PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 33433354-1 2021 BACKGROUND AND PURPOSE: Indolamine 2,3-dioxygenase (IDO), an enzyme that catalyses the metabolism of tryptophan, may play a detrimental role in ischemia-reperfusion injury (IRI). Tryptophan 101-111 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 24-50 34021461-1 2021 Indoleamine 2,3-dioxygenase 1 (IDO1) is an enzyme for tryptophan metabolism, involved in immune cell differentiation/maturation and cancer biology. Tryptophan 54-64 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 0-29 34021461-1 2021 Indoleamine 2,3-dioxygenase 1 (IDO1) is an enzyme for tryptophan metabolism, involved in immune cell differentiation/maturation and cancer biology. Tryptophan 54-64 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 31-35 33838298-1 2021 Background Indoleamine 2,3-dioxygenase (IDO) can promote tryptophan metabolism to kynurenine and modulate regulatory T cells (Tregs), thereby maintains lower efficiency to induce tolerance. Tryptophan 57-67 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 11-38 33838298-1 2021 Background Indoleamine 2,3-dioxygenase (IDO) can promote tryptophan metabolism to kynurenine and modulate regulatory T cells (Tregs), thereby maintains lower efficiency to induce tolerance. Tryptophan 57-67 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 40-43 33433354-1 2021 BACKGROUND AND PURPOSE: Indolamine 2,3-dioxygenase (IDO), an enzyme that catalyses the metabolism of tryptophan, may play a detrimental role in ischemia-reperfusion injury (IRI). Tryptophan 101-111 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 52-55 33116524-0 2020 Electroacupuncture Relieves LPS-Induced Depression-Like Behaviour in Rats Through IDO-Mediated Tryptophan-Degrading Pathway. Tryptophan 95-105 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 82-85 33116524-8 2020 Conclusion: Electroacupuncture treatment provided protection against LPS-induced depressive-like behaviour, and the associated mechanisms may be related to inhibiting the inflammatory response, regulating the IDO-mediated tryptophan-degrading pathway, and inhibiting NR2B activation. Tryptophan 222-232 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 209-212 32469935-2 2020 IDO is known to cause immunosuppression through breakdown of tryptophan in the tumor microenvironment. Tryptophan 61-71 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 0-3 31176083-3 2019 99% of brain tryptophan metabolism via its degradation to kynurenine (KYN) catalyzed by indoleamine 2,3-dioxygenase (IDO). Tryptophan 13-23 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 88-115 31685866-5 2019 IDO and tryptophan 2,3-dioxygenase (TDO) catalyze the same rate-limiting step of tryptophan metabolism along a common pathway, which leads to tryptophan starvation and generation of catabolites collectively known as kynurenines. Tryptophan 81-91 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 0-3 31685866-14 2019 This phenomenon was concomitant with a significant reduction of IDO activity in EAO testis measured by tryptophan and kynurenine concentrations (HPLC). Tryptophan 103-113 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 64-67 32198742-7 2020 Activation of Indoleamine-2,3-dioxygenase (IDO), (an enzyme that participates in the tryptophan metabolism), leads to a decrease of serotonin (5-HT) levels. Tryptophan 85-95 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 14-41 32198742-7 2020 Activation of Indoleamine-2,3-dioxygenase (IDO), (an enzyme that participates in the tryptophan metabolism), leads to a decrease of serotonin (5-HT) levels. Tryptophan 85-95 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 43-46 32198742-11 2020 Further, it reduced the elevated hippocampal IL-6 & TNFalpha and reversed the increased activity of IDO as measured by ratio of hippocampal KYN/TRP and 5HT/TRP in stressed rats. Tryptophan 144-147 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 100-103 32198742-11 2020 Further, it reduced the elevated hippocampal IL-6 & TNFalpha and reversed the increased activity of IDO as measured by ratio of hippocampal KYN/TRP and 5HT/TRP in stressed rats. Tryptophan 156-159 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 100-103 31176083-3 2019 99% of brain tryptophan metabolism via its degradation to kynurenine (KYN) catalyzed by indoleamine 2,3-dioxygenase (IDO). Tryptophan 13-23 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 117-120 29725904-2 2019 This stimulation induces indoleamine 2,3-dioxygenase (IDO), an enzyme that reduces the tryptophan bioavailability to synthesize serotonin. Tryptophan 87-97 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 25-52 31010933-2 2019 The substrate for IDO1 is tryptophan and there is a theoretical concern that inhibition of IDO1 may increase the concentrations of tryptophan and subsequently serotonin, potentially leading to serotonin syndrome (SS). Tryptophan 26-36 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 18-22 31010933-2 2019 The substrate for IDO1 is tryptophan and there is a theoretical concern that inhibition of IDO1 may increase the concentrations of tryptophan and subsequently serotonin, potentially leading to serotonin syndrome (SS). Tryptophan 131-141 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 18-22 31010933-2 2019 The substrate for IDO1 is tryptophan and there is a theoretical concern that inhibition of IDO1 may increase the concentrations of tryptophan and subsequently serotonin, potentially leading to serotonin syndrome (SS). Tryptophan 131-141 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 91-95 29725904-2 2019 This stimulation induces indoleamine 2,3-dioxygenase (IDO), an enzyme that reduces the tryptophan bioavailability to synthesize serotonin. Tryptophan 87-97 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 54-57 30587994-12 2019 Xiaoyaosan could improve the tryptophan metabolism by regulating the expression levels of TPH2 and IDO1, thus exerting an antidepressant-like effect. Tryptophan 29-39 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 99-103 28659861-4 2017 Tryptophan 2,3-dioxygenase (TDO) and indoleamine 2,3-dioxygenase (IDO) convert l-tryptophan to N-formyl-l-kynurenine, to be further transformed to l-kynurenine. Tryptophan 79-91 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 37-64 30103191-1 2018 Indoleamine 2,3-dioxygenase 1 (IDO1) mediated kynurenine pathway of tryptophan degradation is identified as an appealing and novel target in immunotherapy for the treatment of cancer. Tryptophan 68-78 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 0-29 30103191-1 2018 Indoleamine 2,3-dioxygenase 1 (IDO1) mediated kynurenine pathway of tryptophan degradation is identified as an appealing and novel target in immunotherapy for the treatment of cancer. Tryptophan 68-78 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 31-35 29301550-0 2018 Role of the indoleamine-2,3-dioxygenase/kynurenine pathway of tryptophan metabolism in behavioral alterations in a hepatic encephalopathy rat model. Tryptophan 62-72 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 12-39 29301550-1 2018 BACKGROUND: This study aims to explore the role of indoleamine-2,3-dioxygenase (IDO)/kynurenine (KYN) pathway of tryptophan (TRY) metabolism in behavioral alterations observed in hepatic encephalopathy (HE) rats. Tryptophan 113-123 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 51-78 29301550-1 2018 BACKGROUND: This study aims to explore the role of indoleamine-2,3-dioxygenase (IDO)/kynurenine (KYN) pathway of tryptophan (TRY) metabolism in behavioral alterations observed in hepatic encephalopathy (HE) rats. Tryptophan 113-123 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 80-83 27730347-3 2017 This study was designed to investigate the hypothesis that CoQ10 by its anti-oxidant and anti-inflammatory potentials can alleviate depressive- like behavior by restoring the balance of the tryptophan catabolites kynurenine/serotonin toward the serotonin pathway by down-regulation of hippocampal indoleamine 2,3-dioxygenase 1 (IDO-1). Tryptophan 190-200 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 297-326 27730347-3 2017 This study was designed to investigate the hypothesis that CoQ10 by its anti-oxidant and anti-inflammatory potentials can alleviate depressive- like behavior by restoring the balance of the tryptophan catabolites kynurenine/serotonin toward the serotonin pathway by down-regulation of hippocampal indoleamine 2,3-dioxygenase 1 (IDO-1). Tryptophan 190-200 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 328-333 26671617-2 2016 However, the activation of the indoleamine-2,3-dioxygenase (IDO), an enzyme that participate of the tryptophan metabolism leading to a decrease of serotonin (5-HT) levels and whose expression is associated with an immune system activation, has been proposed as a common mechanism that links depression and diabetes. Tryptophan 100-110 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 60-63 28118532-11 2017 In conclusion, this study suggests a link between melatonin, JNK, FoxO1 and IDO1 that acts as a potential balance regulator of tryptophan metabolism, and offers a new approach to treat diseases related to dysregulation of tryptophan metabolism. Tryptophan 127-137 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 76-80 28118532-11 2017 In conclusion, this study suggests a link between melatonin, JNK, FoxO1 and IDO1 that acts as a potential balance regulator of tryptophan metabolism, and offers a new approach to treat diseases related to dysregulation of tryptophan metabolism. Tryptophan 222-232 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 76-80 27364617-5 2017 These results indicate that WIRS enhances hepatic Trp catabolism by inducing both IDO1 and TDO in rats. Tryptophan 50-53 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 82-86 27994058-1 2017 Indoleamine 2,3-dioxygenase 1 (IDO1) is a single chain oxidoreductase that catalyzes tryptophan degradation to kynurenine. Tryptophan 85-95 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 0-29 27994058-1 2017 Indoleamine 2,3-dioxygenase 1 (IDO1) is a single chain oxidoreductase that catalyzes tryptophan degradation to kynurenine. Tryptophan 85-95 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 31-35 27870896-6 2016 The expression and activity of cytokine-responsive indoleamine 2,3-dioxygenase (IDO-1), a catabolic enzyme of serotonin and tryptophan, was significantly increased in the CORT-treated group with lowered levels of serotonin. Tryptophan 124-134 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 80-85 24594021-2 2014 In this study, we report that indoleamine 2,3-dioxygenase 1 (IDO1), a rate-limiting enzyme in tryptophan metabolism, plays a key role in epilepsy-associated depressive-like behavior. Tryptophan 94-104 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 30-59 27232241-2 2016 The aqueous extract of Pc (AEPc) treatment reduced systolic blood pressure (SBP) in spontaneously hypertensive rats (SHR) via mechanisms mediated by the tryptophan metabolizing enzyme indoleamine 2,3-dioxygenase (IDO). Tryptophan 153-163 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 184-211 24594021-2 2014 In this study, we report that indoleamine 2,3-dioxygenase 1 (IDO1), a rate-limiting enzyme in tryptophan metabolism, plays a key role in epilepsy-associated depressive-like behavior. Tryptophan 94-104 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 61-65 24594021-7 2014 The upregulation of IDO1 subsequently increased the kynurenine/tryptophan ratio and decreased the serotonin/tryptophan ratio in the hippocampus, which contributed to epilepsy-associated depressive-like behavior. Tryptophan 63-73 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 20-24 24594021-7 2014 The upregulation of IDO1 subsequently increased the kynurenine/tryptophan ratio and decreased the serotonin/tryptophan ratio in the hippocampus, which contributed to epilepsy-associated depressive-like behavior. Tryptophan 108-118 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 20-24 23696839-8 2013 Moreover, the results of Western blot analysis of aromatic L-amino acid decarboxylase (DDC) and indoleamine 2, 3-dioxygenase (IDO) in the hippocampus of CUMS-treated rats indicated that depletion of 5-HT and tryptophan, production of 5-MT and altered expression of DDC and IDO together played a key role in the initiation and progression of depression. Tryptophan 208-218 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 126-129 24519862-1 2014 BACKGROUND: Indoleamine 2, 3-dioxygenase (IDO), a heme-containing dioxygenase, can catalyze tryptophan degradation and produce a local microenvironment with tryptophan depletion and tryptophan metabolites accumulation, which may suppress T cell-mediated immunity and play an important immunosuppressive role in many diseases. Tryptophan 92-102 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 12-40 24519862-1 2014 BACKGROUND: Indoleamine 2, 3-dioxygenase (IDO), a heme-containing dioxygenase, can catalyze tryptophan degradation and produce a local microenvironment with tryptophan depletion and tryptophan metabolites accumulation, which may suppress T cell-mediated immunity and play an important immunosuppressive role in many diseases. Tryptophan 92-102 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 42-45 24519862-1 2014 BACKGROUND: Indoleamine 2, 3-dioxygenase (IDO), a heme-containing dioxygenase, can catalyze tryptophan degradation and produce a local microenvironment with tryptophan depletion and tryptophan metabolites accumulation, which may suppress T cell-mediated immunity and play an important immunosuppressive role in many diseases. Tryptophan 157-167 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 12-40 24519862-1 2014 BACKGROUND: Indoleamine 2, 3-dioxygenase (IDO), a heme-containing dioxygenase, can catalyze tryptophan degradation and produce a local microenvironment with tryptophan depletion and tryptophan metabolites accumulation, which may suppress T cell-mediated immunity and play an important immunosuppressive role in many diseases. Tryptophan 157-167 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 42-45 24519862-1 2014 BACKGROUND: Indoleamine 2, 3-dioxygenase (IDO), a heme-containing dioxygenase, can catalyze tryptophan degradation and produce a local microenvironment with tryptophan depletion and tryptophan metabolites accumulation, which may suppress T cell-mediated immunity and play an important immunosuppressive role in many diseases. Tryptophan 157-167 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 12-40 24519862-1 2014 BACKGROUND: Indoleamine 2, 3-dioxygenase (IDO), a heme-containing dioxygenase, can catalyze tryptophan degradation and produce a local microenvironment with tryptophan depletion and tryptophan metabolites accumulation, which may suppress T cell-mediated immunity and play an important immunosuppressive role in many diseases. Tryptophan 157-167 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 42-45 24519862-2 2014 Previous studies suggested that tryptophan depletion is an important immunosuppressive mechanism of IDO, while recent evidence shows that tryptophan metabolites may also be useful for inducing the T cell immune tolerance. Tryptophan 32-42 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 100-103 21710661-1 2011 BACKGROUND: Indoleamine 2,3-dioxygenase (IDO), the rate-limiting enzyme in the tryptophan catabolism, has recently emerged as an important immunosuppressive enzyme involved in the regulation of both physiologic (maternal tolerance), as well as pathologic (neoplasia, autoimmune diseases, asthma) processes. Tryptophan 79-89 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 12-39 23303207-2 2013 The aim of this study was to investigate host pathways affected by L. johnsonii, with specific focus on the rate-limiting enzyme of tryptophan catabolism, indoleamine 2,3-dioxygenase (IDO). Tryptophan 132-142 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 155-182 22454246-8 2012 CONCLUSIONS: Our results suggested that IDO gene expression correlates with the severity of acute rejection and that IFN-gamma-induced IDO-positive DCs may attenuate acute rejection and catalyze local tryptophan metabolism via IDO enzyme expression, leading to immune tolerance after liver transplantation. Tryptophan 201-211 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 135-138 22454246-8 2012 CONCLUSIONS: Our results suggested that IDO gene expression correlates with the severity of acute rejection and that IFN-gamma-induced IDO-positive DCs may attenuate acute rejection and catalyze local tryptophan metabolism via IDO enzyme expression, leading to immune tolerance after liver transplantation. Tryptophan 201-211 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 135-138 22249930-1 2012 Indoleamine 2,3-dioxygenase (IDO) converts tryptophan to l-kynurenine, and it is noted as a relevant molecule in promoting tolerance and suppressing adaptive immunity. Tryptophan 43-53 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 0-27 22249930-1 2012 Indoleamine 2,3-dioxygenase (IDO) converts tryptophan to l-kynurenine, and it is noted as a relevant molecule in promoting tolerance and suppressing adaptive immunity. Tryptophan 43-53 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 29-32 21841011-1 2011 Indoleamine 2,3-dioxygenase (IDO) metabolizes L-tryptophan to L-kynurenine, promotes immunosuppression, and has been described as a consumer of superoxide. Tryptophan 46-58 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 0-27 21841011-1 2011 Indoleamine 2,3-dioxygenase (IDO) metabolizes L-tryptophan to L-kynurenine, promotes immunosuppression, and has been described as a consumer of superoxide. Tryptophan 46-58 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 29-32 21841011-6 2011 IDO activity (kynurenine-to-tryptophan ratio via HPLC) was detected in visceral and mesenteric artery fat (ratio: ~4) but was highest in perithoracic aortic fat (ratio: 10 +- 1.1). Tryptophan 28-38 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 0-3 22751107-2 2012 Here, we report that brain indoleamine 2,3-dioxygenase 1 (IDO1), a rate-limiting enzyme in tryptophan metabolism, plays a key role in this comorbidity. Tryptophan 91-101 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 27-56 22751107-2 2012 Here, we report that brain indoleamine 2,3-dioxygenase 1 (IDO1), a rate-limiting enzyme in tryptophan metabolism, plays a key role in this comorbidity. Tryptophan 91-101 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 58-62 22751107-4 2012 Upregulation of IDO1 resulted in the increased kynurenine/tryptophan ratio and decreased serotonin/tryptophan ratio in the bilateral hippocampus. Tryptophan 58-68 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 16-20 22751107-4 2012 Upregulation of IDO1 resulted in the increased kynurenine/tryptophan ratio and decreased serotonin/tryptophan ratio in the bilateral hippocampus. Tryptophan 99-109 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 16-20 21710661-1 2011 BACKGROUND: Indoleamine 2,3-dioxygenase (IDO), the rate-limiting enzyme in the tryptophan catabolism, has recently emerged as an important immunosuppressive enzyme involved in the regulation of both physiologic (maternal tolerance), as well as pathologic (neoplasia, autoimmune diseases, asthma) processes. Tryptophan 79-89 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 41-44 20847417-3 2010 Indoleamine 2, 3-dioxygenase (IDO-1) is the first and rate-limiting enzyme in the kynurenine pathway of tryptophan catabolism, which ultimately leads to the production of the excitotoxin quinolinic acid (QUIN). Tryptophan 104-114 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 30-35 19177450-3 2009 A vector encoding the rat IDO gene (rAAV2/8-LSP1-rIDO) was constructed and tested by its ability to induce tryptophan catabolism and kynurenine production in vitro and in vivo. Tryptophan 107-117 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 26-29 19373575-2 2009 Indoleamine 2,3-dioxygenase (IDO), which is expressed in many tissues and which is inducible by interferon-gamma (IFN-gamma), is able to oxidize Trp into kynurenines. Tryptophan 145-148 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 0-27 19373575-2 2009 Indoleamine 2,3-dioxygenase (IDO), which is expressed in many tissues and which is inducible by interferon-gamma (IFN-gamma), is able to oxidize Trp into kynurenines. Tryptophan 145-148 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 29-32 19373575-14 2009 IDO-mediated oxidation of Trp may partly explain the increase in lens KYNA and may thus be implicated in cataractogenesis in concert with the non-enzymic oxidation of Trp by glycated lens proteins. Tryptophan 26-29 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 0-3 19373575-14 2009 IDO-mediated oxidation of Trp may partly explain the increase in lens KYNA and may thus be implicated in cataractogenesis in concert with the non-enzymic oxidation of Trp by glycated lens proteins. Tryptophan 167-170 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 0-3 19177450-6 2009 In untransplanted PVG animals, the rAAV2/8-LSP1-rIDO vector induced, 3 weeks after administration, a 1.8-fold increase (P = 0.0161) in liver IDO activity, which was associated with a fall in serum tryptophan to 0.5 times the baseline level (P < 0.001). Tryptophan 197-207 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 49-52 19177450-7 2009 PVG recipients of PVG liver isografts pretreated with the IDO-expressing vector had a 45% lower level of serum tryptophan than recipients of isografts pretreated with the GFP-expressing vector (P = 0.03). Tryptophan 111-121 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 58-61 15206771-9 2003 Tryptophan-NAD pathway was initiated by cleavage of indole ring of tryptophan by TDO in the liver and IDO in many organs. Tryptophan 0-10 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 102-105 16319139-1 2005 Heme oxygenase-1 (HO-1) is the rate limiting enzyme of heme catabolism whereas indoleamine 2,3 dioxygenase (IDO) catabolizes tryptophan through the kynurenine pathway. Tryptophan 125-135 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 79-106 16319139-1 2005 Heme oxygenase-1 (HO-1) is the rate limiting enzyme of heme catabolism whereas indoleamine 2,3 dioxygenase (IDO) catabolizes tryptophan through the kynurenine pathway. Tryptophan 125-135 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 108-111 15612990-0 2005 Studying the immunosuppressive role of indoleamine 2,3-dioxygenase: tryptophan metabolites suppress rat allogeneic T-cell responses in vitro and in vivo. Tryptophan 68-78 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 39-66 15612990-2 2005 Recent studies pointed to a role of indoleamine 2,3-dioxygenase (IDO), a tryptophan-degrading enzyme expressed in the placenta, in mediation of T-cell suppression. Tryptophan 73-83 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 36-63 15612990-2 2005 Recent studies pointed to a role of indoleamine 2,3-dioxygenase (IDO), a tryptophan-degrading enzyme expressed in the placenta, in mediation of T-cell suppression. Tryptophan 73-83 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 65-68 15612990-4 2005 Here we analyze whether IDO-induced tryptophan metabolites are able to suppress the allogeneic T-cell response and allograft rejection in rats. Tryptophan 36-46 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 24-27 15612990-11 2005 We conclude that IDO-induced tryptophan metabolites suppress the T-cell response and prolong allograft survival in rats. Tryptophan 29-39 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 17-20 18929841-1 2008 OBJECTIVES: Indoleamine 2,3-dioxygenase (IDO), which catalyzes the breakdown of tryptophan into kyneurenine, has immunologic significance for the induction of maternal tolerance and liver allograft tolerance by inhibiting T-cell activation. Tryptophan 80-90 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 12-39 18929841-1 2008 OBJECTIVES: Indoleamine 2,3-dioxygenase (IDO), which catalyzes the breakdown of tryptophan into kyneurenine, has immunologic significance for the induction of maternal tolerance and liver allograft tolerance by inhibiting T-cell activation. Tryptophan 80-90 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 41-44 10719243-1 2000 Indoleamine 2,3-dioxygenase (IDO) reacts with either oxygen or superoxide and tryptophan (trp) or other indoleamines while tryptophan 2,3-dioxygenase (TDO) reacts with oxygen and is specific for trp. Tryptophan 78-88 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 0-27 11147699-1 2000 A tryptophan catabolizer, indoleamine 2,3-dioxygenase (IDO) is highly expressed in the placenta and plays an essential role in maternal tolerance. Tryptophan 2-12 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 26-53 11147699-1 2000 A tryptophan catabolizer, indoleamine 2,3-dioxygenase (IDO) is highly expressed in the placenta and plays an essential role in maternal tolerance. Tryptophan 2-12 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 55-58 10719243-1 2000 Indoleamine 2,3-dioxygenase (IDO) reacts with either oxygen or superoxide and tryptophan (trp) or other indoleamines while tryptophan 2,3-dioxygenase (TDO) reacts with oxygen and is specific for trp. Tryptophan 195-198 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 0-27 10719243-1 2000 Indoleamine 2,3-dioxygenase (IDO) reacts with either oxygen or superoxide and tryptophan (trp) or other indoleamines while tryptophan 2,3-dioxygenase (TDO) reacts with oxygen and is specific for trp. Tryptophan 78-88 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 29-32 10719243-1 2000 Indoleamine 2,3-dioxygenase (IDO) reacts with either oxygen or superoxide and tryptophan (trp) or other indoleamines while tryptophan 2,3-dioxygenase (TDO) reacts with oxygen and is specific for trp. Tryptophan 195-198 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 29-32 10719243-1 2000 Indoleamine 2,3-dioxygenase (IDO) reacts with either oxygen or superoxide and tryptophan (trp) or other indoleamines while tryptophan 2,3-dioxygenase (TDO) reacts with oxygen and is specific for trp. Tryptophan 90-93 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 0-27 10719243-1 2000 Indoleamine 2,3-dioxygenase (IDO) reacts with either oxygen or superoxide and tryptophan (trp) or other indoleamines while tryptophan 2,3-dioxygenase (TDO) reacts with oxygen and is specific for trp. Tryptophan 90-93 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 29-32 34252442-1 2021 Kynurenine Pathway (KP) is the dominant metabolic route of tryptophan which is catalyzed by indoleamine-2,3-dioxygenase (IDO). Tryptophan 59-69 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 92-119 34975590-0 2021 Cang-Ai Volatile Oil Ameliorates Depressive Behavior Induced by Chronic Stress Through IDO-Mediated Tryptophan Degradation Pathway. Tryptophan 100-110 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 87-90 34975590-3 2021 The current study sought to explore whether CAVO exhibits anti-depressant effects of CAVO through inhibition of inflammatory response and regulation of indoleamine 2 and 3-dioxygenase (IDO) mediated tryptophan degradation pathway. Tryptophan 199-209 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 152-183 34975590-3 2021 The current study sought to explore whether CAVO exhibits anti-depressant effects of CAVO through inhibition of inflammatory response and regulation of indoleamine 2 and 3-dioxygenase (IDO) mediated tryptophan degradation pathway. Tryptophan 199-209 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 185-188 33031882-2 2021 In the kynurenine pathway, the enzyme indoleamine 2,3 dioxygenase (IDO) is responsible for the conversion of tryptophan to kynurenine, and dysregulation of this pathway has been associated with psychiatric disorders, such as anxiety and depression. Tryptophan 109-119 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 38-65 33031882-2 2021 In the kynurenine pathway, the enzyme indoleamine 2,3 dioxygenase (IDO) is responsible for the conversion of tryptophan to kynurenine, and dysregulation of this pathway has been associated with psychiatric disorders, such as anxiety and depression. Tryptophan 109-119 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 67-70 34252442-1 2021 Kynurenine Pathway (KP) is the dominant metabolic route of tryptophan which is catalyzed by indoleamine-2,3-dioxygenase (IDO). Tryptophan 59-69 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 121-124 34512234-10 2021 Conclusion: Inflammatory cytokines induced by large abdominal surgery disturb tryptophan metabolism to cause POFS through the activation of the p38MAPK-NF-kappaB/p65-IDO pathway in the hippocampus. Tryptophan 78-88 indoleamine 2,3-dioxygenase 1 Rattus norvegicus 166-169