo sapiens 57-83 29150070-1 2017 BACKGROUND: The tryptophan metabolic pathway mediated by indolamine 2,3-dioxygenase (IDO), a tryptophan-degrading enzyme, plays an important role in controlling the development of allergic inflammation. Tryptophan 93-103 indoleamine 2,3-dioxygenase 1 Homo sapiens 85-88 29163470-1 2017 Cells expressing IDO suppress innate and adaptive immunity to promote tolerance by catabolizing the amino acid tryptophan (Trp) and other indole compounds. Tryptophan 123-126 indoleamine 2,3-dioxygenase 1 Homo sapiens 17-20 29163470-10 2017 Another effect of sustained IDO activity is enhanced pain sensitivity, as some Trp catabolites produced by cells expressing IDO are neuroactive. Tryptophan 79-82 indoleamine 2,3-dioxygenase 1 Homo sapiens 28-31 29163470-10 2017 Another effect of sustained IDO activity is enhanced pain sensitivity, as some Trp catabolites produced by cells expressing IDO are neuroactive. Tryptophan 79-82 indoleamine 2,3-dioxygenase 1 Homo sapiens 124-127 29037255-2 2017 Indoleamine 2,3-dioxygenase (IDO) is the rate-limiting oxidoreductase that catalyzes the degradation of tryptophan to kynurenine. Tryptophan 104-114 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 29037255-2 2017 Indoleamine 2,3-dioxygenase (IDO) is the rate-limiting oxidoreductase that catalyzes the degradation of tryptophan to kynurenine. Tryptophan 104-114 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 29167421-3 2017 Here, we report the crystal structures of hIDO1 in complex with its substrate, Trp, an inhibitor, epacadostat, and/or an effector, indole ethanol (IDE). Tryptophan 79-82 indoleamine 2,3-dioxygenase 1 Homo sapiens 42-47 28557618-2 2017 By converting tryptophan (Trp) into kynurenine (Kyn), IDO1 is involved in the immune response homeostasis, and its dysregulated expression is described in immune-related pathologies, as tumors that hijack it to evade immune destruction. Tryptophan 26-29 indoleamine 2,3-dioxygenase 1 Homo sapiens 54-58 28557618-4 2017 Existing and standard quantitation methods of IDO1 substrate and metabolite(s) are based on the total level of Trp and its metabolites determined by liquid chromatography tandem mass spectrometry analysis in human plasma, cerebrospinal fluid, and brain. Tryptophan 111-114 indoleamine 2,3-dioxygenase 1 Homo sapiens 46-50 28557618-6 2017 Myeloid, glycolysis metabolic signatures, and correlation between IDO1 expression and Trp to Kyn conversion are also shown. Tryptophan 86-89 indoleamine 2,3-dioxygenase 1 Homo sapiens 66-70 29017244-2 2017 Indoleamine 2, 3-dioxygenase (IDO) is an immunoregulatory enzyme that breaks down tryptophan (Trp) to metabolites known as kynurenines (Kyns). Tryptophan 82-92 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-28 29017244-2 2017 Indoleamine 2, 3-dioxygenase (IDO) is an immunoregulatory enzyme that breaks down tryptophan (Trp) to metabolites known as kynurenines (Kyns). Tryptophan 82-92 indoleamine 2,3-dioxygenase 1 Homo sapiens 30-33 29017244-2 2017 Indoleamine 2, 3-dioxygenase (IDO) is an immunoregulatory enzyme that breaks down tryptophan (Trp) to metabolites known as kynurenines (Kyns). Tryptophan 94-97 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-28 29017244-2 2017 Indoleamine 2, 3-dioxygenase (IDO) is an immunoregulatory enzyme that breaks down tryptophan (Trp) to metabolites known as kynurenines (Kyns). Tryptophan 94-97 indoleamine 2,3-dioxygenase 1 Homo sapiens 30-33 29017244-3 2017 We investigated whether IDO activity, as measured by the ratio of Kyn to Trp, could be used to diagnose or predict active tuberculosis disease in HIV-infected adults. Tryptophan 73-76 indoleamine 2,3-dioxygenase 1 Homo sapiens 24-27 29046648-1 2017 It has been suggested that the metabolic enzyme indoleamine 2,3-dioxygenase (IDO) is a biological mediator of inflammation related to the psychopathology of depression, with a Kynurenine (KYN) increase in the Tryptophan (TRP) metabolic pathway, resulting in reduced Serotonin. Tryptophan 209-219 indoleamine 2,3-dioxygenase 1 Homo sapiens 77-80 29046648-1 2017 It has been suggested that the metabolic enzyme indoleamine 2,3-dioxygenase (IDO) is a biological mediator of inflammation related to the psychopathology of depression, with a Kynurenine (KYN) increase in the Tryptophan (TRP) metabolic pathway, resulting in reduced Serotonin. Tryptophan 221-224 indoleamine 2,3-dioxygenase 1 Homo sapiens 77-80 28541512-4 2017 One of the most notable is increased tryptophan metabolism through activation of indoleamine 2,3-dioxygenase 1 (IDO1) and tryptophan 2,3-dioxygenase (TDO). Tryptophan 37-47 indoleamine 2,3-dioxygenase 1 Homo sapiens 81-110 28541512-4 2017 One of the most notable is increased tryptophan metabolism through activation of indoleamine 2,3-dioxygenase 1 (IDO1) and tryptophan 2,3-dioxygenase (TDO). Tryptophan 37-47 indoleamine 2,3-dioxygenase 1 Homo sapiens 112-116 28625979-3 2017 We found that ISX-mediated IL6-induced expression of the tryptophan catabolic enzymes Indoleamine 2,3-dioxygenase 1 (IDO1) and tryptophan 2,3-dioxygenase in hepatocellular carcinoma cells, resulting in an ISX-dependent increase in the tryptophan catabolite kynurenine and its receptor aryl hydrocarbon receptor (AHR). Tryptophan 57-67 indoleamine 2,3-dioxygenase 1 Homo sapiens 86-115 28667875-0 2017 Discovery of potent IDO1 inhibitors derived from tryptophan using scaffold-hopping and structure-based design approaches. Tryptophan 49-59 indoleamine 2,3-dioxygenase 1 Homo sapiens 20-24 29190885-1 2017 The catabolism of tryptophan (Trp) by indoleamine 2,3-dioxygenase (IDO) is a key step in tolerance effected by a variety of cell types, including mesenchymal stromal cells (MSCs). Tryptophan 18-28 indoleamine 2,3-dioxygenase 1 Homo sapiens 38-65 29190885-1 2017 The catabolism of tryptophan (Trp) by indoleamine 2,3-dioxygenase (IDO) is a key step in tolerance effected by a variety of cell types, including mesenchymal stromal cells (MSCs). Tryptophan 18-28 indoleamine 2,3-dioxygenase 1 Homo sapiens 67-70 29190885-1 2017 The catabolism of tryptophan (Trp) by indoleamine 2,3-dioxygenase (IDO) is a key step in tolerance effected by a variety of cell types, including mesenchymal stromal cells (MSCs). Tryptophan 30-33 indoleamine 2,3-dioxygenase 1 Homo sapiens 38-65 29190885-1 2017 The catabolism of tryptophan (Trp) by indoleamine 2,3-dioxygenase (IDO) is a key step in tolerance effected by a variety of cell types, including mesenchymal stromal cells (MSCs). Tryptophan 30-33 indoleamine 2,3-dioxygenase 1 Homo sapiens 67-70 29190885-3 2017 A synthetic analog of Trp, 1-methyl tryptophan (1MT), is a selective inhibitor of IDO enzymatic activity being utilized in cancer immunotherapy trials. Tryptophan 22-25 indoleamine 2,3-dioxygenase 1 Homo sapiens 82-85 28688912-1 2017 Brain glia possess the rate limiting enzyme indoleamine 2, 3-dioxygenase (IDO) which catalyses the conversion of tryptophan to kynurenine. Tryptophan 113-123 indoleamine 2,3-dioxygenase 1 Homo sapiens 74-77 28132413-1 2017 BACKGROUND: The tryptophan-depleting enzyme indoleamine-2,3-dioxygenase (IDO) is critical for the regulation of immunotolerance and plays an important role in immune-associated skin diseases. Tryptophan 16-26 indoleamine 2,3-dioxygenase 1 Homo sapiens 44-71 28132413-1 2017 BACKGROUND: The tryptophan-depleting enzyme indoleamine-2,3-dioxygenase (IDO) is critical for the regulation of immunotolerance and plays an important role in immune-associated skin diseases. Tryptophan 16-26 indoleamine 2,3-dioxygenase 1 Homo sapiens 73-76 28132413-9 2017 Keratinocytes in the skin of healthy controls and the circumcised skin of patients with CA could minimally transform tryptophan into kynurenine, but IDO-competent epidermal cells from warts could transform tryptophan. Tryptophan 206-216 indoleamine 2,3-dioxygenase 1 Homo sapiens 149-152 28765120-4 2017 IDO1 is an immunosuppressive enzyme that degrades tryptophan. Tryptophan 50-60 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-4 28625979-3 2017 We found that ISX-mediated IL6-induced expression of the tryptophan catabolic enzymes Indoleamine 2,3-dioxygenase 1 (IDO1) and tryptophan 2,3-dioxygenase in hepatocellular carcinoma cells, resulting in an ISX-dependent increase in the tryptophan catabolite kynurenine and its receptor aryl hydrocarbon receptor (AHR). Tryptophan 57-67 indoleamine 2,3-dioxygenase 1 Homo sapiens 117-121 27376248-3 2017 Indoleamine 2,3-dioxygenase (IDO) is the key enzyme for the metabolism of tryptophan. Tryptophan 74-84 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 27376248-3 2017 Indoleamine 2,3-dioxygenase (IDO) is the key enzyme for the metabolism of tryptophan. Tryptophan 74-84 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 27376248-12 2017 As we found that FAEs inhibit both IDO expression and enzymatic activity leading to a modulation of tryptophan degradation, we believe this effect may contribute to the clinical efficacy of this drug in psoriasis by downregulating pro-inflammatory mediators generated by the kynurenine pathway. Tryptophan 100-110 indoleamine 2,3-dioxygenase 1 Homo sapiens 35-38 27815661-0 2017 Improved Radiosynthesis and Biological Evaluations of L- and D-1-[18F]Fluoroethyl-Tryptophan for PET Imaging of IDO-Mediated Kynurenine Pathway of Tryptophan Metabolism. Tryptophan 82-92 indoleamine 2,3-dioxygenase 1 Homo sapiens 112-115 28656203-6 2017 IDO expression was markedly increased by IFN-gamma through signal transducer and activator of transcription 1 (STAT1) activation and resulted in the depletion of tryptophan. Tryptophan 162-172 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-3 27815661-1 2017 PURPOSE: Tryptophan metabolism via indoleamine 2,3-dioxygenase (IDO)-mediated kynurenine pathway plays a role in immunomodulation and has been emerging as a plausible target for cancer immunotherapy. Tryptophan 9-19 indoleamine 2,3-dioxygenase 1 Homo sapiens 35-62 27815661-1 2017 PURPOSE: Tryptophan metabolism via indoleamine 2,3-dioxygenase (IDO)-mediated kynurenine pathway plays a role in immunomodulation and has been emerging as a plausible target for cancer immunotherapy. Tryptophan 9-19 indoleamine 2,3-dioxygenase 1 Homo sapiens 64-67 27815661-2 2017 Imaging IDO-mediated kynurenine pathway of tryptophan metabolism with positron emission tomography (PET) could provide valuable information for noninvasive assessment of cancer immunotherapy response. Tryptophan 43-53 indoleamine 2,3-dioxygenase 1 Homo sapiens 8-11 27815661-3 2017 In this work, radiotracer 1-(2-[18F]fluoroethyl)-L-tryptophan (1-L-[18F]FETrp) and its enantioisomer 1-D-[18F]FETrp were synthesized and evaluated for PET imaging of IDO-mediated kynurenine pathway of tryptophan metabolism. Tryptophan 51-61 indoleamine 2,3-dioxygenase 1 Homo sapiens 166-169 27815661-12 2017 Our biological evaluation results suggest that 1-L-[18F]FETrp is a promising radiotracer for PET imaging of IDO-mediated kynurenine pathway of tryptophan metabolism in cancer. Tryptophan 143-153 indoleamine 2,3-dioxygenase 1 Homo sapiens 108-111 28511073-1 2017 Indoleamine and tryptophan 2,3-dioxygenases (IDO1 and TDO2) are pyrrolases catalyzing the oxidative cleavage of the 2,3-double bond of L-tryptophan in kynurenine pathway. Tryptophan 135-147 indoleamine 2,3-dioxygenase 1 Homo sapiens 45-49 28511073-8 2017 In-vitro cell uptake experiments using CT26 cells with doxycycline-induced overexpression of human-IDO1 and human-TDO2 revealed an elevated cell uptake of L-5-[18F]fluorotryptophan upon induction of IDO1 or TDO2 enzymes compared to baseline; however, the uptake was observed only in the presence of low L-tryptophan levels in media. Tryptophan 303-315 indoleamine 2,3-dioxygenase 1 Homo sapiens 99-103 28511073-8 2017 In-vitro cell uptake experiments using CT26 cells with doxycycline-induced overexpression of human-IDO1 and human-TDO2 revealed an elevated cell uptake of L-5-[18F]fluorotryptophan upon induction of IDO1 or TDO2 enzymes compared to baseline; however, the uptake was observed only in the presence of low L-tryptophan levels in media. Tryptophan 303-315 indoleamine 2,3-dioxygenase 1 Homo sapiens 199-203 28769554-5 2017 Recent studies suggest the involvement of IDO in the modulation of immune response, which became more evident after the in vitro demonstration of IDO production by DC and of the ability of these cells to inhibit lymphocyte function through the control of tryptophan metabolism. Tryptophan 255-265 indoleamine 2,3-dioxygenase 1 Homo sapiens 42-45 28735627-1 2017 Indoleamine 2,3-dioxygenase-1 (IDO-1) catalyses the first and rate-limiting step in the metabolism of L-tryptophan. Tryptophan 102-114 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-29 28724796-4 2017 Host IL-6 was identified as a pivotal cytokine mediator, as was host indoleamine 2,3-dioxygenase (IDO-1), which was upregulated in GVHD in an IL-6-dependent manner in microglial cells and was accompanied by dysregulated tryptophan metabolism in the dorsal raphe nucleus and prefrontal cortex. Tryptophan 220-230 indoleamine 2,3-dioxygenase 1 Homo sapiens 98-103 28790848-1 2017 BACKGROUND: Indoleamine 2,3-dioxygenase (IDO) catalyzes the rate-limiting step of tryptophan (Trp) degradation via the kynurenine (Kyn) pathway, which inhibits the proliferation of T cells and induces the apoptosis of T cells, leading to immune tolerance. Tryptophan 82-92 indoleamine 2,3-dioxygenase 1 Homo sapiens 12-39 28790848-1 2017 BACKGROUND: Indoleamine 2,3-dioxygenase (IDO) catalyzes the rate-limiting step of tryptophan (Trp) degradation via the kynurenine (Kyn) pathway, which inhibits the proliferation of T cells and induces the apoptosis of T cells, leading to immune tolerance. Tryptophan 82-92 indoleamine 2,3-dioxygenase 1 Homo sapiens 41-44 28790848-1 2017 BACKGROUND: Indoleamine 2,3-dioxygenase (IDO) catalyzes the rate-limiting step of tryptophan (Trp) degradation via the kynurenine (Kyn) pathway, which inhibits the proliferation of T cells and induces the apoptosis of T cells, leading to immune tolerance. Tryptophan 94-97 indoleamine 2,3-dioxygenase 1 Homo sapiens 12-39 28790848-1 2017 BACKGROUND: Indoleamine 2,3-dioxygenase (IDO) catalyzes the rate-limiting step of tryptophan (Trp) degradation via the kynurenine (Kyn) pathway, which inhibits the proliferation of T cells and induces the apoptosis of T cells, leading to immune tolerance. Tryptophan 94-97 indoleamine 2,3-dioxygenase 1 Homo sapiens 41-44 28790848-7 2017 The IDO activity was determined by calculating the serum Kyn-to-Trp (Kyn/Trp) ratio. Tryptophan 64-67 indoleamine 2,3-dioxygenase 1 Homo sapiens 4-7 28790848-7 2017 The IDO activity was determined by calculating the serum Kyn-to-Trp (Kyn/Trp) ratio. Tryptophan 73-76 indoleamine 2,3-dioxygenase 1 Homo sapiens 4-7 28159919-1 2017 IDO1 is an enzyme catalyzing the initial and rate-limiting step in the catabolism of tryptophan along the kynurenine pathway. Tryptophan 85-95 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-4 28526475-1 2017 Indoleamine 2,3-dioxygenase 1 (IDO1) plays a vital role in the catabolism of tryptophan along with the kynurenine pathway which is involved in many human diseases including cancer, Alzheimer"s disease, etc. Tryptophan 77-87 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-29 28526475-1 2017 Indoleamine 2,3-dioxygenase 1 (IDO1) plays a vital role in the catabolism of tryptophan along with the kynurenine pathway which is involved in many human diseases including cancer, Alzheimer"s disease, etc. Tryptophan 77-87 indoleamine 2,3-dioxygenase 1 Homo sapiens 31-35 28758106-4 2017 Neopterin synthesis is induced by interferon-gamma that also induces indoleamine 2,3-dioxygenase (IDO), an enzyme catalyzing catabolism of tryptophan to kynurenine. Tryptophan 139-149 indoleamine 2,3-dioxygenase 1 Homo sapiens 69-96 28758106-4 2017 Neopterin synthesis is induced by interferon-gamma that also induces indoleamine 2,3-dioxygenase (IDO), an enzyme catalyzing catabolism of tryptophan to kynurenine. Tryptophan 139-149 indoleamine 2,3-dioxygenase 1 Homo sapiens 98-101 28053021-1 2017 Purpose: Indoleamine 2,3-dioxygenase-1 (IDO1) catalyzes the degradation of tryptophan to N-formyl-kynurenine. Tryptophan 75-85 indoleamine 2,3-dioxygenase 1 Homo sapiens 9-38 28053021-1 2017 Purpose: Indoleamine 2,3-dioxygenase-1 (IDO1) catalyzes the degradation of tryptophan to N-formyl-kynurenine. Tryptophan 75-85 indoleamine 2,3-dioxygenase 1 Homo sapiens 40-44 28285360-4 2017 Our recent investigations have suggested that Kynurenine-rich environment can shift a pro-inflammatory response to an anti-inflammatory response, as is the case in the presence of the enzyme Indoleamine 2,3 dioxygenase (IDO), the rate-limiting enzyme in tryptophan degradation and Kynurenine (Kyn) production. Tryptophan 254-264 indoleamine 2,3-dioxygenase 1 Homo sapiens 191-218 28285360-4 2017 Our recent investigations have suggested that Kynurenine-rich environment can shift a pro-inflammatory response to an anti-inflammatory response, as is the case in the presence of the enzyme Indoleamine 2,3 dioxygenase (IDO), the rate-limiting enzyme in tryptophan degradation and Kynurenine (Kyn) production. Tryptophan 254-264 indoleamine 2,3-dioxygenase 1 Homo sapiens 220-223 28735627-1 2017 Indoleamine 2,3-dioxygenase-1 (IDO-1) catalyses the first and rate-limiting step in the metabolism of L-tryptophan. Tryptophan 102-114 indoleamine 2,3-dioxygenase 1 Homo sapiens 31-36 29156701-4 2017 IDO1 is an intracellular enzyme initiating the first and rate-limited step of tryptophan breakdown. Tryptophan 78-88 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-4 29156701-8 2017 We hypothesized a tryptophan starvation theory that since tryptophan is essential for the synthesis of TSP1, IDO1 induce a decrease in tryptophan availability and a reduction in TSP1 synthesis in ECs, leading to overcoming the dormancy state of IDC cells and exacerbating conditions such as tumour invasion and metastasis. Tryptophan 18-28 indoleamine 2,3-dioxygenase 1 Homo sapiens 109-113 28599322-5 2017 Also, the expression of cytokine-responsive indoleamine 2,3-dioxygenase-1 (IDO-1) was significantly augmented in hypoxia, resulting in increased kynurenine/tryptophan ratio and lowered serotonin level in the hippocampus. Tryptophan 156-166 indoleamine 2,3-dioxygenase 1 Homo sapiens 75-80 28076309-1 2017 BACKGROUND: As part of the immune defense during infection, an increase in enzyme activity of indoleamine 2,3-dioxygenase (IDO) leads to a breakdown of tryptophan to kynurenine. Tryptophan 152-162 indoleamine 2,3-dioxygenase 1 Homo sapiens 94-121 28076309-1 2017 BACKGROUND: As part of the immune defense during infection, an increase in enzyme activity of indoleamine 2,3-dioxygenase (IDO) leads to a breakdown of tryptophan to kynurenine. Tryptophan 152-162 indoleamine 2,3-dioxygenase 1 Homo sapiens 123-126 28076309-3 2017 We investigated the prognostic ability of tryptophan, serotonin, kynurenine and IDO (represented by the ratio of kynurenine/tryptophan) to predict adverse clinical outcomes in patients with community-acquired pneumonia (CAP). Tryptophan 124-134 indoleamine 2,3-dioxygenase 1 Homo sapiens 80-83 30108875-2 2017 Recent developments in understanding the catalytic mechanism of the IDO1 enzyme revealed that conversion of l-tryptophan (l-Trp) to N-formylkynurenine proceeded through an epoxide intermediate state. Tryptophan 108-120 indoleamine 2,3-dioxygenase 1 Homo sapiens 68-72 30108875-2 2017 Recent developments in understanding the catalytic mechanism of the IDO1 enzyme revealed that conversion of l-tryptophan (l-Trp) to N-formylkynurenine proceeded through an epoxide intermediate state. Tryptophan 122-127 indoleamine 2,3-dioxygenase 1 Homo sapiens 68-72 30108875-5 2017 Their optimization led to the identification of potent compounds, 6, 22, 23 and 25 (IC50 = 0.19 to 0.62 muM), which are competitive inhibitors of IDO1 with respect to l-Trp. Tryptophan 167-172 indoleamine 2,3-dioxygenase 1 Homo sapiens 146-150 27990653-5 2017 Determination of EPA"s on-target potency, ie, its half-maximal inhibitory concentration (IC50 ) against IDO1, is important for dose selection but complicated by the bioconversion of tryptophan (TRP) to kynurenine (KYN) catalyzed by both IDO1 and TRP 2,3-dioxygenase (TDO). Tryptophan 194-197 indoleamine 2,3-dioxygenase 1 Homo sapiens 237-241 28545736-3 2017 In mammals, IDO1 has remarkably evolved to expand its functions, so to become a prominent homeostatic regulator, capable of modulating infection and immunity in multiple ways, including local tryptophan deprivation, production of biologically active tryptophan catabolites, and non-enzymatic cell-signaling activity. Tryptophan 192-202 indoleamine 2,3-dioxygenase 1 Homo sapiens 12-16 28545736-3 2017 In mammals, IDO1 has remarkably evolved to expand its functions, so to become a prominent homeostatic regulator, capable of modulating infection and immunity in multiple ways, including local tryptophan deprivation, production of biologically active tryptophan catabolites, and non-enzymatic cell-signaling activity. Tryptophan 250-260 indoleamine 2,3-dioxygenase 1 Homo sapiens 12-16 28365507-2 2017 IDO1 can decrease the tryptophan and produce a series of toxic kynurenine metabolites to promote the immune toleration via GCN2 pathway, mTOR pathway, toxic effect of kynurenine and favoring differentiation of Tregs. Tryptophan 22-32 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-4 27990653-8 2017 The model suggests that ~60% and 40% of TRP KYN bioconversion was mediated by IDO1 and TDO, respectively, in the cancer patients at baseline. Tryptophan 40-43 indoleamine 2,3-dioxygenase 1 Homo sapiens 78-82 28434116-1 2017 BACKGROUND/INTRODUCTION: Indoleamine 2,3-dioxygenase (IDO) metabolizes tryptophan to kynurenine. Tryptophan 71-81 indoleamine 2,3-dioxygenase 1 Homo sapiens 25-52 28336214-1 2017 Indoleamine 2,3-dioxygenase 1 (IDO1) plays a key role in the immune system by regulating tryptophan levels and T cell differentiation. Tryptophan 89-99 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-29 28336214-1 2017 Indoleamine 2,3-dioxygenase 1 (IDO1) plays a key role in the immune system by regulating tryptophan levels and T cell differentiation. Tryptophan 89-99 indoleamine 2,3-dioxygenase 1 Homo sapiens 31-35 28336214-4 2017 Many of the IDO1 inhibitors in clinical trials naturally bear structural similarities to the IDO1 substrate tryptophan, as such, they fulfill many of the structural and functional criteria as potential AHR ligands. Tryptophan 108-118 indoleamine 2,3-dioxygenase 1 Homo sapiens 12-16 28336214-4 2017 Many of the IDO1 inhibitors in clinical trials naturally bear structural similarities to the IDO1 substrate tryptophan, as such, they fulfill many of the structural and functional criteria as potential AHR ligands. Tryptophan 108-118 indoleamine 2,3-dioxygenase 1 Homo sapiens 93-97 28434116-1 2017 BACKGROUND/INTRODUCTION: Indoleamine 2,3-dioxygenase (IDO) metabolizes tryptophan to kynurenine. Tryptophan 71-81 indoleamine 2,3-dioxygenase 1 Homo sapiens 54-57