PMID-sentid	Pub_year	Sent_text	compound_name	comp_offset	prot_official_name	organism	prot_offset
34358860-9	2021	The Kynurenine/Tryptophan ratio and CRP levels of the conventional therapy and anti-TNF therapy group were significantly lower than the newly diagnosed AS patients (p < 0.05).	Kynurenine	4-14	tumor necrosis factor	Homo sapiens	84-87
34358860-11	2021	Conventional therapy and anti-TNF-alpha therapy are effective in reducing the Kynurenine/Tryptophan ratio and CRP levels, although the effect of both treatments on other metabolites appears to be limited.	Kynurenine	78-88	tumor necrosis factor	Homo sapiens	30-39
34563230-0	2021	Kynurenine derivative 3-HAA is an agonist ligand for transcription factor YY1.	Kynurenine	0-10	YY1 transcription factor	Homo sapiens	74-77
34505780-7	2021	Additionally, the kidney expression of the aryl hydrocarbon receptor (AHR), an endogenous receptor of l-kynurenine, was enhanced in hyperuricemic mice and further reduced in fisetin-treated mice.	Kynurenine	102-114	aryl-hydrocarbon receptor	Mus musculus	43-68
34505780-7	2021	Additionally, the kidney expression of the aryl hydrocarbon receptor (AHR), an endogenous receptor of l-kynurenine, was enhanced in hyperuricemic mice and further reduced in fisetin-treated mice.	Kynurenine	102-114	aryl-hydrocarbon receptor	Mus musculus	70-73
34505780-8	2021	Finally, in vitro results showed that inhibition of AHR activation attenuated l-kynurenine-induced fibrosis.	Kynurenine	78-90	aryl-hydrocarbon receptor	Mus musculus	52-55
34900804-6	2021	IDO activity was estimated using kynurenine/tryptophan ratio (KTR).	Kynurenine	33-43	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-3
34601342-10	2021	The kynurenine pathway mediates the many depressive-like behavioral effects of peripheral LPS, and similar to pro-inflammatory cytokine gene expression, indoleamine 2,3-dioxygenase (IDO) expression and kynurenine metabolism was exaggerated in BDNF+/- mice.	Kynurenine	4-14	brain derived neurotrophic factor	Mus musculus	243-247
34601342-10	2021	The kynurenine pathway mediates the many depressive-like behavioral effects of peripheral LPS, and similar to pro-inflammatory cytokine gene expression, indoleamine 2,3-dioxygenase (IDO) expression and kynurenine metabolism was exaggerated in BDNF+/- mice.	Kynurenine	202-212	brain derived neurotrophic factor	Mus musculus	243-247
34589400-1	2021	Tryptophan 2,3-dioxygnease 2 (TDO2) is specific for metabolizing tryptophan to kynurenine (KYN), which plays a critical role in mediating immune escape of cancer.	Kynurenine	79-89	tryptophan 2,3-dioxygenase	Mus musculus	30-34
34511126-7	2021	A network interaction analysis showed that in the PFC IL-10 was coupled to the QA branch of the kynurenine pathway (TDO-KMO-QA), whereas IL-10 associated with KMO in CB.	Kynurenine	96-106	interleukin 10	Homo sapiens	54-59
34511126-7	2021	A network interaction analysis showed that in the PFC IL-10 was coupled to the QA branch of the kynurenine pathway (TDO-KMO-QA), whereas IL-10 associated with KMO in CB.	Kynurenine	96-106	tryptophan 2,3-dioxygenase	Homo sapiens	116-119
34511126-7	2021	A network interaction analysis showed that in the PFC IL-10 was coupled to the QA branch of the kynurenine pathway (TDO-KMO-QA), whereas IL-10 associated with KMO in CB.	Kynurenine	96-106	kynurenine 3-monooxygenase	Homo sapiens	120-123
34589400-1	2021	Tryptophan 2,3-dioxygnease 2 (TDO2) is specific for metabolizing tryptophan to kynurenine (KYN), which plays a critical role in mediating immune escape of cancer.	Kynurenine	79-89	tryptophan 2,3-dioxygenase	Mus musculus	0-28
34363411-3	2021	Using CD1 mice, we examined acute and long-term effects of prenatal LPS treatment on the levels of kynurenine and its neuroactive downstream products kynurenic acid (KYNA), 3-hydroxykynurenine (3-HK) and quinolinic acid.	Kynurenine	99-109	CD1 antigen complex	Mus musculus	6-9
34407414-0	2021	Hypoxic preconditioning protects against ischemic kidney injury through the IDO1/kynurenine pathway.	Kynurenine	81-91	indoleamine 2,3-dioxygenase 1	Homo sapiens	76-80
34407414-7	2021	Importantly, exogenous administration of kynurenine restores the hypoxic preconditioning in the context of Ido1 deficiency.	Kynurenine	41-51	indoleamine 2,3-dioxygenase 1	Homo sapiens	107-111
34407414-8	2021	Collectively, our findings demonstrate a critical role of the IDO1-kynurenine axis in mediating hypoxic preconditioning.	Kynurenine	67-77	indoleamine 2,3-dioxygenase 1	Homo sapiens	62-66
34407414-6	2021	Furthermore, we show that indoleamine 2,3-dioxygenase 1 (Ido1) deficiency abolishes the systemic increase of kynurenine and the subsequent renoprotection generated by hypoxic preconditioning and PHD inhibition.	Kynurenine	109-119	indoleamine 2,3-dioxygenase 1	Homo sapiens	26-55
34407414-6	2021	Furthermore, we show that indoleamine 2,3-dioxygenase 1 (Ido1) deficiency abolishes the systemic increase of kynurenine and the subsequent renoprotection generated by hypoxic preconditioning and PHD inhibition.	Kynurenine	109-119	indoleamine 2,3-dioxygenase 1	Homo sapiens	57-61
34338527-2	2021	Expression of TDO2 in cancer cells results in the inhibition of immune-mediated tumor rejection due to an enhancement of l-Trp catabolism via the kynurenine pathway.	Kynurenine	146-156	tryptophan 2,3-dioxygenase	Homo sapiens	14-18
34413774-9	2021	The expression of kynurenine pathway related genes TDO, IDO1, IDO2, and apoptosis-related genes caspase1, 3, 4, 5, 7, 12 in tumor tissues were measured by western blotting and qRT-PCR.	Kynurenine	18-28	tryptophan 2,3-dioxygenase	Mus musculus	51-54
34423034-1	2021	Background: Tryptophan-2,3-dioxygenase (TDO2) converts tryptophan into kynurenine in the initial limiting step of the kynurenine pathway.	Kynurenine	71-81	tryptophan 2,3-dioxygenase	Homo sapiens	40-44
34423034-1	2021	Background: Tryptophan-2,3-dioxygenase (TDO2) converts tryptophan into kynurenine in the initial limiting step of the kynurenine pathway.	Kynurenine	118-128	tryptophan 2,3-dioxygenase	Homo sapiens	40-44
34522212-9	2021	Results: Activating AhR by the endogenous ligand L-Kynurenine (L-KN) or FICZ, or by the exogenous ligand diosmin or indole-3-carbinol (I3C) significantly increases NEP expression and enzyme activity in N2a cells and APP/PS1 mice.	Kynurenine	49-61	aryl-hydrocarbon receptor	Mus musculus	20-23
34522212-9	2021	Results: Activating AhR by the endogenous ligand L-Kynurenine (L-KN) or FICZ, or by the exogenous ligand diosmin or indole-3-carbinol (I3C) significantly increases NEP expression and enzyme activity in N2a cells and APP/PS1 mice.	Kynurenine	49-61	membrane metallo endopeptidase	Mus musculus	164-167
34522212-9	2021	Results: Activating AhR by the endogenous ligand L-Kynurenine (L-KN) or FICZ, or by the exogenous ligand diosmin or indole-3-carbinol (I3C) significantly increases NEP expression and enzyme activity in N2a cells and APP/PS1 mice.	Kynurenine	49-61	presenilin 1	Mus musculus	220-223
34522212-9	2021	Results: Activating AhR by the endogenous ligand L-Kynurenine (L-KN) or FICZ, or by the exogenous ligand diosmin or indole-3-carbinol (I3C) significantly increases NEP expression and enzyme activity in N2a cells and APP/PS1 mice.	Kynurenine	63-67	aryl-hydrocarbon receptor	Mus musculus	20-23
34522212-9	2021	Results: Activating AhR by the endogenous ligand L-Kynurenine (L-KN) or FICZ, or by the exogenous ligand diosmin or indole-3-carbinol (I3C) significantly increases NEP expression and enzyme activity in N2a cells and APP/PS1 mice.	Kynurenine	63-67	membrane metallo endopeptidase	Mus musculus	164-167
34522212-9	2021	Results: Activating AhR by the endogenous ligand L-Kynurenine (L-KN) or FICZ, or by the exogenous ligand diosmin or indole-3-carbinol (I3C) significantly increases NEP expression and enzyme activity in N2a cells and APP/PS1 mice.	Kynurenine	63-67	presenilin 1	Mus musculus	220-223
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.	Kynurenine	128-138	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.	Kynurenine	128-138	indoleamine 2,3-dioxygenase 1	Homo sapiens	40-43
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.	Kynurenine	137-147	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.	Kynurenine	137-147	indoleamine 2,3-dioxygenase 1	Homo sapiens	31-35
34413774-9	2021	The expression of kynurenine pathway related genes TDO, IDO1, IDO2, and apoptosis-related genes caspase1, 3, 4, 5, 7, 12 in tumor tissues were measured by western blotting and qRT-PCR.	Kynurenine	18-28	indoleamine 2,3-dioxygenase 1	Mus musculus	56-60
34413774-9	2021	The expression of kynurenine pathway related genes TDO, IDO1, IDO2, and apoptosis-related genes caspase1, 3, 4, 5, 7, 12 in tumor tissues were measured by western blotting and qRT-PCR.	Kynurenine	18-28	indoleamine 2,3-dioxygenase 2	Mus musculus	62-66
34251022-5	2021	Excess haem can also impair CBS activity by inhibiting it via CO resulting from haem induction of haem oxygenase, and by induction of a functional vitamin B6 deficiency following activation of hepatic tryptophan 2,3-dioxygenase and subsequent utilisation of PLP by enhanced kynurenine aminotransferase and kynureninase activities.	Kynurenine	274-284	tryptophan 2,3-dioxygenase	Homo sapiens	201-227
34341450-0	2021	The genetic architecture of plasma kynurenine includes cardiometabolic disease mechanisms associated with the SH2B3 gene.	Kynurenine	35-45	SH2B adaptor protein 3	Homo sapiens	110-115
34341450-5	2021	We identified single-nucleotide polymorphisms (SNPs) previously associated with plasma kynurenine, including a missense-variant (rs3184504) in the inflammatory gene SH2B3/LNK.	Kynurenine	87-97	SH2B adaptor protein 3	Homo sapiens	165-170
34341450-5	2021	We identified single-nucleotide polymorphisms (SNPs) previously associated with plasma kynurenine, including a missense-variant (rs3184504) in the inflammatory gene SH2B3/LNK.	Kynurenine	87-97	SH2B adaptor protein 3	Homo sapiens	171-174
34341450-6	2021	We examined the association between rs3184504 and plasma kynurenine in independent human samples, and measured kynurenine levels in SH2B3-knock-out mice and during human LPS-evoked endotoxemia.	Kynurenine	111-121	SH2B adaptor protein 3	Homo sapiens	132-137
34341450-8	2021	The SH2B3 missense variant associated with plasma kynurenine levels and SH2B3-/- mice had significant tissue-specific differences in kynurenine levels.LPS, an acute inflammatory stimulus, increased plasma kynurenine in humans.	Kynurenine	50-60	SH2B adaptor protein 3	Mus musculus	4-9
34341450-8	2021	The SH2B3 missense variant associated with plasma kynurenine levels and SH2B3-/- mice had significant tissue-specific differences in kynurenine levels.LPS, an acute inflammatory stimulus, increased plasma kynurenine in humans.	Kynurenine	133-143	SH2B adaptor protein 3	Mus musculus	4-9
34341450-8	2021	The SH2B3 missense variant associated with plasma kynurenine levels and SH2B3-/- mice had significant tissue-specific differences in kynurenine levels.LPS, an acute inflammatory stimulus, increased plasma kynurenine in humans.	Kynurenine	205-215	SH2B adaptor protein 3	Mus musculus	4-9
34341450-9	2021	Mendelian randomization showed increased waist-circumference, a marker of central obesity, associated with increased kynurenine, and increased kynurenine associated with C-reactive protein (CRP).	Kynurenine	143-153	C-reactive protein	Homo sapiens	170-188
34341450-9	2021	Mendelian randomization showed increased waist-circumference, a marker of central obesity, associated with increased kynurenine, and increased kynurenine associated with C-reactive protein (CRP).	Kynurenine	143-153	C-reactive protein	Homo sapiens	190-193
34341450-11	2021	Plasma kynurenine may be a biomarker of acute and chronic inflammation involving the SH2B3 pathways.	Kynurenine	7-17	SH2B adaptor protein 3	Homo sapiens	85-90
34394118-2	2021	Indoleamine 2,3-dioxygenase 1 (IDO1) is an enzyme that catalyzes the first step in the kynurenine pathway by transforming l-tryptophan (Trp) into l-kynurenine (Kyn), a metabolite endowed with anti-inflammatory and immunoregulatory effects.	Kynurenine	87-97	indoleamine 2,3-dioxygenase 1	Mus musculus	0-29
34394118-2	2021	Indoleamine 2,3-dioxygenase 1 (IDO1) is an enzyme that catalyzes the first step in the kynurenine pathway by transforming l-tryptophan (Trp) into l-kynurenine (Kyn), a metabolite endowed with anti-inflammatory and immunoregulatory effects.	Kynurenine	87-97	indoleamine 2,3-dioxygenase 1	Mus musculus	31-35
34394118-2	2021	Indoleamine 2,3-dioxygenase 1 (IDO1) is an enzyme that catalyzes the first step in the kynurenine pathway by transforming l-tryptophan (Trp) into l-kynurenine (Kyn), a metabolite endowed with anti-inflammatory and immunoregulatory effects.	Kynurenine	146-158	indoleamine 2,3-dioxygenase 1	Mus musculus	0-29
34394118-2	2021	Indoleamine 2,3-dioxygenase 1 (IDO1) is an enzyme that catalyzes the first step in the kynurenine pathway by transforming l-tryptophan (Trp) into l-kynurenine (Kyn), a metabolite endowed with anti-inflammatory and immunoregulatory effects.	Kynurenine	146-158	indoleamine 2,3-dioxygenase 1	Mus musculus	31-35
34394118-2	2021	Indoleamine 2,3-dioxygenase 1 (IDO1) is an enzyme that catalyzes the first step in the kynurenine pathway by transforming l-tryptophan (Trp) into l-kynurenine (Kyn), a metabolite endowed with anti-inflammatory and immunoregulatory effects.	Kynurenine	160-163	indoleamine 2,3-dioxygenase 1	Mus musculus	0-29
34394118-2	2021	Indoleamine 2,3-dioxygenase 1 (IDO1) is an enzyme that catalyzes the first step in the kynurenine pathway by transforming l-tryptophan (Trp) into l-kynurenine (Kyn), a metabolite endowed with anti-inflammatory and immunoregulatory effects.	Kynurenine	160-163	indoleamine 2,3-dioxygenase 1	Mus musculus	31-35
34393855-0	2021	Associations Between the Kynurenine Pathway, Proinflammatory Cytokines, and Brain-Derived Neurotrophic Factor in Hospitalized Patients With Chronic Schizophrenia: A Preliminary Study.	Kynurenine	25-35	brain derived neurotrophic factor	Homo sapiens	76-109
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.	Kynurenine	79-89	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.	Kynurenine	79-89	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.	Kynurenine	91-94	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.	Kynurenine	91-94	indoleamine 2,3-dioxygenase 1	Homo sapiens	41-44
34335614-4	2021	Here, we exploited the hypothesis that ZIKV-induced neurodegeneration can be rescued by blocking a target enzyme of the kynurenine pathway, the Indoleamine 2,3-dioxygenase (IDO-1).	Kynurenine	120-130	indoleamine 2,3-dioxygenase 1	Homo sapiens	173-178
34289794-6	2021	Indole metabolites and kynurenine interact with aryl hydrocarbon receptor (AHR) to induce T regulatory cells differentiation, confine Th17 and Th1 response and produce anti-inflammatory mediators.	Kynurenine	23-33	aryl hydrocarbon receptor	Homo sapiens	48-73
34289794-6	2021	Indole metabolites and kynurenine interact with aryl hydrocarbon receptor (AHR) to induce T regulatory cells differentiation, confine Th17 and Th1 response and produce anti-inflammatory mediators.	Kynurenine	23-33	aryl hydrocarbon receptor	Homo sapiens	75-78
34289794-7	2021	Kynurenine decreases tumor-infiltrating CD8+ cells and mediates tumor cells immune evasion.	Kynurenine	0-10	CD8a molecule	Homo sapiens	40-43
34299117-2	2021	Human skin is constantly exposed to selected tryptophan-derived aryl hydrocarbon receptor (AhR) ligands, including kynurenine (KYN) and kynurenic acid (KYNA), as they are endogenously produced and present in various tissues and body fluids.	Kynurenine	115-125	aryl hydrocarbon receptor	Homo sapiens	64-89
34299117-2	2021	Human skin is constantly exposed to selected tryptophan-derived aryl hydrocarbon receptor (AhR) ligands, including kynurenine (KYN) and kynurenic acid (KYNA), as they are endogenously produced and present in various tissues and body fluids.	Kynurenine	115-125	aryl hydrocarbon receptor	Homo sapiens	91-94
34299117-2	2021	Human skin is constantly exposed to selected tryptophan-derived aryl hydrocarbon receptor (AhR) ligands, including kynurenine (KYN) and kynurenic acid (KYNA), as they are endogenously produced and present in various tissues and body fluids.	Kynurenine	127-130	aryl hydrocarbon receptor	Homo sapiens	64-89
34299117-2	2021	Human skin is constantly exposed to selected tryptophan-derived aryl hydrocarbon receptor (AhR) ligands, including kynurenine (KYN) and kynurenic acid (KYNA), as they are endogenously produced and present in various tissues and body fluids.	Kynurenine	127-130	aryl hydrocarbon receptor	Homo sapiens	91-94
34273987-10	2021	Finally, we report an association between the kynurenine/tryptophan ratio and CRP.	Kynurenine	46-56	C-reactive protein	Homo sapiens	78-81
34396103-6	2021	Higher levels of one acylcarnitine (C3; propionylcarnitine) and one biogenic amine (kynurenine) were associated with decreased amyloid-beta accumulation and higher memory scores.	Kynurenine	84-94	amyloid beta precursor protein	Homo sapiens	127-139
34281987-7	2021	Metabolomics analysis indicated that GCH1 overexpression reprogrammed tryptophan metabolism, resulting in L-5-hydroxytryptophan (5-HTP) accumulation in the cytoplasm accompanied by kynurenine accumulation and tryptophan reduction in the supernatant.	Kynurenine	181-191	GTP cyclohydrolase 1	Homo sapiens	37-41
34210797-8	2021	These effects are not observed with kynurenine, another AhR ligand.	Kynurenine	36-46	aryl-hydrocarbon receptor	Mus musculus	56-59
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.	Kynurenine	61-71	aryl hydrocarbon receptor	Homo sapiens	35-38
34262289-0	2021	The Effects of Maternal Interleukin-17A on Social Behavior, Cognitive Function, and Depression-Like Behavior in Mice with Altered Kynurenine Metabolites.	Kynurenine	130-140	interleukin 17A	Mus musculus	24-39
34202246-6	2021	KYN, kynurenic acid, xanthurenic acid and cinnabarinic acid are aryl hydrocarbon receptor ligands that serve as immunomodulators.	Kynurenine	0-3	aryl hydrocarbon receptor	Homo sapiens	64-89
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.	Kynurenine	146-156	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.	Kynurenine	146-156	indoleamine 2,3-dioxygenase 1	Homo sapiens	31-35
34065885-0	2021	Human Indoleamine 2,3-dioxygenase 1 (IDO1) Expressed in Plant Cells Induces Kynurenine Production.	Kynurenine	76-86	indoleamine 2,3-dioxygenase 1	Homo sapiens	6-35
34065885-0	2021	Human Indoleamine 2,3-dioxygenase 1 (IDO1) Expressed in Plant Cells Induces Kynurenine Production.	Kynurenine	76-86	indoleamine 2,3-dioxygenase 1	Homo sapiens	37-41
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.	Kynurenine	30-40	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.	Kynurenine	30-40	indoleamine 2,3-dioxygenase 1	Homo sapiens	218-222
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.	Kynurenine	255-265	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.	Kynurenine	255-265	indoleamine 2,3-dioxygenase 1	Homo sapiens	218-222
34065885-5	2021	Analysis of transiently transfected tobacco protoplasts demonstrated that the IDO1-GFP gene led to the expression of a detectable protein and to the production of kynurenine in the protoplast medium.	Kynurenine	163-173	indoleamine 2,3-dioxygenase 1	Homo sapiens	78-82
34065885-7	2021	To the best of our knowledge, this is the first report on the expression of human IDO1 enzyme capable of secreting kynurenines in plant cells.	Kynurenine	115-126	indoleamine 2,3-dioxygenase 1	Homo sapiens	82-86
34207309-2	2021	The present study aimed to establish potential interactions between endogenous parathyroid hormone (PTH) and activation of the bone kynurenine (KYN) pathway in relation to bone turnover and strength in young rats after one month (CKD-1) and three months (CKD-3) of experimental CKD.	Kynurenine	132-142	parathyroid hormone	Rattus norvegicus	79-98
34207309-2	2021	The present study aimed to establish potential interactions between endogenous parathyroid hormone (PTH) and activation of the bone kynurenine (KYN) pathway in relation to bone turnover and strength in young rats after one month (CKD-1) and three months (CKD-3) of experimental CKD.	Kynurenine	132-142	parathyroid hormone	Rattus norvegicus	100-103
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.	Kynurenine	15-25	indoleamine 2,3-dioxygenase 1	Homo sapiens	113-140
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.	Kynurenine	129-139	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.	Kynurenine	129-139	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.	Kynurenine	141-144	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.	Kynurenine	141-144	indoleamine 2,3-dioxygenase 1	Homo sapiens	163-166
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.	Kynurenine	61-71	indoleamine 2,3-dioxygenase 1	Homo sapiens	138-142
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.	Kynurenine	61-71	tryptophan 2,3-dioxygenase	Homo sapiens	147-150
35582948-0	2022	Indoleamine 2,3-Dioxygenase 1 Deletion-Mediated Kynurenine Insufficiency in Vascular Smooth Muscle Cells Exacerbates Arterial Calcification.	Kynurenine	48-58	indoleamine 2,3-dioxygenase 1	Mus musculus	0-29
34087454-4	2021	In this study, we demonstrated that kynurenine (Kyn), a metabolite catalyzed by indoleamine 2,3-dioxygenase (IDO), was required for IDO-mediated T cells function, and adaptive immunity indeed played a critical role in CRC.	Kynurenine	36-46	indoleamine 2,3-dioxygenase 1	Mus musculus	80-107
34087454-4	2021	In this study, we demonstrated that kynurenine (Kyn), a metabolite catalyzed by indoleamine 2,3-dioxygenase (IDO), was required for IDO-mediated T cells function, and adaptive immunity indeed played a critical role in CRC.	Kynurenine	36-46	indoleamine 2,3-dioxygenase 1	Mus musculus	109-112
34087454-4	2021	In this study, we demonstrated that kynurenine (Kyn), a metabolite catalyzed by indoleamine 2,3-dioxygenase (IDO), was required for IDO-mediated T cells function, and adaptive immunity indeed played a critical role in CRC.	Kynurenine	36-46	indoleamine 2,3-dioxygenase 1	Mus musculus	132-135
34087454-4	2021	In this study, we demonstrated that kynurenine (Kyn), a metabolite catalyzed by indoleamine 2,3-dioxygenase (IDO), was required for IDO-mediated T cells function, and adaptive immunity indeed played a critical role in CRC.	Kynurenine	48-51	indoleamine 2,3-dioxygenase 1	Mus musculus	80-107
34087454-4	2021	In this study, we demonstrated that kynurenine (Kyn), a metabolite catalyzed by indoleamine 2,3-dioxygenase (IDO), was required for IDO-mediated T cells function, and adaptive immunity indeed played a critical role in CRC.	Kynurenine	48-51	indoleamine 2,3-dioxygenase 1	Mus musculus	109-112
34087454-4	2021	In this study, we demonstrated that kynurenine (Kyn), a metabolite catalyzed by indoleamine 2,3-dioxygenase (IDO), was required for IDO-mediated T cells function, and adaptive immunity indeed played a critical role in CRC.	Kynurenine	48-51	indoleamine 2,3-dioxygenase 1	Mus musculus	132-135
35582948-9	2022	In contrast, administration of kynurenine via intraperitoneal injection markedly delayed the progression of intimal calcification in parallel with decreased RUNX2 expression in both Apoe-/- and Apoe-/- Ido1-/- mice.	Kynurenine	31-41	runt related transcription factor 2	Mus musculus	157-162
35582948-9	2022	In contrast, administration of kynurenine via intraperitoneal injection markedly delayed the progression of intimal calcification in parallel with decreased RUNX2 expression in both Apoe-/- and Apoe-/- Ido1-/- mice.	Kynurenine	31-41	apolipoprotein E	Mus musculus	182-186
35582948-9	2022	In contrast, administration of kynurenine via intraperitoneal injection markedly delayed the progression of intimal calcification in parallel with decreased RUNX2 expression in both Apoe-/- and Apoe-/- Ido1-/- mice.	Kynurenine	31-41	apolipoprotein E	Mus musculus	194-198
35582948-9	2022	In contrast, administration of kynurenine via intraperitoneal injection markedly delayed the progression of intimal calcification in parallel with decreased RUNX2 expression in both Apoe-/- and Apoe-/- Ido1-/- mice.	Kynurenine	31-41	indoleamine 2,3-dioxygenase 1	Mus musculus	202-206
35582948-11	2022	Kynurenine administration downregulated RUNX2 in an aryl hydrocarbon receptor-dependent manner.	Kynurenine	0-10	runt related transcription factor 2	Mus musculus	40-45
35582948-11	2022	Kynurenine administration downregulated RUNX2 in an aryl hydrocarbon receptor-dependent manner.	Kynurenine	0-10	aryl-hydrocarbon receptor	Mus musculus	52-77
35582948-12	2022	Kynurenine acted as the endogenous ligand of aryl hydrocarbon receptor, controlled resultant interactions between cullin 4B and aryl hydrocarbon receptor to form an E3 ubiquitin ligase that bound with RUNX2, and subsequently promoted ubiquitin-mediated instability of RUNX2 in VSMCs.	Kynurenine	0-10	aryl-hydrocarbon receptor	Mus musculus	45-70
35582948-12	2022	Kynurenine acted as the endogenous ligand of aryl hydrocarbon receptor, controlled resultant interactions between cullin 4B and aryl hydrocarbon receptor to form an E3 ubiquitin ligase that bound with RUNX2, and subsequently promoted ubiquitin-mediated instability of RUNX2 in VSMCs.	Kynurenine	0-10	cullin 4B	Mus musculus	114-123
35582948-12	2022	Kynurenine acted as the endogenous ligand of aryl hydrocarbon receptor, controlled resultant interactions between cullin 4B and aryl hydrocarbon receptor to form an E3 ubiquitin ligase that bound with RUNX2, and subsequently promoted ubiquitin-mediated instability of RUNX2 in VSMCs.	Kynurenine	0-10	aryl-hydrocarbon receptor	Mus musculus	128-153
35582948-12	2022	Kynurenine acted as the endogenous ligand of aryl hydrocarbon receptor, controlled resultant interactions between cullin 4B and aryl hydrocarbon receptor to form an E3 ubiquitin ligase that bound with RUNX2, and subsequently promoted ubiquitin-mediated instability of RUNX2 in VSMCs.	Kynurenine	0-10	runt related transcription factor 2	Mus musculus	201-206
35582948-12	2022	Kynurenine acted as the endogenous ligand of aryl hydrocarbon receptor, controlled resultant interactions between cullin 4B and aryl hydrocarbon receptor to form an E3 ubiquitin ligase that bound with RUNX2, and subsequently promoted ubiquitin-mediated instability of RUNX2 in VSMCs.	Kynurenine	0-10	runt related transcription factor 2	Mus musculus	268-273
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.	Kynurenine	13-23	indoleamine 2,3-dioxygenase 1	Homo sapiens	28-32
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.	Kynurenine	13-23	RUNX family transcription factor 2	Homo sapiens	87-92
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.	Kynurenine	13-23	aryl-hydrocarbon receptor	Mus musculus	169-194
35582948-15	2022	Insufficient kynurenine exerts the deleterious role of IDO1 ablation in promoting RUNX2-mediated VSMCs osteogenic reprogramming and calcification in vivo.	Kynurenine	13-23	RUNX family transcription factor 2	Homo sapiens	82-87
35226727-8	2022	Notably, PB502 was by far superior to the endogenous AHR ligand, L-Kynurenine, in promoting the differentiation of both mouse and human FoxP3+ regulatory CD4+ T cells.	Kynurenine	65-77	aryl-hydrocarbon receptor	Mus musculus	53-56
35358315-7	2022	The kynurenine/tryptophan ratio (KTR-a proxy of indoleamine-2,3-dioxygenase which degrades tryptophan to kynurenine and contribute to a pro-inflammatory status) mediated 42% of the significant association between the anti-atherogenic IL-13 and mortality.	Kynurenine	4-14	interleukin 13	Homo sapiens	234-239
35226727-8	2022	Notably, PB502 was by far superior to the endogenous AHR ligand, L-Kynurenine, in promoting the differentiation of both mouse and human FoxP3+ regulatory CD4+ T cells.	Kynurenine	65-77	forkhead box P3	Homo sapiens	136-141
35226727-8	2022	Notably, PB502 was by far superior to the endogenous AHR ligand, L-Kynurenine, in promoting the differentiation of both mouse and human FoxP3+ regulatory CD4+ T cells.	Kynurenine	65-77	CD4 molecule	Homo sapiens	154-157
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).	Kynurenine	169-179	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-29
35623392-7	2022	Investigation into the possible mechanisms indicated that a combination of growth factor, G-CSF, and metabolites, Kynurenine and lactic acid produced by AECs is responsible for inducing tolerance in macrophages.	Kynurenine	114-124	colony stimulating factor 3	Homo sapiens	90-95
35623392-8	2022	Interestingly, all these molecules had differential effect on macrophages with G-CSF inducing TGF-beta, Kynurenine elevating IL-10, and lactic acid upregulating CD200R.	Kynurenine	104-114	colony stimulating factor 3	Homo sapiens	79-84
35623392-8	2022	Interestingly, all these molecules had differential effect on macrophages with G-CSF inducing TGF-beta, Kynurenine elevating IL-10, and lactic acid upregulating CD200R.	Kynurenine	104-114	interleukin 10	Homo sapiens	125-130
35377087-3	2022	This pathway indicates that, chronic stress primarily promotes the release of excessive cortisol from the adrenal gland, which tends to activate microglia and further increases kynurenine and its downstream pathway, resulting in excessive quinolinic acid (QA), which further impairs brain derived neurotrophic factor (BDNF) levels and leads to neurodegeneration.	Kynurenine	177-187	brain derived neurotrophic factor	Mus musculus	283-316
35377087-3	2022	This pathway indicates that, chronic stress primarily promotes the release of excessive cortisol from the adrenal gland, which tends to activate microglia and further increases kynurenine and its downstream pathway, resulting in excessive quinolinic acid (QA), which further impairs brain derived neurotrophic factor (BDNF) levels and leads to neurodegeneration.	Kynurenine	177-187	brain derived neurotrophic factor	Mus musculus	318-322
35466092-6	2022	IDO is an intracellular monomeric enzyme that is also responsible for breaking down and consuming tryptophan in the Kynurenine pathway.	Kynurenine	116-126	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-3
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).	Kynurenine	169-179	indoleamine 2,3-dioxygenase 1	Homo sapiens	31-35
35181297-1	2022	Kynurenine (Kyn) is involved in a variety of physiological/pathological reactions via activating aryl hydrocarbon receptor (Ahr).	Kynurenine	0-10	aryl hydrocarbon receptor	Homo sapiens	97-122
35247909-6	2022	The upregulation of IDO1 in cancer cells acted as an immunosuppressive feedback mechanism to limit the proliferation and function of cytotoxic CD8+ T lymphocytes through iron-dependent kynurenine production and subsequent TSPAN5-mediated kynurenine secretion.	Kynurenine	185-195	indoleamine 2,3-dioxygenase 1	Mus musculus	20-24
35247909-6	2022	The upregulation of IDO1 in cancer cells acted as an immunosuppressive feedback mechanism to limit the proliferation and function of cytotoxic CD8+ T lymphocytes through iron-dependent kynurenine production and subsequent TSPAN5-mediated kynurenine secretion.	Kynurenine	238-248	indoleamine 2,3-dioxygenase 1	Mus musculus	20-24
35247909-6	2022	The upregulation of IDO1 in cancer cells acted as an immunosuppressive feedback mechanism to limit the proliferation and function of cytotoxic CD8+ T lymphocytes through iron-dependent kynurenine production and subsequent TSPAN5-mediated kynurenine secretion.	Kynurenine	238-248	tetraspanin 5	Mus musculus	222-228
35626147-3	2022	Here, we demonstrated that NRF2 alters tryptophan metabolism through the kynurenine pathway that is associated with a tumor-promoting, immune suppressed microenvironment.	Kynurenine	73-83	NFE2 like bZIP transcription factor 2	Homo sapiens	27-31
35626147-4	2022	Specifically, proteomic profiles of 47 lung adenocarcinoma (LUAD) cell lines (11 KEAP1 mutant and 36 KEAP1 wild-type) revealed the tryptophan-kynurenine enzyme kynureninase (KYNU) as a top overexpressed protein associated with activated NRF2.	Kynurenine	142-152	kelch like ECH associated protein 1	Homo sapiens	81-86
35626147-4	2022	Specifically, proteomic profiles of 47 lung adenocarcinoma (LUAD) cell lines (11 KEAP1 mutant and 36 KEAP1 wild-type) revealed the tryptophan-kynurenine enzyme kynureninase (KYNU) as a top overexpressed protein associated with activated NRF2.	Kynurenine	142-152	kelch like ECH associated protein 1	Homo sapiens	101-106
35626147-4	2022	Specifically, proteomic profiles of 47 lung adenocarcinoma (LUAD) cell lines (11 KEAP1 mutant and 36 KEAP1 wild-type) revealed the tryptophan-kynurenine enzyme kynureninase (KYNU) as a top overexpressed protein associated with activated NRF2.	Kynurenine	142-152	kynureninase	Homo sapiens	160-172
35626147-4	2022	Specifically, proteomic profiles of 47 lung adenocarcinoma (LUAD) cell lines (11 KEAP1 mutant and 36 KEAP1 wild-type) revealed the tryptophan-kynurenine enzyme kynureninase (KYNU) as a top overexpressed protein associated with activated NRF2.	Kynurenine	142-152	kynureninase	Homo sapiens	174-178
35626147-4	2022	Specifically, proteomic profiles of 47 lung adenocarcinoma (LUAD) cell lines (11 KEAP1 mutant and 36 KEAP1 wild-type) revealed the tryptophan-kynurenine enzyme kynureninase (KYNU) as a top overexpressed protein associated with activated NRF2.	Kynurenine	142-152	NFE2 like bZIP transcription factor 2	Homo sapiens	237-241
35181297-1	2022	Kynurenine (Kyn) is involved in a variety of physiological/pathological reactions via activating aryl hydrocarbon receptor (Ahr).	Kynurenine	0-10	aryl hydrocarbon receptor	Homo sapiens	124-127
35181297-1	2022	Kynurenine (Kyn) is involved in a variety of physiological/pathological reactions via activating aryl hydrocarbon receptor (Ahr).	Kynurenine	12-15	aryl hydrocarbon receptor	Homo sapiens	97-122
35181297-1	2022	Kynurenine (Kyn) is involved in a variety of physiological/pathological reactions via activating aryl hydrocarbon receptor (Ahr).	Kynurenine	12-15	aryl hydrocarbon receptor	Homo sapiens	124-127
35603278-2	2022	Methods: The purpose of this exploratory study was to assess short-term PROs and serum kynurenine metabolites for associated neurotoxicity among patients treated in an anti-CD20, anti-CD19 (LV20.19) CAR T cell phase I clinical trial (NCT03019055).	Kynurenine	87-97	keratin 20	Homo sapiens	173-177
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.	Kynurenine	139-149	indoleamine 2,3-dioxygenase 1	Homo sapiens	61-65
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.	Kynurenine	139-149	tryptophan 2,3-dioxygenase	Homo sapiens	70-74
35603278-2	2022	Methods: The purpose of this exploratory study was to assess short-term PROs and serum kynurenine metabolites for associated neurotoxicity among patients treated in an anti-CD20, anti-CD19 (LV20.19) CAR T cell phase I clinical trial (NCT03019055).	Kynurenine	87-97	CD19 molecule	Homo sapiens	184-188
35603278-2	2022	Methods: The purpose of this exploratory study was to assess short-term PROs and serum kynurenine metabolites for associated neurotoxicity among patients treated in an anti-CD20, anti-CD19 (LV20.19) CAR T cell phase I clinical trial (NCT03019055).	Kynurenine	87-97	nuclear receptor subfamily 1 group I member 3	Homo sapiens	199-202
35603278-7	2022	Conclusions: Elevated levels of kynurenine pathway metabolites among CAR T cell recipients are associated with depressed mood and neurotoxicity.	Kynurenine	32-42	nuclear receptor subfamily 1 group I member 3	Homo sapiens	69-72
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.	Kynurenine	135-145	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-30
35563591-6	2022	As expected, a lower L-kynurenine/Trp (Kyn/Trp) ratio was found in the plasma and arteries of Apoe-/-Ido1-/- mice compared to controls.	Kynurenine	21-33	apolipoprotein E	Mus musculus	94-98
35563591-6	2022	As expected, a lower L-kynurenine/Trp (Kyn/Trp) ratio was found in the plasma and arteries of Apoe-/-Ido1-/- mice compared to controls.	Kynurenine	21-33	indoleamine 2,3-dioxygenase 1	Mus musculus	101-105
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.	Kynurenine	135-145	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.	Kynurenine	135-145	tryptophan 2,3-dioxygenase	Homo sapiens	42-69
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.	Kynurenine	135-145	tryptophan 2,3-dioxygenase	Homo sapiens	71-74
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.	Kynurenine	151-154	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.	Kynurenine	151-154	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.	Kynurenine	151-154	tryptophan 2,3-dioxygenase	Homo sapiens	42-69
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.	Kynurenine	151-154	tryptophan 2,3-dioxygenase	Homo sapiens	71-74
35481813-2	2022	Aryl hydrocarbon receptor (AHR), together with its endogenous ligand kynurenine is known to mediate free radical accumulation and neuronal excitotoxicity in central nervous systems.	Kynurenine	69-79	aryl hydrocarbon receptor	Homo sapiens	0-25
35563591-11	2022	Our data indicate that the overexpression of TDO2 is an important mechanism that helps in balancing the kynurenine pathway and inflammation in the liver, but not in the artery wall, which likely determined disease outcome in these two target tissues.	Kynurenine	104-114	tryptophan 2,3-dioxygenase	Homo sapiens	45-49
35552175-0	2022	Kynurenine-PARP-1 Link Mediated by MicroRNA 210 May Be Dysregulated in Pulmonary Hypertension.	Kynurenine	0-10	poly(ADP-ribose) polymerase 1	Homo sapiens	11-17
35552175-13	2022	CONCLUSIONS: We report a novel relationship between the kynurenine and poly-ADP- ribose polymerase-1 signaling pathways that could be mediated by miRNA-210.	Kynurenine	56-66	poly(ADP-ribose) polymerase 1	Homo sapiens	71-100
35032499-9	2022	IDO1, the rate limiting enzyme for kynurenine production, had increased intestinal expression at G15, which was associated with mild systemic and gut inflammation.	Kynurenine	35-45	indoleamine 2,3-dioxygenase 1	Mus musculus	0-4
35032499-10	2022	Pharmacologic and genetic inhibition of IDO1 inhibited kynurenine levels and reversed pregnancy-associated IR.	Kynurenine	55-65	indoleamine 2,3-dioxygenase 1	Mus musculus	40-44
35032499-12	2022	CONCLUSIONS: GM changes accompanying pregnancy shift IDO1-dependent tryptophan metabolism toward kynurenine production, intestinal inflammation and gestational IR, a; phenotype reversed by genetic deletion or inhibition of IDO1.	Kynurenine	97-107	indoleamine 2,3-dioxygenase 1	Mus musculus	53-57
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.	Kynurenine	25-35	indoleamine 2,3-dioxygenase 1	Homo sapiens	108-111
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.	Kynurenine	25-35	interferon gamma	Homo sapiens	145-153
34978092-1	2022	sKynurenine (KYN) is synthesized from an essential amino acid, tryptophan by tryptophan 2,3-dioxygenase or indoleamine 2,3-dioxygenase via N-formyl- KYN in vivo.	Kynurenine	0-11	tryptophan 2,3-dioxygenase	Homo sapiens	77-103
34978092-1	2022	sKynurenine (KYN) is synthesized from an essential amino acid, tryptophan by tryptophan 2,3-dioxygenase or indoleamine 2,3-dioxygenase via N-formyl- KYN in vivo.	Kynurenine	13-16	tryptophan 2,3-dioxygenase	Homo sapiens	77-103
35481813-2	2022	Aryl hydrocarbon receptor (AHR), together with its endogenous ligand kynurenine is known to mediate free radical accumulation and neuronal excitotoxicity in central nervous systems.	Kynurenine	69-79	aryl hydrocarbon receptor	Homo sapiens	27-30
35481813-8	2022	Finally, we reported exogenous kynurenine aggravated AHR activation and mediated brain damage above mentioned.	Kynurenine	31-41	aryl-hydrocarbon receptor	Mus musculus	53-56
35481813-9	2022	INNOVATION: We show for the first time Kynurenine/AHR mediate mitochondria death and free radical accumulation at least partially via RhoA/Bax signaling pathway.	Kynurenine	39-49	aryl-hydrocarbon receptor	Mus musculus	50-53
35481813-9	2022	INNOVATION: We show for the first time Kynurenine/AHR mediate mitochondria death and free radical accumulation at least partially via RhoA/Bax signaling pathway.	Kynurenine	39-49	ras homolog family member A	Homo sapiens	134-138
35481813-9	2022	INNOVATION: We show for the first time Kynurenine/AHR mediate mitochondria death and free radical accumulation at least partially via RhoA/Bax signaling pathway.	Kynurenine	39-49	BCL2 associated X, apoptosis regulator	Homo sapiens	139-142
35481813-11	2022	CONCLUSIONS: Kynurenine/AHR may serve as a potential therapeutic target to attenuate mitochondria-mediated oxidative stress and neuronal cells impairment in patients with ICH.	Kynurenine	13-23	aryl hydrocarbon receptor	Homo sapiens	24-27
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).	Kynurenine	183-193	cytochrome P450 family 1 subfamily B member 1	Homo sapiens	93-99
35571116-4	2022	In IDO1- or TDO2- overexpressing cell lines, STS decreased kynurenine (kyn) synthesis.	Kynurenine	59-69	indoleamine 2,3-dioxygenase 1	Mus musculus	3-7
35571116-4	2022	In IDO1- or TDO2- overexpressing cell lines, STS decreased kynurenine (kyn) synthesis.	Kynurenine	59-69	tryptophan 2,3-dioxygenase	Mus musculus	12-16
35571116-4	2022	In IDO1- or TDO2- overexpressing cell lines, STS decreased kynurenine (kyn) synthesis.	Kynurenine	71-74	indoleamine 2,3-dioxygenase 1	Mus musculus	3-7
35571116-4	2022	In IDO1- or TDO2- overexpressing cell lines, STS decreased kynurenine (kyn) synthesis.	Kynurenine	71-74	tryptophan 2,3-dioxygenase	Mus musculus	12-16
35440600-5	2022	Animal studies showed that KYN supplementation resulted in a marked elevation of absorptive surface of rat intestine and in enhanced expression of both, aryl hydrocarbon receptor and G protein-coupled receptor 35 in the intestinal tissue in rats.	Kynurenine	27-30	aryl hydrocarbon receptor	Rattus norvegicus	153-178
35440600-5	2022	Animal studies showed that KYN supplementation resulted in a marked elevation of absorptive surface of rat intestine and in enhanced expression of both, aryl hydrocarbon receptor and G protein-coupled receptor 35 in the intestinal tissue in rats.	Kynurenine	27-30	G protein-coupled receptor 35	Rattus norvegicus	183-212
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).	Kynurenine	183-193	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).	Kynurenine	183-193	indoleamine 2,3-dioxygenase 1	Homo sapiens	133-136
35355679-0	2022	Superior antitumor immunotherapy efficacy of kynureninase modified CAR-T cells through targeting kynurenine metabolism.	Kynurenine	97-107	kynureninase	Homo sapiens	45-57
35413710-0	2022	The Role of Kynurenines Produced by Indolamine-2,3-Dioxygenase 1 in Sepsis.	Kynurenine	12-23	indoleamine 2,3-dioxygenase 1	Homo sapiens	36-64
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.	Kynurenine	94-104	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.	Kynurenine	94-104	indoleamine 2,3-dioxygenase 1	Homo sapiens	53-57
35494242-6	2022	Functionally, tryptophan and its microbial product tryptamine increased T cell metabolism and mTOR activation, while kynurenine promoted interferon gamma production, all of which have been associated with lupus.	Kynurenine	117-127	interferon gamma	Mus musculus	137-153
35479493-7	2022	Results: Elevated serum kynurenine levels were associated with signs of neuroinflammation, specifically in the DPCC, left SM1 and right DLPFC, and signs of neurodegeneration, specifically in the left HPC, left MTC and left SM1, after adjusting for age, sex and fat percentage (fat%).	Kynurenine	24-34	SM1	Homo sapiens	122-125
35479493-7	2022	Results: Elevated serum kynurenine levels were associated with signs of neuroinflammation, specifically in the DPCC, left SM1 and right DLPFC, and signs of neurodegeneration, specifically in the left HPC, left MTC and left SM1, after adjusting for age, sex and fat percentage (fat%).	Kynurenine	24-34	SM1	Homo sapiens	223-226
35046097-4	2022	AML progression requires the presence of serotonin receptor-1b (HTR1B) in osteoblasts and is driven by AML-secreted kynurenine, which acts as an oncometabolite and HTR1B ligand.	Kynurenine	116-126	5-hydroxytryptamine receptor 1B	Homo sapiens	41-62
35046097-4	2022	AML progression requires the presence of serotonin receptor-1b (HTR1B) in osteoblasts and is driven by AML-secreted kynurenine, which acts as an oncometabolite and HTR1B ligand.	Kynurenine	116-126	5-hydroxytryptamine receptor 1B	Homo sapiens	64-69
35046097-4	2022	AML progression requires the presence of serotonin receptor-1b (HTR1B) in osteoblasts and is driven by AML-secreted kynurenine, which acts as an oncometabolite and HTR1B ligand.	Kynurenine	116-126	5-hydroxytryptamine receptor 1B	Homo sapiens	164-169
35046097-5	2022	AML cells utilize kynurenine to induce a pro-inflammatory state in osteoblasts which, through the acute-phase protein serum amyloid A (SAA), acts in a positive feedback-loop on leukemia cells by increasing expression of IDO1 -the rate-limiting enzyme for kynurenine synthesis-, thereby enabling AML progression.	Kynurenine	18-28	serum amyloid A1 cluster	Homo sapiens	118-133
35046097-5	2022	AML cells utilize kynurenine to induce a pro-inflammatory state in osteoblasts which, through the acute-phase protein serum amyloid A (SAA), acts in a positive feedback-loop on leukemia cells by increasing expression of IDO1 -the rate-limiting enzyme for kynurenine synthesis-, thereby enabling AML progression.	Kynurenine	18-28	serum amyloid A1 cluster	Homo sapiens	135-138
35046097-5	2022	AML cells utilize kynurenine to induce a pro-inflammatory state in osteoblasts which, through the acute-phase protein serum amyloid A (SAA), acts in a positive feedback-loop on leukemia cells by increasing expression of IDO1 -the rate-limiting enzyme for kynurenine synthesis-, thereby enabling AML progression.	Kynurenine	18-28	indoleamine 2,3-dioxygenase 1	Homo sapiens	220-224
35046097-5	2022	AML cells utilize kynurenine to induce a pro-inflammatory state in osteoblasts which, through the acute-phase protein serum amyloid A (SAA), acts in a positive feedback-loop on leukemia cells by increasing expression of IDO1 -the rate-limiting enzyme for kynurenine synthesis-, thereby enabling AML progression.	Kynurenine	255-265	serum amyloid A1 cluster	Homo sapiens	118-133
35046097-5	2022	AML cells utilize kynurenine to induce a pro-inflammatory state in osteoblasts which, through the acute-phase protein serum amyloid A (SAA), acts in a positive feedback-loop on leukemia cells by increasing expression of IDO1 -the rate-limiting enzyme for kynurenine synthesis-, thereby enabling AML progression.	Kynurenine	255-265	serum amyloid A1 cluster	Homo sapiens	135-138
35046097-5	2022	AML cells utilize kynurenine to induce a pro-inflammatory state in osteoblasts which, through the acute-phase protein serum amyloid A (SAA), acts in a positive feedback-loop on leukemia cells by increasing expression of IDO1 -the rate-limiting enzyme for kynurenine synthesis-, thereby enabling AML progression.	Kynurenine	255-265	indoleamine 2,3-dioxygenase 1	Homo sapiens	220-224
35046097-6	2022	This leukemia-osteoblast crosstalk, conferred by the kynurenine-HTR1B-SAA-IDO1 axis, could be exploited as a niche-focused therapeutic approach against AML, opening new avenues for cancer treatment.	Kynurenine	53-63	5-hydroxytryptamine receptor 1B	Homo sapiens	64-69
35046097-6	2022	This leukemia-osteoblast crosstalk, conferred by the kynurenine-HTR1B-SAA-IDO1 axis, could be exploited as a niche-focused therapeutic approach against AML, opening new avenues for cancer treatment.	Kynurenine	53-63	serum amyloid A1 cluster	Homo sapiens	70-73
35046097-6	2022	This leukemia-osteoblast crosstalk, conferred by the kynurenine-HTR1B-SAA-IDO1 axis, could be exploited as a niche-focused therapeutic approach against AML, opening new avenues for cancer treatment.	Kynurenine	53-63	indoleamine 2,3-dioxygenase 1	Homo sapiens	74-78
35353612-0	2022	Gastric Cancer Cell-Derived Kynurenines Hyperactive Regulatory T Cells to Promote Chemoresistance via the IL-10/STAT3/BCL2 Signaling Pathway.	Kynurenine	28-39	interleukin 10	Homo sapiens	106-111
35353612-0	2022	Gastric Cancer Cell-Derived Kynurenines Hyperactive Regulatory T Cells to Promote Chemoresistance via the IL-10/STAT3/BCL2 Signaling Pathway.	Kynurenine	28-39	signal transducer and activator of transcription 3	Homo sapiens	112-117
35353612-0	2022	Gastric Cancer Cell-Derived Kynurenines Hyperactive Regulatory T Cells to Promote Chemoresistance via the IL-10/STAT3/BCL2 Signaling Pathway.	Kynurenine	28-39	BCL2 apoptosis regulator	Homo sapiens	118-122
35051489-3	2022	This study was to investigate the hypothesis that BBR treats depressive-like behavior by shifting the balance of the kynurenine (KYN)/serotonin (5-HT) pathway toward the 5-HT pathway through downregulated indoleamine 2,3-dioxygenase 1 (IDO1), monoamine oxidase A (MAOA) and upregulated dopamine decarboxylase (DDC) in hippocampus.	Kynurenine	117-127	indoleamine 2,3-dioxygenase 1	Mus musculus	205-234
35051489-3	2022	This study was to investigate the hypothesis that BBR treats depressive-like behavior by shifting the balance of the kynurenine (KYN)/serotonin (5-HT) pathway toward the 5-HT pathway through downregulated indoleamine 2,3-dioxygenase 1 (IDO1), monoamine oxidase A (MAOA) and upregulated dopamine decarboxylase (DDC) in hippocampus.	Kynurenine	129-132	indoleamine 2,3-dioxygenase 1	Mus musculus	205-234
35355679-3	2022	We screened oncometabolites for the inhibition of glucose uptake in CD8 + T cells and found Kynurenine (Kyn) showed the strongest inhibiting effect on glucose uptake.	Kynurenine	92-102	CD8a molecule	Homo sapiens	68-71
35355679-3	2022	We screened oncometabolites for the inhibition of glucose uptake in CD8 + T cells and found Kynurenine (Kyn) showed the strongest inhibiting effect on glucose uptake.	Kynurenine	104-107	CD8a molecule	Homo sapiens	68-71
35371018-0	2022	Induction of IDO1 and Kynurenine by Serine Proteases Subtilisin, Prostate Specific Antigen, CD26 and HtrA: A New Form of Immunosuppression?	Kynurenine	22-32	kallikrein related peptidase 3	Homo sapiens	65-90
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.	Kynurenine	54-64	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.	Kynurenine	111-123	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.	Kynurenine	111-123	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.	Kynurenine	125-128	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.	Kynurenine	125-128	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.	Kynurenine	125-128	aryl hydrocarbon receptor	Homo sapiens	165-168
35371054-4	2022	Interferon (IFN)-gamma induces IDO1 expression through the Jak/STAT1 pathway and mediates Kyn production concomitantly with Trp consumption in CLL-conditioned media, while INCB018424 (ruxolitinib), a JAK1/2 inhibitor, impaired both effects.	Kynurenine	90-93	interferon gamma	Homo sapiens	0-22
35371018-0	2022	Induction of IDO1 and Kynurenine by Serine Proteases Subtilisin, Prostate Specific Antigen, CD26 and HtrA: A New Form of Immunosuppression?	Kynurenine	22-32	dipeptidyl peptidase 4	Homo sapiens	92-96
35371018-0	2022	Induction of IDO1 and Kynurenine by Serine Proteases Subtilisin, Prostate Specific Antigen, CD26 and HtrA: A New Form of Immunosuppression?	Kynurenine	22-32	HtrA serine peptidase 1	Homo sapiens	101-105
35371018-2	2022	Activation of the kynurenine pathway enzyme indoleamine-2,3-dioxygenase (IDO1) modulates cellular activity in the brain, tolerogenesis in the immune system and is a major checkpoint in cancer development.	Kynurenine	18-28	indoleamine 2,3-dioxygenase 1	Homo sapiens	73-77
35217532-7	2022	Each IFN has a unique metabolic signature, with IFNG being the most associated with activation of the kynurenine pathway.	Kynurenine	102-112	interferon gamma	Homo sapiens	48-52
35371018-3	2022	We now report that IDO1 mRNA and IDO1 protein expression (generating kynurenine) are induced in human monocyte-derived macrophages by several chymotryptic serine proteases with direct links to tumorigenesis, including Prostate Specific Antigen (PSA), CD26 (Dipeptidyl-peptidase-4, CD26/DPP-4), High Temperature Requirement protein-A (HtrA), and the bacterial virulence factor subtilisin.	Kynurenine	69-79	indoleamine 2,3-dioxygenase 1	Homo sapiens	19-23
35371018-3	2022	We now report that IDO1 mRNA and IDO1 protein expression (generating kynurenine) are induced in human monocyte-derived macrophages by several chymotryptic serine proteases with direct links to tumorigenesis, including Prostate Specific Antigen (PSA), CD26 (Dipeptidyl-peptidase-4, CD26/DPP-4), High Temperature Requirement protein-A (HtrA), and the bacterial virulence factor subtilisin.	Kynurenine	69-79	indoleamine 2,3-dioxygenase 1	Homo sapiens	33-37
35371018-3	2022	We now report that IDO1 mRNA and IDO1 protein expression (generating kynurenine) are induced in human monocyte-derived macrophages by several chymotryptic serine proteases with direct links to tumorigenesis, including Prostate Specific Antigen (PSA), CD26 (Dipeptidyl-peptidase-4, CD26/DPP-4), High Temperature Requirement protein-A (HtrA), and the bacterial virulence factor subtilisin.	Kynurenine	69-79	kallikrein related peptidase 3	Homo sapiens	218-243
35371018-3	2022	We now report that IDO1 mRNA and IDO1 protein expression (generating kynurenine) are induced in human monocyte-derived macrophages by several chymotryptic serine proteases with direct links to tumorigenesis, including Prostate Specific Antigen (PSA), CD26 (Dipeptidyl-peptidase-4, CD26/DPP-4), High Temperature Requirement protein-A (HtrA), and the bacterial virulence factor subtilisin.	Kynurenine	69-79	dipeptidyl peptidase 4	Homo sapiens	251-255
35371018-3	2022	We now report that IDO1 mRNA and IDO1 protein expression (generating kynurenine) are induced in human monocyte-derived macrophages by several chymotryptic serine proteases with direct links to tumorigenesis, including Prostate Specific Antigen (PSA), CD26 (Dipeptidyl-peptidase-4, CD26/DPP-4), High Temperature Requirement protein-A (HtrA), and the bacterial virulence factor subtilisin.	Kynurenine	69-79	dipeptidyl peptidase 4	Homo sapiens	257-279
35371018-3	2022	We now report that IDO1 mRNA and IDO1 protein expression (generating kynurenine) are induced in human monocyte-derived macrophages by several chymotryptic serine proteases with direct links to tumorigenesis, including Prostate Specific Antigen (PSA), CD26 (Dipeptidyl-peptidase-4, CD26/DPP-4), High Temperature Requirement protein-A (HtrA), and the bacterial virulence factor subtilisin.	Kynurenine	69-79	dipeptidyl peptidase 4	Homo sapiens	281-285
35371018-3	2022	We now report that IDO1 mRNA and IDO1 protein expression (generating kynurenine) are induced in human monocyte-derived macrophages by several chymotryptic serine proteases with direct links to tumorigenesis, including Prostate Specific Antigen (PSA), CD26 (Dipeptidyl-peptidase-4, CD26/DPP-4), High Temperature Requirement protein-A (HtrA), and the bacterial virulence factor subtilisin.	Kynurenine	69-79	dipeptidyl peptidase 4	Homo sapiens	286-291
35371018-3	2022	We now report that IDO1 mRNA and IDO1 protein expression (generating kynurenine) are induced in human monocyte-derived macrophages by several chymotryptic serine proteases with direct links to tumorigenesis, including Prostate Specific Antigen (PSA), CD26 (Dipeptidyl-peptidase-4, CD26/DPP-4), High Temperature Requirement protein-A (HtrA), and the bacterial virulence factor subtilisin.	Kynurenine	69-79	HtrA serine peptidase 1	Homo sapiens	294-332
35371018-3	2022	We now report that IDO1 mRNA and IDO1 protein expression (generating kynurenine) are induced in human monocyte-derived macrophages by several chymotryptic serine proteases with direct links to tumorigenesis, including Prostate Specific Antigen (PSA), CD26 (Dipeptidyl-peptidase-4, CD26/DPP-4), High Temperature Requirement protein-A (HtrA), and the bacterial virulence factor subtilisin.	Kynurenine	69-79	HtrA serine peptidase 1	Homo sapiens	334-338
35085834-2	2022	IDO1 enzyme catabolizes L-tryptophan (L-Trp) into kynurenine (KYN) thus stimulating the KYN pathway.	Kynurenine	50-60	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-4
35245456-0	2022	Kynurenine importation by SLC7A11 propagates anti-ferroptotic signaling.	Kynurenine	0-10	solute carrier family 7 member 11	Homo sapiens	26-33
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.	Kynurenine	43-53	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.	Kynurenine	55-58	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.	Kynurenine	62-65	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-4
34710259-3	2022	Here, we showed that KYN inhibited tyrosinase expression and melanin content in primary human melanocyte and keratinocyte co-cultures.	Kynurenine	21-24	tyrosinase	Homo sapiens	35-45
35120895-4	2022	It also reduced the expression of IDO1 and the production of kynurenine which is the product catalyzed by IDO1, while didn"t show obvious effect on the expression of major histocompatibility complex-I (MHC-I), a crucial molecule for antigen presentation.	Kynurenine	61-71	indoleamine 2,3-dioxygenase 1	Homo sapiens	106-110
35246476-9	2022	Furthermore, ZNF207 transcriptionally regulated indoleamine 2,3-dioxygenase 1 and elevated kynurenine levels, leading to the exhaustion of CD8+ T cells.	Kynurenine	91-101	zinc finger protein 207	Mus musculus	13-19
35063739-7	2022	The increased KYAT1 and AADAT mRNA indicates that depression is associated with increased activation of the kynurenic acid arm of the kynurenine pathway in the ACC, suggesting an astrocyte response in depression.	Kynurenine	134-144	kynurenine aminotransferase 1	Homo sapiens	14-19
35063739-7	2022	The increased KYAT1 and AADAT mRNA indicates that depression is associated with increased activation of the kynurenic acid arm of the kynurenine pathway in the ACC, suggesting an astrocyte response in depression.	Kynurenine	134-144	aminoadipate aminotransferase	Homo sapiens	24-29
35183714-1	2022	Indoleamine 2,3-dioxygenase 1 (IDO1) catalyzes the rate-limiting step in tryptophan catabolism along the kynurenine (Kyn) pathway and exerts immunosuppressive properties mainly via activation of transcription factor aryl hydrocarbon receptor (AhR) pathway.	Kynurenine	105-115	indoleamine 2,3-dioxygenase 1	Mus musculus	0-29
35150740-3	2022	We found that IDO1 was necessary and sufficient for production of kynurenine, a downstream tryptophan metabolite, in cancer cells.	Kynurenine	66-76	indoleamine 2,3-dioxygenase 1	Homo sapiens	14-18
35150740-6	2022	Furthermore, NKA inhibition by ouabain and digoxin resulted in increased intracellular Na+ levels and downregulation of IDO1 mRNA and protein levels, which was consistent with the reduction in kynurenine levels.	Kynurenine	193-203	tachykinin precursor 1	Homo sapiens	13-16
35150740-6	2022	Furthermore, NKA inhibition by ouabain and digoxin resulted in increased intracellular Na+ levels and downregulation of IDO1 mRNA and protein levels, which was consistent with the reduction in kynurenine levels.	Kynurenine	193-203	indoleamine 2,3-dioxygenase 1	Homo sapiens	120-124
35150740-8	2022	However, ATP1A1 knockdown significantly enhanced the effect of cardiac glycosides on IDO1 expression and kynurenine production.	Kynurenine	105-115	ATPase Na+/K+ transporting subunit alpha 1	Homo sapiens	9-15
35183714-1	2022	Indoleamine 2,3-dioxygenase 1 (IDO1) catalyzes the rate-limiting step in tryptophan catabolism along the kynurenine (Kyn) pathway and exerts immunosuppressive properties mainly via activation of transcription factor aryl hydrocarbon receptor (AhR) pathway.	Kynurenine	105-115	indoleamine 2,3-dioxygenase 1	Mus musculus	31-35
35183714-1	2022	Indoleamine 2,3-dioxygenase 1 (IDO1) catalyzes the rate-limiting step in tryptophan catabolism along the kynurenine (Kyn) pathway and exerts immunosuppressive properties mainly via activation of transcription factor aryl hydrocarbon receptor (AhR) pathway.	Kynurenine	105-115	aryl-hydrocarbon receptor	Mus musculus	216-241
35183714-1	2022	Indoleamine 2,3-dioxygenase 1 (IDO1) catalyzes the rate-limiting step in tryptophan catabolism along the kynurenine (Kyn) pathway and exerts immunosuppressive properties mainly via activation of transcription factor aryl hydrocarbon receptor (AhR) pathway.	Kynurenine	105-115	aryl-hydrocarbon receptor	Mus musculus	243-246
35183714-1	2022	Indoleamine 2,3-dioxygenase 1 (IDO1) catalyzes the rate-limiting step in tryptophan catabolism along the kynurenine (Kyn) pathway and exerts immunosuppressive properties mainly via activation of transcription factor aryl hydrocarbon receptor (AhR) pathway.	Kynurenine	117-120	indoleamine 2,3-dioxygenase 1	Mus musculus	0-29
35183714-1	2022	Indoleamine 2,3-dioxygenase 1 (IDO1) catalyzes the rate-limiting step in tryptophan catabolism along the kynurenine (Kyn) pathway and exerts immunosuppressive properties mainly via activation of transcription factor aryl hydrocarbon receptor (AhR) pathway.	Kynurenine	117-120	indoleamine 2,3-dioxygenase 1	Mus musculus	31-35
35183714-1	2022	Indoleamine 2,3-dioxygenase 1 (IDO1) catalyzes the rate-limiting step in tryptophan catabolism along the kynurenine (Kyn) pathway and exerts immunosuppressive properties mainly via activation of transcription factor aryl hydrocarbon receptor (AhR) pathway.	Kynurenine	117-120	aryl-hydrocarbon receptor	Mus musculus	216-241
35183714-1	2022	Indoleamine 2,3-dioxygenase 1 (IDO1) catalyzes the rate-limiting step in tryptophan catabolism along the kynurenine (Kyn) pathway and exerts immunosuppressive properties mainly via activation of transcription factor aryl hydrocarbon receptor (AhR) pathway.	Kynurenine	117-120	aryl-hydrocarbon receptor	Mus musculus	243-246
35064560-3	2022	Leiomyomas expressing mutated mediator complex subunit 12 (mut-MED12) were reported to contain significantly decreased tryptophan levels; the underlying mechanism and the role of the tryptophan metabolism-kynurenine pathway in leiomyoma tumorigenesis, however, remain unknown.	Kynurenine	205-215	mediator complex subunit 12	Homo sapiens	30-57
35064560-3	2022	Leiomyomas expressing mutated mediator complex subunit 12 (mut-MED12) were reported to contain significantly decreased tryptophan levels; the underlying mechanism and the role of the tryptophan metabolism-kynurenine pathway in leiomyoma tumorigenesis, however, remain unknown.	Kynurenine	205-215	mediator complex subunit 12	Homo sapiens	63-68
35064560-5	2022	Among these, the tissue mRNA levels of tryptophan 2,3-dioxygenase (TDO2), the rate limiting enzyme of tryptophan metabolism through the kynurenine pathway, was 36-fold higher in mut-MED12 compared to adjacent myometrium (P < 0.0001), and 14-fold higher compared to wild type (wt)-MED12 leiomyoma (P < 0.05).	Kynurenine	136-146	tryptophan 2,3-dioxygenase	Homo sapiens	39-65
35064560-5	2022	Among these, the tissue mRNA levels of tryptophan 2,3-dioxygenase (TDO2), the rate limiting enzyme of tryptophan metabolism through the kynurenine pathway, was 36-fold higher in mut-MED12 compared to adjacent myometrium (P < 0.0001), and 14-fold higher compared to wild type (wt)-MED12 leiomyoma (P < 0.05).	Kynurenine	136-146	tryptophan 2,3-dioxygenase	Homo sapiens	67-71
35064560-5	2022	Among these, the tissue mRNA levels of tryptophan 2,3-dioxygenase (TDO2), the rate limiting enzyme of tryptophan metabolism through the kynurenine pathway, was 36-fold higher in mut-MED12 compared to adjacent myometrium (P < 0.0001), and 14-fold higher compared to wild type (wt)-MED12 leiomyoma (P < 0.05).	Kynurenine	136-146	mediator complex subunit 12	Homo sapiens	182-187
35250276-1	2022	Indoleamine-2,3-dioxygenase (IDO) degrades the essential amino acid tryptophan resulting in tryptophan depletion and the accumulation of catabolites such as kynurenine.	Kynurenine	157-167	indoleamine 2,3-dioxygenase 1	Mus musculus	0-27
35250276-1	2022	Indoleamine-2,3-dioxygenase (IDO) degrades the essential amino acid tryptophan resulting in tryptophan depletion and the accumulation of catabolites such as kynurenine.	Kynurenine	157-167	indoleamine 2,3-dioxygenase 1	Mus musculus	29-32
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.	Kynurenine	202-214	indoleamine 2,3-dioxygenase 1	Homo sapiens	30-34
35235888-0	2022	Zi Shen Wan Fang regulates kynurenine metabolism to alleviate diabetes-associated cognitive impairment via activating the skeletal muscle PGC1alpha-PPARalpha signaling.	Kynurenine	27-37	peroxisome proliferative activated receptor, gamma, coactivator 1 alpha	Mus musculus	138-147
35235888-0	2022	Zi Shen Wan Fang regulates kynurenine metabolism to alleviate diabetes-associated cognitive impairment via activating the skeletal muscle PGC1alpha-PPARalpha signaling.	Kynurenine	27-37	peroxisome proliferator activated receptor alpha	Mus musculus	148-157
35051612-8	2022	By uncovering the cellular processes that allocate heme to IDO1 and TDO, our study provides new insight on how their activities and l-kynurenine production may be controlled in health and disease.	Kynurenine	132-144	tryptophan 2,3-dioxygenase	Homo sapiens	68-71
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.	Kynurenine	202-214	tryptophan 2,3-dioxygenase	Homo sapiens	68-71
35187162-1	2022	Background: Indoleamine 2,3-dioxygenase 1 (IDO1) catalyzes the first step of tryptophan catabolism in the kynurenine (Kyn) pathway.	Kynurenine	106-116	indoleamine 2,3-dioxygenase 1	Homo sapiens	12-41
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).	Kynurenine	118-121	indoleamine 2,3-dioxygenase 1	Homo sapiens	39-44
35203299-5	2022	The accumulation of Kyn and the depletion of Trp arrest T cell growth and induce apoptosis, setting up an immune-tolerant condition, whereas AhR and interferon type I (IFN-I) build a mutual inhibitory loop that also involves NF-kB and limits the innate response.	Kynurenine	20-23	aryl hydrocarbon receptor	Homo sapiens	141-144
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).	Kynurenine	106-116	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).	Kynurenine	106-116	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).	Kynurenine	118-121	indoleamine 2,3-dioxygenase 1	Homo sapiens	11-37
35187162-1	2022	Background: Indoleamine 2,3-dioxygenase 1 (IDO1) catalyzes the first step of tryptophan catabolism in the kynurenine (Kyn) pathway.	Kynurenine	106-116	indoleamine 2,3-dioxygenase 1	Homo sapiens	43-47
35187162-1	2022	Background: Indoleamine 2,3-dioxygenase 1 (IDO1) catalyzes the first step of tryptophan catabolism in the kynurenine (Kyn) pathway.	Kynurenine	118-121	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.	Kynurenine	118-121	indoleamine 2,3-dioxygenase 1	Homo sapiens	43-47
35204197-1	2022	Kynurenine 3-monooxygenase (KMO), a key player in the kynurenine pathway (KP) of tryptophan degradation, regulates the synthesis of the neuroactive metabolites 3-hydroxykynurenine (3-HK) and kynurenic acid (KYNA).	Kynurenine	54-64	kynurenine 3-monooxygenase (kynurenine 3-hydroxylase)	Mus musculus	0-26
35204197-1	2022	Kynurenine 3-monooxygenase (KMO), a key player in the kynurenine pathway (KP) of tryptophan degradation, regulates the synthesis of the neuroactive metabolites 3-hydroxykynurenine (3-HK) and kynurenic acid (KYNA).	Kynurenine	54-64	kynurenine 3-monooxygenase (kynurenine 3-hydroxylase)	Mus musculus	28-31
35184386-0	2022	Kynurenine catabolic enzyme KMO regulates HCC growth.	Kynurenine	0-10	kynurenine 3-monooxygenase	Homo sapiens	28-31
35140473-1	2022	Background: This study aimed to assess the importance of selected kynurenines measured in peritoneal fluid, lavage washings, and blood serum in patients with advanced gastric cancer (GC) based on the clinical and pathological staging of TNM for a more precise evaluation of the stage of the disease.	Kynurenine	66-77	teneurin transmembrane protein 1	Homo sapiens	237-240
35186998-8	2022	In addition, we found that high levels of Gd-IgA1, IL-22, and TNF-alpha were associated with the activity of the tryptophan-kynurenine metabolic pathway, as well as lower levels of 3-indolepropionic acid.	Kynurenine	124-134	interleukin 22	Homo sapiens	51-56
35186998-8	2022	In addition, we found that high levels of Gd-IgA1, IL-22, and TNF-alpha were associated with the activity of the tryptophan-kynurenine metabolic pathway, as well as lower levels of 3-indolepropionic acid.	Kynurenine	124-134	tumor necrosis factor	Homo sapiens	62-71
35056756-1	2022	TDO2 is a key enzyme in the kynurenine metabolic pathway, which is the most important pathway of tryptophan metabolism.	Kynurenine	28-38	tryptophan 2,3-dioxygenase	Homo sapiens	0-4
35090836-4	2022	To confirm a role of kynurenine metabolism pathway in spasms protection, indoleamine 2,3-dioxygenase 1 was pharmacologically inhibited and comprehensive metabolomics was applied.	Kynurenine	21-31	indoleamine 2,3-dioxygenase 1	Homo sapiens	73-102
34847078-4	2022	Anakinra promoted H2O2-driven autophagy through a xenobiotic sensing pathway involving the aryl hydrocarbon receptor that, activated through the indoleamine 2,3-dioxygenase 1-kynurenine pathway, transcriptionally activates NADPH Oxidase 4 independent of the IL-1R1.	Kynurenine	175-185	aryl hydrocarbon receptor	Homo sapiens	91-116
34847078-4	2022	Anakinra promoted H2O2-driven autophagy through a xenobiotic sensing pathway involving the aryl hydrocarbon receptor that, activated through the indoleamine 2,3-dioxygenase 1-kynurenine pathway, transcriptionally activates NADPH Oxidase 4 independent of the IL-1R1.	Kynurenine	175-185	indoleamine 2,3-dioxygenase 1	Homo sapiens	145-174
34847078-4	2022	Anakinra promoted H2O2-driven autophagy through a xenobiotic sensing pathway involving the aryl hydrocarbon receptor that, activated through the indoleamine 2,3-dioxygenase 1-kynurenine pathway, transcriptionally activates NADPH Oxidase 4 independent of the IL-1R1.	Kynurenine	175-185	interleukin 1 receptor type 1	Homo sapiens	258-264
35087467-2	2021	Previous studies have suggested a potential role of the tryptophan-serotonin (5-HT)-kynurenine (TSK) axis in ischemic stroke.	Kynurenine	84-94	tsukushi, small leucine rich proteoglycan	Homo sapiens	96-99
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).	Kynurenine	160-170	indoleamine 2,3-dioxygenase 1	Homo sapiens	114-117
35057467-6	2022	IDO activity and its product kynurenine correlated with BMI z-score and body fat mass, whereas concentrations of serotonin, the alternative tryptophan metabolite, negatively correlated with these measures of adiposity.	Kynurenine	29-39	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-3
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.	Kynurenine	182-192	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.	Kynurenine	182-192	indoleamine 2,3-dioxygenase 1	Homo sapiens	63-67
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.	Kynurenine	182-192	indoleamine 2,3-dioxygenase 2	Homo sapiens	70-74
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.	Kynurenine	182-192	tryptophan 2,3-dioxygenase	Homo sapiens	79-105
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.	Kynurenine	182-192	tryptophan 2,3-dioxygenase	Homo sapiens	107-111
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.	Kynurenine	182-192	aryl hydrocarbon receptor	Homo sapiens	266-291
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.	Kynurenine	182-192	aryl hydrocarbon receptor	Homo sapiens	293-296
2503544-4	1989	Cell lines most sensitive to IFN-gamma (inhibited by 10-30 U/ml IFN-gamma in 3 d) were stimulated by IFN-gamma to oxidize tryptophan in media to kynurenine and completely eliminated tryptophan from the culture media after 48-72 h. Addition of L-tryptophan, but not other aromatic amino acids, other essential amino acids, or D-tryptophan, prevented inhibition of cell growth by IFN-gamma.	Kynurenine	145-155	interferon gamma	Homo sapiens	29-38
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.	Kynurenine	139-149	interferon gamma	Homo sapiens	0-9
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.	Kynurenine	139-149	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.	Kynurenine	139-149	indoleamine 2,3-dioxygenase 1	Homo sapiens	62-65
35396024-5	2022	Elevated proinflammatory cytokines (specifically, interleukin-6) in CSF imply the role of neuroinflammation resulting in activation of the tryptophan-kynurenine pathway.	Kynurenine	150-160	interleukin 6	Homo sapiens	50-63
2503544-4	1989	Cell lines most sensitive to IFN-gamma (inhibited by 10-30 U/ml IFN-gamma in 3 d) were stimulated by IFN-gamma to oxidize tryptophan in media to kynurenine and completely eliminated tryptophan from the culture media after 48-72 h. Addition of L-tryptophan, but not other aromatic amino acids, other essential amino acids, or D-tryptophan, prevented inhibition of cell growth by IFN-gamma.	Kynurenine	145-155	interferon gamma	Homo sapiens	64-73
2503544-4	1989	Cell lines most sensitive to IFN-gamma (inhibited by 10-30 U/ml IFN-gamma in 3 d) were stimulated by IFN-gamma to oxidize tryptophan in media to kynurenine and completely eliminated tryptophan from the culture media after 48-72 h. Addition of L-tryptophan, but not other aromatic amino acids, other essential amino acids, or D-tryptophan, prevented inhibition of cell growth by IFN-gamma.	Kynurenine	145-155	interferon gamma	Homo sapiens	64-73
34752422-3	2022	Here, we show that the dietary tryptophan-derived uremic solute including indoxyl sulfate (IS) and Kynurenine (Kyn), at concentrations corresponding to CKD patients suppressed beta-catenin in several cell-types including microvascular endothelial cells (EC), inhibiting Wnt activity and proangiogenic Wnt targets in ECs.	Kynurenine	99-109	catenin beta 1	Homo sapiens	176-188
34752422-3	2022	Here, we show that the dietary tryptophan-derived uremic solute including indoxyl sulfate (IS) and Kynurenine (Kyn), at concentrations corresponding to CKD patients suppressed beta-catenin in several cell-types including microvascular endothelial cells (EC), inhibiting Wnt activity and proangiogenic Wnt targets in ECs.	Kynurenine	111-114	catenin beta 1	Homo sapiens	176-188
2503544-4	1989	Cell lines most sensitive to IFN-gamma (inhibited by 10-30 U/ml IFN-gamma in 3 d) were stimulated by IFN-gamma to oxidize tryptophan in media to kynurenine and completely eliminated tryptophan from the culture media after 48-72 h. Addition of L-tryptophan, but not other aromatic amino acids, other essential amino acids, or D-tryptophan, prevented inhibition of cell growth by IFN-gamma.	Kynurenine	145-155	interferon gamma	Homo sapiens	64-73
2472288-1	1989	Indoleamine 2,3-dioxygenase (IDO) is an interferon (IFN)-induced protein that initiates the metabolism of tryptophan along the kynurenine pathway.	Kynurenine	127-137	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.	Kynurenine	127-137	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.	Kynurenine	127-137	interferon alpha 1	Homo sapiens	52-55
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.	Kynurenine	29-39	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.	Kynurenine	29-39	indoleamine 2,3-dioxygenase 1	Homo sapiens	83-86
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.	Kynurenine	29-39	interferon beta 1	Homo sapiens	205-241
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.	Kynurenine	29-39	interferon gamma	Homo sapiens	293-302
3189792-2	1988	I have developed assays for serum kynurenine and hepatic tryptophan dioxygenase (TDO) activity based on the determination of kynurenine (KYN) by isocratic, reverse phase HPLC with spectrophotometric detection at 365 nm.	Kynurenine	125-135	tryptophan 2,3-dioxygenase	Homo sapiens	81-84
3189792-2	1988	I have developed assays for serum kynurenine and hepatic tryptophan dioxygenase (TDO) activity based on the determination of kynurenine (KYN) by isocratic, reverse phase HPLC with spectrophotometric detection at 365 nm.	Kynurenine	137-140	tryptophan 2,3-dioxygenase	Homo sapiens	81-84
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).	Kynurenine	29-39	indoleamine 2,3-dioxygenase 1	Homo sapiens	54-81
3279850-4	1988	Kynurenine in the urines (which reflects tryptophan oxygenase activity) was measured for a period of 6 hr following the load and showed a significantly enhanced activity of the enzyme shortly after cessation of drinking.	Kynurenine	0-10	tryptophan 2,3-dioxygenase	Homo sapiens	41-61
3227109-2	1988	Irradiation of lysozyme and tryptophan in aerated solution results in the temperature and solvent dependent loss of tryptophan absorption and fluorescence, and the appearance of fluorescent "daughter products," primarily N-formyl-kynurenine and kynurenine.	Kynurenine	230-240	lysozyme	Homo sapiens	15-23
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).	Kynurenine	29-39	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).	Kynurenine	29-39	interferon gamma	Homo sapiens	158-174
3093859-8	1986	When cultures treated with IFN-gamma for 24 h are incubated with medium that contains [3H]tryptophan, the radioactive amino acid is converted to N-formylkynurenine and kynurenine as rapidly as it enters the cell.	Kynurenine	153-163	interferon gamma	Homo sapiens	27-36
2827682-0	1987	Photoinduced electron transfer reaction from N-formyl-L-kynurenine and L-kynurenine to cytochrome C.	Kynurenine	54-66	cytochrome c, somatic	Homo sapiens	87-99
2827682-1	1987	The reduction of cytochrome c was found in the presence of N-formyl-L-kynurenine (NFK) and L-kynurenine (KN) during irradiation, suggesting electron transfer to cytochrome c.	Kynurenine	68-80	cytochrome c, somatic	Homo sapiens	17-29
2827682-1	1987	The reduction of cytochrome c was found in the presence of N-formyl-L-kynurenine (NFK) and L-kynurenine (KN) during irradiation, suggesting electron transfer to cytochrome c.	Kynurenine	68-80	cytochrome c, somatic	Homo sapiens	161-173
6259288-1	1981	Kynurenine-3-hydroxylase, an enzyme that is part of the degradative pathway for tryptophan, was present in the cerebral cortex of neonatal rats and exhibited a Km for L-kynurenine close to that of the liver enzyme.	Kynurenine	167-179	kynurenine 3-monooxygenase	Rattus norvegicus	0-24
2427623-1	1986	We have previously observed that gamma-interferon (IFN-gamma) inhibited the growth of the intracellular protozoan parasite Toxoplasma gondii in cultured human fibroblasts and that this inhibition was related to the disappearance of tryptophan from the medium with the concomitant appearance of kynurenine and N-formylkynurenine.	Kynurenine	294-304	interferon gamma	Homo sapiens	51-60
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.	Kynurenine	300-310	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.	Kynurenine	300-310	interferon gamma	Homo sapiens	137-146
3087883-5	1986	Extracts prepared from IFN-gamma-treated human fibroblasts exhibited indoleamine 2,3-dioxygenase activity, converting tryptophan into products that cochromatographed with N-formylkynurenine and kynurenine; however, extracts prepared from untreated human fibroblasts, untreated L929 cells, recombinant IFN-gamma-treated L929 cells, and mouse lymphokine-treated L929 cells did not degrade tryptophan.	Kynurenine	179-189	interferon gamma	Homo sapiens	23-32
3912651-3	1985	We propose a mechanism by which kynurenines act to reduce the concentration of active insulin in plasma and thus give rise to a diabetic state.	Kynurenine	32-43	insulin	Homo sapiens	86-93
4026305-6	1985	Inhibition of tryptophan 2,3-dioxygenase was seen in pyridoxine deficiency, probably because of the buildup of the kynurenine metabolites.	Kynurenine	115-125	tryptophan 2,3-dioxygenase	Rattus norvegicus	14-40
6811571-2	1982	Kyn 59-RNase T1, fully active for the hydrolysis of GpA and GpC, emitted a 35-fold-enhanced fluorescence of kynurenine relative to acetylnurenine amide with an emission maximum at 455 nm upon excitation at 380 nm.	Kynurenine	108-118	glycophorin C (Gerbich blood group)	Homo sapiens	60-63
13964469-0	1963	Interference by reactions of kynurenine metabolism in the estimation of tryptophan pyrrolase in rat-liver homogenate.	Kynurenine	29-39	tryptophan 2,3-dioxygenase	Rattus norvegicus	72-92
5136463-2	1971	In agreement with previous findings on whole brain, the intraperitoneal injection of hydrocortisone, DL-alpha-methyltryptophan or L-kynurenine decreased the concentrations of 5-hydroxytryptamine (5-HT) and 5-hydroxy-indoleacetic acid (5-HIAA) in different regions of the rat brain.2.	Kynurenine	130-142	POU class 3 homeobox 2	Rattus norvegicus	275-282
5821431-0	1969	[The effect of tryptophan, serotonin, kynurenine, corticosteroids and peroxidases on the activity of tryptophan pyrrolase, the decarboxylase of 5-OH tryptophan and liver catalase in rats].	Kynurenine	38-48	tryptophan 2,3-dioxygenase	Rattus norvegicus	101-121
4285746-2	1965	Action exercised by ACTH and pyridoxin on urinary elimination of kynurenine derivatives].	Kynurenine	65-75	proopiomelanocortin	Homo sapiens	20-24
7367814-1	1980	The kynurenine load test was introduced to distinguish, in vivo, between abnormal tryptophan metabolism caused by induction of tryptophan oxygenase or by impaired kynureninase function.	Kynurenine	4-14	tryptophan 2,3-dioxygenase	Homo sapiens	127-147
5903340-0	1966	Tryptophan pyrrolase induced in human liver by hydrocortisone: effect on excretion of kynurenine.	Kynurenine	86-96	tryptophan 2,3-dioxygenase	Homo sapiens	0-20
5903340-2	1966	Correlation of the higher levels of the enzyme with the amounts of urinary kynurenine suggests that the tryptophan pyrrolase level, which is regulated by adrenocortical hormones, may be the important variable in the increased excretion of tryptophan metabolites that accompanies various diseases.	Kynurenine	75-85	tryptophan 2,3-dioxygenase	Homo sapiens	104-124
33846800-1	2021	Tryptophan 2,3-dioxygenase (TDO2) is a key rate-limiting enzyme in the kynurenine pathway and promotes tumor growth and escape from immune surveillance in different types of cancer.	Kynurenine	71-81	tryptophan 2,3-dioxygenase	Homo sapiens	28-32
33945927-2	2021	The serotonin system is mainly modulated by the serotonin transporter (SERT) which regulates serotonin uptake and the metabolism of its precursor, tryptophan and following kynurenine pathway.	Kynurenine	172-182	solute carrier family 6 member 4	Homo sapiens	48-69
33945927-2	2021	The serotonin system is mainly modulated by the serotonin transporter (SERT) which regulates serotonin uptake and the metabolism of its precursor, tryptophan and following kynurenine pathway.	Kynurenine	172-182	solute carrier family 6 member 4	Homo sapiens	71-75
33945927-8	2021	A negative correlation between the midbrain SERT availability and kynurenine concentration in HC was found.	Kynurenine	66-76	solute carrier family 6 member 4	Homo sapiens	44-48
33945927-9	2021	For the subgroup of HC with high kynurenine/tryptophan ratio, the SERT availability was positively associated with the kynurenine/tryptophan ratio and negatively correlated with tryptophan or kynurenine concentration.	Kynurenine	33-43	solute carrier family 6 member 4	Homo sapiens	66-70
33945927-9	2021	For the subgroup of HC with high kynurenine/tryptophan ratio, the SERT availability was positively associated with the kynurenine/tryptophan ratio and negatively correlated with tryptophan or kynurenine concentration.	Kynurenine	119-129	solute carrier family 6 member 4	Homo sapiens	66-70
33945927-9	2021	For the subgroup of HC with high kynurenine/tryptophan ratio, the SERT availability was positively associated with the kynurenine/tryptophan ratio and negatively correlated with tryptophan or kynurenine concentration.	Kynurenine	119-129	solute carrier family 6 member 4	Homo sapiens	66-70
33846800-1	2021	Tryptophan 2,3-dioxygenase (TDO2) is a key rate-limiting enzyme in the kynurenine pathway and promotes tumor growth and escape from immune surveillance in different types of cancer.	Kynurenine	71-81	tryptophan 2,3-dioxygenase	Homo sapiens	0-26
13784119-0	1960	Rapid spectrophotometric assays for snake venom L-amino acid oxidase based on the oxidation of L-kynurenine or 3,4-dehydro-L-proline.	Kynurenine	95-107	interleukin 4 induced 1	Homo sapiens	48-68
33607168-2	2021	Kynurenine 3-monooxygenase (KMO) is a pivotal enzyme in the metabolism of KYN to 3-hydroxykynurenine.	Kynurenine	74-77	kynurenine 3-monooxygenase (kynurenine 3-hydroxylase)	Mus musculus	0-26
33250293-7	2021	These findings show that the secretion of metabolites belonging to the kynurenine pathway into milk is mediated by ABCG2.	Kynurenine	71-81	ATP binding cassette subfamily G member 2	Bos taurus	115-120
33960391-10	2021	In addition, WT meMSCs stimulated with IL-17A and IFN-gamma increased IDO expression and secretion of kynurenines in vitro, indicating a negative feedback loop.	Kynurenine	102-113	interleukin 17A	Mus musculus	39-45
33960391-10	2021	In addition, WT meMSCs stimulated with IL-17A and IFN-gamma increased IDO expression and secretion of kynurenines in vitro, indicating a negative feedback loop.	Kynurenine	102-113	interferon gamma	Mus musculus	50-59
33243840-4	2021	Using a murine model of influenza infection to further these findings illustrated that there was decreased production of kynurenine in aged lung in an indoleamine-pyrrole 2,3-dioxygenase (IDO1)-dependent manner that was associated with increased inflammatory and diminished regulatory responses.	Kynurenine	121-131	indoleamine 2,3-dioxygenase 1	Mus musculus	151-186
33243840-4	2021	Using a murine model of influenza infection to further these findings illustrated that there was decreased production of kynurenine in aged lung in an indoleamine-pyrrole 2,3-dioxygenase (IDO1)-dependent manner that was associated with increased inflammatory and diminished regulatory responses.	Kynurenine	121-131	indoleamine 2,3-dioxygenase 1	Mus musculus	188-192
33907570-5	2021	In addition, the metabolism of tumor cells promotes tumor growth, particularly in tryptophan synthesis, where some metabolites, such as kynurenine, can activate the AhR pathway, triggering cell proliferation in astrocytomas, medulloblastomas and glioblastomas.	Kynurenine	136-146	aryl hydrocarbon receptor	Homo sapiens	165-168
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.	Kynurenine	111-121	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.	Kynurenine	111-121	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.	Kynurenine	111-121	tryptophan 2,3-dioxygenase	Homo sapiens	72-76
34054556-8	2021	Expression of indoleamine 2,3-dioxygenase 2 (IDO2) and kynurenine 3-monooxygenase (KMO) was increased by poly (I:C) whereas kynurenine aminotransferase II and its metabolite kynurenic acid were not altered.	Kynurenine	55-65	kynurenine 3-monooxygenase (kynurenine 3-hydroxylase)	Mus musculus	83-86
33607168-2	2021	Kynurenine 3-monooxygenase (KMO) is a pivotal enzyme in the metabolism of KYN to 3-hydroxykynurenine.	Kynurenine	74-77	kynurenine 3-monooxygenase (kynurenine 3-hydroxylase)	Mus musculus	28-31
33609532-7	2021	Indoleamine 2,3-dioxygenase (IDO) activity was determined by kynurenine assay and IDO mRNA by RT-PCR.	Kynurenine	61-71	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-27
33550042-2	2021	Indoleamine 2,3-dioxygenase 2 (IDO2) is one of the initial and rate-limiting enzymes of the kynurenine pathway of tryptophan catabolism.	Kynurenine	92-102	indoleamine 2,3-dioxygenase 2	Homo sapiens	0-29
33550042-2	2021	Indoleamine 2,3-dioxygenase 2 (IDO2) is one of the initial and rate-limiting enzymes of the kynurenine pathway of tryptophan catabolism.	Kynurenine	92-102	indoleamine 2,3-dioxygenase 2	Homo sapiens	31-35
33609532-7	2021	Indoleamine 2,3-dioxygenase (IDO) activity was determined by kynurenine assay and IDO mRNA by RT-PCR.	Kynurenine	61-71	indoleamine 2,3-dioxygenase 1	Homo sapiens	29-32
33212094-9	2021	This review summarizes recent advances on IDO and TDO as potential drug targets, and provides the key features and perspectives for further research and development of potent kynurenine pathway inhibitors.	Kynurenine	175-185	indoleamine 2,3-dioxygenase 1	Homo sapiens	42-45
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.	Kynurenine	149-159	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.	Kynurenine	149-159	indoleamine 2,3-dioxygenase 1	Homo sapiens	31-35
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.	Kynurenine	91-101	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.	Kynurenine	103-106	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.	Kynurenine	13-16	indoleamine 2,3-dioxygenase 1	Homo sapiens	53-56
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.	Kynurenine	97-100	indoleamine 2,3-dioxygenase 1	Homo sapiens	120-123
33875612-2	2021	Indoleamine 2,3 dioxygenase (IDO) catabolizes tryptophan (T) to kynurenine (K), regulating immune activity, and IDO activity increases with age.	Kynurenine	64-74	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-27
33922995-1	2021	BACKGROUND: Immune modulatory factors like indoleamine 2,3-dioxygenase 1 (IDO1) generating kynurenine (Kyn) and receptor for advanced glycation end-products (RAGE) contribute to endometrial and cancer microenvironment.	Kynurenine	91-101	indoleamine 2,3-dioxygenase 1	Homo sapiens	43-72
33922995-1	2021	BACKGROUND: Immune modulatory factors like indoleamine 2,3-dioxygenase 1 (IDO1) generating kynurenine (Kyn) and receptor for advanced glycation end-products (RAGE) contribute to endometrial and cancer microenvironment.	Kynurenine	91-101	indoleamine 2,3-dioxygenase 1	Homo sapiens	74-78
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.	Kynurenine	78-88	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.	Kynurenine	78-88	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.	Kynurenine	90-93	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.	Kynurenine	90-93	indoleamine 2,3-dioxygenase 1	Homo sapiens	42-46
33883013-2	2021	Functionally, IDO1 has played a pivotal role in cancer immune escape via catalyzing the initial step of the kynurenine pathway, and overexpression of IDO1 is also associated with poor prognosis in various cancers.	Kynurenine	108-118	indoleamine 2,3-dioxygenase 1	Homo sapiens	14-18
33921805-0	2021	The Tryptophan/Kynurenine Pathway: A Novel Cross-Talk between Nutritional Obesity, Bariatric Surgery and Taste of Fat.	Kynurenine	15-25	bone morphogenetic protein receptor type 2	Homo sapiens	49-53
33921805-0	2021	The Tryptophan/Kynurenine Pathway: A Novel Cross-Talk between Nutritional Obesity, Bariatric Surgery and Taste of Fat.	Kynurenine	15-25	FAT atypical cadherin 1	Homo sapiens	114-117
33937026-5	2021	Kynurenine 3-monooxygenase (KMO), a pivotal enzyme that catalyzes kynurenine metabolism, is essential for several cellular processes.	Kynurenine	66-76	kynurenine 3-monooxygenase	Homo sapiens	0-26
33937026-5	2021	Kynurenine 3-monooxygenase (KMO), a pivotal enzyme that catalyzes kynurenine metabolism, is essential for several cellular processes.	Kynurenine	66-76	kynurenine 3-monooxygenase	Homo sapiens	28-31
34025677-4	2021	We determined that activation of the aryl hydrocarbon receptor (AHR) by kynurenine induced PD-1 expression, and this effect was significantly abrogated by the AHR antagonist CH223191.	Kynurenine	72-82	aryl hydrocarbon receptor	Sus scrofa	37-62
34025677-4	2021	We determined that activation of the aryl hydrocarbon receptor (AHR) by kynurenine induced PD-1 expression, and this effect was significantly abrogated by the AHR antagonist CH223191.	Kynurenine	72-82	aryl hydrocarbon receptor	Sus scrofa	64-67
34025677-4	2021	We determined that activation of the aryl hydrocarbon receptor (AHR) by kynurenine induced PD-1 expression, and this effect was significantly abrogated by the AHR antagonist CH223191.	Kynurenine	72-82	aryl hydrocarbon receptor	Sus scrofa	159-162
34025677-5	2021	Mechanistically, kynurenine alters chromatin accessibility in regulatory regions of T cell inhibitory receptors, allowing AHR to bind to consensus XRE motifs in the promoter region of PD-1.	Kynurenine	17-27	aryl hydrocarbon receptor	Sus scrofa	122-125
33875612-2	2021	Indoleamine 2,3 dioxygenase (IDO) catabolizes tryptophan (T) to kynurenine (K), regulating immune activity, and IDO activity increases with age.	Kynurenine	64-74	indoleamine 2,3-dioxygenase 1	Homo sapiens	29-32
33870196-1	2021	Expression of tryptophan 2,3-dioxygenase (TDO) is a determinant of malignancy in gliomas through kynurenine (KYN) signaling.	Kynurenine	97-107	tryptophan 2,3-dioxygenase	Homo sapiens	14-40
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.	Kynurenine	82-92	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.	Kynurenine	82-92	indoleamine 2,3-dioxygenase 1	Rattus norvegicus	40-43
33838298-11	2021	Increased protein IDO and kynurenine could regulate the accumulation of CD4+Tregs, CD8+Tregs and pDC to induce immune tolerance.	Kynurenine	26-36	Cd4 molecule	Rattus norvegicus	72-75
33920868-1	2021	Indoleamine-2,3-dioxygenase 1 (IDO1), a tryptophan (Trp)-catabolizing enzyme producing metabolites such as kynurenine (Kyn), is expressed by myeloid-derived suppressor cells (MDSCs) and associated with cancer immune escape.	Kynurenine	107-117	indoleamine 2,3-dioxygenase 1	Mus musculus	0-29
33920868-1	2021	Indoleamine-2,3-dioxygenase 1 (IDO1), a tryptophan (Trp)-catabolizing enzyme producing metabolites such as kynurenine (Kyn), is expressed by myeloid-derived suppressor cells (MDSCs) and associated with cancer immune escape.	Kynurenine	107-117	indoleamine 2,3-dioxygenase 1	Mus musculus	31-35
33920868-1	2021	Indoleamine-2,3-dioxygenase 1 (IDO1), a tryptophan (Trp)-catabolizing enzyme producing metabolites such as kynurenine (Kyn), is expressed by myeloid-derived suppressor cells (MDSCs) and associated with cancer immune escape.	Kynurenine	119-122	indoleamine 2,3-dioxygenase 1	Mus musculus	0-29
33920868-1	2021	Indoleamine-2,3-dioxygenase 1 (IDO1), a tryptophan (Trp)-catabolizing enzyme producing metabolites such as kynurenine (Kyn), is expressed by myeloid-derived suppressor cells (MDSCs) and associated with cancer immune escape.	Kynurenine	119-122	indoleamine 2,3-dioxygenase 1	Mus musculus	31-35
33917814-5	2021	Results showed increased hippocampal ROS and NOX2 levels, serotonin turnover, kynurenine, and noradrenaline contents in Abeta-treated rats.	Kynurenine	78-88	amyloid beta precursor protein	Rattus norvegicus	120-125
33917814-6	2021	Both n-6/n-3 balanced and n-3 PUFA enriched diets reduced ROS production, NOX1 and malondialdehyde levels, serotonin turnover, and kynurenine amount in Abeta-injected rats, while increasing NOX2, superoxide dismutase 1, and serotonin contents.	Kynurenine	131-141	amyloid beta precursor protein	Rattus norvegicus	152-157
33735338-11	2021	Liquid chromatography/tandem mass spectrometry (LC-MS/MS) analysis of Trp metabolites showed significant reductions in the level of kynurenine (kyn) in the serum of OVA mice, as compared to NC and FOS mice.	Kynurenine	132-142	serine (or cysteine) peptidase inhibitor, clade B, member 1, pseudogene	Mus musculus	165-168
33870196-1	2021	Expression of tryptophan 2,3-dioxygenase (TDO) is a determinant of malignancy in gliomas through kynurenine (KYN) signaling.	Kynurenine	97-107	tryptophan 2,3-dioxygenase	Homo sapiens	42-45
33870196-1	2021	Expression of tryptophan 2,3-dioxygenase (TDO) is a determinant of malignancy in gliomas through kynurenine (KYN) signaling.	Kynurenine	109-112	tryptophan 2,3-dioxygenase	Homo sapiens	14-40
33870196-1	2021	Expression of tryptophan 2,3-dioxygenase (TDO) is a determinant of malignancy in gliomas through kynurenine (KYN) signaling.	Kynurenine	109-112	tryptophan 2,3-dioxygenase	Homo sapiens	42-45
33709099-6	2021	Activating AHR with L-kynurenine (Kyn) increased AHR expression, which was accompanied by an increase in mitochondrial dehydrogenase content and MMP in MDS/AML cells.	Kynurenine	20-32	aryl hydrocarbon receptor	Homo sapiens	11-14
33607146-0	2021	Increased kynurenine concentration attenuates serotonergic neurotoxicity induced by 3,4-methylenedioxymethamphetamine (MDMA) in rats through activation of aryl hydrocarbon receptor.	Kynurenine	10-20	aryl hydrocarbon receptor	Rattus norvegicus	155-180
33529725-8	2021	For instance, kynurenine pathway interacts with phospoinosisitide-3 kinase (PI3K), extracellular signal-regulated kinase (ERK), Wnt/beta-catenin, P53, bridging integrator 1 (BIN-1), cyclooxygenase 2 (COX-2), cyclin-dependent kinase (CDK) and collagen type XII alpha1 chain (COL12A1).	Kynurenine	14-24	mitogen-activated protein kinase 1	Homo sapiens	83-120
33529725-8	2021	For instance, kynurenine pathway interacts with phospoinosisitide-3 kinase (PI3K), extracellular signal-regulated kinase (ERK), Wnt/beta-catenin, P53, bridging integrator 1 (BIN-1), cyclooxygenase 2 (COX-2), cyclin-dependent kinase (CDK) and collagen type XII alpha1 chain (COL12A1).	Kynurenine	14-24	mitogen-activated protein kinase 1	Homo sapiens	122-125
33529725-8	2021	For instance, kynurenine pathway interacts with phospoinosisitide-3 kinase (PI3K), extracellular signal-regulated kinase (ERK), Wnt/beta-catenin, P53, bridging integrator 1 (BIN-1), cyclooxygenase 2 (COX-2), cyclin-dependent kinase (CDK) and collagen type XII alpha1 chain (COL12A1).	Kynurenine	14-24	catenin beta 1	Homo sapiens	132-144
33529725-8	2021	For instance, kynurenine pathway interacts with phospoinosisitide-3 kinase (PI3K), extracellular signal-regulated kinase (ERK), Wnt/beta-catenin, P53, bridging integrator 1 (BIN-1), cyclooxygenase 2 (COX-2), cyclin-dependent kinase (CDK) and collagen type XII alpha1 chain (COL12A1).	Kynurenine	14-24	tumor protein p53	Homo sapiens	146-149
33529725-8	2021	For instance, kynurenine pathway interacts with phospoinosisitide-3 kinase (PI3K), extracellular signal-regulated kinase (ERK), Wnt/beta-catenin, P53, bridging integrator 1 (BIN-1), cyclooxygenase 2 (COX-2), cyclin-dependent kinase (CDK) and collagen type XII alpha1 chain (COL12A1).	Kynurenine	14-24	bridging integrator 1	Homo sapiens	151-172
33529725-8	2021	For instance, kynurenine pathway interacts with phospoinosisitide-3 kinase (PI3K), extracellular signal-regulated kinase (ERK), Wnt/beta-catenin, P53, bridging integrator 1 (BIN-1), cyclooxygenase 2 (COX-2), cyclin-dependent kinase (CDK) and collagen type XII alpha1 chain (COL12A1).	Kynurenine	14-24	bridging integrator 1	Homo sapiens	174-179
33529725-8	2021	For instance, kynurenine pathway interacts with phospoinosisitide-3 kinase (PI3K), extracellular signal-regulated kinase (ERK), Wnt/beta-catenin, P53, bridging integrator 1 (BIN-1), cyclooxygenase 2 (COX-2), cyclin-dependent kinase (CDK) and collagen type XII alpha1 chain (COL12A1).	Kynurenine	14-24	prostaglandin-endoperoxide synthase 2	Homo sapiens	182-198
33529725-8	2021	For instance, kynurenine pathway interacts with phospoinosisitide-3 kinase (PI3K), extracellular signal-regulated kinase (ERK), Wnt/beta-catenin, P53, bridging integrator 1 (BIN-1), cyclooxygenase 2 (COX-2), cyclin-dependent kinase (CDK) and collagen type XII alpha1 chain (COL12A1).	Kynurenine	14-24	prostaglandin-endoperoxide synthase 2	Homo sapiens	200-205
33529725-8	2021	For instance, kynurenine pathway interacts with phospoinosisitide-3 kinase (PI3K), extracellular signal-regulated kinase (ERK), Wnt/beta-catenin, P53, bridging integrator 1 (BIN-1), cyclooxygenase 2 (COX-2), cyclin-dependent kinase (CDK) and collagen type XII alpha1 chain (COL12A1).	Kynurenine	14-24	collagen type XII alpha 1 chain	Homo sapiens	274-281
33529725-9	2021	Overactivation of kynurenine pathway, particularly overactivation of indoleamine 2,3-dioxygenase (IDO) predicts poor prognosis of several cancers such as gastrointestinal cancers, gynecological cancers, hematologic malignancies, breast cancer, lung cancer, glioma, melanoma, prostate cancer and pancreatic cancer.	Kynurenine	18-28	indoleamine 2,3-dioxygenase 1	Homo sapiens	69-96
33529725-9	2021	Overactivation of kynurenine pathway, particularly overactivation of indoleamine 2,3-dioxygenase (IDO) predicts poor prognosis of several cancers such as gastrointestinal cancers, gynecological cancers, hematologic malignancies, breast cancer, lung cancer, glioma, melanoma, prostate cancer and pancreatic cancer.	Kynurenine	18-28	indoleamine 2,3-dioxygenase 1	Homo sapiens	98-101
33607146-7	2021	Autoradiographic quantification of serotonin transporters showed that both the TDO inhibitor 680C91 and the AhR antagonist CH-223191 potentiated the neurotoxicity induced by MDMA, while administration of exogenous L-kynurenine or of the AhR positive modulator 3,3"-diindolylmethane (DIM) partially prevented the serotonergic damage induced by the drug.	Kynurenine	214-226	aryl hydrocarbon receptor	Rattus norvegicus	108-111
33583308-2	2021	We aimed to investigate the interferon gamma-related biomarkers neopterin and kynurenine-tryptophanratio (KT-ratio) in PSC.	Kynurenine	78-88	interferon gamma	Homo sapiens	28-44
33709099-6	2021	Activating AHR with L-kynurenine (Kyn) increased AHR expression, which was accompanied by an increase in mitochondrial dehydrogenase content and MMP in MDS/AML cells.	Kynurenine	20-32	aryl hydrocarbon receptor	Homo sapiens	49-52
33709099-6	2021	Activating AHR with L-kynurenine (Kyn) increased AHR expression, which was accompanied by an increase in mitochondrial dehydrogenase content and MMP in MDS/AML cells.	Kynurenine	34-37	aryl hydrocarbon receptor	Homo sapiens	11-14
33709099-6	2021	Activating AHR with L-kynurenine (Kyn) increased AHR expression, which was accompanied by an increase in mitochondrial dehydrogenase content and MMP in MDS/AML cells.	Kynurenine	34-37	aryl hydrocarbon receptor	Homo sapiens	49-52
33755856-1	2021	The kynurenine pathway (KP, IDO/Kyn pathway) is an important metabolic pathway related to many diseases.	Kynurenine	4-14	indoleamine 2,3-dioxygenase 1	Rattus norvegicus	28-31
33842334-4	2021	Mechanistically, CAFs up-regulated tryptophan 2, 3-dioxygenase (TDO) expression, resulting in enhanced secretion of kynurenine (Kyn).	Kynurenine	116-126	tryptophan 2,3-dioxygenase	Homo sapiens	35-62
33842334-4	2021	Mechanistically, CAFs up-regulated tryptophan 2, 3-dioxygenase (TDO) expression, resulting in enhanced secretion of kynurenine (Kyn).	Kynurenine	116-126	tryptophan 2,3-dioxygenase	Homo sapiens	64-67
33842334-4	2021	Mechanistically, CAFs up-regulated tryptophan 2, 3-dioxygenase (TDO) expression, resulting in enhanced secretion of kynurenine (Kyn).	Kynurenine	128-131	tryptophan 2,3-dioxygenase	Homo sapiens	35-62
33842334-4	2021	Mechanistically, CAFs up-regulated tryptophan 2, 3-dioxygenase (TDO) expression, resulting in enhanced secretion of kynurenine (Kyn).	Kynurenine	128-131	tryptophan 2,3-dioxygenase	Homo sapiens	64-67
33842334-6	2021	Inhibition of AKT signal prevented cancer cells proliferation, while inhibition of the STAT3 signal reverted drugs resistance and cancer migration induced by kynurenine.	Kynurenine	158-168	signal transducer and activator of transcription 3	Homo sapiens	87-92
33758082-0	2021	Hypoxia-Inducible Factor 1alpha (HIF1alpha) Suppresses Virus Replication in Human Cytomegalovirus Infection by Limiting Kynurenine Synthesis.	Kynurenine	120-130	hypoxia inducible factor 1 subunit alpha	Homo sapiens	0-31
33841677-0	2021	Role of kynurenine in promoting the generation of exhausted CD8+ T cells in colorectal cancer.	Kynurenine	8-18	CD8a molecule	Homo sapiens	60-63
33758082-0	2021	Hypoxia-Inducible Factor 1alpha (HIF1alpha) Suppresses Virus Replication in Human Cytomegalovirus Infection by Limiting Kynurenine Synthesis.	Kynurenine	120-130	hypoxia inducible factor 1 subunit alpha	Homo sapiens	33-42
33758082-7	2021	We discovered that in HCMV-infected cells, HIF1alpha suppresses intracellular and extracellular concentrations of kynurenine.	Kynurenine	114-124	hypoxia inducible factor 1 subunit alpha	Homo sapiens	43-52
33758082-8	2021	HIF1alpha also suppressed the expression of indoleamine 2,3-dioxygenase 1 (IDO1), the rate-limiting enzyme in kynurenine synthesis.	Kynurenine	110-120	hypoxia inducible factor 1 subunit alpha	Homo sapiens	0-9
33758082-8	2021	HIF1alpha also suppressed the expression of indoleamine 2,3-dioxygenase 1 (IDO1), the rate-limiting enzyme in kynurenine synthesis.	Kynurenine	110-120	indoleamine 2,3-dioxygenase 1	Homo sapiens	44-73
33758082-8	2021	HIF1alpha also suppressed the expression of indoleamine 2,3-dioxygenase 1 (IDO1), the rate-limiting enzyme in kynurenine synthesis.	Kynurenine	110-120	indoleamine 2,3-dioxygenase 1	Homo sapiens	75-79
33758082-9	2021	In addition to its role in tryptophan metabolism, kynurenine acts as a signaling messenger by activating aryl hydrocarbon receptor (AhR).	Kynurenine	50-60	aryl hydrocarbon receptor	Homo sapiens	105-130
33758082-9	2021	In addition to its role in tryptophan metabolism, kynurenine acts as a signaling messenger by activating aryl hydrocarbon receptor (AhR).	Kynurenine	50-60	aryl hydrocarbon receptor	Homo sapiens	132-135
33758082-15	2021	Further, we found that HIF1alpha suppresses kynurenine synthesis, a metabolite that can promote HCMV replication by signaling through the aryl hydrocarbon receptor (AhR).	Kynurenine	44-54	hypoxia inducible factor 1 subunit alpha	Homo sapiens	23-32
33758082-15	2021	Further, we found that HIF1alpha suppresses kynurenine synthesis, a metabolite that can promote HCMV replication by signaling through the aryl hydrocarbon receptor (AhR).	Kynurenine	44-54	aryl hydrocarbon receptor	Homo sapiens	138-163
33758082-15	2021	Further, we found that HIF1alpha suppresses kynurenine synthesis, a metabolite that can promote HCMV replication by signaling through the aryl hydrocarbon receptor (AhR).	Kynurenine	44-54	aryl hydrocarbon receptor	Homo sapiens	165-168
33758082-16	2021	In infected cells, the rate-limiting enzyme in kynurenine synthesis, indoleamine 2,3-dioxygenase 1 (IDO1), is suppressed by a HIF1alpha-dependent mechanism.	Kynurenine	47-57	indoleamine 2,3-dioxygenase 1	Homo sapiens	69-98
33758082-16	2021	In infected cells, the rate-limiting enzyme in kynurenine synthesis, indoleamine 2,3-dioxygenase 1 (IDO1), is suppressed by a HIF1alpha-dependent mechanism.	Kynurenine	47-57	indoleamine 2,3-dioxygenase 1	Homo sapiens	100-104
33758082-16	2021	In infected cells, the rate-limiting enzyme in kynurenine synthesis, indoleamine 2,3-dioxygenase 1 (IDO1), is suppressed by a HIF1alpha-dependent mechanism.	Kynurenine	47-57	hypoxia inducible factor 1 subunit alpha	Homo sapiens	126-135
33828565-5	2021	We found that inhibition of the antitumor effect of CAR-T cells in ESCC was dependent on the IDO1 metabolite kynurenine.	Kynurenine	109-119	nuclear receptor subfamily 1 group I member 3	Homo sapiens	52-55
33828565-5	2021	We found that inhibition of the antitumor effect of CAR-T cells in ESCC was dependent on the IDO1 metabolite kynurenine.	Kynurenine	109-119	indoleamine 2,3-dioxygenase 1	Homo sapiens	93-97
33828565-6	2021	Kynurenine could suppress CAR-T cell cytokine secretion and cytotoxic activity.	Kynurenine	0-10	nuclear receptor subfamily 1 group I member 3	Homo sapiens	26-29
33723080-2	2021	Kynurenine is an endogenous aryl hydrocarbon receptor (AhR) ligand.	Kynurenine	0-10	aryl hydrocarbon receptor	Homo sapiens	28-53
33723080-2	2021	Kynurenine is an endogenous aryl hydrocarbon receptor (AhR) ligand.	Kynurenine	0-10	aryl hydrocarbon receptor	Homo sapiens	55-58
33723080-6	2021	In sum, AhR is activated by kynurenine and perhaps other ligands produced during HCMV infection, it profoundly alters the infected-cell transcriptome, and one outcome of its activity is a block to cell cycle progression, providing mechanistic insight to a long-known element of the virus-host cell interaction.	Kynurenine	28-38	aryl hydrocarbon receptor	Homo sapiens	8-11
33841677-2	2021	In this study, we showed that the levels of indoleamine 2,3-dioxygenase 1 (IDO1) and its catabolite kynurenine (Kyn) were higher in late stages (stages III and IV) than in early stages (stages I and II) of CRC patients.	Kynurenine	100-110	indoleamine 2,3-dioxygenase 1	Homo sapiens	44-73
33841677-2	2021	In this study, we showed that the levels of indoleamine 2,3-dioxygenase 1 (IDO1) and its catabolite kynurenine (Kyn) were higher in late stages (stages III and IV) than in early stages (stages I and II) of CRC patients.	Kynurenine	100-110	indoleamine 2,3-dioxygenase 1	Homo sapiens	75-79
33841677-3	2021	We found that Kyn could induce the expression of immune checkpoints and exhaustion markers in CD8+ tumor-infiltrating T cells.	Kynurenine	14-17	CD8a molecule	Homo sapiens	94-97
33712669-5	2021	Kynurenine binding sequences were enriched through phage display panning using a kynurenine-binding oriented human synthetic Fab library.	Kynurenine	0-10	FA complementation group B	Homo sapiens	125-128
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.	Kynurenine	63-73	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.	Kynurenine	63-73	indoleamine 2,3-dioxygenase 1	Homo sapiens	36-39
33712669-5	2021	Kynurenine binding sequences were enriched through phage display panning using a kynurenine-binding oriented human synthetic Fab library.	Kynurenine	81-91	FA complementation group B	Homo sapiens	125-128
33750843-1	2021	Kynurenine 3-monooxygenase (KMO) regulates the levels of neuroactive metabolites in the kynurenine pathway (KP), dysregulation of which is associated with Huntington"s disease (HD) pathogenesis.	Kynurenine	88-98	kynurenine 3-monooxygenase (kynurenine 3-hydroxylase)	Mus musculus	0-26
33707411-6	2021	Given that products of the kynurenine pathway including anthranilic acid have immunosuppressive properties, we speculate on the therapeutic utility to inhibit the rate-limiting enzymes of this pathway including indoleamine 2,3-dioxygenase and tryptophan 2,3-dioxygenase.	Kynurenine	27-37	tryptophan 2,3-dioxygenase	Homo sapiens	243-269
33750843-1	2021	Kynurenine 3-monooxygenase (KMO) regulates the levels of neuroactive metabolites in the kynurenine pathway (KP), dysregulation of which is associated with Huntington"s disease (HD) pathogenesis.	Kynurenine	88-98	kynurenine 3-monooxygenase (kynurenine 3-hydroxylase)	Mus musculus	28-31
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.	Kynurenine	185-195	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.	Kynurenine	185-195	indoleamine 2,3-dioxygenase 1	Homo sapiens	108-111
33675038-6	2021	IDO expressed by conventional DCs is functionally active as measured by kynurenine production.	Kynurenine	72-82	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-3
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.	Kynurenine	52-62	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.	Kynurenine	52-62	indoleamine 2,3-dioxygenase 1	Homo sapiens	121-124
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.	Kynurenine	52-62	tryptophan 2,3-dioxygenase	Homo sapiens	130-156
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.	Kynurenine	52-62	tryptophan 2,3-dioxygenase	Homo sapiens	158-161
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.	Kynurenine	64-67	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.	Kynurenine	64-67	indoleamine 2,3-dioxygenase 1	Homo sapiens	121-124
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.	Kynurenine	64-67	tryptophan 2,3-dioxygenase	Homo sapiens	130-156
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.	Kynurenine	64-67	tryptophan 2,3-dioxygenase	Homo sapiens	158-161
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).	Kynurenine	127-137	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).	Kynurenine	127-137	indoleamine 2,3-dioxygenase 1	Homo sapiens	31-35
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.	Kynurenine	111-122	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.	Kynurenine	111-122	indoleamine 2,3-dioxygenase 1	Homo sapiens	58-62
33737337-10	2021	Furthermore, inhibition of MYCN expression in NB results into accumulation of IDO1 and consequently of kynurenines, which negatively affect the immune surveillance.	Kynurenine	103-114	MYCN proto-oncogene, bHLH transcription factor	Homo sapiens	27-31
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.	Kynurenine	170-180	indoleamine 2,3-dioxygenase 1	Homo sapiens	16-45
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.	Kynurenine	61-71	indoleamine 2,3-dioxygenase 1	Homo sapiens	10-14
33609988-0	2021	Association of the kynurenine pathway metabolites with clinical, cognitive features and IL-1beta levels in patients with schizophrenia spectrum disorder and their siblings.	Kynurenine	19-29	interleukin 1 alpha	Homo sapiens	88-96
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.	Kynurenine	170-180	indoleamine 2,3-dioxygenase 1	Homo sapiens	47-51
33708223-5	2021	Here we hypothesise that tryptophan acts as a rheostat of kynurenine-mediated immunosuppression by competing with kynurenine for entry into immune T-cells through the amino acid transporter called System L. This hypothesis stems from the observations that elevated tryptophan levels in TDO-knockout mice relieve immunosuppression instigated by IDO1, and that the vacancy of System L transporter modulates kynurenine entry into CD4+ T-cells.	Kynurenine	58-68	tryptophan 2,3-dioxygenase	Mus musculus	286-289
33708223-5	2021	Here we hypothesise that tryptophan acts as a rheostat of kynurenine-mediated immunosuppression by competing with kynurenine for entry into immune T-cells through the amino acid transporter called System L. This hypothesis stems from the observations that elevated tryptophan levels in TDO-knockout mice relieve immunosuppression instigated by IDO1, and that the vacancy of System L transporter modulates kynurenine entry into CD4+ T-cells.	Kynurenine	58-68	indoleamine 2,3-dioxygenase 1	Mus musculus	344-348
33708223-5	2021	Here we hypothesise that tryptophan acts as a rheostat of kynurenine-mediated immunosuppression by competing with kynurenine for entry into immune T-cells through the amino acid transporter called System L. This hypothesis stems from the observations that elevated tryptophan levels in TDO-knockout mice relieve immunosuppression instigated by IDO1, and that the vacancy of System L transporter modulates kynurenine entry into CD4+ T-cells.	Kynurenine	58-68	CD4 antigen	Mus musculus	427-430
33679331-1	2021	Background: Indoleamine-2,3-dioxygenase 1 (IDO1) is the initial and rate-limiting enzyme in the metabolism of tryptophan (TRP) to kynurenine (KYN).	Kynurenine	130-140	indoleamine 2,3-dioxygenase 1	Mus musculus	12-41
33679737-4	2021	The liver regulates global Trp supply by the immunosuppressive enzyme tryptophan-2,3-dioxygenase (TDO2), which degrades Trp down the kynurenine pathway (KP).	Kynurenine	133-143	tryptophan 2,3-dioxygenase	Mus musculus	98-102
33679331-1	2021	Background: Indoleamine-2,3-dioxygenase 1 (IDO1) is the initial and rate-limiting enzyme in the metabolism of tryptophan (TRP) to kynurenine (KYN).	Kynurenine	130-140	indoleamine 2,3-dioxygenase 1	Mus musculus	43-47
33679331-1	2021	Background: Indoleamine-2,3-dioxygenase 1 (IDO1) is the initial and rate-limiting enzyme in the metabolism of tryptophan (TRP) to kynurenine (KYN).	Kynurenine	142-145	indoleamine 2,3-dioxygenase 1	Mus musculus	12-41
33679331-1	2021	Background: Indoleamine-2,3-dioxygenase 1 (IDO1) is the initial and rate-limiting enzyme in the metabolism of tryptophan (TRP) to kynurenine (KYN).	Kynurenine	142-145	indoleamine 2,3-dioxygenase 1	Mus musculus	43-47
33272024-5	2021	Results: We show that Kynurenine (Kyn) generation through IDO is markedly induced after MI in mice.	Kynurenine	22-32	indoleamine 2,3-dioxygenase 1	Mus musculus	58-61
33272024-5	2021	Results: We show that Kynurenine (Kyn) generation through IDO is markedly induced after MI in mice.	Kynurenine	22-25	indoleamine 2,3-dioxygenase 1	Mus musculus	58-61
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.	Kynurenine	124-134	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.	Kynurenine	124-134	indoleamine 2,3-dioxygenase 1	Homo sapiens	31-35
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.	Kynurenine	185-195	indoleamine 2,3-dioxygenase 1	Homo sapiens	6-35
33562472-2	2021	Two important products of tryptophan metabolism, viz kynurenine and interleukin (IL)4-inducible1 (IL41)-driven indole 3 pyruvate (I3P), activate the aryl hydrocarbon receptor (AhR), thereby altering the nature of immune responses to SARS-CoV-2 infection.	Kynurenine	53-63	aryl hydrocarbon receptor	Homo sapiens	149-174
33562472-2	2021	Two important products of tryptophan metabolism, viz kynurenine and interleukin (IL)4-inducible1 (IL41)-driven indole 3 pyruvate (I3P), activate the aryl hydrocarbon receptor (AhR), thereby altering the nature of immune responses to SARS-CoV-2 infection.	Kynurenine	53-63	aryl hydrocarbon receptor	Homo sapiens	176-179
33613454-2	2020	Quinolinate phosphoribosyltransferase (QPRT) is the rate-limiting enzyme in the kynurenine pathway participating in NAD+ generation.	Kynurenine	80-90	quinolinate phosphoribosyltransferase	Mus musculus	0-37
33613454-2	2020	Quinolinate phosphoribosyltransferase (QPRT) is the rate-limiting enzyme in the kynurenine pathway participating in NAD+ generation.	Kynurenine	80-90	quinolinate phosphoribosyltransferase	Mus musculus	39-43
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.	Kynurenine	185-195	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.	Kynurenine	185-195	tryptophan 2,3-dioxygenase	Homo sapiens	78-82
33491319-0	2021	Kynurenine-Induced Aryl Hydrocarbon Receptor Signaling in Mice Causes Body Mass Gain, Liver Steatosis, and Hyperglycemia.	Kynurenine	0-10	aryl-hydrocarbon receptor	Mus musculus	19-44
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.	Kynurenine	110-120	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.	Kynurenine	110-120	indoleamine 2,3-dioxygenase 1	Homo sapiens	31-35
33509174-11	2021	Although treatment with IFNT promoted the expression of IDO in PBMCs from both groups, it did so at a substantially reduced rate among the repeat breeder cows, suggesting that decreased levels of kynurenine may relate to the reduced IDO expression in repeat breeder cows.	Kynurenine	196-206	interferon-tau 3g	Bos taurus	24-28
33584686-5	2020	In a syngeneic mouse model using IDO1-overexpressing B16F10 melanoma cells, NTRC 3883-0 effectively counteracted the IDO1-induced modulation of L-tryptophan and L-kynurenine levels, demonstrating its in vivo target modulation.	Kynurenine	161-173	indoleamine 2,3-dioxygenase 1	Mus musculus	33-37
33584686-5	2020	In a syngeneic mouse model using IDO1-overexpressing B16F10 melanoma cells, NTRC 3883-0 effectively counteracted the IDO1-induced modulation of L-tryptophan and L-kynurenine levels, demonstrating its in vivo target modulation.	Kynurenine	161-173	indoleamine 2,3-dioxygenase 1	Mus musculus	117-121
32840656-7	2021	Conjugates obtained by combining an immune checkpoint TDO inhibitor with irinotecan via different linkers could improve tumor immune microenvironment by inhibiting the TDO enzyme expression to block kynurenine production and induce HepG2 cancer cell apoptosis via DNA damage through releasing a TDO inhibitor and irinotecan in cancer cells.	Kynurenine	199-209	tryptophan 2,3-dioxygenase	Homo sapiens	54-57
32840656-7	2021	Conjugates obtained by combining an immune checkpoint TDO inhibitor with irinotecan via different linkers could improve tumor immune microenvironment by inhibiting the TDO enzyme expression to block kynurenine production and induce HepG2 cancer cell apoptosis via DNA damage through releasing a TDO inhibitor and irinotecan in cancer cells.	Kynurenine	199-209	tryptophan 2,3-dioxygenase	Homo sapiens	168-171
32840656-7	2021	Conjugates obtained by combining an immune checkpoint TDO inhibitor with irinotecan via different linkers could improve tumor immune microenvironment by inhibiting the TDO enzyme expression to block kynurenine production and induce HepG2 cancer cell apoptosis via DNA damage through releasing a TDO inhibitor and irinotecan in cancer cells.	Kynurenine	199-209	tryptophan 2,3-dioxygenase	Homo sapiens	168-171
33421663-0	2021	Kynurenine promotes the cytotoxicity of NK cells through aryl hydrocarbon receptor in early pregnancy.	Kynurenine	0-10	aryl hydrocarbon receptor	Homo sapiens	57-82
33421663-5	2021	Compared with AhR- NK cells, cytotoxic activity-related molecules (NKP30, NKP46, NKG2D, perforin, granzyme B and IFN-gamma) was highly expressed in both AhR+ peripheral and decidual NK cells, and kynurenine stimulation promoted the expression of killer receptors and the cytoplasmic granules in an AhR-dependent manner.	Kynurenine	196-206	aryl hydrocarbon receptor	Homo sapiens	153-156
33421663-5	2021	Compared with AhR- NK cells, cytotoxic activity-related molecules (NKP30, NKP46, NKG2D, perforin, granzyme B and IFN-gamma) was highly expressed in both AhR+ peripheral and decidual NK cells, and kynurenine stimulation promoted the expression of killer receptors and the cytoplasmic granules in an AhR-dependent manner.	Kynurenine	196-206	aryl hydrocarbon receptor	Homo sapiens	153-156
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.	Kynurenine	73-83	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.	Kynurenine	73-83	indoleamine 2,3-dioxygenase 1	Homo sapiens	137-141
33491319-2	2021	In vitro studies revealed that the tryptophan metabolite kynurenine (Kyn) activates AHR signaling in cultured hepatocytes.	Kynurenine	57-67	aryl-hydrocarbon receptor	Mus musculus	84-87
33491319-2	2021	In vitro studies revealed that the tryptophan metabolite kynurenine (Kyn) activates AHR signaling in cultured hepatocytes.	Kynurenine	69-72	aryl-hydrocarbon receptor	Mus musculus	84-87
33499346-4	2021	Tryptophan metabolites are distinguished among the groups of natural and synthetic AhR ligands, and these include kynurenine, kynurenic acid and 6-formylindolo[3,2-b]carbazole (FICZ).	Kynurenine	114-124	aryl hydrocarbon receptor	Homo sapiens	83-86
33498837-1	2021	The link between the kynurenine pathway and immunomodulatory molecules-fractalkine and soluble intercellular adhesion molecule-1 (sICAM-1)-in anorexia nervosa (AN) remains unknown.	Kynurenine	21-31	C-X3-C motif chemokine ligand 1	Homo sapiens	71-82
33498837-1	2021	The link between the kynurenine pathway and immunomodulatory molecules-fractalkine and soluble intercellular adhesion molecule-1 (sICAM-1)-in anorexia nervosa (AN) remains unknown.	Kynurenine	21-31	intercellular adhesion molecule 1	Homo sapiens	95-128
33491663-3	2021	Mice infected intranasally with gamma-herpesvirus 68 (gammaHV-68) following BMT displayed elevated levels of the AHR ligand, kynurenine (kyn), in comparison with control mice.	Kynurenine	125-135	aryl hydrocarbon receptor	Homo sapiens	113-116
33510640-9	2020	In parallel studies, kynurenine was the plasma metabolite most highly associated with MDD symptom severity and application of a metabolomics-informed pharmacogenomics approach identified DEFB1 and AHR as genes associated with variation in plasma kynurenine levels.	Kynurenine	246-256	defensin beta 1	Homo sapiens	187-192
33275878-3	2021	The inhibition of KMO reduces the production of downstream toxic kynurenine pathway metabolites and shifts the flux to the formation of the neuroprotectant kynurenic acid.	Kynurenine	65-75	kynurenine 3-monooxygenase	Homo sapiens	18-21
33510640-9	2020	In parallel studies, kynurenine was the plasma metabolite most highly associated with MDD symptom severity and application of a metabolomics-informed pharmacogenomics approach identified DEFB1 and AHR as genes associated with variation in plasma kynurenine levels.	Kynurenine	246-256	aryl hydrocarbon receptor	Homo sapiens	197-200
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).	Kynurenine	45-55	indoleamine 2,3-dioxygenase 1	Homo sapiens	99-102
33422142-3	2021	Metabolism via tryptophan hydroxylase results in serotonin synthesis, whilst metabolism via indoleamine 2,3-dioxygenase (IDO) results in kynurenine and its downstream derivatives.	Kynurenine	137-147	indoleamine 2,3-dioxygenase 1	Homo sapiens	92-119
33422142-3	2021	Metabolism via tryptophan hydroxylase results in serotonin synthesis, whilst metabolism via indoleamine 2,3-dioxygenase (IDO) results in kynurenine and its downstream derivatives.	Kynurenine	137-147	indoleamine 2,3-dioxygenase 1	Homo sapiens	121-124
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.	Kynurenine	30-40	indoleamine 2,3-dioxygenase 1	Homo sapiens	155-158
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.	Kynurenine	111-121	indoleamine 2,3-dioxygenase 1	Homo sapiens	155-158
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).	Kynurenine	45-55	tumor necrosis factor alpha induced protein 6	Mus musculus	132-137
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).	Kynurenine	45-55	aryl hydrocarbon receptor	Homo sapiens	179-204
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).	Kynurenine	45-55	aryl hydrocarbon receptor	Homo sapiens	206-209
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).	Kynurenine	57-60	indoleamine 2,3-dioxygenase 1	Homo sapiens	99-102
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).	Kynurenine	57-60	tumor necrosis factor alpha induced protein 6	Mus musculus	132-137
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).	Kynurenine	57-60	aryl hydrocarbon receptor	Homo sapiens	179-204
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.	Kynurenine	55-65	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-3
33132153-5	2021	The AhR-IDO1-Kynurenine pathway is an important checkpoint, which leads to fatal consequences in SARS-CoV-2 infection and immune evasion in the context of Treg/Th17 imbalance and cytokine storm.	Kynurenine	13-23	aryl hydrocarbon receptor	Homo sapiens	4-7
33132153-5	2021	The AhR-IDO1-Kynurenine pathway is an important checkpoint, which leads to fatal consequences in SARS-CoV-2 infection and immune evasion in the context of Treg/Th17 imbalance and cytokine storm.	Kynurenine	13-23	indoleamine 2,3-dioxygenase 1	Homo sapiens	8-12
33707791-7	2021	In the co-cultures of activated CD4+ T-cells with HD/ASCs and AS/ASCs significant increases of kynurenines, PGE-2, and IL-1Ra, but not IL-10, production were observed.	Kynurenine	95-106	CD4 molecule	Homo sapiens	32-35
33447045-2	2020	The kynurenine (Kyn) pathway, which is controlled by tryptophan 2,3-dioxygenase (TDO), produces neuroactive and anti-inflammatory metabolites.	Kynurenine	4-14	tryptophan 2,3-dioxygenase	Mus musculus	81-84
33447045-2	2020	The kynurenine (Kyn) pathway, which is controlled by tryptophan 2,3-dioxygenase (TDO), produces neuroactive and anti-inflammatory metabolites.	Kynurenine	16-19	tryptophan 2,3-dioxygenase	Mus musculus	53-79
33447045-2	2020	The kynurenine (Kyn) pathway, which is controlled by tryptophan 2,3-dioxygenase (TDO), produces neuroactive and anti-inflammatory metabolites.	Kynurenine	16-19	tryptophan 2,3-dioxygenase	Mus musculus	81-84
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).	Kynurenine	171-181	indoleamine 2,3-dioxygenase 1	Homo sapiens	36-65
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).	Kynurenine	171-181	indoleamine 2,3-dioxygenase 2	Homo sapiens	70-99
33447047-4	2020	Immunoreactivity of kynurenine, the immediate downstream product of indoleamine 2,3-dioxygenase-mediated tryptophan metabolism, showed the same localization as that of indoleamine 2,3-dioxygenase-1 and indoleamine 2,3-dioxygenase-2, suggesting these are functional enzymes.	Kynurenine	20-30	indoleamine 2,3-dioxygenase 1	Homo sapiens	168-197
33447047-4	2020	Immunoreactivity of kynurenine, the immediate downstream product of indoleamine 2,3-dioxygenase-mediated tryptophan metabolism, showed the same localization as that of indoleamine 2,3-dioxygenase-1 and indoleamine 2,3-dioxygenase-2, suggesting these are functional enzymes.	Kynurenine	20-30	indoleamine 2,3-dioxygenase 2	Homo sapiens	202-231
33298635-0	2021	Upregulated Kynurenine Pathway Enzymes in Aortic Atherosclerotic Aneurysm: Macrophage Kynureninase Downregulates Inflammation.	Kynurenine	12-22	kynureninase	Homo sapiens	86-98
33298635-12	2021	Kynureninase may negatively regulate inflammation via the kynurenine pathway itself in macrophages.	Kynurenine	58-68	kynureninase	Homo sapiens	0-12
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.	Kynurenine	85-95	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.	Kynurenine	85-95	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.	Kynurenine	97-100	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.	Kynurenine	97-100	indoleamine 2,3-dioxygenase 1	Homo sapiens	43-46
33418116-3	2021	In mammalian cells, the kynurenine pathway is initiated by the rate-limiting enzymes tryptophan-2,3-dioxygenase (TDO) and interferon responsive indoleamine 2,3-dioxygenase (IDO1) and is the major route for tryptophan catabolism.	Kynurenine	24-34	tryptophan 2,3-dioxygenase	Homo sapiens	85-111
33418116-3	2021	In mammalian cells, the kynurenine pathway is initiated by the rate-limiting enzymes tryptophan-2,3-dioxygenase (TDO) and interferon responsive indoleamine 2,3-dioxygenase (IDO1) and is the major route for tryptophan catabolism.	Kynurenine	24-34	tryptophan 2,3-dioxygenase	Homo sapiens	113-116
33418116-3	2021	In mammalian cells, the kynurenine pathway is initiated by the rate-limiting enzymes tryptophan-2,3-dioxygenase (TDO) and interferon responsive indoleamine 2,3-dioxygenase (IDO1) and is the major route for tryptophan catabolism.	Kynurenine	24-34	indoleamine 2,3-dioxygenase 1	Homo sapiens	173-177
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.	Kynurenine	48-58	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.	Kynurenine	48-58	indoleamine 2,3-dioxygenase 1	Homo sapiens	180-184
33887987-1	2021	Kynurenine 3-monooxygenase (KMO) is the pivotal enzyme in the kynurenine pathway and is located on the mitochondrial outer membrane.	Kynurenine	62-72	kynurenine 3-monooxygenase	Homo sapiens	0-26
33887987-1	2021	Kynurenine 3-monooxygenase (KMO) is the pivotal enzyme in the kynurenine pathway and is located on the mitochondrial outer membrane.	Kynurenine	62-72	kynurenine 3-monooxygenase	Homo sapiens	28-31
33390854-8	2021	IFN-gamma treatment and IDO1 overexpression promoted tryptophan depletion and kynurenine accumulation in cervical cancer cells.	Kynurenine	78-88	interferon gamma	Homo sapiens	0-9
33390854-8	2021	IFN-gamma treatment and IDO1 overexpression promoted tryptophan depletion and kynurenine accumulation in cervical cancer cells.	Kynurenine	78-88	indoleamine 2,3-dioxygenase 1	Homo sapiens	24-28
33390854-11	2021	Conclusions: IFN-gamma promoted induction of autophagy and macrophage phagocytosis in cervical cancer cells possibly via IDO1 expression and kynurenine metabolism.	Kynurenine	141-151	interferon gamma	Mus musculus	13-22
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.	Kynurenine	101-111	indoleamine 2,3-dioxygenase 1	Homo sapiens	138-141
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.	Kynurenine	101-111	tryptophan 2,3-dioxygenase	Homo sapiens	142-145
33447045-0	2020	The Effect of Tryptophan 2,3-Dioxygenase Inhibition on Kynurenine Metabolism and Cognitive Function in the APP23 Mouse Model of Alzheimer"s Disease.	Kynurenine	55-65	tryptophan 2,3-dioxygenase	Mus musculus	14-40
33447045-2	2020	The kynurenine (Kyn) pathway, which is controlled by tryptophan 2,3-dioxygenase (TDO), produces neuroactive and anti-inflammatory metabolites.	Kynurenine	4-14	tryptophan 2,3-dioxygenase	Mus musculus	53-79
33363543-1	2020	Indoleamine 2,3-dioxygenase 1 (IDO1) and tryptophan 2,3-dioxygenase (TDO) catalyze the rate-limiting step of tryptophan catabolism along the kynurenine pathway, which has important immuno suppressive properties, particularly in tumor cells and dendritic cells.	Kynurenine	141-151	indoleamine 2,3-dioxygenase 1	Mus musculus	0-29
33363543-1	2020	Indoleamine 2,3-dioxygenase 1 (IDO1) and tryptophan 2,3-dioxygenase (TDO) catalyze the rate-limiting step of tryptophan catabolism along the kynurenine pathway, which has important immuno suppressive properties, particularly in tumor cells and dendritic cells.	Kynurenine	141-151	indoleamine 2,3-dioxygenase 1	Mus musculus	31-35
33363543-1	2020	Indoleamine 2,3-dioxygenase 1 (IDO1) and tryptophan 2,3-dioxygenase (TDO) catalyze the rate-limiting step of tryptophan catabolism along the kynurenine pathway, which has important immuno suppressive properties, particularly in tumor cells and dendritic cells.	Kynurenine	141-151	tryptophan 2,3-dioxygenase	Mus musculus	41-67
33363543-1	2020	Indoleamine 2,3-dioxygenase 1 (IDO1) and tryptophan 2,3-dioxygenase (TDO) catalyze the rate-limiting step of tryptophan catabolism along the kynurenine pathway, which has important immuno suppressive properties, particularly in tumor cells and dendritic cells.	Kynurenine	141-151	tryptophan 2,3-dioxygenase	Mus musculus	69-72
32871341-1	2020	Indoleamine 2,3-dioxygenase 1 (IDO1) and tryptophan 2,3-dioxygenase (TDO), which mediate kynurenine pathway of tryptophan degradation, have emerged as potential new targets in immunotherapy for treatment of cancer because of their critical role in immunosuppression in the tumor microenvironment.	Kynurenine	89-99	indoleamine 2,3-dioxygenase 1	Mus musculus	0-29
32871341-1	2020	Indoleamine 2,3-dioxygenase 1 (IDO1) and tryptophan 2,3-dioxygenase (TDO), which mediate kynurenine pathway of tryptophan degradation, have emerged as potential new targets in immunotherapy for treatment of cancer because of their critical role in immunosuppression in the tumor microenvironment.	Kynurenine	89-99	indoleamine 2,3-dioxygenase 1	Mus musculus	31-35
32871341-1	2020	Indoleamine 2,3-dioxygenase 1 (IDO1) and tryptophan 2,3-dioxygenase (TDO), which mediate kynurenine pathway of tryptophan degradation, have emerged as potential new targets in immunotherapy for treatment of cancer because of their critical role in immunosuppression in the tumor microenvironment.	Kynurenine	89-99	tryptophan 2,3-dioxygenase	Mus musculus	41-67
32871341-1	2020	Indoleamine 2,3-dioxygenase 1 (IDO1) and tryptophan 2,3-dioxygenase (TDO), which mediate kynurenine pathway of tryptophan degradation, have emerged as potential new targets in immunotherapy for treatment of cancer because of their critical role in immunosuppression in the tumor microenvironment.	Kynurenine	89-99	tryptophan 2,3-dioxygenase	Mus musculus	69-72
32976029-2	2020	IDO is the rate-limiting step in tryptophan metabolism catabolism into its byproducts - kynurenines.	Kynurenine	88-99	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-3
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.	Kynurenine	119-129	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.	Kynurenine	119-129	indoleamine 2,3-dioxygenase 1	Homo sapiens	31-35
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.	Kynurenine	67-70	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-3
32988295-4	2020	IFN-gamma increased kynurenine and interleukin-6 (IL-6) production by SCAP, without affecting the cell viability.	Kynurenine	20-30	interferon gamma	Homo sapiens	0-9
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.	Kynurenine	74-84	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.	Kynurenine	74-84	indoleamine 2,3-dioxygenase 1	Homo sapiens	31-35
32466694-2	2020	Herein, a variety of secondary sulphonamides were synthesised and evaluated in the HeLa cell-based IDO1/kynurenine assay, leading to the identification of new IDO1 inhibitors.	Kynurenine	104-114	indoleamine 2,3-dioxygenase 1	Homo sapiens	159-163
33040279-2	2020	Evidence has suggested that the activation of indoleamine-2,3-dioxygenase (IDO), the rate-limiting enzyme in the kynurenine pathway (KP), plays a crucial role in inflammation-related diseases.	Kynurenine	113-123	indoleamine 2,3-dioxygenase 1	Mus musculus	75-78
33040279-6	2020	Besides, IDO inhibitor causes a significant decrease in the levels of tryptophan, kynurenine and neurotoxic metabolites of KP, such as 3-hydroxykynurenine (3-HK) and quinolinic acid (QUIN) in the prefrontal cortex, hippocampus, spinal cord, spleen and lymph node of EAE mice.	Kynurenine	82-92	indoleamine 2,3-dioxygenase 1	Mus musculus	9-12
32891681-5	2020	A factor that contributes to the development of depression is the brain activation of indoleamine 2,3-dioxygenase (IDO), the rate-limiting enzyme of kynurenine pathway (KP).	Kynurenine	149-159	indoleamine 2,3-dioxygenase 1	Mus musculus	86-113
32891681-5	2020	A factor that contributes to the development of depression is the brain activation of indoleamine 2,3-dioxygenase (IDO), the rate-limiting enzyme of kynurenine pathway (KP).	Kynurenine	149-159	indoleamine 2,3-dioxygenase 1	Mus musculus	115-118
33247138-7	2020	Interestingly, animals with anti-inflammatory responses including high IL-10:IL-6 and kynurenine to tryptophan ratios show less severe illness.	Kynurenine	86-96	interleukin 10	Homo sapiens	71-76
33135582-4	2022	We posit that a phenomenon known as cytokine storm dramatically activates the enzyme indoleamine 2,3-dioxygenase (IDO-1), resulting in the increase in kynurenine metabolites.	Kynurenine	151-161	indoleamine 2,3-dioxygenase 1	Homo sapiens	114-119
33222028-4	2021	The ratio of Kyn to Trp can be used as an indicator to assess IDO activity.	Kynurenine	13-16	indoleamine 2,3-dioxygenase 1	Homo sapiens	62-65
33170836-1	2020	The enzyme kynurenine 3-monooxygenase (KMO) operates at a critical branch-point in the kynurenine pathway (KP), the major route of tryptophan metabolism.	Kynurenine	11-21	kynurenine 3-monooxygenase	Homo sapiens	39-42
33135582-5	2022	Kynurenine is metabolized by IDO-1 in the brain, producing chemokines, in which a prolonged exposure may result long-term brain impairment.	Kynurenine	0-10	indoleamine 2,3-dioxygenase 1	Homo sapiens	29-34
33135582-7	2022	Thereby, angiotensin II could increase kynurenine metabolites producing pro-oxidative and pro-inflammatory effects, resulting in impairment of cognitive function, enhanced oxidative stress and decreased brain-derived neurotrophic factor.	Kynurenine	39-49	angiotensinogen	Homo sapiens	9-23
33135582-7	2022	Thereby, angiotensin II could increase kynurenine metabolites producing pro-oxidative and pro-inflammatory effects, resulting in impairment of cognitive function, enhanced oxidative stress and decreased brain-derived neurotrophic factor.	Kynurenine	39-49	brain derived neurotrophic factor	Homo sapiens	203-236
32710594-10	2020	Plasma C-reactive protein and serum amyloid alpha were associated with signs of increased kynurenine pathway activity in the CSF of PD patients, but not in controls.	Kynurenine	90-100	C-reactive protein	Homo sapiens	7-25
32684242-3	2020	Indoleamine 2,3-dioxygenase 1 (IDO-1) is involved in the kynurenine pathway in tryptophan metabolism and plays a role as an anti-oxidant.	Kynurenine	57-67	indoleamine 2,3-dioxygenase 1	Mus musculus	0-29
32684242-3	2020	Indoleamine 2,3-dioxygenase 1 (IDO-1) is involved in the kynurenine pathway in tryptophan metabolism and plays a role as an anti-oxidant.	Kynurenine	57-67	indoleamine 2,3-dioxygenase 1	Mus musculus	31-36
33114603-0	2020	Kynurenine Promotes RANKL-Induced Osteoclastogenesis In Vitro by Activating the Aryl Hydrocarbon Receptor Pathway.	Kynurenine	0-10	tumor necrosis factor (ligand) superfamily, member 11	Mus musculus	20-25
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).	Kynurenine	67-78	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-4
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).	Kynurenine	67-78	aryl hydrocarbon receptor	Homo sapiens	148-172
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).	Kynurenine	67-78	aryl hydrocarbon receptor	Homo sapiens	174-177
33138259-2	2020	The bulk of dietary TRP flows into the synthesis of body"s proteins, but the TRP metabolism also involves several biochemical reactions (i.e., serotonin and kynurenine pathways).	Kynurenine	157-167	transient receptor potential cation channel subfamily C member 5	Bos taurus	77-80
32805560-1	2020	Kynurenine 3-monooxygenase (KMO) regulates the levels of bioactive substances in the kynurenine pathway of tryptophan catabolism and its activity is tied to so many diseases that finding an appropriate inhibitor for KMO has become an urgent task.	Kynurenine	85-95	kynurenine 3-monooxygenase	Homo sapiens	0-26
32805560-1	2020	Kynurenine 3-monooxygenase (KMO) regulates the levels of bioactive substances in the kynurenine pathway of tryptophan catabolism and its activity is tied to so many diseases that finding an appropriate inhibitor for KMO has become an urgent task.	Kynurenine	85-95	kynurenine 3-monooxygenase	Homo sapiens	28-31
32805560-1	2020	Kynurenine 3-monooxygenase (KMO) regulates the levels of bioactive substances in the kynurenine pathway of tryptophan catabolism and its activity is tied to so many diseases that finding an appropriate inhibitor for KMO has become an urgent task.	Kynurenine	85-95	kynurenine 3-monooxygenase	Homo sapiens	216-219
32871117-1	2020	Indoleamine-2,3-dioxygenase 1 (IDO1) and tryptophan-2,3-dioxygenase 2 (TDO2) degrade tryptophan (Trp) to kynurenine (Kyn), and these enzymes have promise as therapeutic targets.	Kynurenine	105-115	indoleamine 2,3-dioxygenase 1	Mus musculus	0-29
32871117-1	2020	Indoleamine-2,3-dioxygenase 1 (IDO1) and tryptophan-2,3-dioxygenase 2 (TDO2) degrade tryptophan (Trp) to kynurenine (Kyn), and these enzymes have promise as therapeutic targets.	Kynurenine	105-115	indoleamine 2,3-dioxygenase 1	Mus musculus	31-35
32871117-1	2020	Indoleamine-2,3-dioxygenase 1 (IDO1) and tryptophan-2,3-dioxygenase 2 (TDO2) degrade tryptophan (Trp) to kynurenine (Kyn), and these enzymes have promise as therapeutic targets.	Kynurenine	105-115	tryptophan 2,3-dioxygenase	Mus musculus	41-69
32871117-1	2020	Indoleamine-2,3-dioxygenase 1 (IDO1) and tryptophan-2,3-dioxygenase 2 (TDO2) degrade tryptophan (Trp) to kynurenine (Kyn), and these enzymes have promise as therapeutic targets.	Kynurenine	105-115	tryptophan 2,3-dioxygenase	Mus musculus	71-75
32871117-5	2020	For catabolism of Trp to Kyn and anthranilic acid, both substrates were decreased in liver of Tdo2 and dual KO mice.	Kynurenine	25-28	tryptophan 2,3-dioxygenase	Mus musculus	94-98
33114603-4	2020	Here, we report the direct effect of KYN on receptor activator of nuclear factor kappa-B ligand (RANKL)-induced osteoclastogenesis in Raw 264.7 macrophage cells, and we propose a potential mechanism for these KYN-mediated effects.	Kynurenine	37-40	tumor necrosis factor (ligand) superfamily, member 11	Mus musculus	44-95
33114603-4	2020	Here, we report the direct effect of KYN on receptor activator of nuclear factor kappa-B ligand (RANKL)-induced osteoclastogenesis in Raw 264.7 macrophage cells, and we propose a potential mechanism for these KYN-mediated effects.	Kynurenine	37-40	tumor necrosis factor (ligand) superfamily, member 11	Mus musculus	97-102
33114713-1	2020	Tryptophan metabolites: kynurenine (KYN), kynurenic acid (KYNA) and 6-formylindolo[3,2-b]carbazole (FICZ) are considered aryl hydrocarbon receptor (AhR) ligands.	Kynurenine	24-34	aryl hydrocarbon receptor	Homo sapiens	121-146
33114603-0	2020	Kynurenine Promotes RANKL-Induced Osteoclastogenesis In Vitro by Activating the Aryl Hydrocarbon Receptor Pathway.	Kynurenine	0-10	aryl-hydrocarbon receptor	Mus musculus	80-105
33114713-1	2020	Tryptophan metabolites: kynurenine (KYN), kynurenic acid (KYNA) and 6-formylindolo[3,2-b]carbazole (FICZ) are considered aryl hydrocarbon receptor (AhR) ligands.	Kynurenine	24-34	aryl hydrocarbon receptor	Homo sapiens	148-151
32731051-2	2020	Significant reductions in interleukin-37 and tryptophan were found in CRPS subjects, along with positive correlations between kynurenine/tryptophan ratio and TNF-alpha levels with kinesiophobia, tetrahydrobiopterin levels with McGill pain score, sRAGE, and xanthurenic acid and neopterin levels with depression, anxiety and stress scores.	Kynurenine	126-136	tumor necrosis factor	Homo sapiens	158-167
33095942-1	2021	Indoleamine 2,3-dioxygenase 1 (IDO1) is the first rate-limiting enzyme that metabolizes tryptophan to the kynurenine pathway.	Kynurenine	106-116	indoleamine 2,3-dioxygenase 1	Mus musculus	0-29
33095942-1	2021	Indoleamine 2,3-dioxygenase 1 (IDO1) is the first rate-limiting enzyme that metabolizes tryptophan to the kynurenine pathway.	Kynurenine	106-116	indoleamine 2,3-dioxygenase 1	Mus musculus	31-35
33037467-2	2020	It is metabolized in the body using the kynurenine pathway which involves the enzyme indoleamine 2,3 dioxygenase (IDO) and its transport is regulated through the L-type amino acid transporters (LAT 1).	Kynurenine	40-50	indoleamine 2,3-dioxygenase 1	Homo sapiens	85-112
33178611-6	2020	We demonstrated that TDO2 overexpression in nonresponsive patients correlates with kynurenine plasma levels.	Kynurenine	83-93	tryptophan 2,3-dioxygenase	Homo sapiens	21-25
33045014-6	2020	IFN-I specifically rewired tryptophan metabolism and induced hepatic tryptophan oxidation to kynurenine via Tdo2, correlating with altered concentrations of serum metabolites upon viral infection.	Kynurenine	93-103	tryptophan 2,3-dioxygenase	Homo sapiens	108-112
33045014-7	2020	Infected Tdo2-deficient animals displayed elevated serum levels of tryptophan and, unexpectedly, also vast increases in the downstream immune-suppressive metabolite kynurenine.	Kynurenine	165-175	tryptophan 2,3-dioxygenase	Homo sapiens	9-13
33037467-2	2020	It is metabolized in the body using the kynurenine pathway which involves the enzyme indoleamine 2,3 dioxygenase (IDO) and its transport is regulated through the L-type amino acid transporters (LAT 1).	Kynurenine	40-50	indoleamine 2,3-dioxygenase 1	Homo sapiens	114-117
33037467-2	2020	It is metabolized in the body using the kynurenine pathway which involves the enzyme indoleamine 2,3 dioxygenase (IDO) and its transport is regulated through the L-type amino acid transporters (LAT 1).	Kynurenine	40-50	solute carrier family 7 member 5	Homo sapiens	194-199
32726686-0	2020	Kynurenine pathway is altered in BDNF Val66Met knock-in mice: effect of physical exercise.	Kynurenine	0-10	brain derived neurotrophic factor	Mus musculus	33-37
32726686-5	2020	The aim of the present study was to assess whether the kynurenine pathway was differentially regulated in sedentary and exercising wild-type (BDNFVal/Val) and homozygous knock-in BDNF Val66Met (BDNFMet/Met) mice.	Kynurenine	55-65	brain derived neurotrophic factor	Mus musculus	142-146
32726686-10	2020	Overall our results showing an overactivation of the kynurenine pathway in the BDNFMet/Met mice may suggest a possible mechanism underlying the cognitive deficits reported in the BDNF Val66Met carriers.	Kynurenine	53-63	brain derived neurotrophic factor	Mus musculus	79-83
33061415-2	2020	In T1D, the levels of kynurenine-the first byproduct of tryptophan degradation via IDO1-are significantly lower than in nondiabetic controls, such that defective immune regulation by IDO1 has been recognized as potentially contributing to autoimmunity in T1D.	Kynurenine	22-32	indoleamine 2,3-dioxygenase 1	Homo sapiens	83-87
32435912-10	2020	Tryptophan deficiency and kynurenine accumulation may account for the complicated effects of IDO.	Kynurenine	26-36	indoleamine 2,3-dioxygenase 1	Homo sapiens	93-96
31302732-1	2020	Preclinical studies indicate a link between the kynurenine pathway and monocyte chemoattractant protein-1 (MCP-1), but there is a lack of clinical studies examining this further.	Kynurenine	48-58	C-C motif chemokine ligand 2	Homo sapiens	71-105
31302732-1	2020	Preclinical studies indicate a link between the kynurenine pathway and monocyte chemoattractant protein-1 (MCP-1), but there is a lack of clinical studies examining this further.	Kynurenine	48-58	C-C motif chemokine ligand 2	Homo sapiens	107-112
31383940-4	2020	Knockdown (KD) of AOX1 in normal bladder epithelial cells re-wires the tryptophan-kynurenine pathway resulting in elevated NADP levels which may increase metabolic flux through the pentose phosphate (PPP) pathway, enabling increased nucleotide synthesis, and promoting cell invasion.	Kynurenine	82-92	aldehyde oxidase 1	Homo sapiens	18-22
32822738-4	2020	After screening our chemical library, we found that salinomycin potently inhibited IFN-gamma-stimulated kynurenine synthesis with IC50 values of 3.36-4.66 muM in both human cervical and breast cancer cells.	Kynurenine	104-114	interferon gamma	Homo sapiens	83-92
32822738-11	2020	These findings suggest that salinomycin suppresses kynurenine synthesis by inhibiting the catalytic activity of IDO1 and its expression by inhibiting the JAK/STAT and NF-kappaB pathways.	Kynurenine	51-61	indoleamine 2,3-dioxygenase 1	Homo sapiens	112-116
33061415-2	2020	In T1D, the levels of kynurenine-the first byproduct of tryptophan degradation via IDO1-are significantly lower than in nondiabetic controls, such that defective immune regulation by IDO1 has been recognized as potentially contributing to autoimmunity in T1D.	Kynurenine	22-32	indoleamine 2,3-dioxygenase 1	Homo sapiens	183-187
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.	Kynurenine	76-86	indoleamine 2,3-dioxygenase 1	Homo sapiens	12-39
33072086-1	2020	Indoleamine 2,3-dioxygenase 1 (IDO1) is a cytosolic haem-containing enzyme involved in the degradation of tryptophan to kynurenine.	Kynurenine	120-130	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.	Kynurenine	120-130	indoleamine 2,3-dioxygenase 1	Homo sapiens	31-35
32907554-2	2020	IDO1 breaks-down tryptophan to generate kynurenine derivatives, which may activate the aryl hydrocarbon receptor (AHR).	Kynurenine	40-50	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-4
32907554-2	2020	IDO1 breaks-down tryptophan to generate kynurenine derivatives, which may activate the aryl hydrocarbon receptor (AHR).	Kynurenine	40-50	aryl hydrocarbon receptor	Homo sapiens	87-112
32907554-2	2020	IDO1 breaks-down tryptophan to generate kynurenine derivatives, which may activate the aryl hydrocarbon receptor (AHR).	Kynurenine	40-50	aryl hydrocarbon receptor	Homo sapiens	114-117
32935119-7	2020	Analysis of Genotype-Tissue Expression (GTEx) data revealed that expression of kynurenine aminotransferase, which regulates KA production, correlates most strongly with cytokine levels and aryl hydrocarbon receptor activation in older males.	Kynurenine	79-89	aryl hydrocarbon receptor	Homo sapiens	189-214
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).	Kynurenine	68-78	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).	Kynurenine	68-78	indoleamine 2,3-dioxygenase 1	Homo sapiens	286-290
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.	Kynurenine	76-86	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.	Kynurenine	76-86	indoleamine 2,3-dioxygenase 1	Homo sapiens	41-44
32867244-2	2020	The rise in pro-inflammatory cytokines during the "cytokine storm" induce indoleamine 2,3-dioxygenase (IDO), leading to an increase in kynurenine that activates the AhR, thereby heightening the initial pro-inflammatory cytokine phase and suppressing the endogenous anti-viral response.	Kynurenine	135-145	indoleamine 2,3-dioxygenase	None	74-101
32782183-0	2020	Effect of IFN-gamma on the kynurenine/tryptophan ratio in monolayer-cultured keratinocytes and a 3D reconstructed human epidermis model.	Kynurenine	27-37	interferon gamma	Homo sapiens	10-19
32782183-4	2020	OBJECTIVE: The aim of this study was to establish a human epidermis model in order to quantify cytokine and kyn/trp secretion from IFN-gamma stimulated cells and tissues.	Kynurenine	108-111	interferon gamma	Homo sapiens	131-140
32867244-2	2020	The rise in pro-inflammatory cytokines during the "cytokine storm" induce indoleamine 2,3-dioxygenase (IDO), leading to an increase in kynurenine that activates the AhR, thereby heightening the initial pro-inflammatory cytokine phase and suppressing the endogenous anti-viral response.	Kynurenine	135-145	indoleamine 2,3-dioxygenase 1	Homo sapiens	103-106
32867244-2	2020	The rise in pro-inflammatory cytokines during the "cytokine storm" induce indoleamine 2,3-dioxygenase (IDO), leading to an increase in kynurenine that activates the AhR, thereby heightening the initial pro-inflammatory cytokine phase and suppressing the endogenous anti-viral response.	Kynurenine	135-145	aryl hydrocarbon receptor	Homo sapiens	165-168
32825192-9	2020	Changes in TDO expression affecting the kynurenine pathway activity were related to the imbalance between peripheral serotonin and 25-hydroxyvitamin D.	Kynurenine	40-50	tryptophan 2,3-dioxygenase	Rattus norvegicus	11-14
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.	Kynurenine	153-163	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.	Kynurenine	153-163	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.	Kynurenine	153-163	tryptophan 2,3-dioxygenase	Homo sapiens	107-133
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.	Kynurenine	153-163	tryptophan 2,3-dioxygenase	Homo sapiens	135-138
32842609-3	2020	Another enzyme of interest in the kynurenine signaling pathway is kynurenine 3-monooxygenase (KMO).	Kynurenine	34-44	kynurenine 3-monooxygenase	Homo sapiens	66-92
32842609-3	2020	Another enzyme of interest in the kynurenine signaling pathway is kynurenine 3-monooxygenase (KMO).	Kynurenine	34-44	kynurenine 3-monooxygenase	Homo sapiens	94-97
32814718-4	2020	In humans, kynurenine strongly correlated with age, frailty status, TNF-alphaR1 and IL-6, weaker grip strength, and slower walking speed.	Kynurenine	11-21	interleukin 6	Homo sapiens	84-88
32781018-0	2020	Tryptophan and kynurenine stimulate human decidualization via activating Aryl hydrocarbon receptor: Short title: Kynurenine action on human decidualization.	Kynurenine	15-25	aryl hydrocarbon receptor	Homo sapiens	73-98
32782249-0	2020	Blockade of the AHR restricts a Treg-macrophage suppressive axis induced by L-Kynurenine.	Kynurenine	76-88	aryl hydrocarbon receptor	Sus scrofa	16-19
32782249-2	2020	The tryptophan metabolite L-Kynurenine (Kyn) interacts with the ligand-activated transcription factor aryl hydrocarbon receptor (AHR) to drive the generation of Tregs and tolerogenic myeloid cells and PD-1 up-regulation in CD8+ T cells.	Kynurenine	26-38	aryl hydrocarbon receptor	Sus scrofa	102-127
32782249-2	2020	The tryptophan metabolite L-Kynurenine (Kyn) interacts with the ligand-activated transcription factor aryl hydrocarbon receptor (AHR) to drive the generation of Tregs and tolerogenic myeloid cells and PD-1 up-regulation in CD8+ T cells.	Kynurenine	26-38	aryl hydrocarbon receptor	Sus scrofa	129-132
32782249-2	2020	The tryptophan metabolite L-Kynurenine (Kyn) interacts with the ligand-activated transcription factor aryl hydrocarbon receptor (AHR) to drive the generation of Tregs and tolerogenic myeloid cells and PD-1 up-regulation in CD8+ T cells.	Kynurenine	26-38	MHC class I antigen 1	Sus scrofa	201-205
32782249-2	2020	The tryptophan metabolite L-Kynurenine (Kyn) interacts with the ligand-activated transcription factor aryl hydrocarbon receptor (AHR) to drive the generation of Tregs and tolerogenic myeloid cells and PD-1 up-regulation in CD8+ T cells.	Kynurenine	28-31	aryl hydrocarbon receptor	Sus scrofa	102-127
32782249-2	2020	The tryptophan metabolite L-Kynurenine (Kyn) interacts with the ligand-activated transcription factor aryl hydrocarbon receptor (AHR) to drive the generation of Tregs and tolerogenic myeloid cells and PD-1 up-regulation in CD8+ T cells.	Kynurenine	28-31	aryl hydrocarbon receptor	Sus scrofa	129-132
32782249-2	2020	The tryptophan metabolite L-Kynurenine (Kyn) interacts with the ligand-activated transcription factor aryl hydrocarbon receptor (AHR) to drive the generation of Tregs and tolerogenic myeloid cells and PD-1 up-regulation in CD8+ T cells.	Kynurenine	28-31	MHC class I antigen 1	Sus scrofa	201-205
32781018-0	2020	Tryptophan and kynurenine stimulate human decidualization via activating Aryl hydrocarbon receptor: Short title: Kynurenine action on human decidualization.	Kynurenine	113-123	aryl hydrocarbon receptor	Homo sapiens	73-98
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.	Kynurenine	206-216	indoleamine 2,3-dioxygenase 1	Homo sapiens	96-125
32781018-7	2020	Aryl hydrocarbon receptor and its target genes (P450 1A1 and P450 1B1) are significantly increased by tryptophan and kynurenine.	Kynurenine	117-127	aryl hydrocarbon receptor	Homo sapiens	0-25
32781018-7	2020	Aryl hydrocarbon receptor and its target genes (P450 1A1 and P450 1B1) are significantly increased by tryptophan and kynurenine.	Kynurenine	117-127	cytochrome P450 family 1 subfamily B member 1	Homo sapiens	61-69
32781018-8	2020	The induction of tryptophan and kynurenine on insulin growth factor binding protein 1 is abrogated by CH223191, an aryl hydrocarbon receptor inhibitor.	Kynurenine	32-42	aryl hydrocarbon receptor	Homo sapiens	115-140
32781018-13	2020	Our data indicate that Interferon-gamma-induced kynurenine pathway promotes human decidualization via aryl hydrocarbon receptor signaling.	Kynurenine	48-58	interferon gamma	Homo sapiens	23-39
32781018-13	2020	Our data indicate that Interferon-gamma-induced kynurenine pathway promotes human decidualization via aryl hydrocarbon receptor signaling.	Kynurenine	48-58	aryl hydrocarbon receptor	Homo sapiens	102-127
32488348-1	2020	AIM: Indoleamine 2,3-dioxygenase 1 (IDO) is responsible for the progression of the kynurenine pathway, which has been implicated in the pathophysiology of inflammation-induced depression.	Kynurenine	83-93	indoleamine 2,3-dioxygenase 1	Mus musculus	5-34
32753686-8	2021	Downregulation of TSPAN5 expression by ethanol or acamprosate treatment was also associated with decreased concentrations of kynurenine, a major metabolite of tryptophan that plays a role in neuroinflammation.	Kynurenine	125-135	tetraspanin 5	Homo sapiens	18-24
32753686-11	2021	In conclusion, TSPAN5 can modulate the concentrations of 5-HT and kynurenine.	Kynurenine	66-76	tetraspanin 5	Homo sapiens	15-21
31512038-4	2020	We performed a systematic review of studies reporting on such F-18-labeled tryptophan tracers to summarize and compare their biological characteristics and their potential for tumor imaging, with a particular focus on key enzymes of the kynurenine pathway (indoleamine 2,3-dioxygenase [IDO] and tryptophan 2,3-dioxygenase [TDO]), which play an important role in tumoral immune resistance.	Kynurenine	237-247	indoleamine 2,3-dioxygenase 1	Homo sapiens	257-284
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.	Kynurenine	110-120	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-28
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.	Kynurenine	110-120	indoleamine 2,3-dioxygenase 1	Homo sapiens	30-33
32753686-0	2021	TSPAN5 influences serotonin and kynurenine: pharmacogenomic mechanisms related to alcohol use disorder and acamprosate treatment response.	Kynurenine	32-42	tetraspanin 5	Homo sapiens	0-6
32753686-3	2021	The present study was designed to explore the biological function of TSPAN5 with a focus on 5-HT and kynurenine concentrations in the tryptophan pathway.	Kynurenine	101-111	tetraspanin 5	Homo sapiens	69-75
32752186-2	2020	IDO2 is an isoform of IDO1, recently identified as a catalytic enzyme in the tryptophan-kynurenine pathway, which is expressed in dendritic cells and monocytes.	Kynurenine	88-98	indoleamine 2,3-dioxygenase 2	Mus musculus	0-4
32752186-2	2020	IDO2 is an isoform of IDO1, recently identified as a catalytic enzyme in the tryptophan-kynurenine pathway, which is expressed in dendritic cells and monocytes.	Kynurenine	88-98	indoleamine 2,3-dioxygenase 1	Mus musculus	22-26
32690969-4	2020	Specifically, ZIKV infection induces kynurenine (Kyn) production, which activates AHR, limiting the production of type I interferons (IFN-I) involved in antiviral immunity.	Kynurenine	37-47	aryl hydrocarbon receptor	Homo sapiens	82-85
32690969-4	2020	Specifically, ZIKV infection induces kynurenine (Kyn) production, which activates AHR, limiting the production of type I interferons (IFN-I) involved in antiviral immunity.	Kynurenine	49-52	aryl hydrocarbon receptor	Homo sapiens	82-85
32488348-1	2020	AIM: Indoleamine 2,3-dioxygenase 1 (IDO) is responsible for the progression of the kynurenine pathway, which has been implicated in the pathophysiology of inflammation-induced depression.	Kynurenine	83-93	indoleamine 2,3-dioxygenase 1	Mus musculus	36-39
32559180-0	2020	COVID-19 infection alters kynurenine and fatty acid metabolism, correlating with IL-6 levels and renal status.	Kynurenine	26-36	interleukin 6	Homo sapiens	81-85
32722276-10	2020	kynurenine, a tryptophan-derived ligand that activates and bridges AhR to chronic inflammation and breast carcinogenesis.	Kynurenine	0-10	aryl hydrocarbon receptor	Homo sapiens	67-70
32708997-10	2020	Elevated hs-C reactive protein (CRP) was associated with new-onset CKD (OR: 1.045, 95% CI: 1.005-1.086); however, this association disappeared following adjustment with the kynurenine:tryptophan ratio.	Kynurenine	173-183	C-reactive protein	Homo sapiens	9-30
32801823-4	2020	The brief review proposes the hypothesis that FFA arises as a result of excessive facial photo-protection with a resultant disturbance in immunological homeostasis mediated via the aryl hydrocarbon receptor-kynurenine pathway axis (AHR/KP) leading to the collapse of immune privilege at the hair bulge.	Kynurenine	207-217	aryl hydrocarbon receptor	Homo sapiens	181-206
32708997-10	2020	Elevated hs-C reactive protein (CRP) was associated with new-onset CKD (OR: 1.045, 95% CI: 1.005-1.086); however, this association disappeared following adjustment with the kynurenine:tryptophan ratio.	Kynurenine	173-183	C-reactive protein	Homo sapiens	32-35
33095140-10	2020	CONCLUSIONS: Kynurenines are biomarkers of greater adipose infiltration in LSGB and glandular dysfunction suggesting that activation of interferon-gamma pathway is involved in the salivary and lacrimal glands damage.	Kynurenine	13-24	interferon gamma	Homo sapiens	136-152
32551517-4	2020	PEG2k-Fmoc-1-MT prodrug micelles presented enhanced inhibition ability of IDO with decreased kynurenine production and increased the proliferation in dose-dependent manners of effector CD4+ and CD8+ T cells.	Kynurenine	93-103	indoleamine 2,3-dioxygenase 1	Mus musculus	74-77
32331779-1	2020	We present high resolution fast, cost-effective and sensitive Capillary zone electrophoresis (CZE) methods for determination of enantiomeric compounds of Kynurenine pathway, i.e. D, L-Kynurenine (KYN), in human serum and urine samples by cationic-beta-CD and its synergistic dual chiral selector system (SD-CSs) with alpha-CD in 50 mM borax borate buffer (pH 9.0) as BGE.	Kynurenine	154-164	ACD shelterin complex subunit and telomerase recruitment factor	Homo sapiens	247-254
32331779-1	2020	We present high resolution fast, cost-effective and sensitive Capillary zone electrophoresis (CZE) methods for determination of enantiomeric compounds of Kynurenine pathway, i.e. D, L-Kynurenine (KYN), in human serum and urine samples by cationic-beta-CD and its synergistic dual chiral selector system (SD-CSs) with alpha-CD in 50 mM borax borate buffer (pH 9.0) as BGE.	Kynurenine	154-164	ACD shelterin complex subunit and telomerase recruitment factor	Homo sapiens	317-325
32331779-6	2020	The chiral recognition mechanism was investigated by molecular docking and molecular mechanics, which revealed strong hydrogen bonding between Kynurenine enantiomers and the SD-CSs as compared to individual CS as the key player in binding, formation of stable complexes which led to the ultimate separation.	Kynurenine	143-153	citrate synthase	Homo sapiens	177-179
32733441-2	2020	Indoleamine-2,3-dioxygenase (IDO) has been proposed as a mechanism of resistance to anti-PD-1 treatment, and serum kynurenine/tryptophan (kyn/trp) ratio represents a possible marker of IDO activity.	Kynurenine	115-125	indoleamine 2,3-dioxygenase 1	Homo sapiens	185-188
32733441-2	2020	Indoleamine-2,3-dioxygenase (IDO) has been proposed as a mechanism of resistance to anti-PD-1 treatment, and serum kynurenine/tryptophan (kyn/trp) ratio represents a possible marker of IDO activity.	Kynurenine	115-118	indoleamine 2,3-dioxygenase 1	Homo sapiens	185-188
32390008-1	2020	BACKGROUND: Indoleamine 2,3-dioxygenase (IDO), the first step in the kynurenine pathway (KP), is upregulated in some cancers and represents an attractive therapeutic target given its role in tumour immune evasion.	Kynurenine	69-79	indoleamine 2,3-dioxygenase 1	Homo sapiens	12-39
32390008-1	2020	BACKGROUND: Indoleamine 2,3-dioxygenase (IDO), the first step in the kynurenine pathway (KP), is upregulated in some cancers and represents an attractive therapeutic target given its role in tumour immune evasion.	Kynurenine	69-79	indoleamine 2,3-dioxygenase 1	Homo sapiens	41-44
32637034-5	2020	Further, indoximod modulates the differentiation of CD4+ T cells via the aryl hydrocarbon receptor (AhR), which controls transcription of several genes in response to different ligands including kynurenine (Kyn).	Kynurenine	195-205	CD4 molecule	Homo sapiens	52-55
32324593-5	2020	Surprisingly, blocking glutamine metabolism also inhibited IDO expression of both the tumor and myeloid derived cells leading to a marked decrease in kynurenine levels.	Kynurenine	150-160	indoleamine 2,3-dioxygenase 1	Homo sapiens	59-62
32637034-5	2020	Further, indoximod modulates the differentiation of CD4+ T cells via the aryl hydrocarbon receptor (AhR), which controls transcription of several genes in response to different ligands including kynurenine (Kyn).	Kynurenine	195-205	aryl hydrocarbon receptor	Homo sapiens	73-98
32637034-5	2020	Further, indoximod modulates the differentiation of CD4+ T cells via the aryl hydrocarbon receptor (AhR), which controls transcription of several genes in response to different ligands including kynurenine (Kyn).	Kynurenine	195-205	aryl hydrocarbon receptor	Homo sapiens	100-103
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].	Kynurenine	145-155	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-27
32637034-5	2020	Further, indoximod modulates the differentiation of CD4+ T cells via the aryl hydrocarbon receptor (AhR), which controls transcription of several genes in response to different ligands including kynurenine (Kyn).	Kynurenine	207-210	CD4 molecule	Homo sapiens	52-55
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].	Kynurenine	145-155	indoleamine 2,3-dioxygenase 1	Homo sapiens	29-32
32637034-5	2020	Further, indoximod modulates the differentiation of CD4+ T cells via the aryl hydrocarbon receptor (AhR), which controls transcription of several genes in response to different ligands including kynurenine (Kyn).	Kynurenine	207-210	aryl hydrocarbon receptor	Homo sapiens	73-98
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].	Kynurenine	145-155	indoleamine 2,3-dioxygenase 1	Homo sapiens	141-144
32637034-5	2020	Further, indoximod modulates the differentiation of CD4+ T cells via the aryl hydrocarbon receptor (AhR), which controls transcription of several genes in response to different ligands including kynurenine (Kyn).	Kynurenine	207-210	aryl hydrocarbon receptor	Homo sapiens	100-103
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).	Kynurenine	95-105	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-29
32606795-1	2020	Purpose: Tryptophan 2,3-dioxygenase (TDO), encoded by the gene TDO2, is an enzyme that catalyses the first and rate-limiting step of tryptophan (Try) degradation in the kynurenine (Kyn) pathway in the liver.	Kynurenine	169-179	tryptophan 2,3-dioxygenase	Homo sapiens	9-35
32606795-1	2020	Purpose: Tryptophan 2,3-dioxygenase (TDO), encoded by the gene TDO2, is an enzyme that catalyses the first and rate-limiting step of tryptophan (Try) degradation in the kynurenine (Kyn) pathway in the liver.	Kynurenine	169-179	tryptophan 2,3-dioxygenase	Homo sapiens	37-40
32606795-1	2020	Purpose: Tryptophan 2,3-dioxygenase (TDO), encoded by the gene TDO2, is an enzyme that catalyses the first and rate-limiting step of tryptophan (Try) degradation in the kynurenine (Kyn) pathway in the liver.	Kynurenine	169-179	tryptophan 2,3-dioxygenase	Homo sapiens	63-67
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.	Kynurenine	146-157	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.	Kynurenine	146-157	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.	Kynurenine	146-157	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.	Kynurenine	78-88	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).	Kynurenine	95-105	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).	Kynurenine	213-225	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).	Kynurenine	213-225	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.	Kynurenine	22-32	indoleamine 2,3-dioxygenase 1	Homo sapiens	69-73
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).	Kynurenine	227-230	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).	Kynurenine	227-230	indoleamine 2,3-dioxygenase 1	Homo sapiens	31-35
32545442-10	2020	Furthermore, kynurenine increased the tumorsphere formation capability and the expression of cancer stemness genes including Oct4 and Sox2.	Kynurenine	13-23	POU class 5 homeobox 1	Homo sapiens	125-129
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.	Kynurenine	114-117	indoleamine 2,3-dioxygenase 1	Homo sapiens	52-56
32545442-10	2020	Furthermore, kynurenine increased the tumorsphere formation capability and the expression of cancer stemness genes including Oct4 and Sox2.	Kynurenine	13-23	SRY-box transcription factor 2	Homo sapiens	134-138
32493904-3	2020	We also find that over-expressing BNA2, the first Biosynthesis of NAD+ (kynurenine) pathway gene, reduces LD accumulation during aging and extends lifespan.	Kynurenine	72-82	dioxygenase BNA2	Saccharomyces cerevisiae S288C	34-38
32162104-8	2020	Attenuation of KYN- or 4-Cl-KYN-induced deficits was assessed by co-administration of galantamine (GAL, 3 mg/kg) or PAM-2 (1 mg/kg), two positive modulators of alpha7nAChR function.	Kynurenine	15-18	galectin 3	Rattus norvegicus	86-105
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.	Kynurenine	129-139	nitric oxide synthase 2	Homo sapiens	105-109
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.	Kynurenine	129-139	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.	Kynurenine	129-139	aryl hydrocarbon receptor	Homo sapiens	214-239
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.	Kynurenine	129-139	aryl hydrocarbon receptor	Homo sapiens	241-244
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.	Kynurenine	129-139	NFE2 like bZIP transcription factor 2	Homo sapiens	269-275
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.	Kynurenine	129-139	NFE2 like bZIP transcription factor 2	Homo sapiens	277-281
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.	Kynurenine	129-139	serpin family B member 2	Homo sapiens	284-292
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.	Kynurenine	129-139	interleukin 1 beta	Homo sapiens	294-298
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.	Kynurenine	129-139	interleukin 6	Homo sapiens	300-303
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.	Kynurenine	129-139	C-X-C motif chemokine ligand 8	Homo sapiens	308-311
31609478-11	2020	Mechanistically, NO  -induced IDO1/Kynurenine/AHR signaling was mediated by RUNX3 transcription factor.	Kynurenine	35-45	indoleamine 2,3-dioxygenase 1	Homo sapiens	30-34
31609478-11	2020	Mechanistically, NO  -induced IDO1/Kynurenine/AHR signaling was mediated by RUNX3 transcription factor.	Kynurenine	35-45	aryl hydrocarbon receptor	Homo sapiens	46-49
31609478-11	2020	Mechanistically, NO  -induced IDO1/Kynurenine/AHR signaling was mediated by RUNX3 transcription factor.	Kynurenine	35-45	RUNX family transcription factor 3	Homo sapiens	76-81
31609478-12	2020	Our findings identified a novel NO  /RUNX3/Kynurenine metabolic axis, which enhances disease aggressiveness in pancreatic cancer and may have potential translational significance in improving disease outcome.	Kynurenine	43-53	RUNX family transcription factor 3	Homo sapiens	37-42
32289347-1	2020	Kynurenine (Kyn) plays an important role as an immune check-point molecule and regulates various immune responses through its aryl hydrocarbon receptor (Ahr).	Kynurenine	0-10	aryl-hydrocarbon receptor	Mus musculus	126-151
32289347-1	2020	Kynurenine (Kyn) plays an important role as an immune check-point molecule and regulates various immune responses through its aryl hydrocarbon receptor (Ahr).	Kynurenine	0-10	aryl-hydrocarbon receptor	Mus musculus	153-156
32289347-1	2020	Kynurenine (Kyn) plays an important role as an immune check-point molecule and regulates various immune responses through its aryl hydrocarbon receptor (Ahr).	Kynurenine	0-3	aryl-hydrocarbon receptor	Mus musculus	126-151
32289347-1	2020	Kynurenine (Kyn) plays an important role as an immune check-point molecule and regulates various immune responses through its aryl hydrocarbon receptor (Ahr).	Kynurenine	0-3	aryl-hydrocarbon receptor	Mus musculus	153-156
31609478-7	2020	The level of kynurenine, a tryptophan metabolite, was associated with high NOS2 expression, and a higher level of kynurenine predicted poor survival in patients (n = 63, p = 0.01).	Kynurenine	13-23	nitric oxide synthase 2	Homo sapiens	75-79
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.	Kynurenine	0-10	indoleamine 2,3-dioxygenase 1	Homo sapiens	186-213
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.	Kynurenine	0-10	indoleamine 2,3-dioxygenase 1	Homo sapiens	215-218
32314169-5	2020	Tryptophan was assessed by HPLC (high-performance liquid chromatography); kynurenine was measured using an enzyme-linked immunosorbent assay kit; IDO activity (%) was calculated with the formula (kynurenine/tryptophan) x 100.	Kynurenine	196-206	indoleamine 2,3-dioxygenase 1	Homo sapiens	146-149
32289347-0	2020	Kynurenine produced by indoleamine 2,3-dioxygenase 2 exacerbates acute liver injury by carbon tetrachloride in mice.	Kynurenine	0-10	indoleamine 2,3-dioxygenase 2	Mus musculus	23-52
32162104-8	2020	Attenuation of KYN- or 4-Cl-KYN-induced deficits was assessed by co-administration of galantamine (GAL, 3 mg/kg) or PAM-2 (1 mg/kg), two positive modulators of alpha7nAChR function.	Kynurenine	28-31	galectin 3	Rattus norvegicus	86-105
32456621-1	2020	BACKGROUND: Indoleamine 2,3-dioxygenase (IDO) is a rate-limiting enzyme in the metabolism of tryptophan into kynurenine.	Kynurenine	109-119	indoleamine 2,3-dioxygenase 1	Homo sapiens	12-39
32456621-1	2020	BACKGROUND: Indoleamine 2,3-dioxygenase (IDO) is a rate-limiting enzyme in the metabolism of tryptophan into kynurenine.	Kynurenine	109-119	indoleamine 2,3-dioxygenase 1	Homo sapiens	41-44
32414200-1	2020	Kynurenic acid, a metabolite of the kynurenine pathway of tryptophan catabolism, acts as an antagonist for both the alpha7 nicotinic acetylcholine receptor and glycine coagonist sites of the N-methyl-d-aspartic acid receptor at endogenous brain concentrations.	Kynurenine	36-46	cholinergic receptor nicotinic alpha 7 subunit	Homo sapiens	116-155
32511571-0	2020	COVID-19 infection results in alterations of the kynurenine pathway and fatty acid metabolism that correlate with IL-6 levels and renal status.	Kynurenine	49-59	interleukin 6	Homo sapiens	114-118
32384638-2	2020	The enzyme indoleamine-2,3-dioxgenase (IDO) is often overexpressed in PDAC and its downstream metabolite kynurenine has been reported to inhibit T cell activation and proliferation.	Kynurenine	105-115	indoleamine 2,3-dioxygenase 1	Homo sapiens	11-37
32384638-2	2020	The enzyme indoleamine-2,3-dioxgenase (IDO) is often overexpressed in PDAC and its downstream metabolite kynurenine has been reported to inhibit T cell activation and proliferation.	Kynurenine	105-115	indoleamine 2,3-dioxygenase 1	Homo sapiens	39-42
32395570-0	2020	Age-related increase of kynurenine enhances miR29b-1-5p to decrease both CXCL12 signaling and the epigenetic enzyme Hdac3 in bone marrow stromal cells.	Kynurenine	24-34	microRNA 29b-1	Mus musculus	44-52
32370297-1	2020	Indolamine-2,3-dioxygenase (IDO) is an intracellular enzyme that catalyzes amino acid tryptophan to L-kynurenine.	Kynurenine	100-112	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.	Kynurenine	100-112	indoleamine 2,3-dioxygenase 1	Homo sapiens	28-31
32301149-1	2020	Indoleamine 2,3-dioxygenase (IDO) is the rate-limiting enzyme in conversion of tryptophan to kynurenines, feeding de novo nicotinamide synthesis.	Kynurenine	93-104	indoleamine 2,3-dioxygenase 1	Homo sapiens	29-32
32339939-0	2020	Kynurenine pathway enzyme KMO in cancer progression: A tip of the Iceberg.	Kynurenine	0-10	kynurenine 3-monooxygenase	Homo sapiens	26-29
32395570-0	2020	Age-related increase of kynurenine enhances miR29b-1-5p to decrease both CXCL12 signaling and the epigenetic enzyme Hdac3 in bone marrow stromal cells.	Kynurenine	24-34	chemokine (C-X-C motif) ligand 12	Mus musculus	73-79
32395570-0	2020	Age-related increase of kynurenine enhances miR29b-1-5p to decrease both CXCL12 signaling and the epigenetic enzyme Hdac3 in bone marrow stromal cells.	Kynurenine	24-34	histone deacetylase 3	Mus musculus	116-121
32268268-2	2020	Kynurenine 3-monooxygenase (KMO), a crucial kynurenine metabolic enzyme, is involved in inflammation, immune response and tumorigenesis.	Kynurenine	44-54	kynurenine 3-monooxygenase (kynurenine 3-hydroxylase)	Mus musculus	0-26
32290514-7	2020	Our aim was to assess whether there is an association of the neurodegenerative biomarker NFL with the markers of neuroinflammation, e.g., kynurenine metabolites and neopterin, in the cerebrospinal fluid (CSF).	Kynurenine	138-148	neurofilament light chain	Homo sapiens	89-92
32127391-9	2020	IDO1 inhibition sensitized colorectal cancer to radiation-induced cell death, whereas the IDO1 metabolite kynurenine promoted radioprotection.	Kynurenine	106-116	indoleamine 2,3-dioxygenase 1	Homo sapiens	90-94
32268268-2	2020	Kynurenine 3-monooxygenase (KMO), a crucial kynurenine metabolic enzyme, is involved in inflammation, immune response and tumorigenesis.	Kynurenine	44-54	kynurenine 3-monooxygenase (kynurenine 3-hydroxylase)	Mus musculus	28-31
32151061-4	2020	We generated a knockout mouse strain of kynurenine 3-monooxygenase (KMO), an enzyme in the kynurenine pathway that produces neurotoxic 3-hydroxykynurenine.	Kynurenine	40-50	kynurenine 3-monooxygenase (kynurenine 3-hydroxylase)	Mus musculus	68-71
32256470-7	2020	Kynurenine elevation was positively correlated with serum IFN-gamma levels in acute infection, whereas, it was negatively correlated with parasite load and P. vivax LDH levels.	Kynurenine	0-10	interferon gamma	Homo sapiens	58-67
32153151-4	2020	KAT activity was measured in the presence of 1 mM pyruvate and 2 microM or 100 microM L-kynurenine and KYNA production was assessed by high-performance liquid chromatography.	Kynurenine	86-98	thiosulfate sulfurtransferase like domain containing 1	Homo sapiens	0-3
32292562-2	2020	Kynurenine pathway modulation was demonstrated in vivo, which enabled evaluation of TDO as a potential cancer immunotherapy target.	Kynurenine	0-10	tryptophan 2,3-dioxygenase	Homo sapiens	84-87
32226425-4	2020	IDO1 degrades L-tryptophan to L-kynurenine-an activating ligand for AhR-thus establishing a feed-forward loop.	Kynurenine	30-42	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-4
32226425-4	2020	IDO1 degrades L-tryptophan to L-kynurenine-an activating ligand for AhR-thus establishing a feed-forward loop.	Kynurenine	30-42	aryl hydrocarbon receptor	Homo sapiens	68-71
32226425-5	2020	In this study, we further demonstrate that L-kynurenine also promotes the dissociation of the Src kinase-AhR cytosolic complex, leading to the activation of both genomic and non-genomic events in conventional dendritic cells (cDCs) primed with LPS.	Kynurenine	43-55	aryl hydrocarbon receptor	Homo sapiens	105-108
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.	Kynurenine	83-93	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-4
32194572-7	2020	Kynurenine involvement may account for the protection afforded to animals with cerebral malaria and trypanosomiasis when they are treated with an inhibitor of kynurenine-3-monoxygenase (KMO).	Kynurenine	0-10	kynurenine 3-monooxygenase	Homo sapiens	159-184
32194572-7	2020	Kynurenine involvement may account for the protection afforded to animals with cerebral malaria and trypanosomiasis when they are treated with an inhibitor of kynurenine-3-monoxygenase (KMO).	Kynurenine	0-10	kynurenine 3-monooxygenase	Homo sapiens	186-189
32194572-8	2020	There is some evidence that changes in IL-10 may contribute to this protection and the relationship between kynurenines and IL-10 in arthritis and other inflammatory conditions should be explored.	Kynurenine	108-119	interleukin 10	Homo sapiens	124-129
32194572-9	2020	In addition, metabolites of kynurenine downstream of KMO, such as anthranilic acid and 3-hydroxy-anthranilic acid can influence inflammation, and the ratio of these compounds is a valuable biomarker of inflammatory status although the underlying molecular mechanisms of the changes require clarification.	Kynurenine	28-38	kynurenine 3-monooxygenase	Homo sapiens	53-56
31884118-1	2020	The IDO/kynurenine pathway is now established as a major regulator of immune system function.	Kynurenine	8-18	indoleamine 2,3-dioxygenase 1	Homo sapiens	4-7
32008091-10	2020	Altogether, our data suggest that only the combination of DC-restricted antigen and ubiquitous IDO expression attenuated asthma responses in mice, most probably by forming a tryptophan-depleted and kynurenine-enriched micromilieu known to affect neutrophils and T cells.	Kynurenine	198-208	indoleamine 2,3-dioxygenase 1	Mus musculus	95-98
31884118-6	2020	The long-term regulation of autoimmune disorders may be influenced by the epigenetic modulation of kynurenine pathway genes, with recent data suggesting that methylation of IDO may be involved.	Kynurenine	99-109	indoleamine 2,3-dioxygenase 1	Homo sapiens	173-176
31884118-8	2020	This review discusses evidence to date on the role of the IDO/kynurenine pathway and the highly prevalent age-related disorders of osteoporosis and rheumatoid arthritis and identifies key areas that require further research.	Kynurenine	62-72	indoleamine 2,3-dioxygenase 1	Homo sapiens	58-61
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.	Kynurenine	144-154	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-29
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).	Kynurenine	88-99	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).	Kynurenine	88-99	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).	Kynurenine	88-99	forkhead box P3	Homo sapiens	165-170
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.	Kynurenine	144-154	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.	Kynurenine	144-154	indoleamine 2,3-dioxygenase 2	Homo sapiens	38-67
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.	Kynurenine	144-154	indoleamine 2,3-dioxygenase 2	Homo sapiens	69-73
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.	Kynurenine	144-154	tryptophan 2,3-dioxygenase	Homo sapiens	80-106
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.	Kynurenine	144-154	tryptophan 2,3-dioxygenase	Homo sapiens	108-111
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.	Kynurenine	226-238	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.	Kynurenine	226-238	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.	Kynurenine	226-238	indoleamine 2,3-dioxygenase 2	Homo sapiens	38-67
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.	Kynurenine	226-238	indoleamine 2,3-dioxygenase 2	Homo sapiens	69-73
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.	Kynurenine	226-238	tryptophan 2,3-dioxygenase	Homo sapiens	80-106
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.	Kynurenine	226-238	tryptophan 2,3-dioxygenase	Homo sapiens	108-111
32024760-2	2020	The kynurenine pathway is a paramount source of several immunoregulatory metabolites, including l-kynurenine (Kyn), the main product of indoleamine 2,3-dioxygenase 1 (IDO1) that catalyzes the rate-limiting step of the pathway.	Kynurenine	4-14	indoleamine 2,3-dioxygenase 1	Homo sapiens	136-165
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.	Kynurenine	25-35	indoleamine 2,3-dioxygenase 1	Homo sapiens	141-176
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).	Kynurenine	130-140	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).	Kynurenine	130-140	indoleamine 2,3-dioxygenase 1	Homo sapiens	29-32
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).	Kynurenine	130-140	tryptophan 2,3-dioxygenase	Homo sapiens	38-64
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).	Kynurenine	130-140	tryptophan 2,3-dioxygenase	Homo sapiens	66-70
32024760-2	2020	The kynurenine pathway is a paramount source of several immunoregulatory metabolites, including l-kynurenine (Kyn), the main product of indoleamine 2,3-dioxygenase 1 (IDO1) that catalyzes the rate-limiting step of the pathway.	Kynurenine	4-14	indoleamine 2,3-dioxygenase 1	Homo sapiens	167-171
32024760-2	2020	The kynurenine pathway is a paramount source of several immunoregulatory metabolites, including l-kynurenine (Kyn), the main product of indoleamine 2,3-dioxygenase 1 (IDO1) that catalyzes the rate-limiting step of the pathway.	Kynurenine	96-108	indoleamine 2,3-dioxygenase 1	Homo sapiens	136-165
32024760-2	2020	The kynurenine pathway is a paramount source of several immunoregulatory metabolites, including l-kynurenine (Kyn), the main product of indoleamine 2,3-dioxygenase 1 (IDO1) that catalyzes the rate-limiting step of the pathway.	Kynurenine	96-108	indoleamine 2,3-dioxygenase 1	Homo sapiens	167-171
32024760-2	2020	The kynurenine pathway is a paramount source of several immunoregulatory metabolites, including l-kynurenine (Kyn), the main product of indoleamine 2,3-dioxygenase 1 (IDO1) that catalyzes the rate-limiting step of the pathway.	Kynurenine	110-113	indoleamine 2,3-dioxygenase 1	Homo sapiens	136-165
32024760-2	2020	The kynurenine pathway is a paramount source of several immunoregulatory metabolites, including l-kynurenine (Kyn), the main product of indoleamine 2,3-dioxygenase 1 (IDO1) that catalyzes the rate-limiting step of the pathway.	Kynurenine	110-113	indoleamine 2,3-dioxygenase 1	Homo sapiens	167-171
32116558-1	2020	Objective: Our study was designed to investigate whether the indoleamine-2,3-dioxygenase (IDO)-mediated kynurenine/tryptophan (KYN/TRP) pathway participates in the development of emotional deficits from ethanol addiction/withdrawal mice.	Kynurenine	104-115	indoleamine 2,3-dioxygenase 1	Mus musculus	90-93
32116558-1	2020	Objective: Our study was designed to investigate whether the indoleamine-2,3-dioxygenase (IDO)-mediated kynurenine/tryptophan (KYN/TRP) pathway participates in the development of emotional deficits from ethanol addiction/withdrawal mice.	Kynurenine	127-130	indoleamine 2,3-dioxygenase 1	Mus musculus	90-93
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.	Kynurenine	200-210	indoleamine 2,3-dioxygenase 1	Homo sapiens	161-165
32116558-10	2020	Conclusion: Our results suggested that the TRP/KYN pathway, medicated by IDO1, in the hippocampus, cerebral cortex, and amygdala, plays an important role in the development of emotional deficits caused by ethanol addiction and withdrawal.	Kynurenine	47-50	indoleamine 2,3-dioxygenase 1	Mus musculus	73-77
31830637-4	2020	Moreover, HT2 could enhance T-cell immune responses in vitro by releasing a TDO inhibitor to suppress TDO expression and blockade kynurenine production.	Kynurenine	130-140	tryptophan 2,3-dioxygenase	Mus musculus	76-79
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).	Kynurenine	175-185	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-30
31812582-0	2020	Kynurenine inhibits autophagy and promotes senescence in aged bone marrow mesenchymal stem cells through the aryl hydrocarbon receptor pathway.	Kynurenine	0-10	aryl-hydrocarbon receptor	Mus musculus	109-134
31812582-3	2020	One key upstream mechanism that appears to target a number of osteogenic pathways with age is kynurenine, a tryptophan metabolite and an endogenous Aryl hydrocarbon receptor (AhR) agonist.	Kynurenine	94-104	aryl-hydrocarbon receptor	Mus musculus	175-178
31812582-8	2020	We found that physiological levels of kynurenine (10 and 100 muM) disrupted autophagic flux as evidenced by the reduction of LC3B-II, and autophagolysosomal production, as well as a significant increase of p62 protein level.	Kynurenine	38-48	microtubule-associated protein 1 light chain 3 beta	Mus musculus	125-129
31812582-8	2020	We found that physiological levels of kynurenine (10 and 100 muM) disrupted autophagic flux as evidenced by the reduction of LC3B-II, and autophagolysosomal production, as well as a significant increase of p62 protein level.	Kynurenine	38-48	nucleoporin 62	Mus musculus	206-209
31812582-9	2020	Additionally, kynurenine also induced a senescent phenotype in BMSCs as shown by the increased expression of several senescence markers including senescence associated beta-galactosidase in BMSCs.	Kynurenine	14-24	galactosidase, beta 1	Mus musculus	168-186
31812582-10	2020	Additionally, western blotting reveals that levels of p21, another marker of senescence, also increased in kynurenine-treated BMSCs, while senescent-associated aggregation of nuclear H3K9me3 also showed a significant increase in response to kynurenine treatment.	Kynurenine	107-117	cyclin-dependent kinase inhibitor 1A (P21)	Mus musculus	54-57
31812582-12	2020	Indeed, AhR inhibition restored kynurenine-suppressed autophagy levels as shown by levels of LC3B-II, p62 and autophagolysosomal formation demonstrating a rescuing of autophagic flux.	Kynurenine	32-42	aryl-hydrocarbon receptor	Mus musculus	8-11
31812582-12	2020	Indeed, AhR inhibition restored kynurenine-suppressed autophagy levels as shown by levels of LC3B-II, p62 and autophagolysosomal formation demonstrating a rescuing of autophagic flux.	Kynurenine	32-42	nucleoporin 62	Mus musculus	102-105
31812582-13	2020	Furthermore, inhibition of AhR signaling prevented the kynurenine-induced increase in senescence associated beta-galactosidase and p21 levels, as well as blocking aggregation of nuclear H3K9me3.	Kynurenine	55-65	aryl-hydrocarbon receptor	Mus musculus	27-30
31812582-13	2020	Furthermore, inhibition of AhR signaling prevented the kynurenine-induced increase in senescence associated beta-galactosidase and p21 levels, as well as blocking aggregation of nuclear H3K9me3.	Kynurenine	55-65	galactosidase, beta 1	Mus musculus	108-126
31812582-13	2020	Furthermore, inhibition of AhR signaling prevented the kynurenine-induced increase in senescence associated beta-galactosidase and p21 levels, as well as blocking aggregation of nuclear H3K9me3.	Kynurenine	55-65	cyclin-dependent kinase inhibitor 1A (P21)	Mus musculus	131-134
31812582-14	2020	Taken together, our results suggest that kynurenine inhibits autophagy and induces senescence in BMSCs via AhR signaling, and that this may be a novel target to prevent or reduce age-associated bone loss and osteoporosis.	Kynurenine	41-51	aryl-hydrocarbon receptor	Mus musculus	107-110
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.	Kynurenine	217-227	tryptophan 2,3-dioxygenase	Homo sapiens	112-138
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.	Kynurenine	217-227	tryptophan 2,3-dioxygenase	Homo sapiens	140-143
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.	Kynurenine	217-227	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.	Kynurenine	217-227	indoleamine 2,3-dioxygenase 1	Homo sapiens	178-181
32148781-1	2020	Kynurenine-3-monooxygenase (KMO) is an enzyme that relies on nicotinamide adenine dinucleotide phosphate (NADP), a key site in the kynurenine pathway (KP), which has great effects on neurological diseases, cancer, and peripheral inflammation.	Kynurenine	131-141	kynurenine 3-monooxygenase	Homo sapiens	0-26
32148781-1	2020	Kynurenine-3-monooxygenase (KMO) is an enzyme that relies on nicotinamide adenine dinucleotide phosphate (NADP), a key site in the kynurenine pathway (KP), which has great effects on neurological diseases, cancer, and peripheral inflammation.	Kynurenine	131-141	kynurenine 3-monooxygenase	Homo sapiens	28-31
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).	Kynurenine	190-200	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).	Kynurenine	190-200	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).	Kynurenine	190-200	tryptophan 2,3-dioxygenase	Homo sapiens	92-96
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).	Kynurenine	202-205	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).	Kynurenine	202-205	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).	Kynurenine	202-205	tryptophan 2,3-dioxygenase	Homo sapiens	92-96
31862422-4	2020	Additionally, as an extension of earlier studies with dietary administration of kynurenine, we investigated the effects of kynurenine on Hdac3 and NCoR1 expression and enzymatic deacetylase activity as potential mechanistic contributors to the effects of kynurenine on osteoblasts.	Kynurenine	123-133	histone deacetylase 3	Homo sapiens	137-142
31862422-4	2020	Additionally, as an extension of earlier studies with dietary administration of kynurenine, we investigated the effects of kynurenine on Hdac3 and NCoR1 expression and enzymatic deacetylase activity as potential mechanistic contributors to the effects of kynurenine on osteoblasts.	Kynurenine	123-133	histone deacetylase 3	Homo sapiens	137-142
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.	Kynurenine	183-193	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.	Kynurenine	183-193	indoleamine 2,3-dioxygenase 1	Homo sapiens	57-61
30924357-3	2020	Many of tryptophan (Trp) metabolites, such as kynurenine and indole, generated under a series of endogenous enzymes or microbial metabolism, have been reported enable to bind and activate the aryl hydrocarbon receptor (AhR), this series of process is termed the Trp-AhR pathway.	Kynurenine	46-56	aryl hydrocarbon receptor	Homo sapiens	192-217
30924357-3	2020	Many of tryptophan (Trp) metabolites, such as kynurenine and indole, generated under a series of endogenous enzymes or microbial metabolism, have been reported enable to bind and activate the aryl hydrocarbon receptor (AhR), this series of process is termed the Trp-AhR pathway.	Kynurenine	46-56	aryl hydrocarbon receptor	Homo sapiens	219-222
30924357-3	2020	Many of tryptophan (Trp) metabolites, such as kynurenine and indole, generated under a series of endogenous enzymes or microbial metabolism, have been reported enable to bind and activate the aryl hydrocarbon receptor (AhR), this series of process is termed the Trp-AhR pathway.	Kynurenine	46-56	aryl hydrocarbon receptor	Homo sapiens	266-269
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).	Kynurenine	175-185	indoleamine 2,3-dioxygenase 1	Homo sapiens	32-36
31927462-2	2020	TDO and IDO are enzymes that catalyze the first and rate-limiting step of the kynurenine pathway.	Kynurenine	78-88	tryptophan 2,3-dioxygenase	Mus musculus	0-3
31927462-2	2020	TDO and IDO are enzymes that catalyze the first and rate-limiting step of the kynurenine pathway.	Kynurenine	78-88	indoleamine 2,3-dioxygenase 1	Mus musculus	8-11
31228000-8	2019	PGC1alpha changes the metabolism of kynurenine towards, and, in turn, it reduces glutamatergic neurotoxicity.	Kynurenine	36-46	PPARG coactivator 1 alpha	Homo sapiens	0-9
32597823-10	2020	Because lack of physical exercise activates AhRs via the IDO1-kynurenine-AhR signaling pathway increasing risk of infection, physical exercise should be encouraged during quarantines and stay-at-home orders during pandemic outbreaks.	Kynurenine	62-72	indoleamine 2,3-dioxygenase 1	Homo sapiens	57-61
31866995-4	2019	TDO2 catalyses the oxidation of tryptophan to N-formyl kynurenine, which is the first and rate-limiting step of Trp degradation along the kynurenine pathway (KP).	Kynurenine	55-65	tryptophan 2,3-dioxygenase	Homo sapiens	0-4
30815792-1	2019	PURPOSE: Fluorine-18 labeled tryptophan analog L-1-[18F]fluoroethyl-tryptophan (L-1-[18F]FETrp) was designed for positron emission tomography (PET) imaging of cancer by dual targeting of the overexpressed amino acid transporters and altered indoleamine 2,3-dioxygenase (IDO)-mediated kynurenine pathway of tryptophan metabolism.	Kynurenine	284-294	L1 cell adhesion molecule	Mus musculus	47-50
30815792-1	2019	PURPOSE: Fluorine-18 labeled tryptophan analog L-1-[18F]fluoroethyl-tryptophan (L-1-[18F]FETrp) was designed for positron emission tomography (PET) imaging of cancer by dual targeting of the overexpressed amino acid transporters and altered indoleamine 2,3-dioxygenase (IDO)-mediated kynurenine pathway of tryptophan metabolism.	Kynurenine	284-294	L1 cell adhesion molecule	Mus musculus	80-83
31737575-4	2019	IDO is the rate-limiting enzyme converting tryptophan to kynurenine.	Kynurenine	57-67	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-3
31525567-8	2019	CONCLUSIONS: These data provide evidence of a biological link between metabolites of the kynurenine pathway, the endocannabinoid system and IL-6 and suggest that these factors may influence personality traits.	Kynurenine	89-99	interleukin 6	Homo sapiens	140-144
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.	Kynurenine	216-227	tryptophan 2,3-dioxygenase	Rattus norvegicus	36-39
31685866-14	2019	This phenomenon was concomitant with a significant reduction of IDO activity in EAO testis measured by tryptophan and kynurenine concentrations (HPLC).	Kynurenine	118-128	indoleamine 2,3-dioxygenase 1	Rattus norvegicus	64-67
30507339-12	2019	In CT26 tumor bearing mice, the IDO inhibition of S-EPA and EPA on plasma or tumor kynurenine was generally consistent.	Kynurenine	83-93	indoleamine 2,3-dioxygenase 1	Mus musculus	32-35
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.	Kynurenine	216-227	indoleamine 2,3-dioxygenase 1	Rattus norvegicus	0-3
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.	Kynurenine	216-227	tryptophan 2,3-dioxygenase	Rattus norvegicus	8-34
31431462-0	2019	Activation of Aryl Hydrocarbon Receptor by Kynurenine Impairs Progression and Metastasis of Neuroblastoma.	Kynurenine	43-53	aryl hydrocarbon receptor	Homo sapiens	14-39
31431462-7	2019	In addition, activation of AHR by the endogenous ligand kynurenine (Kyn) inhibited cell proliferation and promoted cell differentiation in vitro and in vivo.	Kynurenine	56-66	aryl hydrocarbon receptor	Homo sapiens	27-30
31431462-7	2019	In addition, activation of AHR by the endogenous ligand kynurenine (Kyn) inhibited cell proliferation and promoted cell differentiation in vitro and in vivo.	Kynurenine	68-71	aryl hydrocarbon receptor	Homo sapiens	27-30
31431462-8	2019	Kyn treatment also upregulated the expression of KISS1, a tumor metastasis suppressor, and attenuated metastasis in the xenograft model.	Kynurenine	0-3	KiSS-1 metastasis suppressor	Homo sapiens	49-54
31580660-1	2019	Indoleamine 2,3-dioxygenase 1 (IDO1), which catalyzes the initial and rate-limiting step of the kynurenine pathway of tryptophan catabolism, has emerged as a key target in cancer immunotherapy because of its role in enabling cancers to evade the immune system.	Kynurenine	96-106	indoleamine 2,3-dioxygenase 1	Mus musculus	0-29
31580660-1	2019	Indoleamine 2,3-dioxygenase 1 (IDO1), which catalyzes the initial and rate-limiting step of the kynurenine pathway of tryptophan catabolism, has emerged as a key target in cancer immunotherapy because of its role in enabling cancers to evade the immune system.	Kynurenine	96-106	indoleamine 2,3-dioxygenase 1	Mus musculus	31-35
31628327-3	2019	Immune cells of people with DS overexpress IDO1, the rate-limiting enzyme in the kynurenine pathway (KP) and a known interferon (IFN)-stimulated gene.	Kynurenine	81-91	indoleamine 2,3-dioxygenase 1	Homo sapiens	43-47
31591195-7	2019	Neuronal EAAT2 deletion leads to dysregulation of the kynurenine pathway, and astrocytic EAAT2 deficiency results in dysfunction of innate and adaptive immune pathways, which correlate with cognitive decline.	Kynurenine	54-64	solute carrier family 1 member 2	Homo sapiens	9-14
31737181-0	2019	Kynurenine, a Tryptophan Metabolite That Increases with Age, Induces Muscle Atrophy and Lipid Peroxidation.	Kynurenine	0-10	renin binding protein	Mus musculus	56-59
31737181-2	2019	Kynurenine (KYN) is a circulating tryptophan metabolite that is known to increase with age and is a ligand of the aryl hydrocarbon receptor (Ahr).	Kynurenine	0-10	renin binding protein	Mus musculus	87-90
31737181-2	2019	Kynurenine (KYN) is a circulating tryptophan metabolite that is known to increase with age and is a ligand of the aryl hydrocarbon receptor (Ahr).	Kynurenine	0-10	aryl-hydrocarbon receptor	Mus musculus	114-139
31737181-2	2019	Kynurenine (KYN) is a circulating tryptophan metabolite that is known to increase with age and is a ligand of the aryl hydrocarbon receptor (Ahr).	Kynurenine	0-10	aryl-hydrocarbon receptor	Mus musculus	141-144
31737181-2	2019	Kynurenine (KYN) is a circulating tryptophan metabolite that is known to increase with age and is a ligand of the aryl hydrocarbon receptor (Ahr).	Kynurenine	12-15	renin binding protein	Mus musculus	87-90
31737181-2	2019	Kynurenine (KYN) is a circulating tryptophan metabolite that is known to increase with age and is a ligand of the aryl hydrocarbon receptor (Ahr).	Kynurenine	12-15	aryl-hydrocarbon receptor	Mus musculus	114-139
31737181-2	2019	Kynurenine (KYN) is a circulating tryptophan metabolite that is known to increase with age and is a ligand of the aryl hydrocarbon receptor (Ahr).	Kynurenine	12-15	aryl-hydrocarbon receptor	Mus musculus	141-144
31737181-9	2019	Our data suggest that IDO inhibition may represent a novel therapeutic approach for the prevention of sarcopenia and possibly other age-associated conditions associated with KYN accumulation such as bone loss and neurodegeneration.	Kynurenine	174-177	indoleamine 2,3-dioxygenase 1	Mus musculus	22-25
31737181-9	2019	Our data suggest that IDO inhibition may represent a novel therapeutic approach for the prevention of sarcopenia and possibly other age-associated conditions associated with KYN accumulation such as bone loss and neurodegeneration.	Kynurenine	174-177	renin binding protein	Mus musculus	132-135
31601232-0	2019	Plasma neurofilament light chain and amyloid-beta are associated with the kynurenine pathway metabolites in preclinical Alzheimer"s disease.	Kynurenine	74-84	amyloid beta precursor protein	Homo sapiens	37-49
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.	Kynurenine	77-87	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.	Kynurenine	77-87	indoleamine 2,3-dioxygenase 1	Homo sapiens	31-35
31601232-5	2019	RESULTS: A positive correlation between NFL and the kynurenine to tryptophan ratio (K/T) reflecting indoleamine 2,3-dioxygenase activity was observed (r = .451, p < .0001).	Kynurenine	52-62	neurofilament light chain	Homo sapiens	40-43
31601232-6	2019	Positive correlations were also observed between NFL and kynurenine (r = .364, p < .0005), kynurenic acid (r = .384, p < .0001), 3-hydroxykynurenine (r = .246, p = .014), anthranilic acid (r = .311, p = .002), and quinolinic acid (r = .296, p = .003).	Kynurenine	57-67	neurofilament light chain	Homo sapiens	49-52
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.	Kynurenine	129-139	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-29
31432072-8	2019	Analyses using KEGG-defined pathways revealed statistically significant differences in tryptophan metabolism between diets, with kynurenine and melatonin positively associated with serum C-reactive protein concentrations.	Kynurenine	129-139	C-reactive protein	Homo sapiens	187-205
31444833-8	2019	Furthermore, Ido2 depletion altered the tumor microenvironment, such as tryptophan accumulation and kynurenine reduction, leading to enhancement of immune cell invasion.	Kynurenine	100-110	indoleamine 2,3-dioxygenase 2	Mus musculus	13-17
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.	Kynurenine	129-139	indoleamine 2,3-dioxygenase 1	Homo sapiens	31-35
31012492-3	2019	A genomewide association study for PGRN-AMPS plasma metabolites associated with SSRI response (serotonin) and baseline MDD severity (kynurenine) identified single nucleotide polymorphisms (SNPs) in DEFB1, ERICH3, AHR, and TSPAN5 that we tested as predictors.	Kynurenine	133-143	granulin precursor	Homo sapiens	35-39
31279682-9	2019	On the other hand, IBU increased the level of anti-inflammatory markers, decreased tryptophan 2,3-dioxygenase (TDO2), the first step in the kynurenine pathway known to be activated during inflammatory conditions, and PGE2 levels.	Kynurenine	140-150	tryptophan 2,3-dioxygenase	Mus musculus	83-109
31279682-9	2019	On the other hand, IBU increased the level of anti-inflammatory markers, decreased tryptophan 2,3-dioxygenase (TDO2), the first step in the kynurenine pathway known to be activated during inflammatory conditions, and PGE2 levels.	Kynurenine	140-150	tryptophan 2,3-dioxygenase	Mus musculus	111-115
31012492-3	2019	A genomewide association study for PGRN-AMPS plasma metabolites associated with SSRI response (serotonin) and baseline MDD severity (kynurenine) identified single nucleotide polymorphisms (SNPs) in DEFB1, ERICH3, AHR, and TSPAN5 that we tested as predictors.	Kynurenine	133-143	adenylosuccinate lyase	Homo sapiens	40-44
31012492-3	2019	A genomewide association study for PGRN-AMPS plasma metabolites associated with SSRI response (serotonin) and baseline MDD severity (kynurenine) identified single nucleotide polymorphisms (SNPs) in DEFB1, ERICH3, AHR, and TSPAN5 that we tested as predictors.	Kynurenine	133-143	defensin beta 1	Homo sapiens	198-203
31012492-3	2019	A genomewide association study for PGRN-AMPS plasma metabolites associated with SSRI response (serotonin) and baseline MDD severity (kynurenine) identified single nucleotide polymorphisms (SNPs) in DEFB1, ERICH3, AHR, and TSPAN5 that we tested as predictors.	Kynurenine	133-143	glutamate rich 3	Homo sapiens	205-211
31012492-3	2019	A genomewide association study for PGRN-AMPS plasma metabolites associated with SSRI response (serotonin) and baseline MDD severity (kynurenine) identified single nucleotide polymorphisms (SNPs) in DEFB1, ERICH3, AHR, and TSPAN5 that we tested as predictors.	Kynurenine	133-143	aryl hydrocarbon receptor	Homo sapiens	213-216
31012492-3	2019	A genomewide association study for PGRN-AMPS plasma metabolites associated with SSRI response (serotonin) and baseline MDD severity (kynurenine) identified single nucleotide polymorphisms (SNPs) in DEFB1, ERICH3, AHR, and TSPAN5 that we tested as predictors.	Kynurenine	133-143	tetraspanin 5	Homo sapiens	222-228
31128239-10	2019	Amino acid analysis of the irradiated proteins showed consumption of Trp, His, Tyr and Phe, and formation of kynurenine (from Trp), methionine sulfoxide (from Met) and DOPA (from Tyr).	Kynurenine	109-119	transient receptor potential cation channel subfamily C member 5	Bos taurus	126-129
29988087-2	2019	Circulating kynurenine is transported into the brain by the large amino transporter LAT1 at the level of the blood-brain barrier.	Kynurenine	12-22	solute carrier family 7 (cationic amino acid transporter, y+ system), member 5	Mus musculus	84-88
29988087-3	2019	We hypothesized that administration of leucine that has a high affinity for LAT1 should prevent the entry of kynurenine into the brain and attenuate the formation of neurotoxic kynurenine metabolites.	Kynurenine	109-119	solute carrier family 7 (cationic amino acid transporter, y+ system), member 5	Mus musculus	76-80
29988087-3	2019	We hypothesized that administration of leucine that has a high affinity for LAT1 should prevent the entry of kynurenine into the brain and attenuate the formation of neurotoxic kynurenine metabolites.	Kynurenine	177-187	solute carrier family 7 (cationic amino acid transporter, y+ system), member 5	Mus musculus	76-80
29988087-10	2019	Additional experiments using an in vitro model of the blood-brain barrier confirmed that kynurenine competes with leucine at the level of the amino acid transporter LAT1 for brain uptake.	Kynurenine	89-99	solute carrier family 7 (cationic amino acid transporter, y+ system), member 5	Mus musculus	165-169
31436417-9	2019	The muM affinity of polysulfides for IDO1 implicates these polysulfides as important signaling factors in immune regulation through the kynurenine pathway.	Kynurenine	136-146	indoleamine 2,3-dioxygenase 1	Homo sapiens	37-41
31076094-3	2019	A review of the literature has indicated that metabolites of the kynurenine pathway have the potential to; (i) induce vasorelaxation of resistance arteries and reduce blood pressure; (ii) exert antioxidant effects and reduce the effects of poly-ADP ribose polymerase activation (iii) prevent endothelial dysfunction and promote endothelial nitric oxide production; (iv) cause T cell differentiation into tolerogenic regulatory T cells and induce apoptosis of pro-inflammatory Th1 cells.	Kynurenine	65-75	poly(ADP-ribose) polymerase 1	Homo sapiens	240-266
31416966-0	2019	MYC promotes tryptophan uptake and metabolism by the kynurenine pathway in colon cancer.	Kynurenine	53-63	MYC proto-oncogene, bHLH transcription factor	Homo sapiens	0-3
31416966-4	2019	Using high-performance liquid chromatography (HPLC)-tandem mass spectrometry (LC-MS/MS), we found that MYC increased intracellular levels of tryptophan and tryptophan metabolites in the kynurenine pathway.	Kynurenine	186-196	MYC proto-oncogene, bHLH transcription factor	Homo sapiens	103-106
31416966-5	2019	MYC induced the expression of the tryptophan transporters SLC7A5 and SLC1A5 and the enzyme arylformamidase (AFMID), involved in the conversion of tryptophan into kynurenine.	Kynurenine	162-172	MYC proto-oncogene, bHLH transcription factor	Homo sapiens	0-3
31416966-5	2019	MYC induced the expression of the tryptophan transporters SLC7A5 and SLC1A5 and the enzyme arylformamidase (AFMID), involved in the conversion of tryptophan into kynurenine.	Kynurenine	162-172	solute carrier family 7 member 5	Homo sapiens	58-64
31416966-5	2019	MYC induced the expression of the tryptophan transporters SLC7A5 and SLC1A5 and the enzyme arylformamidase (AFMID), involved in the conversion of tryptophan into kynurenine.	Kynurenine	162-172	arylformamidase	Homo sapiens	108-113
31416966-9	2019	We found that only kynurenine and no other tryptophan metabolite promotes the nuclear translocation of the transcription factor aryl hydrocarbon receptor (AHR).	Kynurenine	19-29	aryl hydrocarbon receptor	Homo sapiens	128-153
31416966-9	2019	We found that only kynurenine and no other tryptophan metabolite promotes the nuclear translocation of the transcription factor aryl hydrocarbon receptor (AHR).	Kynurenine	19-29	aryl hydrocarbon receptor	Homo sapiens	155-158
31416966-11	2019	Therefore, we propose that limiting cellular kynurenine or its downstream targets could present a new strategy to reduce the proliferation of MYC-dependent cancer cells.	Kynurenine	45-55	MYC proto-oncogene, bHLH transcription factor	Homo sapiens	142-145
31194647-3	2019	The indoleamine 2,3 dioxygenase (IDO) gene encodes one of first enzymes (IDO) of the kynurenine pathway.	Kynurenine	85-95	indoleamine 2,3-dioxygenase 1	Homo sapiens	4-31
31194647-3	2019	The indoleamine 2,3 dioxygenase (IDO) gene encodes one of first enzymes (IDO) of the kynurenine pathway.	Kynurenine	85-95	indoleamine 2,3-dioxygenase 1	Homo sapiens	33-36
31194647-3	2019	The indoleamine 2,3 dioxygenase (IDO) gene encodes one of first enzymes (IDO) of the kynurenine pathway.	Kynurenine	85-95	indoleamine 2,3-dioxygenase 1	Homo sapiens	73-76
31434983-0	2019	Exhaustion of CD4+ T-cells mediated by the Kynurenine Pathway in Melanoma.	Kynurenine	43-53	CD4 molecule	Homo sapiens	14-17
31461509-8	2019	IDO1 is an enzyme that catabolizes cellular tryptophan to kynurenine metabolites thereby reducing tryptophan availability in cells.	Kynurenine	58-68	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).	Kynurenine	11-21	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).	Kynurenine	38-41	indoleamine 2,3-dioxygenase 1	Homo sapiens	180-183
31488951-5	2019	These are hepatic tryptophan 2,3-dioxygenase (TDO) activity and the flux of plasma-free Trp down the Kyn pathway.	Kynurenine	101-104	tryptophan 2,3-dioxygenase	Homo sapiens	46-49
31434983-1	2019	Kynurenine pathway (KP) activation by the enzymatic activity of indoleamine 2,3-dioxygenase1 (IDO1) and kynurenine (KYN) production represents an attractive target for reducing tumour progression and improving anti-tumour immunity in multiple cancers.	Kynurenine	0-10	indoleamine 2,3-dioxygenase 1	Homo sapiens	64-92
31434983-1	2019	Kynurenine pathway (KP) activation by the enzymatic activity of indoleamine 2,3-dioxygenase1 (IDO1) and kynurenine (KYN) production represents an attractive target for reducing tumour progression and improving anti-tumour immunity in multiple cancers.	Kynurenine	0-10	indoleamine 2,3-dioxygenase 1	Homo sapiens	94-98
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.	Kynurenine	69-79	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.	Kynurenine	69-79	indoleamine 2,3-dioxygenase 1	Homo sapiens	31-35
31481962-2	2019	L-kynurenine (Kyn), the first byproduct by IDO1, promotes immunoregulatory effects via activation of the Aryl hydrocarbon Receptor (AhR) in dendritic cells (DCs) and T lymphocytes.	Kynurenine	0-12	indoleamine 2,3-dioxygenase 1	Homo sapiens	43-47
31481962-2	2019	L-kynurenine (Kyn), the first byproduct by IDO1, promotes immunoregulatory effects via activation of the Aryl hydrocarbon Receptor (AhR) in dendritic cells (DCs) and T lymphocytes.	Kynurenine	0-12	aryl hydrocarbon receptor	Homo sapiens	105-130
31481962-2	2019	L-kynurenine (Kyn), the first byproduct by IDO1, promotes immunoregulatory effects via activation of the Aryl hydrocarbon Receptor (AhR) in dendritic cells (DCs) and T lymphocytes.	Kynurenine	0-12	aryl hydrocarbon receptor	Homo sapiens	132-135
31481962-2	2019	L-kynurenine (Kyn), the first byproduct by IDO1, promotes immunoregulatory effects via activation of the Aryl hydrocarbon Receptor (AhR) in dendritic cells (DCs) and T lymphocytes.	Kynurenine	14-17	indoleamine 2,3-dioxygenase 1	Homo sapiens	43-47
31481962-2	2019	L-kynurenine (Kyn), the first byproduct by IDO1, promotes immunoregulatory effects via activation of the Aryl hydrocarbon Receptor (AhR) in dendritic cells (DCs) and T lymphocytes.	Kynurenine	14-17	aryl hydrocarbon receptor	Homo sapiens	105-130
31481962-2	2019	L-kynurenine (Kyn), the first byproduct by IDO1, promotes immunoregulatory effects via activation of the Aryl hydrocarbon Receptor (AhR) in dendritic cells (DCs) and T lymphocytes.	Kynurenine	14-17	aryl hydrocarbon receptor	Homo sapiens	132-135
31481962-3	2019	We here identified the nuclear coactivator 7 (NCOA7) as a molecular target of 3-hydroxyanthranilic acid (3-HAA), a Trp metabolite produced downstream of Kyn along the kynurenine pathway.	Kynurenine	167-177	nuclear receptor coactivator 7	Homo sapiens	46-51
31481962-6	2019	In cocultures of CD4+ T cells with cDCs, the co-addition of Kyn and 3-HAA significantly increased the induction of Foxp3+ regulatory T cells and the production of immunosuppressive transforming growth factor beta in an NCOA7-dependent fashion.	Kynurenine	60-63	forkhead box P3	Homo sapiens	115-120
31481962-6	2019	In cocultures of CD4+ T cells with cDCs, the co-addition of Kyn and 3-HAA significantly increased the induction of Foxp3+ regulatory T cells and the production of immunosuppressive transforming growth factor beta in an NCOA7-dependent fashion.	Kynurenine	60-63	nuclear receptor coactivator 7	Homo sapiens	219-224
31176083-3	2019	99% of brain tryptophan metabolism via its degradation to kynurenine (KYN) catalyzed by indoleamine 2,3-dioxygenase (IDO).	Kynurenine	58-68	indoleamine 2,3-dioxygenase 1	Rattus norvegicus	88-115
31440253-7	2019	We also found that lactate enhances tryptophan metabolism and kynurenine production by pDCs which contribute to induction of FoxP3+ CD4+ regulatory T cells, the major immunosuppressive immune cell subset in tumor microenvironment.	Kynurenine	62-72	forkhead box P3	Homo sapiens	125-130
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).	Kynurenine	134-144	indoleamine 2,3-dioxygenase 1	Mus musculus	0-27
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).	Kynurenine	134-144	indoleamine 2,3-dioxygenase 1	Homo sapiens	29-32
31534532-0	2019	Galectin 3 protects from cisplatin-induced acute kidney injury by promoting TLR-2-dependent activation of IDO1/Kynurenine pathway in renal DCs.	Kynurenine	111-121	lectin, galactose binding, soluble 3	Mus musculus	0-10
31534532-0	2019	Galectin 3 protects from cisplatin-induced acute kidney injury by promoting TLR-2-dependent activation of IDO1/Kynurenine pathway in renal DCs.	Kynurenine	111-121	toll-like receptor 2	Mus musculus	76-81
31534532-0	2019	Galectin 3 protects from cisplatin-induced acute kidney injury by promoting TLR-2-dependent activation of IDO1/Kynurenine pathway in renal DCs.	Kynurenine	111-121	indoleamine 2,3-dioxygenase 1	Mus musculus	106-110
31176083-5	2019	KYN is further converted by kynurenine aminotransferase (KAT) to the more neuroprotective kynurenic acid or by kynurenine 3-monooxygenase (KMO) to neurotoxic 3-hydroxykynurenine.	Kynurenine	0-3	kynurenine 3-monooxygenase	Rattus norvegicus	111-137
31176083-5	2019	KYN is further converted by kynurenine aminotransferase (KAT) to the more neuroprotective kynurenic acid or by kynurenine 3-monooxygenase (KMO) to neurotoxic 3-hydroxykynurenine.	Kynurenine	0-3	kynurenine 3-monooxygenase	Rattus norvegicus	139-142
31176083-3	2019	99% of brain tryptophan metabolism via its degradation to kynurenine (KYN) catalyzed by indoleamine 2,3-dioxygenase (IDO).	Kynurenine	58-68	indoleamine 2,3-dioxygenase 1	Rattus norvegicus	117-120
31176083-3	2019	99% of brain tryptophan metabolism via its degradation to kynurenine (KYN) catalyzed by indoleamine 2,3-dioxygenase (IDO).	Kynurenine	70-73	indoleamine 2,3-dioxygenase 1	Rattus norvegicus	88-115
31176083-3	2019	99% of brain tryptophan metabolism via its degradation to kynurenine (KYN) catalyzed by indoleamine 2,3-dioxygenase (IDO).	Kynurenine	70-73	indoleamine 2,3-dioxygenase 1	Rattus norvegicus	117-120
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.	Kynurenine	129-141	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-29
31093659-5	2019	THP-1 macrophages mainly expressed IL-33 variant 5, which in turn was strongly induced by the AhR agonists 2, 3, 7, 8-tetrachlorodibenzo-p-dioxin (TCDD) and kynurenine (KYN).	Kynurenine	157-167	interleukin 33	Mus musculus	35-40
31093659-5	2019	THP-1 macrophages mainly expressed IL-33 variant 5, which in turn was strongly induced by the AhR agonists 2, 3, 7, 8-tetrachlorodibenzo-p-dioxin (TCDD) and kynurenine (KYN).	Kynurenine	157-167	aryl-hydrocarbon receptor	Mus musculus	94-97
31093659-5	2019	THP-1 macrophages mainly expressed IL-33 variant 5, which in turn was strongly induced by the AhR agonists 2, 3, 7, 8-tetrachlorodibenzo-p-dioxin (TCDD) and kynurenine (KYN).	Kynurenine	169-172	interleukin 33	Mus musculus	35-40
31093659-5	2019	THP-1 macrophages mainly expressed IL-33 variant 5, which in turn was strongly induced by the AhR agonists 2, 3, 7, 8-tetrachlorodibenzo-p-dioxin (TCDD) and kynurenine (KYN).	Kynurenine	169-172	aryl-hydrocarbon receptor	Mus musculus	94-97
31055163-0	2019	Correlation between plasma and CSF concentrations of kynurenine pathway metabolites in Alzheimer"s disease and relationship to amyloid-beta and tau.	Kynurenine	53-63	microtubule associated protein tau	Homo sapiens	144-147
31055163-6	2019	Furthermore, in AD CSF, increased 3-hydroxykynurenine/KYN ratio correlated with t-tau (r = 0.58, p = 0.009) and p-tau (r = 0.52, p = 0.020).	Kynurenine	54-57	microtubule associated protein tau	Homo sapiens	82-85
31055163-6	2019	Furthermore, in AD CSF, increased 3-hydroxykynurenine/KYN ratio correlated with t-tau (r = 0.58, p = 0.009) and p-tau (r = 0.52, p = 0.020).	Kynurenine	54-57	microtubule associated protein tau	Homo sapiens	114-117
31337401-10	2019	We observed a lower plasmatic tryptophan and a higher kynurenine/tryptophan ratio in hormone receptor-negative patients compared to hormone receptor-positive cancers.	Kynurenine	54-64	nuclear receptor subfamily 4 group A member 1	Homo sapiens	85-101
31337401-16	2019	The Kyn/Trp ratio and Trp also showed different values according to hormone receptor status, TNM stage, T grade and histology.	Kynurenine	4-7	nuclear receptor subfamily 4 group A member 1	Homo sapiens	68-84
31337401-16	2019	The Kyn/Trp ratio and Trp also showed different values according to hormone receptor status, TNM stage, T grade and histology.	Kynurenine	4-7	teneurin transmembrane protein 1	Homo sapiens	93-96
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.	Kynurenine	129-141	indoleamine 2,3-dioxygenase 1	Homo sapiens	31-35
31171720-3	2019	The AhR and its ligands also inhibit colon carcinogenesis, but it has been reported that the AhR and its ligand kynurenine enhance glioblastoma (GBM).	Kynurenine	112-122	aryl hydrocarbon receptor	Homo sapiens	4-7
31324754-12	2019	The combination of BET inhibitors with the IDO1 inhibitor further reduced L-kynurenine, though only marginally.	Kynurenine	74-86	indoleamine 2,3-dioxygenase 1	Homo sapiens	43-47
31315643-4	2019	Increased IDO1 expression strongly promoted cell migration via its metabolite kynurenine and was associated with pathways of immune activation according to GSEA (Gene Set Enrichment Analysis).	Kynurenine	78-88	indoleamine 2,3-dioxygenase 1	Homo sapiens	10-14
31315643-11	2019	This bioprocess was mediated by IDO1 metabolite kynurenine and integrin beta1.	Kynurenine	48-58	indoleamine 2,3-dioxygenase 1	Homo sapiens	32-36
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.	Kynurenine	67-77	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-27
31177094-6	2019	Deletion of kmo-1, which encodes a kynurenine 3-monooxygenase that converts KYN to 3HKYN, drastically reduced RQ but not Q levels.	Kynurenine	76-79	Kynurenine 3-monooxygenase	Caenorhabditis elegans	12-17
31177094-6	2019	Deletion of kmo-1, which encodes a kynurenine 3-monooxygenase that converts KYN to 3HKYN, drastically reduced RQ but not Q levels.	Kynurenine	76-79	FAD_binding_3 domain-containing protein	Caenorhabditis elegans	35-61
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.	Kynurenine	67-77	indoleamine 2,3-dioxygenase 1	Homo sapiens	29-32
30837717-8	2019	Exercise also increases the PGC1alpha-dependent muscular expression of kynurenine aminotransferase enzymes, which induces a beneficial shift in the balance between the neurotoxic kynurenine and the neuroprotective kynurenic acid, thereby reducing depression-like symptoms.	Kynurenine	71-81	PPARG coactivator 1 alpha	Homo sapiens	28-37
31115516-0	2019	Fr-HMGB1 and ds-HMGB1 activate the kynurenine pathway via different mechanisms in association with depressive-like behavior.	Kynurenine	35-45	high mobility group box 1	Homo sapiens	3-8
31115516-0	2019	Fr-HMGB1 and ds-HMGB1 activate the kynurenine pathway via different mechanisms in association with depressive-like behavior.	Kynurenine	35-45	high mobility group box 1	Homo sapiens	16-21
31115516-2	2019	In the present study, the induction of depression via the kynurenine pathway by different redox states of HMGB1 was investigated in vivo and in vitro.	Kynurenine	58-68	high mobility group box 1	Homo sapiens	106-111
31115516-5	2019	Following intracerebroventricular injection of ds- and fr-HMGB1, behavioral tests were performed, revealing the presentation of depressive-like behavior, and essential proteins in the kynurenine pathway were demonstrated to be upregulated at the mRNA level, suggesting that ds- and fr-HMGB1 contributed to the development of this behavior via the kynurenine pathway.	Kynurenine	184-194	high mobility group box 1	Homo sapiens	58-63
31115516-5	2019	Following intracerebroventricular injection of ds- and fr-HMGB1, behavioral tests were performed, revealing the presentation of depressive-like behavior, and essential proteins in the kynurenine pathway were demonstrated to be upregulated at the mRNA level, suggesting that ds- and fr-HMGB1 contributed to the development of this behavior via the kynurenine pathway.	Kynurenine	184-194	high mobility group box 1	Homo sapiens	285-290
31115516-5	2019	Following intracerebroventricular injection of ds- and fr-HMGB1, behavioral tests were performed, revealing the presentation of depressive-like behavior, and essential proteins in the kynurenine pathway were demonstrated to be upregulated at the mRNA level, suggesting that ds- and fr-HMGB1 contributed to the development of this behavior via the kynurenine pathway.	Kynurenine	347-357	high mobility group box 1	Homo sapiens	58-63
31115516-6	2019	ds-HMGB1 directly activated the kynurenine pathway and cytokines such as tumor necrosis factor-alpha (TNF-alpha) and interleukin-1beta (IL-1beta) in the hippocampal tissue.	Kynurenine	32-42	high mobility group box 1	Homo sapiens	3-8
31115516-8	2019	These findings indicated that ds-HMGB1 induced depression in a manner associated with the kynurenine pathway, whereas oxidation of fr-HMGB1 evoked activation of the kynurenine pathway, resulting in depressive behavior.	Kynurenine	90-100	high mobility group box 1	Homo sapiens	33-38
31115516-8	2019	These findings indicated that ds-HMGB1 induced depression in a manner associated with the kynurenine pathway, whereas oxidation of fr-HMGB1 evoked activation of the kynurenine pathway, resulting in depressive behavior.	Kynurenine	165-175	high mobility group box 1	Homo sapiens	134-139
31239324-3	2019	In undifferentiated hESCs, kynurenine stimulated the AhR to promote the expression of self-renewal genes.	Kynurenine	27-37	aryl hydrocarbon receptor	Homo sapiens	53-56
31247950-2	2019	Kynurenine (KYN), known to be associated with disturbed mental health, can be metabolized in muscle by kynurenine aminotransferases (KAT) 1-4.	Kynurenine	0-10	kynurenine aminotransferase 1	Homo sapiens	103-141
31247950-2	2019	Kynurenine (KYN), known to be associated with disturbed mental health, can be metabolized in muscle by kynurenine aminotransferases (KAT) 1-4.	Kynurenine	12-15	kynurenine aminotransferase 1	Homo sapiens	103-141
31239324-0	2019	Kynurenine signaling through the aryl hydrocarbon receptor maintains the undifferentiated state of human embryonic stem cells.	Kynurenine	0-10	aryl hydrocarbon receptor	Homo sapiens	33-58
31239324-8	2019	When ESCs were induced to undergo ectodermal differentiation, the abundance of kynurenine in the medium was reduced through activation of the main kynurenine catabolic pathway mediated by kynurenine aminotransferase 2 (KAT2, also known as AADAT), resulting in the secretion of 2-aminoadipic acid (2-AAA) into the culture medium.	Kynurenine	79-89	aminoadipate aminotransferase	Homo sapiens	188-217
31239324-1	2019	Kynurenine, which is generated from tryptophan by indoleamine 2,3-dioxygenase 1 (IDO1), binds to the aryl hydrocarbon receptor (AhR).	Kynurenine	0-10	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).	Kynurenine	0-10	indoleamine 2,3-dioxygenase 1	Homo sapiens	81-85
31239324-8	2019	When ESCs were induced to undergo ectodermal differentiation, the abundance of kynurenine in the medium was reduced through activation of the main kynurenine catabolic pathway mediated by kynurenine aminotransferase 2 (KAT2, also known as AADAT), resulting in the secretion of 2-aminoadipic acid (2-AAA) into the culture medium.	Kynurenine	79-89	aminoadipate aminotransferase	Homo sapiens	219-223
31239324-1	2019	Kynurenine, which is generated from tryptophan by indoleamine 2,3-dioxygenase 1 (IDO1), binds to the aryl hydrocarbon receptor (AhR).	Kynurenine	0-10	aryl hydrocarbon receptor	Homo sapiens	101-126
31239324-1	2019	Kynurenine, which is generated from tryptophan by indoleamine 2,3-dioxygenase 1 (IDO1), binds to the aryl hydrocarbon receptor (AhR).	Kynurenine	0-10	aryl hydrocarbon receptor	Homo sapiens	128-131
31239324-8	2019	When ESCs were induced to undergo ectodermal differentiation, the abundance of kynurenine in the medium was reduced through activation of the main kynurenine catabolic pathway mediated by kynurenine aminotransferase 2 (KAT2, also known as AADAT), resulting in the secretion of 2-aminoadipic acid (2-AAA) into the culture medium.	Kynurenine	79-89	aminoadipate aminotransferase	Homo sapiens	239-244
31239324-8	2019	When ESCs were induced to undergo ectodermal differentiation, the abundance of kynurenine in the medium was reduced through activation of the main kynurenine catabolic pathway mediated by kynurenine aminotransferase 2 (KAT2, also known as AADAT), resulting in the secretion of 2-aminoadipic acid (2-AAA) into the culture medium.	Kynurenine	147-157	aminoadipate aminotransferase	Homo sapiens	188-217
31316502-10	2019	KYNA and KYNA analogs have an important role in influencing TSG-6 expression, and there is a possible benefit of targeting TSG-6 expression by kynurenines in inflammatory conditions following infections.	Kynurenine	143-154	TNF alpha induced protein 6	Homo sapiens	123-128
31249813-8	2019	Detection of the tryptophan degradation product kynurenine and the impact of IDO inhibition on Chlamydia muridarum growth proved that the IDO1-2 proteins were functionally active.	Kynurenine	48-58	indoleamine 2,3-dioxygenase 1	Mus musculus	138-144
31212870-6	2019	Also, thyroid cancer cells produce kynurenine using IDO, which causes NK cell dysfunction.	Kynurenine	35-45	indoleamine 2,3-dioxygenase 1	Homo sapiens	52-55
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.	Kynurenine	151-161	indoleamine 2,3-dioxygenase 1	Homo sapiens	78-82
31212870-7	2019	Kynurenine enters NK cells via the aryl hydrocarbon receptor (AhR) on the surfaces of the NK cells, which decreases NK cell function and NK receptor expression via the signal transducer and activator of transcription (STAT) 1 and STAT3 pathways.	Kynurenine	0-10	aryl hydrocarbon receptor	Homo sapiens	35-60
31212870-7	2019	Kynurenine enters NK cells via the aryl hydrocarbon receptor (AhR) on the surfaces of the NK cells, which decreases NK cell function and NK receptor expression via the signal transducer and activator of transcription (STAT) 1 and STAT3 pathways.	Kynurenine	0-10	aryl hydrocarbon receptor	Homo sapiens	62-65
31212870-7	2019	Kynurenine enters NK cells via the aryl hydrocarbon receptor (AhR) on the surfaces of the NK cells, which decreases NK cell function and NK receptor expression via the signal transducer and activator of transcription (STAT) 1 and STAT3 pathways.	Kynurenine	0-10	killer cell immunoglobulin like receptor, three Ig domains and long cytoplasmic tail 1	Homo sapiens	137-148
31212870-7	2019	Kynurenine enters NK cells via the aryl hydrocarbon receptor (AhR) on the surfaces of the NK cells, which decreases NK cell function and NK receptor expression via the signal transducer and activator of transcription (STAT) 1 and STAT3 pathways.	Kynurenine	0-10	signal transducer and activator of transcription 1	Homo sapiens	168-225
31212870-7	2019	Kynurenine enters NK cells via the aryl hydrocarbon receptor (AhR) on the surfaces of the NK cells, which decreases NK cell function and NK receptor expression via the signal transducer and activator of transcription (STAT) 1 and STAT3 pathways.	Kynurenine	0-10	signal transducer and activator of transcription 3	Homo sapiens	230-235
31212870-9	2019	Conclusively, NK cell function may be impaired in thyroid cancer patients by IDO-induced kynurenine production.	Kynurenine	89-99	indoleamine 2,3-dioxygenase 1	Homo sapiens	77-80
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.	Kynurenine	78-88	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.	Kynurenine	78-88	indoleamine 2,3-dioxygenase 1	Homo sapiens	29-32
30121843-12	2019	Our findings indicate a role of the kynurenine pathway in the development of PDS, rs10108662 genetic polymorphism resulting in changes of IDO activity might contribute to PDS pathogenesis.	Kynurenine	36-46	indoleamine 2,3-dioxygenase 1	Homo sapiens	138-141
30933897-1	2019	Indoleamine-2,3-dioxygenase (IDO1) is an enzyme which converts tryptophan (Trp) into kynurenine (Kyn).	Kynurenine	85-95	indoleamine 2,3-dioxygenase 1	Mus musculus	29-33
30933897-1	2019	Indoleamine-2,3-dioxygenase (IDO1) is an enzyme which converts tryptophan (Trp) into kynurenine (Kyn).	Kynurenine	97-100	indoleamine 2,3-dioxygenase 1	Mus musculus	29-33
30933897-2	2019	Having a critical role in tumor immune escape by decreasing Trp and increasing Kyn levels in the microenvironment, IDO1 was one of the first targets for small molecules drug discovery in the field of immuno-oncology.	Kynurenine	79-82	indoleamine 2,3-dioxygenase 1	Mus musculus	115-119
31082908-2	2019	SUMMARY BACKGROUND DATA: IDO1 is a primary enzyme that generates immunosuppressive metabolites such as tryptophan and kynurenine.	Kynurenine	118-128	indoleamine 2,3-dioxygenase 1	Homo sapiens	25-29
30715395-9	2019	Higher kynurenine concentrations were significantly associated with higher TRAP-5b and RANKL levels, but not with BSALP and OPG levels, in BM plasma.	Kynurenine	7-17	TNF superfamily member 11	Homo sapiens	87-92
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).	Kynurenine	93-103	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).	Kynurenine	105-108	indoleamine 2,3-dioxygenase 1	Homo sapiens	9-13
30689168-0	2019	Involvement of Aryl Hydrocarbon Receptor in L-Kynurenine-Mediated Parathyroid Hormone-Related Peptide Expression.	Kynurenine	44-56	aryl hydrocarbon receptor	Homo sapiens	15-40
30689168-0	2019	Involvement of Aryl Hydrocarbon Receptor in L-Kynurenine-Mediated Parathyroid Hormone-Related Peptide Expression.	Kynurenine	44-56	parathyroid hormone like hormone	Homo sapiens	66-101
30689168-7	2019	Additionally, L-Kyn (50 muM) increased the expression of the nuclear translocation of Ahr and cytochrome P450 1A1.	Kynurenine	14-19	aryl hydrocarbon receptor	Homo sapiens	86-89
30689168-7	2019	Additionally, L-Kyn (50 muM) increased the expression of the nuclear translocation of Ahr and cytochrome P450 1A1.	Kynurenine	14-19	cytochrome P450 family 1 subfamily A member 1	Homo sapiens	94-113
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.	Kynurenine	21-31	indoleamine 2,3-dioxygenase 1	Homo sapiens	174-201
30952082-6	2019	Furthermore, complex 3 was effective to enhance T-cell immune responses by inhibiting the TDO enzyme expression to block the kynurenine production and inactivating the downstream of aryl hydrocarbon receptor (AHR).	Kynurenine	125-135	tryptophan 2,3-dioxygenase	Homo sapiens	90-93
31153376-1	2019	BACKGROUND: Indoleamine 2, 3-dioxygenase 1 (IDO) is responsible for the progression of the kynurenine pathway.	Kynurenine	91-101	indoleamine 2,3-dioxygenase 1	Mus musculus	12-42
31153376-1	2019	BACKGROUND: Indoleamine 2, 3-dioxygenase 1 (IDO) is responsible for the progression of the kynurenine pathway.	Kynurenine	91-101	indoleamine 2,3-dioxygenase 1	Mus musculus	44-47
31093946-0	2019	Involvement of miR-30b in kynurenine-mediated lysyl oxidase expression.	Kynurenine	26-36	microRNA 30b	Homo sapiens	15-22
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.	Kynurenine	21-31	indoleamine 2,3-dioxygenase 1	Homo sapiens	203-206
31093946-0	2019	Involvement of miR-30b in kynurenine-mediated lysyl oxidase expression.	Kynurenine	26-36	lysyl oxidase	Homo sapiens	46-59
31093946-8	2019	Most importantly, not only was Kyn-induced increase of LOX mRNA significantly attenuated on miR-30b mimics treatment, but also Kyn-mediated the upregulation of the mRNA, and secreted levels of LOX were distinctly strengthened on miR-30b inhibitor treatment.	Kynurenine	31-34	lysyl oxidase	Homo sapiens	55-58
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.	Kynurenine	240-250	indoleamine 2,3-dioxygenase 1	Homo sapiens	174-201
31093946-8	2019	Most importantly, not only was Kyn-induced increase of LOX mRNA significantly attenuated on miR-30b mimics treatment, but also Kyn-mediated the upregulation of the mRNA, and secreted levels of LOX were distinctly strengthened on miR-30b inhibitor treatment.	Kynurenine	31-34	microRNA 30b	Homo sapiens	92-99
31093946-8	2019	Most importantly, not only was Kyn-induced increase of LOX mRNA significantly attenuated on miR-30b mimics treatment, but also Kyn-mediated the upregulation of the mRNA, and secreted levels of LOX were distinctly strengthened on miR-30b inhibitor treatment.	Kynurenine	31-34	lysyl oxidase	Homo sapiens	193-196
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.	Kynurenine	240-250	indoleamine 2,3-dioxygenase 1	Homo sapiens	203-206
31093946-8	2019	Most importantly, not only was Kyn-induced increase of LOX mRNA significantly attenuated on miR-30b mimics treatment, but also Kyn-mediated the upregulation of the mRNA, and secreted levels of LOX were distinctly strengthened on miR-30b inhibitor treatment.	Kynurenine	31-34	microRNA 30b	Homo sapiens	229-236
30959226-6	2019	In patients, IL-2R levels, which are involved in the regulation of IDO, were significantly associated with levels of kynurenine (p = .029), but this association was not observed in controls.	Kynurenine	117-127	interleukin 2 receptor subunit alpha	Homo sapiens	13-18
30959226-6	2019	In patients, IL-2R levels, which are involved in the regulation of IDO, were significantly associated with levels of kynurenine (p = .029), but this association was not observed in controls.	Kynurenine	117-127	indoleamine 2,3-dioxygenase 1	Homo sapiens	67-70
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.	Kynurenine	38-48	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-4
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).	Kynurenine	92-102	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).	Kynurenine	104-107	indoleamine 2,3-dioxygenase 1	Homo sapiens	58-61
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.	Kynurenine	63-73	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-3
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.	Kynurenine	75-78	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.	Kynurenine	152-162	indoleamine 2,3-dioxygenase 1	Homo sapiens	30-59
31098404-5	2019	L-Ornithine increases the level of aryl hydrocarbon receptor ligand L-kynurenine produced from tryptophan metabolism in gut epithelial cells, which in turn increases RORgammat (+)IL-22(+) ILC3 cells.	Kynurenine	68-80	interleukin 22	Homo sapiens	179-184
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.	Kynurenine	152-162	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.	Kynurenine	152-162	indoleamine 2,3-dioxygenase 1	Homo sapiens	247-251
30962630-2	2019	Here we report that kynurenine produced by glioblastoma cells activates aryl hydrocarbon receptor (AHR) in TAMs to modulate their function and T cell immunity.	Kynurenine	20-30	aryl hydrocarbon receptor	Homo sapiens	72-97
30623620-7	2019	IDO-1 enzyme activity was calculated using tryptophan and kynurenine levels.	Kynurenine	58-68	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-5
30962630-2	2019	Here we report that kynurenine produced by glioblastoma cells activates aryl hydrocarbon receptor (AHR) in TAMs to modulate their function and T cell immunity.	Kynurenine	20-30	aryl hydrocarbon receptor	Homo sapiens	99-102
30107503-1	2019	BACKGROUND: Indoleamine 2,3-dioxygenase (IDO) is an immunoregulatory enzyme that metabolizes tryptophan to immunosuppressive kynurenines.	Kynurenine	125-136	indoleamine 2,3-dioxygenase 1	Homo sapiens	41-44
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).	Kynurenine	89-100	indoleamine 2,3-dioxygenase 1	Homo sapiens	39-43
30844963-1	2019	The amino-acid tryptophan (TRY) is converted into kynurenine (KYN) and subsequent metabolites by the tryptophan/catabolites (TRY/CAT) pathway (kynurenine pathway).	Kynurenine	50-60	catalase	Homo sapiens	129-132
30844963-1	2019	The amino-acid tryptophan (TRY) is converted into kynurenine (KYN) and subsequent metabolites by the tryptophan/catabolites (TRY/CAT) pathway (kynurenine pathway).	Kynurenine	62-65	catalase	Homo sapiens	129-132
30844963-1	2019	The amino-acid tryptophan (TRY) is converted into kynurenine (KYN) and subsequent metabolites by the tryptophan/catabolites (TRY/CAT) pathway (kynurenine pathway).	Kynurenine	143-153	catalase	Homo sapiens	129-132
30844963-6	2019	We propose a comprehensive survey of the TRY/CAT pathway (kynurenine pathway) abnormalities in stress and inflammation-induced MDD and neurodegenerative diseases.	Kynurenine	58-68	catalase	Homo sapiens	45-48
30770561-2	2019	Indoleamine 2,3-dioxygenase 1 (Ido1) is induced by inflammatory cytokines and functions to metabolize tryptophan to kynurenine.	Kynurenine	116-126	indoleamine 2,3-dioxygenase 1	Mus musculus	0-29
30770561-2	2019	Indoleamine 2,3-dioxygenase 1 (Ido1) is induced by inflammatory cytokines and functions to metabolize tryptophan to kynurenine.	Kynurenine	116-126	indoleamine 2,3-dioxygenase 1	Mus musculus	31-35
30712941-9	2019	This enzyme converts tryptophan to kynurenine, which alters immune function by creating a localized tryptophan deficiency and by activation of the aryl hydrocarbon receptor and induction of downstream tolerogenic mediators.	Kynurenine	35-45	LOC522736	Bos taurus	147-172
30679179-0	2019	IDO1 and Kynurenine Pathway Metabolites Activate PI3K-Akt Signaling in the Neoplastic Colon Epithelium to Promote Cancer Cell Proliferation and Inhibit Apoptosis.	Kynurenine	9-19	thymoma viral proto-oncogene 1	Mus musculus	54-57
30679179-2	2019	We previously demonstrated that the IDO1-kynurenine pathway (KP) also directly supports colorectal cancer growth by promoting activation of beta-catenin and driving neoplastic growth in mice lacking intact adaptive immunity.	Kynurenine	41-51	indoleamine 2,3-dioxygenase 1	Mus musculus	36-40
30679179-2	2019	We previously demonstrated that the IDO1-kynurenine pathway (KP) also directly supports colorectal cancer growth by promoting activation of beta-catenin and driving neoplastic growth in mice lacking intact adaptive immunity.	Kynurenine	41-51	catenin (cadherin associated protein), beta 1	Mus musculus	140-152
30862026-2	2019	Interferon gamma-inducible (the production of which is dependent on the IFNgamma rs2430561 polymorphism) tryptophan-kynurenine inflammatory cascade helps to understand the increased association between inflammatory process and MetS, which is why we seek the relationship between the IFNgamma gene polymorphisms and serum levels of markers of interferon-gamma (IFNgamma)-inducible inflammatory cascade.	Kynurenine	116-126	interferon gamma	Homo sapiens	72-80
30930794-4	2019	The present study describes a mechanism by which liver CEBPbeta (CCAAT/enhancer-binding protein beta) induced by hypoxic environment alters the kynurenine (KYN) metabolism and causes the suppression of motility function recession.	Kynurenine	144-154	CCAAT/enhancer binding protein (C/EBP), beta	Mus musculus	55-63
30930794-4	2019	The present study describes a mechanism by which liver CEBPbeta (CCAAT/enhancer-binding protein beta) induced by hypoxic environment alters the kynurenine (KYN) metabolism and causes the suppression of motility function recession.	Kynurenine	144-154	CCAAT/enhancer binding protein (C/EBP), beta	Mus musculus	65-100
30930794-4	2019	The present study describes a mechanism by which liver CEBPbeta (CCAAT/enhancer-binding protein beta) induced by hypoxic environment alters the kynurenine (KYN) metabolism and causes the suppression of motility function recession.	Kynurenine	156-159	CCAAT/enhancer binding protein (C/EBP), beta	Mus musculus	55-63
30930794-4	2019	The present study describes a mechanism by which liver CEBPbeta (CCAAT/enhancer-binding protein beta) induced by hypoxic environment alters the kynurenine (KYN) metabolism and causes the suppression of motility function recession.	Kynurenine	156-159	CCAAT/enhancer binding protein (C/EBP), beta	Mus musculus	65-100
30930794-5	2019	The activation of CEBPbeta under hypoxia increases the liver expression of tryptophan dioxygenase, thereby enhancing the conversion of tryptophan into KYN; the KYN metabolite can traverse the blood-brain barrier and result in the suppression of motility function.	Kynurenine	151-154	CCAAT/enhancer binding protein (C/EBP), beta	Mus musculus	18-26
30862026-2	2019	Interferon gamma-inducible (the production of which is dependent on the IFNgamma rs2430561 polymorphism) tryptophan-kynurenine inflammatory cascade helps to understand the increased association between inflammatory process and MetS, which is why we seek the relationship between the IFNgamma gene polymorphisms and serum levels of markers of interferon-gamma (IFNgamma)-inducible inflammatory cascade.	Kynurenine	116-126	interferon gamma	Homo sapiens	283-291
30862026-2	2019	Interferon gamma-inducible (the production of which is dependent on the IFNgamma rs2430561 polymorphism) tryptophan-kynurenine inflammatory cascade helps to understand the increased association between inflammatory process and MetS, which is why we seek the relationship between the IFNgamma gene polymorphisms and serum levels of markers of interferon-gamma (IFNgamma)-inducible inflammatory cascade.	Kynurenine	116-126	interferon gamma	Homo sapiens	342-358
30862026-2	2019	Interferon gamma-inducible (the production of which is dependent on the IFNgamma rs2430561 polymorphism) tryptophan-kynurenine inflammatory cascade helps to understand the increased association between inflammatory process and MetS, which is why we seek the relationship between the IFNgamma gene polymorphisms and serum levels of markers of interferon-gamma (IFNgamma)-inducible inflammatory cascade.	Kynurenine	116-126	interferon gamma	Homo sapiens	283-291
30862026-6	2019	In the group with MetS, the A/T genotype of the IFNgamma gene was accompanied by higher kynurenine levels.	Kynurenine	88-98	interferon gamma	Homo sapiens	48-56
30862026-8	2019	A disparity in the kynurenine level, as well as the relationship between the presence of the A/T genotype of the IFNgamma gene and a higher level of kynurenine in the group of women with MetS, may indicate an association between inflammation, metabolic disorders and tryptophan-kynurenine inflammatory cascade.	Kynurenine	149-159	interferon gamma	Homo sapiens	113-121
30862026-8	2019	A disparity in the kynurenine level, as well as the relationship between the presence of the A/T genotype of the IFNgamma gene and a higher level of kynurenine in the group of women with MetS, may indicate an association between inflammation, metabolic disorders and tryptophan-kynurenine inflammatory cascade.	Kynurenine	149-159	interferon gamma	Homo sapiens	113-121
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.	Kynurenine	110-120	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-28
30832615-1	2019	BACKGROUND: Indoleamine 2, 3-dioxygenase (IDO) is a key enzyme in the degradation of tryptophan (Trp) to kynurenine (Kyn).	Kynurenine	105-115	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).	Kynurenine	105-115	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).	Kynurenine	117-120	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).	Kynurenine	117-120	indoleamine 2,3-dioxygenase 1	Homo sapiens	42-45
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.	Kynurenine	110-120	indoleamine 2,3-dioxygenase 1	Homo sapiens	30-33
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.	Kynurenine	142-152	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.	Kynurenine	142-152	indoleamine 2,3-dioxygenase 1	Homo sapiens	87-90
30760699-3	2019	We show that KMO is highly expressed in the kidney and exerts major metabolic control over the biologically active kynurenine metabolites 3-hydroxykynurenine, kynurenic acid, and downstream metabolites.	Kynurenine	115-125	kynurenine 3-monooxygenase (kynurenine 3-hydroxylase)	Mus musculus	13-16
30377198-0	2019	Reimagining IDO Pathway Inhibition in Cancer Immunotherapy via Downstream Focus on the Tryptophan-Kynurenine-Aryl Hydrocarbon Axis.	Kynurenine	98-108	indoleamine 2,3-dioxygenase 1	Homo sapiens	12-15
30585477-1	2019	The heme enzyme indoleamine 2,3-dioxygenase-1 (IDO1) catalyzes the first reaction of l-tryptophan oxidation along the kynurenine pathway.	Kynurenine	118-128	indoleamine 2,3-dioxygenase 1	Homo sapiens	47-51
30800661-0	2019	Modulation of Enzyme Activity in the Kynurenine Pathway by Kynurenine Monooxygenase Inhibition.	Kynurenine	37-47	kynurenine 3-monooxygenase	Rattus norvegicus	59-83
30800661-6	2019	The first generation of KMO inhibitors was based on structural analogs of the substrate, L-kynurenine.	Kynurenine	89-101	kynurenine 3-monooxygenase	Rattus norvegicus	24-27
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.	Kynurenine	132-142	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-29
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.	Kynurenine	132-142	indoleamine 2,3-dioxygenase 1	Homo sapiens	31-35
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.	Kynurenine	132-142	tryptophan 2,3-dioxygenase	Homo sapiens	71-75
30987575-9	2019	Incubation of the cells with AhR blocker either alone or together with L-kynurenine or L-tryptophan resulted in the opposite effect, leading to the downregulation of IAPs and Bcl-2, upregulation of Bax and caspases expression.	Kynurenine	71-83	aryl hydrocarbon receptor	Homo sapiens	29-32
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.	Kynurenine	159-162	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.	Kynurenine	159-162	indoleamine 2,3-dioxygenase 1	Homo sapiens	224-229
30666511-4	2019	The stage of liver disease and grade of liver biopsies in AIH-1 patients negatively correlated with the Kyn/Trp ratios.The serum Kyn levels and Kyn/Trp ratio of AIH patients, within or below the normal range, indicate a trend of IDO activity lower than non-autoimmune WD or AATD.	Kynurenine	104-107	amelogenin X-linked	Homo sapiens	58-63
30666511-4	2019	The stage of liver disease and grade of liver biopsies in AIH-1 patients negatively correlated with the Kyn/Trp ratios.The serum Kyn levels and Kyn/Trp ratio of AIH patients, within or below the normal range, indicate a trend of IDO activity lower than non-autoimmune WD or AATD.	Kynurenine	129-132	amelogenin X-linked	Homo sapiens	58-63
30666511-4	2019	The stage of liver disease and grade of liver biopsies in AIH-1 patients negatively correlated with the Kyn/Trp ratios.The serum Kyn levels and Kyn/Trp ratio of AIH patients, within or below the normal range, indicate a trend of IDO activity lower than non-autoimmune WD or AATD.	Kynurenine	129-132	indoleamine 2,3-dioxygenase 1	Homo sapiens	229-232
30666511-4	2019	The stage of liver disease and grade of liver biopsies in AIH-1 patients negatively correlated with the Kyn/Trp ratios.The serum Kyn levels and Kyn/Trp ratio of AIH patients, within or below the normal range, indicate a trend of IDO activity lower than non-autoimmune WD or AATD.	Kynurenine	129-132	amelogenin X-linked	Homo sapiens	58-63
30666511-4	2019	The stage of liver disease and grade of liver biopsies in AIH-1 patients negatively correlated with the Kyn/Trp ratios.The serum Kyn levels and Kyn/Trp ratio of AIH patients, within or below the normal range, indicate a trend of IDO activity lower than non-autoimmune WD or AATD.	Kynurenine	129-132	indoleamine 2,3-dioxygenase 1	Homo sapiens	229-232
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.	Kynurenine	76-86	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.	Kynurenine	76-86	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.	Kynurenine	76-86	indoleamine 2,3-dioxygenase 1	Homo sapiens	118-121
30567628-14	2019	While there were changes in kynurenine metabolites in response to IFN-alpha, there was no association with persistent fatigue.	Kynurenine	28-38	interferon alpha 1	Homo sapiens	66-75
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.	Kynurenine	82-92	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.	Kynurenine	82-92	indoleamine 2,3-dioxygenase 1	Homo sapiens	46-49
30987575-9	2019	Incubation of the cells with AhR blocker either alone or together with L-kynurenine or L-tryptophan resulted in the opposite effect, leading to the downregulation of IAPs and Bcl-2, upregulation of Bax and caspases expression.	Kynurenine	71-83	BCL2 apoptosis regulator	Homo sapiens	175-180
30987575-9	2019	Incubation of the cells with AhR blocker either alone or together with L-kynurenine or L-tryptophan resulted in the opposite effect, leading to the downregulation of IAPs and Bcl-2, upregulation of Bax and caspases expression.	Kynurenine	71-83	BCL2 associated X, apoptosis regulator	Homo sapiens	198-201
30987575-9	2019	Incubation of the cells with AhR blocker either alone or together with L-kynurenine or L-tryptophan resulted in the opposite effect, leading to the downregulation of IAPs and Bcl-2, upregulation of Bax and caspases expression.	Kynurenine	71-83	caspase 9	Homo sapiens	206-214
30987575-10	2019	CONCLUSION: 1) L-kynurenine and its precursor promote anti-apoptotic effects through the modulation of IDOdependent pathway and regulation of IAPs, Bcl-2 and NF-kappaB family members in pancreatic carcinoma cells 2) inhibition of AhR by CH223191 exerts an apoptosis-promoting effect, and this observation might suggest the potential use of this compound in pancreatic cancer therapy.	Kynurenine	15-27	BCL2 apoptosis regulator	Homo sapiens	148-153
30987575-10	2019	CONCLUSION: 1) L-kynurenine and its precursor promote anti-apoptotic effects through the modulation of IDOdependent pathway and regulation of IAPs, Bcl-2 and NF-kappaB family members in pancreatic carcinoma cells 2) inhibition of AhR by CH223191 exerts an apoptosis-promoting effect, and this observation might suggest the potential use of this compound in pancreatic cancer therapy.	Kynurenine	15-27	aryl hydrocarbon receptor	Homo sapiens	230-233
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.	Kynurenine	141-151	indoleamine 2,3-dioxygenase 1	Homo sapiens	33-61
30987575-1	2019	BACKGROUND: L-kynurenine, derivate of L-tryptophan, is synthetized by indoleamine 2,3-dioxygenase (IDO).	Kynurenine	12-24	indoleamine 2,3-dioxygenase 1	Homo sapiens	70-97
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.	Kynurenine	141-151	indoleamine 2,3-dioxygenase 1	Homo sapiens	63-66
30987575-1	2019	BACKGROUND: L-kynurenine, derivate of L-tryptophan, is synthetized by indoleamine 2,3-dioxygenase (IDO).	Kynurenine	12-24	indoleamine 2,3-dioxygenase 1	Homo sapiens	99-102
30987575-2	2019	The effects of L-kynurenine depend on its binding to an aryl hydrocarbon receptor (AhR).	Kynurenine	15-27	aryl hydrocarbon receptor	Homo sapiens	56-81
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.	Kynurenine	153-156	indoleamine 2,3-dioxygenase 1	Homo sapiens	33-61
30987575-2	2019	The effects of L-kynurenine depend on its binding to an aryl hydrocarbon receptor (AhR).	Kynurenine	15-27	aryl hydrocarbon receptor	Homo sapiens	83-86
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.	Kynurenine	153-156	indoleamine 2,3-dioxygenase 1	Homo sapiens	63-66
30987575-3	2019	OBJECTIVE: The aim of this study was to investigate the changes within the apoptotic pathway in PANC-1 cells subjected to L-kynurenine or L-tryptophan considering the production of anti-apoptotic proteins from the IAPs and Bcl-2 family, as well as the regulation of NF-kappaB signaling.	Kynurenine	122-134	BCL2 apoptosis regulator	Homo sapiens	223-228
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.	Kynurenine	10-13	indoleamine 2,3-dioxygenase 1	Homo sapiens	79-83
31464185-3	2019	Indoleamine 2,3-dioxygenase (IDO) is an enzyme that catalyses degradation of tryptophan (Trp) through the kynurenine (Kyn) pathway; it can control inflammation and immune response by inducing Trp starvation.	Kynurenine	106-116	indoleamine 2,3-dioxygenase 1	Mus musculus	0-27
30987575-6	2019	RESULTS: Incubation of PANC-1 cells with L-kynurenine or L-tryptophan resulted in the increase in antiapoptotic cIAP-1, cIAP-2, XIAP and Bcl-2 expression and a decrease in pro-apoptotic Bax.	Kynurenine	41-53	baculoviral IAP repeat containing 2	Homo sapiens	112-118
30987575-6	2019	RESULTS: Incubation of PANC-1 cells with L-kynurenine or L-tryptophan resulted in the increase in antiapoptotic cIAP-1, cIAP-2, XIAP and Bcl-2 expression and a decrease in pro-apoptotic Bax.	Kynurenine	41-53	baculoviral IAP repeat containing 3	Homo sapiens	120-126
30987575-6	2019	RESULTS: Incubation of PANC-1 cells with L-kynurenine or L-tryptophan resulted in the increase in antiapoptotic cIAP-1, cIAP-2, XIAP and Bcl-2 expression and a decrease in pro-apoptotic Bax.	Kynurenine	41-53	X-linked inhibitor of apoptosis	Homo sapiens	128-132
30987575-6	2019	RESULTS: Incubation of PANC-1 cells with L-kynurenine or L-tryptophan resulted in the increase in antiapoptotic cIAP-1, cIAP-2, XIAP and Bcl-2 expression and a decrease in pro-apoptotic Bax.	Kynurenine	41-53	BCL2 apoptosis regulator	Homo sapiens	137-142
30987575-6	2019	RESULTS: Incubation of PANC-1 cells with L-kynurenine or L-tryptophan resulted in the increase in antiapoptotic cIAP-1, cIAP-2, XIAP and Bcl-2 expression and a decrease in pro-apoptotic Bax.	Kynurenine	41-53	BCL2 associated X, apoptosis regulator	Homo sapiens	186-189
30407222-5	2019	Exercise training activation of kynurenine pathway in skeletal muscles increases lipid metabolism and thermogenesis, and it limits weight gain, inflammation, insulin resistance, and glucose intolerance in rodents fed a high-fat diet.	Kynurenine	32-42	insulin	Homo sapiens	158-165
31464185-3	2019	Indoleamine 2,3-dioxygenase (IDO) is an enzyme that catalyses degradation of tryptophan (Trp) through the kynurenine (Kyn) pathway; it can control inflammation and immune response by inducing Trp starvation.	Kynurenine	106-116	indoleamine 2,3-dioxygenase 1	Mus musculus	29-32
31464185-3	2019	Indoleamine 2,3-dioxygenase (IDO) is an enzyme that catalyses degradation of tryptophan (Trp) through the kynurenine (Kyn) pathway; it can control inflammation and immune response by inducing Trp starvation.	Kynurenine	118-121	indoleamine 2,3-dioxygenase 1	Mus musculus	0-27
31464185-3	2019	Indoleamine 2,3-dioxygenase (IDO) is an enzyme that catalyses degradation of tryptophan (Trp) through the kynurenine (Kyn) pathway; it can control inflammation and immune response by inducing Trp starvation.	Kynurenine	118-121	indoleamine 2,3-dioxygenase 1	Mus musculus	29-32
30143553-3	2019	In this study, primary human immune cells were isolated from the peripheral blood of patients and used to demonstrate that the tryptophan catabolite kynurenine induces CD8 T-cell death.	Kynurenine	149-159	CD8a molecule	Homo sapiens	168-171
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).	Kynurenine	248-258	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).	Kynurenine	248-258	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).	Kynurenine	260-263	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).	Kynurenine	260-263	indoleamine 2,3-dioxygenase 1	Homo sapiens	154-158
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).	Kynurenine	122-134	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).	Kynurenine	122-134	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).	Kynurenine	136-139	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).	Kynurenine	136-139	indoleamine 2,3-dioxygenase 1	Homo sapiens	31-35
30213797-5	2019	The data demonstrate that miR-200c targeted TDO2 directly resulting in reduced production of the immunosuppressive metabolite kynurenine.	Kynurenine	126-136	microRNA 200c	Homo sapiens	26-34
30213797-5	2019	The data demonstrate that miR-200c targeted TDO2 directly resulting in reduced production of the immunosuppressive metabolite kynurenine.	Kynurenine	126-136	tryptophan 2,3-dioxygenase	Homo sapiens	44-48
30143553-7	2019	Interestingly, both tryptophan and kynurenine were lower in the plasma from patients with breast cancer compared with controls, particularly in women with estrogen receptor (ER)-negative and stage III and IV breast cancer.	Kynurenine	35-45	estrogen receptor 1	Homo sapiens	155-172
30143553-7	2019	Interestingly, both tryptophan and kynurenine were lower in the plasma from patients with breast cancer compared with controls, particularly in women with estrogen receptor (ER)-negative and stage III and IV breast cancer.	Kynurenine	35-45	estrogen receptor 1	Homo sapiens	174-176
30693061-11	2018	Conclusions: Our results suggest that the IDO1-dependent neurotoxic kynurenine metabolism induced by microglia functions in PSD pathogenesis.	Kynurenine	68-78	indoleamine 2,3-dioxygenase 1	Mus musculus	42-46
30544839-5	2018	Recent studies have confirmed that the kynurenine metabolic pathway (KP) can be stimulated by interferon-gamma (IFN-gamma) and other cytokines, activating indoleamine 2,3-dioxygenase (IDO) in SS.	Kynurenine	39-49	interferon gamma	Homo sapiens	94-110
30544839-5	2018	Recent studies have confirmed that the kynurenine metabolic pathway (KP) can be stimulated by interferon-gamma (IFN-gamma) and other cytokines, activating indoleamine 2,3-dioxygenase (IDO) in SS.	Kynurenine	39-49	interferon gamma	Homo sapiens	112-121
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.	Kynurenine	171-181	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-4
30391205-1	2018	Indoleamine 2,3 dioxygenase 1 (IDO1) is a metabolic enzyme that catalyzes the conversion of the essential amino acid tryptophan (Trp) into a series of immunoactive catabolites, collectively known as kynurenines.	Kynurenine	199-210	indoleamine 2,3-dioxygenase 1	Mus musculus	0-29
30391205-1	2018	Indoleamine 2,3 dioxygenase 1 (IDO1) is a metabolic enzyme that catalyzes the conversion of the essential amino acid tryptophan (Trp) into a series of immunoactive catabolites, collectively known as kynurenines.	Kynurenine	199-210	indoleamine 2,3-dioxygenase 1	Mus musculus	31-35
30391205-2	2018	Through the depletion of Trp and the generation of kynurenines, IDO1 represents a key regulator of the immune responses involved in physiologic homeostasis as well as in neoplastic and autoimmune pathologies.	Kynurenine	51-62	indoleamine 2,3-dioxygenase 1	Mus musculus	64-68
30175442-4	2018	The KYN:TRP ratio reflected IDO activity.	Kynurenine	4-7	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.	Kynurenine	145-155	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.	Kynurenine	145-155	indoleamine 2,3-dioxygenase 1	Homo sapiens	111-114
30306723-9	2018	RESULTS: We demonstrate, that ATP at concentrations between 0.062 and 0.5 mM increases dose dependently the expression of IDO in MSCs with subsequent increased kynurenine concentrations within the supernatant at about 60%.	Kynurenine	160-170	indoleamine 2,3-dioxygenase 1	Homo sapiens	122-125
30006478-2	2018	Changes in indoleamine 2,3 dioxygenase (IDO) activity, which catabolizes the degradation of tryptophan to kynurenine, may predict rejection.	Kynurenine	106-116	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.	Kynurenine	106-116	indoleamine 2,3-dioxygenase 1	Homo sapiens	40-43
30006478-9	2018	KMO generates the immunosuppressive kynurenine, 3-hydroxykynurenine.	Kynurenine	36-46	kynurenine 3-monooxygenase	Homo sapiens	0-3
30014175-4	2018	IDO and TDO are the first and rate-limiting enzymes in the kynurenine pathway and regulate the production of active metabolites.	Kynurenine	59-69	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-3
30014175-4	2018	IDO and TDO are the first and rate-limiting enzymes in the kynurenine pathway and regulate the production of active metabolites.	Kynurenine	59-69	tryptophan 2,3-dioxygenase	Homo sapiens	8-11
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.	Kynurenine	171-181	interferon gamma	Homo sapiens	60-68
30232146-7	2018	It reversed IDO1-induced T-cell anergy in vitro In mice carrying syngeneic tumor grafts, PF-06840003 reduced intratumoral kynurenine levels by over 80% and inhibited tumor growth both in monotherapy and, with an increased efficacy, in combination with antibodies blocking the immune checkpoint ligand PD-L1.	Kynurenine	122-132	indoleamine 2,3-dioxygenase 1	Mus musculus	12-16
30470234-9	2018	Neopterin and IP-10 were associated with marked changes in KP metabolites in CSF with increasing kynurenine/tryptophan ratio reflecting indoleamine 2,3-dioxygenase activity.	Kynurenine	97-107	C-X-C motif chemokine ligand 10	Homo sapiens	14-19
30051373-2	2018	Interferon-gamma is a cytokine that acts as a mediator between immune stimulation and the kynurenine pathway and may be related to cognitive abilities.	Kynurenine	90-100	interferon gamma	Homo sapiens	0-16
30051373-9	2018	The negative correlations between interferon-gamma and cognition in patients with schizophrenia suggest the hypothesis that inflammation and the kynurenine pathway have important roles in this disorder.	Kynurenine	145-155	interferon gamma	Homo sapiens	34-50
29366745-5	2018	Enzyme activity of indoleamine-2,3-dioxygenase (IDO) was recorded with the ratio of kynurenine (KYN) / tryptophan (Trp).	Kynurenine	84-94	indoleamine 2,3-dioxygenase 1	Mus musculus	19-46
30213497-3	2018	The G protein-coupled receptor 35 (GPR35) is important for kynurenine pathway activation.	Kynurenine	59-69	G protein-coupled receptor 35	Rattus norvegicus	4-33
30213497-3	2018	The G protein-coupled receptor 35 (GPR35) is important for kynurenine pathway activation.	Kynurenine	59-69	G protein-coupled receptor 35	Rattus norvegicus	35-40
29366745-5	2018	Enzyme activity of indoleamine-2,3-dioxygenase (IDO) was recorded with the ratio of kynurenine (KYN) / tryptophan (Trp).	Kynurenine	84-94	indoleamine 2,3-dioxygenase 1	Mus musculus	48-51
29366745-5	2018	Enzyme activity of indoleamine-2,3-dioxygenase (IDO) was recorded with the ratio of kynurenine (KYN) / tryptophan (Trp).	Kynurenine	96-99	indoleamine 2,3-dioxygenase 1	Mus musculus	19-46
29366745-5	2018	Enzyme activity of indoleamine-2,3-dioxygenase (IDO) was recorded with the ratio of kynurenine (KYN) / tryptophan (Trp).	Kynurenine	96-99	indoleamine 2,3-dioxygenase 1	Mus musculus	48-51
29366745-7	2018	Along with depressive-like behaviors, IDO, the rate-limiting enzyme of the kynurenine pathway (KP), was upregulated at the level of mRNA expression, and enzyme activity was also elevated in stressed hippocampi and LPS/HMGB1-treated hippocampus slices.	Kynurenine	75-85	indoleamine 2,3-dioxygenase 1	Mus musculus	38-41
30153331-3	2018	IFNgamma enhanced inositol 1,4,5-trisphosphate (IP3 ) receptor agonist (adenophostin A, AdA)-induced astroglial release of kynurenine-pathway metabolites, without affecting AMPA-induced release.	Kynurenine	123-133	interferon gamma	Rattus norvegicus	0-8
30153331-7	2018	Furthermore, LEV inhibited stimulatory effects of chronic IFNgamma on AdA-induced release of kynurenine-pathway metabolites.	Kynurenine	93-103	interferon gamma	Rattus norvegicus	58-66
30354938-6	2018	RESULTS:: Maternal kynurenine treatment raised kynurenic acid levels significantly more in the brain of heterozygous offspring of Kmo+/- than in the brain of Kmo+/+ offspring.	Kynurenine	19-29	kynurenine 3-monooxygenase (kynurenine 3-hydroxylase)	Mus musculus	130-133
30354938-6	2018	RESULTS:: Maternal kynurenine treatment raised kynurenic acid levels significantly more in the brain of heterozygous offspring of Kmo+/- than in the brain of Kmo+/+ offspring.	Kynurenine	19-29	kynurenine 3-monooxygenase (kynurenine 3-hydroxylase)	Mus musculus	158-161
30354938-7	2018	Conversely, 3-hydroxykynurenine and quinolinic acid levels in the fetal brain tended to be lower in heterozygous animals derived from kynurenine-treated Kmo+/- mice than in corresponding Kmo+/+ offspring.	Kynurenine	21-31	kynurenine 3-monooxygenase (kynurenine 3-hydroxylase)	Mus musculus	153-156
30354938-9	2018	Kynurenine treatment also caused a preferential elevation in cerebral kynurenic acid levels in Kmo+/- compared to Kmo+/+ dams.	Kynurenine	0-10	kynurenine 3-monooxygenase (kynurenine 3-hydroxylase)	Mus musculus	95-98
30354938-9	2018	Kynurenine treatment also caused a preferential elevation in cerebral kynurenic acid levels in Kmo+/- compared to Kmo+/+ dams.	Kynurenine	0-10	kynurenine 3-monooxygenase (kynurenine 3-hydroxylase)	Mus musculus	114-117
29442266-3	2018	It has been demonstrated that L-kynurenine (L-Kyn), a physiological ligand of Aryl hydrocarbon receptor (Ahr), promotes cancer cells to metastasize.	Kynurenine	30-42	aryl hydrocarbon receptor	Homo sapiens	78-103
29442266-3	2018	It has been demonstrated that L-kynurenine (L-Kyn), a physiological ligand of Aryl hydrocarbon receptor (Ahr), promotes cancer cells to metastasize.	Kynurenine	30-42	aryl hydrocarbon receptor	Homo sapiens	105-108
29442266-3	2018	It has been demonstrated that L-kynurenine (L-Kyn), a physiological ligand of Aryl hydrocarbon receptor (Ahr), promotes cancer cells to metastasize.	Kynurenine	44-49	aryl hydrocarbon receptor	Homo sapiens	78-103
29442266-3	2018	It has been demonstrated that L-kynurenine (L-Kyn), a physiological ligand of Aryl hydrocarbon receptor (Ahr), promotes cancer cells to metastasize.	Kynurenine	44-49	aryl hydrocarbon receptor	Homo sapiens	105-108
30098337-12	2018	Our findings suggest that excess QA levels, due to mutations in the kynurenine pathway, for example, may lead to the formation of metabolite assemblies that seed alpha-synuclein aggregation, resulting in neuronal toxicity and induction of Parkinson"s disease.	Kynurenine	68-78	synuclein, alpha	Mus musculus	162-177
30005281-2	2018	The balance of inflammatory signals in the tryptophan pathway can skew the activity of indoleamine-pyrrole 2,3 dioxygenase (IDO1) towards the metabolization of tryptophan into kynurenine (rather than serotonin), and towards neuroprotective or neurotoxic metabolites.	Kynurenine	176-186	indoleamine 2,3-dioxygenase 1	Mus musculus	87-122
30005281-2	2018	The balance of inflammatory signals in the tryptophan pathway can skew the activity of indoleamine-pyrrole 2,3 dioxygenase (IDO1) towards the metabolization of tryptophan into kynurenine (rather than serotonin), and towards neuroprotective or neurotoxic metabolites.	Kynurenine	176-186	indoleamine 2,3-dioxygenase 1	Mus musculus	124-128
30374077-1	2018	Indoleamine 2,3-dioxygenase 2 (Ido2) is a recently identified catalytic enzyme in the tryptophan-kynurenine pathway that is expressed primarily in monocytes and dendritic cells.	Kynurenine	97-107	indoleamine 2,3-dioxygenase 2	Mus musculus	0-29
29607498-1	2018	Indoleamine 2,3-dioxygenase 1 (IDO1), known as IDO, catabolizes tryptophan through kynurenine pathway, whose activity is correlated with impaired clinical outcome of colorectal cancer.	Kynurenine	83-93	indoleamine 2,3-dioxygenase 1	Mus musculus	0-29
30007645-2	2018	IDO expression and kynurenine production from LSP-treated HepG2 cells following IFN-gamma stimulation were dramatically inhibited by LSP treatment.	Kynurenine	19-29	interferon gamma	Homo sapiens	80-89
30055888-1	2018	Kynurenine is biosynthesised from tryptophan catalysed by indoleamine 2,3-dioxygenase (IDO).	Kynurenine	0-10	indoleamine 2,3-dioxygenase 1	Homo sapiens	58-85
30055888-1	2018	Kynurenine is biosynthesised from tryptophan catalysed by indoleamine 2,3-dioxygenase (IDO).	Kynurenine	0-10	indoleamine 2,3-dioxygenase 1	Homo sapiens	87-90
30055888-3	2018	In the course of our IDO inhibitor programme, formal cyclisation of the isothiourea moiety of the IDO inhibitor 1 afforded the 5-Cl-benzimidazole derivative 2b-6, which inhibited both recombinant human IDO (rhIDO) activity and cellular kynurenine production.	Kynurenine	236-246	indoleamine 2,3-dioxygenase 1	Homo sapiens	21-24
30055888-3	2018	In the course of our IDO inhibitor programme, formal cyclisation of the isothiourea moiety of the IDO inhibitor 1 afforded the 5-Cl-benzimidazole derivative 2b-6, which inhibited both recombinant human IDO (rhIDO) activity and cellular kynurenine production.	Kynurenine	236-246	indoleamine 2,3-dioxygenase 1	Homo sapiens	98-101
30055888-3	2018	In the course of our IDO inhibitor programme, formal cyclisation of the isothiourea moiety of the IDO inhibitor 1 afforded the 5-Cl-benzimidazole derivative 2b-6, which inhibited both recombinant human IDO (rhIDO) activity and cellular kynurenine production.	Kynurenine	236-246	indoleamine 2,3-dioxygenase 1	Homo sapiens	98-101
30223437-8	2018	CNP also reduced IFN-gamma mediated kynurenine generation by the IFN-gamma regulated enzyme indoleamine-2,3-deoxygenase (IDO).	Kynurenine	36-46	natriuretic peptide C	Homo sapiens	0-3
31336879-6	2019	Regulatory DCs in Galectin-3:Toll-like receptor-4:Kynurenine-dependent manner promoted the expansion of colon-infiltrated T regulatory cells (Tregs) and suppressed Th1 and Th17 cell-driven colon inflammation.	Kynurenine	50-60	galectin 3	Homo sapiens	18-28
31336879-6	2019	Regulatory DCs in Galectin-3:Toll-like receptor-4:Kynurenine-dependent manner promoted the expansion of colon-infiltrated T regulatory cells (Tregs) and suppressed Th1 and Th17 cell-driven colon inflammation.	Kynurenine	50-60	toll like receptor 4	Homo sapiens	29-49
30150287-8	2018	IDO and its metabolite kynurenine in the tumor microenvironment were screened as an upstream regulator of miR-143.	Kynurenine	23-33	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-3
30150287-8	2018	IDO and its metabolite kynurenine in the tumor microenvironment were screened as an upstream regulator of miR-143.	Kynurenine	23-33	microRNA 143	Homo sapiens	106-113
30154211-7	2018	Finally, we show that expression of wild-type Scarlet is neuroprotective in a model of PD, suggesting that manipulating kynurenine metabolism may be a potential therapeutic option in treating PD.This article has an associated First Person interview with the first author of the paper.	Kynurenine	120-130	scarlet	Drosophila melanogaster	46-53
30019623-5	2018	We found that 1) pro- and anti-inflammatory cytokine levels in the brain injury area were differentially regulated in a time-dependent manner post-injury; 2) indoleamine 2,3 dioxygeenase 1 (IDO1) was upregulated around the injury area in TBI kits that persisted at 21 days post-injury; 3) mean length of serotonin-staining fibers was significantly reduced in the injured brain region in TBI kits for at least 21 days post-injury; and 4) kynurenine level significantly increased at 7 days post-injury.	Kynurenine	437-447	indoleamine 2,3-dioxygenase 1	Oryctolagus cuniculus	158-188
30019623-5	2018	We found that 1) pro- and anti-inflammatory cytokine levels in the brain injury area were differentially regulated in a time-dependent manner post-injury; 2) indoleamine 2,3 dioxygeenase 1 (IDO1) was upregulated around the injury area in TBI kits that persisted at 21 days post-injury; 3) mean length of serotonin-staining fibers was significantly reduced in the injured brain region in TBI kits for at least 21 days post-injury; and 4) kynurenine level significantly increased at 7 days post-injury.	Kynurenine	437-447	indoleamine 2,3-dioxygenase 1	Oryctolagus cuniculus	190-194
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.	Kynurenine	46-56	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.	Kynurenine	46-56	indoleamine 2,3-dioxygenase 1	Rattus norvegicus	31-35
30103191-4	2018	In addition, compounds T28, T44 and T53 decreased the kynurenine levels in rat plasma by 30%-50%.	Kynurenine	54-64	peroxisomal membrane protein 2	Rattus norvegicus	28-31
29959909-5	2018	Reaction conditions for TDO2-mediated conversion of l-tryptophan to kynurenine were optimized.	Kynurenine	68-78	tryptophan 2,3-dioxygenase	Homo sapiens	24-28
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.	Kynurenine	88-98	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.	Kynurenine	88-98	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.	Kynurenine	88-98	programmed cell death 1	Homo sapiens	200-203
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.	Kynurenine	100-103	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.	Kynurenine	100-103	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.	Kynurenine	100-103	programmed cell death 1	Homo sapiens	200-203
30010674-2	2018	Whether these effects are due to Trp depletion in the TME or mediated by the accumulation of the IDO1 and/or TDO (hereafter referred to as IDO1/TDO) product kynurenine (Kyn) remains controversial.	Kynurenine	157-167	tryptophan 2,3-dioxygenase	Homo sapiens	109-112
30010674-2	2018	Whether these effects are due to Trp depletion in the TME or mediated by the accumulation of the IDO1 and/or TDO (hereafter referred to as IDO1/TDO) product kynurenine (Kyn) remains controversial.	Kynurenine	157-167	indoleamine 2,3-dioxygenase 1	Homo sapiens	139-143
30010674-2	2018	Whether these effects are due to Trp depletion in the TME or mediated by the accumulation of the IDO1 and/or TDO (hereafter referred to as IDO1/TDO) product kynurenine (Kyn) remains controversial.	Kynurenine	157-167	tryptophan 2,3-dioxygenase	Homo sapiens	144-147
30010674-2	2018	Whether these effects are due to Trp depletion in the TME or mediated by the accumulation of the IDO1 and/or TDO (hereafter referred to as IDO1/TDO) product kynurenine (Kyn) remains controversial.	Kynurenine	169-172	tryptophan 2,3-dioxygenase	Homo sapiens	109-112
30175526-1	2018	AIM: Indoleamine 2,3-dioxygenase 1 (IDO1) metabolizes the essential amino acid tryptophan into kynurenine derivatives, which are involved in neural activity via the kynurenine pathway (KP).	Kynurenine	95-105	indoleamine 2,3-dioxygenase 1	Mus musculus	5-34
30175526-1	2018	AIM: Indoleamine 2,3-dioxygenase 1 (IDO1) metabolizes the essential amino acid tryptophan into kynurenine derivatives, which are involved in neural activity via the kynurenine pathway (KP).	Kynurenine	95-105	indoleamine 2,3-dioxygenase 1	Mus musculus	36-40
30175526-1	2018	AIM: Indoleamine 2,3-dioxygenase 1 (IDO1) metabolizes the essential amino acid tryptophan into kynurenine derivatives, which are involved in neural activity via the kynurenine pathway (KP).	Kynurenine	165-175	indoleamine 2,3-dioxygenase 1	Mus musculus	5-34
30175526-1	2018	AIM: Indoleamine 2,3-dioxygenase 1 (IDO1) metabolizes the essential amino acid tryptophan into kynurenine derivatives, which are involved in neural activity via the kynurenine pathway (KP).	Kynurenine	165-175	indoleamine 2,3-dioxygenase 1	Mus musculus	36-40
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.	Kynurenine	4-14	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.	Kynurenine	4-14	indoleamine 2,3-dioxygenase 1	Homo sapiens	107-110
30159037-1	2018	Background: Dendritic cell (DC)-derived indolamine 2,3-dioxygenase (IDO) degrades tryptophan to kynurenine, which promotes conversion of inflammatory T cells in immunosuppressive regulatory T cells (Tregs).	Kynurenine	96-106	indoleamine 2,3-dioxygenase 1	Mus musculus	40-66
30159037-1	2018	Background: Dendritic cell (DC)-derived indolamine 2,3-dioxygenase (IDO) degrades tryptophan to kynurenine, which promotes conversion of inflammatory T cells in immunosuppressive regulatory T cells (Tregs).	Kynurenine	96-106	indoleamine 2,3-dioxygenase 1	Mus musculus	68-71
29921693-6	2018	Fluorescent immunostainings of patient samples confirmed expression of IDO1 protein and also its metabolite kynurenine in primarily N-cadherin-positive areas.	Kynurenine	108-118	cadherin 2	Homo sapiens	132-142
30081936-5	2018	The IDO activity was expressed with kyn/trp ratio.	Kynurenine	36-39	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.	Kynurenine	39-42	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.	Kynurenine	122-125	indoleamine 2,3-dioxygenase 1	Homo sapiens	12-15
30275755-4	2018	The indoleamine 2,3-dioxygenase 1 (IDO) catalyzes conversion of tryptophan to kynurenine to induce immune evasion in tumor microenvironment.	Kynurenine	78-88	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.	Kynurenine	78-88	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.	Kynurenine	165-175	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.	Kynurenine	165-175	indoleamine 2,3-dioxygenase 2	Homo sapiens	40-44
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.	Kynurenine	165-175	tryptophan 2,3-dioxygenase	Homo sapiens	50-77
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.	Kynurenine	165-175	tryptophan 2,3-dioxygenase	Homo sapiens	79-82
30141341-1	2018	AIM: Indoleamine 2,3-dioxygenase (IDO) and tryptophan 2,3-dioxygenase (TDO) catalyze the initial and rate-controlling step of tryptophan metabolism through the kynurenine pathway, which plays an important role in mediating immune response.	Kynurenine	160-170	indoleamine 2,3-dioxygenase 1	Homo sapiens	5-32
30141341-1	2018	AIM: Indoleamine 2,3-dioxygenase (IDO) and tryptophan 2,3-dioxygenase (TDO) catalyze the initial and rate-controlling step of tryptophan metabolism through the kynurenine pathway, which plays an important role in mediating immune response.	Kynurenine	160-170	indoleamine 2,3-dioxygenase 1	Homo sapiens	34-37
30141341-1	2018	AIM: Indoleamine 2,3-dioxygenase (IDO) and tryptophan 2,3-dioxygenase (TDO) catalyze the initial and rate-controlling step of tryptophan metabolism through the kynurenine pathway, which plays an important role in mediating immune response.	Kynurenine	160-170	tryptophan 2,3-dioxygenase	Homo sapiens	43-69
30141341-1	2018	AIM: Indoleamine 2,3-dioxygenase (IDO) and tryptophan 2,3-dioxygenase (TDO) catalyze the initial and rate-controlling step of tryptophan metabolism through the kynurenine pathway, which plays an important role in mediating immune response.	Kynurenine	160-170	tryptophan 2,3-dioxygenase	Homo sapiens	71-74
30141341-2	2018	Accurate measurement of tryptophan and kynurenine is critical for monitoring the activity of IDO/TDO.	Kynurenine	39-49	indoleamine 2,3-dioxygenase 1	Homo sapiens	93-96
30141341-2	2018	Accurate measurement of tryptophan and kynurenine is critical for monitoring the activity of IDO/TDO.	Kynurenine	39-49	tryptophan 2,3-dioxygenase	Homo sapiens	97-100
30141341-7	2018	The assay demonstrated successful application to a clinical study to confirm a transient depletion of kynurenine upon IDO inhibition.	Kynurenine	102-112	indoleamine 2,3-dioxygenase 1	Homo sapiens	118-121
29195782-0	2018	HMGB1 mediates depressive behavior induced by chronic stress through activating the kynurenine pathway.	Kynurenine	84-94	high mobility group box 1	Mus musculus	0-5
29195782-2	2018	Here, the potential mechanism of HMGB1 mediating chronic-stress-induced depression through the kynurenine pathway (KP) was further explored both in vivo and in vitro.	Kynurenine	95-105	high mobility group box 1	Mus musculus	33-38
29195782-5	2018	The ratio of kynurenine (KYN)/tryptophan (Trp) represented the enzyme activity of indoleamine-2,3-dioxygenase (IDO).	Kynurenine	13-23	indoleamine 2,3-dioxygenase 1	Mus musculus	82-109
29195782-5	2018	The ratio of kynurenine (KYN)/tryptophan (Trp) represented the enzyme activity of indoleamine-2,3-dioxygenase (IDO).	Kynurenine	13-23	indoleamine 2,3-dioxygenase 1	Mus musculus	111-114
29195782-5	2018	The ratio of kynurenine (KYN)/tryptophan (Trp) represented the enzyme activity of indoleamine-2,3-dioxygenase (IDO).	Kynurenine	25-28	indoleamine 2,3-dioxygenase 1	Mus musculus	82-109
29195782-5	2018	The ratio of kynurenine (KYN)/tryptophan (Trp) represented the enzyme activity of indoleamine-2,3-dioxygenase (IDO).	Kynurenine	25-28	indoleamine 2,3-dioxygenase 1	Mus musculus	111-114
29558201-6	2018	HBO treatment increased the expression of aryl hydrocarbon receptor over hypoxia-inducible factor 1-alpha (HIF-1alpha), an oxygen-sensitive cytosolic receptor, along with decreased indoleamine 2,3-dioxygenase 1 expression and kynurenine levels.	Kynurenine	226-236	aryl hydrocarbon receptor	Homo sapiens	42-67
29558201-6	2018	HBO treatment increased the expression of aryl hydrocarbon receptor over hypoxia-inducible factor 1-alpha (HIF-1alpha), an oxygen-sensitive cytosolic receptor, along with decreased indoleamine 2,3-dioxygenase 1 expression and kynurenine levels.	Kynurenine	226-236	hypoxia inducible factor 1 subunit alpha	Homo sapiens	107-117
29879409-1	2018	Kynurenine 3-monooxygenase (KMO) is an essential enzyme of the kynurenine pathway, converting kynurenine into 3-hydroxykynurenine.	Kynurenine	63-73	kynurenine 3-monooxygenase (kynurenine 3-hydroxylase)	Mus musculus	0-26
29879409-1	2018	Kynurenine 3-monooxygenase (KMO) is an essential enzyme of the kynurenine pathway, converting kynurenine into 3-hydroxykynurenine.	Kynurenine	63-73	kynurenine 3-monooxygenase (kynurenine 3-hydroxylase)	Mus musculus	28-31
29879409-1	2018	Kynurenine 3-monooxygenase (KMO) is an essential enzyme of the kynurenine pathway, converting kynurenine into 3-hydroxykynurenine.	Kynurenine	94-104	kynurenine 3-monooxygenase (kynurenine 3-hydroxylase)	Mus musculus	0-26
29879409-1	2018	Kynurenine 3-monooxygenase (KMO) is an essential enzyme of the kynurenine pathway, converting kynurenine into 3-hydroxykynurenine.	Kynurenine	94-104	kynurenine 3-monooxygenase (kynurenine 3-hydroxylase)	Mus musculus	28-31
29879409-2	2018	Inhibition of KMO increases kynurenine, resulting in elevated levels of kynurenic acid (KYNA), an endogenous N-methyl-d-aspartate and alpha*7-nicotinic receptor antagonist.	Kynurenine	28-38	kynurenine 3-monooxygenase (kynurenine 3-hydroxylase)	Mus musculus	14-17
29775873-8	2018	RESULTS: In both cohorts, inflammation as measured by higher levels of CRP, sVCAM1 and sICAM1 was associated with kynurenine/tryptophan ratio and thus enhanced tryptophan breakdown (beta: 0.145-0.429).	Kynurenine	114-124	C-reactive protein	Homo sapiens	71-74
30112109-4	2018	Endogenous IDO1 expression is induced in a cancer cell line with interferon gamma and its activity is assessed by measuring kynurenine secreted into the media.	Kynurenine	124-134	indoleamine 2,3-dioxygenase 1	Homo sapiens	11-15
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.	Kynurenine	57-60	indoleamine 2,3-dioxygenase 1	Homo sapiens	4-8
30349892-11	2018	Inhibition of the aryl hydrocarbon receptor that binds to Kyn, also reduced Kyn-induced TF expression in activated macrophages.	Kynurenine	58-61	coagulation factor III, tissue factor	Homo sapiens	88-90
30349892-11	2018	Inhibition of the aryl hydrocarbon receptor that binds to Kyn, also reduced Kyn-induced TF expression in activated macrophages.	Kynurenine	76-79	coagulation factor III, tissue factor	Homo sapiens	88-90
30050435-7	2018	The results of our studies show that the kynurenine pathway is an important mediator of neuropathic pain pathology in rats and indicate that IDO2 and KMO represent novel pharmacological targets for treating neuropathy.	Kynurenine	41-51	indoleamine 2,3-dioxygenase 2	Rattus norvegicus	141-145
30050435-7	2018	The results of our studies show that the kynurenine pathway is an important mediator of neuropathic pain pathology in rats and indicate that IDO2 and KMO represent novel pharmacological targets for treating neuropathy.	Kynurenine	41-51	kynurenine 3-monooxygenase	Rattus norvegicus	150-153
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.	Kynurenine	175-185	indoleamine 2,3-dioxygenase 1	Homo sapiens	33-36
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.	Kynurenine	175-178	indoleamine 2,3-dioxygenase 1	Homo sapiens	33-36
30073204-3	2018	This study aims to determine whether the low molecular weight fraction of 5% human serum albumin (LMWF5A) and N-acetyl kynurenine (NAK), an N-acetyl tryptophan (NAT) breakdown product in LMWF5A, can regulate inflammation by inhibiting macrophage activation through the AhR since kynurenine is a known AhR agonist.	Kynurenine	119-129	aryl hydrocarbon receptor	Homo sapiens	269-272
30073204-3	2018	This study aims to determine whether the low molecular weight fraction of 5% human serum albumin (LMWF5A) and N-acetyl kynurenine (NAK), an N-acetyl tryptophan (NAT) breakdown product in LMWF5A, can regulate inflammation by inhibiting macrophage activation through the AhR since kynurenine is a known AhR agonist.	Kynurenine	119-129	aryl hydrocarbon receptor	Homo sapiens	301-304
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.	Kynurenine	123-133	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.	Kynurenine	123-133	indoleamine 2,3-dioxygenase 1	Homo sapiens	81-84
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.	Kynurenine	193-203	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.	Kynurenine	193-203	indoleamine 2,3-dioxygenase 1	Homo sapiens	156-159
29520060-5	2018	Kynurenine levels were significantly correlated with levels of interferon-gamma (p &lt; .001), which is involved in the regulation of IDO, in both patients and controls.	Kynurenine	0-10	interferon gamma	Homo sapiens	63-79
29520060-5	2018	Kynurenine levels were significantly correlated with levels of interferon-gamma (p &lt; .001), which is involved in the regulation of IDO, in both patients and controls.	Kynurenine	0-10	indoleamine 2,3-dioxygenase 1	Homo sapiens	134-137
29537924-1	2018	Kynurenine aminotransferase-II (KAT-II) is a pyridoxal 5"-phosphate (PLP)-dependent enzyme that acts in the tryptophan metabolic pathway by catalyzing the transamination of kynurenine into kynurenic acid (KYNA).	Kynurenine	173-183	aminoadipate aminotransferase	Homo sapiens	0-30
29537924-1	2018	Kynurenine aminotransferase-II (KAT-II) is a pyridoxal 5"-phosphate (PLP)-dependent enzyme that acts in the tryptophan metabolic pathway by catalyzing the transamination of kynurenine into kynurenic acid (KYNA).	Kynurenine	173-183	aminoadipate aminotransferase	Homo sapiens	32-38
29537924-1	2018	Kynurenine aminotransferase-II (KAT-II) is a pyridoxal 5"-phosphate (PLP)-dependent enzyme that acts in the tryptophan metabolic pathway by catalyzing the transamination of kynurenine into kynurenic acid (KYNA).	Kynurenine	173-183	pyridoxal phosphatase	Homo sapiens	69-72
29703752-0	2018	Reassignment of the human aldehyde dehydrogenase ALDH8A1 (ALDH12) to the kynurenine pathway in tryptophan catabolism.	Kynurenine	73-83	aldehyde dehydrogenase 8 family member A1	Homo sapiens	49-56
29703752-0	2018	Reassignment of the human aldehyde dehydrogenase ALDH8A1 (ALDH12) to the kynurenine pathway in tryptophan catabolism.	Kynurenine	73-83	aldehyde dehydrogenase 8 family member A1	Homo sapiens	58-64
29703752-6	2018	Here, we provide compelling bioinformatics and experimental evidence that human ALDH8A1 should be reassigned to the missing 2-AMS dehydrogenase of the kynurenine metabolic pathway.	Kynurenine	151-161	aldehyde dehydrogenase 8 family member A1	Homo sapiens	80-87
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.	Kynurenine	92-102	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.	Kynurenine	92-102	indoleamine 2,3-dioxygenase 1	Homo sapiens	43-47
29921320-13	2018	CONCLUSIONS: Navoximod was well-tolerated at doses up to 800 mg BID decreasing plasma kynurenine levels consistent with its half-life.	Kynurenine	86-96	BH3 interacting domain death agonist	Homo sapiens	64-67
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.	Kynurenine	113-123	microRNA 99b	Homo sapiens	13-20
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.	Kynurenine	113-123	microRNA let-7e	Homo sapiens	21-27
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.	Kynurenine	113-123	microRNA 125a	Homo sapiens	28-36
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.	Kynurenine	113-123	indoleamine 2,3-dioxygenase 1	Homo sapiens	201-204
29963055-0	2018	An Expanded Neuroimmunomodulation Axis: sCD83-Indoleamine 2,3-Dioxygenase-Kynurenine Pathway and Updates of Kynurenine Pathway in Neurologic Diseases.	Kynurenine	74-84	indoleamine 2,3-dioxygenase 1	Homo sapiens	46-73
29679555-1	2018	BACKGROUND: Indoleamine-2,3-dioxygenase (IDO) catalyzes the first step of tryptophan (Trp) catabolism, yielding kynurenine (Kyn) metabolites.	Kynurenine	112-122	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.	Kynurenine	112-122	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.	Kynurenine	124-127	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.	Kynurenine	124-127	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.	Kynurenine	4-14	indoleamine 2,3-dioxygenase 1	Homo sapiens	79-82
30106261-1	2018	AIMS: Tryptophan 2,3-dioxygenase (TDO2) is an initial rate-limiting enzyme of the kynurenine (Kyn) pathway in tryptophan (Trp) metabolism.	Kynurenine	82-92	tryptophan 2,3-dioxygenase	Mus musculus	6-32
30106261-1	2018	AIMS: Tryptophan 2,3-dioxygenase (TDO2) is an initial rate-limiting enzyme of the kynurenine (Kyn) pathway in tryptophan (Trp) metabolism.	Kynurenine	82-92	tryptophan 2,3-dioxygenase	Mus musculus	34-38
30106261-1	2018	AIMS: Tryptophan 2,3-dioxygenase (TDO2) is an initial rate-limiting enzyme of the kynurenine (Kyn) pathway in tryptophan (Trp) metabolism.	Kynurenine	94-97	tryptophan 2,3-dioxygenase	Mus musculus	6-32
30106261-1	2018	AIMS: Tryptophan 2,3-dioxygenase (TDO2) is an initial rate-limiting enzyme of the kynurenine (Kyn) pathway in tryptophan (Trp) metabolism.	Kynurenine	94-97	tryptophan 2,3-dioxygenase	Mus musculus	34-38
30223437-8	2018	CNP also reduced IFN-gamma mediated kynurenine generation by the IFN-gamma regulated enzyme indoleamine-2,3-deoxygenase (IDO).	Kynurenine	36-46	interferon gamma	Homo sapiens	17-26
30223437-8	2018	CNP also reduced IFN-gamma mediated kynurenine generation by the IFN-gamma regulated enzyme indoleamine-2,3-deoxygenase (IDO).	Kynurenine	36-46	interferon gamma	Homo sapiens	65-74
30223437-8	2018	CNP also reduced IFN-gamma mediated kynurenine generation by the IFN-gamma regulated enzyme indoleamine-2,3-deoxygenase (IDO).	Kynurenine	36-46	indoleamine 2,3-dioxygenase 1	Homo sapiens	92-119
30223437-8	2018	CNP also reduced IFN-gamma mediated kynurenine generation by the IFN-gamma regulated enzyme indoleamine-2,3-deoxygenase (IDO).	Kynurenine	36-46	indoleamine 2,3-dioxygenase 1	Homo sapiens	121-124
29607498-1	2018	Indoleamine 2,3-dioxygenase 1 (IDO1), known as IDO, catabolizes tryptophan through kynurenine pathway, whose activity is correlated with impaired clinical outcome of colorectal cancer.	Kynurenine	83-93	indoleamine 2,3-dioxygenase 1	Mus musculus	31-35
29607498-1	2018	Indoleamine 2,3-dioxygenase 1 (IDO1), known as IDO, catabolizes tryptophan through kynurenine pathway, whose activity is correlated with impaired clinical outcome of colorectal cancer.	Kynurenine	83-93	indoleamine 2,3-dioxygenase 1	Mus musculus	31-34
29773791-1	2018	The tryptophan metabolite kynurenine has critical immunomodulatory properties and can function as an aryl hydrocarbon receptor (AHR) ligand.	Kynurenine	26-36	aryl hydrocarbon receptor	Homo sapiens	101-126
29868176-9	2018	Results: The kynurenine/tryptophan ratio, as a measure of indoleamine 2,3-dioxygenase (IDO) activity, was increased in patients with SLE.	Kynurenine	13-23	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.	Kynurenine	13-23	indoleamine 2,3-dioxygenase 1	Homo sapiens	87-90
29868176-15	2018	Drugs targeting enzymes in the kynurenine pathway, for example, IDO inhibitors or niacin (B12) supplementation, which suppresses IDO activity, merit further investigation as treatments in SLE.	Kynurenine	31-41	indoleamine 2,3-dioxygenase 1	Homo sapiens	64-67
29868176-15	2018	Drugs targeting enzymes in the kynurenine pathway, for example, IDO inhibitors or niacin (B12) supplementation, which suppresses IDO activity, merit further investigation as treatments in SLE.	Kynurenine	31-41	indoleamine 2,3-dioxygenase 1	Homo sapiens	129-132
29773791-1	2018	The tryptophan metabolite kynurenine has critical immunomodulatory properties and can function as an aryl hydrocarbon receptor (AHR) ligand.	Kynurenine	26-36	aryl hydrocarbon receptor	Homo sapiens	128-131
29773791-3	2018	Kynurenine is transported across the T-cell membrane by the System L transporter SLC7A5.	Kynurenine	0-10	solute carrier family 7 member 5	Homo sapiens	81-87
29773791-4	2018	Accordingly, the ability of kynurenine to activate the AHR is restricted to T cells that express SLC7A5.	Kynurenine	28-38	aryl hydrocarbon receptor	Homo sapiens	55-58
29773791-4	2018	Accordingly, the ability of kynurenine to activate the AHR is restricted to T cells that express SLC7A5.	Kynurenine	28-38	solute carrier family 7 member 5	Homo sapiens	97-103
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.	Kynurenine	296-306	indoleamine 2,3-dioxygenase 1	Homo sapiens	186-213
29141444-6	2018	Neopterin was correlated with KYN/TRP, suggesting that the indoleamine 2,3-dioxygenase-1 (IDO-1) enzyme was activated.	Kynurenine	30-33	indoleamine 2,3-dioxygenase 1	Homo sapiens	59-88
29141444-6	2018	Neopterin was correlated with KYN/TRP, suggesting that the indoleamine 2,3-dioxygenase-1 (IDO-1) enzyme was activated.	Kynurenine	30-33	indoleamine 2,3-dioxygenase 1	Homo sapiens	90-95
29867939-3	2018	The expression of the enzyme indoleamine 2,3-dioxygenase-1 (IDO1), which catalyzes the degradation of tryptophan (Trp) along the kynurenine pathway, has been implicated in the induction and expansion of Treg populations.	Kynurenine	129-139	indoleamine 2,3-dioxygenase 1	Mus musculus	29-58
29867939-3	2018	The expression of the enzyme indoleamine 2,3-dioxygenase-1 (IDO1), which catalyzes the degradation of tryptophan (Trp) along the kynurenine pathway, has been implicated in the induction and expansion of Treg populations.	Kynurenine	129-139	indoleamine 2,3-dioxygenase 1	Mus musculus	60-64
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.	Kynurenine	167-178	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.	Kynurenine	167-178	indoleamine 2,3-dioxygenase 1	Homo sapiens	32-36
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.	Kynurenine	296-306	indoleamine 2,3-dioxygenase 1	Homo sapiens	215-218
29795752-1	2018	Tryptophan 2,3-dioxygenase 2 (TDO2) catalyzes the conversion of tryptophan to the immunosuppressive metabolite kynurenine.	Kynurenine	111-121	tryptophan 2,3-dioxygenase	Homo sapiens	0-28
29685162-1	2018	BACKGROUND: Indoleamine 2,3-dioxygenase 1 (IDO1) catalyzes the first and rate-limiting step in converting tryptophan to kynurenine.	Kynurenine	120-130	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.	Kynurenine	120-130	indoleamine 2,3-dioxygenase 1	Homo sapiens	43-47
29306989-0	2018	Kynurenine is correlated with IL-1beta in plasma of schizophrenia patients.	Kynurenine	0-10	interleukin 1 beta	Homo sapiens	30-38
29719533-1	2018	Indoleamine 2,3-dioxygenase (IDO), which catalyzes the breakdown of the essential amino acid tryptophan into kynurenine, is understood to have a key role in cancer immunotherapy.	Kynurenine	109-119	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-27
29719533-1	2018	Indoleamine 2,3-dioxygenase (IDO), which catalyzes the breakdown of the essential amino acid tryptophan into kynurenine, is understood to have a key role in cancer immunotherapy.	Kynurenine	109-119	indoleamine 2,3-dioxygenase 1	Homo sapiens	29-32
29719533-11	2018	The ratio of Kyn and trp (kyn/trp) was calculated to estimate IDO-enzyme activity.	Kynurenine	13-16	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.	Kynurenine	26-29	indoleamine 2,3-dioxygenase 1	Homo sapiens	62-65
29795752-1	2018	Tryptophan 2,3-dioxygenase 2 (TDO2) catalyzes the conversion of tryptophan to the immunosuppressive metabolite kynurenine.	Kynurenine	111-121	tryptophan 2,3-dioxygenase	Homo sapiens	30-34
29526577-3	2018	These ideas include the inflammation-induced activation of the kynurenine pathway and its role in feeding and metabolism by activation of the aryl hydrocarbon receptor (AHR) and by modulating synaptic transmission in the brain.	Kynurenine	63-73	aryl hydrocarbon receptor	Homo sapiens	142-167
29183965-7	2018	The findings in our study extend understanding of an immunologic effect of Kyn that links Trp metabolism and inflammatory signaling in depression pathology, with potential therapeutic implications for depressive disorders.-Zang, X., Zheng, X., Hou, Y., Hu, M., Wang, H., Bao, X., Zhou, F., Wang, G., Hao, H. Regulation of proinflammatory monocyte activation by the kynurenine-AhR axis underlies immunometabolic control of depressive behavior in mice.	Kynurenine	75-78	aryl-hydrocarbon receptor	Mus musculus	376-379
29208702-4	2018	Here, we report biochemistry studies on hKMO and crystal structures of an hKMO homolog, pfKMO from Pseudomonas fluorescens, in complex with the substrate l-kynurenine and Ro 61-8048.	Kynurenine	154-166	kynurenine 3-monooxygenase	Homo sapiens	40-44
29208702-4	2018	Here, we report biochemistry studies on hKMO and crystal structures of an hKMO homolog, pfKMO from Pseudomonas fluorescens, in complex with the substrate l-kynurenine and Ro 61-8048.	Kynurenine	154-166	kynurenine 3-monooxygenase	Homo sapiens	74-78
29526577-3	2018	These ideas include the inflammation-induced activation of the kynurenine pathway and its role in feeding and metabolism by activation of the aryl hydrocarbon receptor (AHR) and by modulating synaptic transmission in the brain.	Kynurenine	63-73	aryl hydrocarbon receptor	Homo sapiens	169-172
29393500-2	2018	IDO-mediated catabolic products, which are additionally termed "kynurenines", exerts important immunosuppressive functions primarily via regulating T effector cell anergy and inducing the proliferation of T regulatory cells.	Kynurenine	64-75	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-3
29473428-2	2018	Activation of IDO1 depletes tryptophan and produces kynurenine, which induces T cell anergy and suppresses tumor control by the immune system.	Kynurenine	52-62	indoleamine 2,3-dioxygenase 1	Homo sapiens	14-18
29369791-1	2018	An increasing body of evidence indicates that the activation of indoleamine-2,3-dyoxigenase (IDO), a first and rate-limiting enzyme in the kynurenine (KYN) pathway, is involved in Abeta1-42-neurotoxicity and AD pathogenesis.	Kynurenine	139-149	indoleamine 2,3-dioxygenase 1	Mus musculus	64-91
29369791-1	2018	An increasing body of evidence indicates that the activation of indoleamine-2,3-dyoxigenase (IDO), a first and rate-limiting enzyme in the kynurenine (KYN) pathway, is involved in Abeta1-42-neurotoxicity and AD pathogenesis.	Kynurenine	139-149	indoleamine 2,3-dioxygenase 1	Mus musculus	93-96
29369791-1	2018	An increasing body of evidence indicates that the activation of indoleamine-2,3-dyoxigenase (IDO), a first and rate-limiting enzyme in the kynurenine (KYN) pathway, is involved in Abeta1-42-neurotoxicity and AD pathogenesis.	Kynurenine	151-154	indoleamine 2,3-dioxygenase 1	Mus musculus	64-91
29369791-1	2018	An increasing body of evidence indicates that the activation of indoleamine-2,3-dyoxigenase (IDO), a first and rate-limiting enzyme in the kynurenine (KYN) pathway, is involved in Abeta1-42-neurotoxicity and AD pathogenesis.	Kynurenine	151-154	indoleamine 2,3-dioxygenase 1	Mus musculus	93-96
29155324-8	2018	Stress also downregulated intestinal amino acid transporter, ACE2/B0AT-1, and activity of intestinal mammalian target of rapamycin (mTOR) and p70 S6 kinase (p70S6K), resulting in decrease in alpha-defensins, changes in intestinal microbial contents, and perturbation of tryptophan metabolism with activation of the kynurenine pathway.	Kynurenine	315-325	mechanistic target of rapamycin kinase	Homo sapiens	101-130
29436668-0	2018	Kynurenine promotes the goblet cell differentiation of HT-29 colon carcinoma cells by modulating Wnt, Notch and AhR signals.	Kynurenine	0-10	aryl hydrocarbon receptor	Homo sapiens	112-115
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.	Kynurenine	194-204	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.	Kynurenine	178-188	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.	Kynurenine	178-188	indoleamine 2,3-dioxygenase 1	Homo sapiens	31-35
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.	Kynurenine	190-193	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.	Kynurenine	190-193	indoleamine 2,3-dioxygenase 1	Homo sapiens	31-35
29533786-4	2018	Kyn induces and activates AhR and thereby upregulates PD-1 expression.	Kynurenine	0-3	aryl hydrocarbon receptor	Sus scrofa	26-29
29241670-2	2018	Induction of immune and stress pathways is accompanied by increased tryptophan entry into the Kynurenine (Kyn) Pathway as governed by the rate-limiting enzymes indoleamine/tryptophan 2,3-dioxygenases (DO"s: Ido1, Ido2, Tdo2).	Kynurenine	94-104	indoleamine 2,3-dioxygenase 1	Mus musculus	207-211
29241670-2	2018	Induction of immune and stress pathways is accompanied by increased tryptophan entry into the Kynurenine (Kyn) Pathway as governed by the rate-limiting enzymes indoleamine/tryptophan 2,3-dioxygenases (DO"s: Ido1, Ido2, Tdo2).	Kynurenine	94-104	indoleamine 2,3-dioxygenase 2	Mus musculus	213-217
29241670-2	2018	Induction of immune and stress pathways is accompanied by increased tryptophan entry into the Kynurenine (Kyn) Pathway as governed by the rate-limiting enzymes indoleamine/tryptophan 2,3-dioxygenases (DO"s: Ido1, Ido2, Tdo2).	Kynurenine	94-104	tryptophan 2,3-dioxygenase	Mus musculus	219-223
29533786-2	2018	Here, we show that tumor-repopulating cells (TRCs) drive PD-1 upregulation in CD8+ T cells through a transcellular kynurenine (Kyn)-aryl hydrocarbon receptor (AhR) pathway.	Kynurenine	115-125	aryl hydrocarbon receptor	Sus scrofa	159-162
29155324-8	2018	Stress also downregulated intestinal amino acid transporter, ACE2/B0AT-1, and activity of intestinal mammalian target of rapamycin (mTOR) and p70 S6 kinase (p70S6K), resulting in decrease in alpha-defensins, changes in intestinal microbial contents, and perturbation of tryptophan metabolism with activation of the kynurenine pathway.	Kynurenine	315-325	mechanistic target of rapamycin kinase	Homo sapiens	132-136
29241670-2	2018	Induction of immune and stress pathways is accompanied by increased tryptophan entry into the Kynurenine (Kyn) Pathway as governed by the rate-limiting enzymes indoleamine/tryptophan 2,3-dioxygenases (DO"s: Ido1, Ido2, Tdo2).	Kynurenine	94-97	indoleamine 2,3-dioxygenase 1	Mus musculus	207-211
29241670-2	2018	Induction of immune and stress pathways is accompanied by increased tryptophan entry into the Kynurenine (Kyn) Pathway as governed by the rate-limiting enzymes indoleamine/tryptophan 2,3-dioxygenases (DO"s: Ido1, Ido2, Tdo2).	Kynurenine	94-97	indoleamine 2,3-dioxygenase 2	Mus musculus	213-217
29155324-8	2018	Stress also downregulated intestinal amino acid transporter, ACE2/B0AT-1, and activity of intestinal mammalian target of rapamycin (mTOR) and p70 S6 kinase (p70S6K), resulting in decrease in alpha-defensins, changes in intestinal microbial contents, and perturbation of tryptophan metabolism with activation of the kynurenine pathway.	Kynurenine	315-325	ribosomal protein S6 kinase B1	Homo sapiens	142-155
29241670-2	2018	Induction of immune and stress pathways is accompanied by increased tryptophan entry into the Kynurenine (Kyn) Pathway as governed by the rate-limiting enzymes indoleamine/tryptophan 2,3-dioxygenases (DO"s: Ido1, Ido2, Tdo2).	Kynurenine	94-97	tryptophan 2,3-dioxygenase	Mus musculus	219-223
29155324-8	2018	Stress also downregulated intestinal amino acid transporter, ACE2/B0AT-1, and activity of intestinal mammalian target of rapamycin (mTOR) and p70 S6 kinase (p70S6K), resulting in decrease in alpha-defensins, changes in intestinal microbial contents, and perturbation of tryptophan metabolism with activation of the kynurenine pathway.	Kynurenine	315-325	ribosomal protein S6 kinase B1	Homo sapiens	157-163
29343519-9	2018	Mechanistic probing revealed that kynurenine enhances thrombosis after vascular injury in an animal model and regulates thrombosis in an AHR-dependent manner.	Kynurenine	34-44	aryl hydrocarbon receptor	Homo sapiens	137-140
29217180-0	2018	Structure based mimicking of Phthalic acid esters (PAEs) and inhibition of hACMSD, an important enzyme of the tryptophan kynurenine metabolism pathway.	Kynurenine	121-131	aminocarboxymuconate semialdehyde decarboxylase	Homo sapiens	75-81
29217180-1	2018	Human alpha-amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase (hACMSD) is a zinc containing amidohydrolase which is a vital enzyme of the kynurenine pathway in tryptophan metabolism.	Kynurenine	150-160	aminocarboxymuconate semialdehyde decarboxylase	Homo sapiens	75-81
29217180-8	2018	The results emphasize that PAEs can structurally mimic the binding pattern of tryptophan metabolites to hACMSD, which further leads to inhibition of its activity and accumulation of the quinolate in the kynurenine pathway of tryptophan metabolism.	Kynurenine	203-213	aminocarboxymuconate semialdehyde decarboxylase	Homo sapiens	104-110
29315929-6	2018	In addition, the wdr5a-1 mutant had higher production and activity levels of the auxin biosynthetic enzyme TRYPTOPHAN AMINOTRANSFERASE OF ARABIDOPSIS1 (TAA1), in contrast to its reduced expression and activity in the WDR5a overexpression lines, and the increased root meristem growth in wdr5a-1 was suppressed by treatment with l-kynurenine, which inhibits TAA1, as well as by mutating TAA1.	Kynurenine	328-340	Transducin/WD40 repeat-like superfamily protein	Arabidopsis thaliana	17-22
29494675-3	2018	Indoleamine 2-3 dioxygenase 1 (IDO) is the first and rate-limiting enzyme involved in the conversion of tryptophan (Trp) into kynurenine (Kyn) pathway.	Kynurenine	126-136	indoleamine 2,3-dioxygenase 1	Mus musculus	0-29
29494675-3	2018	Indoleamine 2-3 dioxygenase 1 (IDO) is the first and rate-limiting enzyme involved in the conversion of tryptophan (Trp) into kynurenine (Kyn) pathway.	Kynurenine	126-136	indoleamine 2,3-dioxygenase 1	Mus musculus	31-34
29494675-3	2018	Indoleamine 2-3 dioxygenase 1 (IDO) is the first and rate-limiting enzyme involved in the conversion of tryptophan (Trp) into kynurenine (Kyn) pathway.	Kynurenine	138-141	indoleamine 2,3-dioxygenase 1	Mus musculus	0-29
29494675-3	2018	Indoleamine 2-3 dioxygenase 1 (IDO) is the first and rate-limiting enzyme involved in the conversion of tryptophan (Trp) into kynurenine (Kyn) pathway.	Kynurenine	138-141	indoleamine 2,3-dioxygenase 1	Mus musculus	31-34
29315929-6	2018	In addition, the wdr5a-1 mutant had higher production and activity levels of the auxin biosynthetic enzyme TRYPTOPHAN AMINOTRANSFERASE OF ARABIDOPSIS1 (TAA1), in contrast to its reduced expression and activity in the WDR5a overexpression lines, and the increased root meristem growth in wdr5a-1 was suppressed by treatment with l-kynurenine, which inhibits TAA1, as well as by mutating TAA1.	Kynurenine	328-340	tryptophan aminotransferase of Arabidopsis 1	Arabidopsis thaliana	107-150
29279331-0	2018	Trace derivatives of kynurenine potently activate the aryl hydrocarbon receptor (AHR).	Kynurenine	21-31	aryl hydrocarbon receptor	Homo sapiens	54-79
29254698-1	2018	Indoleamine 2,3-dioxygenase 1 (IDO1) and tryptophan 2,3-dioxygenase 2 (TDO2) catalyze the commitment step of the kynurenine (KYN) metabolic pathway.	Kynurenine	113-123	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-29
29254698-1	2018	Indoleamine 2,3-dioxygenase 1 (IDO1) and tryptophan 2,3-dioxygenase 2 (TDO2) catalyze the commitment step of the kynurenine (KYN) metabolic pathway.	Kynurenine	113-123	indoleamine 2,3-dioxygenase 1	Homo sapiens	31-35
29254698-1	2018	Indoleamine 2,3-dioxygenase 1 (IDO1) and tryptophan 2,3-dioxygenase 2 (TDO2) catalyze the commitment step of the kynurenine (KYN) metabolic pathway.	Kynurenine	113-123	tryptophan 2,3-dioxygenase	Homo sapiens	41-69
29254698-1	2018	Indoleamine 2,3-dioxygenase 1 (IDO1) and tryptophan 2,3-dioxygenase 2 (TDO2) catalyze the commitment step of the kynurenine (KYN) metabolic pathway.	Kynurenine	113-123	tryptophan 2,3-dioxygenase	Homo sapiens	71-75
29254698-1	2018	Indoleamine 2,3-dioxygenase 1 (IDO1) and tryptophan 2,3-dioxygenase 2 (TDO2) catalyze the commitment step of the kynurenine (KYN) metabolic pathway.	Kynurenine	125-128	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-29
29254698-1	2018	Indoleamine 2,3-dioxygenase 1 (IDO1) and tryptophan 2,3-dioxygenase 2 (TDO2) catalyze the commitment step of the kynurenine (KYN) metabolic pathway.	Kynurenine	125-128	indoleamine 2,3-dioxygenase 1	Homo sapiens	31-35
29254698-1	2018	Indoleamine 2,3-dioxygenase 1 (IDO1) and tryptophan 2,3-dioxygenase 2 (TDO2) catalyze the commitment step of the kynurenine (KYN) metabolic pathway.	Kynurenine	125-128	tryptophan 2,3-dioxygenase	Homo sapiens	41-69
29254698-1	2018	Indoleamine 2,3-dioxygenase 1 (IDO1) and tryptophan 2,3-dioxygenase 2 (TDO2) catalyze the commitment step of the kynurenine (KYN) metabolic pathway.	Kynurenine	125-128	tryptophan 2,3-dioxygenase	Homo sapiens	71-75
29279331-0	2018	Trace derivatives of kynurenine potently activate the aryl hydrocarbon receptor (AHR).	Kynurenine	21-31	aryl hydrocarbon receptor	Homo sapiens	81-84
29279331-3	2018	Despite its atypical, non-ligand-like, highly polar structure, kynurenine activates the aryl hydrocarbon receptor (AHR), a PER, ARNT, SIM (PAS) family transcription factor that responds to diverse environmental and cellular ligands.	Kynurenine	63-73	aryl hydrocarbon receptor	Homo sapiens	88-113
29279331-3	2018	Despite its atypical, non-ligand-like, highly polar structure, kynurenine activates the aryl hydrocarbon receptor (AHR), a PER, ARNT, SIM (PAS) family transcription factor that responds to diverse environmental and cellular ligands.	Kynurenine	63-73	aryl hydrocarbon receptor	Homo sapiens	115-118
29279331-3	2018	Despite its atypical, non-ligand-like, highly polar structure, kynurenine activates the aryl hydrocarbon receptor (AHR), a PER, ARNT, SIM (PAS) family transcription factor that responds to diverse environmental and cellular ligands.	Kynurenine	63-73	aryl hydrocarbon receptor nuclear translocator	Homo sapiens	128-132
29279331-4	2018	The activity of kynurenine is increased 100-1000-fold by incubation or long-term storage and relies on the hydrophobic ligand-binding pocket of AHR, with identical structural signatures for AHR induction before and after activation.	Kynurenine	16-26	aryl hydrocarbon receptor	Homo sapiens	144-147
29279331-4	2018	The activity of kynurenine is increased 100-1000-fold by incubation or long-term storage and relies on the hydrophobic ligand-binding pocket of AHR, with identical structural signatures for AHR induction before and after activation.	Kynurenine	16-26	aryl hydrocarbon receptor	Homo sapiens	190-193
29279331-7	2018	Our study provides evidence that kynurenine acts as an AHR pro-ligand, which requires novel chemical conversions to act as a receptor agonist.	Kynurenine	33-43	aryl hydrocarbon receptor	Homo sapiens	55-58
29118088-3	2018	IDO-mediated production of kynurenine and the kynurenine:tryptophan ratio in patient blood serum were determined for stage III NSCLC patients at times before, during, and after RT administration and then correlated to overall survival (OS), progression-free survival, and disease progression rate in patients.	Kynurenine	27-37	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-3
29468141-6	2018	Among Trp metabolites, AhR ligands consist of endogenous metabolites, including kynurenine, kynurenic acid, xanthurenic acid, and cinnabarinic acid, and bacterial metabolites, including indole, indole propionic acid, indole acetic acid, skatole, and tryptamine.	Kynurenine	80-90	aryl hydrocarbon receptor	Homo sapiens	23-26
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.	Kynurenine	97-100	indoleamine 2,3-dioxygenase 1	Rattus norvegicus	51-78
28689792-2	2018	Kynurenine (KYN), an endogenous tryptophan metabolite, can promote allergen-induced mast cell activation through the aryl hydrocarbon receptor (AhR).	Kynurenine	0-10	aryl-hydrocarbon receptor	Mus musculus	117-142
28689792-2	2018	Kynurenine (KYN), an endogenous tryptophan metabolite, can promote allergen-induced mast cell activation through the aryl hydrocarbon receptor (AhR).	Kynurenine	0-10	aryl-hydrocarbon receptor	Mus musculus	144-147
28689792-2	2018	Kynurenine (KYN), an endogenous tryptophan metabolite, can promote allergen-induced mast cell activation through the aryl hydrocarbon receptor (AhR).	Kynurenine	12-15	aryl-hydrocarbon receptor	Mus musculus	117-142
28689792-2	2018	Kynurenine (KYN), an endogenous tryptophan metabolite, can promote allergen-induced mast cell activation through the aryl hydrocarbon receptor (AhR).	Kynurenine	12-15	aryl-hydrocarbon receptor	Mus musculus	144-147
28689792-12	2018	Mast cells from ROS-resistant CaMKII MMVVdelta mice or pretreated with CaMKII inhibitor showed protection against KYN-promoted OVA-induced mast cell activation.	Kynurenine	114-117	calcium/calmodulin-dependent protein kinase II, beta	Mus musculus	30-36
28689792-12	2018	Mast cells from ROS-resistant CaMKII MMVVdelta mice or pretreated with CaMKII inhibitor showed protection against KYN-promoted OVA-induced mast cell activation.	Kynurenine	114-117	calcium/calmodulin-dependent protein kinase II, beta	Mus musculus	71-77
29317604-8	2018	Functional studies demonstrated that DEFB1 could neutralize lipopolysaccharide-stimulated expression of KYN-biosynthesizing enzymes in monocytic cells, resulting in altered KYN concentrations in the culture media.	Kynurenine	104-107	defensin beta 1	Homo sapiens	37-42
29317604-8	2018	Functional studies demonstrated that DEFB1 could neutralize lipopolysaccharide-stimulated expression of KYN-biosynthesizing enzymes in monocytic cells, resulting in altered KYN concentrations in the culture media.	Kynurenine	173-176	defensin beta 1	Homo sapiens	37-42
29317604-9	2018	In addition, we demonstrated that AHR was involved in regulating the expression of enzymes in the KYN pathway and altered KYN biosynthesis in cell lines of hepatocyte and astrocyte origin.	Kynurenine	98-101	aryl hydrocarbon receptor	Homo sapiens	34-37
29317604-9	2018	In addition, we demonstrated that AHR was involved in regulating the expression of enzymes in the KYN pathway and altered KYN biosynthesis in cell lines of hepatocyte and astrocyte origin.	Kynurenine	122-125	aryl hydrocarbon receptor	Homo sapiens	34-37
29343967-1	2018	IFN-gamma activation of mononuclear phagocytes significantly increases indoleamine 2,3-dioxygenase (IDO) and flux through the kynurenine pathway (KP).	Kynurenine	126-136	interferon gamma	Homo sapiens	0-9
29387039-9	2017	This is the first study to provide evidence for a direct link between PACAP and the kynurenine system during TS activation.	Kynurenine	84-94	adenylate cyclase activating polypeptide 1	Rattus norvegicus	70-75
29320557-9	2018	High AHR expression was correlated with high expression of several genes involved in signaling pathways related to inflammation (IL1B, IL6, TNF, IL8 and CXCR4), metabolism (IDO1 and TDO2 from the kynurenine pathway), invasion (MMP1, MMP2 and PLAU), and IGF signaling (IGF2R, IGF1R and TGFB1).	Kynurenine	196-206	aryl hydrocarbon receptor	Homo sapiens	5-8
29320557-9	2018	High AHR expression was correlated with high expression of several genes involved in signaling pathways related to inflammation (IL1B, IL6, TNF, IL8 and CXCR4), metabolism (IDO1 and TDO2 from the kynurenine pathway), invasion (MMP1, MMP2 and PLAU), and IGF signaling (IGF2R, IGF1R and TGFB1).	Kynurenine	196-206	indoleamine 2,3-dioxygenase 1	Homo sapiens	173-177
29320557-9	2018	High AHR expression was correlated with high expression of several genes involved in signaling pathways related to inflammation (IL1B, IL6, TNF, IL8 and CXCR4), metabolism (IDO1 and TDO2 from the kynurenine pathway), invasion (MMP1, MMP2 and PLAU), and IGF signaling (IGF2R, IGF1R and TGFB1).	Kynurenine	196-206	tryptophan 2,3-dioxygenase	Homo sapiens	182-186
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.	Kynurenine	97-100	indoleamine 2,3-dioxygenase 1	Rattus norvegicus	80-83
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.	Kynurenine	123-126	indoleamine 2,3-dioxygenase 1	Homo sapiens	50-77
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).	Kynurenine	180-190	interferon gamma	Homo sapiens	25-34
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).	Kynurenine	180-190	tumor necrosis factor	Homo sapiens	36-44
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).	Kynurenine	180-190	interleukin 1 beta	Homo sapiens	49-57
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).	Kynurenine	180-190	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).	Kynurenine	180-190	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).	Kynurenine	192-195	interferon gamma	Homo sapiens	25-34
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).	Kynurenine	192-195	tumor necrosis factor	Homo sapiens	36-44
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).	Kynurenine	192-195	interleukin 1 beta	Homo sapiens	49-57
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).	Kynurenine	192-195	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).	Kynurenine	192-195	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.	Kynurenine	123-126	indoleamine 2,3-dioxygenase 1	Homo sapiens	79-82
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.	Kynurenine	187-197	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.	Kynurenine	187-197	indoleamine 2,3-dioxygenase 1	Homo sapiens	48-52
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.	Kynurenine	136-146	indoleamine 2,3-dioxygenase 1	Homo sapiens	17-46
30134237-2	2018	Upregulation of IDO1 decreases tryptophan levels and increases the accumulation of kynurenine and its metabolites.	Kynurenine	83-93	indoleamine 2,3-dioxygenase 1	Homo sapiens	16-20
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.	Kynurenine	136-146	indoleamine 2,3-dioxygenase 1	Homo sapiens	48-52
30430940-9	2018	Activated immune-inflammatory pathways induce indoleamine-2,3-dioxynease (IDO) and the tryptophan catabolite (TRYCAT) pathway thereby increasing tryptophan degradation and increasing the production of TRYCATs including kynurenine and quinolinic acid, which may create an overall anxiogenic effect.	Kynurenine	219-229	indoleamine 2,3-dioxygenase 1	Homo sapiens	74-77
29080383-1	2018	Indoleamine 2,3-dioxygenase 1 (IDO) is an enzyme catabolizing tryptophan (Trp) into the kynurenine (Kyn) pathway.	Kynurenine	88-98	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.	Kynurenine	88-98	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.	Kynurenine	100-103	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.	Kynurenine	100-103	indoleamine 2,3-dioxygenase 1	Homo sapiens	31-34
29080383-10	2018	Indoleamine 2,3-dioxygenase 1 was produced by macrophages/dendritic cells, but not by HL tumor cells, and IDO levels determined by immunohistochemistry had a significant positive correlation with the serum Kyn/Trp ratio.	Kynurenine	206-209	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-29
29080383-10	2018	Indoleamine 2,3-dioxygenase 1 was produced by macrophages/dendritic cells, but not by HL tumor cells, and IDO levels determined by immunohistochemistry had a significant positive correlation with the serum Kyn/Trp ratio.	Kynurenine	206-209	indoleamine 2,3-dioxygenase 1	Homo sapiens	106-109
28978552-3	2017	METHODS: Indoleamine 2,3-dioxygenase (IDO) is the first and rate-limiting enzyme in the kynurenine pathway of tryptophan metabolism.	Kynurenine	88-98	indoleamine 2,3-dioxygenase 1	Mus musculus	38-41
29807576-1	2018	Tryptophan is metabolized primarily via the kynurenine pathway (KP), which involves several enzymes, including indoleamine 2,3-dioxygenase, tryptophan 2,3 dioxygenase (TDO), kynurenine aminotransferases (KATs), kynurenine monooxygenase (KMO) etc.	Kynurenine	44-54	tryptophan 2,3-dioxygenase	Homo sapiens	140-166
29807576-1	2018	Tryptophan is metabolized primarily via the kynurenine pathway (KP), which involves several enzymes, including indoleamine 2,3-dioxygenase, tryptophan 2,3 dioxygenase (TDO), kynurenine aminotransferases (KATs), kynurenine monooxygenase (KMO) etc.	Kynurenine	44-54	tryptophan 2,3-dioxygenase	Homo sapiens	168-171
29807576-1	2018	Tryptophan is metabolized primarily via the kynurenine pathway (KP), which involves several enzymes, including indoleamine 2,3-dioxygenase, tryptophan 2,3 dioxygenase (TDO), kynurenine aminotransferases (KATs), kynurenine monooxygenase (KMO) etc.	Kynurenine	44-54	kynurenine 3-monooxygenase	Homo sapiens	211-235
29807576-1	2018	Tryptophan is metabolized primarily via the kynurenine pathway (KP), which involves several enzymes, including indoleamine 2,3-dioxygenase, tryptophan 2,3 dioxygenase (TDO), kynurenine aminotransferases (KATs), kynurenine monooxygenase (KMO) etc.	Kynurenine	44-54	kynurenine 3-monooxygenase	Homo sapiens	237-240
29153599-4	2017	We confirmed that systemic blockade of kynurenine-3 monooxygenase in conjunction with kynurenine administration results in significant increases in Nrgn phosphorylation and a significant reduction of CaMKII phosphorylation in the mPFC.	Kynurenine	39-49	neurogranin	Homo sapiens	148-152
29153599-4	2017	We confirmed that systemic blockade of kynurenine-3 monooxygenase in conjunction with kynurenine administration results in significant increases in Nrgn phosphorylation and a significant reduction of CaMKII phosphorylation in the mPFC.	Kynurenine	39-49	calcium/calmodulin dependent protein kinase II gamma	Homo sapiens	200-206
29102224-18	2018	Another endogenous AHR agonist, kynurenine, also inhibited the TGF-beta-mediated ACTA2 and collagen I upregulation in NHDFs in an AHR-independent manner; however, its effects were insignificant in comparison with those of FICZ.	Kynurenine	32-42	aryl hydrocarbon receptor	Homo sapiens	19-22
29102224-18	2018	Another endogenous AHR agonist, kynurenine, also inhibited the TGF-beta-mediated ACTA2 and collagen I upregulation in NHDFs in an AHR-independent manner; however, its effects were insignificant in comparison with those of FICZ.	Kynurenine	32-42	transforming growth factor beta 1	Homo sapiens	63-71
29102224-18	2018	Another endogenous AHR agonist, kynurenine, also inhibited the TGF-beta-mediated ACTA2 and collagen I upregulation in NHDFs in an AHR-independent manner; however, its effects were insignificant in comparison with those of FICZ.	Kynurenine	32-42	actin alpha 2, smooth muscle	Homo sapiens	81-86
29102224-18	2018	Another endogenous AHR agonist, kynurenine, also inhibited the TGF-beta-mediated ACTA2 and collagen I upregulation in NHDFs in an AHR-independent manner; however, its effects were insignificant in comparison with those of FICZ.	Kynurenine	32-42	aryl hydrocarbon receptor	Homo sapiens	130-133
29856028-0	2018	Assessing and Modulating Kynurenine Pathway Dynamics in Huntington"s Disease: Focus on Kynurenine 3-Monooxygenase.	Kynurenine	25-35	kynurenine 3-monooxygenase	Homo sapiens	87-113
28805262-9	2018	MSCs significantly attenuated CCl4 -induced liver fibrosis by decreasing serum levels of inflammatory IL-17, increasing immunosuppressive IL-10, IDO, and kynurenine, reducing number of IL-17 producing Th17 cells, and increasing percentage of CD4+ IL-10+ T cells.	Kynurenine	154-164	chemokine (C-C motif) ligand 4	Mus musculus	30-34
28470889-7	2017	Although in vivo IL-2 administration increased low Trp + Kyn iTreg persistence on adoptive transfer into immunodeficient mice given peripheral blood mononuclear cells to induce GVHD, IL-2-supported iTregs did not improve recipient survival.	Kynurenine	57-60	interleukin 2	Mus musculus	17-21
28470889-7	2017	Although in vivo IL-2 administration increased low Trp + Kyn iTreg persistence on adoptive transfer into immunodeficient mice given peripheral blood mononuclear cells to induce GVHD, IL-2-supported iTregs did not improve recipient survival.	Kynurenine	57-60	interleukin 2	Mus musculus	183-187
29120388-4	2017	Among the compounds synthesized, compound 8a inhibited both tryptophan depletion and kynurenine production through the IDO1 enzyme.	Kynurenine	85-95	indoleamine 2,3-dioxygenase 1	Homo sapiens	119-123
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.	Kynurenine	156-166	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.	Kynurenine	36-46	indoleamine 2,3-dioxygenase 1	Homo sapiens	54-58
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.	Kynurenine	48-51	indoleamine 2,3-dioxygenase 1	Homo sapiens	54-58
28557618-6	2017	Myeloid, glycolysis metabolic signatures, and correlation between IDO1 expression and Trp to Kyn conversion are also shown.	Kynurenine	93-96	indoleamine 2,3-dioxygenase 1	Homo sapiens	66-70
28187857-1	2017	BACKGROUND: Kynurenine 3-monooxygenase converts kynurenine to 3-hydroxykynurenine, and its inhibition shunts the kynurenine pathway-which is implicated as dysfunctional in various psychiatric disorders-toward enhanced synthesis of kynurenic acid, an antagonist of both alpha7 nicotinic acetylcholine and N-methyl-D-aspartate receptors.	Kynurenine	48-58	kynurenine 3-monooxygenase (kynurenine 3-hydroxylase)	Mus musculus	12-38
28187857-1	2017	BACKGROUND: Kynurenine 3-monooxygenase converts kynurenine to 3-hydroxykynurenine, and its inhibition shunts the kynurenine pathway-which is implicated as dysfunctional in various psychiatric disorders-toward enhanced synthesis of kynurenic acid, an antagonist of both alpha7 nicotinic acetylcholine and N-methyl-D-aspartate receptors.	Kynurenine	71-81	kynurenine 3-monooxygenase (kynurenine 3-hydroxylase)	Mus musculus	12-38
28709913-3	2017	We investigated whether brain interleukin (IL)-1 signaling and activity of kynurenine 3-monoxygenase (KMO), a key enzyme for metabolism of kynurenine into the neurotoxic NMDA receptor agonist quinolinic acid, are necessary for comorbid neuropathic pain and depression-like behavior.	Kynurenine	75-85	kynurenine 3-monooxygenase (kynurenine 3-hydroxylase)	Mus musculus	102-105
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.	Kynurenine	196-206	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.	Kynurenine	196-206	indoleamine 2,3-dioxygenase 1	Homo sapiens	127-130
28727234-10	2017	Further, kyn treatment significantly increased bone marrow adiposity, and BMSCs isolated from the kyn-injected mice exhibited decreased mRNA expression of Hdac3 and its cofactor NCoR1 and increased expression of lipid storage genes Cidec and Plin1.	Kynurenine	98-101	nuclear receptor co-repressor 1	Mus musculus	178-183
28727234-10	2017	Further, kyn treatment significantly increased bone marrow adiposity, and BMSCs isolated from the kyn-injected mice exhibited decreased mRNA expression of Hdac3 and its cofactor NCoR1 and increased expression of lipid storage genes Cidec and Plin1.	Kynurenine	98-101	histone deacetylase 3	Mus musculus	155-160
28727234-10	2017	Further, kyn treatment significantly increased bone marrow adiposity, and BMSCs isolated from the kyn-injected mice exhibited decreased mRNA expression of Hdac3 and its cofactor NCoR1 and increased expression of lipid storage genes Cidec and Plin1.	Kynurenine	98-101	cell death-inducing DFFA-like effector c	Mus musculus	232-237
28727234-8	2017	Levels of serum markers of osteoclastic activity (pyridinoline [PYD] and RANKL) increased significantly with kyn treatment.	Kynurenine	109-112	tumor necrosis factor (ligand) superfamily, member 11	Mus musculus	73-78
28727234-10	2017	Further, kyn treatment significantly increased bone marrow adiposity, and BMSCs isolated from the kyn-injected mice exhibited decreased mRNA expression of Hdac3 and its cofactor NCoR1 and increased expression of lipid storage genes Cidec and Plin1.	Kynurenine	98-101	perilipin 1	Mus musculus	242-247
29163188-13	2017	In conclusion, our data suggest that CKD-induced elevated levels of peripheral kynurenine cause pathological changes in bone structure via AhR pathway.	Kynurenine	79-89	aryl hydrocarbon receptor	Rattus norvegicus	139-142
29051706-1	2017	Indoleamine 2,3-dioxygenase-2 (IDO2) is 1 of the 3 enzymes that can catalyze the first step in the kynurenine pathway of tryptophan metabolism.	Kynurenine	99-109	indoleamine 2,3-dioxygenase 2	Mus musculus	0-29
29017244-2	2017	Indoleamine 2, 3-dioxygenase (IDO) is an immunoregulatory enzyme that breaks down tryptophan (Trp) to metabolites known as kynurenines (Kyns).	Kynurenine	123-134	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).	Kynurenine	123-134	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.	Kynurenine	66-69	indoleamine 2,3-dioxygenase 1	Homo sapiens	24-27
29037255-2	2017	Indoleamine 2,3-dioxygenase (IDO) is the rate-limiting oxidoreductase that catalyzes the degradation of tryptophan to kynurenine.	Kynurenine	118-128	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.	Kynurenine	118-128	indoleamine 2,3-dioxygenase 1	Homo sapiens	29-32
29051706-1	2017	Indoleamine 2,3-dioxygenase-2 (IDO2) is 1 of the 3 enzymes that can catalyze the first step in the kynurenine pathway of tryptophan metabolism.	Kynurenine	99-109	indoleamine 2,3-dioxygenase 2	Mus musculus	31-35
29038460-1	2017	Indoleamine 2,3 dioxygenase-1 (IDO-1) is an enzyme in the kynurenine pathway which augments tumor-induced immune tolerance.	Kynurenine	58-68	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-29
29051706-6	2017	Our analysis, undertaken in Ido2 +/+ and Ido2-/- mice using immunohistochemistry and measurement of tryptophan and kynurenine levels, suggested an even more restricted pattern of tissue expression than previously reported.	Kynurenine	115-125	indoleamine 2,3-dioxygenase 2	Mus musculus	41-45
29038460-1	2017	Indoleamine 2,3 dioxygenase-1 (IDO-1) is an enzyme in the kynurenine pathway which augments tumor-induced immune tolerance.	Kynurenine	58-68	indoleamine 2,3-dioxygenase 1	Homo sapiens	31-36
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.	Kynurenine	176-186	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.	Kynurenine	188-191	indoleamine 2,3-dioxygenase 1	Homo sapiens	77-80
28529072-6	2017	Moreover, EPA and DHA also reversed the IL-1beta-induced increase in kynurenine, as well as mRNA levels of indolamine-2,3-dioxygenase (IDO); while DHA and sertraline reverted the IL-1beta-induced increase in quinolinic acid and mRNA levels of kynurenine 3-monooxygenase (KMO).	Kynurenine	69-79	interleukin 1 beta	Homo sapiens	40-48
28905195-0	2017	Experimental evidences for miR-30b as a negative regulator of FOXO3 upregulated by kynurenine.	Kynurenine	83-93	microRNA 30b	Homo sapiens	27-34
28905195-0	2017	Experimental evidences for miR-30b as a negative regulator of FOXO3 upregulated by kynurenine.	Kynurenine	83-93	forkhead box O3	Homo sapiens	62-67
28905195-2	2017	On one hand, kynurenine (Kyn), one of the microenvironment components, plays key roles in the metastasis of cancer cells in vivo; on the other hand, forkhead box O3 (FOXO3) can serve as a therapeutic target of various anticancer drugs.	Kynurenine	13-23	forkhead box O3	Homo sapiens	149-164
28905195-2	2017	On one hand, kynurenine (Kyn), one of the microenvironment components, plays key roles in the metastasis of cancer cells in vivo; on the other hand, forkhead box O3 (FOXO3) can serve as a therapeutic target of various anticancer drugs.	Kynurenine	13-23	forkhead box O3	Homo sapiens	166-171
28905195-2	2017	On one hand, kynurenine (Kyn), one of the microenvironment components, plays key roles in the metastasis of cancer cells in vivo; on the other hand, forkhead box O3 (FOXO3) can serve as a therapeutic target of various anticancer drugs.	Kynurenine	25-28	forkhead box O3	Homo sapiens	166-171
28905195-7	2017	More importantly, miR-30b-induced suppression of FOXO3 protein was significantly attenuated on Kyn treatment, which demonstrated that Kyn-mediated increase of FOXO3 depended at least partly on miR-30b.	Kynurenine	95-98	microRNA 30b	Homo sapiens	18-25
28905195-7	2017	More importantly, miR-30b-induced suppression of FOXO3 protein was significantly attenuated on Kyn treatment, which demonstrated that Kyn-mediated increase of FOXO3 depended at least partly on miR-30b.	Kynurenine	95-98	forkhead box O3	Homo sapiens	49-54
28905195-7	2017	More importantly, miR-30b-induced suppression of FOXO3 protein was significantly attenuated on Kyn treatment, which demonstrated that Kyn-mediated increase of FOXO3 depended at least partly on miR-30b.	Kynurenine	95-98	forkhead box O3	Homo sapiens	159-164
28905195-7	2017	More importantly, miR-30b-induced suppression of FOXO3 protein was significantly attenuated on Kyn treatment, which demonstrated that Kyn-mediated increase of FOXO3 depended at least partly on miR-30b.	Kynurenine	95-98	microRNA 30b	Homo sapiens	193-200
28905195-7	2017	More importantly, miR-30b-induced suppression of FOXO3 protein was significantly attenuated on Kyn treatment, which demonstrated that Kyn-mediated increase of FOXO3 depended at least partly on miR-30b.	Kynurenine	134-137	microRNA 30b	Homo sapiens	18-25
28905195-7	2017	More importantly, miR-30b-induced suppression of FOXO3 protein was significantly attenuated on Kyn treatment, which demonstrated that Kyn-mediated increase of FOXO3 depended at least partly on miR-30b.	Kynurenine	134-137	forkhead box O3	Homo sapiens	49-54
28905195-7	2017	More importantly, miR-30b-induced suppression of FOXO3 protein was significantly attenuated on Kyn treatment, which demonstrated that Kyn-mediated increase of FOXO3 depended at least partly on miR-30b.	Kynurenine	134-137	forkhead box O3	Homo sapiens	159-164
28905195-7	2017	More importantly, miR-30b-induced suppression of FOXO3 protein was significantly attenuated on Kyn treatment, which demonstrated that Kyn-mediated increase of FOXO3 depended at least partly on miR-30b.	Kynurenine	134-137	microRNA 30b	Homo sapiens	193-200
28905195-8	2017	In addition, Kyn-mediated upregulation of migration, a method of measuring cancer metastasis, was markedly decreased on miR-30b treatment, in vitro, which was altered in some degree via regulating FOXO3.	Kynurenine	13-16	microRNA 30b	Homo sapiens	120-127
28905195-8	2017	In addition, Kyn-mediated upregulation of migration, a method of measuring cancer metastasis, was markedly decreased on miR-30b treatment, in vitro, which was altered in some degree via regulating FOXO3.	Kynurenine	13-16	forkhead box O3	Homo sapiens	197-202
28631232-6	2017	These results implicate IDO as a critical molecular mediator of STZ-induced depressive-like behavior, likely through activation of the kynurenine pathway and subsequent reduction of BDNF levels.	Kynurenine	135-145	indoleamine 2,3-dioxygenase 1	Mus musculus	24-27
28631232-8	2017	The present study not only provides evidence that IDO plays a critical role in mediating inflammation-induced depression but also supports the notion that neuroinflammation and the kynurenine pathway are important targets for novel therapeutic drugs for depression.	Kynurenine	181-191	indoleamine 2,3-dioxygenase 1	Mus musculus	50-53
28402179-1	2017	While upregulation of 2,3-dioxygenase (IDO) accompanied by degradation of tryptophan along the kynurenine pathway have been reported to exert antimicrobial effects against a wide range of infectious agents, its role in the replication of influenza A virus remains uncertain.	Kynurenine	95-105	indoleamine 2,3-dioxygenase 1	Mus musculus	39-42
28963435-7	2017	To demonstrate the inhibition in intact cells, AhR (aryl hydrocarbon receptor) activity was monitored as readout for IDO1-mediated generation of the endogenous AhR agonist kynurenine in pancreatic and liver cancer cells.	Kynurenine	172-182	indoleamine 2,3-dioxygenase 1	Homo sapiens	117-121
28963435-7	2017	To demonstrate the inhibition in intact cells, AhR (aryl hydrocarbon receptor) activity was monitored as readout for IDO1-mediated generation of the endogenous AhR agonist kynurenine in pancreatic and liver cancer cells.	Kynurenine	172-182	aryl hydrocarbon receptor	Homo sapiens	160-163
28922389-5	2017	The association to kynurenine points towards a pro-inflammatory state with increasing OCN.	Kynurenine	19-29	bone gamma-carboxyglutamate protein	Homo sapiens	86-89
28688912-1	2017	Brain glia possess the rate limiting enzyme indoleamine 2, 3-dioxygenase (IDO) which catalyses the conversion of tryptophan to kynurenine.	Kynurenine	127-137	indoleamine 2,3-dioxygenase 1	Homo sapiens	74-77
28688912-3	2017	The aim of this study was to examine the effect of IFNgamma-stimulated kynurenine pathway (KP) induction in microglia on neurite outgrowth and complexity, and to determine whether alterations could be abrogated using pharmacological inhibitors of the KP.	Kynurenine	71-81	interferon gamma	Homo sapiens	51-59
28688912-6	2017	Results show increased mRNA expression of IDO, KMO and KYNU, and increased concentrations of tryptophan, kynurenine, and 3-hydroxykynurenine in the CM of IFNgamma-stimulated BV-2 microglia.	Kynurenine	105-115	interferon gamma	Homo sapiens	154-162
28098246-4	2017	In parallel, we demonstrated that IFNgamma induction of indoleamine 2,3-dioxygenase 1, an enzyme that catalyzes the conversion of Trp to kynurenine (Kyn), induces IL-10R1 expression.	Kynurenine	137-147	interferon gamma	Mus musculus	34-42
28098246-4	2017	In parallel, we demonstrated that IFNgamma induction of indoleamine 2,3-dioxygenase 1, an enzyme that catalyzes the conversion of Trp to kynurenine (Kyn), induces IL-10R1 expression.	Kynurenine	137-147	indoleamine 2,3-dioxygenase 1	Mus musculus	56-85
28098246-4	2017	In parallel, we demonstrated that IFNgamma induction of indoleamine 2,3-dioxygenase 1, an enzyme that catalyzes the conversion of Trp to kynurenine (Kyn), induces IL-10R1 expression.	Kynurenine	137-147	interleukin 10 receptor, alpha	Mus musculus	163-170
28098246-4	2017	In parallel, we demonstrated that IFNgamma induction of indoleamine 2,3-dioxygenase 1, an enzyme that catalyzes the conversion of Trp to kynurenine (Kyn), induces IL-10R1 expression.	Kynurenine	149-152	interferon gamma	Mus musculus	34-42
28098246-4	2017	In parallel, we demonstrated that IFNgamma induction of indoleamine 2,3-dioxygenase 1, an enzyme that catalyzes the conversion of Trp to kynurenine (Kyn), induces IL-10R1 expression.	Kynurenine	149-152	indoleamine 2,3-dioxygenase 1	Mus musculus	56-85
28098246-4	2017	In parallel, we demonstrated that IFNgamma induction of indoleamine 2,3-dioxygenase 1, an enzyme that catalyzes the conversion of Trp to kynurenine (Kyn), induces IL-10R1 expression.	Kynurenine	149-152	interleukin 10 receptor, alpha	Mus musculus	163-170
28098246-9	2017	Finally, reduction of murine dextran sodium sulfate colitis through Kyn administration correlates with colonic IL-10R1 expression.	Kynurenine	68-71	interleukin 10 receptor, alpha	Mus musculus	111-118
27376248-6	2017	IDO activity was determined by measuring the concentration of kynurenine in the culture medium using a HPLC technique.	Kynurenine	62-72	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-3
29190885-2	2017	Trp catabolism generates molecules known as kynurenines, whose tolerance mechanisms involve activation of the Aryl Hydrocarbon Receptor (AHR).	Kynurenine	44-55	aryl hydrocarbon receptor	Homo sapiens	110-135
29190885-2	2017	Trp catabolism generates molecules known as kynurenines, whose tolerance mechanisms involve activation of the Aryl Hydrocarbon Receptor (AHR).	Kynurenine	44-55	aryl hydrocarbon receptor	Homo sapiens	137-140
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).	Kynurenine	257-267	intestine specific homeobox	Homo sapiens	14-17
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).	Kynurenine	257-267	interleukin 6	Homo sapiens	27-30
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).	Kynurenine	257-267	indoleamine 2,3-dioxygenase 1	Homo sapiens	86-115
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).	Kynurenine	257-267	indoleamine 2,3-dioxygenase 1	Homo sapiens	117-121
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).	Kynurenine	257-267	tryptophan 2,3-dioxygenase	Homo sapiens	127-153
28792876-7	2017	RESULTS: Variants were identified in two genes that encode enzymes of the kynurenine pathway, 3-hydroxyanthranilic acid 3,4-dioxygenase (HAAO) and kynureninase (KYNU).	Kynurenine	74-84	3-hydroxyanthranilate 3,4-dioxygenase	Homo sapiens	94-135
28792876-7	2017	RESULTS: Variants were identified in two genes that encode enzymes of the kynurenine pathway, 3-hydroxyanthranilic acid 3,4-dioxygenase (HAAO) and kynureninase (KYNU).	Kynurenine	74-84	3-hydroxyanthranilate 3,4-dioxygenase	Homo sapiens	137-141
28792876-7	2017	RESULTS: Variants were identified in two genes that encode enzymes of the kynurenine pathway, 3-hydroxyanthranilic acid 3,4-dioxygenase (HAAO) and kynureninase (KYNU).	Kynurenine	74-84	kynureninase	Homo sapiens	161-165
27376248-8	2017	Our results demonstrated that DMF and MMF dose-dependently reduced the levels of L-kynurenine in PBMCs activated by interferon-gamma (IFN-gamma).	Kynurenine	81-93	interferon gamma	Homo sapiens	116-132
27376248-8	2017	Our results demonstrated that DMF and MMF dose-dependently reduced the levels of L-kynurenine in PBMCs activated by interferon-gamma (IFN-gamma).	Kynurenine	81-93	interferon gamma	Homo sapiens	134-143
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.	Kynurenine	275-285	indoleamine 2,3-dioxygenase 1	Homo sapiens	35-38
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.	Kynurenine	151-161	indoleamine 2,3-dioxygenase 1	Homo sapiens	45-49
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.	Kynurenine	78-88	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.	Kynurenine	78-88	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.	Kynurenine	21-31	indoleamine 2,3-dioxygenase 1	Homo sapiens	8-11
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.	Kynurenine	121-131	indoleamine 2,3-dioxygenase 1	Homo sapiens	108-111
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.	Kynurenine	125-135	indoleamine 2,3-dioxygenase 1	Homo sapiens	112-115
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.	Kynurenine	151-161	tryptophan 2,3-dioxygenase	Homo sapiens	54-58
28159919-1	2017	IDO1 is an enzyme catalyzing the initial and rate-limiting step in the catabolism of tryptophan along the kynurenine pathway.	Kynurenine	106-116	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-4
28502732-1	2017	Emerging evidence indicates that the activation of indoleamine-2,3-dioxygenase (IDO), a first and rate-limiting enzyme in the kynurenine (KYN) pathway, is involved in amyloid-beta (Abeta1-42)-neurotoxicity and Alzheimer"s disease (AD) pathogenesis.	Kynurenine	126-136	indoleamine 2,3-dioxygenase 1	Mus musculus	80-83
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.	Kynurenine	119-129	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.	Kynurenine	119-129	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.	Kynurenine	131-134	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.	Kynurenine	131-134	indoleamine 2,3-dioxygenase 1	Homo sapiens	41-44
28419874-4	2017	We determined, in adult Wistar rats, if the orally available KAT II inhibitor BFF816 a) prevents KYNA elevations in prefrontal cortex (PFC) after a systemic kynurenine injection and b) reverses the kynurenine-induced attenuation of evoked prefrontal glutamate release caused by stimulation of the nucleus accumbens shell (NAcSh).	Kynurenine	157-167	aminoadipate aminotransferase	Rattus norvegicus	61-67
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.	Kynurenine	103-113	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.	Kynurenine	103-113	indoleamine 2,3-dioxygenase 1	Homo sapiens	31-35
28419874-4	2017	We determined, in adult Wistar rats, if the orally available KAT II inhibitor BFF816 a) prevents KYNA elevations in prefrontal cortex (PFC) after a systemic kynurenine injection and b) reverses the kynurenine-induced attenuation of evoked prefrontal glutamate release caused by stimulation of the nucleus accumbens shell (NAcSh).	Kynurenine	198-208	aminoadipate aminotransferase	Rattus norvegicus	61-67
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.	Kynurenine	46-56	indoleamine 2,3-dioxygenase 1	Homo sapiens	191-218
28559281-8	2017	Supplementation with kynurenine pathway intermediates also boosted NAD+ levels and partially reversed NAD+-dependent phenotypes caused by mutation of pnc-1, which encodes a nicotinamidase required for NAD+ salvage biosynthesis, demonstrating contribution of de novo synthesis to NAD+ homeostasis.	Kynurenine	21-31	Isochorismatase domain-containing protein	Caenorhabditis elegans	150-155
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.	Kynurenine	153-163	interferon gamma	Homo sapiens	34-50
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.	Kynurenine	153-163	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.	Kynurenine	153-163	indoleamine 2,3-dioxygenase 1	Homo sapiens	98-101
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.	Kynurenine	46-56	indoleamine 2,3-dioxygenase 1	Homo sapiens	220-223
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.	Kynurenine	281-291	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.	Kynurenine	281-291	indoleamine 2,3-dioxygenase 1	Homo sapiens	220-223
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.	Kynurenine	46-49	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.	Kynurenine	46-49	indoleamine 2,3-dioxygenase 1	Homo sapiens	220-223
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.	Kynurenine	166-176	indoleamine 2,3-dioxygenase 1	Homo sapiens	94-121
28456683-12	2017	By comparison, up-regulation of IDO-1 and TPH-1 protein expression in DSS group was suppressed by PA, which was in line with the declined levels of kynurenine (Kyn) and 5-hydroxytryptophan (5-HTP) in plasma.	Kynurenine	148-158	indoleamine 2,3-dioxygenase 1	Mus musculus	32-37
28456683-12	2017	By comparison, up-regulation of IDO-1 and TPH-1 protein expression in DSS group was suppressed by PA, which was in line with the declined levels of kynurenine (Kyn) and 5-hydroxytryptophan (5-HTP) in plasma.	Kynurenine	160-163	indoleamine 2,3-dioxygenase 1	Mus musculus	32-37
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.	Kynurenine	166-176	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).	Kynurenine	113-123	indoleamine 2,3-dioxygenase 1	Homo sapiens	80-83
28076309-7	2017	IDO and kynurenine showed a strong positive correlation with markers of infection (procalcitonin) and inflammation (C-reactive protein) as well as sepsis and CAP severity scores.	Kynurenine	8-18	C-reactive protein	Homo sapiens	116-134
28465467-1	2017	Indoleamine 2,3-dioxygenase 1 (IDO1) is an intracellular rate-limiting enzyme in the metabolism of tryptophan along the kynurenine pathway, subsequently mediating the immune response; however, the role of IDO1 in liver fibrosis and cirrhosis is still unclear.	Kynurenine	120-130	indoleamine 2,3-dioxygenase 1	Mus musculus	0-29
28465467-1	2017	Indoleamine 2,3-dioxygenase 1 (IDO1) is an intracellular rate-limiting enzyme in the metabolism of tryptophan along the kynurenine pathway, subsequently mediating the immune response; however, the role of IDO1 in liver fibrosis and cirrhosis is still unclear.	Kynurenine	120-130	indoleamine 2,3-dioxygenase 1	Mus musculus	31-35
28478038-0	2017	Successful metformin treatment of insulin resistance is associated with down-regulation of the kynurenine pathway.	Kynurenine	95-105	insulin	Homo sapiens	34-41
28478038-1	2017	CONTEXT: An extensive body of literature indicates a relationship between insulin resistance and the up-regulation of the kynurenine pathway, i.e. the preferential conversion of tryptophan to kynurenine, with subsequent overproduction of diabetogenic downstream metabolites, such as kynurenic acid.	Kynurenine	122-132	insulin	Homo sapiens	74-81
28478038-1	2017	CONTEXT: An extensive body of literature indicates a relationship between insulin resistance and the up-regulation of the kynurenine pathway, i.e. the preferential conversion of tryptophan to kynurenine, with subsequent overproduction of diabetogenic downstream metabolites, such as kynurenic acid.	Kynurenine	192-202	insulin	Homo sapiens	74-81
28478038-7	2017	CONCLUSION: The data indicates that kynurenine pathway metabolites are increased in subjects with insulin resistance prior to overt manifestation of hyperglycemia.	Kynurenine	36-46	insulin	Homo sapiens	98-105
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.	Kynurenine	145-155	indoleamine 2,3-dioxygenase 1	Homo sapiens	75-80
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.	Kynurenine	104-116	tryptophan 2,3-dioxygenase	Rattus norvegicus	0-26
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.	Kynurenine	104-116	tryptophan 2,3-dioxygenase	Rattus norvegicus	28-31
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.	Kynurenine	104-116	indoleamine 2,3-dioxygenase 1	Rattus norvegicus	37-64
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.	Kynurenine	63-73	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-4
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.	Kynurenine	167-177	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-4
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.	Kynurenine	63-73	eukaryotic translation initiation factor 2 alpha kinase 4	Homo sapiens	123-127
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.	Kynurenine	63-73	mechanistic target of rapamycin kinase	Homo sapiens	137-141
28434116-1	2017	BACKGROUND/INTRODUCTION: Indoleamine 2,3-dioxygenase (IDO) metabolizes tryptophan to kynurenine.	Kynurenine	85-95	indoleamine 2,3-dioxygenase 1	Homo sapiens	25-52
28319697-2	2017	Kynurenine 3-monooxygenase (KMO) is a rate-limiting enzyme of the KP, where it catalyzes the conversion of kynurenine (KYN) to 3-hydroxykynurenine (3-HK).	Kynurenine	107-117	kynurenine 3-monooxygenase	Homo sapiens	0-26
28319697-2	2017	Kynurenine 3-monooxygenase (KMO) is a rate-limiting enzyme of the KP, where it catalyzes the conversion of kynurenine (KYN) to 3-hydroxykynurenine (3-HK).	Kynurenine	107-117	kynurenine 3-monooxygenase	Homo sapiens	28-31
28319697-2	2017	Kynurenine 3-monooxygenase (KMO) is a rate-limiting enzyme of the KP, where it catalyzes the conversion of kynurenine (KYN) to 3-hydroxykynurenine (3-HK).	Kynurenine	119-122	kynurenine 3-monooxygenase	Homo sapiens	0-26
28319697-2	2017	Kynurenine 3-monooxygenase (KMO) is a rate-limiting enzyme of the KP, where it catalyzes the conversion of kynurenine (KYN) to 3-hydroxykynurenine (3-HK).	Kynurenine	119-122	kynurenine 3-monooxygenase	Homo sapiens	28-31
28463241-8	2017	Our results are consistent with reports of elevations in proinflammatory cytokines in psychosis, and preclinical work showing that inflammation upregulates the enzyme, kynurenine mono-oxygenase (KMO), which converts kynurenine into 3-hydroxykynurenine and quinolinic acid.	Kynurenine	168-178	kynurenine 3-monooxygenase	Homo sapiens	195-198
27783115-2	2017	Here, we show that AhR ligands 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD), the tryptophan derivatives 6-formylindolo[3,2-b] carbazole (FICZ), kynurenine (kyn), and the natural dietary compound indole-3-carbinol (I3C) differentially modify cytokine expression in human monocyte-derived DCs (MoDCs).	Kynurenine	142-152	aryl hydrocarbon receptor	Homo sapiens	19-22
27783115-2	2017	Here, we show that AhR ligands 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD), the tryptophan derivatives 6-formylindolo[3,2-b] carbazole (FICZ), kynurenine (kyn), and the natural dietary compound indole-3-carbinol (I3C) differentially modify cytokine expression in human monocyte-derived DCs (MoDCs).	Kynurenine	142-145	aryl hydrocarbon receptor	Homo sapiens	19-22
27730347-14	2017	This could be attributed to its ability to reduce IDO-1 leading to shift the balance of the Kynurenine/ serotonin toward the serotonin pathway.	Kynurenine	92-102	indoleamine 2,3-dioxygenase 1	Rattus norvegicus	50-55
28320838-4	2017	An important function of DC involves activation of the kynurenine pathway via indoleamine 2,3-dioxygenase (IDO).	Kynurenine	55-65	chemokine (C-C motif) ligand 22	Mus musculus	25-27
28476779-3	2017	Indoleamine 2,3-dioxygenase (IDO) and tryptophan 2,3-dioxygenase (TDO) are produced, accelerating metabolism along the kynurenine pathway and resulting in excess levels of quinolinic acid, 3-hydroxyanthranilic acid and other neurotoxic molecules.	Kynurenine	119-129	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-27
28476779-3	2017	Indoleamine 2,3-dioxygenase (IDO) and tryptophan 2,3-dioxygenase (TDO) are produced, accelerating metabolism along the kynurenine pathway and resulting in excess levels of quinolinic acid, 3-hydroxyanthranilic acid and other neurotoxic molecules.	Kynurenine	119-129	indoleamine 2,3-dioxygenase 1	Homo sapiens	29-32
28476779-3	2017	Indoleamine 2,3-dioxygenase (IDO) and tryptophan 2,3-dioxygenase (TDO) are produced, accelerating metabolism along the kynurenine pathway and resulting in excess levels of quinolinic acid, 3-hydroxyanthranilic acid and other neurotoxic molecules.	Kynurenine	119-129	tryptophan 2,3-dioxygenase	Homo sapiens	38-64
28476779-3	2017	Indoleamine 2,3-dioxygenase (IDO) and tryptophan 2,3-dioxygenase (TDO) are produced, accelerating metabolism along the kynurenine pathway and resulting in excess levels of quinolinic acid, 3-hydroxyanthranilic acid and other neurotoxic molecules.	Kynurenine	119-129	tryptophan 2,3-dioxygenase	Homo sapiens	66-69
28476779-7	2017	This implies that to obtain optimal results in the treatment of GBM, one may need to add an inhibitor of the kynurenine pathway to therapy with a CTLA4 or PD1 inhibitor, or use agents which can suppress multiple checkpoint molecules.	Kynurenine	109-119	cytotoxic T-lymphocyte associated protein 4	Homo sapiens	146-151
28434116-1	2017	BACKGROUND/INTRODUCTION: Indoleamine 2,3-dioxygenase (IDO) metabolizes tryptophan to kynurenine.	Kynurenine	85-95	indoleamine 2,3-dioxygenase 1	Homo sapiens	54-57
28155213-7	2017	Our study not only extends the evidence that IDO has a critical role in mediating inflammation-induced depression but also supports the notion that neuroinflammation and the kynurenine pathway are important targets of novel therapeutic drugs for depression.	Kynurenine	174-184	indoleamine 2,3-dioxygenase 1	Mus musculus	45-48
28507519-6	2017	LPS-induced hypotension in mice was prevented by pre-treatment with the kynurenine monooxygenase (KMO) inhibitor, Ro-618048, which lowered serum levels of XA but enhanced serum levels of L-kynurenine.	Kynurenine	187-199	kynurenine 3-monooxygenase (kynurenine 3-hydroxylase)	Mus musculus	98-101
28179106-3	2017	The enzymatic activity of IDO1 is associated with the conversion of tryptophan into downstream kynurenine (Kyn), which has previously been hypothesized to contribute toward the suppression of tumor immunity.	Kynurenine	95-105	indoleamine 2,3-dioxygenase 1	Mus musculus	26-30
28179106-3	2017	The enzymatic activity of IDO1 is associated with the conversion of tryptophan into downstream kynurenine (Kyn), which has previously been hypothesized to contribute toward the suppression of tumor immunity.	Kynurenine	107-110	indoleamine 2,3-dioxygenase 1	Mus musculus	26-30
28357780-1	2017	Tryptophan-2,3-dioxygenase (TDO) is a homotetrameric heme-containing protein catalyzing the initial step in the kynurenine pathway, which oxidates the 2,3-double bond of the indole ring in L-tryptophan and catalyzes it into kynurenine (KYN).	Kynurenine	112-122	tryptophan 2,3-dioxygenase	Homo sapiens	0-26
28357780-1	2017	Tryptophan-2,3-dioxygenase (TDO) is a homotetrameric heme-containing protein catalyzing the initial step in the kynurenine pathway, which oxidates the 2,3-double bond of the indole ring in L-tryptophan and catalyzes it into kynurenine (KYN).	Kynurenine	112-122	tryptophan 2,3-dioxygenase	Homo sapiens	28-31
28357780-1	2017	Tryptophan-2,3-dioxygenase (TDO) is a homotetrameric heme-containing protein catalyzing the initial step in the kynurenine pathway, which oxidates the 2,3-double bond of the indole ring in L-tryptophan and catalyzes it into kynurenine (KYN).	Kynurenine	224-234	tryptophan 2,3-dioxygenase	Homo sapiens	0-26
28357780-1	2017	Tryptophan-2,3-dioxygenase (TDO) is a homotetrameric heme-containing protein catalyzing the initial step in the kynurenine pathway, which oxidates the 2,3-double bond of the indole ring in L-tryptophan and catalyzes it into kynurenine (KYN).	Kynurenine	224-234	tryptophan 2,3-dioxygenase	Homo sapiens	28-31
28357780-1	2017	Tryptophan-2,3-dioxygenase (TDO) is a homotetrameric heme-containing protein catalyzing the initial step in the kynurenine pathway, which oxidates the 2,3-double bond of the indole ring in L-tryptophan and catalyzes it into kynurenine (KYN).	Kynurenine	236-239	tryptophan 2,3-dioxygenase	Homo sapiens	0-26
28357780-1	2017	Tryptophan-2,3-dioxygenase (TDO) is a homotetrameric heme-containing protein catalyzing the initial step in the kynurenine pathway, which oxidates the 2,3-double bond of the indole ring in L-tryptophan and catalyzes it into kynurenine (KYN).	Kynurenine	236-239	tryptophan 2,3-dioxygenase	Homo sapiens	28-31
28357780-2	2017	The upregulation of TDO results in a decrease in tryptophan and the accumulation of KYN and its metabolites.	Kynurenine	84-87	tryptophan 2,3-dioxygenase	Homo sapiens	20-23
28223212-9	2017	We also demonstrated that n-BP functions by regulating the early part of the kynurenine pathway through the downregulation of tryptophan 2, 3-dioxygenase (TDO2), which decreases the downstream neurotoxic product, quinolinic acid (QA).	Kynurenine	77-87	tryptophan 2,3-dioxygenase	Homo sapiens	126-153
28223212-9	2017	We also demonstrated that n-BP functions by regulating the early part of the kynurenine pathway through the downregulation of tryptophan 2, 3-dioxygenase (TDO2), which decreases the downstream neurotoxic product, quinolinic acid (QA).	Kynurenine	77-87	tryptophan 2,3-dioxygenase	Homo sapiens	155-159
28445957-2	2017	Because IDO metabolizes tryptophan into kynurenine, the plasma kynurenine/tryptophan (Kyn/Trp) ratio has been widely used as a marker of systemic IDO.	Kynurenine	40-50	indoleamine 2,3-dioxygenase 1	Homo sapiens	8-11
28375145-2	2017	3HAO is a non-heme iron-containing, ring-cleaving extradiol dioxygenase that catalyzes the addition of both atoms of O2 to the kynurenine pathway metabolite 3-hydroxyanthranilic acid (3-HANA) to form quinolinic acid (QUIN).	Kynurenine	127-137	3-hydroxyanthranilate 3,4-dioxygenase	Homo sapiens	0-4
28375145-1	2017	3-Hydroxyanthranilate 3,4-dioxygenase (3HAO) is an enzyme in the microglial branch of the kynurenine pathway of tryptophan degradation.	Kynurenine	90-100	3-hydroxyanthranilate 3,4-dioxygenase	Homo sapiens	0-37
28375145-1	2017	3-Hydroxyanthranilate 3,4-dioxygenase (3HAO) is an enzyme in the microglial branch of the kynurenine pathway of tryptophan degradation.	Kynurenine	90-100	3-hydroxyanthranilate 3,4-dioxygenase	Homo sapiens	39-43
28445957-2	2017	Because IDO metabolizes tryptophan into kynurenine, the plasma kynurenine/tryptophan (Kyn/Trp) ratio has been widely used as a marker of systemic IDO.	Kynurenine	63-73	indoleamine 2,3-dioxygenase 1	Homo sapiens	8-11
28445957-2	2017	Because IDO metabolizes tryptophan into kynurenine, the plasma kynurenine/tryptophan (Kyn/Trp) ratio has been widely used as a marker of systemic IDO.	Kynurenine	63-73	indoleamine 2,3-dioxygenase 1	Homo sapiens	146-149
28445957-2	2017	Because IDO metabolizes tryptophan into kynurenine, the plasma kynurenine/tryptophan (Kyn/Trp) ratio has been widely used as a marker of systemic IDO.	Kynurenine	86-89	indoleamine 2,3-dioxygenase 1	Homo sapiens	8-11
28445957-2	2017	Because IDO metabolizes tryptophan into kynurenine, the plasma kynurenine/tryptophan (Kyn/Trp) ratio has been widely used as a marker of systemic IDO.	Kynurenine	86-89	indoleamine 2,3-dioxygenase 1	Homo sapiens	146-149
28454699-4	2017	IDO and TDO mRNA and protein expression, responsible for kynurenine production from tryptophan, were significantly lower in placentas from FGR pregnancies compared with control.	Kynurenine	57-67	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-3
28165296-12	2017	In contrast, tryptophan 2,3-dioxygenase activity and plasma kynurenine metabolites positively correlated with blood pressure values as well as with Ang II levels in these animals.	Kynurenine	60-70	angiotensinogen	Rattus norvegicus	148-154
28165296-13	2017	Moreover, kynurenine was independently connected with MBP.	Kynurenine	10-20	myelin basic protein	Rattus norvegicus	54-57
28165296-15	2017	Tryptophan 2,3-dioxygenase and part of the kynurenine metabolites in plasma and tissues positively correlated with blood pressure values and Ang II levels.	Kynurenine	43-53	angiotensinogen	Rattus norvegicus	141-147
28285566-7	2017	Furthermore, kynurenine (KYN), an endogenous AhR agonist and a tryptophan metabolite catalyzed by indoleamine 2,3-dioxygenase (IDO), was increased in the serums of mice that aspirated ZnONPs.	Kynurenine	13-23	aryl-hydrocarbon receptor	Mus musculus	45-48
28285566-7	2017	Furthermore, kynurenine (KYN), an endogenous AhR agonist and a tryptophan metabolite catalyzed by indoleamine 2,3-dioxygenase (IDO), was increased in the serums of mice that aspirated ZnONPs.	Kynurenine	25-28	aryl-hydrocarbon receptor	Mus musculus	45-48
28454699-4	2017	IDO and TDO mRNA and protein expression, responsible for kynurenine production from tryptophan, were significantly lower in placentas from FGR pregnancies compared with control.	Kynurenine	57-67	tryptophan 2,3-dioxygenase	Homo sapiens	8-11
28454699-5	2017	Explants prepared from 1st and 3rd trimester placentas actively produced all the major kynurenine pathway metabolites which, together with expression of IDO, TDO, KYN-OHase and 3HAO mRNAs, were significantly lower after 24 h exposure to 5-8% O2 compared to 20% O2 CONCLUSIONS: Expression and activity of the kynurenine pathway is present in the placenta from early gestation, and is down-regulated by hypoxia and in FGR pregnancies.	Kynurenine	87-97	indoleamine 2,3-dioxygenase 1	Homo sapiens	153-156
28454699-5	2017	Explants prepared from 1st and 3rd trimester placentas actively produced all the major kynurenine pathway metabolites which, together with expression of IDO, TDO, KYN-OHase and 3HAO mRNAs, were significantly lower after 24 h exposure to 5-8% O2 compared to 20% O2 CONCLUSIONS: Expression and activity of the kynurenine pathway is present in the placenta from early gestation, and is down-regulated by hypoxia and in FGR pregnancies.	Kynurenine	87-97	tryptophan 2,3-dioxygenase	Homo sapiens	158-161
28303855-1	2017	BACKGROUND: Indoleamine 2,3-dioxygenase (IDO), an enzyme for tryptophan metabolism through the kynurenine pathway, exhibits an immunosuppressive effect and induces immune tolerance in tumor cells.	Kynurenine	95-105	indoleamine 2,3-dioxygenase 1	Homo sapiens	12-39
28303855-1	2017	BACKGROUND: Indoleamine 2,3-dioxygenase (IDO), an enzyme for tryptophan metabolism through the kynurenine pathway, exhibits an immunosuppressive effect and induces immune tolerance in tumor cells.	Kynurenine	95-105	indoleamine 2,3-dioxygenase 1	Homo sapiens	41-44
28113063-2	2017	An intriguing member of this family is indoleamine 2,3-dioxygenase (IDO), which catalyzes the first and rate-limiting step of the main branch of tryptophan (Trp) degradation, the kynurenine pathway.	Kynurenine	179-189	indoleamine 2,3-dioxygenase 1	Homo sapiens	39-66
28325761-6	2017	Furthermore, treatment of oral epithelial cells with interferon gamma inhibits fungal endocytosis by inducing the synthesis of kynurenines, which cause prolonged activation of AhR and SFKs, thereby interfering with C. albicans-induced EGFR signaling.	Kynurenine	127-138	aryl-hydrocarbon receptor	Mus musculus	176-179
28325761-6	2017	Furthermore, treatment of oral epithelial cells with interferon gamma inhibits fungal endocytosis by inducing the synthesis of kynurenines, which cause prolonged activation of AhR and SFKs, thereby interfering with C. albicans-induced EGFR signaling.	Kynurenine	127-138	epidermal growth factor receptor	Mus musculus	235-239
28266612-6	2017	Mechanistically, we identified that Lactobacillus-derived reactive oxygen species may suppress host kynurenine metabolism, by inhibiting the expression of the metabolizing enzyme, IDO1, in the intestine.	Kynurenine	100-110	indoleamine 2,3-dioxygenase 1	Mus musculus	180-184
27258822-7	2017	RESULTS: Analysis of the kynurenine-to-tryptophan ratio in serum samples indicated higher IDO activity in patients with psoriasis than in healthy controls.	Kynurenine	25-35	indoleamine 2,3-dioxygenase 1	Homo sapiens	90-93
28013248-9	2017	The association between tryptophan oxidation and CNS inflammatory responses as measured by CSF interleukin 6 (IL-6) concentration supports a role of kynurenine metabolites in the inflammatory pathogenesis of late-stage HAT.	Kynurenine	149-159	interleukin 6	Homo sapiens	110-114
28469469-7	2017	The KYN/TRP ratio was utilized as a surrogate marker for indoleamine 2,3-dioxygenase 1 (IDO1) enzyme activity.	Kynurenine	4-7	indoleamine 2,3-dioxygenase 1	Homo sapiens	57-86
28113063-2	2017	An intriguing member of this family is indoleamine 2,3-dioxygenase (IDO), which catalyzes the first and rate-limiting step of the main branch of tryptophan (Trp) degradation, the kynurenine pathway.	Kynurenine	179-189	indoleamine 2,3-dioxygenase 1	Homo sapiens	68-71
28113063-5	2017	We also show that the apparent antiviral effect of IDO on PIV3 is not due to the generation of the kynurenine pathway metabolites, but rather due to the depletion of intracellular Trp by IDO, as a result of which this rare amino acid becomes unavailable for the alternative, proviral 5-HTP pathway.	Kynurenine	99-109	indoleamine 2,3-dioxygenase 1	Homo sapiens	51-54
28469467-3	2017	Similarly, the aryl hydrocarbon receptor is activated by both kynurenic acid and kynurenine, leading to CYP1A2 and melatonin metabolism, whereas melatonin may act to inhibit the aryl hydrocarbon receptor.	Kynurenine	81-91	aryl hydrocarbon receptor	Homo sapiens	15-40
28469467-3	2017	Similarly, the aryl hydrocarbon receptor is activated by both kynurenic acid and kynurenine, leading to CYP1A2 and melatonin metabolism, whereas melatonin may act to inhibit the aryl hydrocarbon receptor.	Kynurenine	81-91	cytochrome P450 family 1 subfamily A member 2	Homo sapiens	104-110
28469467-3	2017	Similarly, the aryl hydrocarbon receptor is activated by both kynurenic acid and kynurenine, leading to CYP1A2 and melatonin metabolism, whereas melatonin may act to inhibit the aryl hydrocarbon receptor.	Kynurenine	81-91	aryl hydrocarbon receptor	Homo sapiens	178-203
27693848-3	2017	Kynurenine 3-monooxygenase (KMO), a pivotal enzyme in the KP, has been suggested to play major roles in physiological and pathological events mediated by bioactive kynurenine metabolites.	Kynurenine	164-174	kynurenine 3-monooxygenase (kynurenine 3-hydroxylase)	Mus musculus	28-31
28003141-2	2017	Optimization of a micromolar hit through iterative cycles of synthesis and screening in an assay measuring IDO-mediated intracellular conversion of tryptophan to kynurenine led to potent inhibitors with favorable selectivity and metabolic stability profiles.	Kynurenine	162-172	indoleamine 2,3-dioxygenase 1	Homo sapiens	107-110
27693848-3	2017	Kynurenine 3-monooxygenase (KMO), a pivotal enzyme in the KP, has been suggested to play major roles in physiological and pathological events mediated by bioactive kynurenine metabolites.	Kynurenine	164-174	kynurenine 3-monooxygenase (kynurenine 3-hydroxylase)	Mus musculus	0-26
27994058-1	2017	Indoleamine 2,3-dioxygenase 1 (IDO1) is a single chain oxidoreductase that catalyzes tryptophan degradation to kynurenine.	Kynurenine	111-121	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.	Kynurenine	111-121	indoleamine 2,3-dioxygenase 1	Rattus norvegicus	31-35
28131097-1	2017	INTRODUCTION: Previous studies have shown that indoleamine 2, 3-dioxygenase (IDO), an immunosuppressive enzyme that converts tryptophan to kynurenine, is expressed in the placenta and might play a role in the maintenance of pregnancy, although its associations with the pathogeneses of preeclampsia (PE) and fetal growth restriction (FGR) remain unclear.	Kynurenine	139-149	indoleamine 2,3-dioxygenase 1	Homo sapiens	47-75
28131097-1	2017	INTRODUCTION: Previous studies have shown that indoleamine 2, 3-dioxygenase (IDO), an immunosuppressive enzyme that converts tryptophan to kynurenine, is expressed in the placenta and might play a role in the maintenance of pregnancy, although its associations with the pathogeneses of preeclampsia (PE) and fetal growth restriction (FGR) remain unclear.	Kynurenine	139-149	indoleamine 2,3-dioxygenase 1	Homo sapiens	77-80
28176942-5	2017	IDO is a heme-containing immunosuppressive enzyme, which is responsible for the degradation of tryptophan while increasing the concentration of kynurenine metabolites.	Kynurenine	144-154	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-3
27693848-11	2017	These findings suggested that KMO KO mice show antidepressants-responsive depressive-like behaviors and monoaminergic dysfunctions via abnormality of kynurenine metabolism with good validities as MDD model.	Kynurenine	150-160	kynurenine 3-monooxygenase (kynurenine 3-hydroxylase)	Mus musculus	30-33
28748226-2	2017	Deficiency of kynurenine-3-monooxygenase (KMO), enzyme catalyzing formation of 3-hydroxykynurenine (3-HK) from kynurenine (Kyn), a tryptophan (Trp) metabolite, might contribute to development of MetS as suggested by non-expression of KMO genes in human fat tissue and elevated serum concentrations of Kyn and its metabolites, kynurenic (KYNA) and anthranilic (ANA) acids, in diabetic patients and Zucker fatty rats (ZFR).	Kynurenine	301-304	kynurenine 3-monooxygenase	Homo sapiens	14-40
29275469-3	2017	This is driven by the key and rate-limiting enzymes indoleamine-2,3-dioxygenase 1 (IDO1) and tryptophan-2,3-dioxygenase 2 (TDO), resulting in local depletion of tryptophan, while tryptophan catabolites accumulate, including kynurenine and its derivatives, depending on the presence of downstream enzymes in the kynurenine pathway.	Kynurenine	224-234	indoleamine 2,3-dioxygenase 1	Homo sapiens	52-81
29275469-3	2017	This is driven by the key and rate-limiting enzymes indoleamine-2,3-dioxygenase 1 (IDO1) and tryptophan-2,3-dioxygenase 2 (TDO), resulting in local depletion of tryptophan, while tryptophan catabolites accumulate, including kynurenine and its derivatives, depending on the presence of downstream enzymes in the kynurenine pathway.	Kynurenine	224-234	indoleamine 2,3-dioxygenase 1	Homo sapiens	83-87
29275469-3	2017	This is driven by the key and rate-limiting enzymes indoleamine-2,3-dioxygenase 1 (IDO1) and tryptophan-2,3-dioxygenase 2 (TDO), resulting in local depletion of tryptophan, while tryptophan catabolites accumulate, including kynurenine and its derivatives, depending on the presence of downstream enzymes in the kynurenine pathway.	Kynurenine	224-234	tryptophan 2,3-dioxygenase	Homo sapiens	93-121
29275469-3	2017	This is driven by the key and rate-limiting enzymes indoleamine-2,3-dioxygenase 1 (IDO1) and tryptophan-2,3-dioxygenase 2 (TDO), resulting in local depletion of tryptophan, while tryptophan catabolites accumulate, including kynurenine and its derivatives, depending on the presence of downstream enzymes in the kynurenine pathway.	Kynurenine	224-234	tryptophan 2,3-dioxygenase	Homo sapiens	123-126
29275469-3	2017	This is driven by the key and rate-limiting enzymes indoleamine-2,3-dioxygenase 1 (IDO1) and tryptophan-2,3-dioxygenase 2 (TDO), resulting in local depletion of tryptophan, while tryptophan catabolites accumulate, including kynurenine and its derivatives, depending on the presence of downstream enzymes in the kynurenine pathway.	Kynurenine	311-321	indoleamine 2,3-dioxygenase 1	Homo sapiens	52-81
29275469-3	2017	This is driven by the key and rate-limiting enzymes indoleamine-2,3-dioxygenase 1 (IDO1) and tryptophan-2,3-dioxygenase 2 (TDO), resulting in local depletion of tryptophan, while tryptophan catabolites accumulate, including kynurenine and its derivatives, depending on the presence of downstream enzymes in the kynurenine pathway.	Kynurenine	311-321	indoleamine 2,3-dioxygenase 1	Homo sapiens	83-87
29275469-3	2017	This is driven by the key and rate-limiting enzymes indoleamine-2,3-dioxygenase 1 (IDO1) and tryptophan-2,3-dioxygenase 2 (TDO), resulting in local depletion of tryptophan, while tryptophan catabolites accumulate, including kynurenine and its derivatives, depending on the presence of downstream enzymes in the kynurenine pathway.	Kynurenine	311-321	tryptophan 2,3-dioxygenase	Homo sapiens	93-121
29275469-3	2017	This is driven by the key and rate-limiting enzymes indoleamine-2,3-dioxygenase 1 (IDO1) and tryptophan-2,3-dioxygenase 2 (TDO), resulting in local depletion of tryptophan, while tryptophan catabolites accumulate, including kynurenine and its derivatives, depending on the presence of downstream enzymes in the kynurenine pathway.	Kynurenine	311-321	tryptophan 2,3-dioxygenase	Homo sapiens	123-126
27889626-2	2017	Previously, we have demonstrated that indoleamine 2,3-dioxygenase (IDO), an L-tryptophan - kynurenine pathway (KP) enzyme, affects acute viral myocarditis.	Kynurenine	91-101	indoleamine 2,3-dioxygenase 1	Mus musculus	38-65
27889626-2	2017	Previously, we have demonstrated that indoleamine 2,3-dioxygenase (IDO), an L-tryptophan - kynurenine pathway (KP) enzyme, affects acute viral myocarditis.	Kynurenine	91-101	indoleamine 2,3-dioxygenase 1	Mus musculus	67-70
27889626-4	2017	Kynurenine 3-monooxygenase (KMO) is one of the key regulatory enzymes, which metabolizes kynurenine to 3-hydroxykynurenine in the KP.	Kynurenine	89-99	kynurenine 3-monooxygenase (kynurenine 3-hydroxylase)	Mus musculus	0-26
27889626-4	2017	Kynurenine 3-monooxygenase (KMO) is one of the key regulatory enzymes, which metabolizes kynurenine to 3-hydroxykynurenine in the KP.	Kynurenine	89-99	kynurenine 3-monooxygenase (kynurenine 3-hydroxylase)	Mus musculus	28-31
28748226-2	2017	Deficiency of kynurenine-3-monooxygenase (KMO), enzyme catalyzing formation of 3-hydroxykynurenine (3-HK) from kynurenine (Kyn), a tryptophan (Trp) metabolite, might contribute to development of MetS as suggested by non-expression of KMO genes in human fat tissue and elevated serum concentrations of Kyn and its metabolites, kynurenic (KYNA) and anthranilic (ANA) acids, in diabetic patients and Zucker fatty rats (ZFR).	Kynurenine	14-24	kynurenine 3-monooxygenase	Homo sapiens	42-45
28748226-2	2017	Deficiency of kynurenine-3-monooxygenase (KMO), enzyme catalyzing formation of 3-hydroxykynurenine (3-HK) from kynurenine (Kyn), a tryptophan (Trp) metabolite, might contribute to development of MetS as suggested by non-expression of KMO genes in human fat tissue and elevated serum concentrations of Kyn and its metabolites, kynurenic (KYNA) and anthranilic (ANA) acids, in diabetic patients and Zucker fatty rats (ZFR).	Kynurenine	14-24	kynurenine 3-monooxygenase	Homo sapiens	234-237
28748226-2	2017	Deficiency of kynurenine-3-monooxygenase (KMO), enzyme catalyzing formation of 3-hydroxykynurenine (3-HK) from kynurenine (Kyn), a tryptophan (Trp) metabolite, might contribute to development of MetS as suggested by non-expression of KMO genes in human fat tissue and elevated serum concentrations of Kyn and its metabolites, kynurenic (KYNA) and anthranilic (ANA) acids, in diabetic patients and Zucker fatty rats (ZFR).	Kynurenine	123-126	kynurenine 3-monooxygenase	Homo sapiens	14-40
28748226-2	2017	Deficiency of kynurenine-3-monooxygenase (KMO), enzyme catalyzing formation of 3-hydroxykynurenine (3-HK) from kynurenine (Kyn), a tryptophan (Trp) metabolite, might contribute to development of MetS as suggested by non-expression of KMO genes in human fat tissue and elevated serum concentrations of Kyn and its metabolites, kynurenic (KYNA) and anthranilic (ANA) acids, in diabetic patients and Zucker fatty rats (ZFR).	Kynurenine	123-126	kynurenine 3-monooxygenase	Homo sapiens	42-45
28748226-2	2017	Deficiency of kynurenine-3-monooxygenase (KMO), enzyme catalyzing formation of 3-hydroxykynurenine (3-HK) from kynurenine (Kyn), a tryptophan (Trp) metabolite, might contribute to development of MetS as suggested by non-expression of KMO genes in human fat tissue and elevated serum concentrations of Kyn and its metabolites, kynurenic (KYNA) and anthranilic (ANA) acids, in diabetic patients and Zucker fatty rats (ZFR).	Kynurenine	123-126	kynurenine 3-monooxygenase	Homo sapiens	234-237
28344890-1	2017	Kynurenine formation by tryptophan-catabolic indoleamine-2,3-dioxygenase 1 (IDO1) plays a key role in tumor immune evasion and inhibition of IDO1 is efficacious in preclinical models of breast cancer.	Kynurenine	0-10	indoleamine 2,3-dioxygenase 1	Homo sapiens	45-74
28344890-1	2017	Kynurenine formation by tryptophan-catabolic indoleamine-2,3-dioxygenase 1 (IDO1) plays a key role in tumor immune evasion and inhibition of IDO1 is efficacious in preclinical models of breast cancer.	Kynurenine	0-10	indoleamine 2,3-dioxygenase 1	Homo sapiens	76-80
28344890-1	2017	Kynurenine formation by tryptophan-catabolic indoleamine-2,3-dioxygenase 1 (IDO1) plays a key role in tumor immune evasion and inhibition of IDO1 is efficacious in preclinical models of breast cancer.	Kynurenine	0-10	indoleamine 2,3-dioxygenase 1	Homo sapiens	141-145
28585214-6	2017	One of the two rate-limiting enzymes which can metabolize tryptophan to kynurenine is IDO-1.	Kynurenine	72-82	indoleamine 2,3-dioxygenase 1	Homo sapiens	86-91
27860276-5	2017	Here we showed that IAV infection induced expression of interferons (IFNs), which upregulated production of indoleamine-2,3-dioxygenase (IDO1), which catalysed the kynurenine biosynthesis.	Kynurenine	164-174	indoleamine 2,3-dioxygenase 1	Homo sapiens	137-141
27860276-6	2017	Furthermore, IAV attenuated the IDO1 expression and the production of kynurenine through its NS1 protein.	Kynurenine	70-80	influenza virus NS1A binding protein	Homo sapiens	93-96
28748226-2	2017	Deficiency of kynurenine-3-monooxygenase (KMO), enzyme catalyzing formation of 3-hydroxykynurenine (3-HK) from kynurenine (Kyn), a tryptophan (Trp) metabolite, might contribute to development of MetS as suggested by non-expression of KMO genes in human fat tissue and elevated serum concentrations of Kyn and its metabolites, kynurenic (KYNA) and anthranilic (ANA) acids, in diabetic patients and Zucker fatty rats (ZFR).	Kynurenine	301-304	kynurenine 3-monooxygenase	Homo sapiens	42-45
27696702-1	2017	The enzyme indoleamine 2,3-dioxygenase 1 (IDO1) catalyses the initial, rate-limiting step in tryptophan (Trp) degradation, resulting in tryptophan starvation and the production of immunoregulatory kynurenines.	Kynurenine	197-208	indoleamine 2,3-dioxygenase 1	Homo sapiens	11-40
27696702-1	2017	The enzyme indoleamine 2,3-dioxygenase 1 (IDO1) catalyses the initial, rate-limiting step in tryptophan (Trp) degradation, resulting in tryptophan starvation and the production of immunoregulatory kynurenines.	Kynurenine	197-208	indoleamine 2,3-dioxygenase 1	Homo sapiens	42-46
27876634-2	2017	A role has also been suggested for the Th1-type cytokine, IFN-gamma, with most mechanistic accounts focusing on the cytokine"s capacity to induce indoleamine 2,3-dioxygenase (IDO), leading to diminished tryptophan and the generation of kynurenine metabolites.	Kynurenine	236-246	indoleamine 2,3-dioxygenase 1	Mus musculus	146-173
27245499-6	2017	The kynurenine pathway is also critically regulated by cytokines, and, indeed, the pro-inflammatory cytokines interleukin (IL)-1beta and IL-6 are elevated in schizophrenia and bipolar disorder and stimulate the production of kynurenic acid.	Kynurenine	4-14	interleukin 1 beta	Homo sapiens	110-132
27245499-6	2017	The kynurenine pathway is also critically regulated by cytokines, and, indeed, the pro-inflammatory cytokines interleukin (IL)-1beta and IL-6 are elevated in schizophrenia and bipolar disorder and stimulate the production of kynurenic acid.	Kynurenine	4-14	interleukin 6	Homo sapiens	137-141
27245499-7	2017	One physiological mechanism controlling the activity of the kynurenine pathway originates from the protein sorting nexin 7 (SNX7).	Kynurenine	60-70	sorting nexin 7	Homo sapiens	107-122
27245499-7	2017	One physiological mechanism controlling the activity of the kynurenine pathway originates from the protein sorting nexin 7 (SNX7).	Kynurenine	60-70	sorting nexin 7	Homo sapiens	124-128
27245499-8	2017	This glial signaling pathway initiates a caspase-8-driven activation of IL-1beta that induces tryptophan-2,3-dioxygenase 2 (TDO2), an enzyme in the kynurenine pathway.	Kynurenine	148-158	caspase 8	Homo sapiens	41-50
27245499-8	2017	This glial signaling pathway initiates a caspase-8-driven activation of IL-1beta that induces tryptophan-2,3-dioxygenase 2 (TDO2), an enzyme in the kynurenine pathway.	Kynurenine	148-158	interleukin 1 beta	Homo sapiens	72-80
27245499-8	2017	This glial signaling pathway initiates a caspase-8-driven activation of IL-1beta that induces tryptophan-2,3-dioxygenase 2 (TDO2), an enzyme in the kynurenine pathway.	Kynurenine	148-158	tryptophan 2,3-dioxygenase	Homo sapiens	94-122
27245499-8	2017	This glial signaling pathway initiates a caspase-8-driven activation of IL-1beta that induces tryptophan-2,3-dioxygenase 2 (TDO2), an enzyme in the kynurenine pathway.	Kynurenine	148-158	tryptophan 2,3-dioxygenase	Homo sapiens	124-128
29103054-3	2017	ACMSD is part of the kynurenine pathway, responsible for the catalytic breakdown of tryptophan into NAD+, generating several neuroactive metabolites in the process.	Kynurenine	21-31	aminocarboxymuconate semialdehyde decarboxylase	Homo sapiens	0-5
26617070-5	2017	Under normal conditions, TDO controls Trp flux in liver and availability in plasma and can supply kynurenine for the extrahepatic pathway.	Kynurenine	98-108	tryptophan 2,3-dioxygenase	Homo sapiens	25-28
26767951-4	2017	During an inflammatory response, the initial KP metabolic step is primarily regulated by indoleamine 2,3-dioxygenase 1 (IDO1), which produces KYN from TRP.	Kynurenine	142-145	indoleamine 2,3-dioxygenase 1	Homo sapiens	89-118
26767951-4	2017	During an inflammatory response, the initial KP metabolic step is primarily regulated by indoleamine 2,3-dioxygenase 1 (IDO1), which produces KYN from TRP.	Kynurenine	142-145	indoleamine 2,3-dioxygenase 1	Homo sapiens	120-124
27876634-2	2017	A role has also been suggested for the Th1-type cytokine, IFN-gamma, with most mechanistic accounts focusing on the cytokine"s capacity to induce indoleamine 2,3-dioxygenase (IDO), leading to diminished tryptophan and the generation of kynurenine metabolites.	Kynurenine	236-246	indoleamine 2,3-dioxygenase 1	Mus musculus	175-178
27838184-2	2016	The mHtt induced toxicity can be rescued by inhibiting the kynurenine monooxygenase (KMO) enzyme.	Kynurenine	59-69	kynurenine 3-monooxygenase	Homo sapiens	85-88
28216884-4	2017	All of the isolated compounds were examined for their ability to inhibit IDO, which actively suppresses immune functions by catalyzing the rate limiting reaction in the conversion of tryptophan to kynurenine.	Kynurenine	197-207	indoleamine 2,3-dioxygenase 1	Homo sapiens	73-76
27980422-0	2016	Progesterone Alters Kynurenine Pathway Activation in IFN-gamma-Activated Macrophages - Relevance for Neuroinflammatory Diseases.	Kynurenine	20-30	interferon gamma	Homo sapiens	53-62
27769672-1	2016	Indoleamine 2,3-dioxygenase 1 (IDO1)-mediated kynurenine pathway of tryptophan degradation is identified as an important immune effector pathway in the tumor cells to escape a potentially effective immune response.	Kynurenine	46-56	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-29
27769672-1	2016	Indoleamine 2,3-dioxygenase 1 (IDO1)-mediated kynurenine pathway of tryptophan degradation is identified as an important immune effector pathway in the tumor cells to escape a potentially effective immune response.	Kynurenine	46-56	indoleamine 2,3-dioxygenase 1	Homo sapiens	31-35
28066416-6	2016	Kynurenine (KYN), 3-hydroxykynurenine, quinolinic acid, and the KP enzymes all displayed highly divergent patterns in the sites examined, though IDO1 expression always correlated with local KYN/TRP ratios.	Kynurenine	190-193	indoleamine 2,3-dioxygenase 1	Homo sapiens	145-149
28164545-6	2016	RESULTS: In the AICD cohort, zonulin associated inversely with serum creatinine (p = 0.013), carboxymethyl-lysine calprotectin (p &lt; 0.001), and kynurenine (p = 0.009) and positively with homoarginine (p &lt; 0.001).	Kynurenine	147-157	haptoglobin	Homo sapiens	29-36
28164545-9	2016	CONCLUSIONS: The inverse associations of zonulin with creatinine and markers of cardio-vascular risk (high CMLcalprotectin and kynurenine, low homoarginine) are novel findings that need further experimental and clinical clarification.	Kynurenine	127-137	haptoglobin	Homo sapiens	41-48
27573671-4	2016	We postulated that: 1) malignant cells produce tryptophan-derived AHR ligand(s) through the kynurenine pathway; 2) these metabolites have the potential to drive AHR-dependent breast cancer migration; 3) the AHR controls expression of a rate-limiting kynurenine pathway enzyme(s) in a closed amplification loop; and 4) environmental AHR ligands mimic the effects of endogenous ligands.	Kynurenine	250-260	aryl hydrocarbon receptor	Homo sapiens	161-164
26992058-0	2016	Kynurenine Modulates MMP-1 and Type-I Collagen Expression Via Aryl Hydrocarbon Receptor Activation in Dermal Fibroblasts.	Kynurenine	0-10	matrix metallopeptidase 1	Rattus norvegicus	21-26
26992058-0	2016	Kynurenine Modulates MMP-1 and Type-I Collagen Expression Via Aryl Hydrocarbon Receptor Activation in Dermal Fibroblasts.	Kynurenine	0-10	aryl hydrocarbon receptor	Rattus norvegicus	62-87
27667153-1	2016	Indoleamine 2,3-dioxygenase (IDO) is expressed in antigen-presenting cells and by degrading L-tryptophan along the kynurenine pathway suppresses CD4+ T-cell proliferation, induces apoptosis and promotes differentiation towards a regulatory as opposed to an effector phenotype.	Kynurenine	115-125	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-27
27667153-1	2016	Indoleamine 2,3-dioxygenase (IDO) is expressed in antigen-presenting cells and by degrading L-tryptophan along the kynurenine pathway suppresses CD4+ T-cell proliferation, induces apoptosis and promotes differentiation towards a regulatory as opposed to an effector phenotype.	Kynurenine	115-125	indoleamine 2,3-dioxygenase 1	Homo sapiens	29-32
27627133-14	2016	No association was found between tryptophan metabolism and specific dimensions of fatigue, but kynurenine and the kynurenine/tryptophan ratio correlated with insulin and HOMA-IR.	Kynurenine	95-105	insulin	Homo sapiens	158-165
27627133-14	2016	No association was found between tryptophan metabolism and specific dimensions of fatigue, but kynurenine and the kynurenine/tryptophan ratio correlated with insulin and HOMA-IR.	Kynurenine	114-124	insulin	Homo sapiens	158-165
27392942-0	2016	Tryptophan 2,3-dioxygenase and indoleamine 2,3-dioxygenase 1 make separate, tissue-specific contributions to basal and inflammation-induced kynurenine pathway metabolism in mice.	Kynurenine	140-150	tryptophan 2,3-dioxygenase	Mus musculus	0-26
27392942-0	2016	Tryptophan 2,3-dioxygenase and indoleamine 2,3-dioxygenase 1 make separate, tissue-specific contributions to basal and inflammation-induced kynurenine pathway metabolism in mice.	Kynurenine	140-150	indoleamine 2,3-dioxygenase 1	Mus musculus	31-60
27221136-1	2016	BACKGROUND: Neopterin levels and kynurenine/tryptophan ratios (KTRs) increase with IFN-gamma stimulation, indicating TH1 immunity, and thus might be inversely associated with asthma.	Kynurenine	33-43	interferon gamma	Homo sapiens	83-92
27573671-4	2016	We postulated that: 1) malignant cells produce tryptophan-derived AHR ligand(s) through the kynurenine pathway; 2) these metabolites have the potential to drive AHR-dependent breast cancer migration; 3) the AHR controls expression of a rate-limiting kynurenine pathway enzyme(s) in a closed amplification loop; and 4) environmental AHR ligands mimic the effects of endogenous ligands.	Kynurenine	92-102	aryl hydrocarbon receptor	Homo sapiens	66-69
27573671-4	2016	We postulated that: 1) malignant cells produce tryptophan-derived AHR ligand(s) through the kynurenine pathway; 2) these metabolites have the potential to drive AHR-dependent breast cancer migration; 3) the AHR controls expression of a rate-limiting kynurenine pathway enzyme(s) in a closed amplification loop; and 4) environmental AHR ligands mimic the effects of endogenous ligands.	Kynurenine	92-102	aryl hydrocarbon receptor	Homo sapiens	161-164
27573671-4	2016	We postulated that: 1) malignant cells produce tryptophan-derived AHR ligand(s) through the kynurenine pathway; 2) these metabolites have the potential to drive AHR-dependent breast cancer migration; 3) the AHR controls expression of a rate-limiting kynurenine pathway enzyme(s) in a closed amplification loop; and 4) environmental AHR ligands mimic the effects of endogenous ligands.	Kynurenine	92-102	aryl hydrocarbon receptor	Homo sapiens	161-164
27573671-4	2016	We postulated that: 1) malignant cells produce tryptophan-derived AHR ligand(s) through the kynurenine pathway; 2) these metabolites have the potential to drive AHR-dependent breast cancer migration; 3) the AHR controls expression of a rate-limiting kynurenine pathway enzyme(s) in a closed amplification loop; and 4) environmental AHR ligands mimic the effects of endogenous ligands.	Kynurenine	92-102	aryl hydrocarbon receptor	Homo sapiens	161-164
27573671-4	2016	We postulated that: 1) malignant cells produce tryptophan-derived AHR ligand(s) through the kynurenine pathway; 2) these metabolites have the potential to drive AHR-dependent breast cancer migration; 3) the AHR controls expression of a rate-limiting kynurenine pathway enzyme(s) in a closed amplification loop; and 4) environmental AHR ligands mimic the effects of endogenous ligands.	Kynurenine	250-260	aryl hydrocarbon receptor	Homo sapiens	66-69
27573671-4	2016	We postulated that: 1) malignant cells produce tryptophan-derived AHR ligand(s) through the kynurenine pathway; 2) these metabolites have the potential to drive AHR-dependent breast cancer migration; 3) the AHR controls expression of a rate-limiting kynurenine pathway enzyme(s) in a closed amplification loop; and 4) environmental AHR ligands mimic the effects of endogenous ligands.	Kynurenine	250-260	aryl hydrocarbon receptor	Homo sapiens	161-164
27573671-4	2016	We postulated that: 1) malignant cells produce tryptophan-derived AHR ligand(s) through the kynurenine pathway; 2) these metabolites have the potential to drive AHR-dependent breast cancer migration; 3) the AHR controls expression of a rate-limiting kynurenine pathway enzyme(s) in a closed amplification loop; and 4) environmental AHR ligands mimic the effects of endogenous ligands.	Kynurenine	250-260	aryl hydrocarbon receptor	Homo sapiens	161-164
27573671-5	2016	Data presented in this work indicate that primary human breast cancers, and their metastases, express high levels of AHR and tryptophan-2,3-dioxygenase (TDO); representative ER-/PR-/Her2- cell lines express TDO and produce sufficient intracellular kynurenine and xanthurenic acid concentrations to chronically activate the AHR.	Kynurenine	248-258	aryl hydrocarbon receptor	Homo sapiens	117-120
27573671-5	2016	Data presented in this work indicate that primary human breast cancers, and their metastases, express high levels of AHR and tryptophan-2,3-dioxygenase (TDO); representative ER-/PR-/Her2- cell lines express TDO and produce sufficient intracellular kynurenine and xanthurenic acid concentrations to chronically activate the AHR.	Kynurenine	248-258	tryptophan 2,3-dioxygenase	Homo sapiens	153-156
27573671-6	2016	TDO overexpression, or excess kynurenine or xanthurenic acid, accelerates migration in an AHR-dependent fashion.	Kynurenine	30-40	aryl hydrocarbon receptor	Homo sapiens	90-93
27623092-1	2016	To quantify the full range of tryptophan metabolites along the kynurenine pathway, a liquid chromatography - tandem mass spectrometry method was developed and used to analyse brain extracts of rodents treated with the kynurenine-3-mono-oxygenase (KMO) inhibitor Ro61-8048 during pregnancy.	Kynurenine	63-73	kynurenine 3-monooxygenase (kynurenine 3-hydroxylase)	Mus musculus	218-245
27510585-0	2016	Characterization of the Kynurenine Pathway in CD8+ Human Primary Monocyte-Derived Dendritic Cells.	Kynurenine	24-34	CD8a molecule	Homo sapiens	46-49
27623092-5	2016	The results confirm the marked increase in the accumulation of some neuroactive kynurenines when KMO is inhibited, and re-emphasise the potential importance of changes in anthranilic acid.	Kynurenine	80-91	kynurenine 3-monooxygenase (kynurenine 3-hydroxylase)	Mus musculus	97-100
27623092-0	2016	Kynurenine pathway metabolism following prenatal KMO inhibition and in Mecp2+/- mice, using liquid chromatography-tandem mass spectrometry.	Kynurenine	0-10	kynurenine 3-monooxygenase (kynurenine 3-hydroxylase)	Mus musculus	49-52
27607184-6	2016	Stimulation of TLR-2, TLR-3, TLR-4, TLR-7/8 and TLR-9 was found to induce the production of kynurenine, but only stimulation of TLR-3 increased levels of further downstream metabolites, such as KYNA and QUIN.	Kynurenine	92-102	toll like receptor 2	Homo sapiens	15-20
27623092-0	2016	Kynurenine pathway metabolism following prenatal KMO inhibition and in Mecp2+/- mice, using liquid chromatography-tandem mass spectrometry.	Kynurenine	0-10	methyl CpG binding protein 2	Mus musculus	71-76
27607184-6	2016	Stimulation of TLR-2, TLR-3, TLR-4, TLR-7/8 and TLR-9 was found to induce the production of kynurenine, but only stimulation of TLR-3 increased levels of further downstream metabolites, such as KYNA and QUIN.	Kynurenine	92-102	toll like receptor 4	Homo sapiens	29-34
27607184-6	2016	Stimulation of TLR-2, TLR-3, TLR-4, TLR-7/8 and TLR-9 was found to induce the production of kynurenine, but only stimulation of TLR-3 increased levels of further downstream metabolites, such as KYNA and QUIN.	Kynurenine	92-102	toll like receptor 3	Homo sapiens	22-27
27607184-6	2016	Stimulation of TLR-2, TLR-3, TLR-4, TLR-7/8 and TLR-9 was found to induce the production of kynurenine, but only stimulation of TLR-3 increased levels of further downstream metabolites, such as KYNA and QUIN.	Kynurenine	92-102	toll like receptor 7	Homo sapiens	36-43
27754481-11	2016	Whereas kynurenine metabolism was generally increased in behaviorally salient brain regions, a distinct shift toward KMO-dependent kynurenine metabolism occurred in the dorsal hippocampus in response to LPS.	Kynurenine	131-141	kynurenine 3-monooxygenase (kynurenine 3-hydroxylase)	Mus musculus	117-120
27607184-6	2016	Stimulation of TLR-2, TLR-3, TLR-4, TLR-7/8 and TLR-9 was found to induce the production of kynurenine, but only stimulation of TLR-3 increased levels of further downstream metabolites, such as KYNA and QUIN.	Kynurenine	92-102	toll like receptor 9	Homo sapiens	48-53
27647832-8	2016	IFN-alpha treatment also increased the enzymatic IDO1 activity (Kyn/tryptophan ratio), which in turn activated production of TGF-beta.	Kynurenine	64-67	interferon alpha	Mus musculus	0-9
27799931-0	2016	Immunomodulatory Factors Galectin-9 and Interferon-Gamma Synergize to Induce Expression of Rate-Limiting Enzymes of the Kynurenine Pathway in the Mouse Hippocampus.	Kynurenine	120-130	lectin, galactose binding, soluble 9	Mus musculus	25-35
27799931-0	2016	Immunomodulatory Factors Galectin-9 and Interferon-Gamma Synergize to Induce Expression of Rate-Limiting Enzymes of the Kynurenine Pathway in the Mouse Hippocampus.	Kynurenine	120-130	interferon gamma	Mus musculus	40-56
27994758-2	2016	Indoleamine 2,3-dioxygenase 1 (IDO1) enzyme plays an important role in the metabolism of a local l-Trp through the kynurenine pathway in the immune systems.	Kynurenine	115-125	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-29
27994758-2	2016	Indoleamine 2,3-dioxygenase 1 (IDO1) enzyme plays an important role in the metabolism of a local l-Trp through the kynurenine pathway in the immune systems.	Kynurenine	115-125	indoleamine 2,3-dioxygenase 1	Homo sapiens	31-35
27647832-8	2016	IFN-alpha treatment also increased the enzymatic IDO1 activity (Kyn/tryptophan ratio), which in turn activated production of TGF-beta.	Kynurenine	64-67	indoleamine 2,3-dioxygenase 1	Mus musculus	49-53
27647832-8	2016	IFN-alpha treatment also increased the enzymatic IDO1 activity (Kyn/tryptophan ratio), which in turn activated production of TGF-beta.	Kynurenine	64-67	transforming growth factor, beta 1	Mus musculus	125-133
27867514-2	2016	The aryl hydrocarbon receptor (AhR) is a ubiquitously expressed transcription factor and its activation by environmental chemicals and by its endogenous ligand kynurenine (Kyn) has been implicated in a variety of tumour-promoting processes such as transformation, tumorigenesis and in immunosuppression that enables tumour survival and growth.	Kynurenine	160-170	aryl hydrocarbon receptor	Homo sapiens	4-29
27867514-2	2016	The aryl hydrocarbon receptor (AhR) is a ubiquitously expressed transcription factor and its activation by environmental chemicals and by its endogenous ligand kynurenine (Kyn) has been implicated in a variety of tumour-promoting processes such as transformation, tumorigenesis and in immunosuppression that enables tumour survival and growth.	Kynurenine	160-170	aryl hydrocarbon receptor	Homo sapiens	31-34
27867514-2	2016	The aryl hydrocarbon receptor (AhR) is a ubiquitously expressed transcription factor and its activation by environmental chemicals and by its endogenous ligand kynurenine (Kyn) has been implicated in a variety of tumour-promoting processes such as transformation, tumorigenesis and in immunosuppression that enables tumour survival and growth.	Kynurenine	172-175	aryl hydrocarbon receptor	Homo sapiens	4-29
27867514-2	2016	The aryl hydrocarbon receptor (AhR) is a ubiquitously expressed transcription factor and its activation by environmental chemicals and by its endogenous ligand kynurenine (Kyn) has been implicated in a variety of tumour-promoting processes such as transformation, tumorigenesis and in immunosuppression that enables tumour survival and growth.	Kynurenine	172-175	aryl hydrocarbon receptor	Homo sapiens	31-34
27867514-3	2016	Kyn is generated constitutively by human tumour cells via tryptophan (Trp)-2,3-dioxygenase (TDO), a Trp-degrading enzyme expressed in liver, brain and cancer cells.	Kynurenine	0-3	tryptophan 2,3-dioxygenase	Homo sapiens	92-95
27267006-2	2016	Indoleamine 2,3-dioxygenase 1 (IDO1) plays a key role in tryptophan catabolism in the immune system and it is also considered as an important therapeutic target for the treatment of cancer and other diseases that are linked with kynurenine pathway.	Kynurenine	229-239	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-29
27503512-10	2016	These results strongly suggest that the activity of IDO1 is implicated in the pathophysiology of environmental enteropathy, and demonstrates the utility of tryptophan and kynurenine as biomarkers for this syndrome, particularly in identifying those at risk for hyporesponsivity to oral vaccines.	Kynurenine	171-181	indoleamine 2,3-dioxygenase 1	Homo sapiens	52-56
27572319-4	2016	Here we show indolamine-2,3-dioxygenase-1 (IDO1) expression, a kynurenine pathway enzyme, is increased not only in tumor cells but also in the microenvironment of human RCC compared to normal kidney tissues.	Kynurenine	63-73	indoleamine 2,3-dioxygenase 1	Homo sapiens	13-41
27572319-4	2016	Here we show indolamine-2,3-dioxygenase-1 (IDO1) expression, a kynurenine pathway enzyme, is increased not only in tumor cells but also in the microenvironment of human RCC compared to normal kidney tissues.	Kynurenine	63-73	indoleamine 2,3-dioxygenase 1	Homo sapiens	43-47
27572319-6	2016	However, interferon-gamma (IFNgamma) induced high levels of IDO1 in both RCC and RENCA cells, concomitant with enhanced kynurenine levels in conditioned media.	Kynurenine	120-130	interferon gamma	Mus musculus	9-25
27572319-6	2016	However, interferon-gamma (IFNgamma) induced high levels of IDO1 in both RCC and RENCA cells, concomitant with enhanced kynurenine levels in conditioned media.	Kynurenine	120-130	interferon gamma	Mus musculus	27-35
27267006-2	2016	Indoleamine 2,3-dioxygenase 1 (IDO1) plays a key role in tryptophan catabolism in the immune system and it is also considered as an important therapeutic target for the treatment of cancer and other diseases that are linked with kynurenine pathway.	Kynurenine	229-239	indoleamine 2,3-dioxygenase 1	Homo sapiens	31-35
28955961-1	2016	BACKGROUND: Kynurenine aminotransferase 3 (KAT3) catalyzes the transamination of Kynurenine to kynurenic acid, and is identical to cysteine conjugate beta-lyase 2 (CCBL2) and glutamine transaminase L (GTL).	Kynurenine	12-22	kynurenine aminotransferase 3	Mus musculus	43-47
27760945-2	2016	IDO activitycan be measured using the tryptophan(Trp)/kynurenine(Kyn)ratio.	Kynurenine	54-64	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-3
27760945-2	2016	IDO activitycan be measured using the tryptophan(Trp)/kynurenine(Kyn)ratio.	Kynurenine	65-68	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-3
27552061-6	2016	IDO activity was determined by analyzing plasma levels of tryptophan and kynurenine.	Kynurenine	73-83	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-3
27690129-9	2016	Principle components pathway analyses also showed that L/M with %L, I-FABP and MPO associate with impaired growth, while also (like MPO) associating with a systemic inflammation cluster of kynurenine, LBP, sCD14, SAA and K/T.	Kynurenine	189-199	myeloperoxidase	Homo sapiens	132-135
26946084-5	2016	We tested the hypothesis that skeletal muscle PGC-1alpha1/KAT-kynurenine pathway is altered by exercise and type 2 diabetes.	Kynurenine	62-72	thiosulfate sulfurtransferase like domain containing 1	Homo sapiens	58-61
27632144-9	2016	IP-10 levels (P &lt; 0.05) and kynurenine/tryptophan ratio (P &lt; 0.01) were negatively associated with the CD4 count 2 years after inclusion.	Kynurenine	31-41	CD4 molecule	Homo sapiens	109-112
26666201-4	2016	A series of post-mortem brain tissue and in vitro experiments suggested SNX7 downregulation to result in a caspase-8-driven activation of interleukin-1beta and a subsequent induction of the brain kynurenine pathway.	Kynurenine	196-206	sorting nexin 7	Homo sapiens	72-76
26666201-4	2016	A series of post-mortem brain tissue and in vitro experiments suggested SNX7 downregulation to result in a caspase-8-driven activation of interleukin-1beta and a subsequent induction of the brain kynurenine pathway.	Kynurenine	196-206	caspase 8	Homo sapiens	107-116
28955961-1	2016	BACKGROUND: Kynurenine aminotransferase 3 (KAT3) catalyzes the transamination of Kynurenine to kynurenic acid, and is identical to cysteine conjugate beta-lyase 2 (CCBL2) and glutamine transaminase L (GTL).	Kynurenine	12-22	kynurenine aminotransferase 3	Mus musculus	131-162
28955961-1	2016	BACKGROUND: Kynurenine aminotransferase 3 (KAT3) catalyzes the transamination of Kynurenine to kynurenic acid, and is identical to cysteine conjugate beta-lyase 2 (CCBL2) and glutamine transaminase L (GTL).	Kynurenine	12-22	kynurenine aminotransferase 3	Mus musculus	164-169
27611938-3	2016	Indoleamine-2,3-dioxygenase (IDO) catalyzes the oxidation of tryptophan to kynurenine, the first step in this pathway.	Kynurenine	75-85	indoleamine 2,3-dioxygenase 1	Mus musculus	0-27
27611938-3	2016	Indoleamine-2,3-dioxygenase (IDO) catalyzes the oxidation of tryptophan to kynurenine, the first step in this pathway.	Kynurenine	75-85	indoleamine 2,3-dioxygenase 1	Mus musculus	29-32
27072370-2	2016	Two key KP enzymes that catabolize kynurenine include kynurenine-aminotransferase II (KATII), which yields antioxidative kynurenine acid [KYNA] in astrocytes, and kynurenine-3-monooxygenase (KMO), which produces neurotoxic metabolites in microglia.	Kynurenine	35-45	aminoadipate aminotransferase	Homo sapiens	54-84
27613847-1	2016	Indoleamine 2,3-dioxygenase (IDO) catalyzes the degradation of tryptophan, which plays a critical role in immune suppression through regulating the production of a series of metabolites that are generally referred to as kynurenines.	Kynurenine	220-231	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-27
27613847-1	2016	Indoleamine 2,3-dioxygenase (IDO) catalyzes the degradation of tryptophan, which plays a critical role in immune suppression through regulating the production of a series of metabolites that are generally referred to as kynurenines.	Kynurenine	220-231	indoleamine 2,3-dioxygenase 1	Homo sapiens	29-32
26910189-1	2016	The concentrations of l-tryptophan (Trp) and the metabolite l-kynurenine (KYN) can be used to evaluate the in-vivo activity of indoleamine 2,3-dioxygenase (IDO) and tryptophan 2,3-dioxygenase (TDO).	Kynurenine	60-72	indoleamine 2,3-dioxygenase 1	Homo sapiens	127-154
26910189-1	2016	The concentrations of l-tryptophan (Trp) and the metabolite l-kynurenine (KYN) can be used to evaluate the in-vivo activity of indoleamine 2,3-dioxygenase (IDO) and tryptophan 2,3-dioxygenase (TDO).	Kynurenine	60-72	indoleamine 2,3-dioxygenase 1	Homo sapiens	156-159
26910189-1	2016	The concentrations of l-tryptophan (Trp) and the metabolite l-kynurenine (KYN) can be used to evaluate the in-vivo activity of indoleamine 2,3-dioxygenase (IDO) and tryptophan 2,3-dioxygenase (TDO).	Kynurenine	60-72	tryptophan 2,3-dioxygenase	Homo sapiens	193-196
26910189-1	2016	The concentrations of l-tryptophan (Trp) and the metabolite l-kynurenine (KYN) can be used to evaluate the in-vivo activity of indoleamine 2,3-dioxygenase (IDO) and tryptophan 2,3-dioxygenase (TDO).	Kynurenine	74-77	indoleamine 2,3-dioxygenase 1	Homo sapiens	127-154
26910189-1	2016	The concentrations of l-tryptophan (Trp) and the metabolite l-kynurenine (KYN) can be used to evaluate the in-vivo activity of indoleamine 2,3-dioxygenase (IDO) and tryptophan 2,3-dioxygenase (TDO).	Kynurenine	74-77	indoleamine 2,3-dioxygenase 1	Homo sapiens	156-159
26910189-1	2016	The concentrations of l-tryptophan (Trp) and the metabolite l-kynurenine (KYN) can be used to evaluate the in-vivo activity of indoleamine 2,3-dioxygenase (IDO) and tryptophan 2,3-dioxygenase (TDO).	Kynurenine	74-77	tryptophan 2,3-dioxygenase	Homo sapiens	165-191
26910189-1	2016	The concentrations of l-tryptophan (Trp) and the metabolite l-kynurenine (KYN) can be used to evaluate the in-vivo activity of indoleamine 2,3-dioxygenase (IDO) and tryptophan 2,3-dioxygenase (TDO).	Kynurenine	74-77	tryptophan 2,3-dioxygenase	Homo sapiens	193-196
27489009-8	2016	We observed significant positive associations between serum interleukin-10 (IL-10) and serum kynurenine (P = 0.0002), the kynurenine-to-tryptophan ratio (KTR) (P = 0.003), 3-hydroxykynurenine (P = 0.01), and 3-hydroxyanthranilic acid (P = 0.04).	Kynurenine	93-103	interleukin 10	Homo sapiens	60-74
27489009-8	2016	We observed significant positive associations between serum interleukin-10 (IL-10) and serum kynurenine (P = 0.0002), the kynurenine-to-tryptophan ratio (KTR) (P = 0.003), 3-hydroxykynurenine (P = 0.01), and 3-hydroxyanthranilic acid (P = 0.04).	Kynurenine	93-103	interleukin 10	Homo sapiens	76-81
27072370-2	2016	Two key KP enzymes that catabolize kynurenine include kynurenine-aminotransferase II (KATII), which yields antioxidative kynurenine acid [KYNA] in astrocytes, and kynurenine-3-monooxygenase (KMO), which produces neurotoxic metabolites in microglia.	Kynurenine	35-45	aminoadipate aminotransferase	Homo sapiens	86-91
27489009-8	2016	We observed significant positive associations between serum interleukin-10 (IL-10) and serum kynurenine (P = 0.0002), the kynurenine-to-tryptophan ratio (KTR) (P = 0.003), 3-hydroxykynurenine (P = 0.01), and 3-hydroxyanthranilic acid (P = 0.04).	Kynurenine	122-132	interleukin 10	Homo sapiens	76-81
27072370-2	2016	Two key KP enzymes that catabolize kynurenine include kynurenine-aminotransferase II (KATII), which yields antioxidative kynurenine acid [KYNA] in astrocytes, and kynurenine-3-monooxygenase (KMO), which produces neurotoxic metabolites in microglia.	Kynurenine	35-45	kynurenine 3-monooxygenase	Homo sapiens	163-189
27072370-2	2016	Two key KP enzymes that catabolize kynurenine include kynurenine-aminotransferase II (KATII), which yields antioxidative kynurenine acid [KYNA] in astrocytes, and kynurenine-3-monooxygenase (KMO), which produces neurotoxic metabolites in microglia.	Kynurenine	35-45	kynurenine 3-monooxygenase	Homo sapiens	191-194
27475106-3	2016	Inhibition of kynurenine-3-monooxygenase (KMO) shifts the metabolic kynurenine pathway towards production of kynurenic acid, which leads to a reduction of glutamatergic/NMDAR activity via different mechanisms.	Kynurenine	14-24	kynurenine 3-monooxygenase	Rattus norvegicus	42-45
27489009-12	2016	The observed association between IL-10 and kynurenine is unexpected and suggests that kynurenine-linked mechanisms promoting negative regulation of inflammatory responses are associated with normal immune homeostasis.	Kynurenine	43-53	interleukin 10	Homo sapiens	33-38
27489009-12	2016	The observed association between IL-10 and kynurenine is unexpected and suggests that kynurenine-linked mechanisms promoting negative regulation of inflammatory responses are associated with normal immune homeostasis.	Kynurenine	86-96	interleukin 10	Homo sapiens	33-38
27165635-0	2016	Repeated LPS Injection Induces Distinct Changes in the Kynurenine Pathway in Mice.	Kynurenine	55-65	toll-like receptor 4	Mus musculus	9-12
27165635-3	2016	Recent data indicate that the kynurenine pathway contributes to LPS-induced aberrant behaviors.	Kynurenine	30-40	toll-like receptor 4	Mus musculus	64-67
27165635-5	2016	Here, we therefore aimed to evaluate the effects of single versus repeated administration of LPS on the kynurenine pathway.	Kynurenine	104-114	toll-like receptor 4	Mus musculus	93-96
27165635-8	2016	Animals given repeated injections of LPS showed a more robust induction of the kynurenine pathway in contrast to animals receiving a single injection.	Kynurenine	79-89	toll-like receptor 4	Mus musculus	37-40
27819068-4	2016	Of the immunosuppressive mediators that contribute to the inhibition of productive tumor immunity, indoleamine 2,3 dioxygenase 1 (IDO1), a rate-limiting enzyme that catabolizes tryptophan (Trp) into kynurenine (Kyn), has been demonstrated to be expressed at elevated levels in patients with malignant glioma.	Kynurenine	199-209	indoleamine 2,3-dioxygenase 1	Homo sapiens	99-128
27819068-4	2016	Of the immunosuppressive mediators that contribute to the inhibition of productive tumor immunity, indoleamine 2,3 dioxygenase 1 (IDO1), a rate-limiting enzyme that catabolizes tryptophan (Trp) into kynurenine (Kyn), has been demonstrated to be expressed at elevated levels in patients with malignant glioma.	Kynurenine	199-209	indoleamine 2,3-dioxygenase 1	Homo sapiens	130-134
27819068-4	2016	Of the immunosuppressive mediators that contribute to the inhibition of productive tumor immunity, indoleamine 2,3 dioxygenase 1 (IDO1), a rate-limiting enzyme that catabolizes tryptophan (Trp) into kynurenine (Kyn), has been demonstrated to be expressed at elevated levels in patients with malignant glioma.	Kynurenine	211-214	indoleamine 2,3-dioxygenase 1	Homo sapiens	99-128
27819068-4	2016	Of the immunosuppressive mediators that contribute to the inhibition of productive tumor immunity, indoleamine 2,3 dioxygenase 1 (IDO1), a rate-limiting enzyme that catabolizes tryptophan (Trp) into kynurenine (Kyn), has been demonstrated to be expressed at elevated levels in patients with malignant glioma.	Kynurenine	211-214	indoleamine 2,3-dioxygenase 1	Homo sapiens	130-134
27348627-8	2016	ET was rich in IDO1 and the AhR-ligand kynurenine compared with control tissue, possibly promoting MC activation through AhR.	Kynurenine	39-49	aryl hydrocarbon receptor	Homo sapiens	28-31
27348627-8	2016	ET was rich in IDO1 and the AhR-ligand kynurenine compared with control tissue, possibly promoting MC activation through AhR.	Kynurenine	39-49	aryl hydrocarbon receptor	Homo sapiens	121-124
27540379-5	2016	KP enzymes, indoleamine 2,3-dioxygenase (IDO-1) and tryptophan dioxygenase (highest expression in hepatic cells), are the principal enzymes triggering activation of the KP to produce kynurenine from TRP.	Kynurenine	183-193	indoleamine 2,3-dioxygenase 1	Homo sapiens	41-46
27356894-0	2016	Kynurenine Reduces Memory CD4 T-Cell Survival by Interfering with Interleukin-2 Signaling Early during HIV-1 Infection.	Kynurenine	0-10	CD4 molecule	Homo sapiens	26-29
27356894-0	2016	Kynurenine Reduces Memory CD4 T-Cell Survival by Interfering with Interleukin-2 Signaling Early during HIV-1 Infection.	Kynurenine	0-10	interleukin 2	Homo sapiens	66-79
27356894-3	2016	Herein, we show that the increased production of kynurenine correlates with defective interleukin-2 (IL-2) signaling in memory CD4 T cells from HIV-infected subjects.	Kynurenine	49-59	interleukin 2	Homo sapiens	86-99
27356894-3	2016	Herein, we show that the increased production of kynurenine correlates with defective interleukin-2 (IL-2) signaling in memory CD4 T cells from HIV-infected subjects.	Kynurenine	49-59	interleukin 2	Homo sapiens	101-105
27356894-3	2016	Herein, we show that the increased production of kynurenine correlates with defective interleukin-2 (IL-2) signaling in memory CD4 T cells from HIV-infected subjects.	Kynurenine	49-59	CD4 molecule	Homo sapiens	127-130
27356894-5	2016	Treatment of memory CD4 T cells with the concentration of kynurenine found in plasma inhibited IL-2 signaling through the production of reactive oxygen species.	Kynurenine	58-68	CD4 molecule	Homo sapiens	20-23
27356894-5	2016	Treatment of memory CD4 T cells with the concentration of kynurenine found in plasma inhibited IL-2 signaling through the production of reactive oxygen species.	Kynurenine	58-68	interleukin 2	Homo sapiens	95-99
27356894-7	2016	Early initiation of antiretroviral therapy restored the IL-2 response in memory CD4 T cells by reducing reactive oxygen species and kynurenine production.	Kynurenine	132-142	interleukin 2	Homo sapiens	56-60
27356894-7	2016	Early initiation of antiretroviral therapy restored the IL-2 response in memory CD4 T cells by reducing reactive oxygen species and kynurenine production.	Kynurenine	132-142	CD4 molecule	Homo sapiens	80-83
27356894-8	2016	The study findings provide a kynurenine-dependent mechanism through IL-2 signaling for reduced CD4 T-cell survival, which can be reversed by early treatment initiation in HIV-1 infection.	Kynurenine	29-39	interleukin 2	Homo sapiens	68-72
27356894-8	2016	The study findings provide a kynurenine-dependent mechanism through IL-2 signaling for reduced CD4 T-cell survival, which can be reversed by early treatment initiation in HIV-1 infection.	Kynurenine	29-39	CD4 molecule	Homo sapiens	95-98
27356894-11	2016	These new findings show that the enhanced production of kynurenine, a metabolite related to tryptophan catabolism, also impairs memory CD4 T-cell survival and interferes with IL-2 signaling early during HIV-1 infection.	Kynurenine	56-66	CD4 molecule	Homo sapiens	135-138
27356894-11	2016	These new findings show that the enhanced production of kynurenine, a metabolite related to tryptophan catabolism, also impairs memory CD4 T-cell survival and interferes with IL-2 signaling early during HIV-1 infection.	Kynurenine	56-66	interleukin 2	Homo sapiens	175-179
27072164-1	2016	Tryptophan-2, 3-dioxygenase (TDO) is a heme-containing protein catalyzing the first reaction in the kynurenine pathway, which incorporates oxygen into the indole moiety of tryptophan and catalyzes it into kynurenine (KYN).	Kynurenine	205-215	tryptophan 2,3-dioxygenase	Homo sapiens	0-27
27106797-1	2016	OBJECTIVES: Indoleamine 2,3-Dioxygenase (IDO) catalyses the degradation of the essential amino acid tryptophan leading to the production of immunosuppressive Kynurenine.	Kynurenine	158-168	indoleamine 2,3-dioxygenase 1	Homo sapiens	12-39
27106797-1	2016	OBJECTIVES: Indoleamine 2,3-Dioxygenase (IDO) catalyses the degradation of the essential amino acid tryptophan leading to the production of immunosuppressive Kynurenine.	Kynurenine	158-168	indoleamine 2,3-dioxygenase 1	Homo sapiens	41-44
27106797-2	2016	In the present study, we developed a modified method for measurement of Kynurenine/tryptophan (K/T) ratio in the cervical tissue using HPLC and investigated its relationship with the expression of IDO1 and 2 genes in the cervical tumour milieu.	Kynurenine	72-82	indoleamine 2,3-dioxygenase 1	Homo sapiens	197-207
27358029-1	2016	The role of the amino acid tryptophan in the generation of 5-hydroxy-tryptamine (5-HT) has been expanded over the past 30 years with recognition that its oxidation by indoleamine-2,3-dioxygenase (IDO) results in the formation of kynurenine and metabolites which regulate neuronal excitability, psychiatric status, immune cell activity and balance, and probably implantation and the development of embryos.	Kynurenine	229-239	indoleamine 2,3-dioxygenase 1	Homo sapiens	167-194
27358029-1	2016	The role of the amino acid tryptophan in the generation of 5-hydroxy-tryptamine (5-HT) has been expanded over the past 30 years with recognition that its oxidation by indoleamine-2,3-dioxygenase (IDO) results in the formation of kynurenine and metabolites which regulate neuronal excitability, psychiatric status, immune cell activity and balance, and probably implantation and the development of embryos.	Kynurenine	229-239	indoleamine 2,3-dioxygenase 1	Homo sapiens	196-199
27316681-8	2016	Addition of the tryptophan catabolite kynurenine to DC cultures in which IDO activity was blocked restored long-term IDO expression in wild-type DC but not in AhR-deficient DC, establishing the central role of the kynurenine-AhR pathway in maintaining IDO expression in tolerogenic DC.	Kynurenine	38-48	indoleamine 2,3-dioxygenase 1	Mus musculus	73-76
27316681-8	2016	Addition of the tryptophan catabolite kynurenine to DC cultures in which IDO activity was blocked restored long-term IDO expression in wild-type DC but not in AhR-deficient DC, establishing the central role of the kynurenine-AhR pathway in maintaining IDO expression in tolerogenic DC.	Kynurenine	38-48	indoleamine 2,3-dioxygenase 1	Mus musculus	117-120
27316681-8	2016	Addition of the tryptophan catabolite kynurenine to DC cultures in which IDO activity was blocked restored long-term IDO expression in wild-type DC but not in AhR-deficient DC, establishing the central role of the kynurenine-AhR pathway in maintaining IDO expression in tolerogenic DC.	Kynurenine	38-48	aryl-hydrocarbon receptor	Mus musculus	159-162
27316681-8	2016	Addition of the tryptophan catabolite kynurenine to DC cultures in which IDO activity was blocked restored long-term IDO expression in wild-type DC but not in AhR-deficient DC, establishing the central role of the kynurenine-AhR pathway in maintaining IDO expression in tolerogenic DC.	Kynurenine	38-48	aryl-hydrocarbon receptor	Mus musculus	225-228
27316681-8	2016	Addition of the tryptophan catabolite kynurenine to DC cultures in which IDO activity was blocked restored long-term IDO expression in wild-type DC but not in AhR-deficient DC, establishing the central role of the kynurenine-AhR pathway in maintaining IDO expression in tolerogenic DC.	Kynurenine	38-48	indoleamine 2,3-dioxygenase 1	Mus musculus	117-120
26965653-8	2016	The IDO activation subsequently increased kynurerine production and the kynurenine/tryptophan ratio and decreased the levels of neurotrophic factors in the PFC and HC, which contributed to Abeta-associated behavioral disturbances.	Kynurenine	72-82	indoleamine 2,3-dioxygenase 1	Mus musculus	4-7
27072164-1	2016	Tryptophan-2, 3-dioxygenase (TDO) is a heme-containing protein catalyzing the first reaction in the kynurenine pathway, which incorporates oxygen into the indole moiety of tryptophan and catalyzes it into kynurenine (KYN).	Kynurenine	100-110	tryptophan 2,3-dioxygenase	Homo sapiens	0-27
27072164-1	2016	Tryptophan-2, 3-dioxygenase (TDO) is a heme-containing protein catalyzing the first reaction in the kynurenine pathway, which incorporates oxygen into the indole moiety of tryptophan and catalyzes it into kynurenine (KYN).	Kynurenine	100-110	tryptophan 2,3-dioxygenase	Homo sapiens	29-32
27072164-1	2016	Tryptophan-2, 3-dioxygenase (TDO) is a heme-containing protein catalyzing the first reaction in the kynurenine pathway, which incorporates oxygen into the indole moiety of tryptophan and catalyzes it into kynurenine (KYN).	Kynurenine	205-215	tryptophan 2,3-dioxygenase	Homo sapiens	29-32
27072164-1	2016	Tryptophan-2, 3-dioxygenase (TDO) is a heme-containing protein catalyzing the first reaction in the kynurenine pathway, which incorporates oxygen into the indole moiety of tryptophan and catalyzes it into kynurenine (KYN).	Kynurenine	217-220	tryptophan 2,3-dioxygenase	Homo sapiens	0-27
27072164-1	2016	Tryptophan-2, 3-dioxygenase (TDO) is a heme-containing protein catalyzing the first reaction in the kynurenine pathway, which incorporates oxygen into the indole moiety of tryptophan and catalyzes it into kynurenine (KYN).	Kynurenine	217-220	tryptophan 2,3-dioxygenase	Homo sapiens	29-32
27072164-2	2016	The activation of TDO results in the depletion of tryptophan and the accumulation of kynurenine and its metabolites.	Kynurenine	85-95	tryptophan 2,3-dioxygenase	Homo sapiens	18-21
27088321-1	2016	OBJECTIVE: Plasma kynurenine/tryptophan ratio, a biomarker of indoleamine 2,3-dioxygenase-1 (IDO) activity, is a strong independent predictor of mortality in HIV-infected Ugandans initiating antiretroviral therapy (ART) and may play a key role in HIV pathogenesis.	Kynurenine	18-28	indoleamine 2,3-dioxygenase 1	Homo sapiens	62-91
27088321-6	2016	Several polymorphisms in candidate genes TNF, IFNGR1, and TLR4 were associated with log10 kynurenine/tryptophan ratio (P &lt; 5.0 x 10).	Kynurenine	90-100	tumor necrosis factor	Homo sapiens	41-44
27088321-1	2016	OBJECTIVE: Plasma kynurenine/tryptophan ratio, a biomarker of indoleamine 2,3-dioxygenase-1 (IDO) activity, is a strong independent predictor of mortality in HIV-infected Ugandans initiating antiretroviral therapy (ART) and may play a key role in HIV pathogenesis.	Kynurenine	18-28	indoleamine 2,3-dioxygenase 1	Homo sapiens	93-96
26493952-0	2016	Smaller Dentate Gyrus and CA2 and CA3 Volumes Are Associated with Kynurenine Metabolites in Collegiate Football Athletes.	Kynurenine	66-76	carbonic anhydrase 2	Homo sapiens	26-29
27088321-6	2016	Several polymorphisms in candidate genes TNF, IFNGR1, and TLR4 were associated with log10 kynurenine/tryptophan ratio (P &lt; 5.0 x 10).	Kynurenine	90-100	interferon gamma receptor 1	Homo sapiens	46-52
27088321-6	2016	Several polymorphisms in candidate genes TNF, IFNGR1, and TLR4 were associated with log10 kynurenine/tryptophan ratio (P &lt; 5.0 x 10).	Kynurenine	90-100	toll like receptor 4	Homo sapiens	58-62
26936918-5	2016	In methylthioadenosine phosphorylase (MTAP)-deficient glioblastoma cells, expression of MTAP transgene did not alter methionine dependency, but compromised tumor growth in vivo We discovered that a lack of the kynurenine-metabolizing enzymes kynurenine monooxygenase and/or kynureninase promotes the accumulation of kynurenine, which triggers immune evasion in glioblastoma cells.	Kynurenine	210-220	methylthioadenosine phosphorylase	Homo sapiens	38-42
26936918-5	2016	In methylthioadenosine phosphorylase (MTAP)-deficient glioblastoma cells, expression of MTAP transgene did not alter methionine dependency, but compromised tumor growth in vivo We discovered that a lack of the kynurenine-metabolizing enzymes kynurenine monooxygenase and/or kynureninase promotes the accumulation of kynurenine, which triggers immune evasion in glioblastoma cells.	Kynurenine	210-220	methylthioadenosine phosphorylase	Homo sapiens	88-92
26936918-5	2016	In methylthioadenosine phosphorylase (MTAP)-deficient glioblastoma cells, expression of MTAP transgene did not alter methionine dependency, but compromised tumor growth in vivo We discovered that a lack of the kynurenine-metabolizing enzymes kynurenine monooxygenase and/or kynureninase promotes the accumulation of kynurenine, which triggers immune evasion in glioblastoma cells.	Kynurenine	242-252	methylthioadenosine phosphorylase	Homo sapiens	88-92
26493952-0	2016	Smaller Dentate Gyrus and CA2 and CA3 Volumes Are Associated with Kynurenine Metabolites in Collegiate Football Athletes.	Kynurenine	66-76	carbonic anhydrase 3	Homo sapiens	34-37
26982018-2	2016	Objectives Indoleamine 2,3-dioxygenase (IDO) is expressed in many cells and it catabolises the essential amino acid tryptophan to kynurenine.	Kynurenine	130-140	indoleamine 2,3-dioxygenase 1	Homo sapiens	11-38
26982018-2	2016	Objectives Indoleamine 2,3-dioxygenase (IDO) is expressed in many cells and it catabolises the essential amino acid tryptophan to kynurenine.	Kynurenine	130-140	indoleamine 2,3-dioxygenase 1	Homo sapiens	40-43
26866723-1	2016	OBJECTIVE: Indoleamine 2,3-dioxygenase (IDO), the rate-limiting enzyme that converts tryptophan to kynurenine, is driven in part by type I and type II interferons (IFNs).	Kynurenine	99-109	indoleamine 2,3-dioxygenase 1	Homo sapiens	11-38
26866723-1	2016	OBJECTIVE: Indoleamine 2,3-dioxygenase (IDO), the rate-limiting enzyme that converts tryptophan to kynurenine, is driven in part by type I and type II interferons (IFNs).	Kynurenine	99-109	indoleamine 2,3-dioxygenase 1	Homo sapiens	40-43
26866723-2	2016	Naive T cells are polarized into FoxP3+ Treg cells upon exposure to either IDO+ cells or kynurenine.	Kynurenine	89-99	forkhead box P3	Homo sapiens	33-38
26866723-6	2016	Expression levels of messenger RNA (mRNA) for IDO and downstream enzymes in the kynurenine pathway were assessed in CD14+ monocytes using real-time quantitative polymerase chain reaction.	Kynurenine	80-90	indoleamine 2,3-dioxygenase 1	Homo sapiens	46-49
26866723-8	2016	RESULTS: Significantly increased levels of IDO activity (assessed as the kynurenine:tryptophan ratio) (P = 0.0054) and percentages of CD25(high) FoxP3+ Treg cells (P = 0.039) were observed in the serum from IFN-positive patients with primary SS, and these parameters were significantly correlated with one another (r = 0.511, P = 0.002).	Kynurenine	73-83	indoleamine 2,3-dioxygenase 1	Homo sapiens	43-46
26866723-12	2016	In addition, IFN-positive patients with primary SS exhibit an imbalanced kynurenine pathway, with evidence of a shift toward potentially more proapoptotic and neurotoxic metabolites.	Kynurenine	73-83	interferon alpha 1	Homo sapiens	13-16
27190010-8	2016	The gene most highly downregulated by ibuprofen was neuronal tryptophan 2,3-dioxygenase (Tdo2), which encodes an enzyme that metabolizes tryptophan to kynurenine.	Kynurenine	151-161	tryptophan 2,3-dioxygenase	Mus musculus	61-87
27190010-8	2016	The gene most highly downregulated by ibuprofen was neuronal tryptophan 2,3-dioxygenase (Tdo2), which encodes an enzyme that metabolizes tryptophan to kynurenine.	Kynurenine	151-161	tryptophan 2,3-dioxygenase	Mus musculus	89-93
26636389-1	2016	OBJECT Indoleamine 2,3-dioxygenase (IDO), a key enzyme of tryptophan (Trp) metabolism, is involved in tumor-derived immune suppression through depletion of Trp and accumulation of the metabolite kynurenine, resulting in inactivation of natural killer cells and generation of regulatory T cells (Tregs).	Kynurenine	195-205	indoleamine 2,3-dioxygenase 1	Mus musculus	36-39
27282934-0	2016	EWS-FLI1 impairs aryl hydrocarbon receptor activation by blocking tryptophan breakdown via the kynurenine pathway.	Kynurenine	95-105	EWS RNA binding protein 1	Homo sapiens	0-3
27282934-0	2016	EWS-FLI1 impairs aryl hydrocarbon receptor activation by blocking tryptophan breakdown via the kynurenine pathway.	Kynurenine	95-105	Fli-1 proto-oncogene, ETS transcription factor	Homo sapiens	4-8
27282934-0	2016	EWS-FLI1 impairs aryl hydrocarbon receptor activation by blocking tryptophan breakdown via the kynurenine pathway.	Kynurenine	95-105	aryl hydrocarbon receptor	Homo sapiens	17-42
27192116-3	2016	Simultaneous treatment with epacadostat and IFN-gamma plus lipopolysaccharide (LPS) did not change the phenotype of matured human DCs, and as expected decreased the tryptophan breakdown and kynurenine production.	Kynurenine	190-200	interferon gamma	Homo sapiens	44-53
26641976-18	2016	No significant change was observed in the IL-8 profile in tryptophan-treated U251 cells except that L-kynurenine at 10 microg/mL produced significantly high level of an inflammatory cytokine IL-8.	Kynurenine	100-112	C-X-C motif chemokine ligand 8	Homo sapiens	191-195
27107370-7	2016	RESULTS: Supernatant fluids from cultures of IDO(+) DCs had decreased tryptophan and increased kynurenine levels, reflecting IDO activity.	Kynurenine	95-105	indoleamine 2,3-dioxygenase 1	Mus musculus	45-48
27107370-7	2016	RESULTS: Supernatant fluids from cultures of IDO(+) DCs had decreased tryptophan and increased kynurenine levels, reflecting IDO activity.	Kynurenine	95-105	indoleamine 2,3-dioxygenase 1	Mus musculus	125-128
27314340-1	2016	Kynurenine aminotransferase isozymes (KATs 1-4) are members of the pyridoxal-5"-phosphate (PLP)-dependent enzyme family, which catalyse the permanent conversion of l-kynurenine (l-KYN) to kynurenic acid (KYNA), a known neuroactive agent.	Kynurenine	164-176	kynurenine aminotransferase 1	Homo sapiens	38-46
27314340-1	2016	Kynurenine aminotransferase isozymes (KATs 1-4) are members of the pyridoxal-5"-phosphate (PLP)-dependent enzyme family, which catalyse the permanent conversion of l-kynurenine (l-KYN) to kynurenic acid (KYNA), a known neuroactive agent.	Kynurenine	164-176	pyridoxal phosphatase	Homo sapiens	91-94
27314340-1	2016	Kynurenine aminotransferase isozymes (KATs 1-4) are members of the pyridoxal-5"-phosphate (PLP)-dependent enzyme family, which catalyse the permanent conversion of l-kynurenine (l-KYN) to kynurenic acid (KYNA), a known neuroactive agent.	Kynurenine	178-183	kynurenine aminotransferase 1	Homo sapiens	38-46
27314340-1	2016	Kynurenine aminotransferase isozymes (KATs 1-4) are members of the pyridoxal-5"-phosphate (PLP)-dependent enzyme family, which catalyse the permanent conversion of l-kynurenine (l-KYN) to kynurenic acid (KYNA), a known neuroactive agent.	Kynurenine	178-183	pyridoxal phosphatase	Homo sapiens	91-94
27272805-6	2016	C-reactive protein (CRP) and interleukin-6 (IL-6) correlated with each other and exhibited positive correlation with age, body-mass index (BMI), leukocyte count, platelet count, kynurenine, kynurenine/tryptophan ratio and urinary neopterin and a negative correlation with vitamin D and retinol.	Kynurenine	178-188	C-reactive protein	Homo sapiens	0-18
27272805-6	2016	C-reactive protein (CRP) and interleukin-6 (IL-6) correlated with each other and exhibited positive correlation with age, body-mass index (BMI), leukocyte count, platelet count, kynurenine, kynurenine/tryptophan ratio and urinary neopterin and a negative correlation with vitamin D and retinol.	Kynurenine	178-188	interleukin 6	Homo sapiens	29-42
27272805-6	2016	C-reactive protein (CRP) and interleukin-6 (IL-6) correlated with each other and exhibited positive correlation with age, body-mass index (BMI), leukocyte count, platelet count, kynurenine, kynurenine/tryptophan ratio and urinary neopterin and a negative correlation with vitamin D and retinol.	Kynurenine	178-188	interleukin 6	Homo sapiens	44-48
27272805-6	2016	C-reactive protein (CRP) and interleukin-6 (IL-6) correlated with each other and exhibited positive correlation with age, body-mass index (BMI), leukocyte count, platelet count, kynurenine, kynurenine/tryptophan ratio and urinary neopterin and a negative correlation with vitamin D and retinol.	Kynurenine	190-200	C-reactive protein	Homo sapiens	0-18
27272805-6	2016	C-reactive protein (CRP) and interleukin-6 (IL-6) correlated with each other and exhibited positive correlation with age, body-mass index (BMI), leukocyte count, platelet count, kynurenine, kynurenine/tryptophan ratio and urinary neopterin and a negative correlation with vitamin D and retinol.	Kynurenine	190-200	interleukin 6	Homo sapiens	29-42
27272805-6	2016	C-reactive protein (CRP) and interleukin-6 (IL-6) correlated with each other and exhibited positive correlation with age, body-mass index (BMI), leukocyte count, platelet count, kynurenine, kynurenine/tryptophan ratio and urinary neopterin and a negative correlation with vitamin D and retinol.	Kynurenine	190-200	interleukin 6	Homo sapiens	44-48
26725996-2	2016	One pathway with immunomodulatory ability is the tryptophan metabolism pathway, which promotes immune suppression through the enzyme indoleamine 2,3-dioxygenase (IDO) and subsequent production of kynurenine.	Kynurenine	196-206	indoleamine 2,3-dioxygenase 1	Homo sapiens	162-165
27260779-1	2016	INTRODUCTION: Indoleamine 2,3-dioxygenase (IDO) catalyzes the initial step in the catabolism of l-tryptophan along the kynurenine pathway and exerts immunosuppressive properties in inflammatory and tumor tissues by blocking locally T-lymphocyte proliferation.	Kynurenine	119-129	indoleamine 2,3-dioxygenase 1	Homo sapiens	14-41
27260779-1	2016	INTRODUCTION: Indoleamine 2,3-dioxygenase (IDO) catalyzes the initial step in the catabolism of l-tryptophan along the kynurenine pathway and exerts immunosuppressive properties in inflammatory and tumor tissues by blocking locally T-lymphocyte proliferation.	Kynurenine	119-129	indoleamine 2,3-dioxygenase 1	Homo sapiens	43-46
26923060-7	2016	These Pichia expressed proteins can effectively heterodimerize and form the ternary AHR/ARNT/enhancer complex in the presence of beta-naphthoflavone or kynurenine.	Kynurenine	152-162	aryl hydrocarbon receptor	Homo sapiens	84-87
26923060-7	2016	These Pichia expressed proteins can effectively heterodimerize and form the ternary AHR/ARNT/enhancer complex in the presence of beta-naphthoflavone or kynurenine.	Kynurenine	152-162	aryl hydrocarbon receptor nuclear translocator	Homo sapiens	88-92
27020609-1	2016	Model for AHR activation by kynurenine via oxidized-LDL, TLR2/4, TGFbeta, and IDO1.	Kynurenine	28-38	aryl-hydrocarbon receptor	Mus musculus	10-13
27020609-1	2016	Model for AHR activation by kynurenine via oxidized-LDL, TLR2/4, TGFbeta, and IDO1.	Kynurenine	28-38	toll-like receptor 2	Mus musculus	57-63
27020609-1	2016	Model for AHR activation by kynurenine via oxidized-LDL, TLR2/4, TGFbeta, and IDO1.	Kynurenine	28-38	transforming growth factor, beta 1	Mus musculus	65-72
27020609-1	2016	Model for AHR activation by kynurenine via oxidized-LDL, TLR2/4, TGFbeta, and IDO1.	Kynurenine	28-38	indoleamine 2,3-dioxygenase 1	Mus musculus	78-82
27020609-10	2016	At physiological levels, kynurenine but not kynurenic acid (both tryptophan metabolites and known AHR agonists) activated AHR-directed luciferase expression.	Kynurenine	25-35	aryl-hydrocarbon receptor	Mus musculus	122-125
27020609-11	2016	We propose a hepatocyte-based model, in which kynurenine production is increased by enhanced IDO1 activity stimulated by TGFbeta1 and TLR2/4 signaling, via PI3K and NF-kappaB, to perpetuate a cycle of AHR activation to cause obesity; and inhibition of the AHR, in turn, blocks the cycle"s output to prevent obesity.	Kynurenine	46-56	indoleamine 2,3-dioxygenase 1	Mus musculus	93-97
27020609-11	2016	We propose a hepatocyte-based model, in which kynurenine production is increased by enhanced IDO1 activity stimulated by TGFbeta1 and TLR2/4 signaling, via PI3K and NF-kappaB, to perpetuate a cycle of AHR activation to cause obesity; and inhibition of the AHR, in turn, blocks the cycle"s output to prevent obesity.	Kynurenine	46-56	transforming growth factor, beta 1	Mus musculus	121-129
27020609-11	2016	We propose a hepatocyte-based model, in which kynurenine production is increased by enhanced IDO1 activity stimulated by TGFbeta1 and TLR2/4 signaling, via PI3K and NF-kappaB, to perpetuate a cycle of AHR activation to cause obesity; and inhibition of the AHR, in turn, blocks the cycle"s output to prevent obesity.	Kynurenine	46-56	toll-like receptor 2	Mus musculus	134-140
27020609-11	2016	We propose a hepatocyte-based model, in which kynurenine production is increased by enhanced IDO1 activity stimulated by TGFbeta1 and TLR2/4 signaling, via PI3K and NF-kappaB, to perpetuate a cycle of AHR activation to cause obesity; and inhibition of the AHR, in turn, blocks the cycle"s output to prevent obesity.	Kynurenine	46-56	aryl-hydrocarbon receptor	Mus musculus	201-204
27020609-11	2016	We propose a hepatocyte-based model, in which kynurenine production is increased by enhanced IDO1 activity stimulated by TGFbeta1 and TLR2/4 signaling, via PI3K and NF-kappaB, to perpetuate a cycle of AHR activation to cause obesity; and inhibition of the AHR, in turn, blocks the cycle"s output to prevent obesity.	Kynurenine	46-56	aryl-hydrocarbon receptor	Mus musculus	256-259
27080473-6	2016	Gene expression analyses showed significant modifications in the expression of the AhR target genes CYP1B1 and AHRR in AIP-mutated fibroblasts, both before and after stimulation with the endogenous AhR ligand kynurenine.	Kynurenine	209-219	aryl hydrocarbon receptor	Rattus norvegicus	83-86
27168185-6	2016	Moreover, kynurenine (Kyn), a tryptophan catabolite made by cells expressing IDO, incited pain hypersensitivity in uninfected IDO1-deficient mice and Kyn potentiated pain hypersensitivity due to MuLV infection.	Kynurenine	10-20	indoleamine 2,3-dioxygenase 1	Mus musculus	77-80
27168185-6	2016	Moreover, kynurenine (Kyn), a tryptophan catabolite made by cells expressing IDO, incited pain hypersensitivity in uninfected IDO1-deficient mice and Kyn potentiated pain hypersensitivity due to MuLV infection.	Kynurenine	22-25	indoleamine 2,3-dioxygenase 1	Mus musculus	77-80
27114543-0	2016	Tryptophan-2,3-dioxygenase (TDO) inhibition ameliorates neurodegeneration by modulation of kynurenine pathway metabolites.	Kynurenine	91-101	vermilion	Drosophila melanogaster	0-26
27114543-0	2016	Tryptophan-2,3-dioxygenase (TDO) inhibition ameliorates neurodegeneration by modulation of kynurenine pathway metabolites.	Kynurenine	91-101	vermilion	Drosophila melanogaster	28-31
27142940-1	2016	BACKGROUND: Increased tryptophan metabolism towards the production of kynurenine via indoleamine/tryptophan-2,3-dioxygenases (DOs: Ido1, Ido2, and Tdo2) is strongly associated with the prevalence of major depressive disorder in patients and the induction of depression-like behaviors in animal models.	Kynurenine	70-80	indoleamine 2,3-dioxygenase 1	Homo sapiens	131-135
27142940-1	2016	BACKGROUND: Increased tryptophan metabolism towards the production of kynurenine via indoleamine/tryptophan-2,3-dioxygenases (DOs: Ido1, Ido2, and Tdo2) is strongly associated with the prevalence of major depressive disorder in patients and the induction of depression-like behaviors in animal models.	Kynurenine	70-80	indoleamine 2,3-dioxygenase 2	Homo sapiens	137-141
27142940-1	2016	BACKGROUND: Increased tryptophan metabolism towards the production of kynurenine via indoleamine/tryptophan-2,3-dioxygenases (DOs: Ido1, Ido2, and Tdo2) is strongly associated with the prevalence of major depressive disorder in patients and the induction of depression-like behaviors in animal models.	Kynurenine	70-80	tryptophan 2,3-dioxygenase	Homo sapiens	147-151
27050278-4	2016	Mechanistically, condition medium of CAF or exogenous kynurenine stimulated AKT, with no lysine 1 (WNK1) and cAMP response element-bindingprotein (CREB) phosphorylation in lung cancer cells.	Kynurenine	54-64	thymoma viral proto-oncogene 1	Mus musculus	76-79
27050278-5	2016	Inhibition of the AKT/CREB pathway prevents cancer proliferation, while inhibition of the AKT/ WNK1 reverted epithelial-to-mesenchymal transition and cancer migration induced by kynurenine.	Kynurenine	178-188	thymoma viral proto-oncogene 1	Mus musculus	90-93
27050278-5	2016	Inhibition of the AKT/CREB pathway prevents cancer proliferation, while inhibition of the AKT/ WNK1 reverted epithelial-to-mesenchymal transition and cancer migration induced by kynurenine.	Kynurenine	178-188	WNK lysine deficient protein kinase 1	Mus musculus	95-99
27080473-6	2016	Gene expression analyses showed significant modifications in the expression of the AhR target genes CYP1B1 and AHRR in AIP-mutated fibroblasts, both before and after stimulation with the endogenous AhR ligand kynurenine.	Kynurenine	209-219	cytochrome P450, family 1, subfamily b, polypeptide 1	Rattus norvegicus	100-106
27080473-6	2016	Gene expression analyses showed significant modifications in the expression of the AhR target genes CYP1B1 and AHRR in AIP-mutated fibroblasts, both before and after stimulation with the endogenous AhR ligand kynurenine.	Kynurenine	209-219	aryl-hydrocarbon receptor repressor	Rattus norvegicus	111-115
27080473-6	2016	Gene expression analyses showed significant modifications in the expression of the AhR target genes CYP1B1 and AHRR in AIP-mutated fibroblasts, both before and after stimulation with the endogenous AhR ligand kynurenine.	Kynurenine	209-219	aryl-hydrocarbon receptor-interacting protein	Rattus norvegicus	119-122
27080473-6	2016	Gene expression analyses showed significant modifications in the expression of the AhR target genes CYP1B1 and AHRR in AIP-mutated fibroblasts, both before and after stimulation with the endogenous AhR ligand kynurenine.	Kynurenine	209-219	aryl hydrocarbon receptor	Rattus norvegicus	198-201
27080473-7	2016	Kynurenine increased Cyp1b1 expression to a greater extent in GH3 cells overexpressing wild type compared with cells expressing mutant AIP Knockdown of endogenous Aip in these cells attenuated Cyp1b1 induction by the AhR ligand.	Kynurenine	0-10	cytochrome P450, family 1, subfamily b, polypeptide 1	Rattus norvegicus	21-27
27080473-7	2016	Kynurenine increased Cyp1b1 expression to a greater extent in GH3 cells overexpressing wild type compared with cells expressing mutant AIP Knockdown of endogenous Aip in these cells attenuated Cyp1b1 induction by the AhR ligand.	Kynurenine	0-10	aryl-hydrocarbon receptor-interacting protein	Rattus norvegicus	163-166
27080473-7	2016	Kynurenine increased Cyp1b1 expression to a greater extent in GH3 cells overexpressing wild type compared with cells expressing mutant AIP Knockdown of endogenous Aip in these cells attenuated Cyp1b1 induction by the AhR ligand.	Kynurenine	0-10	cytochrome P450, family 1, subfamily b, polypeptide 1	Rattus norvegicus	193-199
27080473-7	2016	Kynurenine increased Cyp1b1 expression to a greater extent in GH3 cells overexpressing wild type compared with cells expressing mutant AIP Knockdown of endogenous Aip in these cells attenuated Cyp1b1 induction by the AhR ligand.	Kynurenine	0-10	aryl hydrocarbon receptor	Rattus norvegicus	217-220
27080473-8	2016	Both mutant AIP expression and knockdown of endogenous Aip affected the kynurenine-dependent GH secretion of GH3 cells.	Kynurenine	72-82	aryl-hydrocarbon receptor-interacting protein	Rattus norvegicus	12-15
27080473-8	2016	Both mutant AIP expression and knockdown of endogenous Aip affected the kynurenine-dependent GH secretion of GH3 cells.	Kynurenine	72-82	aryl-hydrocarbon receptor-interacting protein	Rattus norvegicus	55-58
26857571-8	2016	Finally, kynurenines represent known ligands of the mammalian aryl hydrocarbon receptor (AHR), and UPEC infection of Ahr(-/-)mice recapitulated the derepressed PMN recruitment observed previously in Ido1(-/-)mice.	Kynurenine	9-20	aryl hydrocarbon receptor	Homo sapiens	62-87
27077813-2	2016	The preferred KMO substrate, kynurenine, is converted to 3-hydroxykynurenine (3HK), and this product exhibits cytotoxicity through mechanisms that culminate in apoptosis.	Kynurenine	29-39	kynurenine 3-monooxygenase	Homo sapiens	14-17
27077813-6	2016	By defining expression of pathway components upstream and downstream of KMO, we observed alterations in other key kynurenine pathway components, particularly tryptophan-2,3-dioxygenase upregulation, through bidirectional nonlinear feedback.	Kynurenine	114-124	kynurenine 3-monooxygenase	Homo sapiens	72-75
26980746-5	2016	Moreover, NZ restored the doxorubicin-induced immunogenic cell death and reversed the tumor-induced immunosuppression due to the production of kynurenine, by inhibiting the STAT3/indoleamine 2,3 dioxygenase axis.	Kynurenine	143-153	signal transducer and activator of transcription 3	Mus musculus	173-178
26508338-9	2016	Furthermore, a single peripheral kynurenine administration, the metabolic product of IDO, induced a deficit in the cognitive impairment in the sham mice.	Kynurenine	33-43	indoleamine 2,3-dioxygenase 1	Mus musculus	85-88
26508338-11	2016	In conclusion, our study implicates IDO-dependent neurotoxic kynurenine metabolism as a critical factor responsible for the sepsis-induced cognitive impairment and a potential novel target for the treatment of SAE.	Kynurenine	61-71	indoleamine 2,3-dioxygenase 1	Mus musculus	36-39
26857571-9	2016	UPEC therefore suppresses neutrophil migration early in bacterial cystitis by eliciting an IDO-mediated increase in local production of kynurenines, which act through the AHR to impair neutrophil chemotaxis.	Kynurenine	136-147	aryl hydrocarbon receptor	Homo sapiens	171-174
26841279-2	2016	Indoleamine 2,3-dioxygenase (IDO) is the enzyme that catalyzes the degradation of tryptophan into kynurenine.	Kynurenine	98-108	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-27
27023527-1	2016	Kynurenine aminotransferase II (KAT-II) is a 47 kDa pyridoxal phosphate (PLP)-dependent enzyme, active as a homodimer, which catalyses the transamination of the amino acids kynurenine (KYN) and 3-hydroxykynurenine (3-HK) in the tryptophan pathway, and is responsible for producing metabolites that lead to kynurenic acid (KYNA), which is implicated in several neurological diseases such as schizophrenia.	Kynurenine	185-188	aminoadipate aminotransferase	Homo sapiens	0-30
27023527-1	2016	Kynurenine aminotransferase II (KAT-II) is a 47 kDa pyridoxal phosphate (PLP)-dependent enzyme, active as a homodimer, which catalyses the transamination of the amino acids kynurenine (KYN) and 3-hydroxykynurenine (3-HK) in the tryptophan pathway, and is responsible for producing metabolites that lead to kynurenic acid (KYNA), which is implicated in several neurological diseases such as schizophrenia.	Kynurenine	185-188	aminoadipate aminotransferase	Homo sapiens	32-38
27023527-1	2016	Kynurenine aminotransferase II (KAT-II) is a 47 kDa pyridoxal phosphate (PLP)-dependent enzyme, active as a homodimer, which catalyses the transamination of the amino acids kynurenine (KYN) and 3-hydroxykynurenine (3-HK) in the tryptophan pathway, and is responsible for producing metabolites that lead to kynurenic acid (KYNA), which is implicated in several neurological diseases such as schizophrenia.	Kynurenine	185-188	pyridoxal phosphatase	Homo sapiens	73-76
26841279-2	2016	Indoleamine 2,3-dioxygenase (IDO) is the enzyme that catalyzes the degradation of tryptophan into kynurenine.	Kynurenine	98-108	indoleamine 2,3-dioxygenase 1	Homo sapiens	29-32
26708701-5	2016	Stimulation with prostaglandin E2 (PGE2 ) up-regulated TDO-mediated kynurenine release in human glioma cell lines, whereas knockdown of the PGE2 receptor EP4 inhibited TDO expression and activity.	Kynurenine	68-78	tryptophan 2,3-dioxygenase	Homo sapiens	55-58
26436613-7	2016	Elevated kynurenine levels in HIV/HCV patients with liver fibrosis correlated with the prognostic aspartate aminotransaminase to platelet ratio (APRI scores) and insulin levels.	Kynurenine	9-19	insulin	Homo sapiens	162-169
27375855-7	2016	Conversion of Trp to Kyn is regulated not only by TDO activity but by intracellular Trp transport via ATP-binding cassette (ABC) transporter encoded by white gene in Drosophila.	Kynurenine	21-24	vermilion	Drosophila melanogaster	50-53
26914138-1	2016	OBJECTIVES: Indoleamine 2,3-dioxygenase-1 (IDO1) is an immune-modulatory enzyme that catalyzes the degradation of tryptophan (Trp) to kynurenine (Kyn) and is strongly induced by interferon (IFN)-gamma.	Kynurenine	134-144	indoleamine 2,3-dioxygenase 1	Mus musculus	12-41
26914138-1	2016	OBJECTIVES: Indoleamine 2,3-dioxygenase-1 (IDO1) is an immune-modulatory enzyme that catalyzes the degradation of tryptophan (Trp) to kynurenine (Kyn) and is strongly induced by interferon (IFN)-gamma.	Kynurenine	146-149	indoleamine 2,3-dioxygenase 1	Mus musculus	43-47
26524415-9	2016	The results of our studies show that the kynurenine pathway is an important mediator of neuropathic pain pathology and indicate that Kmo represents a novel pharmacological target for the treatment of neuropathy.	Kynurenine	41-51	kynurenine 3-monooxygenase	Rattus norvegicus	133-136
26914138-1	2016	OBJECTIVES: Indoleamine 2,3-dioxygenase-1 (IDO1) is an immune-modulatory enzyme that catalyzes the degradation of tryptophan (Trp) to kynurenine (Kyn) and is strongly induced by interferon (IFN)-gamma.	Kynurenine	146-149	interferon gamma	Mus musculus	178-200
26914138-1	2016	OBJECTIVES: Indoleamine 2,3-dioxygenase-1 (IDO1) is an immune-modulatory enzyme that catalyzes the degradation of tryptophan (Trp) to kynurenine (Kyn) and is strongly induced by interferon (IFN)-gamma.	Kynurenine	134-144	indoleamine 2,3-dioxygenase 1	Mus musculus	43-47
26914138-1	2016	OBJECTIVES: Indoleamine 2,3-dioxygenase-1 (IDO1) is an immune-modulatory enzyme that catalyzes the degradation of tryptophan (Trp) to kynurenine (Kyn) and is strongly induced by interferon (IFN)-gamma.	Kynurenine	134-144	interferon gamma	Mus musculus	178-200
26914138-1	2016	OBJECTIVES: Indoleamine 2,3-dioxygenase-1 (IDO1) is an immune-modulatory enzyme that catalyzes the degradation of tryptophan (Trp) to kynurenine (Kyn) and is strongly induced by interferon (IFN)-gamma.	Kynurenine	146-149	indoleamine 2,3-dioxygenase 1	Mus musculus	12-41
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.	Kynurenine	82-92	indoleamine 2,3-dioxygenase 1	Homo sapiens	12-39
26646699-4	2016	Following identification of the role played by the enzyme indoleamine dioxygenase 1 (IDO1) in mediating maternal foetal tolerance, the kynurenine pathway (KP) of tryptophan metabolism has emerged as a key metabolic pathway contributing to immune escape.	Kynurenine	135-145	indoleamine 2,3-dioxygenase 1	Homo sapiens	85-89
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.	Kynurenine	82-92	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.	Kynurenine	94-97	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.	Kynurenine	94-97	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).	Kynurenine	9-12	indoleamine 2,3-dioxygenase 1	Homo sapiens	18-21
26565027-6	2016	The crystal structure of xanthurenic acid bound to the active site of SPR reveals why among all kynurenine pathway metabolites xanthurenic acid is the most potent SPR inhibitor.	Kynurenine	96-106	sepiapterin reductase	Homo sapiens	70-73
26589832-1	2016	Kynurenine monooxygenase (KMO) is an enzyme of the kynurenine (Kyn) pathway (KP), which is the major catabolic route of tryptophan.	Kynurenine	51-61	kynurenine 3-monooxygenase	Homo sapiens	0-24
26589832-1	2016	Kynurenine monooxygenase (KMO) is an enzyme of the kynurenine (Kyn) pathway (KP), which is the major catabolic route of tryptophan.	Kynurenine	51-61	kynurenine 3-monooxygenase	Homo sapiens	26-29
26589832-1	2016	Kynurenine monooxygenase (KMO) is an enzyme of the kynurenine (Kyn) pathway (KP), which is the major catabolic route of tryptophan.	Kynurenine	0-3	kynurenine 3-monooxygenase	Homo sapiens	26-29
26590946-2	2016	Previous studies have revealed that L-kynurenine (L-Kyn) level was changed significantly in patient with cancer and that miR-30b play different role in tumor cells and immune cells.	Kynurenine	36-48	microRNA 30b	Homo sapiens	121-128
26590946-2	2016	Previous studies have revealed that L-kynurenine (L-Kyn) level was changed significantly in patient with cancer and that miR-30b play different role in tumor cells and immune cells.	Kynurenine	50-55	microRNA 30b	Homo sapiens	121-128
26590946-3	2016	Moreover, it has been also conformed that miR-30b involved in the process of L-Kyn-mediated suppression of humoral immune responses induced by lipopolysaccharide (LPS) in human normal B cells separated from volunteers" peripheral blood.	Kynurenine	77-82	microRNA 30b	Homo sapiens	42-49
26590946-5	2016	The current study demonstrated that the selected concentration of L-Kyn (100, 1000 muM) significantly reduced the immunoglobulin M secretion induced by LPS when compared with the control group in B lymphoma, CH12.LX, and BCL-1 cells, which had, at least, incomplete dependence on Aryl hydrocarbon receptor, the receptor of L-Kyn.	Kynurenine	66-71	aryl-hydrocarbon receptor	Mus musculus	280-305
26590946-8	2016	These results suggest that genetic difference among cells has a great influence on the miR-30b role in the process of L-Kyn-mediated suppression of humoral immune responses induced by LPS.	Kynurenine	118-123	microRNA 30b	Mus musculus	87-94
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.	Kynurenine	83-93	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.	Kynurenine	83-93	indoleamine 2,3-dioxygenase 1	Homo sapiens	29-32
26752518-7	2016	A medicinal chemistry strategy based on modifications of the kynurenine substrate led to the discovery of the oxazolidinone GSK180 as a potent and specific inhibitor of KMO.	Kynurenine	61-71	kynurenine 3-monooxygenase	Rattus norvegicus	169-172
26651356-0	2016	Kynurenine Signaling Increases DNA Polymerase Kappa Expression and Promotes Genomic Instability in Glioblastoma Cells.	Kynurenine	0-10	DNA polymerase kappa	Homo sapiens	31-51
26651356-4	2016	Pharmacological inhibition of tryptophan-2,3-dioxygenase (TDO), the enzyme largely responsible for activating AhR in glioblastoma, led to a decrease in the endogenous AhR agonist kynurenine and a corresponding decrease in hpol kappa protein levels.	Kynurenine	179-189	tryptophan 2,3-dioxygenase	Homo sapiens	30-56
26651356-4	2016	Pharmacological inhibition of tryptophan-2,3-dioxygenase (TDO), the enzyme largely responsible for activating AhR in glioblastoma, led to a decrease in the endogenous AhR agonist kynurenine and a corresponding decrease in hpol kappa protein levels.	Kynurenine	179-189	tryptophan 2,3-dioxygenase	Homo sapiens	58-61
26651356-4	2016	Pharmacological inhibition of tryptophan-2,3-dioxygenase (TDO), the enzyme largely responsible for activating AhR in glioblastoma, led to a decrease in the endogenous AhR agonist kynurenine and a corresponding decrease in hpol kappa protein levels.	Kynurenine	179-189	aryl hydrocarbon receptor	Homo sapiens	167-170
26565027-6	2016	The crystal structure of xanthurenic acid bound to the active site of SPR reveals why among all kynurenine pathway metabolites xanthurenic acid is the most potent SPR inhibitor.	Kynurenine	96-106	sepiapterin reductase	Homo sapiens	163-166
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.	Kynurenine	157-167	indoleamine 2,3-dioxygenase 1	Homo sapiens	58-88
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.	Kynurenine	89-101	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.	Kynurenine	89-101	indoleamine 2,3-dioxygenase 1	Homo sapiens	29-32
26727596-5	2016	HCC overexpressed IDO and L-kynurenine compared to surrounding normal tissue in the DEN-treated IDO-WT mice.	Kynurenine	26-38	indoleamine 2,3-dioxygenase 1	Mus musculus	96-99
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.	Kynurenine	157-167	indoleamine 2,3-dioxygenase 1	Homo sapiens	90-93
26524378-1	2016	A key link between amino acid catabolism and immune regulation in cancer is the augmented tryptophan (Trp) catabolism through the kynurenine pathway (KP), a metabolic route induced by interferon-gamma (IFN-gamma) and related to poor prognosis in melanomas.	Kynurenine	130-140	interferon gamma	Homo sapiens	184-200
26524378-1	2016	A key link between amino acid catabolism and immune regulation in cancer is the augmented tryptophan (Trp) catabolism through the kynurenine pathway (KP), a metabolic route induced by interferon-gamma (IFN-gamma) and related to poor prognosis in melanomas.	Kynurenine	130-140	interferon gamma	Homo sapiens	202-211
26241945-13	2015	Because AMT is a substrate of indoleamine-pyrrole 2,3-dioxygenase (IDO), an enzyme that produces the immune regulatory molecule kynurenine, AMT imaging can provide novel insight of host response.	Kynurenine	128-138	indoleamine 2,3-dioxygenase 1	Mus musculus	30-65
26325330-0	2016	Kynurenine, by activating aryl hydrocarbon receptor, decreases erythropoietin and increases hepcidin production in HepG2 cells: A new mechanism for anemia of inflammation.	Kynurenine	0-10	aryl hydrocarbon receptor	Homo sapiens	26-51
26325330-0	2016	Kynurenine, by activating aryl hydrocarbon receptor, decreases erythropoietin and increases hepcidin production in HepG2 cells: A new mechanism for anemia of inflammation.	Kynurenine	0-10	erythropoietin	Homo sapiens	63-77
26325330-0	2016	Kynurenine, by activating aryl hydrocarbon receptor, decreases erythropoietin and increases hepcidin production in HepG2 cells: A new mechanism for anemia of inflammation.	Kynurenine	0-10	hepcidin antimicrobial peptide	Homo sapiens	92-100
26325330-3	2016	The effect of kynurenine, an endogenous AhR activator that increases in inflammation, on EPO and hepcidin production was evaluated.	Kynurenine	14-24	erythropoietin	Homo sapiens	89-92
26325330-3	2016	The effect of kynurenine, an endogenous AhR activator that increases in inflammation, on EPO and hepcidin production was evaluated.	Kynurenine	14-24	hepcidin antimicrobial peptide	Homo sapiens	97-105
26325330-11	2016	In conclusion, kynurenine, by competing with HIF-2alpha, may contribute to anemia of inflammation by decreasing EPO and increasing hepcidin production.	Kynurenine	15-25	erythropoietin	Homo sapiens	112-115
26325330-11	2016	In conclusion, kynurenine, by competing with HIF-2alpha, may contribute to anemia of inflammation by decreasing EPO and increasing hepcidin production.	Kynurenine	15-25	hepcidin antimicrobial peptide	Homo sapiens	131-139
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.	Kynurenine	239-249	indoleamine 2,3-dioxygenase 1	Homo sapiens	139-167
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.	Kynurenine	150-162	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.	Kynurenine	150-162	indoleamine 2,3-dioxygenase 1	Homo sapiens	61-64
26654773-3	2016	Here, we look at the role that the kynurenine pathways and associated tyrptophan catabolites (TRYCATs) play in glioma, linking this to changes in oxidative and nitrosative stress (O&amp;NS), immuneinflammatory activity, the aryl hydrocarbon receptor (AhR), and the melatoninergic pathways.	Kynurenine	35-45	aryl hydrocarbon receptor	Homo sapiens	224-249
26654773-3	2016	Here, we look at the role that the kynurenine pathways and associated tyrptophan catabolites (TRYCATs) play in glioma, linking this to changes in oxidative and nitrosative stress (O&amp;NS), immuneinflammatory activity, the aryl hydrocarbon receptor (AhR), and the melatoninergic pathways.	Kynurenine	35-45	aryl hydrocarbon receptor	Homo sapiens	251-254
26654773-4	2016	It is suggested that the interactions of O&amp;NS and the immune-inflammatory processes in glioma contribute to the induction of the TRYCATs via the kynurenine activation of the AhR, leading to increased indoleamine 2,3-dioxygenase, which deprives tryptophan for the necessary serotonin that is required as a precursor for the melatoninergic pathways.	Kynurenine	149-159	aryl hydrocarbon receptor	Homo sapiens	178-181
27563172-2	2016	The liver enzyme tryptophan 2,3-dioxygenase (TDO) provokes, by its ability to degrade tryptophan to N-formylkynurenine, the precursor of the immune-relevant kynurenines, direct and indirect antimicrobial and immunoregulatory states.	Kynurenine	157-168	tryptophan 2,3-dioxygenase	Homo sapiens	17-43
27563172-2	2016	The liver enzyme tryptophan 2,3-dioxygenase (TDO) provokes, by its ability to degrade tryptophan to N-formylkynurenine, the precursor of the immune-relevant kynurenines, direct and indirect antimicrobial and immunoregulatory states.	Kynurenine	157-168	tryptophan 2,3-dioxygenase	Homo sapiens	45-48
26241945-13	2015	Because AMT is a substrate of indoleamine-pyrrole 2,3-dioxygenase (IDO), an enzyme that produces the immune regulatory molecule kynurenine, AMT imaging can provide novel insight of host response.	Kynurenine	128-138	indoleamine 2,3-dioxygenase 1	Mus musculus	67-70
26643205-2	2015	We report here that the kynurenine metabolite, xanturenic acid (XA), interacts with, and activates mGlu2 and mGlu3 metabotropic glutamate receptors in heterologous expression systems.	Kynurenine	24-34	glutamate receptor, metabotropic 3	Mus musculus	109-114
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).	Kynurenine	226-236	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).	Kynurenine	226-236	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).	Kynurenine	226-236	indoleamine 2,3-dioxygenase 2	Homo sapiens	39-43
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).	Kynurenine	226-236	tryptophan 2,3-dioxygenase	Homo sapiens	49-76
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).	Kynurenine	226-236	tryptophan 2,3-dioxygenase	Homo sapiens	78-81
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).	Kynurenine	238-241	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).	Kynurenine	238-241	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).	Kynurenine	238-241	indoleamine 2,3-dioxygenase 2	Homo sapiens	39-43
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).	Kynurenine	238-241	tryptophan 2,3-dioxygenase	Homo sapiens	49-76
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).	Kynurenine	238-241	tryptophan 2,3-dioxygenase	Homo sapiens	78-81
26561720-5	2015	Compound 2 effectively kills hormone-dependent, cisplatin-resistant human ovarian cancer cells, inhibiting IDO by transcriptional deregulation of the autocrine-signaling loop IDO-AHR-IL6, which blocks kynurenine production and promotes T-cell proliferation.	Kynurenine	201-211	indoleamine 2,3-dioxygenase 1	Homo sapiens	175-178
26545369-5	2015	Pearson"s r correlation showed significance between the  IL-1beta and both the  CES-D score (r = 0.740, p &lt; 0.01) and the  KYN/TRP (kynurenine/tryptophan) ratio (r = 0.536, p = 0.02).	Kynurenine	126-129	interleukin 1 beta	Homo sapiens	57-65
26475400-4	2015	The pro-inflammatory cytokine IFN-gamma induces the conversion of the essential amino acid tryptophan into kynurenine via the enzyme indoleamine-2,3-dioxygenase (IDO-1).	Kynurenine	107-117	interferon gamma	Homo sapiens	30-39
26475400-4	2015	The pro-inflammatory cytokine IFN-gamma induces the conversion of the essential amino acid tryptophan into kynurenine via the enzyme indoleamine-2,3-dioxygenase (IDO-1).	Kynurenine	107-117	indoleamine 2,3-dioxygenase 1	Homo sapiens	162-167
26610689-1	2015	Indoleamine 2,3 -dioxygenase 1 (IDO1) catalyzes L-tryptophan to kynurenine in the first and rate-limiting step of tryptophan metabolism.	Kynurenine	64-74	indoleamine 2,3-dioxygenase 1	Mus musculus	0-30
26610689-1	2015	Indoleamine 2,3 -dioxygenase 1 (IDO1) catalyzes L-tryptophan to kynurenine in the first and rate-limiting step of tryptophan metabolism.	Kynurenine	64-74	indoleamine 2,3-dioxygenase 1	Mus musculus	32-36
26545369-5	2015	Pearson"s r correlation showed significance between the  IL-1beta and both the  CES-D score (r = 0.740, p &lt; 0.01) and the  KYN/TRP (kynurenine/tryptophan) ratio (r = 0.536, p = 0.02).	Kynurenine	135-145	interleukin 1 beta	Homo sapiens	57-65
26130057-4	2015	Additionally, preclinical work has demonstrated a number of mood-related depressive-like behaviors to be dependent on indoleamine 2,3-dioxygenase-1 (IDO1), the inflammation-induced rate-limiting enzyme of the kynurenine pathway.	Kynurenine	209-219	indoleamine 2,3-dioxygenase 1	Mus musculus	118-147
26173174-7	2015	Co-injection of TNF blocker etanercept with CD40AB prevented each of SBS, reduced saccharin drinking, and kynurenine pathway activation in plasma and brain.	Kynurenine	106-116	tumor necrosis factor	Mus musculus	16-19
26363006-4	2015	TNBC cells in suspension upregulated multiple genes in the kynurenine pathway of tryptophan catabolism, including the enzyme tryptophan 2,3-dioxygenase (TDO2), in an NF-kappaB-dependent manner.	Kynurenine	59-69	tryptophan 2,3-dioxygenase	Homo sapiens	125-151
26363006-4	2015	TNBC cells in suspension upregulated multiple genes in the kynurenine pathway of tryptophan catabolism, including the enzyme tryptophan 2,3-dioxygenase (TDO2), in an NF-kappaB-dependent manner.	Kynurenine	59-69	tryptophan 2,3-dioxygenase	Homo sapiens	153-157
26363006-5	2015	Kynurenine production mediated by TDO2 in TNBC cells was sufficient to activate aryl hydrocarbon receptor (AhR), an endogenous kynurenine receptor.	Kynurenine	0-10	tryptophan 2,3-dioxygenase	Homo sapiens	34-38
26363006-5	2015	Kynurenine production mediated by TDO2 in TNBC cells was sufficient to activate aryl hydrocarbon receptor (AhR), an endogenous kynurenine receptor.	Kynurenine	0-10	aryl hydrocarbon receptor	Homo sapiens	80-105
26363006-5	2015	Kynurenine production mediated by TDO2 in TNBC cells was sufficient to activate aryl hydrocarbon receptor (AhR), an endogenous kynurenine receptor.	Kynurenine	0-10	aryl hydrocarbon receptor	Homo sapiens	107-110
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.	Kynurenine	154-164	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.	Kynurenine	154-164	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.	Kynurenine	49-59	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-3
26416282-3	2015	These included IDO1 and tryptophan 2,3-dioxygenase, which catalyze the rate-limiting step in the kynurenine pathway, producing ligands for the aryl hydrocarbon receptor (AHR).	Kynurenine	97-107	aryl hydrocarbon receptor	Homo sapiens	170-173
26416282-6	2015	AHR target gene expression was further enhanced by exogenous kynurenine, and exogenous tryptophan, kynurenine, or synthetic agonist indirubin reduced mycobacterial viability.	Kynurenine	61-71	aryl hydrocarbon receptor	Homo sapiens	0-3
26416282-6	2015	AHR target gene expression was further enhanced by exogenous kynurenine, and exogenous tryptophan, kynurenine, or synthetic agonist indirubin reduced mycobacterial viability.	Kynurenine	99-109	aryl hydrocarbon receptor	Homo sapiens	0-3
26173174-9	2015	This study provides novel evidence that CD40-TNF activation induces deficits in saccharin drinking and Pavlovian fear learning and activates the kynurenine pathway, and that CD40-TNF activation of the kynurenine pathway is not necessary for induction of the acute or extended SBS effects.	Kynurenine	145-155	CD40 antigen	Mus musculus	40-44
26173174-9	2015	This study provides novel evidence that CD40-TNF activation induces deficits in saccharin drinking and Pavlovian fear learning and activates the kynurenine pathway, and that CD40-TNF activation of the kynurenine pathway is not necessary for induction of the acute or extended SBS effects.	Kynurenine	145-155	tumor necrosis factor	Mus musculus	45-48
26130057-4	2015	Additionally, preclinical work has demonstrated a number of mood-related depressive-like behaviors to be dependent on indoleamine 2,3-dioxygenase-1 (IDO1), the inflammation-induced rate-limiting enzyme of the kynurenine pathway.	Kynurenine	209-219	indoleamine 2,3-dioxygenase 1	Mus musculus	149-153
26173174-9	2015	This study provides novel evidence that CD40-TNF activation induces deficits in saccharin drinking and Pavlovian fear learning and activates the kynurenine pathway, and that CD40-TNF activation of the kynurenine pathway is not necessary for induction of the acute or extended SBS effects.	Kynurenine	145-155	tumor necrosis factor	Mus musculus	179-182
26173174-9	2015	This study provides novel evidence that CD40-TNF activation induces deficits in saccharin drinking and Pavlovian fear learning and activates the kynurenine pathway, and that CD40-TNF activation of the kynurenine pathway is not necessary for induction of the acute or extended SBS effects.	Kynurenine	201-211	CD40 antigen	Mus musculus	40-44
26130057-8	2015	A single peripheral injection of kynurenine, the metabolic product of IDO1, was sufficient to induce a deficit in recognition memory in both control and IDO null mice.	Kynurenine	33-43	indoleamine 2,3-dioxygenase 1	Mus musculus	70-74
26173174-9	2015	This study provides novel evidence that CD40-TNF activation induces deficits in saccharin drinking and Pavlovian fear learning and activates the kynurenine pathway, and that CD40-TNF activation of the kynurenine pathway is not necessary for induction of the acute or extended SBS effects.	Kynurenine	201-211	tumor necrosis factor	Mus musculus	45-48
26130057-8	2015	A single peripheral injection of kynurenine, the metabolic product of IDO1, was sufficient to induce a deficit in recognition memory in both control and IDO null mice.	Kynurenine	33-43	indoleamine 2,3-dioxygenase 1	Mus musculus	70-73
26173174-9	2015	This study provides novel evidence that CD40-TNF activation induces deficits in saccharin drinking and Pavlovian fear learning and activates the kynurenine pathway, and that CD40-TNF activation of the kynurenine pathway is not necessary for induction of the acute or extended SBS effects.	Kynurenine	201-211	CD40 antigen	Mus musculus	174-178
26173174-9	2015	This study provides novel evidence that CD40-TNF activation induces deficits in saccharin drinking and Pavlovian fear learning and activates the kynurenine pathway, and that CD40-TNF activation of the kynurenine pathway is not necessary for induction of the acute or extended SBS effects.	Kynurenine	201-211	tumor necrosis factor	Mus musculus	179-182
26130057-10	2015	These data implicate IDO-dependent neurotoxic kynurenine metabolism as a pathogenic factor for cognitive dysfunction in inflammation-induced depressive disorders and a potential novel target for the treatment of these disorders.	Kynurenine	46-56	indoleamine 2,3-dioxygenase 1	Mus musculus	21-24
26292018-1	2015	Kynurenine 3-monooxygenase (KMO), a pivotal enzyme in the kynurenine pathway, was identified as a potential therapeutic target for treating neurodegenerative and psychiatric disorders.	Kynurenine	58-68	kynurenine 3-monooxygenase	Homo sapiens	0-26
26329338-10	2015	Kynurenine concentration correlated inversely with CRP concentration in RA SF but not in OA SF (r -0.65, p &lt; 0.05).	Kynurenine	0-10	C-reactive protein	Homo sapiens	51-54
26459907-1	2016	The heme-containing enzymes indoleamine 2,3-dioxygenase-1 (IDO-1) and IDO-2 catalyze the conversion of the essential amino acid tryptophan into kynurenine.	Kynurenine	144-154	indoleamine 2,3-dioxygenase 1	Mus musculus	28-57
26459907-1	2016	The heme-containing enzymes indoleamine 2,3-dioxygenase-1 (IDO-1) and IDO-2 catalyze the conversion of the essential amino acid tryptophan into kynurenine.	Kynurenine	144-154	indoleamine 2,3-dioxygenase 1	Mus musculus	59-64
26459907-1	2016	The heme-containing enzymes indoleamine 2,3-dioxygenase-1 (IDO-1) and IDO-2 catalyze the conversion of the essential amino acid tryptophan into kynurenine.	Kynurenine	144-154	indoleamine 2,3-dioxygenase 2	Mus musculus	70-75
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.	Kynurenine	103-113	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.	Kynurenine	103-113	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.	Kynurenine	103-113	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.	Kynurenine	115-118	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.	Kynurenine	115-118	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.	Kynurenine	115-118	indoleamine 2,3-dioxygenase 1	Homo sapiens	40-43
26205824-7	2015	There was a trend for an increased kynurenine/tryptophan ratio, indicative of indoleamine 2,3-dioxygenase (IDO) activation, and increased quinolinic acid in the hippocampus.	Kynurenine	35-45	indoleamine 2,3-dioxygenase 1	Rattus norvegicus	78-105
26292018-1	2015	Kynurenine 3-monooxygenase (KMO), a pivotal enzyme in the kynurenine pathway, was identified as a potential therapeutic target for treating neurodegenerative and psychiatric disorders.	Kynurenine	58-68	kynurenine 3-monooxygenase	Homo sapiens	28-31
26489554-2	2015	IDO activity can be measured by the tryptophan (Trp)/kynurenine (Kyn) ratio.	Kynurenine	53-63	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.	Kynurenine	213-223	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.	Kynurenine	213-223	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.	Kynurenine	267-277	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-4
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.	Kynurenine	298-308	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-4
26489554-2	2015	IDO activity can be measured by the tryptophan (Trp)/kynurenine (Kyn) ratio.	Kynurenine	65-68	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.	Kynurenine	57-67	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.	Kynurenine	69-72	indoleamine 2,3-dioxygenase 1	Homo sapiens	4-7
26579577-4	2015	Herein, we report that incubation of PANC-1 cells with N(1)-acetyl-N(2)-formyl-5-methoxykynuramine (AFMK) or with L-kynurenine (L-KYN) lead to the overexpression of heat shock protein synthesis and these effects are partially reversed by 5-HT3 or MT1/MT2 receptor antagonists.	Kynurenine	114-126	heat shock protein 90 beta family member 2, pseudogene	Homo sapiens	165-183
26147366-6	2015	By assessing the level of GCN2 kinase or mammalian target of rapamycin complex 1 substrates along with a kynurenine free system we showed that IDO exerts its effect mainly through activation of GCN2 kinase.	Kynurenine	105-115	indoleamine 2,3-dioxygenase 1	Homo sapiens	143-146
26147366-6	2015	By assessing the level of GCN2 kinase or mammalian target of rapamycin complex 1 substrates along with a kynurenine free system we showed that IDO exerts its effect mainly through activation of GCN2 kinase.	Kynurenine	105-115	eukaryotic translation initiation factor 2 alpha kinase 4	Homo sapiens	194-198
25739976-0	2015	Antidepressant Effects of Exercise: A Role for the Adiponectin-PGC-1alpha-kynurenine Triad?	Kynurenine	74-84	adiponectin, C1Q and collagen domain containing	Homo sapiens	51-62
26307092-11	2015	Indoleamine 2,3-dioxygenase 1 expression and activity were measured by western blot analysis and kynurenine assay, respectively.	Kynurenine	97-107	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-29
26579577-4	2015	Herein, we report that incubation of PANC-1 cells with N(1)-acetyl-N(2)-formyl-5-methoxykynuramine (AFMK) or with L-kynurenine (L-KYN) lead to the overexpression of heat shock protein synthesis and these effects are partially reversed by 5-HT3 or MT1/MT2 receptor antagonists.	Kynurenine	128-133	heat shock protein 90 beta family member 2, pseudogene	Homo sapiens	165-183
25739976-0	2015	Antidepressant Effects of Exercise: A Role for the Adiponectin-PGC-1alpha-kynurenine Triad?	Kynurenine	74-84	PPARG coactivator 1 alpha	Homo sapiens	63-73
26579577-6	2015	Both AFMK and L-KYN significantly decreased cytoplasmic HSP27 and this effect was presumably due to increased of its phosphorylation and consequent nuclear translocation, confirmed by immunoprecipitation of phosphorylated form of HSP27.	Kynurenine	16-19	heat shock protein family B (small) member 1	Homo sapiens	56-61
26579577-6	2015	Both AFMK and L-KYN significantly decreased cytoplasmic HSP27 and this effect was presumably due to increased of its phosphorylation and consequent nuclear translocation, confirmed by immunoprecipitation of phosphorylated form of HSP27.	Kynurenine	16-19	heat shock protein family B (small) member 1	Homo sapiens	230-235
25911596-8	2015	An enhanced subcellular level of ROS by spheroidal cluster yielded the high concentrations of L-Kynurenine (1.67 +- 0.6 muM without H2O2, 5.2 +- 1.14 muM with 50 muM of H2O2 and 8.8 +- 0.51 muM with 100 muM of H2O2), supporting the IDO-mediated tryptophan replacement process.	Kynurenine	94-106	latexin	Homo sapiens	120-123
26055228-10	2015	Our results provide further support of "kynurenine hypothesis of insulin resistance and its progression to T2D" that suggested that overproduction of diabetogenic KP metabolites, induced by chronic stress or chronic low-grade inflammation, is one of the mechanisms promoting development of T2D from pre-diabetes.	Kynurenine	40-50	insulin	Homo sapiens	65-72
25911596-8	2015	An enhanced subcellular level of ROS by spheroidal cluster yielded the high concentrations of L-Kynurenine (1.67 +- 0.6 muM without H2O2, 5.2 +- 1.14 muM with 50 muM of H2O2 and 8.8 +- 0.51 muM with 100 muM of H2O2), supporting the IDO-mediated tryptophan replacement process.	Kynurenine	94-106	latexin	Homo sapiens	150-153
25911596-8	2015	An enhanced subcellular level of ROS by spheroidal cluster yielded the high concentrations of L-Kynurenine (1.67 +- 0.6 muM without H2O2, 5.2 +- 1.14 muM with 50 muM of H2O2 and 8.8 +- 0.51 muM with 100 muM of H2O2), supporting the IDO-mediated tryptophan replacement process.	Kynurenine	94-106	latexin	Homo sapiens	150-153
25911596-8	2015	An enhanced subcellular level of ROS by spheroidal cluster yielded the high concentrations of L-Kynurenine (1.67 +- 0.6 muM without H2O2, 5.2 +- 1.14 muM with 50 muM of H2O2 and 8.8 +- 0.51 muM with 100 muM of H2O2), supporting the IDO-mediated tryptophan replacement process.	Kynurenine	94-106	latexin	Homo sapiens	150-153
25911596-8	2015	An enhanced subcellular level of ROS by spheroidal cluster yielded the high concentrations of L-Kynurenine (1.67 +- 0.6 muM without H2O2, 5.2 +- 1.14 muM with 50 muM of H2O2 and 8.8 +- 0.51 muM with 100 muM of H2O2), supporting the IDO-mediated tryptophan replacement process.	Kynurenine	94-106	latexin	Homo sapiens	150-153
25911596-8	2015	An enhanced subcellular level of ROS by spheroidal cluster yielded the high concentrations of L-Kynurenine (1.67 +- 0.6 muM without H2O2, 5.2 +- 1.14 muM with 50 muM of H2O2 and 8.8 +- 0.51 muM with 100 muM of H2O2), supporting the IDO-mediated tryptophan replacement process.	Kynurenine	94-106	indoleamine 2,3-dioxygenase 1	Homo sapiens	232-235
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.	Kynurenine	137-148	indoleamine 2,3-dioxygenase 1	Homo sapiens	52-55
26002283-1	2015	BACKGROUND: Indoleamine 2,3-dioxygenase (IDO), the enzyme that catalyzes the first and rate-limiting step of tryptophan catabolism, suppresses T-cell responses by tryptophan depletion and accumulation of kynurenine metabolites.	Kynurenine	204-214	indoleamine 2,3-dioxygenase 1	Mus musculus	41-44
26013807-1	2015	L-kynurenine (Kyn) is a key element of tryptophan metabolism; it is enzymatically converted by kynurenine aminotransferase II (KAT II) to kynurenic acid (KYNA), which acts as an antagonist to the NMDA receptor-glycine site.	Kynurenine	0-12	aminoadipate aminotransferase	Mus musculus	95-125
26235422-1	2015	Indoleamine 2,3-dioxygenase 1 (Ido1) is a rate-limiting enzyme that catalizes the degradation of tryptophan along the kynurenine pathway.	Kynurenine	118-128	indoleamine 2,3-dioxygenase 1	Mus musculus	0-29
26235422-1	2015	Indoleamine 2,3-dioxygenase 1 (Ido1) is a rate-limiting enzyme that catalizes the degradation of tryptophan along the kynurenine pathway.	Kynurenine	118-128	indoleamine 2,3-dioxygenase 1	Mus musculus	31-35
26013807-1	2015	L-kynurenine (Kyn) is a key element of tryptophan metabolism; it is enzymatically converted by kynurenine aminotransferase II (KAT II) to kynurenic acid (KYNA), which acts as an antagonist to the NMDA receptor-glycine site.	Kynurenine	0-12	aminoadipate aminotransferase	Mus musculus	127-133
26243621-1	2015	Indoleamine 2,3-dioxygenase (IDO) catalyzes the rate-limiting step in the metabolism of tryptophan along the kynurenine pathway.	Kynurenine	109-119	indoleamine 2,3-dioxygenase 1	Mus musculus	0-27
26013807-1	2015	L-kynurenine (Kyn) is a key element of tryptophan metabolism; it is enzymatically converted by kynurenine aminotransferase II (KAT II) to kynurenic acid (KYNA), which acts as an antagonist to the NMDA receptor-glycine site.	Kynurenine	14-17	aminoadipate aminotransferase	Mus musculus	95-125
26013807-1	2015	L-kynurenine (Kyn) is a key element of tryptophan metabolism; it is enzymatically converted by kynurenine aminotransferase II (KAT II) to kynurenic acid (KYNA), which acts as an antagonist to the NMDA receptor-glycine site.	Kynurenine	14-17	aminoadipate aminotransferase	Mus musculus	127-133
26243621-1	2015	Indoleamine 2,3-dioxygenase (IDO) catalyzes the rate-limiting step in the metabolism of tryptophan along the kynurenine pathway.	Kynurenine	109-119	indoleamine 2,3-dioxygenase 1	Mus musculus	29-32
26013807-2	2015	Kyn is also an endogenous ligand of the aryl hydrocarbon receptor (AhR), a transcription factor that regulates the expression of a diverse set of genes.	Kynurenine	0-3	aryl-hydrocarbon receptor	Mus musculus	40-65
26013807-2	2015	Kyn is also an endogenous ligand of the aryl hydrocarbon receptor (AhR), a transcription factor that regulates the expression of a diverse set of genes.	Kynurenine	0-3	aryl-hydrocarbon receptor	Mus musculus	67-70
26033215-1	2015	Indoleamine 2,3-dioxygenase (IDO), an enzyme that degrades the essential amino acid l-tryptophan along the kynurenine pathway, exerts immunomodulatory effects in a number of diseases.	Kynurenine	107-117	indoleamine 2,3-dioxygenase 1	Mus musculus	0-27
26318674-5	2015	l-Kynurenine (10 muM-1 mM) induced concentration-dependent relaxation in rat aortas and mesenteric arteries as well as human omental arteries, whereas linopirdine abolished the relaxation.	Kynurenine	0-12	latexin	Homo sapiens	17-20
26318674-6	2015	l-Kynurenine (1 mM) produced hyperpolarization of vascular smooth muscle, which was reversed by linopirdine (10 muM).	Kynurenine	0-12	latexin	Homo sapiens	112-115
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.	Kynurenine	123-133	indoleamine 2,3-dioxygenase 1	Homo sapiens	34-61
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.	Kynurenine	123-133	indoleamine 2,3-dioxygenase 1	Homo sapiens	63-66
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.	Kynurenine	176-186	indoleamine 2,3-dioxygenase 1	Homo sapiens	34-61
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.	Kynurenine	176-186	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.	Kynurenine	135-145	indoleamine 2,3-dioxygenase 1	Homo sapiens	10-13
26285873-12	2015	Patients" kynurenine pathway metabolites correlated with the levels of inflammatory markers, including that of the major IDO-inducer, interferon-gamma.	Kynurenine	10-20	indoleamine 2,3-dioxygenase 1	Homo sapiens	121-124
26285873-12	2015	Patients" kynurenine pathway metabolites correlated with the levels of inflammatory markers, including that of the major IDO-inducer, interferon-gamma.	Kynurenine	10-20	interferon gamma	Homo sapiens	134-150
26033215-1	2015	Indoleamine 2,3-dioxygenase (IDO), an enzyme that degrades the essential amino acid l-tryptophan along the kynurenine pathway, exerts immunomodulatory effects in a number of diseases.	Kynurenine	107-117	indoleamine 2,3-dioxygenase 1	Mus musculus	29-32
26232788-4	2015	METHODS: We hypothesized that BDNF(+/-) mice would be more susceptible to stress-induced neuroinflammation and kynurenine metabolism, so BDNF(+/-) or wild-type littermate mice were subject to repeated unpredictable mild stress.	Kynurenine	111-121	brain derived neurotrophic factor	Mus musculus	30-34
26232788-8	2015	In BDNF(+/-) mice, kynurenine was metabolized preferentially to the neurotoxic intermediate 3-hydroxykynurenine following repeated unpredictable mild stress.	Kynurenine	19-29	brain derived neurotrophic factor	Mus musculus	3-7
26232788-9	2015	CONCLUSIONS: Our data suggest that BDNF may modulate kynurenine pathway metabolism during stress and provide a novel molecular mechanism of vulnerability and resilience to the development of stress-precipitated psychiatric disorders.	Kynurenine	53-63	brain derived neurotrophic factor	Mus musculus	35-39
25950090-1	2015	Indoleamine 2,3-dioxygenase (IDO) is a Trp-degrading enzyme that catalyzes the first step in the kynurenine pathway.	Kynurenine	97-107	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-27
25637715-7	2015	Our data demonstrate that amino acid oxides (in particular kynurenine) inhibited BMMSC proliferation, alkaline phosphatase expression and activity and the expression of osteogenic markers (Osteocalcin and Runx2).	Kynurenine	59-69	bone gamma-carboxyglutamate protein 2	Mus musculus	189-200
25637715-7	2015	Our data demonstrate that amino acid oxides (in particular kynurenine) inhibited BMMSC proliferation, alkaline phosphatase expression and activity and the expression of osteogenic markers (Osteocalcin and Runx2).	Kynurenine	59-69	runt related transcription factor 2	Mus musculus	205-210
26122290-8	2015	This study demonstrated that ACTH administration increased serum corticosterone levels, KYN, 5-HIAA levels, IDO activity (hippocampus), immobility in the forced swimming test (FST) and the latency to feed in the novelty suppressed feeding test (NSFT).	Kynurenine	88-91	pro-opiomelanocortin-alpha	Mus musculus	29-33
25903543-7	2015	Alternatively, expression of these YUCCA genes was upregulated by the auxin biosynthetic inhibitor kynurenine in Arabidopsis seedlings, accompanied by reduced IAA levels.	Kynurenine	99-109	Flavin-binding monooxygenase family protein	Arabidopsis thaliana	35-40
25728366-4	2015	Induced by inflammatory stimuli, IDO catabolizes tryptophan to kynurenine (KYN), which is subsequently converted into neuroactive metabolites.	Kynurenine	63-73	indoleamine 2,3-dioxygenase 1	Homo sapiens	33-36
25728366-4	2015	Induced by inflammatory stimuli, IDO catabolizes tryptophan to kynurenine (KYN), which is subsequently converted into neuroactive metabolites.	Kynurenine	75-78	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.	Kynurenine	97-107	indoleamine 2,3-dioxygenase 1	Homo sapiens	29-32
25519303-4	2015	The primary function of IDO1 is associated with conversion of the essential amino acid, tryptophan, into downstream catabolites known as kynurenines.	Kynurenine	137-148	indoleamine 2,3-dioxygenase 1	Homo sapiens	24-28
26299865-1	2015	Indoleamine 2,3-dioxygenase 1 (Ido1) is a rate-limiting enzyme which converts the essential amino acid tryptophan to kynurenine.	Kynurenine	117-127	indoleamine 2,3-dioxygenase 1	Mus musculus	0-29
26299865-1	2015	Indoleamine 2,3-dioxygenase 1 (Ido1) is a rate-limiting enzyme which converts the essential amino acid tryptophan to kynurenine.	Kynurenine	117-127	indoleamine 2,3-dioxygenase 1	Mus musculus	31-35
25519303-5	2015	The depletion of tryptophan and/or accumulation of kynurenine has been shown to induce T cell deactivation, apoptosis and/or the induction of immunosuppressive programming via the expression of FoxP3.	Kynurenine	51-61	forkhead box P3	Homo sapiens	194-199
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.	Kynurenine	101-111	indoleamine 2,3-dioxygenase 1	Homo sapiens	9-38
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.	Kynurenine	106-116	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.	Kynurenine	106-116	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.	Kynurenine	118-121	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.	Kynurenine	118-121	indoleamine 2,3-dioxygenase 1	Homo sapiens	63-66
25850816-5	2015	We define the pathway of kynurenine induced aryl hydrocarbon receptor activation in MSCs and how it contributes to the upregulation of COX2 expression and IL-6 downregulation.	Kynurenine	25-35	prostaglandin-endoperoxide synthase 2	Mus musculus	135-139
25850816-5	2015	We define the pathway of kynurenine induced aryl hydrocarbon receptor activation in MSCs and how it contributes to the upregulation of COX2 expression and IL-6 downregulation.	Kynurenine	25-35	interleukin 6	Mus musculus	155-159
26114426-6	2015	In contrast, peripheral monocytes showed a significant elevation of kynurenine pathway enzymes and metabolites when treated with interferon gamma.	Kynurenine	68-78	interferon gamma	Homo sapiens	129-145
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.	Kynurenine	82-92	indoleamine 2,3-dioxygenase 1	Homo sapiens	14-19
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.	Kynurenine	82-92	kynurenine 3-monooxygenase	Homo sapiens	21-24
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.	Kynurenine	82-92	quinolinate phosphoribosyltransferase	Homo sapiens	29-33
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.	Kynurenine	102-112	indoleamine 2,3-dioxygenase 1	Homo sapiens	14-19
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.	Kynurenine	102-112	kynurenine 3-monooxygenase	Homo sapiens	21-24
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.	Kynurenine	102-112	quinolinate phosphoribosyltransferase	Homo sapiens	29-33
26099564-1	2015	Kynurenine 3-monooxygenase (KMO) is a pivotal enzyme in the kynurenine pathway of tryptophan degradation and plays a critical role in Huntington"s and Alzheimer"s diseases.	Kynurenine	60-70	kynurenine 3-monooxygenase	Homo sapiens	0-26
26099564-1	2015	Kynurenine 3-monooxygenase (KMO) is a pivotal enzyme in the kynurenine pathway of tryptophan degradation and plays a critical role in Huntington"s and Alzheimer"s diseases.	Kynurenine	60-70	kynurenine 3-monooxygenase	Homo sapiens	28-31
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.	Kynurenine	101-111	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.	Kynurenine	101-111	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.	Kynurenine	113-116	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.	Kynurenine	113-116	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.	Kynurenine	113-116	indoleamine 2,3-dioxygenase 1	Homo sapiens	40-43
25890721-3	2015	These cytokines also induce indoleamine 2,3-dioxygenase (IDO1) activity; this is the rate-limiting and first enzyme in the l-tryptophan (TRP)-l-kynurenine (KYN) pathway.	Kynurenine	156-159	indoleamine 2,3-dioxygenase 1	Mus musculus	57-61
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.	Kynurenine	137-147	indoleamine 2,3-dioxygenase 1	Homo sapiens	98-102
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.	Kynurenine	80-90	indoleamine 2,3-dioxygenase 1	Homo sapiens	17-21
25890721-3	2015	These cytokines also induce indoleamine 2,3-dioxygenase (IDO1) activity; this is the rate-limiting and first enzyme in the l-tryptophan (TRP)-l-kynurenine (KYN) pathway.	Kynurenine	142-154	indoleamine 2,3-dioxygenase 1	Mus musculus	57-61
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).	Kynurenine	14-24	tryptophan 2,3-dioxygenase	Homo sapiens	89-115
25934804-6	2015	Consistent with this prediction, PPARbeta/delta agonists enhanced macrophage survival under hypoxic stress and stimulated CD8(+) T cell activation, concomitantly with the repression of immune suppressive target genes and their encoded products CD274 (PD-1 ligand), CD32B (inhibitory Fcgamma receptor IIB) and indoleamine 2,3-dioxygenase 1 (IDO-1), as well as a diminished release of the immune suppressive IDO-1 metabolite kynurenine.	Kynurenine	423-433	peroxisome proliferator activated receptor delta	Homo sapiens	33-41
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.	Kynurenine	175-185	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.	Kynurenine	175-185	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.	Kynurenine	175-185	indoleamine 2,3-dioxygenase 1	Homo sapiens	253-257
25961549-3	2015	In other cell types, it is catalyzed by an alternative inducible indoleamine-pyrrole 2, 3-dioxygenase (IDO) under certain pathophysiological conditions, which consequently increases the formation of Kyn metabolites.	Kynurenine	199-202	indoleamine 2,3-dioxygenase 1	Homo sapiens	65-101
25961549-3	2015	In other cell types, it is catalyzed by an alternative inducible indoleamine-pyrrole 2, 3-dioxygenase (IDO) under certain pathophysiological conditions, which consequently increases the formation of Kyn metabolites.	Kynurenine	199-202	indoleamine 2,3-dioxygenase 1	Homo sapiens	103-106
26041992-3	2015	However, alternative routes, including KYNA formation from D-kynurenine (D-KYN) by D-amino acid oxidase (DAAO) and the direct transformation of kynurenine to KYNA by reactive oxygen species (ROS), have been demonstrated in the rat brain.	Kynurenine	61-71	D-amino-acid oxidase	Rattus norvegicus	83-103
25750192-2	2015	Strong evidence implicates indoleamine 2,3-dioxygenase (IDO), the first and rate-limiting enzyme of the kynurenine pathway of tryptophan (Trp) degradation, with immune regulation and anti-inflammatory mechanisms in different diseases.	Kynurenine	104-114	indoleamine 2,3-dioxygenase 1	Mus musculus	27-54
25750192-2	2015	Strong evidence implicates indoleamine 2,3-dioxygenase (IDO), the first and rate-limiting enzyme of the kynurenine pathway of tryptophan (Trp) degradation, with immune regulation and anti-inflammatory mechanisms in different diseases.	Kynurenine	104-114	indoleamine 2,3-dioxygenase 1	Mus musculus	56-59
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).	Kynurenine	14-24	tryptophan 2,3-dioxygenase	Homo sapiens	117-120
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).	Kynurenine	14-24	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).	Kynurenine	14-24	indoleamine 2,3-dioxygenase 1	Homo sapiens	154-158
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).	Kynurenine	14-24	indoleamine 2,3-dioxygenase 2	Homo sapiens	165-194
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).	Kynurenine	14-24	indoleamine 2,3-dioxygenase 2	Homo sapiens	196-200
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.	Kynurenine	173-185	indoleamine 2,3-dioxygenase 1	Homo sapiens	74-82
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).	Kynurenine	47-57	indoleamine 2,3-dioxygenase 1	Homo sapiens	169-172
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.	Kynurenine	173-185	tryptophan 2,3-dioxygenase	Homo sapiens	87-115
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.	Kynurenine	173-185	tryptophan 2,3-dioxygenase	Homo sapiens	117-121
25881064-6	2015	We developed a monoclonal antibody targeting l-kynurenine as an in situ biomarker of IDO-1/-2 or TDO2 activity.	Kynurenine	45-57	indoleamine 2,3-dioxygenase 1	Homo sapiens	85-93
25881064-6	2015	We developed a monoclonal antibody targeting l-kynurenine as an in situ biomarker of IDO-1/-2 or TDO2 activity.	Kynurenine	45-57	tryptophan 2,3-dioxygenase	Homo sapiens	97-101
25712221-1	2015	A cytokine-inducible extrahepatic human indoleamine 2,3-dioxygenase (hIDO1) catalyzes the first step of the kynurenine pathway.	Kynurenine	108-118	indoleamine 2,3-dioxygenase 1	Homo sapiens	69-74
26035167-8	2015	In addition to the activation of the kynurenine pathway by HIV proteins Tat and Nef, the tryptophan-degrading bacteria present in the intestinal flora have been associated with dysfunction of gut mucosal CD4 Th17/Th22 cells, leading to microbial translocation and creating a systemic kynurenine pathway activation cycle.	Kynurenine	37-47	S100 calcium binding protein B	Homo sapiens	80-83
26035167-8	2015	In addition to the activation of the kynurenine pathway by HIV proteins Tat and Nef, the tryptophan-degrading bacteria present in the intestinal flora have been associated with dysfunction of gut mucosal CD4 Th17/Th22 cells, leading to microbial translocation and creating a systemic kynurenine pathway activation cycle.	Kynurenine	284-294	S100 calcium binding protein B	Homo sapiens	80-83
26035167-8	2015	In addition to the activation of the kynurenine pathway by HIV proteins Tat and Nef, the tryptophan-degrading bacteria present in the intestinal flora have been associated with dysfunction of gut mucosal CD4 Th17/Th22 cells, leading to microbial translocation and creating a systemic kynurenine pathway activation cycle.	Kynurenine	284-294	CD4 molecule	Homo sapiens	204-207
25554565-1	2015	Two kynurenine metabolites, 3-hydroxykynurenine and 3-hydroxyanthranilic acid, are known to inhibit melanin polymer formation in in vitro reactions catalyzed by tyrosinase.	Kynurenine	4-14	tyrosinase	Homo sapiens	161-171
25639711-8	2015	RESULTS: Patients with above average AUDIT scores had higher mean serum levels of kynurenine (2.1 muM +- 0.7 vs. 1.8 muM +- 0.6, p = 0.006) and KT ratios (48.6 +- 17.6 vs. 40.4 +- 14.3, p = 0.002) than those with below average scores.	Kynurenine	82-92	latexin	Homo sapiens	98-101
25639711-8	2015	RESULTS: Patients with above average AUDIT scores had higher mean serum levels of kynurenine (2.1 muM +- 0.7 vs. 1.8 muM +- 0.6, p = 0.006) and KT ratios (48.6 +- 17.6 vs. 40.4 +- 14.3, p = 0.002) than those with below average scores.	Kynurenine	82-92	latexin	Homo sapiens	117-120
25596911-8	2015	Antidepressants have an anti-inflammatory effect, including reduction of interferon-gamma and therefore inhibition of IDO, the rate-limiting enzyme of the kynurenine pathway.	Kynurenine	155-165	indoleamine 2,3-dioxygenase 1	Homo sapiens	118-121
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.	Kynurenine	185-195	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.	Kynurenine	185-195	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.	Kynurenine	185-195	tryptophan 2,3-dioxygenase	Homo sapiens	38-64
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.	Kynurenine	185-195	tryptophan 2,3-dioxygenase	Homo sapiens	66-69
25455350-0	2015	Increased levels of IL-6 in the cerebrospinal fluid of patients with chronic schizophrenia--significance for activation of the kynurenine pathway.	Kynurenine	127-137	interleukin 6	Homo sapiens	20-24
25949879-2	2015	IDO degrades the essential amino acid tryptophan leading to immunosuppressive kynurenines production.	Kynurenine	78-89	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-3
25450809-8	2015	Since kynurenine, the catabolic end product of IDO1, is a signaling molecule as an agonist for the aryl hydrocarbon receptor (AhR), we examined if AhR signaling induces the tryptophan-selective transporter.	Kynurenine	6-16	indoleamine 2,3-dioxygenase 1	Mus musculus	47-51
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.	Kynurenine	100-111	indoleamine 2,3-dioxygenase 1	Homo sapiens	17-21
25450809-8	2015	Since kynurenine, the catabolic end product of IDO1, is a signaling molecule as an agonist for the aryl hydrocarbon receptor (AhR), we examined if AhR signaling induces the tryptophan-selective transporter.	Kynurenine	6-16	aryl-hydrocarbon receptor	Mus musculus	99-124
25450809-10	2015	The present studies demonstrate that IFN-gamma coordinately induces IDO1 and a tryptophan-selective transporter to maximize tryptophan depletion in IDO1-expressing cells and that the process involves a positive feedback mechanism via kynurenine-AhR signaling.	Kynurenine	234-244	interferon gamma	Mus musculus	37-46
25450809-8	2015	Since kynurenine, the catabolic end product of IDO1, is a signaling molecule as an agonist for the aryl hydrocarbon receptor (AhR), we examined if AhR signaling induces the tryptophan-selective transporter.	Kynurenine	6-16	aryl-hydrocarbon receptor	Mus musculus	126-129
25450809-10	2015	The present studies demonstrate that IFN-gamma coordinately induces IDO1 and a tryptophan-selective transporter to maximize tryptophan depletion in IDO1-expressing cells and that the process involves a positive feedback mechanism via kynurenine-AhR signaling.	Kynurenine	234-244	indoleamine 2,3-dioxygenase 1	Mus musculus	68-72
25450809-10	2015	The present studies demonstrate that IFN-gamma coordinately induces IDO1 and a tryptophan-selective transporter to maximize tryptophan depletion in IDO1-expressing cells and that the process involves a positive feedback mechanism via kynurenine-AhR signaling.	Kynurenine	234-244	indoleamine 2,3-dioxygenase 1	Mus musculus	148-152
25450809-10	2015	The present studies demonstrate that IFN-gamma coordinately induces IDO1 and a tryptophan-selective transporter to maximize tryptophan depletion in IDO1-expressing cells and that the process involves a positive feedback mechanism via kynurenine-AhR signaling.	Kynurenine	234-244	aryl-hydrocarbon receptor	Mus musculus	245-248
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.	Kynurenine	133-143	indoleamine 2,3-dioxygenase 1	Homo sapiens	29-33
25149761-2	2015	Interleukin 17A (IL-17A) is considered an important component in host defense against Candida infections and is modulated by Candida-induced impairment of tryptophan-kynurenine metabolism.	Kynurenine	166-176	interleukin 17A	Homo sapiens	0-15
25149761-2	2015	Interleukin 17A (IL-17A) is considered an important component in host defense against Candida infections and is modulated by Candida-induced impairment of tryptophan-kynurenine metabolism.	Kynurenine	166-176	interleukin 17A	Homo sapiens	17-23
25149761-8	2015	The statistically significant association between IL-17A and kynurenine levels and candidemia suggests their potential as biomarkers for anticipation of invasive candidiasis.	Kynurenine	61-71	interleukin 17A	Homo sapiens	50-56
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.	Kynurenine	119-129	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.	Kynurenine	131-134	indoleamine 2,3-dioxygenase 1	Homo sapiens	84-87
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.	Kynurenine	91-101	indoleamine 2,3-dioxygenase 1	Homo sapiens	29-32
25544757-8	2015	Kynurenine synthesis was due to the transcription of the indoleamine 1,2 dioxygenase (IDO) enzyme, consequent to the activation of the signal transducer and activator of transcription-3 (STAT3).	Kynurenine	0-10	indoleamine 2,3-dioxygenase 1	Homo sapiens	57-84
25544757-8	2015	Kynurenine synthesis was due to the transcription of the indoleamine 1,2 dioxygenase (IDO) enzyme, consequent to the activation of the signal transducer and activator of transcription-3 (STAT3).	Kynurenine	0-10	indoleamine 2,3-dioxygenase 1	Homo sapiens	86-89
25544757-8	2015	Kynurenine synthesis was due to the transcription of the indoleamine 1,2 dioxygenase (IDO) enzyme, consequent to the activation of the signal transducer and activator of transcription-3 (STAT3).	Kynurenine	0-10	signal transducer and activator of transcription 3	Homo sapiens	135-185
25544757-8	2015	Kynurenine synthesis was due to the transcription of the indoleamine 1,2 dioxygenase (IDO) enzyme, consequent to the activation of the signal transducer and activator of transcription-3 (STAT3).	Kynurenine	0-10	signal transducer and activator of transcription 3	Homo sapiens	187-192
25392945-1	2015	Human alpha-amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase determines the fate of tryptophan metabolites in the kynurenine pathway by controlling the quinolinate levels for de novo nicotinamide adenine dinucleotide biosynthesis.	Kynurenine	127-137	aminocarboxymuconate semialdehyde decarboxylase	Homo sapiens	6-73
25628622-4	2014	In the past years, there has been an increase in our understanding of the regulation and downstream mediators of TRP metabolism, such as the aryl hydrocarbon receptor as a receptor for KYN and kynurenic acid.	Kynurenine	185-188	aryl hydrocarbon receptor	Homo sapiens	141-166
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.	Kynurenine	126-136	indoleamine 2,3-dioxygenase 1	Homo sapiens	52-79
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.	Kynurenine	126-136	indoleamine 2,3-dioxygenase 1	Homo sapiens	81-84
25686005-1	2015	Indoleamine 2,3-dioxygenase (IDO, subsequently named IDO1) can degrade the level of essential amino acid tryptophan in mammals, and catalyze the initial and rate-limiting step through the kynurenine pathway.	Kynurenine	188-198	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-27
25686005-1	2015	Indoleamine 2,3-dioxygenase (IDO, subsequently named IDO1) can degrade the level of essential amino acid tryptophan in mammals, and catalyze the initial and rate-limiting step through the kynurenine pathway.	Kynurenine	188-198	indoleamine 2,3-dioxygenase 1	Homo sapiens	29-32
25686005-1	2015	Indoleamine 2,3-dioxygenase (IDO, subsequently named IDO1) can degrade the level of essential amino acid tryptophan in mammals, and catalyze the initial and rate-limiting step through the kynurenine pathway.	Kynurenine	188-198	indoleamine 2,3-dioxygenase 1	Homo sapiens	53-57
25079795-1	2015	Indoleamine 2,3-dioxygenase (IDO), the first and rate-limiting enzyme in the kynurenine pathway (KP) of tryptophan catabolism, was recently established as one of the potential players involved in the pathogenesis of Alzheimer"s disease (AD).	Kynurenine	77-87	indoleamine 2,3-dioxygenase 1	Mus musculus	0-27
25079795-1	2015	Indoleamine 2,3-dioxygenase (IDO), the first and rate-limiting enzyme in the kynurenine pathway (KP) of tryptophan catabolism, was recently established as one of the potential players involved in the pathogenesis of Alzheimer"s disease (AD).	Kynurenine	77-87	indoleamine 2,3-dioxygenase 1	Mus musculus	29-32
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.	Kynurenine	86-96	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.	Kynurenine	86-96	indoleamine 2,3-dioxygenase 1	Homo sapiens	29-32
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).	Kynurenine	72-82	indoleamine 2,3-dioxygenase 1	Homo sapiens	123-126
25815345-8	2015	PGE2-mediated expression of IDO1 results in the production of kynurenine, in the generation of Tregs, and in the inhibition of either the allogeneic or the autologous antigen-specific stimulatory capacity of DCs.	Kynurenine	62-72	indoleamine 2,3-dioxygenase 1	Homo sapiens	28-32
26366134-0	2015	Comprehensive metabolome analyses reveal N-acetylcysteine-responsive accumulation of kynurenine in systemic lupus erythematosus: implications for activation of the mechanistic target of rapamycin.	Kynurenine	85-95	mechanistic target of rapamycin kinase	Homo sapiens	164-195
26366134-10	2015	Kynurenine stimulated mTOR activity in healthy control PBL in vitro.	Kynurenine	0-10	mechanistic target of rapamycin kinase	Homo sapiens	22-26
26366134-12	2015	The PPP-connected and NAC-responsive accumulation of kynurenine and its stimulation of mTOR are identified as novel metabolic checkpoints in lupus pathogenesis.	Kynurenine	53-63	mechanistic target of rapamycin kinase	Homo sapiens	87-91
25532592-0	2015	Effects of kynurenine on CD3+ and macrophages in wound healing.	Kynurenine	11-21	CD3 antigen, epsilon polypeptide	Mus musculus	25-28
25186311-2	2015	Using microarray expression analysis, we found that IFNgamma upregulates a set of genes associated with a tryptophan degradation pathway, known as the kynurenine pathway, in osteogenic differentiating human mesenchymal stem cells (hMSC).	Kynurenine	151-161	interferon gamma	Homo sapiens	52-60
25186311-2	2015	Using microarray expression analysis, we found that IFNgamma upregulates a set of genes associated with a tryptophan degradation pathway, known as the kynurenine pathway, in osteogenic differentiating human mesenchymal stem cells (hMSC).	Kynurenine	151-161	musculin	Homo sapiens	231-235
25186311-5	2015	We next blocked indoleamine 2,3-dioxygenase-1 (IDO1), the most important enzyme in the kynurenine pathway, using a siRNA and pharmacological approach and observed a strong inhibition of osteoblastogenesis with a concomitant decrease in osteogenic factors.	Kynurenine	87-97	indoleamine 2,3-dioxygenase 1	Mus musculus	16-45
25186311-5	2015	We next blocked indoleamine 2,3-dioxygenase-1 (IDO1), the most important enzyme in the kynurenine pathway, using a siRNA and pharmacological approach and observed a strong inhibition of osteoblastogenesis with a concomitant decrease in osteogenic factors.	Kynurenine	87-97	indoleamine 2,3-dioxygenase 1	Mus musculus	47-51
25186311-8	2015	Finally, we tested whether the end products of the kynurenine pathway have an osteogenic effect on hMSC.	Kynurenine	51-61	musculin	Homo sapiens	99-103
25186311-10	2015	In summary, we demonstrate that the activation of the kynurenine pathway plays an important role during the commitment of hMSC into the osteoblast lineage in vitro, and that this process can be accelerated by exogenous addition of IFNgamma.	Kynurenine	54-64	musculin	Homo sapiens	122-126
25186311-10	2015	In summary, we demonstrate that the activation of the kynurenine pathway plays an important role during the commitment of hMSC into the osteoblast lineage in vitro, and that this process can be accelerated by exogenous addition of IFNgamma.	Kynurenine	54-64	interferon gamma	Mus musculus	231-239
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.	Kynurenine	165-175	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.	Kynurenine	165-175	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).	Kynurenine	59-69	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-4
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).	Kynurenine	119-129	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).	Kynurenine	119-129	indoleamine 2,3-dioxygenase 1	Homo sapiens	31-35
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).	Kynurenine	231-243	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).	Kynurenine	231-243	indoleamine 2,3-dioxygenase 1	Homo sapiens	31-35
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).	Kynurenine	245-248	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).	Kynurenine	245-248	indoleamine 2,3-dioxygenase 1	Homo sapiens	31-35
25453901-3	2014	URI inhibits aryl hydrocarbon (AhR)- and estrogen receptor (ER)-mediated transcription of enzymes implicated in L-tryptophan/kynurenine/nicotinamide adenine dinucleotide (NAD(+)) metabolism, thereby causing DNA damage at early stages of tumorigenesis.	Kynurenine	125-135	URI1 prefoldin like chaperone	Homo sapiens	0-3
25453901-3	2014	URI inhibits aryl hydrocarbon (AhR)- and estrogen receptor (ER)-mediated transcription of enzymes implicated in L-tryptophan/kynurenine/nicotinamide adenine dinucleotide (NAD(+)) metabolism, thereby causing DNA damage at early stages of tumorigenesis.	Kynurenine	125-135	aryl hydrocarbon receptor	Homo sapiens	31-34
25453901-3	2014	URI inhibits aryl hydrocarbon (AhR)- and estrogen receptor (ER)-mediated transcription of enzymes implicated in L-tryptophan/kynurenine/nicotinamide adenine dinucleotide (NAD(+)) metabolism, thereby causing DNA damage at early stages of tumorigenesis.	Kynurenine	125-135	estrogen receptor 1	Homo sapiens	41-58
25453901-3	2014	URI inhibits aryl hydrocarbon (AhR)- and estrogen receptor (ER)-mediated transcription of enzymes implicated in L-tryptophan/kynurenine/nicotinamide adenine dinucleotide (NAD(+)) metabolism, thereby causing DNA damage at early stages of tumorigenesis.	Kynurenine	125-135	estrogen receptor 1	Homo sapiens	60-62
25386651-5	2014	We here show that UVB illumination of the extracellular domain of EGFR (sEGFR) induces protein conformational changes, disulphide bridge breakage and formation of tryptophan and tyrosine photoproducts such as dityrosine, N-formylkynurenine and kynurenine.	Kynurenine	229-239	epidermal growth factor receptor	Homo sapiens	66-70
25359166-7	2014	Finally, we have also found that L-kynurenine, a tryptophan metabolite with AhR agonistic properties, is an endogenous ligand that mediates AhR activation in the brain after middle cerebral artery occlusion.	Kynurenine	33-45	aryl hydrocarbon receptor	Rattus norvegicus	76-79
25359166-7	2014	Finally, we have also found that L-kynurenine, a tryptophan metabolite with AhR agonistic properties, is an endogenous ligand that mediates AhR activation in the brain after middle cerebral artery occlusion.	Kynurenine	33-45	aryl hydrocarbon receptor	Rattus norvegicus	140-143
25464917-4	2014	KMO encodes kynurenine 3-monooxygenase (KMO), the rate-limiting microglial enzyme of cortical kynurenine metabolism.	Kynurenine	12-22	kynurenine 3-monooxygenase	Homo sapiens	0-3
25464917-4	2014	KMO encodes kynurenine 3-monooxygenase (KMO), the rate-limiting microglial enzyme of cortical kynurenine metabolism.	Kynurenine	12-22	kynurenine 3-monooxygenase	Homo sapiens	40-43
25477879-4	2014	Gene expression studies indicate that IDO2 is a basally and more narrowly expressed gene than IDO1 and that IDO2 is uniquely regulated by AhR, which serves as a physiological receptor for the tryptophan catabolite kynurenine.	Kynurenine	214-224	indoleamine 2,3-dioxygenase 2	Homo sapiens	38-42
25477879-4	2014	Gene expression studies indicate that IDO2 is a basally and more narrowly expressed gene than IDO1 and that IDO2 is uniquely regulated by AhR, which serves as a physiological receptor for the tryptophan catabolite kynurenine.	Kynurenine	214-224	indoleamine 2,3-dioxygenase 2	Homo sapiens	108-112
25477879-4	2014	Gene expression studies indicate that IDO2 is a basally and more narrowly expressed gene than IDO1 and that IDO2 is uniquely regulated by AhR, which serves as a physiological receptor for the tryptophan catabolite kynurenine.	Kynurenine	214-224	aryl hydrocarbon receptor	Homo sapiens	138-141
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).	Kynurenine	285-296	indoleamine 2,3-dioxygenase 1	Homo sapiens	117-146
25114116-4	2014	Ido expression in the peritoneal CD11b(+) cells and its metabolite l-kynurenine in the serum were increased after <protein-id="10978">CLP.	Kynurenine	67-79	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-3
25368620-4	2014	Moreover, AHR and IDO/TDO are closely interconnected: AHR regulates IDO and TDO expression, and kynurenine produced by IDO/TDO is an AHR agonist.	Kynurenine	96-106	aryl hydrocarbon receptor	Homo sapiens	10-13
25368620-4	2014	Moreover, AHR and IDO/TDO are closely interconnected: AHR regulates IDO and TDO expression, and kynurenine produced by IDO/TDO is an AHR agonist.	Kynurenine	96-106	indoleamine 2,3-dioxygenase 1	Homo sapiens	18-21
25368620-4	2014	Moreover, AHR and IDO/TDO are closely interconnected: AHR regulates IDO and TDO expression, and kynurenine produced by IDO/TDO is an AHR agonist.	Kynurenine	96-106	tryptophan 2,3-dioxygenase	Homo sapiens	22-25
24974860-2	2014	Tryptophan 2,3-dioxygenase (TDO) enhances immune tolerance by catabolizing tryptophan to kynurenine.	Kynurenine	89-99	tryptophan 2,3-dioxygenase	Homo sapiens	0-26
24974860-2	2014	Tryptophan 2,3-dioxygenase (TDO) enhances immune tolerance by catabolizing tryptophan to kynurenine.	Kynurenine	89-99	tryptophan 2,3-dioxygenase	Homo sapiens	28-31
24974860-13	2014	IL-1beta-treated ESCs increased the production of kynurenine and the effect was inhibited by TDO siRNA.	Kynurenine	50-60	interleukin 1 beta	Homo sapiens	0-8
24974860-13	2014	IL-1beta-treated ESCs increased the production of kynurenine and the effect was inhibited by TDO siRNA.	Kynurenine	50-60	tryptophan 2,3-dioxygenase	Homo sapiens	93-96
25066466-6	2014	IFN-alpha stimulates indoleamine-2,3 dioxygenase-1, activating the kynurenine pathway with reduced formation of the neurotransmitters serotonin and dopamine, excessive formation of the NMDA agonist quinolinic acid, and reduced formation of the NMDA antagonist kynurenic acid.	Kynurenine	67-77	interferon alpha 1	Homo sapiens	0-9
25066466-6	2014	IFN-alpha stimulates indoleamine-2,3 dioxygenase-1, activating the kynurenine pathway with reduced formation of the neurotransmitters serotonin and dopamine, excessive formation of the NMDA agonist quinolinic acid, and reduced formation of the NMDA antagonist kynurenic acid.	Kynurenine	67-77	indoleamine 2,3-dioxygenase 1	Homo sapiens	21-50
25066423-1	2014	Tryptophan 2,3-dioxygenase (TDO), one of the two key enzymes in the kynurenine pathway, catalyzes the indole ring cleavage at the C2-C3 bond of L-tryptophan.	Kynurenine	68-78	tryptophan 2,3-dioxygenase	Homo sapiens	0-26
25066423-1	2014	Tryptophan 2,3-dioxygenase (TDO), one of the two key enzymes in the kynurenine pathway, catalyzes the indole ring cleavage at the C2-C3 bond of L-tryptophan.	Kynurenine	68-78	tryptophan 2,3-dioxygenase	Homo sapiens	28-31
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.	Kynurenine	103-113	indoleamine 2,3-dioxygenase 1	Homo sapiens	13-16
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.	Kynurenine	103-113	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).	Kynurenine	285-296	indoleamine 2,3-dioxygenase 1	Homo sapiens	148-152
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.	Kynurenine	183-195	aryl hydrocarbon receptor	Homo sapiens	41-66
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.	Kynurenine	183-195	aryl hydrocarbon receptor	Homo sapiens	68-71
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.	Kynurenine	183-195	indoleamine 2,3-dioxygenase 1	Homo sapiens	88-92
24878170-0	2014	Effect of maternal immune activation on the kynurenine pathway in preadolescent rat offspring and on MK801-induced hyperlocomotion in adulthood: amelioration by COX-2 inhibition.	Kynurenine	44-54	cytochrome c oxidase II, mitochondrial	Rattus norvegicus	161-166
25105221-0	2014	Vitamins B2 and B6 as determinants of kynurenines and related markers of interferon-gamma-mediated immune activation in the community-based Hordaland Health Study.	Kynurenine	38-49	immunoglobulin kappa variable 5-2	Homo sapiens	9-18
25105221-1	2014	Vitamins B2 and B6 are cofactors in the kynurenine pathway.	Kynurenine	40-50	immunoglobulin kappa variable 5-2	Homo sapiens	9-18
25105221-3	2014	In the present study, we aimed to investigate plasma concentrations of vitamins B2 and B6 as determinants of kynurenines and two markers of interferon-gamma-mediated immune activation (kynurenine:tryptophan ratio (KTR) and neopterin).	Kynurenine	109-120	immunoglobulin kappa variable 5-2	Homo sapiens	80-89
25105221-3	2014	In the present study, we aimed to investigate plasma concentrations of vitamins B2 and B6 as determinants of kynurenines and two markers of interferon-gamma-mediated immune activation (kynurenine:tryptophan ratio (KTR) and neopterin).	Kynurenine	109-119	immunoglobulin kappa variable 5-2	Homo sapiens	80-89
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).	Kynurenine	196-206	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).	Kynurenine	196-206	indoleamine 2,3-dioxygenase 1	Homo sapiens	29-32
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).	Kynurenine	196-206	tryptophan 2,3-dioxygenase	Homo sapiens	38-64
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).	Kynurenine	196-206	tryptophan 2,3-dioxygenase	Homo sapiens	66-69
25324842-5	2014	Kynurenine, a tryptophan breakdown product, is one such endogenous ligand of the AHR.	Kynurenine	0-10	aryl-hydrocarbon receptor	Mus musculus	81-84
25215657-2	2014	We have recently demonstrated that IDO1 does not merely degrade tryptophan and produce immunoregulatory kynurenines, but it also acts as a signal-transducing molecule, independently of its enzymic function.	Kynurenine	104-115	indoleamine 2,3-dioxygenase 1	Mus musculus	35-39
25060701-2	2014	A report by Puccetti and coworkers describes a regulatory pathway by which L-kynurenine (L-Kyn) produced by tryptophan 2,3-dioxygenase 2 (TDO2) activates AhR in cells of the innate immune system to limit endotoxin-triggered inflammation through a mechanism that involves the non-enzymatic anti-inflammatory activities of indoleamine 2,3-dioxygenase 1 (IDO1).	Kynurenine	75-87	tryptophan 2,3-dioxygenase	Homo sapiens	108-136
25060701-2	2014	A report by Puccetti and coworkers describes a regulatory pathway by which L-kynurenine (L-Kyn) produced by tryptophan 2,3-dioxygenase 2 (TDO2) activates AhR in cells of the innate immune system to limit endotoxin-triggered inflammation through a mechanism that involves the non-enzymatic anti-inflammatory activities of indoleamine 2,3-dioxygenase 1 (IDO1).	Kynurenine	75-87	tryptophan 2,3-dioxygenase	Homo sapiens	138-142
25060701-2	2014	A report by Puccetti and coworkers describes a regulatory pathway by which L-kynurenine (L-Kyn) produced by tryptophan 2,3-dioxygenase 2 (TDO2) activates AhR in cells of the innate immune system to limit endotoxin-triggered inflammation through a mechanism that involves the non-enzymatic anti-inflammatory activities of indoleamine 2,3-dioxygenase 1 (IDO1).	Kynurenine	75-87	aryl hydrocarbon receptor	Homo sapiens	154-157
25060701-2	2014	A report by Puccetti and coworkers describes a regulatory pathway by which L-kynurenine (L-Kyn) produced by tryptophan 2,3-dioxygenase 2 (TDO2) activates AhR in cells of the innate immune system to limit endotoxin-triggered inflammation through a mechanism that involves the non-enzymatic anti-inflammatory activities of indoleamine 2,3-dioxygenase 1 (IDO1).	Kynurenine	75-87	indoleamine 2,3-dioxygenase 1	Homo sapiens	321-350
25060701-2	2014	A report by Puccetti and coworkers describes a regulatory pathway by which L-kynurenine (L-Kyn) produced by tryptophan 2,3-dioxygenase 2 (TDO2) activates AhR in cells of the innate immune system to limit endotoxin-triggered inflammation through a mechanism that involves the non-enzymatic anti-inflammatory activities of indoleamine 2,3-dioxygenase 1 (IDO1).	Kynurenine	75-87	indoleamine 2,3-dioxygenase 1	Homo sapiens	352-356
25060701-2	2014	A report by Puccetti and coworkers describes a regulatory pathway by which L-kynurenine (L-Kyn) produced by tryptophan 2,3-dioxygenase 2 (TDO2) activates AhR in cells of the innate immune system to limit endotoxin-triggered inflammation through a mechanism that involves the non-enzymatic anti-inflammatory activities of indoleamine 2,3-dioxygenase 1 (IDO1).	Kynurenine	89-94	tryptophan 2,3-dioxygenase	Homo sapiens	108-136
25060701-2	2014	A report by Puccetti and coworkers describes a regulatory pathway by which L-kynurenine (L-Kyn) produced by tryptophan 2,3-dioxygenase 2 (TDO2) activates AhR in cells of the innate immune system to limit endotoxin-triggered inflammation through a mechanism that involves the non-enzymatic anti-inflammatory activities of indoleamine 2,3-dioxygenase 1 (IDO1).	Kynurenine	89-94	tryptophan 2,3-dioxygenase	Homo sapiens	138-142
25060701-2	2014	A report by Puccetti and coworkers describes a regulatory pathway by which L-kynurenine (L-Kyn) produced by tryptophan 2,3-dioxygenase 2 (TDO2) activates AhR in cells of the innate immune system to limit endotoxin-triggered inflammation through a mechanism that involves the non-enzymatic anti-inflammatory activities of indoleamine 2,3-dioxygenase 1 (IDO1).	Kynurenine	89-94	aryl hydrocarbon receptor	Homo sapiens	154-157
25060701-2	2014	A report by Puccetti and coworkers describes a regulatory pathway by which L-kynurenine (L-Kyn) produced by tryptophan 2,3-dioxygenase 2 (TDO2) activates AhR in cells of the innate immune system to limit endotoxin-triggered inflammation through a mechanism that involves the non-enzymatic anti-inflammatory activities of indoleamine 2,3-dioxygenase 1 (IDO1).	Kynurenine	89-94	indoleamine 2,3-dioxygenase 1	Homo sapiens	321-350
25060701-2	2014	A report by Puccetti and coworkers describes a regulatory pathway by which L-kynurenine (L-Kyn) produced by tryptophan 2,3-dioxygenase 2 (TDO2) activates AhR in cells of the innate immune system to limit endotoxin-triggered inflammation through a mechanism that involves the non-enzymatic anti-inflammatory activities of indoleamine 2,3-dioxygenase 1 (IDO1).	Kynurenine	89-94	indoleamine 2,3-dioxygenase 1	Homo sapiens	352-356
24919418-4	2014	This upregulation was associated with reduced L-tryptophan levels and increased L-kynurenine levels in serum, indicating that IFN-gamma gene transfer increased the IDO activity.	Kynurenine	80-92	interferon gamma	Mus musculus	126-135
25335725-2	2014	IDO activity can be determined using the tryptophan/kynurenine(Trp/Kyn)ratio.	Kynurenine	52-62	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-3
25335725-2	2014	IDO activity can be determined using the tryptophan/kynurenine(Trp/Kyn)ratio.	Kynurenine	67-70	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-3
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.	Kynurenine	208-218	indoleamine 2,3-dioxygenase 2	Homo sapiens	0-29
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.	Kynurenine	208-218	indoleamine 2,3-dioxygenase 2	Homo sapiens	31-35
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.	Kynurenine	208-218	indoleamine 2,3-dioxygenase 1	Homo sapiens	132-136
24768802-0	2014	Kynurenine production mediated by indoleamine 2,3-dioxygenase aggravates liver injury in HBV-specific CTL-induced fulminant hepatitis.	Kynurenine	0-10	indoleamine 2,3-dioxygenase 1	Homo sapiens	34-61
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.	Kynurenine	145-155	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.	Kynurenine	145-155	indoleamine 2,3-dioxygenase 1	Homo sapiens	41-44
24768802-7	2014	The administration of kynurenine aggravated the liver injury in HBV-Tg/IDO-KO mice injected with HBV-specific CTL.	Kynurenine	22-32	indoleamine 2,3-dioxygenase 1	Mus musculus	71-74
24768802-8	2014	Simultaneous injection of recombinant murine interferon (IFN-gamma) and kynurenine also increased the ALT levels in HBV-Tg/IDO-KO mice.	Kynurenine	72-82	glutamic pyruvic transaminase, soluble	Mus musculus	102-105
24768802-8	2014	Simultaneous injection of recombinant murine interferon (IFN-gamma) and kynurenine also increased the ALT levels in HBV-Tg/IDO-KO mice.	Kynurenine	72-82	indoleamine 2,3-dioxygenase 1	Mus musculus	123-126
24919418-4	2014	This upregulation was associated with reduced L-tryptophan levels and increased L-kynurenine levels in serum, indicating that IFN-gamma gene transfer increased the IDO activity.	Kynurenine	80-92	indoleamine 2,3-dioxygenase 1	Mus musculus	164-167
25091696-9	2014	Kynurenine levels were correlated with the expression of tryptophan-degrading enzyme (IDO1).	Kynurenine	0-10	indoleamine 2,3-dioxygenase 1	Homo sapiens	86-90
24844751-4	2014	We now have investigated the roles of two kynurenine pathway enzymes, indoleamine dioxygenase-1 (IDO1) and tryptophan dioxygenase-2 (TDO2), in the pathomechanisms of pneumococcal meningitis.	Kynurenine	42-52	indoleamine 2,3-dioxygenase 1	Mus musculus	70-95
24844751-4	2014	We now have investigated the roles of two kynurenine pathway enzymes, indoleamine dioxygenase-1 (IDO1) and tryptophan dioxygenase-2 (TDO2), in the pathomechanisms of pneumococcal meningitis.	Kynurenine	42-52	indoleamine 2,3-dioxygenase 1	Mus musculus	97-101
25060643-7	2014	RESULTS: Kynurenine, the metabolite generated by IDO, increases in the supernatant of fibroblasts co-cultured with COX-2-overexpressing breast cancer cells.	Kynurenine	9-19	indoleamine 2,3-dioxygenase 1	Homo sapiens	49-52
24817202-1	2014	UNLABELLED: The cytokine interferon gamma (IFN-gamma) stimulates neopterin release and tryptophan degradation into kynurenines through the kynurenine pathway.	Kynurenine	115-126	interferon gamma	Homo sapiens	25-52
24817202-1	2014	UNLABELLED: The cytokine interferon gamma (IFN-gamma) stimulates neopterin release and tryptophan degradation into kynurenines through the kynurenine pathway.	Kynurenine	115-125	interferon gamma	Homo sapiens	25-52
24817202-4	2014	Interferon gamma (IFN-gamma) initiates macrophage release of neopterin and also stimulates degradation of tryptophan along the kynurenine pathway as part of cell-mediated immune activation.	Kynurenine	127-137	interferon gamma	Homo sapiens	0-16
24817202-4	2014	Interferon gamma (IFN-gamma) initiates macrophage release of neopterin and also stimulates degradation of tryptophan along the kynurenine pathway as part of cell-mediated immune activation.	Kynurenine	127-137	interferon gamma	Homo sapiens	18-27
24817202-5	2014	Plasma neopterin and the kynurenine/tryptophan ratio (KTR) are thus markers of IFN-gamma-mediated inflammation.	Kynurenine	25-35	interferon gamma	Homo sapiens	79-88
24585899-0	2014	The kynurenine pathway of tryptophan catabolism, CD4+ T-cell recovery, and mortality among HIV-infected Ugandans initiating antiretroviral therapy.	Kynurenine	4-14	CD4 molecule	Homo sapiens	49-52
24585899-9	2014	CONCLUSIONS: The kynurenine pathway of tryptophan catabolism independently predicts poor CD4(+) T-cell count recovery and increased mortality among HIV-infected Ugandans initiating ART and may be an important target for interventions.	Kynurenine	17-27	CD4 molecule	Homo sapiens	89-92
25060643-7	2014	RESULTS: Kynurenine, the metabolite generated by IDO, increases in the supernatant of fibroblasts co-cultured with COX-2-overexpressing breast cancer cells.	Kynurenine	9-19	prostaglandin-endoperoxide synthase 2	Homo sapiens	115-120
25060643-9	2014	Conversely, fibroblast-secreted kynurenine promotes the formation of the E-cadherin/Aryl hydrocarbon receptor (AhR)/S-phase kinase-associated protein 2 (Skp2) complex, resulting in degradation of E-cadherin to increase breast cancer invasiveness.	Kynurenine	32-42	cadherin 1	Homo sapiens	73-83
25060643-9	2014	Conversely, fibroblast-secreted kynurenine promotes the formation of the E-cadherin/Aryl hydrocarbon receptor (AhR)/S-phase kinase-associated protein 2 (Skp2) complex, resulting in degradation of E-cadherin to increase breast cancer invasiveness.	Kynurenine	32-42	aryl hydrocarbon receptor	Homo sapiens	84-109
25060643-9	2014	Conversely, fibroblast-secreted kynurenine promotes the formation of the E-cadherin/Aryl hydrocarbon receptor (AhR)/S-phase kinase-associated protein 2 (Skp2) complex, resulting in degradation of E-cadherin to increase breast cancer invasiveness.	Kynurenine	32-42	aryl hydrocarbon receptor	Homo sapiens	111-114
25060643-9	2014	Conversely, fibroblast-secreted kynurenine promotes the formation of the E-cadherin/Aryl hydrocarbon receptor (AhR)/S-phase kinase-associated protein 2 (Skp2) complex, resulting in degradation of E-cadherin to increase breast cancer invasiveness.	Kynurenine	32-42	S-phase kinase associated protein 2	Homo sapiens	116-151
25060643-9	2014	Conversely, fibroblast-secreted kynurenine promotes the formation of the E-cadherin/Aryl hydrocarbon receptor (AhR)/S-phase kinase-associated protein 2 (Skp2) complex, resulting in degradation of E-cadherin to increase breast cancer invasiveness.	Kynurenine	32-42	S-phase kinase associated protein 2	Homo sapiens	153-157
25060643-9	2014	Conversely, fibroblast-secreted kynurenine promotes the formation of the E-cadherin/Aryl hydrocarbon receptor (AhR)/S-phase kinase-associated protein 2 (Skp2) complex, resulting in degradation of E-cadherin to increase breast cancer invasiveness.	Kynurenine	32-42	cadherin 1	Homo sapiens	196-206
24647121-8	2014	Furthermore, the KAT II inhibitor significantly reversed l-kynurenine-induced elevations of brain KYNA levels.	Kynurenine	57-69	aminoadipate aminotransferase	Rattus norvegicus	17-23
24935925-6	2014	We further demonstrated the ability of kynurenine to induce apoptosis in bone marrow-derived neutrophils, whereas the presence of tryptophan reversed this effect, providing a possible mechanism for the increased neutrophil accumulation in IDO1(-/-) mice.	Kynurenine	39-49	indoleamine 2,3-dioxygenase 1	Mus musculus	239-243
24368565-4	2014	Most prominent mouse genes induced during the onset of asexual and sexual growth of parasite comprise interferon gamma (IFNgamma)-regulated factors, e.g., immunity-related GTPases (IRGA6/B6/D/M2/M3), guanylate-binding proteins (GBP2/3/5/6/8), chemokines (CxCL9-11), and several enzymes of the kynurenine pathway including indoleamine 2,3-dioxygenase 1 (IDO1).	Kynurenine	293-303	interferon gamma	Mus musculus	120-128
24368565-4	2014	Most prominent mouse genes induced during the onset of asexual and sexual growth of parasite comprise interferon gamma (IFNgamma)-regulated factors, e.g., immunity-related GTPases (IRGA6/B6/D/M2/M3), guanylate-binding proteins (GBP2/3/5/6/8), chemokines (CxCL9-11), and several enzymes of the kynurenine pathway including indoleamine 2,3-dioxygenase 1 (IDO1).	Kynurenine	293-303	interferon inducible GTPase 1	Mus musculus	181-186
24647121-3	2014	Reducing KYNA levels by administering inhibitors of enzymes of the kynurenine pathway, particularly kynurenine aminotransferase II (KAT II), has been proposed as a treatment for such cognitive impairments.	Kynurenine	67-77	aminoadipate aminotransferase	Rattus norvegicus	100-130
24472498-2	2014	TDO drives tryptophan metabolism via the kynurenine pathway (KP) and leads to the production of neuroactive metabolites including kynurenine.	Kynurenine	41-51	tryptophan 2,3-dioxygenase	Rattus norvegicus	0-3
24647121-3	2014	Reducing KYNA levels by administering inhibitors of enzymes of the kynurenine pathway, particularly kynurenine aminotransferase II (KAT II), has been proposed as a treatment for such cognitive impairments.	Kynurenine	67-77	aminoadipate aminotransferase	Rattus norvegicus	132-138
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.	Kynurenine	129-139	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.	Kynurenine	129-139	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).	Kynurenine	64-74	indoleamine 2,3-dioxygenase 1	Homo sapiens	30-33
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.	Kynurenine	0-11	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.	Kynurenine	0-11	indoleamine 2,3-dioxygenase 1	Homo sapiens	93-96
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.	Kynurenine	107-117	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.	Kynurenine	107-117	indoleamine 2,3-dioxygenase 1	Homo sapiens	93-96
24798334-10	2014	A similar formation of AGEs was observed in UVA-irradiated lenses from human IDO/human sodium-dependent vitamin C transporter-2 mice, which contain high levels of kynurenines and ASC.	Kynurenine	163-174	indoleamine 2,3-dioxygenase 1	Homo sapiens	77-80
24798334-10	2014	A similar formation of AGEs was observed in UVA-irradiated lenses from human IDO/human sodium-dependent vitamin C transporter-2 mice, which contain high levels of kynurenines and ASC.	Kynurenine	163-174	solute carrier family 23 member 2	Homo sapiens	87-127
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.	Kynurenine	97-107	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.	Kynurenine	97-107	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.	Kynurenine	109-112	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.	Kynurenine	109-112	indoleamine 2,3-dioxygenase 1	Homo sapiens	165-168
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.	Kynurenine	220-230	interferon gamma	Homo sapiens	36-58
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.	Kynurenine	220-230	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.	Kynurenine	220-230	indoleamine 2,3-dioxygenase 1	Homo sapiens	161-164
24528145-3	2014	Plasma levels of neopterin and the kynurenine/tryptophan ratio (KTR) are thus markers of IFN-gamma-mediated inflammation.	Kynurenine	35-45	interferon gamma	Homo sapiens	89-98
24528145-5	2014	The aim of this study was to investigate associations between markers of IFN-gamma-mediated inflammation and kynurenines with bone mineral density (BMD).	Kynurenine	109-120	interferon gamma	Homo sapiens	73-82
24472498-2	2014	TDO drives tryptophan metabolism via the kynurenine pathway (KP) and leads to the production of neuroactive metabolites including kynurenine.	Kynurenine	130-140	tryptophan 2,3-dioxygenase	Rattus norvegicus	0-3
24472498-6	2014	Increased TDO activity was associated with raised circulating kynurenine concentrations and a reduction in circulating tryptophan concentrations indicative of KP activation.	Kynurenine	62-72	tryptophan 2,3-dioxygenase	Rattus norvegicus	10-13
24976763-4	2014	Along with elevation in serum and hippocampal TNF-alpha and corticosterone levels associated with significant increase in hippocampal kynurenine/tryptophan ratio.	Kynurenine	134-144	tumor necrosis factor	Rattus norvegicus	46-55
24976763-7	2014	It is concluded that increased tryptophan metabolism toward kynurenine secondary to elevated corticosterone and TNF-alpha might be one of the pathohphysiological mechanisms that could explain depression like state observed in this rat model.	Kynurenine	60-70	tumor necrosis factor	Rattus norvegicus	112-121
24976763-8	2014	Further, the observed attenuating effect of HP on TNF-alpha and corticosterone could contribute in its antidepressant effect in this animal model by other ways than their effects on tryptophan-kynurenine metabolism pathway.	Kynurenine	193-203	tumor necrosis factor	Rattus norvegicus	50-59
24904580-1	2014	This review discusses the mechanisms and consequences of degradation of tryptophan (Trp) in the placenta, focusing mainly on the role of indoleamine 2,3-dioxygenase-1 (IDO1), one of three enzymes catalyzing the first step of the kynurenine pathway of Trp degradation.	Kynurenine	229-239	indoleamine 2,3-dioxygenase 1	Mus musculus	137-166
24905525-10	2014	The therapeutic potential of KYN in ALF appears to be fostered by increased expression of KAT-II in astrocytes upon exposure to KYN or Trp.	Kynurenine	29-32	aminoadipate aminotransferase	Rattus norvegicus	90-96
26455230-5	2014	The biological activity of IDO in supernatant was detected by measuring the amount of kynurenine generation.	Kynurenine	86-96	indoleamine 2,3-dioxygenase 1	Rattus norvegicus	27-30
26455230-11	2014	IDO-BMSCs could significantly improved kynurenine concentration in culture medium supernatant when compared with GFP-BMSCs (P &lt; 0.05).	Kynurenine	39-49	indoleamine 2,3-dioxygenase 1	Rattus norvegicus	0-3
24904580-1	2014	This review discusses the mechanisms and consequences of degradation of tryptophan (Trp) in the placenta, focusing mainly on the role of indoleamine 2,3-dioxygenase-1 (IDO1), one of three enzymes catalyzing the first step of the kynurenine pathway of Trp degradation.	Kynurenine	229-239	indoleamine 2,3-dioxygenase 1	Mus musculus	168-172
23940074-0	2014	The IDO1-induced kynurenines play a major role in the antimicrobial effect of human myeloid cells against Listeria monocytogenes.	Kynurenine	17-28	indoleamine 2,3-dioxygenase 1	Homo sapiens	4-8
24517146-1	2014	CONTEXT: Indoleamine 2,3-dioxygenase 1 (IDO1) is a single chain oxidoreductase that catalyzes tryptophan degradation to kynurenine.	Kynurenine	120-130	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.	Kynurenine	120-130	indoleamine 2,3-dioxygenase 1	Homo sapiens	40-44
24517146-10	2014	IDO1 was expressed in human thyroid cancer cell lines in vitro, and FTC-133 cells showed high kynurenine concentration in the conditioned medium and a strong suppressive action on the proliferation of activated lymphocytes in coculture experiments.	Kynurenine	94-104	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-4
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.	Kynurenine	113-123	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-29
24483723-1	2014	Immune cells utilize the IDO enzymatic conversion of trp to kyn to determine T-cell activation vs. anergy/apoptosis.	Kynurenine	60-63	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.	Kynurenine	70-73	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.	Kynurenine	113-123	interferon gamma	Homo sapiens	43-65
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.	Kynurenine	113-123	indoleamine 2,3-dioxygenase 1	Homo sapiens	31-35
24530381-1	2014	Indoleamine 2,3-dioxygenase1 (IDO1) is the rate-limiting enzyme in the kynurenine pathway that converts l-tryptophan to l-kynurenine.	Kynurenine	71-81	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.	Kynurenine	71-81	indoleamine 2,3-dioxygenase 1	Homo sapiens	30-34
24530381-1	2014	Indoleamine 2,3-dioxygenase1 (IDO1) is the rate-limiting enzyme in the kynurenine pathway that converts l-tryptophan to l-kynurenine.	Kynurenine	120-132	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.	Kynurenine	120-132	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.	Kynurenine	136-146	indoleamine 2,3-dioxygenase 1	Homo sapiens	159-185
24381207-1	2014	Kynurenine 3-monooxygenase (KMO) is a therapeutically important target on the eukaryotic tryptophan catabolic pathway, where it converts L-kynurenine (Kyn) to 3-hydroxykynurenine (3-HK).	Kynurenine	137-149	kynurenine 3-monooxygenase	Homo sapiens	0-26
24381207-1	2014	Kynurenine 3-monooxygenase (KMO) is a therapeutically important target on the eukaryotic tryptophan catabolic pathway, where it converts L-kynurenine (Kyn) to 3-hydroxykynurenine (3-HK).	Kynurenine	137-149	kynurenine 3-monooxygenase	Homo sapiens	28-31
24381207-1	2014	Kynurenine 3-monooxygenase (KMO) is a therapeutically important target on the eukaryotic tryptophan catabolic pathway, where it converts L-kynurenine (Kyn) to 3-hydroxykynurenine (3-HK).	Kynurenine	0-3	kynurenine 3-monooxygenase	Homo sapiens	28-31
24397465-0	2014	A tryptophan metabolite, kynurenine, promotes mast cell activation through aryl hydrocarbon receptor.	Kynurenine	25-35	aryl-hydrocarbon receptor	Mus musculus	75-100
24397465-6	2014	RESULTS: Kynurenine, but not KA and QA, enhanced IgE-mediated responses, including degranulation, LTC4 release, and IL-13 production in BMMCs through the activation of PLCgamma1, Akt, MAPK p38, and the increase of intracellular calcium.	Kynurenine	9-19	interleukin 13	Mus musculus	116-121
24397465-6	2014	RESULTS: Kynurenine, but not KA and QA, enhanced IgE-mediated responses, including degranulation, LTC4 release, and IL-13 production in BMMCs through the activation of PLCgamma1, Akt, MAPK p38, and the increase of intracellular calcium.	Kynurenine	9-19	phospholipase C, gamma 1	Mus musculus	168-177
24397465-6	2014	RESULTS: Kynurenine, but not KA and QA, enhanced IgE-mediated responses, including degranulation, LTC4 release, and IL-13 production in BMMCs through the activation of PLCgamma1, Akt, MAPK p38, and the increase of intracellular calcium.	Kynurenine	9-19	thymoma viral proto-oncogene 1	Mus musculus	179-182
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.	Kynurenine	136-146	indoleamine 2,3-dioxygenase 1	Homo sapiens	187-190
23877570-4	2014	Consistent with this finding, kynurenine (Kyn) treatment markedly increased the levels of MMP-1 and MMP-3 expression through activation of the MEK (mitogen-activated protein kinase (MAPK)/extracellular signal-regulated kinase (ERK) kinase)-ERK1/2 MAPK signaling pathway.	Kynurenine	30-40	interstitial collagenase	Oryctolagus cuniculus	90-95
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.	Kynurenine	52-62	indoleamine 2,3-dioxygenase 1	Rattus norvegicus	20-24
24370834-8	2014	Moreover, IFN-gamma strongly upregulates MHC-II molecules and IDO activity in HCEC as reflected by high kynurenine (Kyn) concentrations.	Kynurenine	104-114	interferon gamma	Homo sapiens	10-19
24370834-8	2014	Moreover, IFN-gamma strongly upregulates MHC-II molecules and IDO activity in HCEC as reflected by high kynurenine (Kyn) concentrations.	Kynurenine	116-119	interferon gamma	Homo sapiens	10-19
23877570-4	2014	Consistent with this finding, kynurenine (Kyn) treatment markedly increased the levels of MMP-1 and MMP-3 expression through activation of the MEK (mitogen-activated protein kinase (MAPK)/extracellular signal-regulated kinase (ERK) kinase)-ERK1/2 MAPK signaling pathway.	Kynurenine	30-40	stromelysin-1	Oryctolagus cuniculus	100-105
23877570-4	2014	Consistent with this finding, kynurenine (Kyn) treatment markedly increased the levels of MMP-1 and MMP-3 expression through activation of the MEK (mitogen-activated protein kinase (MAPK)/extracellular signal-regulated kinase (ERK) kinase)-ERK1/2 MAPK signaling pathway.	Kynurenine	42-45	interstitial collagenase	Oryctolagus cuniculus	90-95
23877570-4	2014	Consistent with this finding, kynurenine (Kyn) treatment markedly increased the levels of MMP-1 and MMP-3 expression through activation of the MEK (mitogen-activated protein kinase (MAPK)/extracellular signal-regulated kinase (ERK) kinase)-ERK1/2 MAPK signaling pathway.	Kynurenine	42-45	stromelysin-1	Oryctolagus cuniculus	100-105
24316190-1	2014	Kynurenine 3-monooxygenase (KMO) is an enzyme central to the kynurenine pathway of tryptophan metabolism.	Kynurenine	61-71	kynurenine 3-monooxygenase	Homo sapiens	0-26
24361737-0	2014	Early modulation of the transcription factor Nrf2 in rodent striatal slices by quinolinic acid, a toxic metabolite of the kynurenine pathway.	Kynurenine	122-132	nuclear factor, erythroid derived 2, like 2	Mus musculus	45-49
24361737-3	2014	In this study, we investigated the early profile of Nrf2 modulation in striatal slices of rodents incubated in the presence of the toxic kynurenine pathway metabolite, quinolinic acid (QUIN).	Kynurenine	137-147	nuclear factor, erythroid derived 2, like 2	Mus musculus	52-56
24038671-2	2014	This puts QPRT at the junction of two different pathways, that is, de novo NAD(+) biosynthesis and the kynurenine pathway of tryptophan degradation.	Kynurenine	103-113	quinolinate phosphoribosyltransferase	Homo sapiens	10-14
24657910-5	2014	Inhibition of IL-6 or STAT3 using siRNA and/or pharmacological inhibitors reduced IDO mRNA and protein expression as well as kynurenine formation.	Kynurenine	125-135	interleukin 6	Homo sapiens	14-18
24657910-5	2014	Inhibition of IL-6 or STAT3 using siRNA and/or pharmacological inhibitors reduced IDO mRNA and protein expression as well as kynurenine formation.	Kynurenine	125-135	signal transducer and activator of transcription 3	Homo sapiens	22-27
24316190-1	2014	Kynurenine 3-monooxygenase (KMO) is an enzyme central to the kynurenine pathway of tryptophan metabolism.	Kynurenine	61-71	kynurenine 3-monooxygenase	Homo sapiens	28-31
24200862-8	2014	The external aldimine of kynurenine and PLP is then deprotonated by the epsilon-amino group of Lys-227 to give a quinonoid intermediate, which is reprotonated at C-4" to give a ketimine.	Kynurenine	25-35	complement C4A (Rodgers blood group)	Homo sapiens	162-165
24200862-14	2014	Halogenation of kynurenine at C-5 increases activity with both enzymes, but halogenation at C-3 only increases activity for human kynureninase.	Kynurenine	16-26	complement C5	Homo sapiens	30-33
24533148-6	2014	Galanal attenuated L-kynurenine formation with an IC50 value of 7.7 microM in the assay system using recombinant human IDO1, and an IC50 value of 45 nM in the cell-based assay.	Kynurenine	19-31	indoleamine 2,3-dioxygenase 1	Homo sapiens	119-123
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.	Kynurenine	242-252	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.	Kynurenine	242-252	indoleamine 2,3-dioxygenase 1	Homo sapiens	182-186
24485475-4	2014	Based on the strong association between depressive-like behavior and cytokine-induced brain activation of indoleamine 2,3-dioxygenase (IDO), the enzyme that metabolizes tryptophan along the kynurenine pathway, these results may suggest an impairment of brain IDO activation in db/db mice.	Kynurenine	190-200	indoleamine 2,3-dioxygenase 1	Mus musculus	106-133
24299123-9	2014	Yucasin combined with the TAA1 inhibitor l-kynurenine acted additively in Arabidopsis seedlings, producing a phenotype similar to yucasin-treated sav3-2 seedlings, indicating the importance of IAA biosynthesis via the IPyA pathway in root growth and leaf vascular development.	Kynurenine	41-53	tryptophan aminotransferase of Arabidopsis 1	Arabidopsis thaliana	26-30
24485475-4	2014	Based on the strong association between depressive-like behavior and cytokine-induced brain activation of indoleamine 2,3-dioxygenase (IDO), the enzyme that metabolizes tryptophan along the kynurenine pathway, these results may suggest an impairment of brain IDO activation in db/db mice.	Kynurenine	190-200	indoleamine 2,3-dioxygenase 1	Mus musculus	135-138
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).	Kynurenine	122-132	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-27
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.	Kynurenine	216-226	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.	Kynurenine	216-226	indoleamine 2,3-dioxygenase 1	Homo sapiens	121-124
24281189-5	2014	As expected, AngII increased plasma levels of Kyn- and 3-hydroxykynurenine-modified proteins in endothelial cells in vivo.	Kynurenine	46-49	angiotensinogen (serpin peptidase inhibitor, clade A, member 8)	Mus musculus	13-18
24281189-9	2014	Furthermore, interferon-gamma neutralization eliminates AngII-increased superoxide products and endothelial apoptosis by inhibiting AngII-induced Kynurenines generation, suggesting that AngII-activated Kyn pathway is interferon-gamma-dependent.	Kynurenine	146-157	interferon gamma	Mus musculus	13-29
24281189-9	2014	Furthermore, interferon-gamma neutralization eliminates AngII-increased superoxide products and endothelial apoptosis by inhibiting AngII-induced Kynurenines generation, suggesting that AngII-activated Kyn pathway is interferon-gamma-dependent.	Kynurenine	146-157	angiotensinogen (serpin peptidase inhibitor, clade A, member 8)	Mus musculus	56-61
24281189-9	2014	Furthermore, interferon-gamma neutralization eliminates AngII-increased superoxide products and endothelial apoptosis by inhibiting AngII-induced Kynurenines generation, suggesting that AngII-activated Kyn pathway is interferon-gamma-dependent.	Kynurenine	146-157	angiotensinogen (serpin peptidase inhibitor, clade A, member 8)	Mus musculus	132-137
24281189-9	2014	Furthermore, interferon-gamma neutralization eliminates AngII-increased superoxide products and endothelial apoptosis by inhibiting AngII-induced Kynurenines generation, suggesting that AngII-activated Kyn pathway is interferon-gamma-dependent.	Kynurenine	146-157	angiotensinogen (serpin peptidase inhibitor, clade A, member 8)	Mus musculus	132-137
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).	Kynurenine	122-132	indoleamine 2,3-dioxygenase 1	Homo sapiens	29-32
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).	Kynurenine	134-137	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).	Kynurenine	134-137	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.	Kynurenine	50-53	indoleamine 2,3-dioxygenase 1	Homo sapiens	6-9
24697114-6	2014	Serum tryptophan and kynurenine levels were determined with HPLC-UV method, and kynurenine/tryptophan ratio was evaluated as IDO activity.	Kynurenine	80-90	indoleamine 2,3-dioxygenase 1	Homo sapiens	125-128
23606516-1	2014	Indoleamine 2,3-dioxygenase (IDO) is a rate-limiting enzyme for the degradation of tryptophan (Trp) along the kynurenine (Kyn) pathway, and its increased activation is associated with immunologic disorders.	Kynurenine	110-120	indoleamine 2,3-dioxygenase 1	Sus scrofa	29-32
23606516-1	2014	Indoleamine 2,3-dioxygenase (IDO) is a rate-limiting enzyme for the degradation of tryptophan (Trp) along the kynurenine (Kyn) pathway, and its increased activation is associated with immunologic disorders.	Kynurenine	110-120	indoleamine 2,3-dioxygenase 1	Sus scrofa	0-27
23606516-1	2014	Indoleamine 2,3-dioxygenase (IDO) is a rate-limiting enzyme for the degradation of tryptophan (Trp) along the kynurenine (Kyn) pathway, and its increased activation is associated with immunologic disorders.	Kynurenine	122-125	indoleamine 2,3-dioxygenase 1	Sus scrofa	0-27
23606516-1	2014	Indoleamine 2,3-dioxygenase (IDO) is a rate-limiting enzyme for the degradation of tryptophan (Trp) along the kynurenine (Kyn) pathway, and its increased activation is associated with immunologic disorders.	Kynurenine	122-125	indoleamine 2,3-dioxygenase 1	Sus scrofa	29-32
24136190-4	2014	Guinea pig hepatic cytosolic AhR activated in vitro by equipotent concentrations of TCDD, 3-methylcholanthrene, beta-naphthoflavone, indirubin, L-kynurenine, or YH439 was incubated with a pool of DNA oligonucleotides containing a 15-base pair variable region consisting of all possible nucleotides.	Kynurenine	144-156	aryl hydrocarbon receptor	Cavia porcellus	29-32
25286653-1	2014	Kynurenic acid (KYNA), an endogenous neuroprotectant formed along the kynurenine pathway of tryptophan degradation, is a selective ligand of the GPR35 receptor, which can be found on the surface of various populations of human immune cells.	Kynurenine	70-80	G protein-coupled receptor 35	Homo sapiens	145-150
24988959-2	2014	The enzyme indoleamine 2,3-dioxygenase (IDO) catalyzes the initial step of the kynurenine pathway that converts tryptophan to kynurenine metabolites.	Kynurenine	79-89	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.	Kynurenine	79-89	indoleamine 2,3-dioxygenase 1	Homo sapiens	40-43
24988959-2	2014	The enzyme indoleamine 2,3-dioxygenase (IDO) catalyzes the initial step of the kynurenine pathway that converts tryptophan to kynurenine metabolites.	Kynurenine	126-136	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.	Kynurenine	126-136	indoleamine 2,3-dioxygenase 1	Homo sapiens	40-43
23786539-0	2013	Age-dependent alterations of the kynurenine pathway in the YAC128 mouse model of Huntington disease.	Kynurenine	33-43	renin binding protein	Mus musculus	0-3
24189070-1	2013	Kynurenine 3-monooxygenase (KMO), a pivotal enzyme in the kynurenine pathway (KP) of tryptophan degradation, has been suggested to play a major role in physiological and pathological events involving bioactive KP metabolites.	Kynurenine	58-68	kynurenine 3-monooxygenase (kynurenine 3-hydroxylase)	Mus musculus	0-26
24189070-1	2013	Kynurenine 3-monooxygenase (KMO), a pivotal enzyme in the kynurenine pathway (KP) of tryptophan degradation, has been suggested to play a major role in physiological and pathological events involving bioactive KP metabolites.	Kynurenine	58-68	kynurenine 3-monooxygenase (kynurenine 3-hydroxylase)	Mus musculus	28-31
24190896-1	2014	Tryptophan 2,3-dioxygenase (Tdo2) is a rate-limiting enzyme which directs the conversion of tryptophan to kynurenine.	Kynurenine	106-116	tryptophan 2,3-dioxygenase	Mus musculus	0-26
24190896-1	2014	Tryptophan 2,3-dioxygenase (Tdo2) is a rate-limiting enzyme which directs the conversion of tryptophan to kynurenine.	Kynurenine	106-116	tryptophan 2,3-dioxygenase	Mus musculus	28-32
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.	Kynurenine	352-362	tryptophan 2,3-dioxygenase	Homo sapiens	125-151
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.	Kynurenine	352-362	tryptophan 2,3-dioxygenase	Homo sapiens	153-156
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.	Kynurenine	352-362	indoleamine 2,3-dioxygenase 1	Homo sapiens	162-189
24105077-7	2013	This review focuses on the current knowledge of IDO2 biology and discusses tools that will assist in further characterizing the enzymes of the kynurenine pathway.	Kynurenine	143-153	indoleamine 2,3-dioxygenase 2	Homo sapiens	48-52
24355457-27	2013	Elevated Kyn/Trp ratio is suggested to mirror IDO activity.	Kynurenine	9-12	indoleamine 2,3-dioxygenase 1	Homo sapiens	46-49
23955123-5	2013	Due to the previous association of ACMSD deficiency with the development of epileptic seizures, we concluded that the identified nonsense mutation in the ACMSD gene, which encodes for a critical enzyme of the kynurenine pathway of the tryptophan metabolism, is the disease-segregating mutation most likely to be responsible for the phenotype described in our family.	Kynurenine	209-219	aminocarboxymuconate semialdehyde decarboxylase	Homo sapiens	35-40
24189070-6	2013	The levels of three other KP metabolites: kynurenine, kynurenic acid, and anthranilic acid, were substantially, but differentially, elevated in the liver, brain, and plasma of Kmo(-/-) mice, whereas the liver and brain content of the major end product of the enzymatic cascade, NAD(+), did not differ between Kmo(-/-) and wild-type animals.	Kynurenine	42-52	kynurenine 3-monooxygenase (kynurenine 3-hydroxylase)	Mus musculus	176-179
23786539-1	2013	Indoleamine 2,3 dioxygenase (Ido1), the first and rate-limiting enzyme of the kynurenine pathway (KP), is a striatally enriched gene with increased expression levels in the YAC128 mouse model of Huntington disease (HD).	Kynurenine	78-88	indoleamine 2,3-dioxygenase 1	Mus musculus	29-33
24129513-5	2013	Xenogenic expression of human alpha-synuclein in yeast cells triggers mitochondria-nuclear translocation of EndoG and EndoG-mediated DNA degradation through a mechanism that requires a functional kynurenine pathway and the permeability transition pore.	Kynurenine	196-206	synuclein alpha	Homo sapiens	30-45
24129513-5	2013	Xenogenic expression of human alpha-synuclein in yeast cells triggers mitochondria-nuclear translocation of EndoG and EndoG-mediated DNA degradation through a mechanism that requires a functional kynurenine pathway and the permeability transition pore.	Kynurenine	196-206	endonuclease G	Homo sapiens	108-113
24129513-5	2013	Xenogenic expression of human alpha-synuclein in yeast cells triggers mitochondria-nuclear translocation of EndoG and EndoG-mediated DNA degradation through a mechanism that requires a functional kynurenine pathway and the permeability transition pore.	Kynurenine	196-206	endonuclease G	Homo sapiens	118-123
23994717-6	2013	Finally, through measurement of kynurenine pathway (KP) metabolites in Ido(-/-) mice, we showed decreased levels of 3-HK in the striatum of these mice.	Kynurenine	32-42	indoleamine 2,3-dioxygenase 1	Mus musculus	71-74
23942267-1	2013	AIMS: Indoleamine 2,3-dioxygenase (IDO) inhibits T-cell proliferation by catalyzing the conversion of l-tryptophan to l-kynurenine.	Kynurenine	118-130	indoleamine 2,3-dioxygenase 1	Homo sapiens	6-33
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.	Kynurenine	78-88	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.	Kynurenine	78-88	indoleamine 2,3-dioxygenase 1	Homo sapiens	40-43
24393854-2	2013	IDO activity can be determined by the tryptophan( Trp)/kynurenine( Kyn) ratio.	Kynurenine	55-65	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-3
24393854-2	2013	IDO activity can be determined by the tryptophan( Trp)/kynurenine( Kyn) ratio.	Kynurenine	67-70	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-3
24012176-3	2013	The assessment was performed under basal conditions or following treatment with interferon (IFN)-gamma, tumor necrosis factor (TNF)-alpha, interleukin (IL)-1beta, IL-6, or their combinations, in cells exposed to exogenous kynurenine.	Kynurenine	222-232	interleukin 1 beta	Homo sapiens	139-161
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.	Kynurenine	51-61	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.	Kynurenine	51-61	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.	Kynurenine	63-66	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.	Kynurenine	63-66	indoleamine 2,3-dioxygenase 1	Homo sapiens	100-103
23942267-1	2013	AIMS: Indoleamine 2,3-dioxygenase (IDO) inhibits T-cell proliferation by catalyzing the conversion of l-tryptophan to l-kynurenine.	Kynurenine	118-130	indoleamine 2,3-dioxygenase 1	Homo sapiens	35-38
23690293-1	2013	Kynurenine monooxygenase (KMO) catalyzes the conversion of kynurenine to 3-hydroxykynurenine.	Kynurenine	59-69	kynurenine 3-monooxygenase	Homo sapiens	0-24
23879623-5	2013	We observed a great variability in the levels of IDO1 mRNA expression and kynurenine release between skin cells and melanoma cell lines in response to interferon-gamma, a classical IDO1 inducer.	Kynurenine	74-84	interferon gamma	Homo sapiens	151-167
23981041-2	2013	Polyinosinic:polycytidylic acid (poly(I:C)) is a viral-mimetic double-stranded RNA complex which activates Toll-Like-Receptor-3 and can activate the metabolism of tryptophan through the oxidative kynurenine pathway to compounds that modulate activity of glutamate receptors.	Kynurenine	196-206	toll-like receptor 3	Rattus norvegicus	107-127
23813101-0	2013	Insulin resistance and dysregulation of tryptophan-kynurenine and kynurenine-nicotinamide adenine dinucleotide metabolic pathways.	Kynurenine	51-61	insulin	Homo sapiens	0-7
23813101-0	2013	Insulin resistance and dysregulation of tryptophan-kynurenine and kynurenine-nicotinamide adenine dinucleotide metabolic pathways.	Kynurenine	66-76	insulin	Homo sapiens	0-7
23813101-7	2013	Human and experimental studies suggested that XA and some other KYN metabolites might impair production, release, and biological activity of insulin.	Kynurenine	64-67	insulin	Homo sapiens	141-148
23336953-2	2013	Neopterin production and tryptophan catabolism through the kynurenine pathway, measured by the kynurenine-tryptophan ratio (KTR), are induced by interferon gamma, thus both are considered markers of cell mediated immune activation.	Kynurenine	59-69	interferon gamma	Homo sapiens	145-161
23690293-1	2013	Kynurenine monooxygenase (KMO) catalyzes the conversion of kynurenine to 3-hydroxykynurenine.	Kynurenine	59-69	kynurenine 3-monooxygenase	Homo sapiens	26-29
23417792-3	2013	In the immune system, two distinct enzymes, Indoleamne 2,3 dioxygenase 1 (IDO1) and Indoleamine 2, 3 dioxygenase 2 (IDO2) can initiate metabolic flux through the kynurenine pathway.	Kynurenine	162-172	indoleamine 2,3-dioxygenase 1	Mus musculus	74-78
23417792-3	2013	In the immune system, two distinct enzymes, Indoleamne 2,3 dioxygenase 1 (IDO1) and Indoleamine 2, 3 dioxygenase 2 (IDO2) can initiate metabolic flux through the kynurenine pathway.	Kynurenine	162-172	indoleamine 2,3-dioxygenase 2	Mus musculus	84-114
23417792-3	2013	In the immune system, two distinct enzymes, Indoleamne 2,3 dioxygenase 1 (IDO1) and Indoleamine 2, 3 dioxygenase 2 (IDO2) can initiate metabolic flux through the kynurenine pathway.	Kynurenine	162-172	indoleamine 2,3-dioxygenase 2	Mus musculus	116-120
24039933-2	2013	Indoleamine 2,3-dioxygenase (IDO), an intracellular enzyme that mediates the catabolism of L-tryptophan to L-kynurenine, plays an important role in hepatic immune regulation.	Kynurenine	107-119	indoleamine 2,3-dioxygenase 1	Mus musculus	0-27
24039933-2	2013	Indoleamine 2,3-dioxygenase (IDO), an intracellular enzyme that mediates the catabolism of L-tryptophan to L-kynurenine, plays an important role in hepatic immune regulation.	Kynurenine	107-119	indoleamine 2,3-dioxygenase 1	Mus musculus	29-32
23732870-2	2013	One of the major mechanisms through which IFNgamma exerts these effects is by inducing expression of indoleamine 2,3 dioxygenase-1 (IDO1), an enzyme that catalyses the first, rate-limiting step of the kynurenine pathway.	Kynurenine	201-211	interferon gamma	Homo sapiens	42-50
23902960-0	2013	A mathematical model of tryptophan metabolism via the kynurenine pathway provides insights into the effects of vitamin B-6 deficiency, tryptophan loading, and induction of tryptophan 2,3-dioxygenase on tryptophan metabolites.	Kynurenine	54-64	tryptophan 2,3-dioxygenase	Homo sapiens	172-198
23902960-10	2013	Induction of TDO caused an increase in all metabolites, and TDO induction together with a simulated vitamin B-6 deficiency, as has been reported in oral contraceptive users, yielded increases in kynurenine, 3-hydroxykynurenine, and xanthurenic acid and decreases in kynurenic acid and anthranilic acid.	Kynurenine	195-205	tryptophan 2,3-dioxygenase	Homo sapiens	60-63
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).	Kynurenine	109-121	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).	Kynurenine	111-114	indoleamine 2,3-dioxygenase 1	Homo sapiens	4-31
23732870-2	2013	One of the major mechanisms through which IFNgamma exerts these effects is by inducing expression of indoleamine 2,3 dioxygenase-1 (IDO1), an enzyme that catalyses the first, rate-limiting step of the kynurenine pathway.	Kynurenine	201-211	indoleamine 2,3-dioxygenase 1	Homo sapiens	101-130
23732870-2	2013	One of the major mechanisms through which IFNgamma exerts these effects is by inducing expression of indoleamine 2,3 dioxygenase-1 (IDO1), an enzyme that catalyses the first, rate-limiting step of the kynurenine pathway.	Kynurenine	201-211	indoleamine 2,3-dioxygenase 1	Homo sapiens	132-136
23732870-6	2013	Production of kynurenine has been used as an indicator of human IDO1 activity, and hence as an hIDO1 bioassay.	Kynurenine	14-24	indoleamine 2,3-dioxygenase 1	Homo sapiens	64-68
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.	Kynurenine	65-76	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-29
23732870-6	2013	Production of kynurenine has been used as an indicator of human IDO1 activity, and hence as an hIDO1 bioassay.	Kynurenine	14-24	indoleamine 2,3-dioxygenase 1	Homo sapiens	95-100
23732870-7	2013	Due to IFNgamma"s ability to induce IDO1 expression, kynurenine production can also be a measure of human IFNgamma (hIFNgamma) bioactivity.	Kynurenine	53-63	interferon gamma	Homo sapiens	106-114
23732870-7	2013	Due to IFNgamma"s ability to induce IDO1 expression, kynurenine production can also be a measure of human IFNgamma (hIFNgamma) bioactivity.	Kynurenine	53-63	interferon gamma	Homo sapiens	116-125
23991016-3	2013	METHODOLOGY/PRINCIPAL FINDINGS: The DNA demethylating agent Zebularine, previously demonstrated to induce expression of the genes for the immunosuppressive enzymes indolamine-2,3-deoxygenase-1 (IDO1) and kynureninase of the kynurenine pathway, is tested for capacity to suppress rejection of allotransplants.	Kynurenine	224-234	indoleamine 2,3-dioxygenase 1	Rattus norvegicus	164-192
24048400-2	2013	Cyclooxygenase-2 (COX-2) not only reduces the levels of proinflammatory cytokines, but also affects glutamatergic neurotransmission and tryptophan/kynurenine metabolism.	Kynurenine	147-157	prostaglandin-endoperoxide synthase 2	Homo sapiens	0-16
24048400-2	2013	Cyclooxygenase-2 (COX-2) not only reduces the levels of proinflammatory cytokines, but also affects glutamatergic neurotransmission and tryptophan/kynurenine metabolism.	Kynurenine	147-157	prostaglandin-endoperoxide synthase 2	Homo sapiens	18-23
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.	Kynurenine	65-76	indoleamine 2,3-dioxygenase 1	Homo sapiens	31-35
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.	Kynurenine	78-81	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.	Kynurenine	78-81	indoleamine 2,3-dioxygenase 1	Homo sapiens	31-35
23973990-5	2013	The increased COX-2 and IDO1 expression correlated with heightened production of prostaglandin (PG)E2 and kynurenines, respectively.	Kynurenine	106-117	prostaglandin-endoperoxide synthase 2	Homo sapiens	14-19
23973990-5	2013	The increased COX-2 and IDO1 expression correlated with heightened production of prostaglandin (PG)E2 and kynurenines, respectively.	Kynurenine	106-117	indoleamine 2,3-dioxygenase 1	Homo sapiens	24-28
23511700-2	2013	IDO degrades tryptophan along the kynurenine pathway.	Kynurenine	34-44	indoleamine 2,3-dioxygenase 1	Mus musculus	0-3
23940687-6	2013	Since macrophages play a pivotal role in xenograft rejection, herein we investigated the effect of IDO-induced tryptophan deficiency/kynurenine accumulation on macrophage function/survival.	Kynurenine	133-143	indoleamine 2,3-dioxygenase 1	Mus musculus	99-102
23940687-10	2013	To determine whether IDO-induced tryptophan starvation or kynurenine accumulation is responsible for macrophage apoptosis and inhibition of their proinflammatory activity, Raw264.7 cell viability and proinflammatory responses were evaluated in tryptophan deficient medium or in the presence of kynurenine.	Kynurenine	294-304	indoleamine 2,3-dioxygenase 1	Mus musculus	21-24
23669411-1	2013	BACKGROUND &amp; AIMS: Indoleamine 2,3 dioxygenase-1 (IDO1) catabolizes tryptophan along the kynurenine pathway.	Kynurenine	93-103	indoleamine 2,3-dioxygenase 1	Mus musculus	23-52
23669411-1	2013	BACKGROUND &amp; AIMS: Indoleamine 2,3 dioxygenase-1 (IDO1) catabolizes tryptophan along the kynurenine pathway.	Kynurenine	93-103	indoleamine 2,3-dioxygenase 1	Mus musculus	54-58
23669411-8	2013	Kynurenine pathway metabolites were used to simulate IDO1 activity.	Kynurenine	0-10	indoleamine 2,3-dioxygenase 1	Mus musculus	53-57
23669411-12	2013	Exogenous administration of IDO1 pathway metabolites kynurenine and quinolinic acid led to activation of beta-catenin and proliferation of human colon cancer cells, and increased tumor growth in mice.	Kynurenine	53-63	indoleamine 2,3-dioxygenase 1	Homo sapiens	28-32
23669411-12	2013	Exogenous administration of IDO1 pathway metabolites kynurenine and quinolinic acid led to activation of beta-catenin and proliferation of human colon cancer cells, and increased tumor growth in mice.	Kynurenine	53-63	catenin beta 1	Homo sapiens	105-117
23511700-3	2013	Using mass-spectrometry (LC-MS) analysis of kynurenine metabolites in the brain of mice injected at the periphery with 1 mg/kg LPS, we show that LPS activates the kynurenine 3-monooxygenase pathway that ultimately degrades kynurenine into quinolinic acid.	Kynurenine	44-54	kynurenine 3-monooxygenase (kynurenine 3-hydroxylase)	Mus musculus	163-189
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.	Kynurenine	80-90	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.	Kynurenine	80-90	indoleamine 2,3-dioxygenase 1	Homo sapiens	29-32
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.	Kynurenine	207-218	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.	Kynurenine	207-218	indoleamine 2,3-dioxygenase 1	Homo sapiens	29-32
23866724-2	2013	Systemic immune challenge induces IDO1 in both the periphery and the brain, leading to increased circulating and brain concentrations of kynurenines.	Kynurenine	137-148	indoleamine 2,3-dioxygenase 1	Mus musculus	34-38
23843452-6	2013	Furthermore, this dysbiosis was evident among HIV-infected subjects undergoing HAART, and the extent of dysbiosis correlated with activity of the kynurenine pathway of tryptophan catabolism and plasma concentrations of the inflammatory cytokine interleukin-6 (IL-6), two established markers of disease progression.	Kynurenine	146-156	interleukin 6	Homo sapiens	260-264
23597432-6	2013	The presence of IFNgamma CA repeat allele 2 homozygous has significant association with higher kynurenine concentrations in controls (F=4.47, p=0.038) as well as in patients (F=3.79, p=0.045).	Kynurenine	95-105	interferon gamma	Homo sapiens	16-24
23558111-1	2013	AIMS: In response to acute ethanol consumption, tryptophan 2,3-dioxygenase (TDO) induces the kynurenine pathway (KP) through a glucocorticoid-mediated mechanism, which could lead to a dramatic accumulation of neurotoxic metabolites in association with serotonin depletion.	Kynurenine	93-103	tryptophan 2,3-dioxygenase	Homo sapiens	48-74
23558111-1	2013	AIMS: In response to acute ethanol consumption, tryptophan 2,3-dioxygenase (TDO) induces the kynurenine pathway (KP) through a glucocorticoid-mediated mechanism, which could lead to a dramatic accumulation of neurotoxic metabolites in association with serotonin depletion.	Kynurenine	93-103	tryptophan 2,3-dioxygenase	Homo sapiens	76-79
23624173-8	2013	In addition, EGFP expression can be stimulated by kynurenine, a putative AHR ligand produced during tryptophan metabolism.	Kynurenine	50-60	aryl hydrocarbon receptor	Homo sapiens	73-76
22926082-3	2013	IDO activation and subsequent generation of neuroactive kynurenine metabolites may have a pivotal role in the development of depression.	Kynurenine	56-66	indoleamine 2,3-dioxygenase 1	Mus musculus	0-3
23453284-1	2013	Tryptophan catabolism, which is mediated by the enzymes indoleamine 2,3-dioxygenase (IDO) and tryptophan 2,3-dioxygenase (TDO), produces kynurenine.	Kynurenine	137-147	indoleamine 2,3-dioxygenase 1	Homo sapiens	56-83
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.	Kynurenine	116-126	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.	Kynurenine	116-126	indoleamine 2,3-dioxygenase 1	Homo sapiens	29-32
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.	Kynurenine	116-126	interferon gamma	Homo sapiens	40-56
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.	Kynurenine	116-126	interferon gamma	Homo sapiens	58-67
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.	Kynurenine	128-131	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.	Kynurenine	128-131	indoleamine 2,3-dioxygenase 1	Homo sapiens	29-32
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.	Kynurenine	128-131	interferon gamma	Homo sapiens	40-56
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.	Kynurenine	128-131	interferon gamma	Homo sapiens	58-67
23700344-6	2013	These findings show that the kynurenine formed in extrahepatic tissues by IDO and subsequent enzymes can be metabolized up to 3-HA, but not into QA.	Kynurenine	29-39	indoleamine 2,3-dioxygenase 1	Mus musculus	74-77
23517271-1	2013	Kinetics of the oxidation of tryptophan (Trp) and kynurenine (Kyn), precursors of nitrogenous disinfection byproducts (N-DBP), by ferrate(VI) (Fe(VI)O4(2-), Fe(VI)) were investigated over the acidic to basic pH range.	Kynurenine	50-60	D-box binding PAR bZIP transcription factor	Homo sapiens	121-124
23517271-1	2013	Kinetics of the oxidation of tryptophan (Trp) and kynurenine (Kyn), precursors of nitrogenous disinfection byproducts (N-DBP), by ferrate(VI) (Fe(VI)O4(2-), Fe(VI)) were investigated over the acidic to basic pH range.	Kynurenine	62-65	D-box binding PAR bZIP transcription factor	Homo sapiens	121-124
23325926-1	2013	Mammalian IDO is a heme-containing enzyme whose main activity in mammals is to degrade the essential amino acid tryp into l-kynurenine.	Kynurenine	122-134	indoleamine 2,3-dioxygenase 1	Homo sapiens	10-13
23453284-1	2013	Tryptophan catabolism, which is mediated by the enzymes indoleamine 2,3-dioxygenase (IDO) and tryptophan 2,3-dioxygenase (TDO), produces kynurenine.	Kynurenine	137-147	indoleamine 2,3-dioxygenase 1	Homo sapiens	85-88
23453284-1	2013	Tryptophan catabolism, which is mediated by the enzymes indoleamine 2,3-dioxygenase (IDO) and tryptophan 2,3-dioxygenase (TDO), produces kynurenine.	Kynurenine	137-147	tryptophan 2,3-dioxygenase	Homo sapiens	94-120
23453284-1	2013	Tryptophan catabolism, which is mediated by the enzymes indoleamine 2,3-dioxygenase (IDO) and tryptophan 2,3-dioxygenase (TDO), produces kynurenine.	Kynurenine	137-147	tryptophan 2,3-dioxygenase	Homo sapiens	122-125
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.	Kynurenine	102-112	indoleamine 2,3-dioxygenase 1	Homo sapiens	27-54
23630570-9	2013	This is the first report demonstrating that TDO is highly expressed in the brains of AD mice and in AD patients, suggesting that TDO-mediated activation of the kynurenine pathway could be involved in neurofibrillary tangles formation and associated with senile plaque.	Kynurenine	160-170	tryptophan 2,3-dioxygenase	Mus musculus	44-47
23630570-9	2013	This is the first report demonstrating that TDO is highly expressed in the brains of AD mice and in AD patients, suggesting that TDO-mediated activation of the kynurenine pathway could be involved in neurofibrillary tangles formation and associated with senile plaque.	Kynurenine	160-170	tryptophan 2,3-dioxygenase	Homo sapiens	129-132
23575632-2	2013	KMO is a flavin adenine dinucleotide (FAD)-dependent monooxygenase and is located in the outer mitochondrial membrane where it converts l-kynurenine to 3-hydroxykynurenine.	Kynurenine	136-148	kynurenine 3-monooxygenase (kynurenine 3-hydroxylase)	Mus musculus	0-3
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.	Kynurenine	102-112	indoleamine 2,3-dioxygenase 1	Homo sapiens	56-59
23358471-6	2013	Freshly-resected meningiomas expressed both LAT1, the tryptophan transporter system and IDO, demonstrating an active kynurenine pathway.	Kynurenine	117-127	indoleamine 2,3-dioxygenase 1	Homo sapiens	88-91
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.	Kynurenine	97-107	indoleamine 2,3-dioxygenase 1	Homo sapiens	38-65
23550784-3	2013	Current evidence suggests that the inverse association between plasma PLP and inflammation may be the result of mobilization of this coenzyme to the site of inflammation, for use by the PLP-dependent enzymes of the kynurenine pathway of tryptophan degradation, metabolism of the immunomodulatory sphingolipids, ceramide and sphingosine 1-phosphate, and for serine hydroxymethylase for immune cell proliferation.	Kynurenine	215-225	pyridoxal phosphatase	Homo sapiens	70-73
23550784-3	2013	Current evidence suggests that the inverse association between plasma PLP and inflammation may be the result of mobilization of this coenzyme to the site of inflammation, for use by the PLP-dependent enzymes of the kynurenine pathway of tryptophan degradation, metabolism of the immunomodulatory sphingolipids, ceramide and sphingosine 1-phosphate, and for serine hydroxymethylase for immune cell proliferation.	Kynurenine	215-225	pyridoxal phosphatase	Homo sapiens	186-189
23550784-3	2013	Current evidence suggests that the inverse association between plasma PLP and inflammation may be the result of mobilization of this coenzyme to the site of inflammation, for use by the PLP-dependent enzymes of the kynurenine pathway of tryptophan degradation, metabolism of the immunomodulatory sphingolipids, ceramide and sphingosine 1-phosphate, and for serine hydroxymethylase for immune cell proliferation.	Kynurenine	215-225	serine hydroxymethyltransferase 2	Homo sapiens	357-380
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.	Kynurenine	97-107	indoleamine 2,3-dioxygenase 1	Homo sapiens	67-70
23123095-2	2013	Kynurenine acts on the aryl hydrocarbon receptor, affecting the metabolism of xenobiotics and promoting carcinogenesis.	Kynurenine	0-10	aryl hydrocarbon receptor	Homo sapiens	23-48
23283180-2	2013	IDO1 initiates tryptophan catabolism along a pathway that generates several bioactive kynurenine-based metabolites.	Kynurenine	86-96	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-4
23319400-7	2013	IDO produces kynurenine, an endogenous AhR ligand that directly activates AhR and is proposed to be central to the establishment and maintenance of immunologic tolerance at the maternal-foetal interface.	Kynurenine	13-23	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-3
23319400-7	2013	IDO produces kynurenine, an endogenous AhR ligand that directly activates AhR and is proposed to be central to the establishment and maintenance of immunologic tolerance at the maternal-foetal interface.	Kynurenine	13-23	aryl hydrocarbon receptor	Homo sapiens	39-42
23319400-7	2013	IDO produces kynurenine, an endogenous AhR ligand that directly activates AhR and is proposed to be central to the establishment and maintenance of immunologic tolerance at the maternal-foetal interface.	Kynurenine	13-23	aryl hydrocarbon receptor	Homo sapiens	74-77
23319400-8	2013	We propose that kynurenine activates AhR, leading to the AhR-dependent T(reg)  cells generation, which in turn critically regulates immunological tolerance at the feto-maternal interface.	Kynurenine	16-26	aryl hydrocarbon receptor	Homo sapiens	37-40
23319400-8	2013	We propose that kynurenine activates AhR, leading to the AhR-dependent T(reg)  cells generation, which in turn critically regulates immunological tolerance at the feto-maternal interface.	Kynurenine	16-26	aryl hydrocarbon receptor	Homo sapiens	57-60
23333332-1	2013	Tryptophan 2,3-dioxygenase (TDO) catalyzes the oxidative cleavage of the indole ring of l-tryptophan to N-formylkynurenine in the kynurenine pathway, and is considered as a drug target for cancer immunotherapy.	Kynurenine	112-122	vermilion	Drosophila melanogaster	0-26
23333332-1	2013	Tryptophan 2,3-dioxygenase (TDO) catalyzes the oxidative cleavage of the indole ring of l-tryptophan to N-formylkynurenine in the kynurenine pathway, and is considered as a drug target for cancer immunotherapy.	Kynurenine	112-122	vermilion	Drosophila melanogaster	28-31
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).	Kynurenine	163-173	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).	Kynurenine	163-173	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).	Kynurenine	175-178	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).	Kynurenine	175-178	indoleamine 2,3-dioxygenase 1	Homo sapiens	29-32
23121382-2	2013	IDO modulates the immune response by depletion of the essential amino acid tryptophan by breakdown to kynurenines, which themselves act directly on T lymphocytes.	Kynurenine	102-113	indoleamine 2,3-dioxygenase 1	Mus musculus	0-3
23438698-4	2013	Rate-limiting enzymes of kynurenine formation are two: tryptophan 2,3-dioxygenas (TDO) activated by stress hormones, and indoleamine 2,3-dioxygenase (IDO), activated by proinflammatory cytokines.	Kynurenine	25-35	tryptophan 2,3-dioxygenase	Homo sapiens	82-85
24083022-7	2013	TNF-alpha potentiates interferon-gamma-induced transcriptional activation of indoleamine 2,3-dioxygenase, the rate-limiting enzyme of tryptophan- (TRP-) kynurenine (KYN) metabolism.	Kynurenine	153-163	tumor necrosis factor	Homo sapiens	0-9
24083022-7	2013	TNF-alpha potentiates interferon-gamma-induced transcriptional activation of indoleamine 2,3-dioxygenase, the rate-limiting enzyme of tryptophan- (TRP-) kynurenine (KYN) metabolism.	Kynurenine	153-163	interferon gamma	Homo sapiens	22-38
24083022-7	2013	TNF-alpha potentiates interferon-gamma-induced transcriptional activation of indoleamine 2,3-dioxygenase, the rate-limiting enzyme of tryptophan- (TRP-) kynurenine (KYN) metabolism.	Kynurenine	165-168	tumor necrosis factor	Homo sapiens	0-9
24083022-7	2013	TNF-alpha potentiates interferon-gamma-induced transcriptional activation of indoleamine 2,3-dioxygenase, the rate-limiting enzyme of tryptophan- (TRP-) kynurenine (KYN) metabolism.	Kynurenine	165-168	interferon gamma	Homo sapiens	22-38
23853597-4	2013	IDO1 was responsible for the production of tolerogenic kynurenines, such that replacement therapy with kynurenines restored immunoprotection to VVC.	Kynurenine	55-66	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-4
23853597-4	2013	IDO1 was responsible for the production of tolerogenic kynurenines, such that replacement therapy with kynurenines restored immunoprotection to VVC.	Kynurenine	103-114	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-4
23438698-4	2013	Rate-limiting enzymes of kynurenine formation are two: tryptophan 2,3-dioxygenas (TDO) activated by stress hormones, and indoleamine 2,3-dioxygenase (IDO), activated by proinflammatory cytokines.	Kynurenine	25-35	indoleamine 2,3-dioxygenase 1	Homo sapiens	121-148
23438698-4	2013	Rate-limiting enzymes of kynurenine formation are two: tryptophan 2,3-dioxygenas (TDO) activated by stress hormones, and indoleamine 2,3-dioxygenase (IDO), activated by proinflammatory cytokines.	Kynurenine	25-35	indoleamine 2,3-dioxygenase 1	Homo sapiens	150-153
22895526-1	2012	Indoleamine 2,3-dioxygenase 1 (IDO1) catabolizes tryptophan to kynurenine at the first step of tryptophan metabolism.	Kynurenine	63-73	indoleamine 2,3-dioxygenase 1	Mus musculus	0-29
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.	Kynurenine	113-123	indoleamine 2,3-dioxygenase 1	Homo sapiens	25-28
23216784-1	2012	UNLABELLED:  BACKGROUND: Excessive tryptophan metabolism to kynurenine by the rate-limiting enzyme endothelial indoleamine 2,3-dioxygenase 1 (IDO) controls arterial vessel relaxation and causes hypotension in murine endotoxemia.	Kynurenine	60-70	indoleamine 2,3-dioxygenase 1	Mus musculus	111-140
23216784-1	2012	UNLABELLED:  BACKGROUND: Excessive tryptophan metabolism to kynurenine by the rate-limiting enzyme endothelial indoleamine 2,3-dioxygenase 1 (IDO) controls arterial vessel relaxation and causes hypotension in murine endotoxemia.	Kynurenine	60-70	indoleamine 2,3-dioxygenase 1	Mus musculus	142-145
23267883-2	2012	IDO activity can be measured by the tryptophan(Trp)/kynurenine(Kyn) ratio.	Kynurenine	52-62	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-3
23267883-2	2012	IDO activity can be measured by the tryptophan(Trp)/kynurenine(Kyn) ratio.	Kynurenine	63-66	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-3
23267888-2	2012	IDO activity can be measured by the tryptophan(Trp)/kynurenine(Kyn) ratio.	Kynurenine	52-62	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-3
23267888-2	2012	IDO activity can be measured by the tryptophan(Trp)/kynurenine(Kyn) ratio.	Kynurenine	63-66	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-3
23122865-2	2012	The first and rate-limiting step of the kynurenine pathway can be independently catalysed by tryptophan 2,3-dioxygenase (Tdo2), indoleamine 2,3-dioxygenase 1 (Ido1) or indoleamine 2,3-dioxygenase 2 (Ido2).	Kynurenine	40-50	tryptophan 2,3-dioxygenase	Homo sapiens	93-119
23122865-2	2012	The first and rate-limiting step of the kynurenine pathway can be independently catalysed by tryptophan 2,3-dioxygenase (Tdo2), indoleamine 2,3-dioxygenase 1 (Ido1) or indoleamine 2,3-dioxygenase 2 (Ido2).	Kynurenine	40-50	tryptophan 2,3-dioxygenase	Homo sapiens	121-125
23122865-2	2012	The first and rate-limiting step of the kynurenine pathway can be independently catalysed by tryptophan 2,3-dioxygenase (Tdo2), indoleamine 2,3-dioxygenase 1 (Ido1) or indoleamine 2,3-dioxygenase 2 (Ido2).	Kynurenine	40-50	indoleamine 2,3-dioxygenase 1	Homo sapiens	128-157
23122865-2	2012	The first and rate-limiting step of the kynurenine pathway can be independently catalysed by tryptophan 2,3-dioxygenase (Tdo2), indoleamine 2,3-dioxygenase 1 (Ido1) or indoleamine 2,3-dioxygenase 2 (Ido2).	Kynurenine	40-50	indoleamine 2,3-dioxygenase 1	Homo sapiens	159-163
23122865-2	2012	The first and rate-limiting step of the kynurenine pathway can be independently catalysed by tryptophan 2,3-dioxygenase (Tdo2), indoleamine 2,3-dioxygenase 1 (Ido1) or indoleamine 2,3-dioxygenase 2 (Ido2).	Kynurenine	40-50	indoleamine 2,3-dioxygenase 2	Homo sapiens	168-197
23122865-2	2012	The first and rate-limiting step of the kynurenine pathway can be independently catalysed by tryptophan 2,3-dioxygenase (Tdo2), indoleamine 2,3-dioxygenase 1 (Ido1) or indoleamine 2,3-dioxygenase 2 (Ido2).	Kynurenine	40-50	indoleamine 2,3-dioxygenase 2	Homo sapiens	199-203
23122865-3	2012	Tdo2 or Ido1 enzymatic activity has been implicated in a number of actions of the kynurenine pathway, including immune evasion by tumors.	Kynurenine	82-92	tryptophan 2,3-dioxygenase	Homo sapiens	0-4
23122865-3	2012	Tdo2 or Ido1 enzymatic activity has been implicated in a number of actions of the kynurenine pathway, including immune evasion by tumors.	Kynurenine	82-92	indoleamine 2,3-dioxygenase 1	Homo sapiens	8-12
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.	Kynurenine	62-72	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.	Kynurenine	62-72	indoleamine 2,3-dioxygenase 1	Homo sapiens	31-35
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.	Kynurenine	74-77	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.	Kynurenine	74-77	indoleamine 2,3-dioxygenase 1	Homo sapiens	31-35
23124849-7	2012	In addition, the lack of the accumulation of kynurenine and its downstream metabolites in the pre-arthritic lymph nodes coincided with increased mRNA expression for genes involved in the catabolism of kynurenine (Kynureninase, kynurenine 3-monooxygenase, and 3-hydroxyanthranilate 3,4 dioxygenase).	Kynurenine	201-211	kynurenine 3-monooxygenase (kynurenine 3-hydroxylase)	Mus musculus	227-282
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).	Kynurenine	78-88	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).	Kynurenine	78-88	indoleamine 2,3-dioxygenase 2	Homo sapiens	43-47
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).	Kynurenine	78-88	indoleamine 2,3-dioxygenase 1	Homo sapiens	163-167
23090118-9	2012	These immunomodulatory effects of kynurenine are mediated by the aryl hydrocarbon receptor.	Kynurenine	34-44	aryl hydrocarbon receptor	Homo sapiens	65-90
22895526-1	2012	Indoleamine 2,3-dioxygenase 1 (IDO1) catabolizes tryptophan to kynurenine at the first step of tryptophan metabolism.	Kynurenine	63-73	indoleamine 2,3-dioxygenase 1	Mus musculus	31-35
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.	Kynurenine	41-44	indoleamine 2,3-dioxygenase 1	Homo sapiens	77-80
22517796-1	2012	The enzyme indoleamine 2,3-dioxygenase (IDO) converts tryptophan into kynurenine metabolites that suppress effector T-cell function.	Kynurenine	70-80	indoleamine 2,3-dioxygenase 1	Mus musculus	40-43
22638210-1	2012	Indoleamine 2,3-dioxygenase-1 (IDO1) is an intracellular enzyme that catalyses essential amino acid tryptophan along the kynurenine pathway.	Kynurenine	121-131	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-29
22638210-1	2012	Indoleamine 2,3-dioxygenase-1 (IDO1) is an intracellular enzyme that catalyses essential amino acid tryptophan along the kynurenine pathway.	Kynurenine	121-131	indoleamine 2,3-dioxygenase 1	Homo sapiens	31-35
23741252-6	2012	Enzymatic activity of IDO, determined by the concentration of L-kynurenine in the culture medium, was also significantly inhibited by EGCG treatment.	Kynurenine	62-74	indoleamine 2,3-dioxygenase 1	Homo sapiens	22-25
25054303-6	2012	Recent evidence points at alternative routes of tryptophan catabolism via tryptophan-2,3-dioxygenase, which is particularly expressed in malignant gliomas resulting in the production of high amounts of kynurenine.	Kynurenine	202-212	tryptophan 2,3-dioxygenase	Homo sapiens	74-100
25054303-7	2012	Tryptophan-2,3-dioxygenase-derived kynurenine in turn leads to the promotion of glioma growth and invasiveness and the suppression of antitumor immune responses by binding to the aryl hydrocarbon receptor expressed in glioma cells and glioma-infiltrating T cells.	Kynurenine	35-45	tryptophan 2,3-dioxygenase	Homo sapiens	0-26
25054303-7	2012	Tryptophan-2,3-dioxygenase-derived kynurenine in turn leads to the promotion of glioma growth and invasiveness and the suppression of antitumor immune responses by binding to the aryl hydrocarbon receptor expressed in glioma cells and glioma-infiltrating T cells.	Kynurenine	35-45	aryl hydrocarbon receptor	Homo sapiens	179-204
22927396-2	2012	Here, we identify tryptophan 2,3-dioxygenase (tdo-2), the first enzyme in the kynurenine pathway of tryptophan degradation, as a metabolic regulator of age-related alpha-synuclein toxicity in a Caenorhabditis elegans model.	Kynurenine	78-88	Tryptophan 2,3-dioxygenase	Caenorhabditis elegans	18-44
22927396-2	2012	Here, we identify tryptophan 2,3-dioxygenase (tdo-2), the first enzyme in the kynurenine pathway of tryptophan degradation, as a metabolic regulator of age-related alpha-synuclein toxicity in a Caenorhabditis elegans model.	Kynurenine	78-88	Tryptophan 2,3-dioxygenase	Caenorhabditis elegans	46-51
22927396-5	2012	Analysis of metabolite levels in C. elegans strains with mutations in enzymes that act downstream of tdo-2 indicates that this suppression of toxicity is independent of downstream metabolites in the kynurenine pathway.	Kynurenine	199-209	Tryptophan 2,3-dioxygenase	Caenorhabditis elegans	101-106
22690733-1	2012	KFase (kynurenine formamidase), also known as arylformamidase and formylkynurenine formamidase, efficiently catalyses the hydrolysis of NFK (N-formyl-L-kynurenine) to kynurenine.	Kynurenine	7-17	Kynurenine formamidase	Drosophila melanogaster	0-5
22690733-2	2012	KFase is the second enzyme in the kynurenine pathway of tryptophan metabolism.	Kynurenine	34-44	Kynurenine formamidase	Drosophila melanogaster	0-5
22690733-9	2012	The present study provides a molecular basis for future efforts in maintaining or regulating kynurenine metabolism through the molecular and biochemical regulation of KFase.	Kynurenine	93-103	Kynurenine formamidase	Drosophila melanogaster	167-172
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.	Kynurenine	169-179	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.	Kynurenine	169-179	indoleamine 2,3-dioxygenase 1	Homo sapiens	57-60
22876244-8	2012	l-kynurenine concentration in conditioned medium (CM) by MSCs with SF was determined as a measure of IDO activity by MSCs.	Kynurenine	0-12	indoleamine 2,3-dioxygenase 1	Homo sapiens	101-104
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.	Kynurenine	189-199	indoleamine 2,3-dioxygenase 1	Homo sapiens	54-58
22504306-8	2012	Interestingly, acute systemic administration of l-kynurenine, the enzymatic product of IDO, precipitated an anhedonic and anxiogenic effect in naive mice without effect on eLMA.	Kynurenine	48-60	indoleamine 2,3-dioxygenase 1	Mus musculus	87-90
22751107-4	2012	Upregulation of IDO1 resulted in the increased kynurenine/tryptophan ratio and decreased serotonin/tryptophan ratio in the bilateral hippocampus.	Kynurenine	47-57	indoleamine 2,3-dioxygenase 1	Rattus norvegicus	16-20
22481272-1	2012	Indoleamine 2,3-dioxygenase (IDO), a metabolic enzyme that catalyzes tryptophan conversion into kynurenines, is a crucial regulator of immunity.	Kynurenine	96-107	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.	Kynurenine	96-107	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.	Kynurenine	4-14	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.	Kynurenine	4-14	indoleamine 2,3-dioxygenase 1	Homo sapiens	106-109
22564706-2	2012	In fungi, the primary role of IDO is to supply nicotinamide adenine dinucleotide (NAD(+)) via the kynurenine pathway.	Kynurenine	98-108	indoleamine 2,3-dioxygenase 1	Homo sapiens	30-33
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.	Kynurenine	104-114	indoleamine 2,3-dioxygenase 1	Homo sapiens	27-56
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.	Kynurenine	104-114	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.	Kynurenine	32-42	indoleamine 2,3-dioxygenase 1	Homo sapiens	73-77
22237484-0	2012	Effects of antidepressants and cyclooxygenase-2 inhibitor on cytokines and kynurenines in stimulated in vitro blood culture from depressed patients.	Kynurenine	75-86	prostaglandin-endoperoxide synthase 2	Homo sapiens	31-47
22471748-10	2012	Although KA and kynurenine are both AHR agonists, these ligands behaved differently in regards to degranulation and IL-6 expression, indicating that they may function outside of AHR pathways.	Kynurenine	16-26	aryl hydrocarbon receptor	Rattus norvegicus	36-39
22535959-1	2012	The obligate intracellular apicomplexan parasites, e.g. Toxoplasma gondii and Plasmodium species, induce an IFNgamma-driven induction of host indoleamine 2,3-dioxygenase (IDO), the first and rate-limiting enzyme of tryptophan catabolism in the kynurenine pathway.	Kynurenine	244-254	interferon gamma	Mus musculus	108-116
22535959-1	2012	The obligate intracellular apicomplexan parasites, e.g. Toxoplasma gondii and Plasmodium species, induce an IFNgamma-driven induction of host indoleamine 2,3-dioxygenase (IDO), the first and rate-limiting enzyme of tryptophan catabolism in the kynurenine pathway.	Kynurenine	244-254	indoleamine 2,3-dioxygenase 1	Mus musculus	171-174
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.	Kynurenine	57-69	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.	Kynurenine	57-69	indoleamine 2,3-dioxygenase 1	Rattus norvegicus	29-32
22344459-8	2012	These results suggest that KYNA levels generated from 20 muM kynurenine inhibit tonically active alpha7 nAChR-dependent GABAergic transmission to the pyramidal neurons.	Kynurenine	61-71	cholinergic receptor nicotinic alpha 4 subunit	Homo sapiens	104-109
22512552-4	2012	Structural comparison between the three most representative families of compounds (kynurenines, kynurenamines and 4,5-dihydro-1H-pyrazole derivatives) allows the establishment of structure-activity relationships for the inhibition of nNOS, and a pharmacophore model that fulfills all of the observed SARs were developed.	Kynurenine	83-94	nitric oxide synthase 1	Rattus norvegicus	234-238
22737628-2	2012	The tryptophan metabolite kynurenine has now been identified as an endogenous ligand of the human AHR constitutively produced by gliomas and other types of cancer via tryptophan-2,3-dioxygenase (TDO), thereby suppressing antitumor immune responses via the AHR.	Kynurenine	26-36	aryl hydrocarbon receptor	Homo sapiens	98-101
22737628-2	2012	The tryptophan metabolite kynurenine has now been identified as an endogenous ligand of the human AHR constitutively produced by gliomas and other types of cancer via tryptophan-2,3-dioxygenase (TDO), thereby suppressing antitumor immune responses via the AHR.	Kynurenine	26-36	tryptophan 2,3-dioxygenase	Homo sapiens	167-193
22737628-2	2012	The tryptophan metabolite kynurenine has now been identified as an endogenous ligand of the human AHR constitutively produced by gliomas and other types of cancer via tryptophan-2,3-dioxygenase (TDO), thereby suppressing antitumor immune responses via the AHR.	Kynurenine	26-36	tryptophan 2,3-dioxygenase	Homo sapiens	195-198
22737628-2	2012	The tryptophan metabolite kynurenine has now been identified as an endogenous ligand of the human AHR constitutively produced by gliomas and other types of cancer via tryptophan-2,3-dioxygenase (TDO), thereby suppressing antitumor immune responses via the AHR.	Kynurenine	26-36	aryl hydrocarbon receptor	Homo sapiens	256-259
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.	Kynurenine	181-191	indoleamine 2,3-dioxygenase 1	Homo sapiens	95-122
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.	Kynurenine	149-159	indoleamine 2,3-dioxygenase 1	Homo sapiens	219-222
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.	Kynurenine	149-159	interferon gamma	Homo sapiens	227-243
22257103-8	2012	Furthermore, our study suggests that IDO activity measured as kynurenine levels could be used as a marker of the response to the chemotherapy treatments, although further studies are necessary.	Kynurenine	62-72	indoleamine 2,3-dioxygenase 1	Homo sapiens	37-40
22422885-1	2012	The activity of IDO that catalyzes the degradation of tryptophan (Trp) into kynurenine (Kyn) increases after diseases caused by different infectious agents.	Kynurenine	76-86	indoleamine 2,3-dioxygenase 1	Mus musculus	16-19
22422885-1	2012	The activity of IDO that catalyzes the degradation of tryptophan (Trp) into kynurenine (Kyn) increases after diseases caused by different infectious agents.	Kynurenine	88-91	indoleamine 2,3-dioxygenase 1	Mus musculus	16-19
22422885-11	2012	Specifically, IDO increases the accumulation of Kyn pathway metabolites, which suppress type I IFNs production and enhance viral replication.	Kynurenine	48-51	indoleamine 2,3-dioxygenase 1	Mus musculus	14-17
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.	Kynurenine	181-191	indoleamine 2,3-dioxygenase 1	Homo sapiens	124-127
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.	Kynurenine	131-134	indoleamine 2,3-dioxygenase 1	Homo sapiens	45-72
22048879-5	2012	Tumor specimens were immunostained for the L: -type amino acid transporter 1 (LAT1) and indoleamine 2,3-dioxygenase (IDO), a key enzyme of the immunomodulatory kynurenine pathway.	Kynurenine	160-170	indoleamine 2,3-dioxygenase 1	Homo sapiens	88-115
22048879-5	2012	Tumor specimens were immunostained for the L: -type amino acid transporter 1 (LAT1) and indoleamine 2,3-dioxygenase (IDO), a key enzyme of the immunomodulatory kynurenine pathway.	Kynurenine	160-170	indoleamine 2,3-dioxygenase 1	Homo sapiens	117-120
22048879-10	2012	These results indicate that accumulation of tryptophan in DNTs is driven by high amino acid transport, mediated by LAT1, which can provide the substrate for tumoral tryptophan metabolism through the kynurenine pathway, that can produce epileptogenic metabolites.	Kynurenine	199-209	solute carrier family 7 member 5	Homo sapiens	115-119
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.	Kynurenine	131-134	indoleamine 2,3-dioxygenase 1	Homo sapiens	74-77
22224417-5	2012	Both of these effects were duplicated by perfusion of 2 muM l-kynurenine.	Kynurenine	60-72	latexin	Homo sapiens	56-59
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.	Kynurenine	143-153	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.	Kynurenine	143-153	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.	Kynurenine	155-158	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.	Kynurenine	155-158	indoleamine 2,3-dioxygenase 1	Homo sapiens	29-32
22219312-6	2012	IDO activity was estimated by calculating the serum Kyn-to-Trp ratio.	Kynurenine	52-55	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-3
22219312-9	2012	The patients who died had significantly higher concentrations of Kyn and significantly lower Trp concentrations, resulting in significantly higher IDO activity (P &lt; 0.0001, P &lt; 0.0001, and P &lt; 0.0001, respectively).	Kynurenine	65-68	indoleamine 2,3-dioxygenase 1	Homo sapiens	147-150
22071871-4	2012	Analysis of the enzymes that regulate the kynurenine pathway showed that IL-1beta induced an upregulation of transcripts for indolamine-2,3-dioxygenase (IDO), kynurenine 3-monooxygenase (KMO), and kynureninase (42-, 12- and 30-fold increase, respectively, under differentiating conditions), the enzymes involved in the neurotoxic arm of the kynurenine pathway.	Kynurenine	42-52	indoleamine 2,3-dioxygenase 1	Homo sapiens	153-156
22071871-4	2012	Analysis of the enzymes that regulate the kynurenine pathway showed that IL-1beta induced an upregulation of transcripts for indolamine-2,3-dioxygenase (IDO), kynurenine 3-monooxygenase (KMO), and kynureninase (42-, 12- and 30-fold increase, respectively, under differentiating conditions), the enzymes involved in the neurotoxic arm of the kynurenine pathway.	Kynurenine	42-52	kynurenine 3-monooxygenase	Homo sapiens	159-185
22071871-4	2012	Analysis of the enzymes that regulate the kynurenine pathway showed that IL-1beta induced an upregulation of transcripts for indolamine-2,3-dioxygenase (IDO), kynurenine 3-monooxygenase (KMO), and kynureninase (42-, 12- and 30-fold increase, respectively, under differentiating conditions), the enzymes involved in the neurotoxic arm of the kynurenine pathway.	Kynurenine	42-52	kynurenine 3-monooxygenase	Homo sapiens	187-190
22071871-4	2012	Analysis of the enzymes that regulate the kynurenine pathway showed that IL-1beta induced an upregulation of transcripts for indolamine-2,3-dioxygenase (IDO), kynurenine 3-monooxygenase (KMO), and kynureninase (42-, 12- and 30-fold increase, respectively, under differentiating conditions), the enzymes involved in the neurotoxic arm of the kynurenine pathway.	Kynurenine	159-169	interleukin 1 beta	Homo sapiens	73-81
22071871-5	2012	Moreover, treatment with IL-1beta resulted in an increase in kynurenine, the catabolic product of IDO-induced tryptophan metabolism.	Kynurenine	61-71	interleukin 1 beta	Homo sapiens	25-33
22282879-1	2012	The essential amino acid tryptophan is the precursor to serotonin, but it can also be metabolized into kynurenine through indoleamine-2,3-dioxygenase (IDO).	Kynurenine	103-113	indoleamine 2,3-dioxygenase 1	Homo sapiens	122-149
22282879-1	2012	The essential amino acid tryptophan is the precursor to serotonin, but it can also be metabolized into kynurenine through indoleamine-2,3-dioxygenase (IDO).	Kynurenine	103-113	indoleamine 2,3-dioxygenase 1	Homo sapiens	151-154
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.	Kynurenine	64-74	indoleamine 2,3-dioxygenase 1	Homo sapiens	27-30
22071871-0	2012	Interleukin-1beta: a new regulator of the kynurenine pathway affecting human hippocampal neurogenesis.	Kynurenine	42-52	interleukin 1 beta	Homo sapiens	0-17
22071871-4	2012	Analysis of the enzymes that regulate the kynurenine pathway showed that IL-1beta induced an upregulation of transcripts for indolamine-2,3-dioxygenase (IDO), kynurenine 3-monooxygenase (KMO), and kynureninase (42-, 12- and 30-fold increase, respectively, under differentiating conditions), the enzymes involved in the neurotoxic arm of the kynurenine pathway.	Kynurenine	42-52	interleukin 1 beta	Homo sapiens	73-81
22071871-4	2012	Analysis of the enzymes that regulate the kynurenine pathway showed that IL-1beta induced an upregulation of transcripts for indolamine-2,3-dioxygenase (IDO), kynurenine 3-monooxygenase (KMO), and kynureninase (42-, 12- and 30-fold increase, respectively, under differentiating conditions), the enzymes involved in the neurotoxic arm of the kynurenine pathway.	Kynurenine	42-52	indoleamine 2,3-dioxygenase 1	Homo sapiens	125-151
22071871-5	2012	Moreover, treatment with IL-1beta resulted in an increase in kynurenine, the catabolic product of IDO-induced tryptophan metabolism.	Kynurenine	61-71	indoleamine 2,3-dioxygenase 1	Homo sapiens	98-101
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.	Kynurenine	174-184	indoleamine 2,3-dioxygenase 1	Homo sapiens	107-134
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.	Kynurenine	151-161	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-29
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.	Kynurenine	151-161	indoleamine 2,3-dioxygenase 1	Homo sapiens	31-36
21744051-3	2012	Indoleamine 2,3-dioxygenase (IDO) occupies a key position connecting the immune system and the kynurenine pathway.	Kynurenine	95-105	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-27
21744051-3	2012	Indoleamine 2,3-dioxygenase (IDO) occupies a key position connecting the immune system and the kynurenine pathway.	Kynurenine	95-105	indoleamine 2,3-dioxygenase 1	Homo sapiens	29-32
21744051-5	2012	Following the interferon (IFN)-mediated activation of antigen presenting cells, the induction of IDO and the kynurenine system exerts a counter-regulating effect, maintaining the homeostasis.	Kynurenine	109-119	interferon alpha 1	Homo sapiens	14-31
22308364-2	2012	Tryptophan 2,3-dioxygenase (TDO) is an unrelated hepatic enzyme that also degrades tryptophan along the kynurenine pathway.	Kynurenine	104-114	tryptophan 2,3-dioxygenase	Mus musculus	0-26
22308364-2	2012	Tryptophan 2,3-dioxygenase (TDO) is an unrelated hepatic enzyme that also degrades tryptophan along the kynurenine pathway.	Kynurenine	104-114	tryptophan 2,3-dioxygenase	Mus musculus	28-31
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.	Kynurenine	174-184	indoleamine 2,3-dioxygenase 1	Homo sapiens	136-139
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).	Kynurenine	145-155	indoleamine 2,3-dioxygenase 1	Homo sapiens	168-195
22108572-3	2012	The uptake of p-aminohippurate in hOAT1-expressing oocytes and of estrone sulfate in hOAT3-expressing oocytes was strongly inhibited by kynurenic acid, and other tryptophan catabolites, kynurenine and quinolinic acid, showed moderate and no inhibition, respectively.	Kynurenine	186-196	solute carrier family 22 member 8	Homo sapiens	85-90
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.	Kynurenine	158-168	indoleamine 2,3-dioxygenase 1	Homo sapiens	61-64
22963664-1	2012	The enzyme indoleamine 2,3-dioxygenase 1 (IDO1) finely regulates both innate and adaptive immune responses through the degradation of the essential amino acid tryptophan into kynurenine and other downstream metabolites, which suppress effector T-cell function and promote the differentiation of regulatory T cells.	Kynurenine	175-185	indoleamine 2,3-dioxygenase 1	Homo sapiens	11-40
22963664-1	2012	The enzyme indoleamine 2,3-dioxygenase 1 (IDO1) finely regulates both innate and adaptive immune responses through the degradation of the essential amino acid tryptophan into kynurenine and other downstream metabolites, which suppress effector T-cell function and promote the differentiation of regulatory T cells.	Kynurenine	175-185	indoleamine 2,3-dioxygenase 1	Homo sapiens	42-46
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.	Kynurenine	117-127	indoleamine 2,3-dioxygenase 1	Homo sapiens	17-20
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.	Kynurenine	214-224	indoleamine 2,3-dioxygenase 1	Homo sapiens	61-64
23300346-12	2012	Correlation analyses between kynurenine parameters revealed association between high ratio KAT I/KAT II and increased kynurenic acid level and lower L-kynurenine in the frontal cortex and cerebellum of HIV and LY subgroups.	Kynurenine	29-39	kynurenine aminotransferase 1	Homo sapiens	91-103
23300346-12	2012	Correlation analyses between kynurenine parameters revealed association between high ratio KAT I/KAT II and increased kynurenic acid level and lower L-kynurenine in the frontal cortex and cerebellum of HIV and LY subgroups.	Kynurenine	149-161	kynurenine aminotransferase 1	Homo sapiens	91-103
22693634-7	2012	Furthermore, we show that LXA4- and L-kynurenine-induced AhR activation, its subsequent nuclear translocation, leading SOCS2 expression and TRAF6 Lys47-linked poly-ubiquitination and proteosome-mediated degradation of the adapter proteins.	Kynurenine	36-48	TNF receptor associated factor 6	Homo sapiens	140-145
21693093-2	2012	This compound is an end-metabolite of the kynurenine pathway, and its formation indirectly depends on the activity of kynurenine 3-monooxygenase (KMO), the enzyme converting kynurenine to 3-hydroxykynurenine.	Kynurenine	42-52	kynurenine 3-monooxygenase	Homo sapiens	118-144
21693093-2	2012	This compound is an end-metabolite of the kynurenine pathway, and its formation indirectly depends on the activity of kynurenine 3-monooxygenase (KMO), the enzyme converting kynurenine to 3-hydroxykynurenine.	Kynurenine	42-52	kynurenine 3-monooxygenase	Homo sapiens	146-149
21693093-2	2012	This compound is an end-metabolite of the kynurenine pathway, and its formation indirectly depends on the activity of kynurenine 3-monooxygenase (KMO), the enzyme converting kynurenine to 3-hydroxykynurenine.	Kynurenine	118-128	kynurenine 3-monooxygenase	Homo sapiens	146-149
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.	Kynurenine	95-107	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.	Kynurenine	95-107	indoleamine 2,3-dioxygenase 1	Homo sapiens	48-51
21835273-1	2011	Indoleamine 2,3-dioxygenase (IDO1) catalyzes the first step in tryptophan breakdown along the kynurenine pathway.	Kynurenine	94-104	indoleamine 2,3-dioxygenase 1	Homo sapiens	29-33
22693634-6	2012	We demonstrate that Tumor necrosis factor receptor-associated factor (TRAF)6--member of a family of adapter molecules that couple the TNF receptor and interleukin-1 receptor/Toll-like receptor families to intracellular signaling events essential for the development of immune responses--is targeted by both lipoxins and L-kynurenine via an AhR/SOCS2-dependent pathway.	Kynurenine	320-332	TNF receptor associated factor 6	Homo sapiens	70-76
22693634-6	2012	We demonstrate that Tumor necrosis factor receptor-associated factor (TRAF)6--member of a family of adapter molecules that couple the TNF receptor and interleukin-1 receptor/Toll-like receptor families to intracellular signaling events essential for the development of immune responses--is targeted by both lipoxins and L-kynurenine via an AhR/SOCS2-dependent pathway.	Kynurenine	320-332	aryl hydrocarbon receptor	Homo sapiens	340-343
22693634-6	2012	We demonstrate that Tumor necrosis factor receptor-associated factor (TRAF)6--member of a family of adapter molecules that couple the TNF receptor and interleukin-1 receptor/Toll-like receptor families to intracellular signaling events essential for the development of immune responses--is targeted by both lipoxins and L-kynurenine via an AhR/SOCS2-dependent pathway.	Kynurenine	320-332	suppressor of cytokine signaling 2	Homo sapiens	344-349
22693634-7	2012	Furthermore, we show that LXA4- and L-kynurenine-induced AhR activation, its subsequent nuclear translocation, leading SOCS2 expression and TRAF6 Lys47-linked poly-ubiquitination and proteosome-mediated degradation of the adapter proteins.	Kynurenine	36-48	aryl hydrocarbon receptor	Homo sapiens	57-60
22693634-7	2012	Furthermore, we show that LXA4- and L-kynurenine-induced AhR activation, its subsequent nuclear translocation, leading SOCS2 expression and TRAF6 Lys47-linked poly-ubiquitination and proteosome-mediated degradation of the adapter proteins.	Kynurenine	36-48	suppressor of cytokine signaling 2	Homo sapiens	119-124
22693634-10	2012	In summary, our results establish proteasome degradation of TRAF6 as a key molecular target for the anti-inflammatory pathway triggered by lipoxins and L-kynurenine, critical counter-regulatory mediators in the innate and adaptive immune systems.	Kynurenine	152-164	TNF receptor associated factor 6	Homo sapiens	60-65
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.	Kynurenine	109-119	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.	Kynurenine	109-119	indoleamine 2,3-dioxygenase 1	Homo sapiens	42-45
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.	Kynurenine	93-103	indoleamine 2,3-dioxygenase 1	Homo sapiens	12-41
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).	Kynurenine	144-154	interferon gamma	Homo sapiens	46-62
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).	Kynurenine	144-154	interferon gamma	Homo sapiens	64-68
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).	Kynurenine	144-154	indoleamine 2,3-dioxygenase 1	Homo sapiens	200-203
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).	Kynurenine	156-159	interferon gamma	Homo sapiens	46-62
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).	Kynurenine	156-159	interferon gamma	Homo sapiens	64-68
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).	Kynurenine	156-159	indoleamine 2,3-dioxygenase 1	Homo sapiens	200-203
22396896-3	2011	Activation of IDO shunts TRY metabolism from production of serotonin (substrate of antidepressant effect) and its derivatives: N-acetylserotonin (an agonist to the receptors of brain derived neurotropic factor), and melatonin (regulator of sleep and other circadian rhythms), towards production of KYN and its derivatives (anxiogenic, neurotoxic and pro-oxidant factors).	Kynurenine	298-301	indoleamine 2,3-dioxygenase 1	Homo sapiens	14-17
22396896-4	2011	Some of kynurenines up-regulate nitric oxide synthase (NOS).	Kynurenine	8-19	nitric oxide synthase 2	Homo sapiens	32-53
22018876-3	2011	Selectivity of these compounds against IDO and TDO, two enzymes sharing substrate similarity with MAO and involved in the serotonergic and kynurenine pathways was also studied.	Kynurenine	139-149	indoleamine 2,3-dioxygenase 1	Homo sapiens	39-42
21952237-6	2011	The activity of IDO was also increased by poly(I:C) given that the L-kynurenine concentrations were elevated in conditioned media.	Kynurenine	67-79	indoleamine 2,3-dioxygenase 1	Homo sapiens	16-19
22018876-3	2011	Selectivity of these compounds against IDO and TDO, two enzymes sharing substrate similarity with MAO and involved in the serotonergic and kynurenine pathways was also studied.	Kynurenine	139-149	tryptophan 2,3-dioxygenase	Homo sapiens	47-50
21896552-0	2011	Tryptophan in alcoholism treatment I: kynurenine metabolites inhibit the rat liver mitochondrial low Km aldehyde dehydrogenase activity, elevate blood acetaldehyde concentration and induce aversion to alcohol.	Kynurenine	38-48	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	104-126
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.	Kynurenine	74-84	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.	Kynurenine	74-84	indoleamine 2,3-dioxygenase 1	Homo sapiens	29-32
21896552-1	2011	AIMS: The aims were to provide proofs of mechanism and principle by establishing the ability of kynurenine metabolites to inhibit the liver mitochondrial low K(m) aldehyde dehydrogenase (ALDH) activity after administration and in vivo, and to induce aversion to alcohol.	Kynurenine	96-106	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	163-185
21896552-1	2011	AIMS: The aims were to provide proofs of mechanism and principle by establishing the ability of kynurenine metabolites to inhibit the liver mitochondrial low K(m) aldehyde dehydrogenase (ALDH) activity after administration and in vivo, and to induce aversion to alcohol.	Kynurenine	96-106	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	187-191
21896552-7	2011	CONCLUSIONS: The above kynurenine metabolites of tryptophan induce aversion to alcohol by inhibiting ALDH activity.	Kynurenine	23-33	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	101-105
21711334-9	2011	Addition of CXCL11 upregulated IDO2 and increased l-kynurenine concentration in a dose-dependent manner in hBCCs while normal primary keratinocytes exhibited no response.	Kynurenine	50-62	C-X-C motif chemokine ligand 11	Homo sapiens	12-18
21711334-10	2011	CONCLUSIONS: The expression of IDO at both mRNA and protein levels in hBCC tissues, the upregulation of IDO2 and the IDO-mediated l-kynurenine production in hBCCs with CXCL11 treatment suggest that functional IDO is synthesized by hBCC tumours and may be used as a method of immunoprotection during tumorigenesis.	Kynurenine	130-142	C-X-C motif chemokine ligand 11	Homo sapiens	168-174
22202242-2	2011	IDO activity can be measured by kynurenine( Kyn)/tryptophan (Trp) ratio.	Kynurenine	32-42	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-3
22202242-2	2011	IDO activity can be measured by kynurenine( Kyn)/tryptophan (Trp) ratio.	Kynurenine	44-47	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-3
22108404-0	2011	A small-molecule screen identifies L-kynurenine as a competitive inhibitor of TAA1/TAR activity in ethylene-directed auxin biosynthesis and root growth in Arabidopsis.	Kynurenine	35-47	tryptophan aminotransferase of Arabidopsis 1	Arabidopsis thaliana	78-82
21911470-2	2011	IDO1 depletes tryptophan by catabolizing it to kynurenine with consequences for C. trachomatis, which is a tryptophan auxotroph.	Kynurenine	47-57	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-4
22108404-5	2011	Moreover, Kyn application decreased ethylene-induced auxin biosynthesis in roots, and TRYPTOPHAN AMINOTRANSFERASE OF ARABIDOPSIS1/TRYPTOPHAN AMINOTRANSFERASE RELATEDs (TAA1/TARs), the key enzymes in the indole-3-pyruvic acid pathway of auxin biosynthesis, were identified as the molecular targets of Kyn.	Kynurenine	10-13	tryptophan aminotransferase of Arabidopsis 1	Arabidopsis thaliana	168-172
22108404-6	2011	Further biochemical and phenotypic analyses revealed that Kyn, being an alternate substrate, competitively inhibits TAA1/TAR activity, and Kyn treatment mimicked the loss of TAA1/TAR functions.	Kynurenine	58-61	tryptophan aminotransferase of Arabidopsis 1	Arabidopsis thaliana	116-120
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.	Kynurenine	62-74	indoleamine 2,3-dioxygenase 1	Rattus norvegicus	0-27
21976023-3	2011	Here we identify the tryptophan (Trp) catabolite kynurenine (Kyn) as an endogenous ligand of the human AHR that is constitutively generated by human tumour cells via tryptophan-2,3-dioxygenase (TDO), a liver- and neuron-derived Trp-degrading enzyme not yet implicated in cancer biology.	Kynurenine	49-59	aryl hydrocarbon receptor	Homo sapiens	103-106
21976023-3	2011	Here we identify the tryptophan (Trp) catabolite kynurenine (Kyn) as an endogenous ligand of the human AHR that is constitutively generated by human tumour cells via tryptophan-2,3-dioxygenase (TDO), a liver- and neuron-derived Trp-degrading enzyme not yet implicated in cancer biology.	Kynurenine	49-59	tryptophan 2,3-dioxygenase	Homo sapiens	166-192
21976023-3	2011	Here we identify the tryptophan (Trp) catabolite kynurenine (Kyn) as an endogenous ligand of the human AHR that is constitutively generated by human tumour cells via tryptophan-2,3-dioxygenase (TDO), a liver- and neuron-derived Trp-degrading enzyme not yet implicated in cancer biology.	Kynurenine	49-59	tryptophan 2,3-dioxygenase	Homo sapiens	194-197
21976023-3	2011	Here we identify the tryptophan (Trp) catabolite kynurenine (Kyn) as an endogenous ligand of the human AHR that is constitutively generated by human tumour cells via tryptophan-2,3-dioxygenase (TDO), a liver- and neuron-derived Trp-degrading enzyme not yet implicated in cancer biology.	Kynurenine	61-64	aryl hydrocarbon receptor	Homo sapiens	103-106
21976023-3	2011	Here we identify the tryptophan (Trp) catabolite kynurenine (Kyn) as an endogenous ligand of the human AHR that is constitutively generated by human tumour cells via tryptophan-2,3-dioxygenase (TDO), a liver- and neuron-derived Trp-degrading enzyme not yet implicated in cancer biology.	Kynurenine	61-64	tryptophan 2,3-dioxygenase	Homo sapiens	166-192
21976023-3	2011	Here we identify the tryptophan (Trp) catabolite kynurenine (Kyn) as an endogenous ligand of the human AHR that is constitutively generated by human tumour cells via tryptophan-2,3-dioxygenase (TDO), a liver- and neuron-derived Trp-degrading enzyme not yet implicated in cancer biology.	Kynurenine	61-64	tryptophan 2,3-dioxygenase	Homo sapiens	194-197
21976023-6	2011	Because Kyn is produced during cancer progression and inflammation in the local microenvironment in amounts sufficient for activating the human AHR, these results provide evidence for a previously unidentified pathophysiological function of the AHR with profound implications for cancer and immune biology.	Kynurenine	8-11	aryl hydrocarbon receptor	Homo sapiens	144-147
21976023-6	2011	Because Kyn is produced during cancer progression and inflammation in the local microenvironment in amounts sufficient for activating the human AHR, these results provide evidence for a previously unidentified pathophysiological function of the AHR with profound implications for cancer and immune biology.	Kynurenine	8-11	aryl hydrocarbon receptor	Homo sapiens	245-248
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).	Kynurenine	14-24	indoleamine 2,3-dioxygenase 1	Rattus norvegicus	0-3
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.	Kynurenine	62-74	indoleamine 2,3-dioxygenase 1	Rattus norvegicus	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.	Kynurenine	21-31	indoleamine 2,3-dioxygenase 1	Homo sapiens	65-92
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.	Kynurenine	161-171	indoleamine 2,3-dioxygenase 1	Homo sapiens	29-32
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.	Kynurenine	161-171	tryptophan 2,3-dioxygenase	Homo sapiens	66-69
21742032-1	2011	The anti-proliferative and immunomodulatory enzyme indoleamine 2,3-dioxygenase (IDO) degrades the essential amino acid tryptophan via the kynurenine pathway.	Kynurenine	138-148	indoleamine 2,3-dioxygenase 1	Homo sapiens	51-78
21784100-1	2011	OBJECTIVES: Indoleamine 2,3-dioxygenase (IDO) catalyzes the rate-limiting step of tryptophan (Trp) degradation in the kynurenine (Kyn) pathway.	Kynurenine	118-128	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.	Kynurenine	118-128	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.	Kynurenine	130-133	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.	Kynurenine	130-133	indoleamine 2,3-dioxygenase 1	Homo sapiens	41-44
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.	Kynurenine	78-81	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.	Kynurenine	96-99	indoleamine 2,3-dioxygenase 1	Homo sapiens	50-53
21742032-1	2011	The anti-proliferative and immunomodulatory enzyme indoleamine 2,3-dioxygenase (IDO) degrades the essential amino acid tryptophan via the kynurenine pathway.	Kynurenine	138-148	indoleamine 2,3-dioxygenase 1	Homo sapiens	80-83
21742032-3	2011	IDO activity is estimated by calculating the kynurenine to tryptophan ratio (Kyn/Trp).	Kynurenine	45-55	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).	Kynurenine	77-80	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-3
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.	Kynurenine	69-79	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-27
21742973-1	2011	IDO is the rate-limiting enzyme in the kynurenine pathway, catabolizing tryptophan to kynurenine.	Kynurenine	39-49	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.	Kynurenine	86-96	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-3
21352963-2	2011	Here we demonstrate the pro-apoptotic effect of L-kynurenine, a tryptophan catabolite of IDO, on human NK cell line, NK92 MI.	Kynurenine	48-60	indoleamine 2,3-dioxygenase 1	Homo sapiens	89-92
21352963-4	2011	Treatment with the antioxidant NAC completely protected cells from L-kynurenine-induced apoptosis.	Kynurenine	67-79	synuclein alpha	Homo sapiens	31-34
21352963-6	2011	We observed that the presence of NAC blocks cytochrome c release and activation of caspase-3 during L-kynurenine-induced apoptosis.	Kynurenine	100-112	synuclein alpha	Homo sapiens	33-36
21352963-6	2011	We observed that the presence of NAC blocks cytochrome c release and activation of caspase-3 during L-kynurenine-induced apoptosis.	Kynurenine	100-112	caspase 3	Homo sapiens	83-92
21352963-7	2011	Overall, we conclude that L-kynurenine resulting from IDO can cause cell death via ROS pathway in NK cells.	Kynurenine	26-38	indoleamine 2,3-dioxygenase 1	Homo sapiens	54-57
21683717-7	2011	These effects functionally correlated with changes in IDO1 activity: l-kynurenine contents in the culture media were significantly reduced by C16:0 sulfatide (-29 +- 4% at 0.01muM), while it was increased by C18:0 or C24:1 sulfatide (+61 +- 8% and +48 +- 4% at 1muM, respectively) over negative controls.	Kynurenine	69-81	indoleamine 2,3-dioxygenase 1	Homo sapiens	54-58
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.	Kynurenine	69-79	indoleamine 2,3-dioxygenase 1	Homo sapiens	29-32
21476605-4	2011	Three metabolites, indoxyl sulfate, kynurenine, and xanthurenic acid, were elevated in the plasma and interacted strongly and directly with Oat1 in vitro with IC50 of 18, 12, and 50 muM, respectively.	Kynurenine	36-46	solute carrier family 22 (organic anion transporter), member 6	Mus musculus	140-144
21858269-2	2011	Indoleamine 2,3-dioxygenase (IDO) is an enzyme expressed in many cells involved in the catabolism of the essential amino acid tryptophan to kynurenine.	Kynurenine	140-150	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-27
21858269-2	2011	Indoleamine 2,3-dioxygenase (IDO) is an enzyme expressed in many cells involved in the catabolism of the essential amino acid tryptophan to kynurenine.	Kynurenine	140-150	indoleamine 2,3-dioxygenase 1	Homo sapiens	29-32
21277567-8	2011	Increased inflammation was related to reduced tryptophan concentrations and increased kynurenine levels, suggestive of IDO-induced increased tryptophan catabolism.	Kynurenine	86-96	indoleamine 2,3-dioxygenase 1	Homo sapiens	119-122
21727251-3	2011	The proximal cause may be an impairment of kynurenine 3-monooxygenase (KMO), a rate-limiting enzyme at the branching point of the kynurenine pathway.	Kynurenine	43-53	kynurenine 3-monooxygenase	Homo sapiens	71-74
22308202-9	2011	PLP is a cofactor of IFNG-induced key enzymes of tryptophan-kynurenine metabolism.	Kynurenine	60-70	pyridoxal phosphatase	Homo sapiens	0-3
21402064-5	2011	RESULTS: Metabolic profiling revealed that kynurenine, N-acetylglucosaminylamine, N-acetylglucosamine and hydroxyphenylpyruvate increased in NPC patient sera.	Kynurenine	43-53	NPC intracellular cholesterol transporter 1	Homo sapiens	141-144
21402064-10	2011	CONCLUSION: The results reveal that kynurenine, N-acetylglucosaminylamine, N-acetylglucosamine and hydroxyphenylpyruvate are potentially markers of NPC for diagnosis and therapy.	Kynurenine	36-46	NPC intracellular cholesterol transporter 1	Homo sapiens	148-151
21439022-4	2011	The transamination and the beta-lytic activity of KATII towards the substrates kynurenine and alpha-aminoadipate, the substrate analog beta-chloroalanine and the inhibitors (R)-2-amino-4-(4-(ethylsulfonyl))-4-oxobutanoic acid and cysteine sulfinate were investigated with both conventional assays and a novel continuous spectrophotometric assay.	Kynurenine	79-89	aminoadipate aminotransferase	Homo sapiens	50-55
22308202-9	2011	PLP is a cofactor of IFNG-induced key enzymes of tryptophan-kynurenine metabolism.	Kynurenine	60-70	interferon gamma	Homo sapiens	21-25
22308202-10	2011	Since PLP deficiency is associated with the increased production of diabetogenic kynurenine derivative, xanthurenic acid, our results suggest that up-regulated IFNG production might contribute to the development of insulin resistance.	Kynurenine	81-91	pyridoxal phosphatase	Homo sapiens	6-9
21270133-1	2011	In the mouse hippocampus normal levels of kynurenic acid (KYNA), a neuroactive metabolite synthesized in astrocytes primarily by kynurenine aminotransferase II (KAT II)-catalyzed transamination of L-kynurenine, maintain a degree of tonic inhibition of alpha7 nicotinic acetylcholine receptors (nAChRs).	Kynurenine	197-209	aminoadipate aminotransferase	Mus musculus	129-159
21110987-3	2011	In the present work, we showed that GPR35 is present in the dorsal root ganglia and in the spinal cord and in order to test the hypothesis that GPR35 activation could cause analgesia, we administered suitable doses of zaprinast or we increased the local concentration of KYNA by administering a precursor (kynurenine) or by inhibiting its disposal from the CNS (with probenecid).	Kynurenine	306-316	G protein-coupled receptor 35	Mus musculus	36-41
21270133-1	2011	In the mouse hippocampus normal levels of kynurenic acid (KYNA), a neuroactive metabolite synthesized in astrocytes primarily by kynurenine aminotransferase II (KAT II)-catalyzed transamination of L-kynurenine, maintain a degree of tonic inhibition of alpha7 nicotinic acetylcholine receptors (nAChRs).	Kynurenine	197-209	aminoadipate aminotransferase	Mus musculus	161-167
21270133-4	2011	Kynurenine conversion to KYNA was significantly decreased by the KAT II inhibitor (S)-(-)-9-(4-aminopiperazine-1-yl)-8-fluoro-3-methyl-6-oxo-2,3,5,6-tetrahydro-4H-1-oxa-3a-azaphenalene-5carboxylic acid (BFF122) (100 muM) and was more effective in slices from postweaned than preweaned rats.	Kynurenine	0-10	aminoadipate aminotransferase	Mus musculus	65-71
21270133-5	2011	Incubation of slices from postweaned rats with kynurenine inhibited alpha7 nAChRs and extrasynaptic N-methyl-D-aspartate receptors (NMDARs) on CA1 stratum radiatum interneurons.	Kynurenine	47-57	carbonic anhydrase 1	Rattus norvegicus	143-146
21419832-5	2011	The four kynurenines assayed counteracted the effects of MPTP, reducing iNOS/i-mtNOS activity, and restoring the activity of the complex I. Consequently, the cytosolic and mitochondrial oxidative/nitrosative stress returned to control values.	Kynurenine	9-20	nitric oxide synthase 2, inducible	Mus musculus	72-76
21212175-10	2011	CONCLUSIONS: The production of kynurenines, in particular 3HK and 3HAA, may be one mechanism (in addition to tryptophan depletion) by which IDO prolongs graft survival.	Kynurenine	31-42	indoleamine 2,3-dioxygenase 1	Mus musculus	140-143
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).	Kynurenine	161-171	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).	Kynurenine	161-171	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).	Kynurenine	173-176	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).	Kynurenine	173-176	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).	Kynurenine	192-195	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).	Kynurenine	192-195	indoleamine 2,3-dioxygenase 1	Homo sapiens	97-100
21377330-4	2011	METHODS: Kynurenine (kyn)/trp serum ratio, as an indicator of IDO activity was analyzed in 271 carefully classified epilepsy patients, and 309 healthy adults.	Kynurenine	9-19	indoleamine 2,3-dioxygenase 1	Homo sapiens	62-65
21277902-9	2011	Furthermore, IL-18 significantly reduced L-kynurenine-induced down-regulation of NKG2D expression in NK cells.	Kynurenine	41-53	interleukin 18	Homo sapiens	13-18
21277902-9	2011	Furthermore, IL-18 significantly reduced L-kynurenine-induced down-regulation of NKG2D expression in NK cells.	Kynurenine	41-53	killer cell lectin like receptor K1	Homo sapiens	81-86
21359968-1	2011	Indoleamine 2,3-dioxygenases-1 (Ido1) and -2 initiate the kynurenine pathway of tryptophan metabolism.	Kynurenine	58-68	indoleamine 2,3-dioxygenase 1	Mus musculus	0-30
21359968-1	2011	Indoleamine 2,3-dioxygenases-1 (Ido1) and -2 initiate the kynurenine pathway of tryptophan metabolism.	Kynurenine	58-68	indoleamine 2,3-dioxygenase 1	Mus musculus	32-36
21359968-9	2011	In addition, Ido activity was estimated by plasma kynurenine and tryptophan, and Ido1 expression was examined in cerebral arterioles.	Kynurenine	50-60	indoleamine 2,3-dioxygenase 1	Mus musculus	13-16
21277902-6	2011	Incubation with L-kynurenine, an IDO metabolite, down-modulated NKG2D expression in NK cells in a dose- and time-dependent manner.	Kynurenine	16-28	indoleamine 2,3-dioxygenase 1	Homo sapiens	33-36
21277902-6	2011	Incubation with L-kynurenine, an IDO metabolite, down-modulated NKG2D expression in NK cells in a dose- and time-dependent manner.	Kynurenine	16-28	killer cell lectin like receptor K1	Homo sapiens	64-69
21277902-8	2011	In addition, we observed that the effect of L-kynurenine was blocked by JNK agonist, anisomycin, suggesting the involvement of the JNK pathway in the signal transduction of L-kynurenine-reduced NKG2D expression.	Kynurenine	44-56	mitogen-activated protein kinase 8	Homo sapiens	72-75
21277902-8	2011	In addition, we observed that the effect of L-kynurenine was blocked by JNK agonist, anisomycin, suggesting the involvement of the JNK pathway in the signal transduction of L-kynurenine-reduced NKG2D expression.	Kynurenine	44-56	mitogen-activated protein kinase 8	Homo sapiens	131-134
21277902-8	2011	In addition, we observed that the effect of L-kynurenine was blocked by JNK agonist, anisomycin, suggesting the involvement of the JNK pathway in the signal transduction of L-kynurenine-reduced NKG2D expression.	Kynurenine	44-56	killer cell lectin like receptor K1	Homo sapiens	194-199
21277902-8	2011	In addition, we observed that the effect of L-kynurenine was blocked by JNK agonist, anisomycin, suggesting the involvement of the JNK pathway in the signal transduction of L-kynurenine-reduced NKG2D expression.	Kynurenine	173-185	mitogen-activated protein kinase 8	Homo sapiens	72-75
21277902-8	2011	In addition, we observed that the effect of L-kynurenine was blocked by JNK agonist, anisomycin, suggesting the involvement of the JNK pathway in the signal transduction of L-kynurenine-reduced NKG2D expression.	Kynurenine	173-185	mitogen-activated protein kinase 8	Homo sapiens	131-134
21277902-8	2011	In addition, we observed that the effect of L-kynurenine was blocked by JNK agonist, anisomycin, suggesting the involvement of the JNK pathway in the signal transduction of L-kynurenine-reduced NKG2D expression.	Kynurenine	173-185	killer cell lectin like receptor K1	Homo sapiens	194-199
21189261-4	2011	In the caput epididymis of Ido1(-/-) animals, the lack of IDO activity was not compensated by other tryptophan-catabolizing enzymes and led to the loss of kynurenine production.	Kynurenine	155-165	indoleamine 2,3-dioxygenase 1	Homo sapiens	58-61
21328391-6	2011	The kynurenine to tryptophan (kyn/trp) ratio reflecting IDO activity was calculated.	Kynurenine	4-14	indoleamine 2,3-dioxygenase 1	Homo sapiens	56-59
21328391-6	2011	The kynurenine to tryptophan (kyn/trp) ratio reflecting IDO activity was calculated.	Kynurenine	4-7	indoleamine 2,3-dioxygenase 1	Homo sapiens	56-59
21328391-8	2011	A maximum kyn/trp ratio &gt;202 micromol/mmol (high IDO level) was also associated with other parameters reflecting the severity of the disease and renal impairment.	Kynurenine	10-13	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&lt;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&lt;0.001) compared to patients with kyn/trp ratio &lt;= 202 micromol/mmol.	Kynurenine	253-256	indoleamine 2,3-dioxygenase 1	Homo sapiens	19-22
21392042-1	2011	Tryptophan catabolism via the kynurenine pathway is dependent on the enzyme Indoleamine 2,3-dioxygenase (IDO).	Kynurenine	30-40	indoleamine 2,3-dioxygenase 1	Mus musculus	76-103
21392042-1	2011	Tryptophan catabolism via the kynurenine pathway is dependent on the enzyme Indoleamine 2,3-dioxygenase (IDO).	Kynurenine	30-40	indoleamine 2,3-dioxygenase 1	Mus musculus	105-108
21189261-1	2011	Indoleamine 2,3-dioxygenase (IDO) is the first and rate-limiting enzyme of tryptophan catabolism through the kynurenine pathway.	Kynurenine	109-119	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.	Kynurenine	114-124	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.	Kynurenine	109-119	indoleamine 2,3-dioxygenase 1	Homo sapiens	29-32
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.	Kynurenine	114-124	indoleamine 2,3-dioxygenase 1	Homo sapiens	29-32
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.	Kynurenine	161-171	indoleamine 2,3-dioxygenase 1	Homo sapiens	230-233
21183733-2	2011	In activated macrophages, IFN-gamma stimulates production of neopterin and conversion of tryptophan to kynurenine.	Kynurenine	103-113	interferon gamma	Homo sapiens	26-35
21517752-1	2011	The enzyme indoleamine 2,3-dioxygenase 1 (IDO1) degrades the essential amino acid tryptophan into kynurenine and other downstream metabolites that suppress effector T-cell function and favor the differentiation of regulatory T cells.	Kynurenine	98-108	indoleamine 2,3-dioxygenase 1	Homo sapiens	11-40
20822828-5	2011	Kyn/trp correlated strongly with concentrations of cytokine IL-6, of soluble interleukin-2 receptor-alpha and 75 kDa TNF-alpha receptor and of the macrophage marker neopterin (all p&lt;0.001 or p&lt;0.01) but not with TNF-alpha.	Kynurenine	0-3	interleukin 6	Homo sapiens	60-64
20822828-5	2011	Kyn/trp correlated strongly with concentrations of cytokine IL-6, of soluble interleukin-2 receptor-alpha and 75 kDa TNF-alpha receptor and of the macrophage marker neopterin (all p&lt;0.001 or p&lt;0.01) but not with TNF-alpha.	Kynurenine	0-3	interleukin 2 receptor subunit alpha	Homo sapiens	77-105
20822828-5	2011	Kyn/trp correlated strongly with concentrations of cytokine IL-6, of soluble interleukin-2 receptor-alpha and 75 kDa TNF-alpha receptor and of the macrophage marker neopterin (all p&lt;0.001 or p&lt;0.01) but not with TNF-alpha.	Kynurenine	0-3	tumor necrosis factor	Homo sapiens	117-126
20822828-5	2011	Kyn/trp correlated strongly with concentrations of cytokine IL-6, of soluble interleukin-2 receptor-alpha and 75 kDa TNF-alpha receptor and of the macrophage marker neopterin (all p&lt;0.001 or p&lt;0.01) but not with TNF-alpha.	Kynurenine	0-3	tumor necrosis factor	Homo sapiens	218-227
20825285-6	2011	Furthermore, IDO gene transfer led to decreased infiltrating CD4+ T cells with enhanced apoptosis, reduced CD68+ macrophage numbers, increased kynurenine levels, lower IL-17 concentrations, and decreased RORgammat expression within the ankle joints.	Kynurenine	143-153	indoleamine 2,3-dioxygenase 1	Rattus norvegicus	13-16
20825285-8	2011	Our results demonstrate for the first time that intra-articular delivery of IDO gene ameliorated ankle arthritis of CIA rats by induction of CD4+ T-cell apoptosis and reduction of synovial IL-17 production through the supplement of kynurenine.	Kynurenine	232-242	indoleamine 2,3-dioxygenase 1	Rattus norvegicus	76-79
20825285-8	2011	Our results demonstrate for the first time that intra-articular delivery of IDO gene ameliorated ankle arthritis of CIA rats by induction of CD4+ T-cell apoptosis and reduction of synovial IL-17 production through the supplement of kynurenine.	Kynurenine	232-242	interleukin 17A	Rattus norvegicus	189-194
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.	Kynurenine	111-121	interferon gamma	Homo sapiens	0-4
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.	Kynurenine	111-121	interferon alpha 1	Homo sapiens	9-18
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.	Kynurenine	111-121	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.	Kynurenine	111-121	indoleamine 2,3-dioxygenase 1	Homo sapiens	73-76
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.	Kynurenine	123-126	interferon gamma	Homo sapiens	0-4
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.	Kynurenine	123-126	interferon alpha 1	Homo sapiens	9-18
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.	Kynurenine	123-126	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.	Kynurenine	123-126	indoleamine 2,3-dioxygenase 1	Homo sapiens	73-76
21161299-9	2011	IFN-induced up-regulation of IDO triggers depression by shifting TRY metabolism from formation of serotonin to production of neuroactive kynurenines.	Kynurenine	137-148	interferon alpha 1	Homo sapiens	0-3
21161299-9	2011	IFN-induced up-regulation of IDO triggers depression by shifting TRY metabolism from formation of serotonin to production of neuroactive kynurenines.	Kynurenine	137-148	indoleamine 2,3-dioxygenase 1	Homo sapiens	29-32
21517752-1	2011	The enzyme indoleamine 2,3-dioxygenase 1 (IDO1) degrades the essential amino acid tryptophan into kynurenine and other downstream metabolites that suppress effector T-cell function and favor the differentiation of regulatory T cells.	Kynurenine	98-108	indoleamine 2,3-dioxygenase 1	Homo sapiens	42-46
21517752-7	2011	Pharmacological blockade of COX-2 in animal models of cancer translates into down-regulation of IDO1 expression at tumor sites and decreased levels of kynurenine in the circulation, underpinning the view that IDO1 might be downstream of COX-2.	Kynurenine	151-161	mitochondrially encoded cytochrome c oxidase II	Homo sapiens	28-33
21517752-7	2011	Pharmacological blockade of COX-2 in animal models of cancer translates into down-regulation of IDO1 expression at tumor sites and decreased levels of kynurenine in the circulation, underpinning the view that IDO1 might be downstream of COX-2.	Kynurenine	151-161	indoleamine 2,3-dioxygenase 1	Homo sapiens	209-213
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.	Kynurenine	159-169	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.	Kynurenine	159-169	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.	Kynurenine	118-129	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-3
21517758-5	2011	Tryptophan starvation and presence of kynurenines can induce the conversion of naive CD4(+)CD25(-) T cells into highly suppressive CD4(+)CD25(+)Foxp3(+) T(reg) cells.	Kynurenine	38-49	forkhead box P3	Homo sapiens	144-149
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.	Kynurenine	171-181	indoleamine 2,3-dioxygenase 1	Homo sapiens	11-38
21076293-4	2011	Within Th1-type immune response the enzyme indoleamine 2,3-dioxygenase (IDO) is induced, which degrades the essential amino acid tryptophan to form kynurenine derivatives.	Kynurenine	148-158	negative elongation factor complex member C/D	Homo sapiens	7-10
21076293-4	2011	Within Th1-type immune response the enzyme indoleamine 2,3-dioxygenase (IDO) is induced, which degrades the essential amino acid tryptophan to form kynurenine derivatives.	Kynurenine	148-158	indoleamine 2,3-dioxygenase 1	Homo sapiens	43-70
21076293-4	2011	Within Th1-type immune response the enzyme indoleamine 2,3-dioxygenase (IDO) is induced, which degrades the essential amino acid tryptophan to form kynurenine derivatives.	Kynurenine	148-158	indoleamine 2,3-dioxygenase 1	Homo sapiens	72-75
20811799-0	2011	Interferon-gamma-inducible kynurenines/pteridines inflammation cascade: implications for aging and aging-associated psychiatric and medical disorders.	Kynurenine	27-38	interferon gamma	Homo sapiens	0-16
20811799-1	2011	This review of literature and our data suggests that up-regulated production of interferon-gamma (IFNG) in periphery and brain triggers a merger of tryptophan (TRY)-kynurenine (KYN) and guanine-tetrahydrobiopterin (BH4) metabolic pathways into inflammation cascade involved in aging and aging-associated medical and psychiatric disorders (AAMPD) (metabolic syndrome, depression, vascular cognitive impairment).	Kynurenine	165-175	interferon gamma	Homo sapiens	80-96
20811799-1	2011	This review of literature and our data suggests that up-regulated production of interferon-gamma (IFNG) in periphery and brain triggers a merger of tryptophan (TRY)-kynurenine (KYN) and guanine-tetrahydrobiopterin (BH4) metabolic pathways into inflammation cascade involved in aging and aging-associated medical and psychiatric disorders (AAMPD) (metabolic syndrome, depression, vascular cognitive impairment).	Kynurenine	165-175	interferon gamma	Homo sapiens	98-102
20811799-1	2011	This review of literature and our data suggests that up-regulated production of interferon-gamma (IFNG) in periphery and brain triggers a merger of tryptophan (TRY)-kynurenine (KYN) and guanine-tetrahydrobiopterin (BH4) metabolic pathways into inflammation cascade involved in aging and aging-associated medical and psychiatric disorders (AAMPD) (metabolic syndrome, depression, vascular cognitive impairment).	Kynurenine	177-180	interferon gamma	Homo sapiens	80-96
20811799-1	2011	This review of literature and our data suggests that up-regulated production of interferon-gamma (IFNG) in periphery and brain triggers a merger of tryptophan (TRY)-kynurenine (KYN) and guanine-tetrahydrobiopterin (BH4) metabolic pathways into inflammation cascade involved in aging and aging-associated medical and psychiatric disorders (AAMPD) (metabolic syndrome, depression, vascular cognitive impairment).	Kynurenine	177-180	interferon gamma	Homo sapiens	98-102
20811799-2	2011	IFNG-inducible KYN/pteridines inflammation cascade is characterized by up-regulation of nitric oxide synthase (NOS) activity (induced by KYN) and decreased formation of NOS cofactor, BH4, that results in uncoupling of NOS that shifting arginine from NO to superoxide anion production.	Kynurenine	15-18	interferon gamma	Homo sapiens	0-4
20811799-2	2011	IFNG-inducible KYN/pteridines inflammation cascade is characterized by up-regulation of nitric oxide synthase (NOS) activity (induced by KYN) and decreased formation of NOS cofactor, BH4, that results in uncoupling of NOS that shifting arginine from NO to superoxide anion production.	Kynurenine	15-18	nitric oxide synthase 2	Homo sapiens	88-109
20811799-2	2011	IFNG-inducible KYN/pteridines inflammation cascade is characterized by up-regulation of nitric oxide synthase (NOS) activity (induced by KYN) and decreased formation of NOS cofactor, BH4, that results in uncoupling of NOS that shifting arginine from NO to superoxide anion production.	Kynurenine	137-140	interferon gamma	Homo sapiens	0-4
20811799-2	2011	IFNG-inducible KYN/pteridines inflammation cascade is characterized by up-regulation of nitric oxide synthase (NOS) activity (induced by KYN) and decreased formation of NOS cofactor, BH4, that results in uncoupling of NOS that shifting arginine from NO to superoxide anion production.	Kynurenine	137-140	nitric oxide synthase 2	Homo sapiens	88-109
20811799-4	2011	IFNG-induced up-regulation of indoleamine 2,3-dioxygenase (IDO), rate-limiting enzyme of TRY-KYN pathway, decreases TRY conversion into serotonin (substrate of antidepressant effect) and increases production of KYN associated with diabetes [xanthurenic acid (XA)], anxiety (KYN), psychoses and cognitive impairment (kynurenic acid).	Kynurenine	93-96	interferon gamma	Homo sapiens	0-4
20811799-5	2011	IFNG-inducible KYN/pteridines inflammation cascade is impacted by IFNG (+874) T/A genotypes, encoding cytokine production.	Kynurenine	15-18	interferon gamma	Homo sapiens	0-4
20811799-5	2011	IFNG-inducible KYN/pteridines inflammation cascade is impacted by IFNG (+874) T/A genotypes, encoding cytokine production.	Kynurenine	15-18	interferon gamma	Homo sapiens	66-70
20941617-3	2011	Its immunoregulatory effects are mainly mediated by dendritic cells (DCs) and involve not only tryptophan deprivation but also production of kynurenines that act on IDO(-) DCs--thus rendering an otherwise stimulatory DC capable of regulatory effects--as well as on T cells.	Kynurenine	141-152	indoleamine 2,3-dioxygenase 1	Homo sapiens	165-168
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.	Kynurenine	74-84	indoleamine 2,3-dioxygenase 1	Homo sapiens	26-29
21980470-1	2011	BACKGROUND: Indoleamine 2,3-dioxygenase (IDO) catalyzes the first and rate-limiting step of the kynurenine pathway that is an important component of immunomodulatory and neuromodulatory processes.	Kynurenine	96-106	indoleamine 2,3-dioxygenase 1	Homo sapiens	12-39
21980470-1	2011	BACKGROUND: Indoleamine 2,3-dioxygenase (IDO) catalyzes the first and rate-limiting step of the kynurenine pathway that is an important component of immunomodulatory and neuromodulatory processes.	Kynurenine	96-106	indoleamine 2,3-dioxygenase 1	Homo sapiens	41-44
21731667-2	2011	In response to infection, interferon-gamma activates indoleamine 2,3-dioxygenase (IDO) which metabolizes the essential amino acid tryptophan to the toxic metabolite kynurenine.	Kynurenine	165-175	interferon gamma	Homo sapiens	26-42
21731667-2	2011	In response to infection, interferon-gamma activates indoleamine 2,3-dioxygenase (IDO) which metabolizes the essential amino acid tryptophan to the toxic metabolite kynurenine.	Kynurenine	165-175	indoleamine 2,3-dioxygenase 1	Homo sapiens	53-80
21731667-2	2011	In response to infection, interferon-gamma activates indoleamine 2,3-dioxygenase (IDO) which metabolizes the essential amino acid tryptophan to the toxic metabolite kynurenine.	Kynurenine	165-175	indoleamine 2,3-dioxygenase 1	Homo sapiens	82-85
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.	Kynurenine	40-50	indoleamine 2,3-dioxygenase 1	Homo sapiens	10-13
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.	Kynurenine	209-219	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.	Kynurenine	209-212	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-3
20802227-1	2010	l-kynurenine 3-monooxygenase (KMO) is an NAD(P)H-dependent flavin monooxygenase that catalyses the hydroxylation of l-kynurenine to 3-hydroxykynurenine, and is localized as an oligomer in the mitochondrial outer membrane.	Kynurenine	0-12	kynurenine 3-monooxygenase	Sus scrofa	30-33
21517759-5	2011	IDO, through production of kynurenine and other downstream metabolites, can regulate immune responses, suppressing effector T-cell function and favouring the differentiation of regulatory T cells.	Kynurenine	27-37	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-3
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.	Kynurenine	171-181	indoleamine 2,3-dioxygenase 1	Homo sapiens	40-43
20451602-1	2010	Indoleamine 2,3-dioxygenase (IDO) is an intracellular heme-containing enzyme that is activated by proinflammatory cytokines, including interferon-gamma (IFNgamma), and metabolizes tryptophan along the kynurenine pathway.	Kynurenine	201-211	indoleamine 2,3-dioxygenase 1	Mus musculus	0-27
21041655-0	2010	Aryl hydrocarbon receptor negatively regulates dendritic cell immunogenicity via a kynurenine-dependent mechanism.	Kynurenine	83-93	aryl hydrocarbon receptor	Homo sapiens	0-25
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.	Kynurenine	160-170	aryl hydrocarbon receptor	Homo sapiens	27-30
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.	Kynurenine	160-170	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.	Kynurenine	160-170	indoleamine 2,3-dioxygenase 1	Homo sapiens	82-85
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.	Kynurenine	172-175	aryl hydrocarbon receptor	Homo sapiens	27-30
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.	Kynurenine	172-175	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.	Kynurenine	172-175	indoleamine 2,3-dioxygenase 1	Homo sapiens	82-85
20451602-1	2010	Indoleamine 2,3-dioxygenase (IDO) is an intracellular heme-containing enzyme that is activated by proinflammatory cytokines, including interferon-gamma (IFNgamma), and metabolizes tryptophan along the kynurenine pathway.	Kynurenine	201-211	indoleamine 2,3-dioxygenase 1	Mus musculus	29-32
20451602-1	2010	Indoleamine 2,3-dioxygenase (IDO) is an intracellular heme-containing enzyme that is activated by proinflammatory cytokines, including interferon-gamma (IFNgamma), and metabolizes tryptophan along the kynurenine pathway.	Kynurenine	201-211	interferon gamma	Mus musculus	135-151
20451602-1	2010	Indoleamine 2,3-dioxygenase (IDO) is an intracellular heme-containing enzyme that is activated by proinflammatory cytokines, including interferon-gamma (IFNgamma), and metabolizes tryptophan along the kynurenine pathway.	Kynurenine	201-211	interferon gamma	Mus musculus	153-161
20451602-8	2010	These data establish that IDO regulation in murine microglia is not restrained by NO, thereby permitting the accumulation of kynurenine and its downstream metabolites in the central nervous system.	Kynurenine	125-135	indoleamine 2,3-dioxygenase 1	Mus musculus	26-29
19702697-5	2010	Also ESR and CRP and neopterin concentrations were increased in the patients (all P &lt; 0.001), and there was a weak correlation between kynurenine to tryptophan ratio and ESR, CRP and neopterin concentrations.	Kynurenine	138-148	C-reactive protein	Homo sapiens	178-181
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.	Kynurenine	120-130	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.	Kynurenine	120-130	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.	Kynurenine	132-135	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.	Kynurenine	132-135	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.	Kynurenine	199-210	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.	Kynurenine	199-210	indoleamine 2,3-dioxygenase 1	Homo sapiens	29-32
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).	Kynurenine	40-50	indoleamine 2,3-dioxygenase 1	Homo sapiens	167-194
21224538-2	2010	IDO activity can be measured by tryptophan (Trp)/kynurenine (Kyn) ratio.	Kynurenine	49-59	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-3
21224538-2	2010	IDO activity can be measured by tryptophan (Trp)/kynurenine (Kyn) ratio.	Kynurenine	61-64	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).	Kynurenine	40-50	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).	Kynurenine	40-50	tryptophan 2,3-dioxygenase	Homo sapiens	206-232
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).	Kynurenine	40-50	tryptophan 2,3-dioxygenase	Homo sapiens	234-237
20844202-1	2010	IDO converts tryptophan to l-kynurenine, and it is noted as a relevant molecule in promoting tolerance and suppressing adaptive immunity.	Kynurenine	27-39	indoleamine 2,3-dioxygenase 1	Mus musculus	0-3
20884048-0	2010	NFkappaB-dependent increase of kynurenine pathway activity in human placenta: inhibition by sulfasalazine.	Kynurenine	31-41	nuclear factor kappa B subunit 1	Homo sapiens	0-8
20884048-2	2010	In this study we determined if activation of NFkappaB is involved in the inflammation-induced increase of kynurenine pathway activity in the human placenta.	Kynurenine	106-116	nuclear factor kappa B subunit 1	Homo sapiens	45-53
20884048-10	2010	These observations show that kynurenine pathway activity in the human placenta is increased by a NFkappaB dependent pathway, and suggests a new therapeutic strategy for the management of pregnancies with in utero infection.	Kynurenine	29-39	nuclear factor kappa B subunit 1	Homo sapiens	97-105
20687219-5	2010	The levels of the substrate for IDO (tryptophane) and its product (kynurenine) was measured by HPLC.	Kynurenine	67-77	indoleamine 2,3-dioxygenase 1	Mus musculus	32-35
20687219-6	2010	RESULTS: We found that systemic IDO activity, determined as the kynurenine/tryptophan ratio in serum, correlated with the presence of palpable tumor.	Kynurenine	64-74	indoleamine 2,3-dioxygenase 1	Mus musculus	32-35
20511543-2	2010	Based on recent mouse studies, the lack of O(2)( )-dependent interferon gamma (IFNgamma)-induced synthesis of kynurenine (kyn), an anti-inflammatory tryptophan metabolite produced by indolamine 2,3 deoxygenase (IDO), was proposed as a cause of hyperinflammation in CGD and this pathway has been considered for clinical intervention.	Kynurenine	110-120	interferon gamma	Mus musculus	61-77
20511543-2	2010	Based on recent mouse studies, the lack of O(2)( )-dependent interferon gamma (IFNgamma)-induced synthesis of kynurenine (kyn), an anti-inflammatory tryptophan metabolite produced by indolamine 2,3 deoxygenase (IDO), was proposed as a cause of hyperinflammation in CGD and this pathway has been considered for clinical intervention.	Kynurenine	110-120	interferon gamma	Mus musculus	79-87
20511543-3	2010	Here, we show that IFNgamma induces normal levels of kynurenine in cultures of O(2)( )-deficient monocytes, dendritic cells, and polymorphonuclear leukocytes from gp91(PHOX)- or p47(PHOX)-deficient human CGD donors.	Kynurenine	53-63	interferon gamma	Homo sapiens	19-27
20435158-2	2010	IFN-gamma induces the expression of indoleamine 2,3-dioxygenase (IDO) and thereby enhances the production of kynurenines from l-tryptophan.	Kynurenine	109-120	interferon gamma	Homo sapiens	0-9
20720200-0	2010	An interaction between kynurenine and the aryl hydrocarbon receptor can generate regulatory T cells.	Kynurenine	23-33	aryl-hydrocarbon receptor	Mus musculus	42-67
20720200-3	2010	In this paper, we demonstrate that kynurenine, the first breakdown product in the IDO-dependent tryptophan degradation pathway, activates the AHR.	Kynurenine	35-45	indoleamine 2,3-dioxygenase 1	Mus musculus	82-85
20720200-3	2010	In this paper, we demonstrate that kynurenine, the first breakdown product in the IDO-dependent tryptophan degradation pathway, activates the AHR.	Kynurenine	35-45	aryl-hydrocarbon receptor	Mus musculus	142-145
20688518-2	2010	Subsequent optimization of the initial hit 3a lead to the identification of sub-muM inhibitors 3r and 10h, both of which suppressed kynurenine production in A431 cells.	Kynurenine	132-142	latexin	Homo sapiens	80-83
20435158-3	2010	The present study was designed to investigate the role of IDO and kynurenines in the IFN-gamma-mediated apoptosis of lens epithelial cells and to determine the signaling pathways involved.	Kynurenine	66-77	interferon gamma	Homo sapiens	85-94
20435158-7	2010	The intracellular production of kynurenines was completely blocked by 1-methyl-DL-tryptophan (MT), an inhibitor of IDO.	Kynurenine	32-43	indoleamine 2,3-dioxygenase 1	Homo sapiens	115-118
20435158-14	2010	These data suggest that IDO-mediated kynurenine formation could play a role in cataract formation related to chronic inflammation.	Kynurenine	37-47	indoleamine 2,3-dioxygenase 1	Homo sapiens	24-27
20435158-2	2010	IFN-gamma induces the expression of indoleamine 2,3-dioxygenase (IDO) and thereby enhances the production of kynurenines from l-tryptophan.	Kynurenine	109-120	indoleamine 2,3-dioxygenase 1	Homo sapiens	36-63
20435158-2	2010	IFN-gamma induces the expression of indoleamine 2,3-dioxygenase (IDO) and thereby enhances the production of kynurenines from l-tryptophan.	Kynurenine	109-120	indoleamine 2,3-dioxygenase 1	Homo sapiens	65-68
20490917-7	2010	The KYN/TRP ratio at admission correlated with CRP levels, ESR and NLR.	Kynurenine	4-7	C-reactive protein	Homo sapiens	47-50
20478381-5	2010	Our data also show that KYN inhibits FGF2-induced Akt and ERK1/2 phosphorylation in mLEC, which are required for crystallin and MIP26 expression in the lens.	Kynurenine	24-27	mitogen-activated protein kinase 3	Mus musculus	58-64
20678226-5	2010	Enzymatic activity of IDO was estimated as the amount of kynurenine produced from tryptophan as determined by high pressure liquid chromatography (HPLC) with electrochemical detection.	Kynurenine	57-67	indoleamine 2,3-dioxygenase 1	Mus musculus	22-25
21028859-3	2010	In this contribution, we report an electron-transfer reaction in a human transporter protein (HSA) cavity which causes the tryptophan residue (Trp214) to undergo chemical modification to form one of its metabolites kynurenine (Kyn214).	Kynurenine	215-225	albumin	Homo sapiens	94-97
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).	Kynurenine	150-160	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).	Kynurenine	162-165	indoleamine 2,3-dioxygenase 1	Homo sapiens	107-110
20478381-0	2010	Kynurenine inhibits fibroblast growth factor 2-mediated expression of crystallins and MIP26 in lens epithelial cells.	Kynurenine	0-10	fibroblast growth factor 2	Mus musculus	20-46
20547831-6	2010	Notably, unlike peripheral blood NK (pNK) cells, dNK cells are resistant to inhibition by the IDO metabolite L-kynurenine.	Kynurenine	109-121	deoxyribonucleoside kinase	Drosophila melanogaster	49-52
20478381-0	2010	Kynurenine inhibits fibroblast growth factor 2-mediated expression of crystallins and MIP26 in lens epithelial cells.	Kynurenine	0-10	major intrinsic protein of lens fiber	Mus musculus	86-91
20478381-2	2010	We had previously shown that kynurenine (KYN) produced from the overexpression of indoleamine 2,3-dioxygenase (IDO) causes defects in the differentiation of fiber cells, induces fiber cell apoptosis and cataract formation in the mouse lens, and leads to cell cycle arrest in cultured mouse lens epithelial cells (mLEC).	Kynurenine	29-39	indoleamine 2,3-dioxygenase 1	Mus musculus	82-109
20478381-2	2010	We had previously shown that kynurenine (KYN) produced from the overexpression of indoleamine 2,3-dioxygenase (IDO) causes defects in the differentiation of fiber cells, induces fiber cell apoptosis and cataract formation in the mouse lens, and leads to cell cycle arrest in cultured mouse lens epithelial cells (mLEC).	Kynurenine	29-39	indoleamine 2,3-dioxygenase 1	Mus musculus	111-114
20478381-2	2010	We had previously shown that kynurenine (KYN) produced from the overexpression of indoleamine 2,3-dioxygenase (IDO) causes defects in the differentiation of fiber cells, induces fiber cell apoptosis and cataract formation in the mouse lens, and leads to cell cycle arrest in cultured mouse lens epithelial cells (mLEC).	Kynurenine	41-44	indoleamine 2,3-dioxygenase 1	Mus musculus	82-109
20478381-2	2010	We had previously shown that kynurenine (KYN) produced from the overexpression of indoleamine 2,3-dioxygenase (IDO) causes defects in the differentiation of fiber cells, induces fiber cell apoptosis and cataract formation in the mouse lens, and leads to cell cycle arrest in cultured mouse lens epithelial cells (mLEC).	Kynurenine	41-44	indoleamine 2,3-dioxygenase 1	Mus musculus	111-114
20478381-4	2010	We show that endogenously produced KYN in mLEC of IDO transgenic animals causes similar defects in FGF2-induced protein expression and that a competitive inhibitor of IDO prevents such defects.	Kynurenine	35-38	indoleamine 2,3-dioxygenase 1	Mus musculus	50-53
20478381-4	2010	We show that endogenously produced KYN in mLEC of IDO transgenic animals causes similar defects in FGF2-induced protein expression and that a competitive inhibitor of IDO prevents such defects.	Kynurenine	35-38	fibroblast growth factor 2	Mus musculus	99-103
20478381-4	2010	We show that endogenously produced KYN in mLEC of IDO transgenic animals causes similar defects in FGF2-induced protein expression and that a competitive inhibitor of IDO prevents such defects.	Kynurenine	35-38	indoleamine 2,3-dioxygenase 1	Mus musculus	167-170
20478381-5	2010	Our data also show that KYN inhibits FGF2-induced Akt and ERK1/2 phosphorylation in mLEC, which are required for crystallin and MIP26 expression in the lens.	Kynurenine	24-27	fibroblast growth factor 2	Mus musculus	37-41
20478381-5	2010	Our data also show that KYN inhibits FGF2-induced Akt and ERK1/2 phosphorylation in mLEC, which are required for crystallin and MIP26 expression in the lens.	Kynurenine	24-27	thymoma viral proto-oncogene 1	Mus musculus	50-53
20478381-5	2010	Our data also show that KYN inhibits FGF2-induced Akt and ERK1/2 phosphorylation in mLEC, which are required for crystallin and MIP26 expression in the lens.	Kynurenine	24-27	major intrinsic protein of lens fiber	Mus musculus	128-133
20478381-6	2010	KYN does not inhibit FGF2 binding to cells but inhibit phosphorylation of FGFR1in mLEC.	Kynurenine	0-3	fibroblast growth factor receptor 1	Mus musculus	74-79
20547831-6	2010	Notably, unlike peripheral blood NK (pNK) cells, dNK cells are resistant to inhibition by the IDO metabolite L-kynurenine.	Kynurenine	109-121	indoleamine 2,3-dioxygenase 1	Homo sapiens	94-97
19925620-1	2010	OBJECTIVE: To examine the efficacy of L-kynurenine and a novel kynurenic acid derivative on the nitroglycerin-induced calmodulin-dependent protein kinase II alpha (CamKIIalpha) and calcitonin gene-related peptide (CGRP) expression changes in the rat caudal trigeminal nucleus.	Kynurenine	38-50	calcitonin-related polypeptide alpha	Rattus norvegicus	181-212
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.	Kynurenine	182-192	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).	Kynurenine	219-229	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).	Kynurenine	219-229	indoleamine 2,3-dioxygenase 1	Homo sapiens	172-175
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).	Kynurenine	231-234	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).	Kynurenine	231-234	indoleamine 2,3-dioxygenase 1	Homo sapiens	172-175
20633104-5	2010	Activation of IDO shifts TRY metabolism from serotonin synthesis to formation of "kynurenines."	Kynurenine	82-93	indoleamine 2,3-dioxygenase 1	Homo sapiens	14-17
20633104-6	2010	Diminished serotonin production is associated with mental depression while increased formation of kynurenines might contribute to development of MetS/AAND via their apoptotic, neurotoxic, and pro-oxidative effects, and upregulation of inducible nitric oxide synthase, phospholipase A2, arachidonic acid, prostaglandin, 5-lipoxygenase, and leukotriene cascade.	Kynurenine	98-109	phospholipase A2 group IB	Homo sapiens	268-284
20633104-6	2010	Diminished serotonin production is associated with mental depression while increased formation of kynurenines might contribute to development of MetS/AAND via their apoptotic, neurotoxic, and pro-oxidative effects, and upregulation of inducible nitric oxide synthase, phospholipase A2, arachidonic acid, prostaglandin, 5-lipoxygenase, and leukotriene cascade.	Kynurenine	98-109	arachidonate 5-lipoxygenase	Homo sapiens	319-333
19765856-9	2010	IFN-gamma stimulated higher kynurenine and neopterin formation in cells cultivated in EGFCM, stimulation with 400U IFN-gamma every other day was most effective.	Kynurenine	28-38	interferon gamma	Homo sapiens	0-9
19765856-9	2010	IFN-gamma stimulated higher kynurenine and neopterin formation in cells cultivated in EGFCM, stimulation with 400U IFN-gamma every other day was most effective.	Kynurenine	28-38	interferon gamma	Homo sapiens	115-124
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.	Kynurenine	60-70	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.	Kynurenine	60-70	indoleamine 2,3-dioxygenase 1	Homo sapiens	226-229
20155828-10	2010	We found diminished serum tryptophan levels and elevated levels of its metabolite kynurenine in patients with MPO AAV as compared with controls.	Kynurenine	82-92	myeloperoxidase	Homo sapiens	110-113
19925620-4	2010	As glutamatergic mechanisms may be crucial in trigeminal pain processing, the aim of our study was to examine the effects of L-kynurenine, a metabolic precursor of the N-methyl D-aspartate receptor antagonist kynurenic acid, on the nitroglycerin-induced changes in CamKIIalpha and CGRP immunoreactivity.	Kynurenine	125-137	calcitonin-related polypeptide alpha	Rattus norvegicus	281-285
19925620-9	2010	Results.- L-kynurenine and 2-(2-N,N-dimethylaminoethylamine-1-carbonyl)-1H-quinolin-4-one hydrochloride pretreatment attenuated the nitroglycerin-induced changes in CamKIIalpha and CGRP immunoreactivity in the rat caudal trigeminal nucleus.	Kynurenine	8-22	calcitonin-related polypeptide alpha	Rattus norvegicus	181-185
19607757-6	2010	In mice infected on postnatal day (P)3 or P4, the levels of several transcripts in the kynurenine pathway were altered at P7, P13 and P24.	Kynurenine	87-97	cytochrome P450, family 2, subfamily b, polypeptide 10	Mus musculus	134-137
19607757-7	2010	Transcripts encoding indoleamine-pyrrole 2,3-dioxygenase (IDO), degrading tryptophan in the first step of the kynurenine pathway were consistently up-regulated at all time-points investigated.	Kynurenine	110-120	indoleamine 2,3-dioxygenase 1	Mus musculus	21-56
19607757-7	2010	Transcripts encoding indoleamine-pyrrole 2,3-dioxygenase (IDO), degrading tryptophan in the first step of the kynurenine pathway were consistently up-regulated at all time-points investigated.	Kynurenine	110-120	indoleamine 2,3-dioxygenase 1	Mus musculus	58-61
20002791-6	2010	This effect was mediated through the propensity of A. fumigatus to metabolize tryptophan and release kynurenine, which modulates the inflammatory response through inhibition of IL-17 production.	Kynurenine	101-111	interleukin 17A	Homo sapiens	177-182
19886804-3	2010	Tryptophan (trp) catabolism by indolamine-2,3-dioxygenase 1 (IDO1) is a chief endogenous metabolic pathway that tightly regulates unwanted immune responses through depletion of trp and generation of immunosuppressive kynurenines (kyn).	Kynurenine	217-228	indoleamine 2,3-dioxygenase 1	Mus musculus	31-59
19886804-3	2010	Tryptophan (trp) catabolism by indolamine-2,3-dioxygenase 1 (IDO1) is a chief endogenous metabolic pathway that tightly regulates unwanted immune responses through depletion of trp and generation of immunosuppressive kynurenines (kyn).	Kynurenine	217-228	indoleamine 2,3-dioxygenase 1	Mus musculus	61-65
19886804-3	2010	Tryptophan (trp) catabolism by indolamine-2,3-dioxygenase 1 (IDO1) is a chief endogenous metabolic pathway that tightly regulates unwanted immune responses through depletion of trp and generation of immunosuppressive kynurenines (kyn).	Kynurenine	217-220	indoleamine 2,3-dioxygenase 1	Mus musculus	31-59
19886804-3	2010	Tryptophan (trp) catabolism by indolamine-2,3-dioxygenase 1 (IDO1) is a chief endogenous metabolic pathway that tightly regulates unwanted immune responses through depletion of trp and generation of immunosuppressive kynurenines (kyn).	Kynurenine	217-220	indoleamine 2,3-dioxygenase 1	Mus musculus	61-65
19995374-0	2010	Serum concentration of L-kynurenine predicts the clinical outcome of patients with diffuse large B-cell lymphoma treated with R-CHOP.	Kynurenine	23-35	DNA damage inducible transcript 3	Homo sapiens	128-132
20197554-9	2010	Analysis of plasma kynurenine/tryptophan levels in patients with cancer affirms that the IDO pathway is activated in multiple tumor types.	Kynurenine	19-29	indoleamine 2,3-dioxygenase 1	Homo sapiens	89-92
20141220-6	2010	Elevated urinary levels of xanthurenic acid in IL10(-/-) mice were attributed to increased production of kynurenine metabolites that may induce T-cell tolerance toward intestinal microbiota.	Kynurenine	105-115	interleukin 10	Mus musculus	47-51
20141220-7	2010	Liquid chromatography-mass spectrometry analysis confirmed that plasma levels of kynurenine and 3-hydroxykynurenine were elevated in IL10(-/-) mice.	Kynurenine	81-91	interleukin 10	Mus musculus	133-137
19995374-4	2010	The activity of IDO can be estimated by measuring the serum concentration of L-kynurenine.	Kynurenine	77-89	indoleamine 2,3-dioxygenase 1	Homo sapiens	16-19
19995374-13	2010	CONCLUSIONS: Serum L-kynurenine might be a novel prognostic factor to determine the treatment outcome of DLBCL with the R-CHOP regimen.	Kynurenine	19-31	DNA damage inducible transcript 3	Homo sapiens	122-126
19487045-1	2010	BACKGROUND: Indoleamine 2,3-dioxygenase (IDO) catalyzes the rate-limiting step of tryptophan (Trp) degradation along the kynurenine (Kyn) pathway.	Kynurenine	121-131	indoleamine 2,3-dioxygenase 1	Homo sapiens	12-39
19918244-0	2010	CSF concentrations of brain tryptophan and kynurenines during immune stimulation with IFN-alpha: relationship to CNS immune responses and depression.	Kynurenine	43-54	interferon alpha 1	Homo sapiens	86-95
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).	Kynurenine	101-113	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).	Kynurenine	101-113	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).	Kynurenine	115-118	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).	Kynurenine	115-118	indoleamine 2,3-dioxygenase 1	Homo sapiens	60-63
19918244-10	2010	Increases in CSF KYN and QUIN were correlated with increased CSF IFN-alpha, soluble tumor necrosis factor-alpha receptor 2 and monocyte chemoattractant protein-1 as well as increased depressive symptoms.	Kynurenine	17-20	interferon alpha 1	Homo sapiens	65-74
19918244-10	2010	Increases in CSF KYN and QUIN were correlated with increased CSF IFN-alpha, soluble tumor necrosis factor-alpha receptor 2 and monocyte chemoattractant protein-1 as well as increased depressive symptoms.	Kynurenine	17-20	C-C motif chemokine ligand 2	Homo sapiens	127-161
21406070-8	2010	The efficiency of the IDO expression and the activity of the enzyme have been confirmed by Western blotting, fluorescence-activated cell sorting analysis, and Kynurenine assay, respectively.	Kynurenine	159-169	indoleamine 2,3-dioxygenase 1	Homo sapiens	22-25
20190767-2	2010	Here we show that metabolism of tryptophan to kynurenine by indoleamine 2,3-dioxygenase (Ido) expressed in endothelial cells contributes to arterial vessel relaxation and the control of blood pressure.	Kynurenine	46-56	indoleamine 2,3-dioxygenase 1	Mus musculus	60-87
20190767-2	2010	Here we show that metabolism of tryptophan to kynurenine by indoleamine 2,3-dioxygenase (Ido) expressed in endothelial cells contributes to arterial vessel relaxation and the control of blood pressure.	Kynurenine	46-56	indoleamine 2,3-dioxygenase 1	Mus musculus	89-92
19487045-1	2010	BACKGROUND: Indoleamine 2,3-dioxygenase (IDO) catalyzes the rate-limiting step of tryptophan (Trp) degradation along the kynurenine (Kyn) pathway.	Kynurenine	121-131	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.	Kynurenine	133-136	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.	Kynurenine	133-136	indoleamine 2,3-dioxygenase 1	Homo sapiens	41-44
19487045-6	2010	The IDO activity was estimated by calculating the serum Kyn-to-Trp ratio (Kyn/Trp ratio).	Kynurenine	56-59	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).	Kynurenine	74-77	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&lt;0.0001).	Kynurenine	35-38	indoleamine 2,3-dioxygenase 1	Homo sapiens	4-7
20469598-1	2010	The importance of tryptophan endogenous metabolites kynurenines in the long-term memory and functioning of the signal cascade GluR - LIMK1 - F-actin, mediating the long-term memory trace storage, was demonstrated.	Kynurenine	52-63	LIM domain kinase 1	Apis mellifera	133-138
19958238-8	2010	Metabolites downstream of IDO (kynurenine, quinolinic acid, kynurenic acid) were all induced in sepsis and declined in the GM-CSF group, but not in controls.	Kynurenine	31-41	indoleamine 2,3-dioxygenase 1	Homo sapiens	26-29
19958238-8	2010	Metabolites downstream of IDO (kynurenine, quinolinic acid, kynurenic acid) were all induced in sepsis and declined in the GM-CSF group, but not in controls.	Kynurenine	31-41	colony stimulating factor 2	Homo sapiens	123-129
19958238-11	2010	Thus, GM-CSF therapy is associated with decreased IDO activity and reduced kynurenine pathway catabolites in sepsis.	Kynurenine	75-85	colony stimulating factor 2	Homo sapiens	6-12
20469598-2	2010	The deficit of kynurenines induced by allopurinol (tryptophanoxygenase inhibitor) suppressed the long-term memory, decreased the LIMK1 expression, and paradoxically increased the F-actin content in the honeybee brain.	Kynurenine	15-26	LIM domain kinase 1	Apis mellifera	129-134
20100004-1	2010	IMPORTANCE OF THE FIELD: The enzyme indoleamine 2,3-dioxygenase (IDO) regulates immune responses through the capacity to degrade the essential amino-acid tryptophan into kynurenine and other downstream metabolites that suppress effector T-cell function and favour the differentiation of regulatory T cells.	Kynurenine	170-180	indoleamine 2,3-dioxygenase 1	Homo sapiens	36-63
19394403-3	2010	Set against a historical background, we review data supporting the idea that metabolites of the kynurenine pathway (KP) of tryptophan degradation provide a critical link between mutant htt and the pathophysiology of HD.	Kynurenine	96-106	huntingtin	Homo sapiens	185-188
20128035-7	2010	RESULTS: Real-time PCR revealed IDO mRNA and FasL mRNA expressions in KC pretreated with IFN-gamma, and IDO catabolic effect was confirmed by a decrease in tryptophan and increase in kynurenine concentration.	Kynurenine	183-193	indoleamine 2,3-dioxygenase 1	Mus musculus	104-107
19577630-3	2010	LPS (10 ng/ml) induced IDO transcripts that peaked at 8h and enzymatic activity at 24h, resulting in an increase in extracellular kynurenine, the catabolic product of IDO-induced tryptophan catabolism.	Kynurenine	130-140	indoleamine 2,3-dioxygenase 1	Mus musculus	23-26
19577630-3	2010	LPS (10 ng/ml) induced IDO transcripts that peaked at 8h and enzymatic activity at 24h, resulting in an increase in extracellular kynurenine, the catabolic product of IDO-induced tryptophan catabolism.	Kynurenine	130-140	indoleamine 2,3-dioxygenase 1	Mus musculus	167-170
20100004-1	2010	IMPORTANCE OF THE FIELD: The enzyme indoleamine 2,3-dioxygenase (IDO) regulates immune responses through the capacity to degrade the essential amino-acid tryptophan into kynurenine and other downstream metabolites that suppress effector T-cell function and favour the differentiation of regulatory T cells.	Kynurenine	170-180	indoleamine 2,3-dioxygenase 1	Homo sapiens	65-68
20124451-2	2010	Expression of indoleamine-2,3-dioxygenase (IDO; IDO1), a rate-limiting enzyme in the catabolism of tryptophan into kynurenine, contributes to this immune evasion.	Kynurenine	115-125	indoleamine 2,3-dioxygenase 1	Mus musculus	14-41
20124451-2	2010	Expression of indoleamine-2,3-dioxygenase (IDO; IDO1), a rate-limiting enzyme in the catabolism of tryptophan into kynurenine, contributes to this immune evasion.	Kynurenine	115-125	indoleamine 2,3-dioxygenase 1	Mus musculus	43-46
20124451-2	2010	Expression of indoleamine-2,3-dioxygenase (IDO; IDO1), a rate-limiting enzyme in the catabolism of tryptophan into kynurenine, contributes to this immune evasion.	Kynurenine	115-125	indoleamine 2,3-dioxygenase 1	Mus musculus	48-52
19487973-6	2010	The kyn-to-trp ratio (kyn/trp), reflecting the activity of the IDO enzyme, was calculated.	Kynurenine	4-7	indoleamine 2,3-dioxygenase 1	Homo sapiens	63-66
19778568-2	2010	IDO metabolizes tryptophan (TRP) into kynurenine (KYN), thereby decreasing TRP availability to the brain.	Kynurenine	38-48	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.	Kynurenine	50-53	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-3
19487973-6	2010	The kyn-to-trp ratio (kyn/trp), reflecting the activity of the IDO enzyme, was calculated.	Kynurenine	22-25	indoleamine 2,3-dioxygenase 1	Homo sapiens	63-66
22084591-1	2010	Indoleamine 2,3-dioxygenase (IDO) catalyzes the initial and rate-limiting step of tryptophan catabolism in a specific pathway, resulting in a series of extracellular messengers collectively known as kynurenines.	Kynurenine	199-210	indoleamine 2,3-dioxygenase 1	Mus musculus	0-27
20439183-7	2010	Kynurenines were positively associated with vWF, TM, sICAM-1 and sVCAM-1, whereas sP-selectin was inversely associated with the most of kynurenines.	Kynurenine	0-11	von Willebrand factor	Homo sapiens	44-47
20439183-7	2010	Kynurenines were positively associated with vWF, TM, sICAM-1 and sVCAM-1, whereas sP-selectin was inversely associated with the most of kynurenines.	Kynurenine	0-11	thrombomodulin	Homo sapiens	49-51
21086789-2	2010	During immune response interferon-gamma stimulates the kynurenine (Kyn) pathway, a major route of L-tryptophan (Trp) degradation.	Kynurenine	55-65	interferon gamma	Homo sapiens	23-39
21086789-2	2010	During immune response interferon-gamma stimulates the kynurenine (Kyn) pathway, a major route of L-tryptophan (Trp) degradation.	Kynurenine	67-70	interferon gamma	Homo sapiens	23-39
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.	Kynurenine	68-78	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.	Kynurenine	80-83	indoleamine 2,3-dioxygenase 1	Homo sapiens	155-158
22084591-1	2010	Indoleamine 2,3-dioxygenase (IDO) catalyzes the initial and rate-limiting step of tryptophan catabolism in a specific pathway, resulting in a series of extracellular messengers collectively known as kynurenines.	Kynurenine	199-210	indoleamine 2,3-dioxygenase 1	Mus musculus	29-32
22084588-8	2010	KYN/TRP correlated with neopterin (p &lt; 0.001) and also with TNF-alpha (p &lt; 0.01) and IL-6 concentrations (p &lt; 0.05) and inversely with the in vitro response of stimulated monocytes.	Kynurenine	0-3	tumor necrosis factor	Homo sapiens	63-72
22084588-8	2010	KYN/TRP correlated with neopterin (p &lt; 0.001) and also with TNF-alpha (p &lt; 0.01) and IL-6 concentrations (p &lt; 0.05) and inversely with the in vitro response of stimulated monocytes.	Kynurenine	0-3	interleukin 6	Homo sapiens	91-95
22084591-3	2010	Its suppressive effects are mostly mediated by dendritic cells (DCs) and involve tryptophan deprivation and/or production of kynurenines, which act on IDO-negative DCs as well as CD4(+) and CD8(+) T cells.	Kynurenine	125-136	indoleamine 2,3-dioxygenase 1	Mus musculus	151-154
22084591-3	2010	Its suppressive effects are mostly mediated by dendritic cells (DCs) and involve tryptophan deprivation and/or production of kynurenines, which act on IDO-negative DCs as well as CD4(+) and CD8(+) T cells.	Kynurenine	125-136	CD4 antigen	Mus musculus	179-182
19715778-0	2009	Quantum mechanics/molecular mechanics (QM/MM) modeling of the irreversible transamination of L-kynurenine to kynurenic acid: the round dance of kynurenine aminotransferase II.	Kynurenine	93-105	aminoadipate aminotransferase	Homo sapiens	144-174
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).	Kynurenine	82-92	indoleamine 2,3-dioxygenase 1	Rattus norvegicus	30-35
20663292-3	2010	To determine the role of the kynurenine pathway in eliciting and continuing oxidative stress within Alzheimer"s diseased brains, we used immunocytochemical methods to show elevated levels of 3-HK modifications and the upstream, rate-limiting enzyme indoleamine 2,3-dioxygenase (IDO-1) in Alzheimer"s diseased brains when compared to controls.	Kynurenine	29-39	indoleamine 2,3-dioxygenase 1	Homo sapiens	278-283
20686200-4	2010	Rate-limiting enzymes of kynurenine formation, tryptophan 2,3-dioxygenase (TDO) and indoleamine 2,3-dioxygenase (IDO) are activated by stress hormones (TDO) and/or by pro-inflammatory cytokines (IDO).	Kynurenine	25-35	tryptophan 2,3-dioxygenase	Homo sapiens	47-73
20686200-4	2010	Rate-limiting enzymes of kynurenine formation, tryptophan 2,3-dioxygenase (TDO) and indoleamine 2,3-dioxygenase (IDO) are activated by stress hormones (TDO) and/or by pro-inflammatory cytokines (IDO).	Kynurenine	25-35	tryptophan 2,3-dioxygenase	Homo sapiens	75-78
20686200-4	2010	Rate-limiting enzymes of kynurenine formation, tryptophan 2,3-dioxygenase (TDO) and indoleamine 2,3-dioxygenase (IDO) are activated by stress hormones (TDO) and/or by pro-inflammatory cytokines (IDO).	Kynurenine	25-35	indoleamine 2,3-dioxygenase 1	Homo sapiens	84-111
20686200-4	2010	Rate-limiting enzymes of kynurenine formation, tryptophan 2,3-dioxygenase (TDO) and indoleamine 2,3-dioxygenase (IDO) are activated by stress hormones (TDO) and/or by pro-inflammatory cytokines (IDO).	Kynurenine	25-35	indoleamine 2,3-dioxygenase 1	Homo sapiens	113-116
20686200-4	2010	Rate-limiting enzymes of kynurenine formation, tryptophan 2,3-dioxygenase (TDO) and indoleamine 2,3-dioxygenase (IDO) are activated by stress hormones (TDO) and/or by pro-inflammatory cytokines (IDO).	Kynurenine	25-35	tryptophan 2,3-dioxygenase	Homo sapiens	152-155
20686200-4	2010	Rate-limiting enzymes of kynurenine formation, tryptophan 2,3-dioxygenase (TDO) and indoleamine 2,3-dioxygenase (IDO) are activated by stress hormones (TDO) and/or by pro-inflammatory cytokines (IDO).	Kynurenine	25-35	indoleamine 2,3-dioxygenase 1	Homo sapiens	195-198
19715778-4	2009	In this study, the transamination mechanism of L-Kyn catalyzed by KAT-II is theoretically determined by performing combined quantum mechanical and molecular mechanical (QM/MM) simulations.	Kynurenine	47-52	aminoadipate aminotransferase	Homo sapiens	66-72
20037301-2	2009	IDO activity can be measured by tryptophan (Trp)/kynurenine (Kyn) ratio.	Kynurenine	49-59	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-3
20037301-2	2009	IDO activity can be measured by tryptophan (Trp)/kynurenine (Kyn) ratio.	Kynurenine	61-64	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.	Kynurenine	108-118	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.	Kynurenine	108-118	indoleamine 2,3-dioxygenase 1	Homo sapiens	41-44
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.	Kynurenine	120-123	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.	Kynurenine	120-123	indoleamine 2,3-dioxygenase 1	Homo sapiens	41-44
19843945-2	2009	In this study, we report that the DCs in mesenteric lymph nodes (MLNs) constitutively express functional IDO, which metabolizes tryptophan to kynurenine.	Kynurenine	142-152	indoleamine 2,3-dioxygenase 1	Mus musculus	105-108
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).	Kynurenine	46-56	indoleamine 2,3-dioxygenase 1	Homo sapiens	76-103
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).	Kynurenine	46-56	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.	Kynurenine	55-65	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.	Kynurenine	93-103	indoleamine 2,3-dioxygenase 1	Homo sapiens	9-13
19434461-1	2009	BACKGROUND: Tryptophan catabolism via the kynurenine pathway, mediated by indoleamine 2,3-dioxygenase (IDO), is a mechanism involved in tumor immunoresistance.	Kynurenine	42-52	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.	Kynurenine	42-52	indoleamine 2,3-dioxygenase 1	Homo sapiens	103-106
19693771-1	2009	Indoleamine 2,3-dioxygenase (IDO) is the rate-limiting enzyme in the kynurenine (Kyn) pathway of tryptophan (Trp) metabolism.	Kynurenine	69-79	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.	Kynurenine	69-79	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.	Kynurenine	81-84	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.	Kynurenine	81-84	indoleamine 2,3-dioxygenase 1	Homo sapiens	29-32
19853722-3	2009	The latter posits that IFN-alpha is responsible for central serotonin (5-HT) depletion by deviating its precursor, tryptophan (TRP), to a catabolic kynurenine (KYN) pathway through induction of indoleamine 2.3 dioxygenase (IDO).	Kynurenine	148-158	interferon alpha 1	Homo sapiens	23-32
19853722-3	2009	The latter posits that IFN-alpha is responsible for central serotonin (5-HT) depletion by deviating its precursor, tryptophan (TRP), to a catabolic kynurenine (KYN) pathway through induction of indoleamine 2.3 dioxygenase (IDO).	Kynurenine	160-163	interferon alpha 1	Homo sapiens	23-32
19268458-7	2009	In Balb/c mice, the gene expression of three kynurenine pathway enzymes (kynurenine aminotransferase I, kynurenine aminotransferase II, and quinolinate phospho-ribosyltransferase) increased 2- to 3.5-fold, whereas those in HIGA mice did not change significantly.	Kynurenine	45-55	kynurenine aminotransferase 1	Mus musculus	73-102
19580819-0	2009	l-kynurenine combined with probenecid and the novel synthetic kynurenic acid derivative attenuate nitroglycerin-induced nNOS in the rat caudal trigeminal nucleus.	Kynurenine	0-12	nitric oxide synthase 1	Rattus norvegicus	120-124
19477487-0	2009	Kynurenines and oxidative status are independently associated with thrombomodulin and von Willebrand factor levels in patients with end-stage renal disease.	Kynurenine	0-11	thrombomodulin	Homo sapiens	67-107
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.	Kynurenine	182-192	indoleamine 2,3-dioxygenase 1	Homo sapiens	35-39
19502010-8	2009	The combined risk posed by these related, complex genotypes is greater than any identified single locus and may derive from co-regulation of the kynurenine pathway by interacting genes, a lack of adequate melanotropin-controlled sequestration of the kynurenine-derived pigments, or the production of melanotropin receptor ligands through kynurenine metabolism.	Kynurenine	145-155	melanocortin 1 receptor	Homo sapiens	300-321
19477487-8	2009	TM and vWF were positively associated with kynurenine pathway metabolites: KYN, 3-HKYN, QA (all p&lt;0.001), and with SOX markers: Cu/Zn SOD (both p&lt;0.0001) and MDA levels (p&lt;0.05, and p&lt;0.0001; respectively) in the whole ESRD group.	Kynurenine	43-53	von Willebrand factor	Homo sapiens	7-10
19477487-8	2009	TM and vWF were positively associated with kynurenine pathway metabolites: KYN, 3-HKYN, QA (all p&lt;0.001), and with SOX markers: Cu/Zn SOD (both p&lt;0.0001) and MDA levels (p&lt;0.05, and p&lt;0.0001; respectively) in the whole ESRD group.	Kynurenine	75-78	von Willebrand factor	Homo sapiens	7-10
19477487-10	2009	Multiple stepwise regression analysis showed that KYN metabolites and oxidative status were the independent variables significantly associated with increased both TM and vWF levels in uremic patients.	Kynurenine	50-53	von Willebrand factor	Homo sapiens	170-173
19363598-4	2009	Compared with healthy donors (HD), the ratio of serum kynurenine to tryptophan (P &lt; 0.0001) was increased in GD patients, which was associated with the increased IDO expression in B cells (P &lt; 0.01) and DCs (P &lt; 0.01).	Kynurenine	54-64	indoleamine 2,3-dioxygenase 1	Homo sapiens	165-168
19268458-7	2009	In Balb/c mice, the gene expression of three kynurenine pathway enzymes (kynurenine aminotransferase I, kynurenine aminotransferase II, and quinolinate phospho-ribosyltransferase) increased 2- to 3.5-fold, whereas those in HIGA mice did not change significantly.	Kynurenine	45-55	aminoadipate aminotransferase	Mus musculus	104-134
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.	Kynurenine	45-55	indoleamine 2,3-dioxygenase 1	Homo sapiens	8-35
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.	Kynurenine	69-79	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-27
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.	Kynurenine	45-55	indoleamine 2,3-dioxygenase 1	Homo sapiens	37-40
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.	Kynurenine	69-79	indoleamine 2,3-dioxygenase 1	Homo sapiens	29-32
18612775-1	2009	Indoleamine 2,3-dioxygenase (IDO) catalyzes the first and rate-limiting step of Kynurenine pathway along the major route of Tryptophan catabolism.	Kynurenine	80-90	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-27
18612775-1	2009	Indoleamine 2,3-dioxygenase (IDO) catalyzes the first and rate-limiting step of Kynurenine pathway along the major route of Tryptophan catabolism.	Kynurenine	80-90	indoleamine 2,3-dioxygenase 1	Homo sapiens	29-32
19519465-1	2009	The enzyme indoleamine 2,3-dioxygenase (IDO) regulates immune responses through the capacity to degrade the essential amino acid tryptophan into kynurenine and other downstream metabolites that suppress effector T-cell function and favour the differentiation of regulatory T cells.	Kynurenine	145-155	indoleamine 2,3-dioxygenase 1	Homo sapiens	11-38
19402226-1	2009	Indoleamine 2,3-dioxygenase (IDO1) and tryptophan 2,3-dioxygenase (TDO) are tryptophan-degrading enzymes that catalyze the first step in tryptophan catabolism via the kynurenine pathway.	Kynurenine	167-177	indoleamine 2,3-dioxygenase 1	Ornithorhynchus anatinus	29-33
19402226-1	2009	Indoleamine 2,3-dioxygenase (IDO1) and tryptophan 2,3-dioxygenase (TDO) are tryptophan-degrading enzymes that catalyze the first step in tryptophan catabolism via the kynurenine pathway.	Kynurenine	167-177	tryptophan 2,3-dioxygenase	Ornithorhynchus anatinus	39-65
19402226-1	2009	Indoleamine 2,3-dioxygenase (IDO1) and tryptophan 2,3-dioxygenase (TDO) are tryptophan-degrading enzymes that catalyze the first step in tryptophan catabolism via the kynurenine pathway.	Kynurenine	167-177	tryptophan 2,3-dioxygenase	Ornithorhynchus anatinus	67-70
19416693-1	2009	Indoleamine 2,3-dioxygenase (IDO1) and tryptophan 2,3-dioxygenase (TDO) are tryptophan-degrading enzymes that catalyze the first step in tryptophan catabolism via the kynurenine pathway.	Kynurenine	167-177	indoleamine 2,3-dioxygenase 1	Ornithorhynchus anatinus	29-33
19416693-1	2009	Indoleamine 2,3-dioxygenase (IDO1) and tryptophan 2,3-dioxygenase (TDO) are tryptophan-degrading enzymes that catalyze the first step in tryptophan catabolism via the kynurenine pathway.	Kynurenine	167-177	tryptophan 2,3-dioxygenase	Ornithorhynchus anatinus	39-65
19416693-1	2009	Indoleamine 2,3-dioxygenase (IDO1) and tryptophan 2,3-dioxygenase (TDO) are tryptophan-degrading enzymes that catalyze the first step in tryptophan catabolism via the kynurenine pathway.	Kynurenine	167-177	tryptophan 2,3-dioxygenase	Ornithorhynchus anatinus	67-70
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.	Kynurenine	87-98	indoleamine 2,3-dioxygenase 1	Homo sapiens	103-106
19519465-1	2009	The enzyme indoleamine 2,3-dioxygenase (IDO) regulates immune responses through the capacity to degrade the essential amino acid tryptophan into kynurenine and other downstream metabolites that suppress effector T-cell function and favour the differentiation of regulatory T cells.	Kynurenine	145-155	indoleamine 2,3-dioxygenase 1	Homo sapiens	40-43
19262614-7	2009	Co-expression of FVIII and IDO in the liver was associated with increased plasma kynurenine levels, an inhibition of T-cell infiltration and increased apoptosis of T cells within the liver.	Kynurenine	81-91	coagulation factor VIII	Mus musculus	17-22
19262614-7	2009	Co-expression of FVIII and IDO in the liver was associated with increased plasma kynurenine levels, an inhibition of T-cell infiltration and increased apoptosis of T cells within the liver.	Kynurenine	81-91	indoleamine 2,3-dioxygenase 1	Mus musculus	27-30
19428689-1	2009	Tryptophan 2,3-dioxygenase (TDO), an initial and rate-limiting enzyme for the kynurenine pathway of tryptophan (Trp) metabolism, is thought to play an important role in systemic Trp metabolism as well as in emotional and psychiatric status.	Kynurenine	78-88	tryptophan 2,3-dioxygenase	Mus musculus	0-26
18562404-3	2009	In this study, we examined kynurenine pathway activity by measuring tryptophan breakdown, a number of pathway metabolites and interferon gamma (IFN-gamma), which is the preferential activator of the first-step enzyme, indoleamine dioxygenase (IDO), in the plasma of patients with major psychotic disorder.	Kynurenine	27-37	interferon gamma	Homo sapiens	126-153
18562404-3	2009	In this study, we examined kynurenine pathway activity by measuring tryptophan breakdown, a number of pathway metabolites and interferon gamma (IFN-gamma), which is the preferential activator of the first-step enzyme, indoleamine dioxygenase (IDO), in the plasma of patients with major psychotic disorder.	Kynurenine	27-37	indoleamine 2,3-dioxygenase 1	Homo sapiens	218-241
18562404-3	2009	In this study, we examined kynurenine pathway activity by measuring tryptophan breakdown, a number of pathway metabolites and interferon gamma (IFN-gamma), which is the preferential activator of the first-step enzyme, indoleamine dioxygenase (IDO), in the plasma of patients with major psychotic disorder.	Kynurenine	27-37	indoleamine 2,3-dioxygenase 1	Homo sapiens	243-246
19308046-0	2009	Indoleamine 2,3-dioxygenase overexpression causes kynurenine-modification of proteins, fiber cell apoptosis and cataract formation in the mouse lens.	Kynurenine	50-60	indoleamine 2,3-dioxygenase 1	Mus musculus	0-27
19308046-1	2009	Indoleamine 2,3-dioxygenase (IDO) is the first enzyme in the kynurenine pathway.	Kynurenine	61-71	indoleamine 2,3-dioxygenase 1	Mus musculus	0-27
19308046-1	2009	Indoleamine 2,3-dioxygenase (IDO) is the first enzyme in the kynurenine pathway.	Kynurenine	61-71	indoleamine 2,3-dioxygenase 1	Mus musculus	29-32
19308046-13	2009	Together these data demonstrate that IDO-mediated production of kynurenines results in defects in fiber cell differentiation and their apoptosis and suggest that IDO activity is kept low in the lens to prevent deleterious effects by kynurenines.	Kynurenine	64-75	indoleamine 2,3-dioxygenase 1	Mus musculus	37-40
19308046-13	2009	Together these data demonstrate that IDO-mediated production of kynurenines results in defects in fiber cell differentiation and their apoptosis and suggest that IDO activity is kept low in the lens to prevent deleterious effects by kynurenines.	Kynurenine	233-244	indoleamine 2,3-dioxygenase 1	Mus musculus	37-40
19308046-13	2009	Together these data demonstrate that IDO-mediated production of kynurenines results in defects in fiber cell differentiation and their apoptosis and suggest that IDO activity is kept low in the lens to prevent deleterious effects by kynurenines.	Kynurenine	233-244	indoleamine 2,3-dioxygenase 1	Mus musculus	162-165
18195714-4	2009	Both minocycline and 1-MT normalize the kynurenine/tryptophan ratio in the plasma and brain of LPS-treated mice without changing the LPS-induced increase in turnover of brain serotonin.	Kynurenine	40-50	toll-like receptor 4	Mus musculus	95-98
18195714-5	2009	Administration of L-kynurenine, a metabolite of tryptophan that is generated by IDO, to naive mice dose dependently induces depressive-like behavior.	Kynurenine	18-30	indoleamine 2,3-dioxygenase 1	Mus musculus	80-83
18195714-6	2009	These results implicate IDO as a critical molecular mediator of inflammation-induced depressive-like behavior, probably through the catabolism of tryptophan along the kynurenine pathway.	Kynurenine	167-177	indoleamine 2,3-dioxygenase 1	Mus musculus	24-27
19384564-6	2009	The results indicate that kynurenine metabolites can be neurotoxic via a caspase-3 independent mechanism, and that the minor metabolite 5HAA is as potent a toxin as the better documented compounds 3HK and 3HAA.	Kynurenine	26-36	caspase 3	Homo sapiens	73-82
19404944-1	2009	OBJECTIVE: Indoleamine 2,3 dioxygenase (IDO) is a catabolic enzyme that initiates the kynurenine pathway of tryptophan degradation and has immunomodulatory properties.	Kynurenine	86-96	indoleamine 2,3-dioxygenase 1	Mus musculus	11-38
19404944-1	2009	OBJECTIVE: Indoleamine 2,3 dioxygenase (IDO) is a catabolic enzyme that initiates the kynurenine pathway of tryptophan degradation and has immunomodulatory properties.	Kynurenine	86-96	indoleamine 2,3-dioxygenase 1	Mus musculus	40-43
19302241-5	2009	Our results showed that activity of IDO, as determined by high performance liquid chromatography analysis of the kynurenine/tryptophan ratio, was increased markedly in the serum and renal tissue of NTN mice, and immunohistochemistry revealed that expression of IDO was up-regulated significantly in glomeruli and renal tubular epithelial cells during NTN.	Kynurenine	113-123	indoleamine 2,3-dioxygenase 1	Mus musculus	36-39
19428689-1	2009	Tryptophan 2,3-dioxygenase (TDO), an initial and rate-limiting enzyme for the kynurenine pathway of tryptophan (Trp) metabolism, is thought to play an important role in systemic Trp metabolism as well as in emotional and psychiatric status.	Kynurenine	78-88	tryptophan 2,3-dioxygenase	Mus musculus	28-31
18986303-2	2009	The cytokine-inducible enzyme IDO (indoleamine 2,3-dioxygenase) initiates the degradation of the essential aromatic amino acid tryptophan via the kynurenine pathway and could contribute to deficient immune responsiveness.	Kynurenine	146-156	indoleamine 2,3-dioxygenase 1	Homo sapiens	35-62
18986303-2	2009	The cytokine-inducible enzyme IDO (indoleamine 2,3-dioxygenase) initiates the degradation of the essential aromatic amino acid tryptophan via the kynurenine pathway and could contribute to deficient immune responsiveness.	Kynurenine	146-156	indoleamine 2,3-dioxygenase 1	Homo sapiens	30-33
18986303-3	2009	Activated IDO is indicated by an increased kyn/trp (kynurenine/tryptophan) ratio.	Kynurenine	43-46	indoleamine 2,3-dioxygenase 1	Homo sapiens	10-13
18986303-3	2009	Activated IDO is indicated by an increased kyn/trp (kynurenine/tryptophan) ratio.	Kynurenine	52-62	indoleamine 2,3-dioxygenase 1	Homo sapiens	10-13
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).	Kynurenine	87-98	indoleamine 2,3-dioxygenase 1	Homo sapiens	134-163
19226371-1	2009	In the mammalian brain, kynurenine aminotransferase II (KAT II) and kynurenine 3-monooxygenase (KMO), key enzymes of the kynurenine pathway (KP) of tryptophan degradation, form the neuroactive metabolites kynurenic acid (KYNA) and 3-hydroxykynurenine (3-HK), respectively.	Kynurenine	24-34	aminoadipate aminotransferase	Homo sapiens	56-62
19226371-1	2009	In the mammalian brain, kynurenine aminotransferase II (KAT II) and kynurenine 3-monooxygenase (KMO), key enzymes of the kynurenine pathway (KP) of tryptophan degradation, form the neuroactive metabolites kynurenic acid (KYNA) and 3-hydroxykynurenine (3-HK), respectively.	Kynurenine	24-34	kynurenine 3-monooxygenase	Homo sapiens	96-99
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.	Kynurenine	154-165	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.	Kynurenine	154-165	indoleamine 2,3-dioxygenase 1	Rattus norvegicus	29-32
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.	Kynurenine	154-165	interferon gamma	Rattus norvegicus	96-112
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.	Kynurenine	154-165	interferon gamma	Rattus norvegicus	114-123
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).	Kynurenine	87-98	indoleamine 2,3-dioxygenase 1	Homo sapiens	165-169
19353519-8	2009	PKR and IFN-beta play a central, previously unidentified role in orchestrating the production of immunosuppressive kynurenines by MSC.	Kynurenine	115-126	eukaryotic translation initiation factor 2 alpha kinase 2	Homo sapiens	0-3
19353519-8	2009	PKR and IFN-beta play a central, previously unidentified role in orchestrating the production of immunosuppressive kynurenines by MSC.	Kynurenine	115-126	interferon beta 1	Homo sapiens	8-16
19209904-1	2009	The initial and rate-limiting step of the kynurenine pathway in humans involves the oxidation of tryptophan to N-formyl kynurenine catalyzed by two hemeproteins, tryptophan 2,3-dioxygenase (hTDO) and indoleamine 2,3-dioxygenase (hIDO).	Kynurenine	42-52	tryptophan 2,3-dioxygenase	Homo sapiens	162-188
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).	Kynurenine	81-91	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).	Kynurenine	81-91	indoleamine 2,3-dioxygenase 1	Homo sapiens	43-46
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).	Kynurenine	184-194	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).	Kynurenine	184-194	indoleamine 2,3-dioxygenase 1	Homo sapiens	43-46
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).	Kynurenine	196-199	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).	Kynurenine	196-199	indoleamine 2,3-dioxygenase 1	Homo sapiens	43-46
19323847-2	2009	Regarding tryptophan (Trp), the initial rate-limiting enzymes for the kynurenine pathway of tryptophan metabolism are tryptophan 2,3-dioxygenase (TDO) and indoleamine 2,3-dioxygenase (IDO).	Kynurenine	70-80	tryptophan 2,3-dioxygenase	Mus musculus	118-144
19323847-2	2009	Regarding tryptophan (Trp), the initial rate-limiting enzymes for the kynurenine pathway of tryptophan metabolism are tryptophan 2,3-dioxygenase (TDO) and indoleamine 2,3-dioxygenase (IDO).	Kynurenine	70-80	tryptophan 2,3-dioxygenase	Mus musculus	146-149
19323847-4	2009	Compared with wild-type littermates, Tdo(-/-) mice showed increased plasma levels of Trp and its metabolites 5-hydroxyindoleacetic acid (5-HIAA) and kynurenine, as well as increased levels of Trp, 5-HT and 5-HIAA in the hippocampus and midbrain.	Kynurenine	149-159	tryptophan 2,3-dioxygenase	Mus musculus	37-40
19209904-1	2009	The initial and rate-limiting step of the kynurenine pathway in humans involves the oxidation of tryptophan to N-formyl kynurenine catalyzed by two hemeproteins, tryptophan 2,3-dioxygenase (hTDO) and indoleamine 2,3-dioxygenase (hIDO).	Kynurenine	42-52	tryptophan 2,3-dioxygenase	Homo sapiens	190-194
18282734-0	2009	Indoleamine 2,3-dioxygenase-2; a new enzyme in the kynurenine pathway.	Kynurenine	51-61	indoleamine 2,3-dioxygenase 2	Mus musculus	0-29
18639339-1	2009	The enzyme indoleamine 2,3-dioxygenase (IDO) converts tryptophan to kynurenine, blocking T-cell activation and inducing immunosuppression.	Kynurenine	68-78	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.	Kynurenine	57-67	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.	Kynurenine	86-89	indoleamine 2,3-dioxygenase 1	Homo sapiens	127-130
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.	Kynurenine	133-143	indoleamine 2,3-dioxygenase 1	Rattus norvegicus	26-29
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.	Kynurenine	196-206	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.	Kynurenine	196-206	indoleamine 2,3-dioxygenase 1	Homo sapiens	134-137
19170761-5	2009	Kynureninase (KYNU) hydrolyzes kynurenine and 3-hydroxykynurenine to anthranilic acid and 3-hydroxyanthranilic acid, respectively.	Kynurenine	31-41	kynureninase	Bombyx mori	0-12
19170761-5	2009	Kynureninase (KYNU) hydrolyzes kynurenine and 3-hydroxykynurenine to anthranilic acid and 3-hydroxyanthranilic acid, respectively.	Kynurenine	31-41	kynureninase	Bombyx mori	14-18
19121343-1	2009	Indoleamine 2, 3-dioxygenase (IDO), which catabolizes L-tryptophan (L-TRP) to L-kynurenine (L-KYN), is an immunoregulatory factor that is up-regulated via an interferon-gamma (IFN-gamma)-dependent and/or -independent mechanism.	Kynurenine	78-90	indoleamine 2,3-dioxygenase 1	Mus musculus	0-28
19121343-1	2009	Indoleamine 2, 3-dioxygenase (IDO), which catabolizes L-tryptophan (L-TRP) to L-kynurenine (L-KYN), is an immunoregulatory factor that is up-regulated via an interferon-gamma (IFN-gamma)-dependent and/or -independent mechanism.	Kynurenine	78-90	indoleamine 2,3-dioxygenase 1	Mus musculus	30-33
19121343-1	2009	Indoleamine 2, 3-dioxygenase (IDO), which catabolizes L-tryptophan (L-TRP) to L-kynurenine (L-KYN), is an immunoregulatory factor that is up-regulated via an interferon-gamma (IFN-gamma)-dependent and/or -independent mechanism.	Kynurenine	78-90	interferon gamma	Mus musculus	158-174
19121343-1	2009	Indoleamine 2, 3-dioxygenase (IDO), which catabolizes L-tryptophan (L-TRP) to L-kynurenine (L-KYN), is an immunoregulatory factor that is up-regulated via an interferon-gamma (IFN-gamma)-dependent and/or -independent mechanism.	Kynurenine	78-90	interferon gamma	Mus musculus	176-185
19121343-1	2009	Indoleamine 2, 3-dioxygenase (IDO), which catabolizes L-tryptophan (L-TRP) to L-kynurenine (L-KYN), is an immunoregulatory factor that is up-regulated via an interferon-gamma (IFN-gamma)-dependent and/or -independent mechanism.	Kynurenine	92-97	indoleamine 2,3-dioxygenase 1	Mus musculus	0-28
19121343-1	2009	Indoleamine 2, 3-dioxygenase (IDO), which catabolizes L-tryptophan (L-TRP) to L-kynurenine (L-KYN), is an immunoregulatory factor that is up-regulated via an interferon-gamma (IFN-gamma)-dependent and/or -independent mechanism.	Kynurenine	92-97	indoleamine 2,3-dioxygenase 1	Mus musculus	30-33
19121343-1	2009	Indoleamine 2, 3-dioxygenase (IDO), which catabolizes L-tryptophan (L-TRP) to L-kynurenine (L-KYN), is an immunoregulatory factor that is up-regulated via an interferon-gamma (IFN-gamma)-dependent and/or -independent mechanism.	Kynurenine	92-97	interferon gamma	Mus musculus	158-174
19121343-1	2009	Indoleamine 2, 3-dioxygenase (IDO), which catabolizes L-tryptophan (L-TRP) to L-kynurenine (L-KYN), is an immunoregulatory factor that is up-regulated via an interferon-gamma (IFN-gamma)-dependent and/or -independent mechanism.	Kynurenine	92-97	interferon gamma	Mus musculus	176-185
19187269-2	2009	Decreases in cortical KYNA levels were achieved by local perfusion of S-ESBA, a selective inhibitor of the astrocytic enzyme kynurenine aminotransferase II (KAT II), which catalyses the formation of KYNA from its precursor L-kynurenine.	Kynurenine	223-235	aminoadipate aminotransferase	Rattus norvegicus	125-155
19187269-2	2009	Decreases in cortical KYNA levels were achieved by local perfusion of S-ESBA, a selective inhibitor of the astrocytic enzyme kynurenine aminotransferase II (KAT II), which catalyses the formation of KYNA from its precursor L-kynurenine.	Kynurenine	223-235	aminoadipate aminotransferase	Rattus norvegicus	157-163
19029248-2	2009	The enzyme was identified based on its high sequence identity with mammalian KAT I, but its activity toward kynurenine and its structural characteristics have not been established.	Kynurenine	108-118	kynurenine aminotransferase 1	Homo sapiens	77-82
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".	Kynurenine	209-220	transforming growth factor beta 1	Homo sapiens	56-64
19029248-5	2009	We established that mKAT III is able to efficiently catalyze the transamination of kynurenine to KYNA and has optimum activity at relatively basic conditions of around pH 9.0 and at relatively high temperatures of 50 to 60 degrees C. In addition, mKAT III is active toward a number of other amino acids.	Kynurenine	83-93	kynurenine aminotransferase 3	Mus musculus	20-28
19029248-5	2009	We established that mKAT III is able to efficiently catalyze the transamination of kynurenine to KYNA and has optimum activity at relatively basic conditions of around pH 9.0 and at relatively high temperatures of 50 to 60 degrees C. In addition, mKAT III is active toward a number of other amino acids.	Kynurenine	83-93	kynurenine aminotransferase 3	Mus musculus	247-255
19029248-7	2009	Through macromolecular crystallography, we determined the mKAT III crystal structure and its structures in complex with kynurenine and glutamine.	Kynurenine	120-130	kynurenine aminotransferase 3	Mus musculus	58-66
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".	Kynurenine	209-220	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".	Kynurenine	209-220	indoleamine 2,3-dioxygenase 1	Homo sapiens	167-170
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.	Kynurenine	233-243	tryptophan 2,3-dioxygenase	Homo sapiens	18-21
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.	Kynurenine	99-109	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-3
19228097-9	2009	The IDO enzymatic activity was determined by measuring the kynurenine level using a colorimetric method.	Kynurenine	59-69	indoleamine 2,3-dioxygenase 1	Homo sapiens	4-7
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.	Kynurenine	233-243	tryptophan 2,3-dioxygenase	Homo sapiens	23-49
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.	Kynurenine	233-243	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.	Kynurenine	233-243	indoleamine 2,3-dioxygenase 1	Homo sapiens	60-87
18823288-10	2008	No difference in IFN-gamma levels was observed between groups; however, IFN-gamma was positively correlated with Kyn:Trp in IBS (r = 0.58, P = 0.005) but not controls (r = 0.12, P = 0.5).	Kynurenine	113-116	interferon gamma	Homo sapiens	72-81
18676626-1	2008	PURPOSE: Indolemine 2,3-dioxygenase (IDO)-mediated oxidation of tryptophan produces kynurenines (KYNs), which may play a role in cataract formation.	Kynurenine	84-95	indoleamine 2,3-dioxygenase 1	Homo sapiens	9-35
18676626-1	2008	PURPOSE: Indolemine 2,3-dioxygenase (IDO)-mediated oxidation of tryptophan produces kynurenines (KYNs), which may play a role in cataract formation.	Kynurenine	84-95	indoleamine 2,3-dioxygenase 1	Homo sapiens	37-40
18676626-1	2008	PURPOSE: Indolemine 2,3-dioxygenase (IDO)-mediated oxidation of tryptophan produces kynurenines (KYNs), which may play a role in cataract formation.	Kynurenine	97-101	indoleamine 2,3-dioxygenase 1	Homo sapiens	9-35
18676626-1	2008	PURPOSE: Indolemine 2,3-dioxygenase (IDO)-mediated oxidation of tryptophan produces kynurenines (KYNs), which may play a role in cataract formation.	Kynurenine	97-101	indoleamine 2,3-dioxygenase 1	Homo sapiens	37-40
18676626-5	2008	IDO activity was measured by quantifying kynurenine (KYN) by HPLC.	Kynurenine	41-51	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-3
18676626-5	2008	IDO activity was measured by quantifying kynurenine (KYN) by HPLC.	Kynurenine	53-56	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-3
18823288-2	2008	Tryptophan forms the substrate for serotonin biosynthesis, but it can alternatively be catabolized to kynurenine (Kyn) by the enzyme indoleamine 2,3-dioxygenase (IDO), the main inducer of which is interferon-gamma.	Kynurenine	102-112	interferon gamma	Homo sapiens	197-213
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.	Kynurenine	174-184	indoleamine 2,3-dioxygenase 1	Homo sapiens	27-30
18823288-2	2008	Tryptophan forms the substrate for serotonin biosynthesis, but it can alternatively be catabolized to kynurenine (Kyn) by the enzyme indoleamine 2,3-dioxygenase (IDO), the main inducer of which is interferon-gamma.	Kynurenine	114-117	interferon gamma	Homo sapiens	197-213
18950381-3	2008	Cytokines including IFN-alpha induce the enzyme indoleamine 2,3-dioxygenase (IDO), which converts TRP to kynurenine (KYN), leading to a shortage of serotonin (5-HT).	Kynurenine	105-115	interferon alpha 1	Homo sapiens	20-29
19106591-2	2008	IDO activity can be measured by tryptophan (Trp)/kynurenine (Kyn) ratio.	Kynurenine	49-59	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-3
19106591-2	2008	IDO activity can be measured by tryptophan (Trp)/kynurenine (Kyn) ratio.	Kynurenine	61-64	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-3
18619832-9	2008	In these patients, IDO gene expression correlated with kynurenine/tryptophan ratio in sera.	Kynurenine	55-65	indoleamine 2,3-dioxygenase 1	Homo sapiens	19-22
18950381-3	2008	Cytokines including IFN-alpha induce the enzyme indoleamine 2,3-dioxygenase (IDO), which converts TRP to kynurenine (KYN), leading to a shortage of serotonin (5-HT).	Kynurenine	117-120	interferon alpha 1	Homo sapiens	20-29
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.	Kynurenine	106-116	indoleamine 2,3-dioxygenase 1	Homo sapiens	17-44
18584961-11	2008	These data are the first to demonstrate that a systemic inflammatory challenge stimulates KMO expression in brain; a situation that is likely to favour kynurenine metabolism in a neurotoxic direction.	Kynurenine	152-162	kynurenine 3-monooxygenase	Rattus norvegicus	90-93
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.	Kynurenine	115-125	indoleamine 2,3-dioxygenase 1	Homo sapiens	29-32
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.	Kynurenine	97-107	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.	Kynurenine	97-107	indoleamine 2,3-dioxygenase 1	Homo sapiens	29-32
18671950-6	2008	This effect was not induced by increased IFN-gamma release by APC, and it was functionally correlated with increased L-kynurenine (L-KYN) release by alpha-GalCer-treated CD1d-transfected THP-1 cells.	Kynurenine	117-129	CD1d molecule	Homo sapiens	170-174
18671950-6	2008	This effect was not induced by increased IFN-gamma release by APC, and it was functionally correlated with increased L-kynurenine (L-KYN) release by alpha-GalCer-treated CD1d-transfected THP-1 cells.	Kynurenine	117-129	GLI family zinc finger 2	Homo sapiens	187-192
18671950-6	2008	This effect was not induced by increased IFN-gamma release by APC, and it was functionally correlated with increased L-kynurenine (L-KYN) release by alpha-GalCer-treated CD1d-transfected THP-1 cells.	Kynurenine	131-136	CD1d molecule	Homo sapiens	170-174
18671950-6	2008	This effect was not induced by increased IFN-gamma release by APC, and it was functionally correlated with increased L-kynurenine (L-KYN) release by alpha-GalCer-treated CD1d-transfected THP-1 cells.	Kynurenine	131-136	GLI family zinc finger 2	Homo sapiens	187-192
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.	Kynurenine	121-133	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-27
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.	Kynurenine	121-133	indoleamine 2,3-dioxygenase 1	Homo sapiens	29-32
18712654-6	2008	Supplementation with interferon-gamma could up-regulate this basal L-kynurenine production.	Kynurenine	67-79	interferon gamma	Homo sapiens	21-37
18426872-5	2008	Kynurenine and picolinic acid, two IDO-generated metabolites of tryptophan, were able to inhibit lipopolysaccharide-induced antibody production by splenocytes in vitro, and kynurenine also induced B-cell apoptosis, findings that provide an explanation for the elevated Ig levels in animals lacking IDO.	Kynurenine	0-10	indoleamine 2,3-dioxygenase 1	Mus musculus	35-38
18426872-5	2008	Kynurenine and picolinic acid, two IDO-generated metabolites of tryptophan, were able to inhibit lipopolysaccharide-induced antibody production by splenocytes in vitro, and kynurenine also induced B-cell apoptosis, findings that provide an explanation for the elevated Ig levels in animals lacking IDO.	Kynurenine	0-10	indoleamine 2,3-dioxygenase 1	Mus musculus	298-301
18426872-5	2008	Kynurenine and picolinic acid, two IDO-generated metabolites of tryptophan, were able to inhibit lipopolysaccharide-induced antibody production by splenocytes in vitro, and kynurenine also induced B-cell apoptosis, findings that provide an explanation for the elevated Ig levels in animals lacking IDO.	Kynurenine	173-183	indoleamine 2,3-dioxygenase 1	Mus musculus	35-38
18501338-1	2008	Indoleamine 2,3-dioxygenase (IDO) is the rate-limiting enzyme in the kynurenine pathway that converts L-tryptophan to L-kynurenine.	Kynurenine	69-79	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-27
18501338-1	2008	Indoleamine 2,3-dioxygenase (IDO) is the rate-limiting enzyme in the kynurenine pathway that converts L-tryptophan to L-kynurenine.	Kynurenine	69-79	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.	Kynurenine	118-130	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-27
18501338-1	2008	Indoleamine 2,3-dioxygenase (IDO) is the rate-limiting enzyme in the kynurenine pathway that converts L-tryptophan to L-kynurenine.	Kynurenine	118-130	indoleamine 2,3-dioxygenase 1	Homo sapiens	29-32
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.	Kynurenine	106-116	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.	Kynurenine	106-116	indoleamine 2,3-dioxygenase 1	Homo sapiens	175-178
18465467-2	2008	The kynurenine (KYN) pathway, which is initiated by indoleamine 2,3-dioxygenase (IDO), is the main TRP metabolic pathway.	Kynurenine	4-14	indoleamine 2,3-dioxygenase 1	Homo sapiens	52-79
17945348-2	2008	Interferon-gamma (IFN-gamma) triggers several antiviral mechanisms in target cells including the induction of indoleamine-2,3-dioxygenase (IDO), which degrades the essential amino acid tryptophan to kynurenine.	Kynurenine	199-209	interferon gamma	Homo sapiens	0-16
17945348-2	2008	Interferon-gamma (IFN-gamma) triggers several antiviral mechanisms in target cells including the induction of indoleamine-2,3-dioxygenase (IDO), which degrades the essential amino acid tryptophan to kynurenine.	Kynurenine	199-209	interferon gamma	Homo sapiens	18-27
17945348-2	2008	Interferon-gamma (IFN-gamma) triggers several antiviral mechanisms in target cells including the induction of indoleamine-2,3-dioxygenase (IDO), which degrades the essential amino acid tryptophan to kynurenine.	Kynurenine	199-209	indoleamine 2,3-dioxygenase 1	Homo sapiens	110-137
17945348-2	2008	Interferon-gamma (IFN-gamma) triggers several antiviral mechanisms in target cells including the induction of indoleamine-2,3-dioxygenase (IDO), which degrades the essential amino acid tryptophan to kynurenine.	Kynurenine	199-209	indoleamine 2,3-dioxygenase 1	Homo sapiens	139-142
18465467-2	2008	The kynurenine (KYN) pathway, which is initiated by indoleamine 2,3-dioxygenase (IDO), is the main TRP metabolic pathway.	Kynurenine	4-14	indoleamine 2,3-dioxygenase 1	Homo sapiens	81-84
18465467-2	2008	The kynurenine (KYN) pathway, which is initiated by indoleamine 2,3-dioxygenase (IDO), is the main TRP metabolic pathway.	Kynurenine	16-19	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.	Kynurenine	16-19	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).	Kynurenine	24-36	tryptophan 2,3-dioxygenase	Homo sapiens	141-167
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).	Kynurenine	24-36	tryptophan 2,3-dioxygenase	Homo sapiens	169-172
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).	Kynurenine	24-36	indoleamine 2,3-dioxygenase 1	Homo sapiens	177-204
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).	Kynurenine	24-36	indoleamine 2,3-dioxygenase 1	Homo sapiens	206-209
18390695-6	2008	Recent data support a view in which IL-23/IL-17 antagonistic strategies, including the administration of synthetic kynurenines, could represent a new means of harnessing progressive or potentially harmful inflammation.	Kynurenine	115-126	interleukin 23 subunit alpha	Homo sapiens	36-41
18390695-6	2008	Recent data support a view in which IL-23/IL-17 antagonistic strategies, including the administration of synthetic kynurenines, could represent a new means of harnessing progressive or potentially harmful inflammation.	Kynurenine	115-126	interleukin 17A	Homo sapiens	42-47
18171698-7	2008	Upon hCG treatment, IDO mRNA expression and its metabolite kynurenine were increased by LPS- and IFN-gamma-stimulated DC, suggesting its involvement in the decreased T cell proliferation.	Kynurenine	59-69	chorionic gonadotropin subunit beta 5	Homo sapiens	5-8
18179817-9	2008	CONCLUSION: During immunotherapy, the tryptophan metabolites kynurenine, 3-hydroxykynurenine, and xanthurenic acid generated through IDO contribute to tolerance induction regarding TH2-dependent allergic airway inflammation.	Kynurenine	61-71	indoleamine 2,3-dioxygenase 1	Mus musculus	133-136
18179817-9	2008	CONCLUSION: During immunotherapy, the tryptophan metabolites kynurenine, 3-hydroxykynurenine, and xanthurenic acid generated through IDO contribute to tolerance induction regarding TH2-dependent allergic airway inflammation.	Kynurenine	61-71	heart and neural crest derivatives expressed 2	Mus musculus	181-184
18171698-7	2008	Upon hCG treatment, IDO mRNA expression and its metabolite kynurenine were increased by LPS- and IFN-gamma-stimulated DC, suggesting its involvement in the decreased T cell proliferation.	Kynurenine	59-69	interferon gamma	Homo sapiens	97-106
18056995-5	2008	In this article, we report a 2.16 A crystal structure of hKAT-II and a 1.95 A structure of its complex with kynurenine.	Kynurenine	108-118	aminoadipate aminotransferase	Homo sapiens	57-64
18158157-0	2008	Diazotization of kynurenine by acidified nitrite secreted from indoleamine 2,3-dioxygenase-expressing myeloid dendritic cells.	Kynurenine	17-27	indoleamine 2,3-dioxygenase 1	Mus musculus	63-90
18158157-1	2008	Indoleamine 2,3-dioxygenase (IDO)-initiated tryptophan metabolism along the kynurenine (Kyn) pathway regulates T-cell responses in some dendritic cells (DC) such as plasmacytoid DC.	Kynurenine	76-86	indoleamine 2,3-dioxygenase 1	Mus musculus	0-27
18158157-1	2008	Indoleamine 2,3-dioxygenase (IDO)-initiated tryptophan metabolism along the kynurenine (Kyn) pathway regulates T-cell responses in some dendritic cells (DC) such as plasmacytoid DC.	Kynurenine	76-86	indoleamine 2,3-dioxygenase 1	Mus musculus	29-32
18158157-1	2008	Indoleamine 2,3-dioxygenase (IDO)-initiated tryptophan metabolism along the kynurenine (Kyn) pathway regulates T-cell responses in some dendritic cells (DC) such as plasmacytoid DC.	Kynurenine	88-91	indoleamine 2,3-dioxygenase 1	Mus musculus	0-27
18158157-1	2008	Indoleamine 2,3-dioxygenase (IDO)-initiated tryptophan metabolism along the kynurenine (Kyn) pathway regulates T-cell responses in some dendritic cells (DC) such as plasmacytoid DC.	Kynurenine	88-91	indoleamine 2,3-dioxygenase 1	Mus musculus	29-32
18179826-0	2008	High-affinity uptake of kynurenine and nitric oxide-mediated inhibition of indoleamine 2,3-dioxygenase in bone marrow-derived myeloid dendritic cells.	Kynurenine	24-34	indoleamine 2,3-dioxygenase 1	Mus musculus	75-102
18179826-1	2008	Indoleamine 2,3-dioxygenase (IDO)-initiated tryptophan metabolism along the kynurenine (Kyn) pathway in some dendritic cells (DC) such as plasmacytoid DC (pDC) regulates T-cell responses.	Kynurenine	76-86	indoleamine 2,3-dioxygenase 1	Mus musculus	0-27
18179826-1	2008	Indoleamine 2,3-dioxygenase (IDO)-initiated tryptophan metabolism along the kynurenine (Kyn) pathway in some dendritic cells (DC) such as plasmacytoid DC (pDC) regulates T-cell responses.	Kynurenine	76-86	indoleamine 2,3-dioxygenase 1	Mus musculus	29-32
18179826-1	2008	Indoleamine 2,3-dioxygenase (IDO)-initiated tryptophan metabolism along the kynurenine (Kyn) pathway in some dendritic cells (DC) such as plasmacytoid DC (pDC) regulates T-cell responses.	Kynurenine	88-91	indoleamine 2,3-dioxygenase 1	Mus musculus	0-27
18179826-1	2008	Indoleamine 2,3-dioxygenase (IDO)-initiated tryptophan metabolism along the kynurenine (Kyn) pathway in some dendritic cells (DC) such as plasmacytoid DC (pDC) regulates T-cell responses.	Kynurenine	88-91	indoleamine 2,3-dioxygenase 1	Mus musculus	29-32
18205391-6	2008	We used combined crystallographic, bioinformatic and biochemical methods to demonstrate that Bna3p is not an FKF but rather is most likely the yeast kynurenine aminotransferase, which converts kynurenine to kynurenic acid.	Kynurenine	149-159	kynurenine--oxoglutarate transaminase	Saccharomyces cerevisiae S288C	93-98
18079112-0	2008	Histone deacetylase inhibition modulates kynurenine pathway activation in yeast, microglia, and mice expressing a mutant huntingtin fragment.	Kynurenine	41-51	histone deacetylase	Saccharomyces cerevisiae S288C	0-19
18079112-0	2008	Histone deacetylase inhibition modulates kynurenine pathway activation in yeast, microglia, and mice expressing a mutant huntingtin fragment.	Kynurenine	41-51	huntingtin	Mus musculus	121-131
18079112-1	2008	The kynurenine pathway of tryptophan degradation is hypothesized to play an important role in Huntington disease, a neurodegenerative disorder caused by a polyglutamine expansion in the protein huntingtin.	Kynurenine	4-14	huntingtin	Mus musculus	194-204
18079112-3	2008	Here we report that expression of a mutant huntingtin fragment was sufficient to induce transcription of the kynurenine pathway in yeast and that this induction was abrogated by impairing the activity of the histone deacetylase Rpd3.	Kynurenine	109-119	huntingtin	Mus musculus	43-53
18079112-3	2008	Here we report that expression of a mutant huntingtin fragment was sufficient to induce transcription of the kynurenine pathway in yeast and that this induction was abrogated by impairing the activity of the histone deacetylase Rpd3.	Kynurenine	109-119	histone deacetylase	Saccharomyces cerevisiae S288C	208-227
18079112-3	2008	Here we report that expression of a mutant huntingtin fragment was sufficient to induce transcription of the kynurenine pathway in yeast and that this induction was abrogated by impairing the activity of the histone deacetylase Rpd3.	Kynurenine	109-119	histone deacetylase RPD3	Saccharomyces cerevisiae S288C	228-232
18079112-4	2008	Moreover, numerous genetic suppressors of mutant huntingtin toxicity that are functionally unrelated converged unexpectedly on the kynurenine pathway, supporting a critical role for the kynurenine pathway in mediating mutant huntingtin toxicity in yeast.	Kynurenine	131-141	huntingtin	Mus musculus	49-59
18079112-4	2008	Moreover, numerous genetic suppressors of mutant huntingtin toxicity that are functionally unrelated converged unexpectedly on the kynurenine pathway, supporting a critical role for the kynurenine pathway in mediating mutant huntingtin toxicity in yeast.	Kynurenine	131-141	huntingtin	Mus musculus	225-235
18079112-4	2008	Moreover, numerous genetic suppressors of mutant huntingtin toxicity that are functionally unrelated converged unexpectedly on the kynurenine pathway, supporting a critical role for the kynurenine pathway in mediating mutant huntingtin toxicity in yeast.	Kynurenine	186-196	huntingtin	Mus musculus	49-59
18079112-4	2008	Moreover, numerous genetic suppressors of mutant huntingtin toxicity that are functionally unrelated converged unexpectedly on the kynurenine pathway, supporting a critical role for the kynurenine pathway in mediating mutant huntingtin toxicity in yeast.	Kynurenine	186-196	huntingtin	Mus musculus	225-235
18079112-5	2008	Histone deacetylase-dependent regulation of the kynurenine pathway was also observed in a mouse model of Huntington disease, in which treatment with a neuroprotective histone deacetylase inhibitor blocked activation of the kynurenine pathway in microglia expressing a mutant huntingtin fragment in vitro and in vivo.	Kynurenine	48-58	histone deacetylase	Saccharomyces cerevisiae S288C	0-19
18079112-5	2008	Histone deacetylase-dependent regulation of the kynurenine pathway was also observed in a mouse model of Huntington disease, in which treatment with a neuroprotective histone deacetylase inhibitor blocked activation of the kynurenine pathway in microglia expressing a mutant huntingtin fragment in vitro and in vivo.	Kynurenine	48-58	histone deacetylase	Saccharomyces cerevisiae S288C	167-186
18079112-5	2008	Histone deacetylase-dependent regulation of the kynurenine pathway was also observed in a mouse model of Huntington disease, in which treatment with a neuroprotective histone deacetylase inhibitor blocked activation of the kynurenine pathway in microglia expressing a mutant huntingtin fragment in vitro and in vivo.	Kynurenine	48-58	huntingtin	Mus musculus	275-285
18079112-5	2008	Histone deacetylase-dependent regulation of the kynurenine pathway was also observed in a mouse model of Huntington disease, in which treatment with a neuroprotective histone deacetylase inhibitor blocked activation of the kynurenine pathway in microglia expressing a mutant huntingtin fragment in vitro and in vivo.	Kynurenine	223-233	histone deacetylase	Saccharomyces cerevisiae S288C	0-19
18079112-5	2008	Histone deacetylase-dependent regulation of the kynurenine pathway was also observed in a mouse model of Huntington disease, in which treatment with a neuroprotective histone deacetylase inhibitor blocked activation of the kynurenine pathway in microglia expressing a mutant huntingtin fragment in vitro and in vivo.	Kynurenine	223-233	histone deacetylase	Saccharomyces cerevisiae S288C	167-186
18079112-5	2008	Histone deacetylase-dependent regulation of the kynurenine pathway was also observed in a mouse model of Huntington disease, in which treatment with a neuroprotective histone deacetylase inhibitor blocked activation of the kynurenine pathway in microglia expressing a mutant huntingtin fragment in vitro and in vivo.	Kynurenine	223-233	huntingtin	Mus musculus	275-285
18311604-1	2008	The kynurenine (KYN) pathway, which is initiated by indoleamine 2,3-dioxygenase (IDO), is a tryptophan (TRP) metabolic pathway.	Kynurenine	4-14	indoleamine 2,3-dioxygenase 1	Mus musculus	52-79
18311604-1	2008	The kynurenine (KYN) pathway, which is initiated by indoleamine 2,3-dioxygenase (IDO), is a tryptophan (TRP) metabolic pathway.	Kynurenine	4-14	indoleamine 2,3-dioxygenase 1	Mus musculus	81-84
18311604-1	2008	The kynurenine (KYN) pathway, which is initiated by indoleamine 2,3-dioxygenase (IDO), is a tryptophan (TRP) metabolic pathway.	Kynurenine	16-19	indoleamine 2,3-dioxygenase 1	Mus musculus	52-79
18311604-1	2008	The kynurenine (KYN) pathway, which is initiated by indoleamine 2,3-dioxygenase (IDO), is a tryptophan (TRP) metabolic pathway.	Kynurenine	16-19	indoleamine 2,3-dioxygenase 1	Mus musculus	81-84
18185592-6	2008	Here we show that a superoxide-dependent step in tryptophan metabolism along the kynurenine pathway is blocked in CGD mice with lethal pulmonary aspergillosis, leading to unrestrained Vgamma1(+) gammadelta T-cell reactivity, dominant production of interleukin (IL)-17, defective regulatory T-cell activity and acute inflammatory lung injury.	Kynurenine	81-91	interleukin 17A	Mus musculus	248-267
18082271-1	2008	The influence of de novo synthesis of nicotinamide adenine dinucleotide (NAD) through the kynurenine (KYN) pathway of tryptophan (TRP) degradation on gene transcription of inducible nitric oxide synthase (iNOS) and nitric oxide (NO) production in chicken interferon gamma (ChIFN-gamma)-stimulated and non-stimulated chicken macrophage cell line HD11 was investigated.	Kynurenine	90-100	lysosomal-associated protein transmembrane 4A	Mus musculus	130-133
18082271-1	2008	The influence of de novo synthesis of nicotinamide adenine dinucleotide (NAD) through the kynurenine (KYN) pathway of tryptophan (TRP) degradation on gene transcription of inducible nitric oxide synthase (iNOS) and nitric oxide (NO) production in chicken interferon gamma (ChIFN-gamma)-stimulated and non-stimulated chicken macrophage cell line HD11 was investigated.	Kynurenine	90-100	nitric oxide synthase 2	Gallus gallus	172-203
18082271-1	2008	The influence of de novo synthesis of nicotinamide adenine dinucleotide (NAD) through the kynurenine (KYN) pathway of tryptophan (TRP) degradation on gene transcription of inducible nitric oxide synthase (iNOS) and nitric oxide (NO) production in chicken interferon gamma (ChIFN-gamma)-stimulated and non-stimulated chicken macrophage cell line HD11 was investigated.	Kynurenine	102-105	lysosomal-associated protein transmembrane 4A	Mus musculus	130-133
18082271-1	2008	The influence of de novo synthesis of nicotinamide adenine dinucleotide (NAD) through the kynurenine (KYN) pathway of tryptophan (TRP) degradation on gene transcription of inducible nitric oxide synthase (iNOS) and nitric oxide (NO) production in chicken interferon gamma (ChIFN-gamma)-stimulated and non-stimulated chicken macrophage cell line HD11 was investigated.	Kynurenine	102-105	nitric oxide synthase 2	Gallus gallus	172-203
17594069-1	2007	The tryptophan-catabolizing enzyme indoleamine-2,3-dioxygenase (IDO) initiates the first and rate-limiting step of the kynurenine pathway.	Kynurenine	119-129	indoleamine 2,3-dioxygenase 1	Homo sapiens	35-62
21249536-0	2008	LIM kinase-1 in the cerebral ganglion of Drosophila with genetic disturbances of kynurenine balance.	Kynurenine	81-91	LIM domain kinase 1	Drosophila melanogaster	0-12
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.	Kynurenine	162-172	interferon gamma	Homo sapiens	14-23
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.	Kynurenine	162-172	nitric oxide synthase 2	Homo sapiens	27-31
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.	Kynurenine	162-172	interferon gamma	Homo sapiens	102-111
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.	Kynurenine	162-172	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.	Kynurenine	229-240	interferon gamma	Homo sapiens	14-23
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.	Kynurenine	229-240	nitric oxide synthase 2	Homo sapiens	27-31
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.	Kynurenine	229-240	interferon gamma	Homo sapiens	102-111
18077563-7	2007	IFN-gamma production is controlled by (IFN-gamma) + 874(T/A) genotypes, suggesting the association of a high promoter T allele with the high rate of IFN-gamma production and, consequently, with activated IDO and enhanced production of kynurenines.	Kynurenine	235-246	interferon gamma	Homo sapiens	0-9
18077563-7	2007	IFN-gamma production is controlled by (IFN-gamma) + 874(T/A) genotypes, suggesting the association of a high promoter T allele with the high rate of IFN-gamma production and, consequently, with activated IDO and enhanced production of kynurenines.	Kynurenine	235-246	interferon gamma	Homo sapiens	39-48
18077563-7	2007	IFN-gamma production is controlled by (IFN-gamma) + 874(T/A) genotypes, suggesting the association of a high promoter T allele with the high rate of IFN-gamma production and, consequently, with activated IDO and enhanced production of kynurenines.	Kynurenine	235-246	interferon gamma	Homo sapiens	39-48
18077563-7	2007	IFN-gamma production is controlled by (IFN-gamma) + 874(T/A) genotypes, suggesting the association of a high promoter T allele with the high rate of IFN-gamma production and, consequently, with activated IDO and enhanced production of kynurenines.	Kynurenine	235-246	indoleamine 2,3-dioxygenase 1	Homo sapiens	204-207
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.	Kynurenine	53-63	interferon gamma	Homo sapiens	14-23
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.	Kynurenine	53-63	nitric oxide synthase 2	Homo sapiens	27-31
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.	Kynurenine	53-63	interferon gamma	Homo sapiens	102-111
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.	Kynurenine	53-63	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.	Kynurenine	53-63	indoleamine 2,3-dioxygenase 1	Homo sapiens	211-214
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.	Kynurenine	53-63	nitric oxide synthase 2	Homo sapiens	294-298
17594069-1	2007	The tryptophan-catabolizing enzyme indoleamine-2,3-dioxygenase (IDO) initiates the first and rate-limiting step of the kynurenine pathway.	Kynurenine	119-129	indoleamine 2,3-dioxygenase 1	Homo sapiens	64-67
17594069-5	2007	This protective effect could to be counteracted by the production of neurotoxic metabolites of the kynurenine pathway such as quinolinic acid, which are produced upon IDO induction.	Kynurenine	99-109	indoleamine 2,3-dioxygenase 1	Homo sapiens	167-170
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.	Kynurenine	65-75	indoleamine 2,3-dioxygenase 1	Homo sapiens	43-46
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.	Kynurenine	185-195	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.	Kynurenine	185-195	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.	Kynurenine	185-195	tryptophan 2,3-dioxygenase	Homo sapiens	38-64
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.	Kynurenine	185-195	tryptophan 2,3-dioxygenase	Homo sapiens	66-69
18063923-9	2007	It is concluded that kynurenine, kynurenic acid, and xanthurenic acid have anti-inflammatory effects trough a reduction of IFNgamma, whereas quinolinic acid has pro-inflammatory effects in particular via significant decreases in IL-10.	Kynurenine	21-31	interleukin 10	Homo sapiens	229-234
18063923-7	2007	Kynurenine, kynurenic acid, and xanthurenic acid, decreased the IFNgamma/IL-10 production ratio, whereas quinolinic acid increased this ratio.	Kynurenine	0-10	interferon gamma	Homo sapiens	64-72
18063923-10	2007	Following inflammation-induced IDO activation, some TRYCATs, i.e. kynurenine, kynurenic acid, and xanthurenic acid, exert a negative feedback control over IFNgamma production thus downregulating the initial inflammation, whereas an excess of quinolinic acid further aggravates the initial inflammation.	Kynurenine	66-76	indoleamine 2,3-dioxygenase 1	Homo sapiens	31-34
18063923-10	2007	Following inflammation-induced IDO activation, some TRYCATs, i.e. kynurenine, kynurenic acid, and xanthurenic acid, exert a negative feedback control over IFNgamma production thus downregulating the initial inflammation, whereas an excess of quinolinic acid further aggravates the initial inflammation.	Kynurenine	66-76	interferon gamma	Homo sapiens	155-163
18063923-7	2007	Kynurenine, kynurenic acid, and xanthurenic acid, decreased the IFNgamma/IL-10 production ratio, whereas quinolinic acid increased this ratio.	Kynurenine	0-10	interleukin 10	Homo sapiens	73-78
18063923-9	2007	It is concluded that kynurenine, kynurenic acid, and xanthurenic acid have anti-inflammatory effects trough a reduction of IFNgamma, whereas quinolinic acid has pro-inflammatory effects in particular via significant decreases in IL-10.	Kynurenine	21-31	interferon gamma	Homo sapiens	123-131
17892481-7	2007	Some form of anti-inflammatory intervention between the rise of S100B and the activation of microglia, including inhibition of the kynurenine pathway, may be valuable in modifying patient morbidity and mortality.	Kynurenine	131-141	S100 calcium binding protein B	Homo sapiens	64-69
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.	Kynurenine	20-30	indoleamine 2,3-dioxygenase 1	Homo sapiens	56-59
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.	Kynurenine	176-186	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.	Kynurenine	176-186	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).	Kynurenine	43-53	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).	Kynurenine	43-46	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.	Kynurenine	65-75	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-3
17870068-11	2007	Culture supernatants from IFN-gamma treated primary and metastatic uveal melanoma cell cultures contained elevated levels of kynurenine.	Kynurenine	125-135	interferon gamma	Homo sapiens	26-35
17870068-12	2007	Addition of the IDO inhibitor 1-methyl dl-tryptophan significantly diminished kynurenine levels in IFN-gamma treated uveal melanoma cell cultures.	Kynurenine	78-88	indoleamine 2,3-dioxygenase 1	Homo sapiens	16-19
17870068-12	2007	Addition of the IDO inhibitor 1-methyl dl-tryptophan significantly diminished kynurenine levels in IFN-gamma treated uveal melanoma cell cultures.	Kynurenine	78-88	interferon gamma	Homo sapiens	99-108
17632406-3	2007	Altogether, these data indicate that, in addition to tryptophan starvation induced by IDO activity, the paracrine production of kynurenines by enzymes downstream of IDO can also contribute to tolerogenesis in DCs, independently of tryptophan deprivation.	Kynurenine	128-139	indoleamine 2,3-dioxygenase 1	Mus musculus	165-168
17896864-9	2007	The strict coupling protects cells that overproduce IDO from kynurenine accumulation.	Kynurenine	61-71	indoleamine 2,3-dioxygenase 1	Homo sapiens	52-55
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).	Kynurenine	79-89	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).	Kynurenine	79-89	indoleamine 2,3-dioxygenase 1	Homo sapiens	29-32
17574268-4	2007	The antibody recognized proteins (human lens proteins, RNase A and BSA) that were modified by either kynurenine or N-formylkynurenine.	Kynurenine	101-111	ribonuclease A family member 1, pancreatic	Homo sapiens	55-62
18069344-0	2007	[Mutations in structural genes of tryptophan metabolic enzymes of the kynurenine pathway modulate some units of the L-glutamate receptor--actin cytoskeleton signaling cascade].	Kynurenine	70-80	Actin 79B	Drosophila melanogaster	136-143
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.	Kynurenine	142-153	indoleamine 2,3-dioxygenase 1	Homo sapiens	11-14
17446300-1	2007	Galantamine, a drug used to treat Alzheimer"s disease, is a nicotinic allosteric potentiating ligand, and kynurenic acid (KYNA), a neuroactive metabolite of the kynurenine pathway, is an endogenous noncompetitive inhibitor of alpha7* nicotinic receptors (nAChRs) [the asterisk next to the nAChR subunit is intended to indicate that the exact subunit composition of the receptor is not known (Pharmacol Rev 51:397-401, 1999)].	Kynurenine	161-171	cholinergic receptor nicotinic beta 1 subunit	Rattus norvegicus	255-260
17382471-0	2007	Prevention of electrical stimulation-induced increase of c-fos immunoreaction in the caudal trigeminal nucleus by kynurenine combined with probenecid.	Kynurenine	114-124	Fos proto-oncogene, AP-1 transcription factor subunit	Homo sapiens	57-62
17499941-1	2007	Indoleamine 2,3-dioxygenase (INDO) and tryptophan 2,3-dioxygenase (TDO) each catalyze the first step in the kynurenine pathway of tryptophan metabolism.	Kynurenine	108-118	tryptophan 2,3-dioxygenase	Mus musculus	39-65
17499941-1	2007	Indoleamine 2,3-dioxygenase (INDO) and tryptophan 2,3-dioxygenase (TDO) each catalyze the first step in the kynurenine pathway of tryptophan metabolism.	Kynurenine	108-118	tryptophan 2,3-dioxygenase	Mus musculus	67-70
17499941-8	2007	We demonstrate that INDOL1 catalyses the conversion of tryptophan to kynurenine therefore a more appropriate nomenclature for the enzymes might be INDO-1 and INDO-2, or the more commonly-used abbreviations, IDO-1 and IDO-2.	Kynurenine	69-79	indoleamine 2,3-dioxygenase 2	Mus musculus	20-26
17499941-8	2007	We demonstrate that INDOL1 catalyses the conversion of tryptophan to kynurenine therefore a more appropriate nomenclature for the enzymes might be INDO-1 and INDO-2, or the more commonly-used abbreviations, IDO-1 and IDO-2.	Kynurenine	69-79	indoleamine 2,3-dioxygenase 1	Mus musculus	207-212
17499941-8	2007	We demonstrate that INDOL1 catalyses the conversion of tryptophan to kynurenine therefore a more appropriate nomenclature for the enzymes might be INDO-1 and INDO-2, or the more commonly-used abbreviations, IDO-1 and IDO-2.	Kynurenine	69-79	indoleamine 2,3-dioxygenase 2	Mus musculus	217-222
17499941-10	2007	This identification of INDOL1 may help to explain the regulation of the diversity of physiological and patho-physiological processes in which the kynurenine pathway is involved.	Kynurenine	146-156	indoleamine 2,3-dioxygenase 2	Mus musculus	23-29
17382471-8	2007	injection of kynurenine combined with probenecid it was found that the stimulation-induced increase in the c-fos immunoreactivity of the secondary sensory neurons does not occur.	Kynurenine	13-23	Fos proto-oncogene, AP-1 transcription factor subunit	Homo sapiens	107-112
17367785-1	2007	Indoleamine 2,3-dioxygenase (IDO) is a rate-limiting enzyme in the L-tryptophan-kynurenine pathway, which converts an essential amino acid, L-tryptophan, to N-formylkynurenine.	Kynurenine	80-90	indoleamine 2,3-dioxygenase 1	Mus musculus	0-27
17425286-4	2007	Intrinsic fluorescence measurements indicated Fenton, but not HOCl, induced conversion of Trp9 of SP-B to hydroxyTrp (OHTrp), N-formylkynurenine (NFKyn), and kynurenine (Kyn).	Kynurenine	134-144	surfactant protein B	Bos taurus	98-102
17425286-4	2007	Intrinsic fluorescence measurements indicated Fenton, but not HOCl, induced conversion of Trp9 of SP-B to hydroxyTrp (OHTrp), N-formylkynurenine (NFKyn), and kynurenine (Kyn).	Kynurenine	148-151	surfactant protein B	Bos taurus	98-102
17504201-2	2007	A side-arm product of the pathway, kynurenic acid (KYNA), which is synthesized by the irreversible transamination of kynurenine (KYN) by kynurenine aminotransferases (KAT I and KAT II), is an excitatory amino acid receptor antagonist.	Kynurenine	117-127	kynurenine aminotransferase 1	Homo sapiens	167-183
17504201-2	2007	A side-arm product of the pathway, kynurenic acid (KYNA), which is synthesized by the irreversible transamination of kynurenine (KYN) by kynurenine aminotransferases (KAT I and KAT II), is an excitatory amino acid receptor antagonist.	Kynurenine	51-54	kynurenine aminotransferase 1	Homo sapiens	167-183
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.	Kynurenine	167-177	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-27
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.	Kynurenine	167-177	indoleamine 2,3-dioxygenase 1	Homo sapiens	29-32
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.	Kynurenine	167-170	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-27
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.	Kynurenine	167-170	indoleamine 2,3-dioxygenase 1	Homo sapiens	29-32
17367785-1	2007	Indoleamine 2,3-dioxygenase (IDO) is a rate-limiting enzyme in the L-tryptophan-kynurenine pathway, which converts an essential amino acid, L-tryptophan, to N-formylkynurenine.	Kynurenine	80-90	indoleamine 2,3-dioxygenase 1	Mus musculus	29-32
17355802-1	2007	BACKGROUND &amp; 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.	Kynurenine	156-166	indoleamine 2,3-dioxygenase 1	Homo sapiens	28-55
17349013-2	2007	The ratio of kynurenine, the main metabolite of tryptophan, to tryptophan (kyn/trp) reflects IDO activity.	Kynurenine	13-23	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.	Kynurenine	13-16	indoleamine 2,3-dioxygenase 1	Homo sapiens	93-96
17229698-2	2007	In chronic hepatitis C, we found upregulation of IDO expression in the liver and an increased serum kynurenine/tryptophan ratio (a reflection of IDO activity).	Kynurenine	100-110	indoleamine 2,3-dioxygenase 1	Homo sapiens	145-148
17355802-1	2007	BACKGROUND &amp; 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.	Kynurenine	156-166	indoleamine 2,3-dioxygenase 1	Homo sapiens	57-60
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.	Kynurenine	117-127	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-27
16897051-10	2007	It and tryptophane 2,3-dioxygenase (TDO) both catalyse the degradation from tryptophan to kynurenine.	Kynurenine	90-100	tryptophan 2,3-dioxygenase	Homo sapiens	7-34
16897051-10	2007	It and tryptophane 2,3-dioxygenase (TDO) both catalyse the degradation from tryptophan to kynurenine.	Kynurenine	90-100	tryptophan 2,3-dioxygenase	Homo sapiens	36-39
16897051-11	2007	Due to the inhibition of IDO, tryptophan is metabolised to kynurenine primarily by TDO.	Kynurenine	59-69	tryptophan 2,3-dioxygenase	Homo sapiens	83-86
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.	Kynurenine	91-101	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.	Kynurenine	91-101	indoleamine 2,3-dioxygenase 1	Homo sapiens	43-46
17511858-7	2007	Activity of IDO, as determined by measuring the levels of kynurenine/tryptophan ratio in the sera, was increased in the acute phase of arthritis and was higher in collagen-immunized mice that did not develop arthritis.	Kynurenine	58-68	indoleamine 2,3-dioxygenase 1	Mus musculus	12-15
17303977-14	2007	Moreover, NO inhibits IDO activity, thereby suppressing kynurenine formation, and at least one member of the kynurenine pathway, 3-hydroxyanthranilic acid, has been shown to inhibit NOS enzyme activity, the expression of NOS mRNA, and activation of the inflammatory transcription factor, nuclear factor-kB.	Kynurenine	56-66	indoleamine 2,3-dioxygenase 1	Homo sapiens	22-25
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.	Kynurenine	117-127	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.	Kynurenine	129-132	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.	Kynurenine	129-132	indoleamine 2,3-dioxygenase 1	Homo sapiens	29-32
17024659-4	2007	Kynurenine aminotransferase II (KAT II), the major biosynthetic enzyme of KYNA in the rat brain, catalyzes the irreversible formation of KYNA from its immediate bioprecursor, kynurenine.	Kynurenine	175-185	aminoadipate aminotransferase	Rattus norvegicus	0-30
17024659-4	2007	Kynurenine aminotransferase II (KAT II), the major biosynthetic enzyme of KYNA in the rat brain, catalyzes the irreversible formation of KYNA from its immediate bioprecursor, kynurenine.	Kynurenine	175-185	aminoadipate aminotransferase	Rattus norvegicus	32-38
17024659-12	2007	This may explain the rapid access of blood-derived kynurenine to KAT II-containing astrocytes.	Kynurenine	51-61	aminoadipate aminotransferase	Rattus norvegicus	65-71
16897600-4	2007	Systemic kynurenine + probenecid treatment significantly diminishes nitroglycerin-induced increase of c-fos immunoreactivity in the brainstem.	Kynurenine	9-19	Fos proto-oncogene, AP-1 transcription factor subunit	Rattus norvegicus	102-107
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.	Kynurenine	161-171	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.	Kynurenine	161-171	indoleamine 2,3-dioxygenase 1	Homo sapiens	29-32
16897600-0	2007	Kynurenine in combination with probenecid mitigates the stimulation-induced increase of c-fos immunoreactivity of the rat caudal trigeminal nucleus in an experimental migraine model.	Kynurenine	0-10	Fos proto-oncogene, AP-1 transcription factor subunit	Rattus norvegicus	88-93
17136028-6	2007	Kynurenine to tryptophan ratio (kyn/trp) was calculated to estimate IDO activity.	Kynurenine	0-10	indoleamine 2,3-dioxygenase 1	Homo sapiens	68-71
17136028-12	2007	Kyn/trp correlated significantly with neopterin suggesting an IFN-gamma-induced increase in IDO activity.	Kynurenine	0-3	interferon gamma	Homo sapiens	62-71
17136028-12	2007	Kyn/trp correlated significantly with neopterin suggesting an IFN-gamma-induced increase in IDO activity.	Kynurenine	0-3	indoleamine 2,3-dioxygenase 1	Homo sapiens	92-95
17184144-6	2007	Recent experimental evidence through transgenic mice models reveal an interesting interaction between expanded CAG triplets, mutant htt, and the increase in toxic metabolites from the kynurenine pathway.	Kynurenine	184-194	huntingtin	Mus musculus	132-135
17023091-1	2007	Kynurenine aminotransferases (KAT I and KAT II) are responsible for the transamination of kynurenine (KYN) to form kynurenic acid (KYNA), an excitatory amino acid receptor antagonist.	Kynurenine	0-10	kynurenine aminotransferase 1	Homo sapiens	30-46
17023091-1	2007	Kynurenine aminotransferases (KAT I and KAT II) are responsible for the transamination of kynurenine (KYN) to form kynurenic acid (KYNA), an excitatory amino acid receptor antagonist.	Kynurenine	90-100	kynurenine aminotransferase 1	Homo sapiens	30-46
16902152-0	2006	The tryptophan catabolite L-kynurenine inhibits the surface expression of NKp46- and NKG2D-activating receptors and regulates NK-cell function.	Kynurenine	26-38	natural cytotoxicity triggering receptor 1	Homo sapiens	74-79
16902152-0	2006	The tryptophan catabolite L-kynurenine inhibits the surface expression of NKp46- and NKG2D-activating receptors and regulates NK-cell function.	Kynurenine	26-38	killer cell lectin like receptor K1	Homo sapiens	85-90
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.	Kynurenine	8-20	indoleamine 2,3-dioxygenase 1	Homo sapiens	62-65
16902152-4	2006	The effect of l-kynurenine appears to be restricted to NKp46 and NKG2D, while it does not affect other surface receptors such as NKp30 or CD16.	Kynurenine	14-26	natural cytotoxicity triggering receptor 1	Homo sapiens	55-60
16902152-4	2006	The effect of l-kynurenine appears to be restricted to NKp46 and NKG2D, while it does not affect other surface receptors such as NKp30 or CD16.	Kynurenine	14-26	killer cell lectin like receptor K1	Homo sapiens	65-70
16902152-5	2006	As a consequence, l-kynurenine-treated NK cells display impaired ability to kill target cells recognized via NKp46 and NKG2D.	Kynurenine	18-30	natural cytotoxicity triggering receptor 1	Homo sapiens	109-114
16902152-5	2006	As a consequence, l-kynurenine-treated NK cells display impaired ability to kill target cells recognized via NKp46 and NKG2D.	Kynurenine	18-30	killer cell lectin like receptor K1	Homo sapiens	119-124
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.	Kynurenine	160-170	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.	Kynurenine	141-151	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-27
16754668-4	2006	Here we show that GPR35, a previously orphan G protein-coupled receptor, functions as a receptor for the kynurenine pathway intermediate kynurenic acid.	Kynurenine	105-115	G protein-coupled receptor 35	Homo sapiens	18-23
16246346-2	2006	The naturally occurring antioxidant 3-hydroxyanthranilic acid (HA), one of l-tryptophan metabolites formed in vivo along the metabolic route known as the kynurenine pathway during inflammation or infection, was found to induce HO-1 expression and to stimulate nuclear translocation of NF-E2 related factor 2 (Nrf2) in human umbilical vein endothelial cells (HUVECs).	Kynurenine	154-164	NFE2 like bZIP transcription factor 2	Homo sapiens	285-307
16246346-2	2006	The naturally occurring antioxidant 3-hydroxyanthranilic acid (HA), one of l-tryptophan metabolites formed in vivo along the metabolic route known as the kynurenine pathway during inflammation or infection, was found to induce HO-1 expression and to stimulate nuclear translocation of NF-E2 related factor 2 (Nrf2) in human umbilical vein endothelial cells (HUVECs).	Kynurenine	154-164	NFE2 like bZIP transcription factor 2	Homo sapiens	309-313
17062375-12	2006	IDO catalyzes the first step in tryptophan metabolism, the degradation from tryptophan to kynurenine, as does tryptophan 2,3-dioxygenase (TDO).	Kynurenine	90-100	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).	Kynurenine	90-100	tryptophan 2,3-dioxygenase	Homo sapiens	110-136
17062375-12	2006	IDO catalyzes the first step in tryptophan metabolism, the degradation from tryptophan to kynurenine, as does tryptophan 2,3-dioxygenase (TDO).	Kynurenine	90-100	tryptophan 2,3-dioxygenase	Homo sapiens	138-141
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.	Kynurenine	41-51	indoleamine 2,3-dioxygenase 1	Homo sapiens	25-28
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.	Kynurenine	41-51	tryptophan 2,3-dioxygenase	Homo sapiens	84-87
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.	Kynurenine	141-151	indoleamine 2,3-dioxygenase 1	Homo sapiens	29-32
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.	Kynurenine	141-144	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.	Kynurenine	141-144	indoleamine 2,3-dioxygenase 1	Homo sapiens	29-32
19412482-10	2006	A hypothesis is proposed that SSRIs modulate the neuro-protective neurotoxic ratio by possibly inhibiting the indole-2,3-dioxygenase induction of the kynurenine pathway.	Kynurenine	150-160	indoleamine 2,3-dioxygenase 1	Homo sapiens	110-132
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.	Kynurenine	160-170	indoleamine 2,3-dioxygenase 1	Homo sapiens	29-32
16842138-5	2006	Interferon-gamma also stimulates the enzyme indoleamine-2,3-dioxygenase, which degrades tryptophan to kynurenine.	Kynurenine	102-112	interferon gamma	Homo sapiens	0-16
16785507-2	2006	However, there are features of this mechanism, initiated by IDO, that are still unclear, including the role of enzymes that are downstream of IDO in the kynurenine pathway and the role of the associated production of kynurenines.	Kynurenine	153-163	indoleamine 2,3-dioxygenase 1	Mus musculus	142-145
16785507-4	2006	Altogether, these data indicate that kynurenine pathway enzymes downstream of IDO can initiate tolerogenesis by DCs independently of tryptophan deprivation.	Kynurenine	37-47	indoleamine 2,3-dioxygenase 1	Mus musculus	78-81
16785507-5	2006	The paracrine production of kynurenines might be one mechanism used by IDO-competent cells to convert DCs lacking functional IDO to a tolerogenic phenotype within an IFN-gamma-rich environment.	Kynurenine	28-39	indoleamine 2,3-dioxygenase 1	Mus musculus	71-74
16785507-5	2006	The paracrine production of kynurenines might be one mechanism used by IDO-competent cells to convert DCs lacking functional IDO to a tolerogenic phenotype within an IFN-gamma-rich environment.	Kynurenine	28-39	indoleamine 2,3-dioxygenase 1	Mus musculus	125-128
16785507-5	2006	The paracrine production of kynurenines might be one mechanism used by IDO-competent cells to convert DCs lacking functional IDO to a tolerogenic phenotype within an IFN-gamma-rich environment.	Kynurenine	28-39	interferon gamma	Mus musculus	166-175
16490253-8	2006	Kynurenine increased HLA-G expression in both TNF-alpha and IFN-gamma+LPS matured DC, and 3-hydroxyanthranilic acid had a very weak effect on HLA-G cell surface expression when present during maturation.	Kynurenine	0-10	major histocompatibility complex, class I, G	Homo sapiens	21-26
16490253-3	2006	IDO degrades Trp to kynurenine, which is further metabolized to 3-hydroxyanthranilic acid.	Kynurenine	20-30	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-3
16490253-8	2006	Kynurenine increased HLA-G expression in both TNF-alpha and IFN-gamma+LPS matured DC, and 3-hydroxyanthranilic acid had a very weak effect on HLA-G cell surface expression when present during maturation.	Kynurenine	0-10	tumor necrosis factor	Homo sapiens	46-55
16490253-6	2006	When monocytes were differentiated to immature DC in presence of either Trp or its metabolites kynurenine or 3-hydroxyanthranilic acid they expressed cell surface HLA-G, and Trp also increased shedding of HLA-G1.	Kynurenine	95-105	major histocompatibility complex, class I, G	Homo sapiens	163-168
16490253-8	2006	Kynurenine increased HLA-G expression in both TNF-alpha and IFN-gamma+LPS matured DC, and 3-hydroxyanthranilic acid had a very weak effect on HLA-G cell surface expression when present during maturation.	Kynurenine	0-10	interferon gamma	Homo sapiens	60-69
16490253-10	2006	Maturation with IFN-gamma+LPS in presence of kynurenine also increased HLA-G5 secretion.	Kynurenine	45-55	interferon gamma	Homo sapiens	16-25
16490253-13	2006	In IFN-gamma+LPS-matured DC this decreased capacity was obtained with kynurenine and 3-hydroxyanthranilic acid.	Kynurenine	70-80	interferon gamma	Homo sapiens	3-12
16522801-1	2006	3-Hydroxyanthranilic acid 3,4-dioxygenase (3HAO) is a non-heme ferrous extradiol dioxygenase in the kynurenine pathway from tryptophan.	Kynurenine	100-110	3-hydroxyanthranilate 3,4-dioxygenase	Homo sapiens	43-47
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.	Kynurenine	170-180	interferon gamma	Homo sapiens	29-45
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.	Kynurenine	170-180	indoleamine 2,3-dioxygenase 1	Homo sapiens	135-138
16892388-0	2006	Modulators of the kynurenine pathway of tryptophan metabolism: synthesis and preliminary biological evaluation of (S)-4-(ethylsulfonyl)benzoylalanine, a potent and selective kynurenine aminotransferase II (KAT II) inhibitor.	Kynurenine	18-28	aminoadipate aminotransferase	Homo sapiens	174-204
16678181-8	2006	Interferon-gamma, a cytokine known to be produced in malaria infection, induces increased expression, by microvascular endothelial cells, of the haem enzyme indoleamine 2,3-dioxygenase, the first enzyme in the kynurenine pathway of tryptophan metabolism.	Kynurenine	210-220	interferon gamma	Homo sapiens	0-16
16513157-1	2006	Indoleamine 2,3-dioxygenase (IDO), an enzyme degrading tryptophan (trp) to kynurenine (kyn), suppresses T cell activity.	Kynurenine	75-85	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.	Kynurenine	75-85	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.	Kynurenine	75-78	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.	Kynurenine	75-78	indoleamine 2,3-dioxygenase 1	Homo sapiens	29-32
16513157-4	2006	We measured kyn/trp, reflecting IDO activity, in 284 nonagenarians and 309 blood donor controls.	Kynurenine	12-15	indoleamine 2,3-dioxygenase 1	Homo sapiens	32-35
16318852-5	2006	The metabolites of the IDO catalysed reaction, l-kynurenine, was also measured.	Kynurenine	47-59	indoleamine 2,3-dioxygenase 1	Mus musculus	23-26
16318852-10	2006	Exposure to UV-B light led to a dose-responding upregulation of IDO; IDO was found competent converting l-tryptophan into l-kynurenine.	Kynurenine	122-134	indoleamine 2,3-dioxygenase 1	Mus musculus	64-67
16318852-10	2006	Exposure to UV-B light led to a dose-responding upregulation of IDO; IDO was found competent converting l-tryptophan into l-kynurenine.	Kynurenine	122-134	indoleamine 2,3-dioxygenase 1	Mus musculus	69-72
16318852-14	2006	IDO and its metabolite l-kynurenine can protect corneal endothelial cells from UV-B-induced oxidative stress and apoptosis.	Kynurenine	23-35	indoleamine 2,3-dioxygenase 1	Mus musculus	0-3
15935693-1	2005	Arylformamidase (AFMID) is the second enzyme of the kynurenine pathway metabolizing tryptophan to nicotinic acid and nicotinamide adenine dinucleotide cofactors.	Kynurenine	52-62	arylformamidase	Mus musculus	0-15
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.	Kynurenine	42-52	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-3
16126232-7	2006	Also the specific activities of other enzymes of the kynurenine pathway in the liver and kidneys, specifically kynurenine 3-monooxygenase, kynureninase and kynurenine-oxoglutarate transaminase, did not show any significant difference in both tissues between the two groups of rabbits.	Kynurenine	53-63	kynurenine 3-monooxygenase	Oryctolagus cuniculus	111-137
16126232-13	2006	This, together with the antioxidant action through the activation of Cu/Zn SOD, might deserve further investigation for evaluating any link between the observed experimental findings at the level of the kynurenine pathway and the clinical effect of the drug.	Kynurenine	203-213	superoxide dismutase [Cu-Zn]	Oryctolagus cuniculus	69-78
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.	Kynurenine	113-123	indoleamine 2,3-dioxygenase 1	Homo sapiens	18-45
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.	Kynurenine	113-123	indoleamine 2,3-dioxygenase 1	Homo sapiens	47-50
16118322-6	2005	We demonstrate also that ATP significantly potentiates the up-regulation of IDO--a negative regulator of T lymphocyte proliferation--and kynurenine production initiated by interferon-gamma (IFN-gamma) in human DCs.	Kynurenine	137-147	interferon gamma	Homo sapiens	172-188
16118322-6	2005	We demonstrate also that ATP significantly potentiates the up-regulation of IDO--a negative regulator of T lymphocyte proliferation--and kynurenine production initiated by interferon-gamma (IFN-gamma) in human DCs.	Kynurenine	137-147	interferon gamma	Homo sapiens	190-199
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.	Kynurenine	148-158	heme oxygenase 1	Rattus norvegicus	0-16
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.	Kynurenine	148-158	heme oxygenase 1	Rattus norvegicus	18-22
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.	Kynurenine	148-158	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.	Kynurenine	148-158	indoleamine 2,3-dioxygenase 1	Rattus norvegicus	108-111
15935693-1	2005	Arylformamidase (AFMID) is the second enzyme of the kynurenine pathway metabolizing tryptophan to nicotinic acid and nicotinamide adenine dinucleotide cofactors.	Kynurenine	52-62	arylformamidase	Mus musculus	17-22
15961516-1	2005	Indoleamine 2,3-dioxygenase (IDO) is the rate-limiting enzyme in the kynurenine pathway of tryptophan metabolism.	Kynurenine	69-79	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-27
16076525-1	2005	Indoleamine 2,3-dioxygenase (IDO) catabolizes tryptophan to kynurenine.	Kynurenine	60-70	indoleamine 2,3-dioxygenase 1	Mus musculus	0-27
16076525-1	2005	Indoleamine 2,3-dioxygenase (IDO) catabolizes tryptophan to kynurenine.	Kynurenine	60-70	indoleamine 2,3-dioxygenase 1	Mus musculus	29-32
15961516-1	2005	Indoleamine 2,3-dioxygenase (IDO) is the rate-limiting enzyme in the kynurenine pathway of tryptophan metabolism.	Kynurenine	69-79	indoleamine 2,3-dioxygenase 1	Homo sapiens	29-32
15866519-0	2005	Effect of arylformamidase (kynurenine formamidase) gene inactivation in mice on enzymatic activity, kynurenine pathway metabolites and phenotype.	Kynurenine	27-37	arylformamidase	Mus musculus	10-25
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.	Kynurenine	4-14	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.	Kynurenine	4-14	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.	Kynurenine	4-7	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.	Kynurenine	4-7	indoleamine 2,3-dioxygenase 1	Homo sapiens	119-122
16178870-6	2005	Female pSS patients with high IDO activity (kyn/trp x 1000 &gt; 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 &lt; 34.0).	Kynurenine	44-47	indoleamine 2,3-dioxygenase 1	Homo sapiens	30-33
16049516-6	2005	Furthermore, we show that this apoptosis could be related to the conversion of tryptophan into kynurenine by indoleamine 2,3-dioxygenase expressed by MSC in the presence of IFNgamma.	Kynurenine	95-105	interferon gamma	Homo sapiens	173-181
15939737-4	2005	IDO activity (determined by HPLC analysis of the kynurenine/tryptophan ratio) was increased in the spleen during the preclinical phase, and within the brain and spinal cord at the onset of symptoms.	Kynurenine	49-59	indoleamine 2,3-dioxygenase 1	Mus musculus	0-3
15866519-3	2005	Afmid-catalyzed hydrolysis of N-formyl-kynurenine is a key step in tryptophan metabolism and biosynthesis of kynurenine-derived products including kynurenic acid, quinolinic acid, nicotinamide, NAD, and NADP.	Kynurenine	39-49	arylformamidase	Mus musculus	0-5
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.	Kynurenine	83-93	indoleamine 2,3-dioxygenase 1	Homo sapiens	11-38
16075385-1	2005	AIM: Indoleamine 2,3-dioxygenase (IDO) catalyzation of tryptophan is the first rate-limiting step of the kynurenine pathway in the majority of tissues.	Kynurenine	105-115	indoleamine 2,3-dioxygenase 1	Mus musculus	5-32
16075385-1	2005	AIM: Indoleamine 2,3-dioxygenase (IDO) catalyzation of tryptophan is the first rate-limiting step of the kynurenine pathway in the majority of tissues.	Kynurenine	105-115	indoleamine 2,3-dioxygenase 1	Mus musculus	34-37
15950064-1	2005	Indoleamine 2,3-dioxygenase (IDO) has been implicated in contributing to immunotolerance in early pregnancy, but the presence in the term placenta of mRNAs for enzymes that produce other biologically active kynurenine end-products suggests other functions for kynurenine pathway metabolites.	Kynurenine	207-217	indoleamine 2,3-dioxygenase 1	Homo sapiens	29-32
15950064-1	2005	Indoleamine 2,3-dioxygenase (IDO) has been implicated in contributing to immunotolerance in early pregnancy, but the presence in the term placenta of mRNAs for enzymes that produce other biologically active kynurenine end-products suggests other functions for kynurenine pathway metabolites.	Kynurenine	260-270	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-27
15950064-1	2005	Indoleamine 2,3-dioxygenase (IDO) has been implicated in contributing to immunotolerance in early pregnancy, but the presence in the term placenta of mRNAs for enzymes that produce other biologically active kynurenine end-products suggests other functions for kynurenine pathway metabolites.	Kynurenine	260-270	indoleamine 2,3-dioxygenase 1	Homo sapiens	29-32
15950064-5	2005	IDO and KYN-OHase mRNAs were also identified, and the enzymes appear to be functional because kynurenine and 3-hydroxy-anthranilic acid (respective products of the activity of these enzyme) were released into the medium when first trimester placental explants were maintained in culture for 48h.	Kynurenine	94-104	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-3
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.	Kynurenine	83-93	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.	Kynurenine	83-93	interferon alpha 1	Homo sapiens	194-203
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.	Kynurenine	95-98	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.	Kynurenine	95-98	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.	Kynurenine	95-98	interferon alpha 1	Homo sapiens	194-203
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.	Kynurenine	322-325	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.	Kynurenine	322-325	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.	Kynurenine	322-325	interferon alpha 1	Homo sapiens	194-203
15494706-7	2005	The MADRS score significantly increased during IFN-alpha treatment as did the KYN/TRP ratio, reflecting IDO activity, and the KYN/KA ratio, reflecting the neurotoxic challenge.	Kynurenine	78-81	interferon alpha 1	Homo sapiens	47-56
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.	Kynurenine	168-178	indoleamine 2,3-dioxygenase 1	Homo sapiens	105-132
16142050-32	2005	Serotoninergic system can also be altered by a peripheral action of IFNalpha on trytophan catabolism by activating a concurrent pathway (known as "kynurenine pathway") to serotonin synthesis.	Kynurenine	147-157	interferon alpha 1	Homo sapiens	68-76
15543532-4	2005	RESULTS: Western blotting and immune staining revealed IDO expression in XS106 DCs transduced with IDO (XS106-IDO DCs), and its catabolic effect was confirmed by an increase in kynurenine concentration.	Kynurenine	177-187	indoleamine 2,3-dioxygenase 1	Mus musculus	104-117
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.	Kynurenine	168-178	indoleamine 2,3-dioxygenase 1	Homo sapiens	134-137
15718917-12	2005	A concomitant increase in kynurenine suggests that the observed tryptophan deficiency is caused, in part, by IDO-mediated tryptophan degradation.	Kynurenine	26-36	indoleamine 2,3-dioxygenase 1	Homo sapiens	109-112
16511030-4	2005	Ph-KAT II exhibited enzymatic activity that catalyzes the transamination of L-kynurenine to produce kynurenic acid.	Kynurenine	76-88	aminoadipate aminotransferase	Homo sapiens	3-9
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.	Kynurenine	98-108	indoleamine 2,3-dioxygenase 1	Homo sapiens	18-53
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.	Kynurenine	98-108	indoleamine 2,3-dioxygenase 1	Homo sapiens	71-74
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.	Kynurenine	98-101	indoleamine 2,3-dioxygenase 1	Homo sapiens	18-53
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.	Kynurenine	98-101	indoleamine 2,3-dioxygenase 1	Homo sapiens	71-74
15952423-2	2005	During the inflammatory process, a cytokine-induced enzyme called indoleamine 2,3-dioxygenase (IDO) has been shown to catabolise Trp into kynurenine (Kyn).	Kynurenine	138-148	indoleamine 2,3-dioxygenase 1	Sus scrofa	66-93
15952423-2	2005	During the inflammatory process, a cytokine-induced enzyme called indoleamine 2,3-dioxygenase (IDO) has been shown to catabolise Trp into kynurenine (Kyn).	Kynurenine	138-148	indoleamine 2,3-dioxygenase 1	Sus scrofa	95-98
15952423-2	2005	During the inflammatory process, a cytokine-induced enzyme called indoleamine 2,3-dioxygenase (IDO) has been shown to catabolise Trp into kynurenine (Kyn).	Kynurenine	150-153	indoleamine 2,3-dioxygenase 1	Sus scrofa	66-93
15952423-2	2005	During the inflammatory process, a cytokine-induced enzyme called indoleamine 2,3-dioxygenase (IDO) has been shown to catabolise Trp into kynurenine (Kyn).	Kynurenine	150-153	indoleamine 2,3-dioxygenase 1	Sus scrofa	95-98
15987253-1	2005	PURPOSE: To evaluate the levels of tryptophan and its metabolites along serotonin (5-HT) and kynurenine (KYN) pathways in serum of progressive myoclonus epilepsy (EPM1) patients and cystatin B (CSTB)-deficient mice, a model system for EPM1.	Kynurenine	93-103	cystatin B	Homo sapiens	163-167
15987253-1	2005	PURPOSE: To evaluate the levels of tryptophan and its metabolites along serotonin (5-HT) and kynurenine (KYN) pathways in serum of progressive myoclonus epilepsy (EPM1) patients and cystatin B (CSTB)-deficient mice, a model system for EPM1.	Kynurenine	105-108	cystatin B	Homo sapiens	163-167
15987253-3	2005	RESULTS: Reduced levels of 5-HT and KYN intermediate metabolite 3-hydroxyanthranilic acid were found in serum of CSTB-deficient mice.	Kynurenine	36-39	cystatin B	Mus musculus	113-117
15995595-1	2005	In this review, the role of the kynurenine pathway enzymes TDO (tryptophan 2,3 dioxygenase) and IDO (indoleamine 2,3 -dioxygenase) as well as the properties of the metabolites of kynurenine degradation present in human saliva described.	Kynurenine	32-42	tryptophan 2,3-dioxygenase	Homo sapiens	59-62
16088227-2	2005	In the brain tissue KYNA is synthesised from L-kynurenine by kynurenine aminotransferases (KAT) I and II.	Kynurenine	45-57	kynurenine aminotransferase 1	Homo sapiens	61-104
15995595-1	2005	In this review, the role of the kynurenine pathway enzymes TDO (tryptophan 2,3 dioxygenase) and IDO (indoleamine 2,3 -dioxygenase) as well as the properties of the metabolites of kynurenine degradation present in human saliva described.	Kynurenine	32-42	tryptophan 2,3-dioxygenase	Homo sapiens	64-90
15995595-1	2005	In this review, the role of the kynurenine pathway enzymes TDO (tryptophan 2,3 dioxygenase) and IDO (indoleamine 2,3 -dioxygenase) as well as the properties of the metabolites of kynurenine degradation present in human saliva described.	Kynurenine	32-42	indoleamine 2,3-dioxygenase 1	Homo sapiens	96-99
15606768-4	2004	This study demonstrates that hKAT-I can catalyze kynurenine to kynurenic acid under physiological pH conditions, indicates indo-3-pyruvate and cysteine as efficient inhibitors for hKAT-I, and also provides biochemical information about the substrate specificity and cosubstrate inhibition of the enzyme.	Kynurenine	49-59	kynurenine aminotransferase 1	Homo sapiens	29-35
15544920-0	2004	Mass spectral evidence for carbonate-anion-radical-induced posttranslational modification of tryptophan to kynurenine in human Cu, Zn superoxide dismutase.	Kynurenine	107-117	superoxide dismutase 1	Homo sapiens	127-154
15544920-2	2004	The carbonate anion radical (CO(3)(-))-induced oxidation of Trp-32 to kynurenine-type oxidation products was proposed to cause the aggregation of hSOD1.	Kynurenine	70-80	superoxide dismutase 1	Homo sapiens	146-151
15544920-4	2004	Results show that a peptide region (31-36) of hSOD1 containing the Trp-32 residue (VWGSIK) is oxidatively modified to the N-formylkynurenine (NFK)- and kynurenine (Kyn)-containing peptides (V(NFK)GSIK) and (V(Kyn)GSIK) during HCO(-)-dependent peroxidase activity of hSOD1.	Kynurenine	130-140	superoxide dismutase 1	Homo sapiens	46-51
15544920-4	2004	Results show that a peptide region (31-36) of hSOD1 containing the Trp-32 residue (VWGSIK) is oxidatively modified to the N-formylkynurenine (NFK)- and kynurenine (Kyn)-containing peptides (V(NFK)GSIK) and (V(Kyn)GSIK) during HCO(-)-dependent peroxidase activity of hSOD1.	Kynurenine	130-140	superoxide dismutase 1	Homo sapiens	266-271
15530458-12	2004	Thus 3-hydroxyanthranilate 3,4-dioxygenase may be an important regulatory mechanism in the control of the flow of tryptophan along the kynurenine pathway to NAD in hypercholesterolemic rabbits.	Kynurenine	135-145	3-hydroxyanthranilate 3,4-dioxygenase	Oryctolagus cuniculus	5-42
15606768-5	2004	hKAT-I is inhibited by Tris under physiological pH conditions, which explains why it has been concluded that the enzyme could not efficiently catalyze kynurenine transamination.	Kynurenine	151-161	kynurenine aminotransferase 1	Homo sapiens	0-6
15509163-3	2004	A structure-activity relationship for the nNOS inhibition can be established from the structural comparison of these new pyrazole derivatives and the described synthetic kynurenines 10.	Kynurenine	170-181	nitric oxide synthase 1	Rattus norvegicus	42-46
15528322-2	2004	Indoleamine 2,3-dioxygenase (IDO)-catalyzed conversion of tryptophan to kynurenines (KYN) regulates T cell function.	Kynurenine	72-83	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.	Kynurenine	72-83	indoleamine 2,3-dioxygenase 1	Homo sapiens	29-32
15112034-13	2004	Antibiotic-mediated TNF-alpha release may induce the kynurenine pathway.	Kynurenine	53-63	tumor necrosis factor	Homo sapiens	20-29
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.	Kynurenine	81-91	indoleamine 2,3-dioxygenase 1	Homo sapiens	16-19
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.	Kynurenine	103-113	indoleamine 2,3-dioxygenase 1	Homo sapiens	16-19
15281097-6	2004	IDO enzyme activity was evaluated by the measurement of kynurenine levels.	Kynurenine	56-66	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-3
15281097-8	2004	Kynurenine levels, as a measure of IDO bioactivity, were significantly higher in IFN-gamma-treated fibroblasts than in controls (P &lt; 0.001).	Kynurenine	0-10	indoleamine 2,3-dioxygenase 1	Homo sapiens	35-38
15281097-8	2004	Kynurenine levels, as a measure of IDO bioactivity, were significantly higher in IFN-gamma-treated fibroblasts than in controls (P &lt; 0.001).	Kynurenine	0-10	interferon gamma	Homo sapiens	81-90
15210815-6	2004	Kynurenine was absent in control conditions, but increased in the basolateral medium after IFN-gamma treatment.	Kynurenine	0-10	interferon gamma	Homo sapiens	91-100
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.	Kynurenine	156-166	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.	Kynurenine	156-166	indoleamine 2,3-dioxygenase 1	Homo sapiens	53-56
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.	Kynurenine	156-166	interferon gamma	Homo sapiens	79-95
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.	Kynurenine	156-166	interferon gamma	Homo sapiens	97-106
15001472-5	2004	Concomitantly, IDO activity resulting in tryptophan depletion and kynurenine production is detected in MSC/MLR coculture supernatants.	Kynurenine	66-76	indoleamine 2,3-dioxygenase 1	Homo sapiens	15-18
15182307-2	2004	Indoleamine-2,3-dioxygenase (IDO) initiates the increased production of kynurenine pathway metabolites like quinolinic acid (QUIN).	Kynurenine	72-82	indoleamine 2,3-dioxygenase 1	Homo sapiens	29-32
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.	Kynurenine	90-100	indoleamine 2,3-dioxygenase 1	Homo sapiens	36-63
15182307-2	2004	Indoleamine-2,3-dioxygenase (IDO) initiates the increased production of kynurenine pathway metabolites like quinolinic acid (QUIN).	Kynurenine	72-82	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-27
15135171-4	2004	The oxidative degradation of tryptophan to kynurenine and N-formyl kynurenine results in the covalent crosslinking and aggregation of hSOD1.	Kynurenine	43-53	superoxide dismutase 1	Homo sapiens	134-139
15016471-17	2004	However, owing to strong competition from other amino acid substrates, the turnover of kynurenine to kynurenate by GTK/KAT I in nervous tissue must be slow unless kynurenine and GTK are sequestered in a compartment distinct from the major amino acid pools.	Kynurenine	87-97	kynurenine aminotransferase 1	Homo sapiens	115-118
15016471-17	2004	However, owing to strong competition from other amino acid substrates, the turnover of kynurenine to kynurenate by GTK/KAT I in nervous tissue must be slow unless kynurenine and GTK are sequestered in a compartment distinct from the major amino acid pools.	Kynurenine	87-97	kynurenine aminotransferase 1	Homo sapiens	119-124
15016471-22	2004	The roles of GTK in (a) brain nitrogen, sulfur, and aromatic amino acid/kynurenine metabolism, (b) brain alpha-keto acid metabolism, (c) bioactivation of certain electrophiles in brain, (d) prodrug targeting, and (e) maintenance of normal blood pressure deserve further study.	Kynurenine	72-82	kynurenine aminotransferase 1	Homo sapiens	13-16
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.	Kynurenine	90-100	indoleamine 2,3-dioxygenase 1	Homo sapiens	65-68
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.	Kynurenine	90-100	interferon gamma	Homo sapiens	138-165
14756555-2	2004	3.7.1.3] is a pyridoxal-5"-phosphate (PLP)-dependent enzyme that catalyzes the hydrolytic cleavage of l-kynurenine to anthranilic acid and l-alanine.	Kynurenine	102-114	pyridoxal phosphatase	Homo sapiens	38-41
14573318-2	2003	BACKGROUND: Tryptophan (TRP) degradation into kynurenine (KYN) by the enzyme, indoleamine-2,3-dioxygenase, during immune activation may contribute to development of depressive symptoms during interferon (IFN)-alpha therapy.	Kynurenine	46-56	interferon alpha 1	Homo sapiens	192-214
14962250-4	2004	In macrophages, IFN-gamma strongly induces indoleamine (2,3)-dioxygenase, an enzyme which degrades tryptophan (trp) to kynurenine (kyn).	Kynurenine	119-129	interferon gamma	Homo sapiens	16-25
14962250-4	2004	In macrophages, IFN-gamma strongly induces indoleamine (2,3)-dioxygenase, an enzyme which degrades tryptophan (trp) to kynurenine (kyn).	Kynurenine	119-122	interferon gamma	Homo sapiens	16-25
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.	Kynurenine	90-100	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.	Kynurenine	90-100	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.	Kynurenine	90-100	indoleamine 2,3-dioxygenase 1	Homo sapiens	145-148
14967480-3	2004	Kynurenine production by MDA-MB-231 cells, which was taken as a measure of enzyme activity, was markedly stimulated by interferon-gamma (1000 units/ml).	Kynurenine	0-10	interferon gamma	Homo sapiens	119-135
14967480-5	2004	1-Methyl-DL-tryptophan (1 mM) inhibited interferon-gamma induced kynurenine production by MBA-MB-231 cells.	Kynurenine	65-75	interferon gamma	Homo sapiens	40-56
14967480-6	2004	Kynurenine production by MCF-7 cells remained at basal levels when cultured in the presence of interferon-gamma.	Kynurenine	0-10	interferon gamma	Homo sapiens	95-111
14969766-5	2004	Following a successful construction of IDO expressing adenoviral vector, the catabolic activity of IDO enzyme was evaluated by measuring the levels of its product, kynurenine in keratinocyte conditioned medium.	Kynurenine	164-174	indoleamine 2,3-dioxygenase 1	Mus musculus	99-102
14969766-6	2004	The results indicated a higher level of kynurenine in IDO expressing cells relative to those of control cells.	Kynurenine	40-50	indoleamine 2,3-dioxygenase 1	Mus musculus	54-57
15505390-4	2004	Deficiency of glutaryl-CoA dehydrogenase blocking the glutarate pathway and activation of indoleamine 2,3-dioxygenase in macrophages/monocytes by intercurrent inflammation may increase flux down the kynurenine pathway towards the production of quinolinic acid.	Kynurenine	199-209	glutaryl-CoA dehydrogenase	Homo sapiens	14-40
14573318-2	2003	BACKGROUND: Tryptophan (TRP) degradation into kynurenine (KYN) by the enzyme, indoleamine-2,3-dioxygenase, during immune activation may contribute to development of depressive symptoms during interferon (IFN)-alpha therapy.	Kynurenine	58-61	interferon alpha 1	Homo sapiens	192-214
14573318-5	2003	RESULTS: Regardless of antidepressant treatment status, all patients exhibited significant increases in KYN, neopterin, and the KYN/TRP ratio during IFN-alpha therapy.	Kynurenine	128-131	interferon alpha 1	Homo sapiens	149-158
14505498-1	2003	BACKGROUND: Kynureninase is a key enzyme on the kynurenine pathway of tryptophan metabolism.	Kynurenine	48-58	kynureninase	Homo sapiens	12-24
14505498-4	2003	RESULTS: Two new kynurenine analogues, 3-hydroxydesaminokynurenine and 3-methoxydesaminokynurenine, were synthesised as inhibitors of kynureninase and tested on the tryptophan-induced bacterial enzyme from Pseudomonas fluorescens, the recombinant human enzyme and the rat hepatic enzyme.	Kynurenine	17-27	kynureninase	Homo sapiens	134-146
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.	Kynurenine	224-234	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-27
12938169-5	2003	IDO enzyme activity was evaluated by measurement of kynurenine and tryptophan levels in the IFN-gamma untreated and treated fibroblasts.	Kynurenine	52-62	interferon gamma	Bos taurus	92-101
12938169-7	2003	The levels of kynurenine and tryptophan measured, as the bioactivity of IDO, were significantly different in the IFN-gamma treated fibroblasts, compared to those of controls (P &lt; 0.001).	Kynurenine	14-24	interferon gamma	Bos taurus	113-122
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.	Kynurenine	71-81	indoleamine 2,3-dioxygenase 1	Homo sapiens	27-30
12963490-7	2003	Exposure to IFN-gamma increased IDO activity from 7+/-1 nmol to 129+/-11 nmol kynurenine/hr/mg protein.	Kynurenine	78-88	interferon gamma	Homo sapiens	12-21
12963490-7	2003	Exposure to IFN-gamma increased IDO activity from 7+/-1 nmol to 129+/-11 nmol kynurenine/hr/mg protein.	Kynurenine	78-88	indoleamine 2,3-dioxygenase 1	Homo sapiens	32-35
12966593-1	2003	OBJECTIVE: Activation of the enzyme indoleamine-(2,3)-dioxygenase (IDO) by interferon (IFN)-g leads to enhanced tryptophan conversion to kynurenine.	Kynurenine	137-147	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.	Kynurenine	137-147	indoleamine 2,3-dioxygenase 1	Homo sapiens	67-70
12966593-1	2003	OBJECTIVE: Activation of the enzyme indoleamine-(2,3)-dioxygenase (IDO) by interferon (IFN)-g leads to enhanced tryptophan conversion to kynurenine.	Kynurenine	137-147	interferon gamma	Homo sapiens	75-93
12950637-4	2003	IDO enzyme activity was evaluated by measurement of kynurenine levels in the interferon-gamma-treated and -untreated cells.	Kynurenine	52-62	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-3
12950637-4	2003	IDO enzyme activity was evaluated by measurement of kynurenine levels in the interferon-gamma-treated and -untreated cells.	Kynurenine	52-62	interferon gamma	Homo sapiens	77-93
12950637-7	2003	The level of kynurenine measured, as the bioactivity of IDO enzyme, was significantly higher in the interferon-gamma-treated fibroblasts and keratinocytes compared to those of controls (p &lt; 0.001).	Kynurenine	13-23	indoleamine 2,3-dioxygenase 1	Homo sapiens	56-59
12950637-7	2003	The level of kynurenine measured, as the bioactivity of IDO enzyme, was significantly higher in the interferon-gamma-treated fibroblasts and keratinocytes compared to those of controls (p &lt; 0.001).	Kynurenine	13-23	interferon gamma	Homo sapiens	100-116
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.	Kynurenine	224-234	indoleamine 2,3-dioxygenase 1	Homo sapiens	29-32
12686560-10	2003	Fluorescence experiments revealed that Trp-32 was further oxidized by CO3., forming kynurenine-type products in the presence of oxygen.	Kynurenine	84-94	thioredoxin like 1	Homo sapiens	39-45
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.	Kynurenine	163-173	interferon gamma	Homo sapiens	9-25
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.	Kynurenine	163-173	indoleamine 2,3-dioxygenase 1	Homo sapiens	123-126
12814390-3	2003	Therefore, immune stimulation is commonly associated with an increased kynurenine to tryptophan ratio (kyn trp-1) indicative for activated indoleamine (2,3)-dioxygenase and a measurable decline of tryptophan.	Kynurenine	71-81	tRNA-Pro (anticodon AGG) 2-5	Homo sapiens	107-112
15206731-4	2003	We have found that tryptophan metabolites in the kynurenine pathway, such as 3-hydroxyanthranilic and quinolinic acids, will induce the selective apoptosis in vitro of murine thymocytes and Th1 but not Th2 cells.	Kynurenine	49-59	negative elongation factor complex member C/D, Th1l	Mus musculus	190-193
12832720-3	2003	These changes were accompanied by increase activity of liver tryptophan 2,3-dioxygenase, the rate-limiting enzyme of kynurenine pathway in rats, while indoleamine 2,3-dioxygenase activity was unchanged.	Kynurenine	117-127	tryptophan 2,3-dioxygenase	Rattus norvegicus	61-87
15206731-4	2003	We have found that tryptophan metabolites in the kynurenine pathway, such as 3-hydroxyanthranilic and quinolinic acids, will induce the selective apoptosis in vitro of murine thymocytes and Th1 but not Th2 cells.	Kynurenine	49-59	heart and neural crest derivatives expressed 2	Mus musculus	202-205
12401473-3	2002	In various cells interferon-gamma induces indoleamine 2,3-dioxygenase (IDO) which degrades tryptophan via the kynurenine pathway.	Kynurenine	110-120	interferon gamma	Homo sapiens	17-33
15206767-10	2003	However, the most active enzyme along the kynurenine pathway was 3-hydroxyanthranilate 3,4-dioxygenase, with liver showing the highest activity; aminocarboxymuconate-semialdehyde decarboxylase, which showed similar values in both liver and kidney, showed activity markedly lower than 3-hydroxyanthranilate 3,4-dioxygenase.	Kynurenine	42-52	3-hydroxyanthranilate 3,4-dioxygenase	Mus musculus	65-102
15206767-10	2003	However, the most active enzyme along the kynurenine pathway was 3-hydroxyanthranilate 3,4-dioxygenase, with liver showing the highest activity; aminocarboxymuconate-semialdehyde decarboxylase, which showed similar values in both liver and kidney, showed activity markedly lower than 3-hydroxyanthranilate 3,4-dioxygenase.	Kynurenine	42-52	3-hydroxyanthranilate 3,4-dioxygenase	Mus musculus	284-321
15206758-6	2003	In conclusion, the increase in the activity of TDO and HK along with disturbances of renal excreting function may be responsible for the elevation in the kynurenine and 3-hydroxykynurenine concentrations in experimental chronic renal failure.	Kynurenine	154-164	tryptophan 2,3-dioxygenase	Rattus norvegicus	47-50
12485374-1	2003	Mononuclear phagocytes appear to synthesize kynurenine-like products from the oxidation of biologically active indole compounds including melatonin, catalyzed by interferon (IFN)-gamma-inducible enzyme indoleamine 2,3-dioxygenase (IDO).	Kynurenine	44-54	interferon gamma	Mus musculus	162-184
12485374-1	2003	Mononuclear phagocytes appear to synthesize kynurenine-like products from the oxidation of biologically active indole compounds including melatonin, catalyzed by interferon (IFN)-gamma-inducible enzyme indoleamine 2,3-dioxygenase (IDO).	Kynurenine	44-54	indoleamine 2,3-dioxygenase 1	Mus musculus	202-229
12485374-1	2003	Mononuclear phagocytes appear to synthesize kynurenine-like products from the oxidation of biologically active indole compounds including melatonin, catalyzed by interferon (IFN)-gamma-inducible enzyme indoleamine 2,3-dioxygenase (IDO).	Kynurenine	44-54	indoleamine 2,3-dioxygenase 1	Mus musculus	231-234
12401473-3	2002	In various cells interferon-gamma induces indoleamine 2,3-dioxygenase (IDO) which degrades tryptophan via the kynurenine pathway.	Kynurenine	110-120	indoleamine 2,3-dioxygenase 1	Homo sapiens	42-69
12401473-3	2002	In various cells interferon-gamma induces indoleamine 2,3-dioxygenase (IDO) which degrades tryptophan via the kynurenine pathway.	Kynurenine	110-120	indoleamine 2,3-dioxygenase 1	Homo sapiens	71-74
12175700-2	2002	The aims of the present study were to examine the effects of pregnancy and delivery on plasma kynurenine, a major tryptophan catabolite synthesized after induction of indoleamine-2, 3 dioxygenase (IDO) by pro-inflammatory cytokines.	Kynurenine	94-104	indoleamine 2,3-dioxygenase 1	Homo sapiens	167-195
12232795-3	2002	We show here that tryptophan metabolites in the kynurenine pathway, such as 3-hydroxyanthranilic and quinolinic acids, will induce the selective apoptosis in vitro of murine thymocytes and of Th1 but not Th2 cells.	Kynurenine	48-58	negative elongation factor complex member C/D, Th1l	Mus musculus	192-195
12232795-3	2002	We show here that tryptophan metabolites in the kynurenine pathway, such as 3-hydroxyanthranilic and quinolinic acids, will induce the selective apoptosis in vitro of murine thymocytes and of Th1 but not Th2 cells.	Kynurenine	48-58	heart and neural crest derivatives expressed 2	Mus musculus	204-207
12175700-2	2002	The aims of the present study were to examine the effects of pregnancy and delivery on plasma kynurenine, a major tryptophan catabolite synthesized after induction of indoleamine-2, 3 dioxygenase (IDO) by pro-inflammatory cytokines.	Kynurenine	94-104	indoleamine 2,3-dioxygenase 1	Homo sapiens	197-200
12429225-4	2002	KYNA is produced from L-kynurenine, by the action of the enzymes kynurenine aminotransferases (KAT I and KAT II).	Kynurenine	22-34	kynurenine aminotransferase 1	Rattus norvegicus	95-111
12234479-0	2002	A modified kynurenine bioassay for quantitative determination of human interferon-gamma.	Kynurenine	11-21	interferon gamma	Homo sapiens	71-87
12217334-7	2002	In agreement, kyn/trp positively correlated with neopterin (r(s) = 0.60, P &lt; 0.001), with virus load (r(s) = 0.37, P = 0.013), and very weakly with CD4(+) cells counts (r(s) = 0.30, P = 0.049).	Kynurenine	14-17	CD4 molecule	Homo sapiens	151-154
12217334-8	2002	The change in the kyn/trp ratio during ART correlated more strongly with the change in neopterin levels (r(s) = 0.49, P = 0.001) than with the change in HIV RNA levels and weakly with the CD4 cell count.	Kynurenine	18-21	CD4 molecule	Homo sapiens	188-191
12075858-2	2002	In parallel, IFN-gamma induces indoleamine 2,3-dioxygenase which degrades 1-tryptophan to kynurenine.	Kynurenine	90-100	interferon gamma	Homo sapiens	13-22
12354294-1	2002	Kynurenine 3-mono-oxygenase (KMO) inhibitors reduce 3-hydroxykynurenine (3-HK) and quinolinic acid (QUIN) neosynthesis and facilitate kynurenine metabolism towards kynurenic acid (KYNA) formation.	Kynurenine	61-71	kynurenine 3-monooxygenase	Homo sapiens	0-27
12354294-1	2002	Kynurenine 3-mono-oxygenase (KMO) inhibitors reduce 3-hydroxykynurenine (3-HK) and quinolinic acid (QUIN) neosynthesis and facilitate kynurenine metabolism towards kynurenic acid (KYNA) formation.	Kynurenine	61-71	kynurenine 3-monooxygenase	Homo sapiens	29-32
12161035-4	2002	We used a murine model of EAE to demonstrate: (1) opposing patterns of spinal cord IDO and interferon-gamma (INF-gamma) mRNA expression through the preclinical, acute and remission I phases of EAE; (2) a change in the kynurenine-to-tryptophan (K/T) ratio during these same phases; and (3) 1-MT-induced exacerbation of clinical and histologic disease parameters during EAE.	Kynurenine	218-228	interferon gamma	Mus musculus	109-118
12007602-4	2002	KFase was isolated here from mouse liver cytosol by (NH4)2SO4 precipitation and three FPLC steps (resulting in 221-fold increase in specific activity for N-formyl-L-kynurenine hydrolysis) followed by conversion to [3H]diethylphosphoryl-KFase and finally isolation by C4 reverse-phase high-performance liquid chromatography.	Kynurenine	162-175	arylformamidase	Mus musculus	0-5
12062417-2	2002	We have identified the genes that encode the enzymes of the kynurenine pathway and for BNA5 (YLR231c) and BNA6 (YFR047c) confirmed that they encode kynureninase and quinolinate phosphoribosyl transferase respectively.	Kynurenine	60-70	kynureninase	Saccharomyces cerevisiae S288C	87-91
12062417-2	2002	We have identified the genes that encode the enzymes of the kynurenine pathway and for BNA5 (YLR231c) and BNA6 (YFR047c) confirmed that they encode kynureninase and quinolinate phosphoribosyl transferase respectively.	Kynurenine	60-70	nicotinate-nucleotide diphosphorylase (carboxylating)	Saccharomyces cerevisiae S288C	106-110
11919709-1	2002	Kynurenine 3-monooxygenase (KMO, EC 1.14.13.9), which catalyzes the oxidation of kynurenine to 3-hydroxykynurenine, is involved in the synthesis of ommochrome pigments in insects.	Kynurenine	81-91	kynurenine 3-monooxygenase	Bombyx mori	0-26
11919709-1	2002	Kynurenine 3-monooxygenase (KMO, EC 1.14.13.9), which catalyzes the oxidation of kynurenine to 3-hydroxykynurenine, is involved in the synthesis of ommochrome pigments in insects.	Kynurenine	81-91	kynurenine 3-monooxygenase	Bombyx mori	28-31
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.	Kynurenine	146-158	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-3
11799348-3	2002	The aims of this study were to examine the effects of IFN-alpha-based immunotherapy on the development of depressive symptoms in relation to its effects on plasma tryptophan and kynurenine and serum serotonin (5-HT).	Kynurenine	178-188	interferon alpha 1	Homo sapiens	54-63
11799348-6	2002	Immunochemotherapy with IFN-alpha (1) significantly increased the MADRS and HAM-A scores and serum kynurenine concentrations and (2) significantly reduced plasma tryptophan and serum 5-HT concentrations.	Kynurenine	99-109	interferon alpha 1	Homo sapiens	24-33
11799348-7	2002	IFN-alpha-based immunotherapy significantly increased the kynurenine per tryptophan quotient, which estimates the activity of indoleamine 2,3-dioxygenase, the major tryptophan-catabolizing enzyme, which is induced by IFNs.	Kynurenine	58-68	interferon alpha 1	Homo sapiens	0-9
11799348-8	2002	There are significant relationships between the IFN-alpha-induced changes in the MADRS score and serum kynurenine (positive) and 5-HT (negative) concentrations.	Kynurenine	103-113	interferon alpha 1	Homo sapiens	48-57
11389182-5	2001	In line with this possibility, we found that ATP levels decreased more rapidly in quinolinate- than in 3OH-kynurenine-exposed cultures and that poly(ADP-ribose) polymer, the product of poly(ADP-ribose) polymerase activity, was more abundant in the nuclei of quinolinic acid than in those of 3OH-kynurenine-exposed neurons.	Kynurenine	107-117	poly(ADP-ribose) polymerase 1	Homo sapiens	185-212
11798468-2	2001	The kynurenine pathway (KP) is chiefly activated by IFN-gamma and IFN-alpha, leading to the production of a variety of neurotoxins.	Kynurenine	4-14	interferon gamma	Homo sapiens	52-61
11798468-2	2001	The kynurenine pathway (KP) is chiefly activated by IFN-gamma and IFN-alpha, leading to the production of a variety of neurotoxins.	Kynurenine	4-14	interferon alpha 1	Homo sapiens	66-75
11579128-6	2001	In addition, there are a limited number of clearly defined circumstances in which the method is confounded by the metabolism of labeled alpha-MTrp via the kynurenine pathway.	Kynurenine	155-165	lysosomal protein transmembrane 4 alpha	Homo sapiens	142-146
11479034-3	2001	Liver tryptophan 2,3-dioxygenase exists only as holoenzyme, but intestine indole 2,3-dioxygenase is very active and can be considered the key enzyme which determines how much tryptophan enters the kynurenine pathway also under physiological conditions.	Kynurenine	197-207	tryptophan 2,3-dioxygenase	Oryctolagus cuniculus	6-32
11479034-5	2001	Kynurenine 3-monooxygenase appeared more active than kynurenine-oxoglutarate transaminase and kynureninase, suggesting that perhaps a major portion of kynurenine available from tryptophan may be metabolized to give 3-hydroxyanthranilic acid, the precursor of nicotinic acid.	Kynurenine	53-63	kynurenine 3-monooxygenase	Oryctolagus cuniculus	0-26
11479034-6	2001	In fact, 3-hydroxyanthranilate 3,4-dioxygenase is much more active than the other previous enzymes of the kynurenine pathway.	Kynurenine	106-116	3-hydroxyanthranilate 3,4-dioxygenase	Oryctolagus cuniculus	9-46
11477543-1	2001	Indoleamine 2,3-dioxygenase (IDO) is a rate-limiting enzyme in the L-tryptophan-kynurenine pathway, which converts an essential amino acid, L-tryptophan, to N-formylkynurenine.	Kynurenine	80-90	indoleamine 2,3-dioxygenase 1	Mus musculus	0-27
11477543-1	2001	Indoleamine 2,3-dioxygenase (IDO) is a rate-limiting enzyme in the L-tryptophan-kynurenine pathway, which converts an essential amino acid, L-tryptophan, to N-formylkynurenine.	Kynurenine	80-90	indoleamine 2,3-dioxygenase 1	Mus musculus	29-32
11784131-0	2002	Inhibition of nNOS activity in rat brain by synthetic kynurenines: structure-activity dependence.	Kynurenine	54-65	nitric oxide synthase 1	Rattus norvegicus	14-18
11784131-8	2002	These results suggest that a structure-related activity of these synthetic kynurenines and a N-H bond in a specific direction is necessary for some kynurenine analogues to inhibit nNOS activity.	Kynurenine	75-86	nitric oxide synthase 1	Rattus norvegicus	180-184
11784131-8	2002	These results suggest that a structure-related activity of these synthetic kynurenines and a N-H bond in a specific direction is necessary for some kynurenine analogues to inhibit nNOS activity.	Kynurenine	75-85	nitric oxide synthase 1	Rattus norvegicus	180-184
11817676-2	2001	In human monocytes/macrophages, interferon-gamma induces increased production of neopterin and an enhanced activity of indoleamine 2,3-dioxygenase, which degrades tryptophan via the kynurenine pathway.	Kynurenine	182-192	interferon gamma	Homo sapiens	32-48
11701274-7	2001	One possibility is that TRH may act as an antiepileptic through a kynurenine mechanism, considering that kynurenic acid acts as an antagonist on the N-methyl-D-aspartate receptor complex.	Kynurenine	66-76	thyrotropin releasing hormone	Homo sapiens	24-27
11559441-1	2001	Indoleamine 2,3-dioxygenase (IDO) activity as determined by increases in serum kynurenine was measured in a group of hepatitis C patients treated with consensus interferon (IFN-con1).	Kynurenine	79-89	indoleamine 2,3-dioxygenase 1	Homo sapiens	29-32
11388614-3	2001	Using human peripheral blood-derived mononuclear cells in vitro, such toxins were shown to induce neopterin production and degradation of the amino acid tryptophan to metabolites such as kynurenine by activating indoleamine (2,3)-dioxygenase via interferon-gamma.	Kynurenine	187-197	interferon gamma	Homo sapiens	246-262
11227029-11	2001	The plasma concentration of kynurenine increased continuously during the post-bolus period and this response was more marked in F56 (P &lt; 0.002) and in B630 piglets (P &lt; 0.02).	Kynurenine	28-38	DLEC1 cilia and flagella associated protein	Homo sapiens	128-131
11040043-0	2000	Structure-related inhibition of calmodulin-dependent neuronal nitric-oxide synthase activity by melatonin and synthetic kynurenines.	Kynurenine	120-131	calmodulin 1	Rattus norvegicus	32-42
11040043-1	2000	We recently described that melatonin and some kynurenines modulate the N-methyl-D-aspartate-dependent excitatory response in rat striatal neurons, an effect that could be related to their inhibition of nNOS.	Kynurenine	46-57	nitric oxide synthase 1	Rattus norvegicus	202-206
11040043-11	2000	The results show that calmodulin is a target involved in the intracellular effects of melatonin and some melatonin-related kynurenines that may account, at least in part, for the neuroprotective properties of these compounds.	Kynurenine	123-134	calmodulin 1	Rattus norvegicus	22-32
11040043-2	2000	In this report, we studied the effect of melatonin and these kynurenines on nNOS activity in both rat striatal homogenate and purified rat brain nNOS.	Kynurenine	61-72	nitric oxide synthase 1	Rattus norvegicus	76-80
11040043-2	2000	In this report, we studied the effect of melatonin and these kynurenines on nNOS activity in both rat striatal homogenate and purified rat brain nNOS.	Kynurenine	61-72	nitric oxide synthase 1	Rattus norvegicus	145-149
11040043-4	2000	Kynurenines carrying an NH(2) group in their benzenic ring (NH(2)-kynurenines) inhibit nNOS activity more strongly than melatonin itself.	Kynurenine	0-11	nitric oxide synthase 1	Rattus norvegicus	87-91
10837188-4	2000	HAM/TSP patients had significantly elevated levels of neopterin (P=.003) and kynurenine (P=.05) and a significantly decreased level of tryptophan (P=.003), compared with patients with ONDs.	Kynurenine	77-87	thrombospondin 1	Homo sapiens	4-7
10966936-6	2000	Liver L-tryptophan 2,3-dioxygenase activity (TDO), a rate-limiting enzyme of the kynurenine pathway, was increased in proportion to blood urea nitrogen and creatinine levels.	Kynurenine	81-91	tryptophan 2,3-dioxygenase	Rattus norvegicus	45-48
10966936-9	2000	We hypothesize the following ideas: that increased serum L-kynurenine concentrations are mainly due to the increased TDO and decreased kynureninase activities in the liver and increased serum Quin concentrations are due to the decreased ACMSDase activities in the body after renal insufficiency.	Kynurenine	57-69	tryptophan 2,3-dioxygenase	Rattus norvegicus	117-120
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).	Kynurenine	196-206	tryptophan 2,3-dioxygenase	Homo sapiens	222-242
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).	Kynurenine	196-206	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).	Kynurenine	196-206	indoleamine 2,3-dioxygenase 1	Homo sapiens	281-284
10947071-1	2000	We evaluated the synthesis of nitric oxide (NO) and of the neurotoxic kynurenine metabolites 3OH-kynurenine and quinolinic acid (QUIN) in interferon-gamma (IFN-gamma)-activated macrophages of the murine BACl.2F5 cell line with the aim of investigating the roles of mononuclear phagocytes in inflammatory neurological disorders.	Kynurenine	70-80	interferon gamma	Mus musculus	138-154
10947071-1	2000	We evaluated the synthesis of nitric oxide (NO) and of the neurotoxic kynurenine metabolites 3OH-kynurenine and quinolinic acid (QUIN) in interferon-gamma (IFN-gamma)-activated macrophages of the murine BACl.2F5 cell line with the aim of investigating the roles of mononuclear phagocytes in inflammatory neurological disorders.	Kynurenine	70-80	interferon gamma	Mus musculus	156-165
10947071-3	2000	Macrophage exposure to norharmane, an IDO inhibitor, resulted in a decreased formation of not only the kynurenine metabolites but also NO.	Kynurenine	103-113	indoleamine 2,3-dioxygenase 1	Mus musculus	38-41
10725715-5	2000	IDO produced from activated DCs was functionally active and capable of metabolizing tryptophan to kynurenine.	Kynurenine	98-108	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-3
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.	Kynurenine	108-118	interferon gamma	Homo sapiens	0-9
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.	Kynurenine	108-118	indoleamine 2,3-dioxygenase 1	Homo sapiens	63-66
10834318-6	2000	Also the kynurenine per tryptophan quotients (K/T), which allow to estimate IDO activity, were significantly higher in patients than in normals (0.043, 0.033-0.062 vs. 0.027, 0.021-0.030; p &lt; 0.0001), indicating enhanced IDO-induced tryptophan degradation in SLE.	Kynurenine	9-19	indoleamine 2,3-dioxygenase 1	Homo sapiens	76-79
10834318-6	2000	Also the kynurenine per tryptophan quotients (K/T), which allow to estimate IDO activity, were significantly higher in patients than in normals (0.043, 0.033-0.062 vs. 0.027, 0.021-0.030; p &lt; 0.0001), indicating enhanced IDO-induced tryptophan degradation in SLE.	Kynurenine	9-19	indoleamine 2,3-dioxygenase 1	Homo sapiens	224-227
10719243-0	2000	Comparative effects of oxygen on indoleamine 2,3-dioxygenase and tryptophan 2,3-dioxygenase of the kynurenine pathway.	Kynurenine	99-109	indoleamine 2,3-dioxygenase 1	Rattus norvegicus	33-60
10719243-0	2000	Comparative effects of oxygen on indoleamine 2,3-dioxygenase and tryptophan 2,3-dioxygenase of the kynurenine pathway.	Kynurenine	99-109	tryptophan 2,3-dioxygenase	Rattus norvegicus	65-91
10719243-2	2000	These enzymes catalyze the rate-limiting step in the kynurenine (KYN) pathway from trp to quinolinic acid (QA) with TDO in kidney and liver and IDO in many tissues, including brain where it is low but inducible.	Kynurenine	53-63	tryptophan 2,3-dioxygenase	Rattus norvegicus	116-119
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.	Kynurenine	119-129	interferon gamma	Homo sapiens	24-40
10719243-2	2000	These enzymes catalyze the rate-limiting step in the kynurenine (KYN) pathway from trp to quinolinic acid (QA) with TDO in kidney and liver and IDO in many tissues, including brain where it is low but inducible.	Kynurenine	53-63	indoleamine 2,3-dioxygenase 1	Rattus norvegicus	144-147
10719243-2	2000	These enzymes catalyze the rate-limiting step in the kynurenine (KYN) pathway from trp to quinolinic acid (QA) with TDO in kidney and liver and IDO in many tissues, including brain where it is low but inducible.	Kynurenine	65-68	tryptophan 2,3-dioxygenase	Rattus norvegicus	116-119
10719243-2	2000	These enzymes catalyze the rate-limiting step in the kynurenine (KYN) pathway from trp to quinolinic acid (QA) with TDO in kidney and liver and IDO in many tissues, including brain where it is low but inducible.	Kynurenine	65-68	indoleamine 2,3-dioxygenase 1	Rattus norvegicus	144-147
10672018-1	2000	The mitochondrial outer membrane enzyme kynurenine 3-hydroxylase (K3H) is an NADPH-dependent flavin mono-oxygenase involved in the tryptophan pathway, where it catalyzes the hydroxylation of kynurenine.	Kynurenine	40-50	kynurenine 3-monooxygenase	Homo sapiens	66-69
11026503-1	2000	The kynurenine pathway intermediate 3-hydroxyanthranilic acid (3-HANA) is converted by 3-HANA 3,4-dioxygenase (3-HAO) to the pro-convulsive excitotoxin quinolinic acid.	Kynurenine	4-14	3-hydroxyanthranilate 3,4-dioxygenase	Mus musculus	87-109
11026503-1	2000	The kynurenine pathway intermediate 3-hydroxyanthranilic acid (3-HANA) is converted by 3-HANA 3,4-dioxygenase (3-HAO) to the pro-convulsive excitotoxin quinolinic acid.	Kynurenine	4-14	3-hydroxyanthranilate 3,4-dioxygenase	Mus musculus	111-116
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.	Kynurenine	119-129	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.	Kynurenine	119-129	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).	Kynurenine	39-49	indoleamine 2,3-dioxygenase 1	Homo sapiens	6-9
10939276-1	2000	Kynurenine-3-monooxygenase (KM), the third enzyme in the kynurenine (KYN) pathway from tryptophan to quinolinic acid (QA), is a monooxygenase requiring oxygen, NADPH and FAD for the catalytic oxidation of L-kynurenine to 3-hydroxykynurenine and water.	Kynurenine	57-67	kynurenine 3-monooxygenase	Homo sapiens	0-26
10939276-1	2000	Kynurenine-3-monooxygenase (KM), the third enzyme in the kynurenine (KYN) pathway from tryptophan to quinolinic acid (QA), is a monooxygenase requiring oxygen, NADPH and FAD for the catalytic oxidation of L-kynurenine to 3-hydroxykynurenine and water.	Kynurenine	69-72	kynurenine 3-monooxygenase	Homo sapiens	0-26
10939276-1	2000	Kynurenine-3-monooxygenase (KM), the third enzyme in the kynurenine (KYN) pathway from tryptophan to quinolinic acid (QA), is a monooxygenase requiring oxygen, NADPH and FAD for the catalytic oxidation of L-kynurenine to 3-hydroxykynurenine and water.	Kynurenine	205-217	kynurenine 3-monooxygenase	Homo sapiens	0-26
9828005-6	1998	Structural analysis by mass spectrometry revealed that tryptophan 9 of alphaA- and tryptophan 60 of alphaB-crystallin were each converted into hydroxytryptophans (HTRP), N-formylkynurenine (NFK), and kynurenine (KYN).	Kynurenine	178-188	crystallin alpha B	Bos taurus	100-117
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.	Kynurenine	225-237	interferon gamma	Homo sapiens	25-34
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.	Kynurenine	225-237	indoleamine 2,3-dioxygenase 1	Homo sapiens	57-60
10217295-1	1999	Although the neurotoxic tryptophan-kynurenine pathway metabolite quinolinic acid originates in brain by both local de novo synthesis and entry from blood, its concentrations in brain parenchyma, extracellular fluid, and CSF are normally below blood values.	Kynurenine	35-45	colony stimulating factor 2	Homo sapiens	220-223
10094134-1	1999	Kynurenine aminotransferase I (KATI) converts kynurenine into kynurenic acid (KYNA), a broadspectrum antagonist at ionotropic excitatory amino acid receptors.	Kynurenine	46-56	kynurenine aminotransferase 1	Rattus norvegicus	0-29
10094134-1	1999	Kynurenine aminotransferase I (KATI) converts kynurenine into kynurenic acid (KYNA), a broadspectrum antagonist at ionotropic excitatory amino acid receptors.	Kynurenine	46-56	kynurenine aminotransferase 1	Rattus norvegicus	31-35
10613517-3	1999	Kynurenic acid, a powerful endogenous excitatory amino acid receptor antagonist, which is therefore widely regarded as a potent neuroprotective agent, is produced from its biological precursor, L-kynurenine, by the action of the enzyme kynurenine aminotransferase-I.	Kynurenine	194-206	kynurenine aminotransferase 1	Rattus norvegicus	236-265
10731095-8	1999	This article reviews findings indicating that redox reactions are involved in the regulation of IDO and Trp metabolism along the Kyn pathway and also participate in the biological activities exhibited by Kyn pathway metabolites.	Kynurenine	129-132	indoleamine 2,3-dioxygenase 1	Homo sapiens	96-99
10619651-0	1999	TRH increases cerebrospinal fluid concentration of kynurenine.	Kynurenine	51-61	thyrotropin releasing hormone	Homo sapiens	0-3
10619651-4	1999	Among monoamine-related substances, only CSF concentrations of kynurenine were increased after TRH therapy.	Kynurenine	63-73	thyrotropin releasing hormone	Homo sapiens	95-98
10721098-1	1999	This article summarises studies supporting the proposal that induction of L-tryptophan (Trp) degradation along the kynurenine pathway in human monocytes and macrophages by interferon-gamma (IFN gamma) represents a novel extracellular antioxidant defence that acts to prevent inadvertent oxidative damage to host tissue during inflammation.	Kynurenine	115-125	interferon gamma	Homo sapiens	172-188
10721098-1	1999	This article summarises studies supporting the proposal that induction of L-tryptophan (Trp) degradation along the kynurenine pathway in human monocytes and macrophages by interferon-gamma (IFN gamma) represents a novel extracellular antioxidant defence that acts to prevent inadvertent oxidative damage to host tissue during inflammation.	Kynurenine	115-125	interferon gamma	Homo sapiens	190-199
10721098-4	1999	Indoleamine 2,3-dioxygenase activity (IDO) is the initial and rate limiting enzyme of Trp degradation along the kynurenine pathway.	Kynurenine	112-122	indoleamine 2,3-dioxygenase 1	Homo sapiens	38-41
10721136-2	1999	Tryptophan is converted to kynurenine by the action of the enzyme indoleamine 2,3-dioxygenase induced by interferon-gamma (IFN-gamma).	Kynurenine	27-37	interferon gamma	Homo sapiens	105-121
10721136-2	1999	Tryptophan is converted to kynurenine by the action of the enzyme indoleamine 2,3-dioxygenase induced by interferon-gamma (IFN-gamma).	Kynurenine	27-37	interferon gamma	Homo sapiens	123-132
10721136-3	1999	Since IFN-gamma is a Th1-cell derived cytokine, an increased tryptophan degradation rate via the kynurenine pathway can be found when the cellular immune system is activated as it is, e.g., in viral infections or in autoimmune diseases.	Kynurenine	97-107	interferon gamma	Homo sapiens	6-15
10721136-3	1999	Since IFN-gamma is a Th1-cell derived cytokine, an increased tryptophan degradation rate via the kynurenine pathway can be found when the cellular immune system is activated as it is, e.g., in viral infections or in autoimmune diseases.	Kynurenine	97-107	negative elongation factor complex member C/D	Homo sapiens	21-24
10721136-4	1999	Thus, the ratio kynurenine per tryptophan provides a possibility to estimate IFN-gamma activity in vivo and furthermore reflects the degree of immune activation.	Kynurenine	16-26	interferon gamma	Homo sapiens	77-86
10731095-0	1999	Redox reactions related to indoleamine 2,3-dioxygenase and tryptophan metabolism along the kynurenine pathway.	Kynurenine	91-101	indoleamine 2,3-dioxygenase 1	Homo sapiens	27-54
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.	Kynurenine	182-192	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.	Kynurenine	182-192	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.	Kynurenine	194-197	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.	Kynurenine	194-197	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.	Kynurenine	49-52	indoleamine 2,3-dioxygenase 1	Homo sapiens	13-16
9870556-0	1998	Effects of oxygen on 3-hydroxyanthranilate oxidase of the kynurenine pathway.	Kynurenine	58-68	3-hydroxyanthranilate 3,4-dioxygenase	Homo sapiens	21-50
9828005-6	1998	Structural analysis by mass spectrometry revealed that tryptophan 9 of alphaA- and tryptophan 60 of alphaB-crystallin were each converted into hydroxytryptophans (HTRP), N-formylkynurenine (NFK), and kynurenine (KYN).	Kynurenine	212-215	crystallin alpha B	Bos taurus	100-117
9873646-1	1998	Kynurenine 3-hydroxylase (KYN 3-OHase) is a key enzyme in the kynurenine pathway of tryptophan degradation and its inhibition may be an effective mechanism for counteracting neuronal excitotoxic damage.	Kynurenine	62-72	kynurenine 3-monooxygenase	Homo sapiens	0-24
9712367-6	1998	The expression of kynurenine synthesis was inhibited by A23817 during the first 4 h after IFN treatment by mechanisms that were independent of cyclooxygenase, calmodulin, and calcineurin.	Kynurenine	18-28	interferon alpha 1	Homo sapiens	90-93
9712367-9	1998	These results indicate that the expression of kynurenine synthesis is modulated at the transcriptional and posttranscriptional levels by protein tyrosine kinase and by a Ser/Thr kinase with properties distinctly different from those of conventional protein kinase C. The capacity for attenuation of this IFN-gamma-induced response over its entire time course by many effectors and through multiple cellular signaling pathways may represent a mechanism for fine-tuning the level of oxidative tryptophan metabolism to meet the needs of a particular cytostatic or antiproliferative response.	Kynurenine	46-56	interferon gamma	Homo sapiens	304-313
9712367-1	1998	Interferon-gamma (IFN-gamma)-induced, indoleamine dioxygenase-catalyzed tryptophan catabolism was studied in cultured human foreskin fibroblasts using the increase in cellular kynurenine synthesis as an index of gene expression.	Kynurenine	176-186	interferon gamma	Homo sapiens	0-27
9712367-2	1998	The time courses of the inhibition of IFN-gamma-induced kynurenine synthesis by actinomycin D and cycloheximide showed that the indoleamine dioxygenase gene was transcribed as early as 2 h and translated as early as 5 h after initiation of IFN treatment.	Kynurenine	56-66	interferon gamma	Homo sapiens	38-47
9712367-2	1998	The time courses of the inhibition of IFN-gamma-induced kynurenine synthesis by actinomycin D and cycloheximide showed that the indoleamine dioxygenase gene was transcribed as early as 2 h and translated as early as 5 h after initiation of IFN treatment.	Kynurenine	56-66	interferon alpha 1	Homo sapiens	38-41
9539135-2	1998	The deduced protein sequence of the gene product is homologous to the human 3-hydroxyanthranilic acid dioxygenase (EC 1.13.11.6) which is part of the kynurenine pathway for the degradation of tryptophan and the biosynthesis of nicotinic acid.	Kynurenine	150-160	3-hydroxyanthranilate 3,4-dioxygenase	Homo sapiens	76-113
9631442-1	1998	Kynurenine aminotransferase I (KAT-I), which also shows glutamine transaminase K (GTK) activity, catalyses the conversion of kynurenine to kynurenic acid, an endogenous glutamate antagonist.	Kynurenine	125-135	kynurenine aminotransferase 1	Rattus norvegicus	0-29
9631442-1	1998	Kynurenine aminotransferase I (KAT-I), which also shows glutamine transaminase K (GTK) activity, catalyses the conversion of kynurenine to kynurenic acid, an endogenous glutamate antagonist.	Kynurenine	125-135	kynurenine aminotransferase 1	Rattus norvegicus	31-36
9631442-1	1998	Kynurenine aminotransferase I (KAT-I), which also shows glutamine transaminase K (GTK) activity, catalyses the conversion of kynurenine to kynurenic acid, an endogenous glutamate antagonist.	Kynurenine	125-135	kynurenine aminotransferase 1	Rattus norvegicus	56-80
9631442-1	1998	Kynurenine aminotransferase I (KAT-I), which also shows glutamine transaminase K (GTK) activity, catalyses the conversion of kynurenine to kynurenic acid, an endogenous glutamate antagonist.	Kynurenine	125-135	kynurenine aminotransferase 1	Rattus norvegicus	82-85
9578134-0	1998	Tryptophan and its metabolite, kynurenine, stimulate expression of nerve growth factor in cultured mouse astroglial cells.	Kynurenine	31-41	nerve growth factor	Mus musculus	67-86
9578134-3	1998	L-Kynurenine, a metabolite of the kynurenine pathway, markedly increased the levels of mRNAs for NGF, the maximal increases (4-5 fold) occurred at its dose of 1 microM.	Kynurenine	0-12	nerve growth factor	Mus musculus	97-100
9578134-3	1998	L-Kynurenine, a metabolite of the kynurenine pathway, markedly increased the levels of mRNAs for NGF, the maximal increases (4-5 fold) occurred at its dose of 1 microM.	Kynurenine	34-44	nerve growth factor	Mus musculus	97-100
9578134-4	1998	Kynurenine-induced increase in mRNA levels for NGF occurred as early as 1 h after the addition of the compound, peaked at 4 h and declined thereafter.	Kynurenine	0-10	nerve growth factor	Mus musculus	47-50
9363902-1	1997	BACKGROUND: In various cells including monocytes the cytokine interferon-gamma as well as lipopolysaccharide induce indoleamine 2,3-dioxygenase which degrades tryptophan to form L-kynurenine.	Kynurenine	178-190	interferon gamma	Homo sapiens	62-78
9466588-3	1998	IFN-gamma is the key inducer of indoleamine 2,3-dioxygenase (IDO), which is the catalyst of the first, and rate-limiting, step in the metabolism of tryptophan (Trp) along the kynurenine (Kyn) pathway.	Kynurenine	175-185	interferon gamma	Mus musculus	0-9
9466588-3	1998	IFN-gamma is the key inducer of indoleamine 2,3-dioxygenase (IDO), which is the catalyst of the first, and rate-limiting, step in the metabolism of tryptophan (Trp) along the kynurenine (Kyn) pathway.	Kynurenine	175-185	indoleamine 2,3-dioxygenase 1	Mus musculus	32-59
9466588-3	1998	IFN-gamma is the key inducer of indoleamine 2,3-dioxygenase (IDO), which is the catalyst of the first, and rate-limiting, step in the metabolism of tryptophan (Trp) along the kynurenine (Kyn) pathway.	Kynurenine	175-185	indoleamine 2,3-dioxygenase 1	Mus musculus	61-64
9466588-3	1998	IFN-gamma is the key inducer of indoleamine 2,3-dioxygenase (IDO), which is the catalyst of the first, and rate-limiting, step in the metabolism of tryptophan (Trp) along the kynurenine (Kyn) pathway.	Kynurenine	187-190	interferon gamma	Mus musculus	0-9
9466588-3	1998	IFN-gamma is the key inducer of indoleamine 2,3-dioxygenase (IDO), which is the catalyst of the first, and rate-limiting, step in the metabolism of tryptophan (Trp) along the kynurenine (Kyn) pathway.	Kynurenine	187-190	indoleamine 2,3-dioxygenase 1	Mus musculus	32-59
9466588-3	1998	IFN-gamma is the key inducer of indoleamine 2,3-dioxygenase (IDO), which is the catalyst of the first, and rate-limiting, step in the metabolism of tryptophan (Trp) along the kynurenine (Kyn) pathway.	Kynurenine	187-190	indoleamine 2,3-dioxygenase 1	Mus musculus	61-64
9871470-4	1998	Nitric oxide (NO) production negatively modulates the expression of IDO activity in IFN-gamma-primed macrophages, thereby indicating a cross-talk between the kynurenine and nitridergic pathways in these cells.	Kynurenine	158-168	indoleamine 2,3-dioxygenase 1	Mus musculus	68-71
9871470-4	1998	Nitric oxide (NO) production negatively modulates the expression of IDO activity in IFN-gamma-primed macrophages, thereby indicating a cross-talk between the kynurenine and nitridergic pathways in these cells.	Kynurenine	158-168	interferon gamma	Mus musculus	84-93
9449433-4	1997	L-Kynurenine had a marked stimulatory effect on NGF production at a dose of 10 microM.	Kynurenine	0-12	nerve growth factor	Mus musculus	48-51
9291104-5	1997	High activities of kynurenine 3-hydroxylase, kynureninase or 3-hydroxyanthranilate 3,4-dioxygenase were found in interferon-gamma-stimulated macrophages, THP-1 cells and SKHEP1 cells, and these cells made large amounts of quinolinate when supplied with L-tryptophan, L-kynurenine, 3-hydroxykynurenine or 3-hydroxyanthranilate.	Kynurenine	267-279	kynurenine 3-monooxygenase	Homo sapiens	19-43
9291104-5	1997	High activities of kynurenine 3-hydroxylase, kynureninase or 3-hydroxyanthranilate 3,4-dioxygenase were found in interferon-gamma-stimulated macrophages, THP-1 cells and SKHEP1 cells, and these cells made large amounts of quinolinate when supplied with L-tryptophan, L-kynurenine, 3-hydroxykynurenine or 3-hydroxyanthranilate.	Kynurenine	267-279	interferon gamma	Homo sapiens	113-129
9291104-5	1997	High activities of kynurenine 3-hydroxylase, kynureninase or 3-hydroxyanthranilate 3,4-dioxygenase were found in interferon-gamma-stimulated macrophages, THP-1 cells and SKHEP1 cells, and these cells made large amounts of quinolinate when supplied with L-tryptophan, L-kynurenine, 3-hydroxykynurenine or 3-hydroxyanthranilate.	Kynurenine	267-279	GLI family zinc finger 2	Homo sapiens	154-159
9214572-2	1997	In the present work we determined the rate constants, k(r), for scavenging .OH radicals by melatonin, 5-methoxytryptamine (5-MeO-T), 5-hydroxytryptamine (serotonin, 5-OH-T), 6-chloromelatonin (6-Cl-MLT), 6-hydroxymelatonin (6-OH-MLT), and kynurenine (KN) in aqueous solutions.	Kynurenine	239-249	mitogen-activated protein kinase kinase kinase 20	Homo sapiens	198-201
9237672-1	1997	Kynurenine 3-monooxygenase, an NADPH-dependent flavin monooxygenase, catalyses the hydroxylation of L-kynurenine to L-3-hydroxykynurenine.	Kynurenine	100-112	kynurenine 3-monooxygenase	Homo sapiens	0-26
9214572-2	1997	In the present work we determined the rate constants, k(r), for scavenging .OH radicals by melatonin, 5-methoxytryptamine (5-MeO-T), 5-hydroxytryptamine (serotonin, 5-OH-T), 6-chloromelatonin (6-Cl-MLT), 6-hydroxymelatonin (6-OH-MLT), and kynurenine (KN) in aqueous solutions.	Kynurenine	239-249	mitogen-activated protein kinase kinase kinase 20	Homo sapiens	229-232
8973572-6	1996	Interferon gamma, an inducer of indoleamine 2,3-dioxygenase, increased the accumulation of L-kynurenine by all three cell types (to more than 40 microM).	Kynurenine	91-103	interferon gamma	Homo sapiens	0-16
8817290-7	1996	RESULTS: IDO activity in the retina extract was 51.5 (+/-10) nmol/g tissue/h, and kynurenine formation was detected.	Kynurenine	82-92	indoleamine 2,3-dioxygenase 1	Homo sapiens	9-12
8906262-0	1996	Regulation of the kynurenine pathway by IFN-gamma in murine cloned macrophages and microglial cells.	Kynurenine	18-28	interferon gamma	Mus musculus	40-49
8769859-0	1996	Regulation of the kynurenine metabolic pathway by interferon-gamma in murine cloned macrophages and microglial cells.	Kynurenine	18-28	interferon gamma	Mus musculus	50-66
8769859-2	1996	In the present work, the regulation of kynurenine pathway enzymes by interferon-gamma (IFN-gamma) was studied in immortalized murine macrophages (MT2) and microglial (N11) cells.	Kynurenine	39-49	interferon gamma	Mus musculus	69-85
8769859-2	1996	In the present work, the regulation of kynurenine pathway enzymes by interferon-gamma (IFN-gamma) was studied in immortalized murine macrophages (MT2) and microglial (N11) cells.	Kynurenine	39-49	interferon gamma	Mus musculus	87-96
8769859-2	1996	In the present work, the regulation of kynurenine pathway enzymes by interferon-gamma (IFN-gamma) was studied in immortalized murine macrophages (MT2) and microglial (N11) cells.	Kynurenine	39-49	metallothionein 2	Mus musculus	146-149
8906257-6	1996	Interferon-gamma also caused a dramatic dose-dependent increase in indoleamine 2,3-dioxygenase mRNA, with consequent depletion of tryptophan and accumulation of kynurenine in the culture media.	Kynurenine	161-171	interferon gamma	Homo sapiens	0-16
8906305-2	1996	Kynurenine-2-oxoglutarate aminotransferase (kynurenine specific, designated here KAT-II) and kynurenine pyruvate aminotransferase (designated here KAT-I) activities were detected in the kidney using 2 microM kynurenine.	Kynurenine	44-54	kynurenine aminotransferase 1	Rattus norvegicus	81-86
8906305-8	1996	KAT-I or GTK activity of purified preparation, however, inhibited strongly addition of glutamine either kynurenine.	Kynurenine	104-114	kynurenine aminotransferase 1	Rattus norvegicus	0-5
8906305-8	1996	KAT-I or GTK activity of purified preparation, however, inhibited strongly addition of glutamine either kynurenine.	Kynurenine	104-114	kynurenine aminotransferase 1	Rattus norvegicus	9-12
8906305-10	1996	Phenylpyruvate or 2-oxo-4-methiolbutyrate reduced the inhibition of purified KAT-I activity by glutamine using 2 microM kynurenine.	Kynurenine	120-130	kynurenine aminotransferase 1	Rattus norvegicus	77-82
7493966-1	1995	Several aminotransferases with kynurenine aminotransferase (KAT) activity are able to convert L-kynurenine into kynurenic acid, a putative endogenous modulator of glutamatergic neurotransmission.	Kynurenine	94-106	thiosulfate sulfurtransferase like domain containing 1	Homo sapiens	60-63
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.	Kynurenine	205-215	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.	Kynurenine	205-215	indoleamine 2,3-dioxygenase 1	Homo sapiens	42-45
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.	Kynurenine	205-215	interferon gamma	Homo sapiens	140-156
8583213-6	1995	CSF L-kynurenine levels increased in parallel to the accumulations in QUIN, which is consistent with increased activity of the first enzyme of the kynurenine pathway, indoleamine-2,3-dioxygenase.	Kynurenine	6-16	colony stimulating factor 2	Homo sapiens	0-3
8583213-6	1995	CSF L-kynurenine levels increased in parallel to the accumulations in QUIN, which is consistent with increased activity of the first enzyme of the kynurenine pathway, indoleamine-2,3-dioxygenase.	Kynurenine	4-16	colony stimulating factor 2	Homo sapiens	0-3
7617307-2	1995	Indoleamine-2,3-dioxygenase (IDO) activity, which regulates kynurenine metabolism, may thus be increased in HIV infection.	Kynurenine	60-70	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-27
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 &gt; 90% depletion of tryptophan, and a corresponding &gt; 30-fold increase in the tryptophan metabolite kynurenine in the culture media.	Kynurenine	243-253	interferon gamma	Homo sapiens	44-53
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 &gt; 90% depletion of tryptophan, and a corresponding &gt; 30-fold increase in the tryptophan metabolite kynurenine in the culture media.	Kynurenine	243-253	indoleamine 2,3-dioxygenase 1	Homo sapiens	125-128
7617307-2	1995	Indoleamine-2,3-dioxygenase (IDO) activity, which regulates kynurenine metabolism, may thus be increased in HIV infection.	Kynurenine	60-70	indoleamine 2,3-dioxygenase 1	Homo sapiens	29-32
7617307-6	1995	IDO activity is increased in HIV-associated dementia and is thus likely to increase kynurenine pathway metabolites, such as 3-hydroxykynurenine and quinolinic acid, and elevated levels of these neurotoxins may contribute to the neuronal deficits underlying HIV-associated dementia.	Kynurenine	84-94	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-3
7955408-5	1994	In vitro studies of indole binding to human serum proteins demonstrated the parallel displacement of bound tryptophan and kynurenine by physiological changes in pH, serum albumin concentration and free fatty acid concentration.	Kynurenine	122-132	albumin	Homo sapiens	165-178
7814143-2	1995	During IFN-gamma therapy all 3 tumours showed a profound depletion in L-tryptophan and a corresponding rise in L-kynurenine.	Kynurenine	111-123	interferon gamma	Homo sapiens	7-16
8182147-4	1994	Exposure of PBMC or MDM to IFN gamma induced the degradation of extracellular Trp with concomitant accumulation of kynurenine, anthranilic and 3-hydroxyanthranilic acid (3HAA) in the culture medium.	Kynurenine	115-125	interferon gamma	Homo sapiens	27-36
7523670-5	1994	RESULTS: In fresh and in &gt; or = 2 month-old cultures, IFN-gamma strongly stimulated IDO activity, a corresponding fall in supernatant tryptophan levels, and an elevation in the supernatant concentration of kynurenine, tryptophan"s principal metabolite, mRNA for IDO was likewise markedly increased in cells after 4 days" incubation with IFN-gamma.	Kynurenine	209-219	interferon gamma	Homo sapiens	57-66
7523670-5	1994	RESULTS: In fresh and in &gt; or = 2 month-old cultures, IFN-gamma strongly stimulated IDO activity, a corresponding fall in supernatant tryptophan levels, and an elevation in the supernatant concentration of kynurenine, tryptophan"s principal metabolite, mRNA for IDO was likewise markedly increased in cells after 4 days" incubation with IFN-gamma.	Kynurenine	209-219	indoleamine 2,3-dioxygenase 1	Homo sapiens	265-268
7523670-5	1994	RESULTS: In fresh and in &gt; or = 2 month-old cultures, IFN-gamma strongly stimulated IDO activity, a corresponding fall in supernatant tryptophan levels, and an elevation in the supernatant concentration of kynurenine, tryptophan"s principal metabolite, mRNA for IDO was likewise markedly increased in cells after 4 days" incubation with IFN-gamma.	Kynurenine	209-219	interferon gamma	Homo sapiens	340-349
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).	Kynurenine	108-118	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-27
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).	Kynurenine	108-118	indoleamine 2,3-dioxygenase 1	Homo sapiens	29-32
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).	Kynurenine	108-118	interferon gamma	Homo sapiens	190-199
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).	Kynurenine	108-118	interferon gamma	Homo sapiens	172-188
8294935-1	1994	Two kynurenine aminotransferases (KATs), arbitrarily termed KAT I and KAT II, are capable of producing the neuroinhibitory brain metabolite kynurenic acid from L-kynurenine in human brain tissue.	Kynurenine	160-172	kynurenine aminotransferase 1	Homo sapiens	60-76
8126705-2	1994	The synthesis of (o-nitrobenzoyl)-, (m-nitrobenzoyl)-, and (p-nitrobenzoyl)alanine (o-, m-, and p-NBA), three new kynurenine analogues, and their evaluation as inhibitors of kynureninase and kynurenine-3-hydroxylase are reported.	Kynurenine	114-124	kynurenine 3-monooxygenase	Rattus norvegicus	191-215
8288893-4	1994	The determination of kynurenine in the supernatant of IFN-gamma activated cells was performed photometrically using a microplate reader.	Kynurenine	21-31	interferon gamma	Homo sapiens	54-63
8288893-12	1994	We conclude that the measurement of kynurenine production induced by IFN-gamma can be used to determinate IFN-gamma content.	Kynurenine	36-46	interferon gamma	Homo sapiens	69-78
8288893-5	1994	It was found that the amount of kynurenine produced was directly proportional to the amount of IFN-gamma used to activate cells.	Kynurenine	32-42	interferon gamma	Homo sapiens	95-104
8288893-12	1994	We conclude that the measurement of kynurenine production induced by IFN-gamma can be used to determinate IFN-gamma content.	Kynurenine	36-46	interferon gamma	Homo sapiens	106-115
7507440-2	1993	Kynurenine formamidase inhibition by organophosphorous acid triesters and methylcarbamates is the proposed primary event resulting in increase in xanthurenic acid urinary excretion and plasma L-kynurenine.	Kynurenine	192-204	arylformamidase	Mus musculus	0-22
8239646-3	1993	The kynurenine 3-hydroxylase assay is based on the conversion of L-kynurenine to 3-hydroxykynurenine in vitro and the quantification of 3-hydroxykynurenine by high-performance liquid chromatography.	Kynurenine	65-77	kynurenine 3-monooxygenase	Homo sapiens	4-28
8239646-9	1993	Kynurenine 3-hydroxylase may have an important role in determining the flux of kynurenine in brain.	Kynurenine	79-89	kynurenine 3-monooxygenase	Homo sapiens	0-24
8155745-7	1994	The effect of whole body immune stimulation on the plasma levels of endogenous L-kynurenine in mice stimulated with interferon-gamma was also quantified.	Kynurenine	79-91	interferon gamma	Mus musculus	116-132
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.	Kynurenine	130-135	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.	Kynurenine	130-135	indoleamine 2,3-dioxygenase 1	Homo sapiens	81-84
8293279-15	1993	These results suggest roles for increased activities of IDO, kynurenine-3-hydroxylase and kynureninase in accelerating the synthesis of QUIN, L-KYN and KYNA in conditions of brain inflammation.	Kynurenine	142-147	indoleamine 2,3-dioxygenase 1	Homo sapiens	56-59
8293279-15	1993	These results suggest roles for increased activities of IDO, kynurenine-3-hydroxylase and kynureninase in accelerating the synthesis of QUIN, L-KYN and KYNA in conditions of brain inflammation.	Kynurenine	142-147	kynurenine 3-monooxygenase	Homo sapiens	61-85
7507440-3	1993	Alteration of the L-kynurenine pathway occurred with compounds that inhibited liver kynurenine formamidase by more than 80%.	Kynurenine	18-30	arylformamidase	Mus musculus	84-106
1419165-7	1992	The possibility that elimination of seizures by ACTH might be related to decreased production of kynurenine metabolites was discussed.	Kynurenine	97-107	proopiomelanocortin	Homo sapiens	48-52
8087205-7	1993	AadAT-II further showed the activity of tryptophan and kynurenine.	Kynurenine	55-65	aminoadipate aminotransferase	Homo sapiens	0-5
1465184-6	1992	Interferon-gamma, pokeweed mitogen and lipopolysaccharide induced indoleamine-2,3-dioxygenase, the first enzyme of the kynurenine pathway, and increased both L-kynurenine and quinolinic acid concentrations of brain and systemic tissues, particularly in the lung, gastrointestinal tract and spleen.	Kynurenine	119-129	interferon gamma	Mus musculus	0-16
1465184-6	1992	Interferon-gamma, pokeweed mitogen and lipopolysaccharide induced indoleamine-2,3-dioxygenase, the first enzyme of the kynurenine pathway, and increased both L-kynurenine and quinolinic acid concentrations of brain and systemic tissues, particularly in the lung, gastrointestinal tract and spleen.	Kynurenine	158-170	interferon gamma	Mus musculus	0-16
1465184-8	1992	Increases in kynurenine pathway metabolism were sustained in mice given daily injections of interferon-gamma for seven days and subsequent responses to interferon-gamma were further enhanced.	Kynurenine	13-23	interferon gamma	Mus musculus	92-108
1465184-8	1992	Increases in kynurenine pathway metabolism were sustained in mice given daily injections of interferon-gamma for seven days and subsequent responses to interferon-gamma were further enhanced.	Kynurenine	13-23	interferon gamma	Mus musculus	152-168
1465184-10	1992	Systemic administration of a monoclonal antibody to mouse interferon-gamma either attenuated or abolished the responses of kynurenine pathway metabolism to pokeweed mitogen and interferon-gamma.	Kynurenine	123-133	interferon gamma	Mus musculus	58-74
1465184-10	1992	Systemic administration of a monoclonal antibody to mouse interferon-gamma either attenuated or abolished the responses of kynurenine pathway metabolism to pokeweed mitogen and interferon-gamma.	Kynurenine	123-133	interferon gamma	Mus musculus	177-193
8353134-2	1993	Both 3-hydroxykynurenine and kynurenine react with solvated electrons with diffusion controlled rate constants (k = 2.5 x 10(10) M-1 s-1 and 2.3 x 10(10) M-1s-1, respectively).	Kynurenine	14-24	myoregulin	Homo sapiens	129-142
8353134-5	1993	Reactions of 3-hydroxykynurenine and kynurenine with hydroxyl radicals proceed with diffusion controlled rate constants (1.2 x 10(10) M-1 s-1 and 1.3 x 10(10) M-1 s-1, respectively).	Kynurenine	22-32	myoregulin	Homo sapiens	134-147
8353134-7	1993	The differences in these rate constants are attributed to differences in the measured oxidation potentials for 3-hydroxykynurenine (+1.0 V vs. NHE) and kynurenine (+1.15 V vs. NHE).	Kynurenine	120-130	solute carrier family 9 member C1	Homo sapiens	143-146
8353134-7	1993	The differences in these rate constants are attributed to differences in the measured oxidation potentials for 3-hydroxykynurenine (+1.0 V vs. NHE) and kynurenine (+1.15 V vs. NHE).	Kynurenine	120-130	solute carrier family 9 member C1	Homo sapiens	176-179
1465184-2	1992	Clinical studies have established that sustained elevations of quinolinic acid, L-kynurenine and kynurenic acid within the cerebrospinal fluid occur in patients with a broad spectrum of inflammatory diseases and correlate with markers of immune activation and interferon-gamma activity.	Kynurenine	80-92	interferon gamma	Homo sapiens	260-276
1465184-3	1992	The present study describes an animal model that replicates these clinical observations and investigates the role of interferon-gamma as a mediator between immune activation and increased kynurenine pathway metabolism.	Kynurenine	188-198	interferon gamma	Mus musculus	117-133
1387655-4	1992	Further, close inter-correlations exist between QUIN kynurenic acid and L-kynurenine with both beta 2-microglobulin and neopterin in CSF and serum.	Kynurenine	72-84	beta-2-microglobulin	Homo sapiens	95-115
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.	Kynurenine	205-215	interferon gamma	Homo sapiens	15-31
1569135-5	1992	The induction of c-fos immunoreactivity in cerebral cortex was also blocked by this dose of L-kynurenine.	Kynurenine	92-104	Fos proto-oncogene, AP-1 transcription factor subunit	Rattus norvegicus	17-22
1612635-6	1992	Also the degradation of tryptophan via the kynurenine pathway is induced by interferon-gamma.	Kynurenine	43-53	interferon gamma	Homo sapiens	76-92
1728387-13	1992	The combination of TNF and gamma-IFN significantly increased urinary kynurenine levels more than either TNF alone or gamma-IFN alone.	Kynurenine	69-79	tumor necrosis factor	Homo sapiens	19-22
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.	Kynurenine	89-99	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.	Kynurenine	89-99	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.	Kynurenine	89-99	interferon gamma	Homo sapiens	191-200
1724602-4	1991	Following treatment, marked increases in 5-HIAA and decreases in kynurenine levels were observed in the CSF of the 5 infants whose seizures were eliminated or reduced by ACTH.	Kynurenine	65-75	proopiomelanocortin	Homo sapiens	170-174
1724602-10	1991	The possibility that elimination of seizures by ACTH may be related to decreased production of certain kynurenine metabolites, particularly quinolinic acid, is discussed.	Kynurenine	103-113	proopiomelanocortin	Homo sapiens	48-52
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.	Kynurenine	205-215	interferon gamma	Homo sapiens	33-42
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.	Kynurenine	205-215	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.	Kynurenine	205-215	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.	Kynurenine	77-87	interferon gamma	Homo sapiens	59-68
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.	Kynurenine	77-87	indoleamine 2,3-dioxygenase 1	Homo sapiens	186-189
1647247-2	1991	In the present study, increased activity of indoleamine-2,3-dioxygenase (IDO), the first enzyme of the kynurenine pathway, occurred in cerebral cortex and lung of macaques with clinical SAIDS.	Kynurenine	103-113	indoleamine 2,3-dioxygenase 1	Homo sapiens	44-71
1830237-2	1991	In the present study, repeated injections of gamma-interferon (5000 IU, every 3 days for 39 days) to C57BL6 mice were associated with persistent activation of indoleamine-2,3-dioxygenase (IDO), the first enzyme of the kynurenine pathway, in lung and brain, sustained increases in brain QUIN concentration and increases in plasma L-kynurenine and QUIN levels.	Kynurenine	218-228	interferon gamma	Mus musculus	45-61
1830237-2	1991	In the present study, repeated injections of gamma-interferon (5000 IU, every 3 days for 39 days) to C57BL6 mice were associated with persistent activation of indoleamine-2,3-dioxygenase (IDO), the first enzyme of the kynurenine pathway, in lung and brain, sustained increases in brain QUIN concentration and increases in plasma L-kynurenine and QUIN levels.	Kynurenine	218-228	indoleamine 2,3-dioxygenase 1	Mus musculus	159-186
1830237-2	1991	In the present study, repeated injections of gamma-interferon (5000 IU, every 3 days for 39 days) to C57BL6 mice were associated with persistent activation of indoleamine-2,3-dioxygenase (IDO), the first enzyme of the kynurenine pathway, in lung and brain, sustained increases in brain QUIN concentration and increases in plasma L-kynurenine and QUIN levels.	Kynurenine	329-341	interferon gamma	Mus musculus	45-61
1830237-2	1991	In the present study, repeated injections of gamma-interferon (5000 IU, every 3 days for 39 days) to C57BL6 mice were associated with persistent activation of indoleamine-2,3-dioxygenase (IDO), the first enzyme of the kynurenine pathway, in lung and brain, sustained increases in brain QUIN concentration and increases in plasma L-kynurenine and QUIN levels.	Kynurenine	329-341	indoleamine 2,3-dioxygenase 1	Mus musculus	159-186
1830237-3	1991	Mice chronically treated with gamma-interferon offer an animal model to investigate the effects of sustained immune stimulation on kynurenine pathway metabolism.	Kynurenine	131-141	interferon gamma	Mus musculus	30-46
1647247-2	1991	In the present study, increased activity of indoleamine-2,3-dioxygenase (IDO), the first enzyme of the kynurenine pathway, occurred in cerebral cortex and lung of macaques with clinical SAIDS.	Kynurenine	103-113	indoleamine 2,3-dioxygenase 1	Homo sapiens	73-76
2166783-4	1990	The negative correlation of tryptophan with kynurenine and neopterin concentrations indicates activity of indoleamine 2,3-dioxygenase (IDO) in patients.	Kynurenine	44-54	indoleamine 2,3-dioxygenase 1	Homo sapiens	106-133
2054604-4	1991	The possibility that arylamine NAT may be involved in the control of kynurenine metabolism in the brain is discussed.	Kynurenine	69-79	N-acetyltransferase 1	Rattus norvegicus	31-34
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.	Kynurenine	172-182	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-27
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.	Kynurenine	172-182	indoleamine 2,3-dioxygenase 1	Homo sapiens	29-32
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.	Kynurenine	184-187	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-27
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.	Kynurenine	184-187	indoleamine 2,3-dioxygenase 1	Homo sapiens	29-32
2321759-1	1990	Kynurenine 3-monooxygenase is a flavin-dependent monooxygenase that catalyzes the oxidation of L-kynurenine to 3-hydroxy-L-kynurenine in the kynurenine pathway of tryptophan metabolism.	Kynurenine	95-107	kynurenine 3-monooxygenase	Homo sapiens	0-26
2321759-1	1990	Kynurenine 3-monooxygenase is a flavin-dependent monooxygenase that catalyzes the oxidation of L-kynurenine to 3-hydroxy-L-kynurenine in the kynurenine pathway of tryptophan metabolism.	Kynurenine	97-107	kynurenine 3-monooxygenase	Homo sapiens	0-26
2300969-6	1990	In repeated nicotinic acid administration plasma tryptophan levels did not diminish, despite the high activation of tryptophan 2,3-dioxygenase (high flux of tryptophan through the kynurenine pathway).	Kynurenine	180-190	tryptophan 2,3-dioxygenase	Homo sapiens	116-142
2166783-4	1990	The negative correlation of tryptophan with kynurenine and neopterin concentrations indicates activity of indoleamine 2,3-dioxygenase (IDO) in patients.	Kynurenine	44-54	indoleamine 2,3-dioxygenase 1	Homo sapiens	135-138
33790369-1	2021	Exercise prevents depression through peroxisome proliferator-activated receptor-gamma coactivator 1alpha (PGC-1alpha)-mediated activation of a particular branch of the kynurenine pathway.	Kynurenine	168-178	peroxisome proliferative activated receptor, gamma, coactivator 1 alpha	Mus musculus	37-104
33790369-1	2021	Exercise prevents depression through peroxisome proliferator-activated receptor-gamma coactivator 1alpha (PGC-1alpha)-mediated activation of a particular branch of the kynurenine pathway.	Kynurenine	168-178	peroxisome proliferative activated receptor, gamma, coactivator 1 alpha	Mus musculus	106-116
33775832-8	2021	Finally, using moderated-mediation, several pro-inflammatory factors partially mediated Kyn/5-HT and negative affect scores in participants with subclinical Abeta (i.e., Abeta-), whereas such associations were fully mediated by Complement 3 in Abeta+ participants.	Kynurenine	88-91	amyloid beta precursor protein	Homo sapiens	157-162
33775832-8	2021	Finally, using moderated-mediation, several pro-inflammatory factors partially mediated Kyn/5-HT and negative affect scores in participants with subclinical Abeta (i.e., Abeta-), whereas such associations were fully mediated by Complement 3 in Abeta+ participants.	Kynurenine	88-91	amyloid beta precursor protein	Homo sapiens	170-175
33775832-8	2021	Finally, using moderated-mediation, several pro-inflammatory factors partially mediated Kyn/5-HT and negative affect scores in participants with subclinical Abeta (i.e., Abeta-), whereas such associations were fully mediated by Complement 3 in Abeta+ participants.	Kynurenine	88-91	amyloid beta precursor protein	Homo sapiens	170-175
33799594-2	2021	As the kynurenine pathway plays an important role connecting inflammation and depression, it is plausible to investigate this pathway for predictive genetic markers for IFN-alpha-induced depression.	Kynurenine	7-17	interferon alpha 1	Homo sapiens	169-178
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.	Kynurenine	142-152	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.	Kynurenine	142-152	indoleamine 2,3-dioxygenase 1	Homo sapiens	70-73
33799594-13	2021	Conclusions: This study provided supportive evidence of the involvement of the kynurenine pathway in IFN-alpha-induced depression.	Kynurenine	79-89	interferon alpha 1	Homo sapiens	101-110
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.	Kynurenine	154-157	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.	Kynurenine	154-157	indoleamine 2,3-dioxygenase 1	Homo sapiens	70-73
33236682-5	2020	The tryptophan metabolite, kynurenine, is one of these ligands that can interact with AHR, leading to immune suppression and subsequently, susceptibility to gastric cancer.	Kynurenine	27-37	aryl hydrocarbon receptor	Homo sapiens	86-89
33777681-3	2021	Mechanistically, chemotherapy-induced intestinal damage triggered the formation of an interleukin-6 (IL-6)-indoleamine 2,3-dioxygenase 1 (IDO1)-aryl hydrocarbon receptor (AHR) positive feedback loop, which accelerated kynurenine pathway metabolism in gut.	Kynurenine	218-228	interleukin 6	Homo sapiens	86-99
33777681-3	2021	Mechanistically, chemotherapy-induced intestinal damage triggered the formation of an interleukin-6 (IL-6)-indoleamine 2,3-dioxygenase 1 (IDO1)-aryl hydrocarbon receptor (AHR) positive feedback loop, which accelerated kynurenine pathway metabolism in gut.	Kynurenine	218-228	indoleamine 2,3-dioxygenase 1	Homo sapiens	138-142
33777681-3	2021	Mechanistically, chemotherapy-induced intestinal damage triggered the formation of an interleukin-6 (IL-6)-indoleamine 2,3-dioxygenase 1 (IDO1)-aryl hydrocarbon receptor (AHR) positive feedback loop, which accelerated kynurenine pathway metabolism in gut.	Kynurenine	218-228	aryl hydrocarbon receptor	Homo sapiens	144-169
33777681-3	2021	Mechanistically, chemotherapy-induced intestinal damage triggered the formation of an interleukin-6 (IL-6)-indoleamine 2,3-dioxygenase 1 (IDO1)-aryl hydrocarbon receptor (AHR) positive feedback loop, which accelerated kynurenine pathway metabolism in gut.	Kynurenine	218-228	aryl hydrocarbon receptor	Homo sapiens	171-174
33777681-7	2021	This work highlights GPR35 and AHR as the guardian of kynurenine pathway metabolism and core component of defense responses against intestinal damage.	Kynurenine	54-64	G protein-coupled receptor 35	Homo sapiens	21-26
33777681-7	2021	This work highlights GPR35 and AHR as the guardian of kynurenine pathway metabolism and core component of defense responses against intestinal damage.	Kynurenine	54-64	aryl hydrocarbon receptor	Homo sapiens	31-34
33235198-6	2020	Evaluation of metabolomics data reveals that AHRR methylation associated with kynurenine levels, which are lower among subjects with PTSD.	Kynurenine	78-88	aryl hydrocarbon receptor repressor	Homo sapiens	45-49
34871928-1	2022	BACKGROUND: Conversion of tryptophan to kynurenine may promote glioma growth and suppress antitumor immune response through activation of the aryl hydrocarbon receptor.	Kynurenine	40-50	aryl hydrocarbon receptor	Homo sapiens	142-167
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.	Kynurenine	7-17	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.	Kynurenine	7-17	indoleamine 2,3-dioxygenase 1	Rattus norvegicus	67-70
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.	Kynurenine	123-133	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.	Kynurenine	123-133	indoleamine 2,3-dioxygenase 1	Rattus norvegicus	67-70
33031882-12	2021	Long-term ethanol withdrawal elevated kynurenine levels, specifically in the prefrontal cortex, suggesting that the depressive-like responses observed after long-term withdrawal might be related to the increased IDO activity.	Kynurenine	38-48	indoleamine 2,3-dioxygenase 1	Rattus norvegicus	212-215
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.	Kynurenine	149-159	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-29
34902346-9	2022	Kynurenine and the KYN/TRP ratio significantly correlated with IL-6 (rho = 0.441 and 0.448, p-values < 0.001).	Kynurenine	0-10	interleukin 6	Homo sapiens	63-67
34902346-9	2022	Kynurenine and the KYN/TRP ratio significantly correlated with IL-6 (rho = 0.441 and 0.448, p-values < 0.001).	Kynurenine	19-22	interleukin 6	Homo sapiens	63-67
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.	Kynurenine	149-159	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.	Kynurenine	161-164	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.	Kynurenine	161-164	indoleamine 2,3-dioxygenase 1	Homo sapiens	31-35
34773309-3	2022	The obtained pH-responsive nanomedicine, coined as acidity-IDO1-modulation nanoparticles (AIM NPs), is able to instantly neutralize protons, and release 4PI to suppress the IDO1 mediated production of kynurenine (Kyn) upon tumor accumulation.	Kynurenine	201-211	indoleamine 2,3-dioxygenase 1	Mus musculus	59-63
34773309-3	2022	The obtained pH-responsive nanomedicine, coined as acidity-IDO1-modulation nanoparticles (AIM NPs), is able to instantly neutralize protons, and release 4PI to suppress the IDO1 mediated production of kynurenine (Kyn) upon tumor accumulation.	Kynurenine	201-211	indoleamine 2,3-dioxygenase 1	Mus musculus	173-177
34773309-3	2022	The obtained pH-responsive nanomedicine, coined as acidity-IDO1-modulation nanoparticles (AIM NPs), is able to instantly neutralize protons, and release 4PI to suppress the IDO1 mediated production of kynurenine (Kyn) upon tumor accumulation.	Kynurenine	213-216	indoleamine 2,3-dioxygenase 1	Mus musculus	59-63
34773309-3	2022	The obtained pH-responsive nanomedicine, coined as acidity-IDO1-modulation nanoparticles (AIM NPs), is able to instantly neutralize protons, and release 4PI to suppress the IDO1 mediated production of kynurenine (Kyn) upon tumor accumulation.	Kynurenine	213-216	indoleamine 2,3-dioxygenase 1	Mus musculus	173-177
34948292-0	2021	Alterations in Kynurenine and NAD+ Salvage Pathways during the Successful Treatment of Inflammatory Bowel Disease Suggest HCAR3 and NNMT as Potential Drug Targets.	Kynurenine	15-25	hydroxycarboxylic acid receptor 3	Homo sapiens	122-127
34099189-8	2022	Secondary analysis of the PGC-SCZ dataset detected an interaction (rs13265509, p = 1.1 x 10-7) in a locus containing IDO2, a kynurenine pathway enzyme with immunoregulatory functions implicated in SCZ, BIP, and MDD.	Kynurenine	125-135	indoleamine 2,3-dioxygenase 2	Homo sapiens	117-121
34969166-10	2022	Kyn restored the inhibitory effect of TDO2 inhibition on activation of AA-FLS.	Kynurenine	0-3	tryptophan 2,3-dioxygenase	Rattus norvegicus	38-42
34817270-1	2022	Administration of branched-chain amino acids (BCAA) has been suggested to enhance mitochondrial biogenesis, including levels of PGC-1alpha, which may, in turn, alter kynurenine metabolism.	Kynurenine	166-176	PPARG coactivator 1 alpha	Homo sapiens	128-138
34714577-1	2022	The aryl hydrocarbon receptor (AHR) pathway modulates the immune system in response to kynurenine, an endogenous tryptophan metabolite.	Kynurenine	87-97	aryl hydrocarbon receptor	Homo sapiens	4-29
34714577-1	2022	The aryl hydrocarbon receptor (AHR) pathway modulates the immune system in response to kynurenine, an endogenous tryptophan metabolite.	Kynurenine	87-97	aryl hydrocarbon receptor	Homo sapiens	31-34
34714577-2	2022	IDO1 and TDO2 catalyze kynurenine production, which promotes cancer progression by compromising host immunosurveillance.	Kynurenine	23-33	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-4
34714577-2	2022	IDO1 and TDO2 catalyze kynurenine production, which promotes cancer progression by compromising host immunosurveillance.	Kynurenine	23-33	tryptophan 2,3-dioxygenase	Homo sapiens	9-13
34714577-8	2022	Thus, our data indicate that the activation of the TDO2-kynurenine-AHR pathway facilitates liver metastasis of colon cancer via PD-L1-mediated immune evasion and maintenance of stemness.	Kynurenine	56-66	tryptophan 2,3-dioxygenase	Homo sapiens	51-55
34714577-8	2022	Thus, our data indicate that the activation of the TDO2-kynurenine-AHR pathway facilitates liver metastasis of colon cancer via PD-L1-mediated immune evasion and maintenance of stemness.	Kynurenine	56-66	aryl hydrocarbon receptor	Homo sapiens	67-70
34714577-8	2022	Thus, our data indicate that the activation of the TDO2-kynurenine-AHR pathway facilitates liver metastasis of colon cancer via PD-L1-mediated immune evasion and maintenance of stemness.	Kynurenine	56-66	CD274 molecule	Homo sapiens	128-133
34944003-0	2021	Inhibition of Human Osteoclast Differentiation by Kynurenine through the Aryl-Hydrocarbon Receptor Pathway.	Kynurenine	50-60	aryl hydrocarbon receptor	Homo sapiens	73-98
34788602-7	2021	Kynurenine, the product of IDO1 catabolism, activates the aryl hydrocarbon receptor in LLPC, reinforcing CD28 expression and survival signaling.	Kynurenine	0-10	indoleamine 2,3-dioxygenase 1	Homo sapiens	27-31
34788602-7	2021	Kynurenine, the product of IDO1 catabolism, activates the aryl hydrocarbon receptor in LLPC, reinforcing CD28 expression and survival signaling.	Kynurenine	0-10	aryl hydrocarbon receptor	Homo sapiens	58-83
34788602-7	2021	Kynurenine, the product of IDO1 catabolism, activates the aryl hydrocarbon receptor in LLPC, reinforcing CD28 expression and survival signaling.	Kynurenine	0-10	CD28 molecule	Homo sapiens	105-109
34944003-6	2021	Kynurenine (Kyn), formylindolo(3,4-b) carbazole (FICZ), and benzopyrene (BaP), which are AhR agonists, inhibited osteoclast formation and Kyn suppressed osteoclast differentiation at an early stage.	Kynurenine	0-10	aryl hydrocarbon receptor	Homo sapiens	89-92
34944003-7	2021	Furthermore, blockade of AhR signaling through CH223191, an AhR antagonist, and knockdown of AhR expression reversed Kyn-induced inhibition of osteoclast differentiation.	Kynurenine	117-120	aryl hydrocarbon receptor	Homo sapiens	25-28
34944003-7	2021	Furthermore, blockade of AhR signaling through CH223191, an AhR antagonist, and knockdown of AhR expression reversed Kyn-induced inhibition of osteoclast differentiation.	Kynurenine	117-120	aryl hydrocarbon receptor	Homo sapiens	93-96
34847455-7	2022	We found an association of immune/inflammatory markers with Kyn/Trp ratio selectively in BD patients: IL-1beta and TNF-alpha showed a positive relationship and IL-2 and IL-9 a negative relationship; in addition, higher IL-4 correlated with lower Kyn levels; higher Kyn/Trp ratio and IL-1beta correlated with lower FA in the CC and IFO.	Kynurenine	60-63	interleukin 1 alpha	Homo sapiens	102-110
34520819-1	2021	Indoleamine 2,3-dioxygenase 1 (IDO1) catalyzing the conversion of tryptophan (Trp) to kynurenine (Kyn) in kynurenine pathway (KP) is involved in the immunosuppression in pancreatic cancer (PC), but the value of IDO1 as an independent prognostic marker for PC is uncertain.	Kynurenine	86-96	indoleamine 2,3-dioxygenase 1	Mus musculus	0-29
34520819-1	2021	Indoleamine 2,3-dioxygenase 1 (IDO1) catalyzing the conversion of tryptophan (Trp) to kynurenine (Kyn) in kynurenine pathway (KP) is involved in the immunosuppression in pancreatic cancer (PC), but the value of IDO1 as an independent prognostic marker for PC is uncertain.	Kynurenine	86-96	indoleamine 2,3-dioxygenase 1	Mus musculus	31-35
34520819-1	2021	Indoleamine 2,3-dioxygenase 1 (IDO1) catalyzing the conversion of tryptophan (Trp) to kynurenine (Kyn) in kynurenine pathway (KP) is involved in the immunosuppression in pancreatic cancer (PC), but the value of IDO1 as an independent prognostic marker for PC is uncertain.	Kynurenine	86-96	pyruvate carboxylase	Mus musculus	189-191
34520819-1	2021	Indoleamine 2,3-dioxygenase 1 (IDO1) catalyzing the conversion of tryptophan (Trp) to kynurenine (Kyn) in kynurenine pathway (KP) is involved in the immunosuppression in pancreatic cancer (PC), but the value of IDO1 as an independent prognostic marker for PC is uncertain.	Kynurenine	106-116	indoleamine 2,3-dioxygenase 1	Mus musculus	0-29
34520819-1	2021	Indoleamine 2,3-dioxygenase 1 (IDO1) catalyzing the conversion of tryptophan (Trp) to kynurenine (Kyn) in kynurenine pathway (KP) is involved in the immunosuppression in pancreatic cancer (PC), but the value of IDO1 as an independent prognostic marker for PC is uncertain.	Kynurenine	106-116	indoleamine 2,3-dioxygenase 1	Mus musculus	31-35
34520819-1	2021	Indoleamine 2,3-dioxygenase 1 (IDO1) catalyzing the conversion of tryptophan (Trp) to kynurenine (Kyn) in kynurenine pathway (KP) is involved in the immunosuppression in pancreatic cancer (PC), but the value of IDO1 as an independent prognostic marker for PC is uncertain.	Kynurenine	106-116	pyruvate carboxylase	Mus musculus	189-191
34529208-1	2021	Tryptophan 2,3-dioxygenase (TDO2) was an initial rate-limiting enzyme of the kynurenine (Kyn) pathway in tryptophan (Trp) metabolism.	Kynurenine	77-87	tryptophan 2,3-dioxygenase	Mus musculus	0-26
34529208-1	2021	Tryptophan 2,3-dioxygenase (TDO2) was an initial rate-limiting enzyme of the kynurenine (Kyn) pathway in tryptophan (Trp) metabolism.	Kynurenine	77-87	tryptophan 2,3-dioxygenase	Mus musculus	28-32
34529208-1	2021	Tryptophan 2,3-dioxygenase (TDO2) was an initial rate-limiting enzyme of the kynurenine (Kyn) pathway in tryptophan (Trp) metabolism.	Kynurenine	89-92	tryptophan 2,3-dioxygenase	Mus musculus	0-26
34529208-1	2021	Tryptophan 2,3-dioxygenase (TDO2) was an initial rate-limiting enzyme of the kynurenine (Kyn) pathway in tryptophan (Trp) metabolism.	Kynurenine	89-92	tryptophan 2,3-dioxygenase	Mus musculus	28-32
34847455-7	2022	We found an association of immune/inflammatory markers with Kyn/Trp ratio selectively in BD patients: IL-1beta and TNF-alpha showed a positive relationship and IL-2 and IL-9 a negative relationship; in addition, higher IL-4 correlated with lower Kyn levels; higher Kyn/Trp ratio and IL-1beta correlated with lower FA in the CC and IFO.	Kynurenine	60-63	tumor necrosis factor	Homo sapiens	115-124
34847455-7	2022	We found an association of immune/inflammatory markers with Kyn/Trp ratio selectively in BD patients: IL-1beta and TNF-alpha showed a positive relationship and IL-2 and IL-9 a negative relationship; in addition, higher IL-4 correlated with lower Kyn levels; higher Kyn/Trp ratio and IL-1beta correlated with lower FA in the CC and IFO.	Kynurenine	60-63	interleukin 2	Homo sapiens	160-164
34847455-7	2022	We found an association of immune/inflammatory markers with Kyn/Trp ratio selectively in BD patients: IL-1beta and TNF-alpha showed a positive relationship and IL-2 and IL-9 a negative relationship; in addition, higher IL-4 correlated with lower Kyn levels; higher Kyn/Trp ratio and IL-1beta correlated with lower FA in the CC and IFO.	Kynurenine	60-63	interleukin 9	Homo sapiens	169-173
34847455-7	2022	We found an association of immune/inflammatory markers with Kyn/Trp ratio selectively in BD patients: IL-1beta and TNF-alpha showed a positive relationship and IL-2 and IL-9 a negative relationship; in addition, higher IL-4 correlated with lower Kyn levels; higher Kyn/Trp ratio and IL-1beta correlated with lower FA in the CC and IFO.	Kynurenine	60-63	interleukin 4	Homo sapiens	219-223
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.	Kynurenine	145-157	indoleamine 2,3-dioxygenase 1	Homo sapiens	66-69
34559190-7	2021	In contrast, NK cells expanded in the presence of the AHR agonist, kynurenine, showed decreased cytotoxicity and altered expression of 97 genes including those strongly associated with oxidative stress and cellular metabolism.	Kynurenine	67-77	aryl hydrocarbon receptor	Homo sapiens	54-57
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.	Kynurenine	159-164	indoleamine 2,3-dioxygenase 1	Homo sapiens	66-69
34869457-1	2021	Indoleamine 2,3-dioxygenase (IDO) is one of the initial rate-limiting enzymes of the kynurenine pathway (KP), which causes immune suppression and induction of T cell anergy.	Kynurenine	85-95	indoleamine 2,3-dioxygenase 1	Homo sapiens	0-27
34829952-7	2021	Changes in kynurenine and 3-hydroxykynurenine were associated with increased kynurenic acid/kynurenine and 3-hydroxykynurenine/kynurenine ratios, indirect measures of kynurenine aminotransferases and kynurenine 3-monooxygenase enzymatic activities, respectively.	Kynurenine	11-21	kynurenine 3-monooxygenase	Homo sapiens	200-226
34869457-1	2021	Indoleamine 2,3-dioxygenase (IDO) is one of the initial rate-limiting enzymes of the kynurenine pathway (KP), which causes immune suppression and induction of T cell anergy.	Kynurenine	85-95	indoleamine 2,3-dioxygenase 1	Homo sapiens	29-32
34775574-0	2022	The effect of 2-amino-3-carboxymuconate-6-semialdehyde decarboxylase gene overexpression in the kynurenine pathway on the expression levels of indoleamine 2,3-dioxygenase 1 and interferon-gamma in inflammatory conditions: an in vitro study.	Kynurenine	96-106	amino carboxymuconate semialdehyde decarboxylase	Mus musculus	14-68
34748328-7	2021	Importantly, tryptophan maintains kynurenine homeostasis through the activation of CaSR during the inflammatory response.	Kynurenine	34-44	calcium sensing receptor	Homo sapiens	83-87
34775574-0	2022	The effect of 2-amino-3-carboxymuconate-6-semialdehyde decarboxylase gene overexpression in the kynurenine pathway on the expression levels of indoleamine 2,3-dioxygenase 1 and interferon-gamma in inflammatory conditions: an in vitro study.	Kynurenine	96-106	indoleamine 2,3-dioxygenase 1	Mus musculus	143-172
34775574-0	2022	The effect of 2-amino-3-carboxymuconate-6-semialdehyde decarboxylase gene overexpression in the kynurenine pathway on the expression levels of indoleamine 2,3-dioxygenase 1 and interferon-gamma in inflammatory conditions: an in vitro study.	Kynurenine	96-106	interferon gamma	Mus musculus	177-193
34735466-1	2021	Indoleamine 2,3-dioxygenase 1 (IDO-1) is an immunosuppressive enzyme expressed in the placenta, neoplastic cells, and macrophages to reject T cells by converting tryptophan into kynurenine.	Kynurenine	178-188	indoleamine 2,3-dioxygenase 1	Mus musculus	0-29
34819875-1	2021	Indoleamine-2,3-dioxygenase (IDO) is the "rate-limiting" enzyme in the kynurenine (Kyn) pathway of the tryptophan (Trp) catabolism.	Kynurenine	71-81	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.	Kynurenine	71-81	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.	Kynurenine	83-86	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.	Kynurenine	83-86	indoleamine 2,3-dioxygenase 1	Homo sapiens	29-32
34676771-1	2021	Recently, two new mechanistic proposals for the kynurenine 3-monooxygenase (KMO) catalyzed hydroxylation reaction of l-Kynurenine (l-Kyn) have been proposed.	Kynurenine	117-129	kynurenine 3-monooxygenase	Homo sapiens	48-74
34676771-1	2021	Recently, two new mechanistic proposals for the kynurenine 3-monooxygenase (KMO) catalyzed hydroxylation reaction of l-Kynurenine (l-Kyn) have been proposed.	Kynurenine	117-129	kynurenine 3-monooxygenase	Homo sapiens	76-79
34676771-1	2021	Recently, two new mechanistic proposals for the kynurenine 3-monooxygenase (KMO) catalyzed hydroxylation reaction of l-Kynurenine (l-Kyn) have been proposed.	Kynurenine	131-136	kynurenine 3-monooxygenase	Homo sapiens	48-74
34676771-1	2021	Recently, two new mechanistic proposals for the kynurenine 3-monooxygenase (KMO) catalyzed hydroxylation reaction of l-Kynurenine (l-Kyn) have been proposed.	Kynurenine	131-136	kynurenine 3-monooxygenase	Homo sapiens	76-79
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.	Kynurenine	73-83	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.	Kynurenine	73-83	indoleamine 2,3-dioxygenase 1	Homo sapiens	56-61
34735466-1	2021	Indoleamine 2,3-dioxygenase 1 (IDO-1) is an immunosuppressive enzyme expressed in the placenta, neoplastic cells, and macrophages to reject T cells by converting tryptophan into kynurenine.	Kynurenine	178-188	indoleamine 2,3-dioxygenase 1	Mus musculus	31-36
34716244-2	2021	Urem ic solutes such as indoxyl sulfate (IS) and kynurenine (Kyn) mediate prothrombotic effect through tissue factor (TF).	Kynurenine	49-59	coagulation factor III	Mus musculus	103-116
34716244-2	2021	Urem ic solutes such as indoxyl sulfate (IS) and kynurenine (Kyn) mediate prothrombotic effect through tissue factor (TF).	Kynurenine	49-59	coagulation factor III	Mus musculus	118-120
34716244-2	2021	Urem ic solutes such as indoxyl sulfate (IS) and kynurenine (Kyn) mediate prothrombotic effect through tissue factor (TF).	Kynurenine	61-64	coagulation factor III	Mus musculus	103-116
34716244-2	2021	Urem ic solutes such as indoxyl sulfate (IS) and kynurenine (Kyn) mediate prothrombotic effect through tissue factor (TF).	Kynurenine	61-64	coagulation factor III	Mus musculus	118-120
34716244-4	2021	We examined the role of indoleamine 2,3-dioxygenase-1 (IDO-1), a rate-limiting enzyme of kynurenine biogenesis, in CKD-associated thrombosis after vascular injury.	Kynurenine	89-99	indoleamine 2,3-dioxygenase 1	Mus musculus	24-53
34716244-4	2021	We examined the role of indoleamine 2,3-dioxygenase-1 (IDO-1), a rate-limiting enzyme of kynurenine biogenesis, in CKD-associated thrombosis after vascular injury.	Kynurenine	89-99	indoleamine 2,3-dioxygenase 1	Mus musculus	55-60
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.	Kynurenine	4-14	indoleamine 2,3-dioxygenase 1	Homo sapiens	88-117
34601221-9	2021	Additionally, inhibition of cPLA2 overexpression by albiflorin corrects abnormal kynurenine pathway of tryptophan metabolism via the cPLA2-protein kinase B (Akt1)-indoleamine 2,3-dioxygenase 1(IDO1) regulatory loop and directs tryptophan catabolism towards more hippocampal serotonin biosynthesis.	Kynurenine	81-91	phospholipase A2, group IVA (cytosolic, calcium-dependent)	Mus musculus	28-33
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.	Kynurenine	4-14	indoleamine 2,3-dioxygenase 1	Homo sapiens	119-123
34657635-9	2021	TDO2 expression in tumor cells accounted for the release of kynurenine (Kyn), which activated aryl hydrocarbon receptor (AhR) to promote liver cancer cells proliferation.	Kynurenine	60-70	tryptophan 2,3-dioxygenase	Homo sapiens	0-4
34769098-8	2021	In functional assays, proliferation and motility-related functions of HCC cells were compromised upon suppression of IDO1, which may partially be rescued by its enzymatic product, kynurenine (KYN), while normal hepatocytes were not affected.	Kynurenine	180-190	indoleamine 2,3-dioxygenase 1	Homo sapiens	117-121
34769098-8	2021	In functional assays, proliferation and motility-related functions of HCC cells were compromised upon suppression of IDO1, which may partially be rescued by its enzymatic product, kynurenine (KYN), while normal hepatocytes were not affected.	Kynurenine	192-195	indoleamine 2,3-dioxygenase 1	Homo sapiens	117-121
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).	Kynurenine	52-62	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).	Kynurenine	52-62	indoleamine 2,3-dioxygenase 1	Homo sapiens	123-126
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).	Kynurenine	52-62	TNF alpha induced protein 6	Homo sapiens	155-176
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).	Kynurenine	52-62	TNF alpha induced protein 6	Homo sapiens	178-182
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).	Kynurenine	52-62	aryl hydrocarbon receptor	Homo sapiens	214-239
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).	Kynurenine	52-62	aryl hydrocarbon receptor	Homo sapiens	241-244
34657603-10	2021	Mechanistically, we demonstrated that Trp metabolite kynurenine (Kyn) promoted the upregulation and nuclear translocation of transcription factor aryl hydrocarbon receptor (AhR).	Kynurenine	53-63	aryl hydrocarbon receptor	Homo sapiens	146-171
34657603-10	2021	Mechanistically, we demonstrated that Trp metabolite kynurenine (Kyn) promoted the upregulation and nuclear translocation of transcription factor aryl hydrocarbon receptor (AhR).	Kynurenine	53-63	aryl hydrocarbon receptor	Homo sapiens	173-176
34657603-10	2021	Mechanistically, we demonstrated that Trp metabolite kynurenine (Kyn) promoted the upregulation and nuclear translocation of transcription factor aryl hydrocarbon receptor (AhR).	Kynurenine	65-68	aryl hydrocarbon receptor	Homo sapiens	146-171
34657603-10	2021	Mechanistically, we demonstrated that Trp metabolite kynurenine (Kyn) promoted the upregulation and nuclear translocation of transcription factor aryl hydrocarbon receptor (AhR).	Kynurenine	65-68	aryl hydrocarbon receptor	Homo sapiens	173-176
34687129-6	2021	Kyn functions as an oncometabolite in cancer cells by promoting the activity of the transcription factor aryl hydrocarbon receptor (AHR), which regulates pro-growth genes.	Kynurenine	0-3	aryl hydrocarbon receptor	Homo sapiens	105-130
34687129-6	2021	Kyn functions as an oncometabolite in cancer cells by promoting the activity of the transcription factor aryl hydrocarbon receptor (AHR), which regulates pro-growth genes.	Kynurenine	0-3	aryl hydrocarbon receptor	Homo sapiens	132-135
34657603-14	2021	CONCLUSION: Our study demonstrates that elevated TOD2 expression promoted Trp metabolism and metabolite Kyn production, thus resulting in the activation of AhR/c-Myc/ABC-SLC transporters signaling pathway.	Kynurenine	104-107	aryl hydrocarbon receptor	Homo sapiens	156-159
34657635-9	2021	TDO2 expression in tumor cells accounted for the release of kynurenine (Kyn), which activated aryl hydrocarbon receptor (AhR) to promote liver cancer cells proliferation.	Kynurenine	60-70	aryl hydrocarbon receptor	Homo sapiens	94-119
34657603-14	2021	CONCLUSION: Our study demonstrates that elevated TOD2 expression promoted Trp metabolism and metabolite Kyn production, thus resulting in the activation of AhR/c-Myc/ABC-SLC transporters signaling pathway.	Kynurenine	104-107	MYC proto-oncogene, bHLH transcription factor	Homo sapiens	160-165
34657635-9	2021	TDO2 expression in tumor cells accounted for the release of kynurenine (Kyn), which activated aryl hydrocarbon receptor (AhR) to promote liver cancer cells proliferation.	Kynurenine	60-70	aryl hydrocarbon receptor	Homo sapiens	121-124
34657635-9	2021	TDO2 expression in tumor cells accounted for the release of kynurenine (Kyn), which activated aryl hydrocarbon receptor (AhR) to promote liver cancer cells proliferation.	Kynurenine	72-75	tryptophan 2,3-dioxygenase	Homo sapiens	0-4
34657603-14	2021	CONCLUSION: Our study demonstrates that elevated TOD2 expression promoted Trp metabolism and metabolite Kyn production, thus resulting in the activation of AhR/c-Myc/ABC-SLC transporters signaling pathway.	Kynurenine	104-107	ATP binding cassette subfamily B member 6 (Langereis blood group)	Homo sapiens	166-169
34657635-9	2021	TDO2 expression in tumor cells accounted for the release of kynurenine (Kyn), which activated aryl hydrocarbon receptor (AhR) to promote liver cancer cells proliferation.	Kynurenine	72-75	aryl hydrocarbon receptor	Homo sapiens	94-119
34657635-9	2021	TDO2 expression in tumor cells accounted for the release of kynurenine (Kyn), which activated aryl hydrocarbon receptor (AhR) to promote liver cancer cells proliferation.	Kynurenine	72-75	aryl hydrocarbon receptor	Homo sapiens	121-124
34720020-2	2021	TDO is a key enzyme of tryptophan metabolism at the entry of the kynurenine pathway (KP) which moderates production of neuroactive compounds primarily outside the central nervous system (CNS).	Kynurenine	65-75	tryptophan 2,3-dioxygenase	Homo sapiens	0-3
34252442-1	2021	Kynurenine Pathway (KP) is the dominant metabolic route of tryptophan which is catalyzed by indoleamine-2,3-dioxygenase (IDO).	Kynurenine	0-10	indoleamine 2,3-dioxygenase 1	Rattus norvegicus	92-119
34252442-1	2021	Kynurenine Pathway (KP) is the dominant metabolic route of tryptophan which is catalyzed by indoleamine-2,3-dioxygenase (IDO).	Kynurenine	0-10	indoleamine 2,3-dioxygenase 1	Rattus norvegicus	121-124