PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
30104401-3	2018	Using data from The Cancer Genome Atlas (TCGA), we analysed the expression levels of xanthine dehydrogenase (XDH) and adenine phosphoribosyltransferase (APRT), two key enzymes in UA production and the purine salvage pathway, respectively.	Uric Acid	179-181	xanthine dehydrogenase	Homo sapiens	85-107
29906649-1	2018	Xanthine oxidoreductase plays an important role in formation of uric acid and its regulation during purine catabolism.	Uric Acid	64-73	xanthine dehydrogenase	Homo sapiens	0-23
29906649-1	2018	Xanthine oxidoreductase plays an important role in formation of uric acid and its regulation during purine catabolism.	purine	100-106	xanthine dehydrogenase	Homo sapiens	0-23
30196191-0	2018	Putting xanthine oxidoreductase and aldehyde oxidase on the NO metabolism map: Nitrite reduction by molybdoenzymes.	Nitrites	79-86	xanthine dehydrogenase	Homo sapiens	8-31
30068899-0	2018	Unexpected high plasma xanthine oxidoreductase activity in female subjects with low levels of uric acid.	Uric Acid	94-103	xanthine dehydrogenase	Homo sapiens	23-46
30068899-2	2018	Xanthine oxidoreductase (XOR) is an enzyme that catalyzes the formation of uric acid from hypoxanthine and xanthine, leading to an increase in superoxide and reactive oxygen species.	Uric Acid	75-84	xanthine dehydrogenase	Homo sapiens	0-23
30068899-2	2018	Xanthine oxidoreductase (XOR) is an enzyme that catalyzes the formation of uric acid from hypoxanthine and xanthine, leading to an increase in superoxide and reactive oxygen species.	Uric Acid	75-84	xanthine dehydrogenase	Homo sapiens	25-28
30068899-2	2018	Xanthine oxidoreductase (XOR) is an enzyme that catalyzes the formation of uric acid from hypoxanthine and xanthine, leading to an increase in superoxide and reactive oxygen species.	Hypoxanthine	90-102	xanthine dehydrogenase	Homo sapiens	0-23
30068899-2	2018	Xanthine oxidoreductase (XOR) is an enzyme that catalyzes the formation of uric acid from hypoxanthine and xanthine, leading to an increase in superoxide and reactive oxygen species.	Hypoxanthine	90-102	xanthine dehydrogenase	Homo sapiens	25-28
30068899-2	2018	Xanthine oxidoreductase (XOR) is an enzyme that catalyzes the formation of uric acid from hypoxanthine and xanthine, leading to an increase in superoxide and reactive oxygen species.	Xanthine	94-102	xanthine dehydrogenase	Homo sapiens	0-23
30068899-2	2018	Xanthine oxidoreductase (XOR) is an enzyme that catalyzes the formation of uric acid from hypoxanthine and xanthine, leading to an increase in superoxide and reactive oxygen species.	Xanthine	94-102	xanthine dehydrogenase	Homo sapiens	25-28
30068899-2	2018	Xanthine oxidoreductase (XOR) is an enzyme that catalyzes the formation of uric acid from hypoxanthine and xanthine, leading to an increase in superoxide and reactive oxygen species.	Superoxides	143-153	xanthine dehydrogenase	Homo sapiens	0-23
30068899-2	2018	Xanthine oxidoreductase (XOR) is an enzyme that catalyzes the formation of uric acid from hypoxanthine and xanthine, leading to an increase in superoxide and reactive oxygen species.	Superoxides	143-153	xanthine dehydrogenase	Homo sapiens	25-28
30068899-2	2018	Xanthine oxidoreductase (XOR) is an enzyme that catalyzes the formation of uric acid from hypoxanthine and xanthine, leading to an increase in superoxide and reactive oxygen species.	Reactive Oxygen Species	158-181	xanthine dehydrogenase	Homo sapiens	0-23
30068899-2	2018	Xanthine oxidoreductase (XOR) is an enzyme that catalyzes the formation of uric acid from hypoxanthine and xanthine, leading to an increase in superoxide and reactive oxygen species.	Reactive Oxygen Species	158-181	xanthine dehydrogenase	Homo sapiens	25-28
30068899-4	2018	We measured plasma XOR activity by a sensitive and accurate assay using a combination of liquid chromatography and triple quadrupole mass spectrometry in subjects with relatively low levels of uric acid (<=4.0 mg/dL) who were recruited from 627 subjects (male/female: 292/335) in the Tanno-Sobetsu Study, a population-based cohort.	Uric Acid	193-202	xanthine dehydrogenase	Homo sapiens	19-22
30068899-7	2018	In 12 (17.9%) of the 67 female subjects with uric acid <=4.0 mg/dL, plasma XOR activities were above the upper quartile value of the 335 female subjects.	Uric Acid	45-54	xanthine dehydrogenase	Homo sapiens	78-81
30068899-9	2018	In conclusion, unexpected high plasma XOR activities were found in some female subjects with relatively low levels of uric acid.	Uric Acid	118-127	xanthine dehydrogenase	Homo sapiens	38-41
30104401-3	2018	Using data from The Cancer Genome Atlas (TCGA), we analysed the expression levels of xanthine dehydrogenase (XDH) and adenine phosphoribosyltransferase (APRT), two key enzymes in UA production and the purine salvage pathway, respectively.	Uric Acid	179-181	xanthine dehydrogenase	Homo sapiens	109-112
30104401-3	2018	Using data from The Cancer Genome Atlas (TCGA), we analysed the expression levels of xanthine dehydrogenase (XDH) and adenine phosphoribosyltransferase (APRT), two key enzymes in UA production and the purine salvage pathway, respectively.	purine	201-207	xanthine dehydrogenase	Homo sapiens	85-107
30104401-3	2018	Using data from The Cancer Genome Atlas (TCGA), we analysed the expression levels of xanthine dehydrogenase (XDH) and adenine phosphoribosyltransferase (APRT), two key enzymes in UA production and the purine salvage pathway, respectively.	purine	201-207	xanthine dehydrogenase	Homo sapiens	109-112
29657221-6	2018	Our patient improved with liberal fluid intake, restriction of high adenine content foods, and oral xanthine dehydrogenase inhibitor febuxostat.	Febuxostat	133-143	xanthine dehydrogenase	Homo sapiens	100-122
29733945-1	2018	Xanthine oxidoreductase (XOR) could contribute to the pathogenesis of metabolic syndrome through the oxidative stress and the inflammatory response induced by XOR-derived reactive oxygen species and uric acid.	Reactive Oxygen Species	171-194	xanthine dehydrogenase	Homo sapiens	0-23
29733945-1	2018	Xanthine oxidoreductase (XOR) could contribute to the pathogenesis of metabolic syndrome through the oxidative stress and the inflammatory response induced by XOR-derived reactive oxygen species and uric acid.	Reactive Oxygen Species	171-194	xanthine dehydrogenase	Homo sapiens	25-28
29733945-1	2018	Xanthine oxidoreductase (XOR) could contribute to the pathogenesis of metabolic syndrome through the oxidative stress and the inflammatory response induced by XOR-derived reactive oxygen species and uric acid.	Reactive Oxygen Species	171-194	xanthine dehydrogenase	Homo sapiens	159-162
29733945-1	2018	Xanthine oxidoreductase (XOR) could contribute to the pathogenesis of metabolic syndrome through the oxidative stress and the inflammatory response induced by XOR-derived reactive oxygen species and uric acid.	Uric Acid	199-208	xanthine dehydrogenase	Homo sapiens	0-23
29733945-1	2018	Xanthine oxidoreductase (XOR) could contribute to the pathogenesis of metabolic syndrome through the oxidative stress and the inflammatory response induced by XOR-derived reactive oxygen species and uric acid.	Uric Acid	199-208	xanthine dehydrogenase	Homo sapiens	25-28
29733945-3	2018	The serum level of XOR is correlated to triglyceride/high density lipoprotein cholesterol ratio, fasting glycemia, fasting insulinemia and insulin resistance index.	Triglycerides	40-52	xanthine dehydrogenase	Homo sapiens	19-22
29372470-2	2018	We attempted to examine the uric acid-lowering effect and the renoprotective effect of topiroxostat, a selective xanthine oxidoreductase inhibitor, in patients with diabetic nephropathy and hyperuricemia in this pilot study.	FYX-051	87-99	xanthine dehydrogenase	Homo sapiens	113-136
29946611-8	2018	This observed hydroxylation reactivity is consistent with the postulated first step of Mo-Cu CODH (nucleophilic attack of the Mo(vi)-oxo on the Cu(i)-bound electrophilic CO) and xanthine oxidoreductase (nucleophilic attack of Mo(vi)-oxo on the electrophilic xanthine carbon).	Carbon	267-273	xanthine dehydrogenase	Homo sapiens	178-201
31458937-4	2018	Compound LH exhibited OR and XOR logic gate behavior with H+, Fe2+, and Cu2+ as inputs.	Luteinizing Hormone	9-11	xanthine dehydrogenase	Homo sapiens	29-32
29643318-1	2018	BACKGROUND: Xanthine oxidoreductase (XOR) is an enzyme that catalyzes the formation of uric acid from hypoxanthine and xanthine, leading to an increase in superoxide and reactive oxygen species.	Uric Acid	87-96	xanthine dehydrogenase	Homo sapiens	12-35
29643318-1	2018	BACKGROUND: Xanthine oxidoreductase (XOR) is an enzyme that catalyzes the formation of uric acid from hypoxanthine and xanthine, leading to an increase in superoxide and reactive oxygen species.	Uric Acid	87-96	xanthine dehydrogenase	Homo sapiens	37-40
29643318-1	2018	BACKGROUND: Xanthine oxidoreductase (XOR) is an enzyme that catalyzes the formation of uric acid from hypoxanthine and xanthine, leading to an increase in superoxide and reactive oxygen species.	Hypoxanthine	102-114	xanthine dehydrogenase	Homo sapiens	12-35
29643318-1	2018	BACKGROUND: Xanthine oxidoreductase (XOR) is an enzyme that catalyzes the formation of uric acid from hypoxanthine and xanthine, leading to an increase in superoxide and reactive oxygen species.	Hypoxanthine	102-114	xanthine dehydrogenase	Homo sapiens	37-40
29643318-1	2018	BACKGROUND: Xanthine oxidoreductase (XOR) is an enzyme that catalyzes the formation of uric acid from hypoxanthine and xanthine, leading to an increase in superoxide and reactive oxygen species.	Xanthine	106-114	xanthine dehydrogenase	Homo sapiens	12-35
29643318-1	2018	BACKGROUND: Xanthine oxidoreductase (XOR) is an enzyme that catalyzes the formation of uric acid from hypoxanthine and xanthine, leading to an increase in superoxide and reactive oxygen species.	Xanthine	106-114	xanthine dehydrogenase	Homo sapiens	37-40
29643318-1	2018	BACKGROUND: Xanthine oxidoreductase (XOR) is an enzyme that catalyzes the formation of uric acid from hypoxanthine and xanthine, leading to an increase in superoxide and reactive oxygen species.	Superoxides	155-165	xanthine dehydrogenase	Homo sapiens	12-35
29643318-1	2018	BACKGROUND: Xanthine oxidoreductase (XOR) is an enzyme that catalyzes the formation of uric acid from hypoxanthine and xanthine, leading to an increase in superoxide and reactive oxygen species.	Superoxides	155-165	xanthine dehydrogenase	Homo sapiens	37-40
29643318-1	2018	BACKGROUND: Xanthine oxidoreductase (XOR) is an enzyme that catalyzes the formation of uric acid from hypoxanthine and xanthine, leading to an increase in superoxide and reactive oxygen species.	Reactive Oxygen Species	170-193	xanthine dehydrogenase	Homo sapiens	12-35
29643318-1	2018	BACKGROUND: Xanthine oxidoreductase (XOR) is an enzyme that catalyzes the formation of uric acid from hypoxanthine and xanthine, leading to an increase in superoxide and reactive oxygen species.	Reactive Oxygen Species	170-193	xanthine dehydrogenase	Homo sapiens	37-40
29643318-3	2018	We investigated the associations between metabolic parameters and plasma XOR activity measured by a sensitive and accurate assay using a combination of liquid chromatography and triple quadrupole mass spectrometry to detect [13C2,15N2]-uric acid using [13C2,15N2]-xanthine as a substrate.Methods and Results:A total of 627 Japanese subjects (M/F, 292/335) from the Tanno-Sobetsu Study, a population-based cohort, were recruited.	[13c2,15n2]	224-235	xanthine dehydrogenase	Homo sapiens	73-76
29643318-3	2018	We investigated the associations between metabolic parameters and plasma XOR activity measured by a sensitive and accurate assay using a combination of liquid chromatography and triple quadrupole mass spectrometry to detect [13C2,15N2]-uric acid using [13C2,15N2]-xanthine as a substrate.Methods and Results:A total of 627 Japanese subjects (M/F, 292/335) from the Tanno-Sobetsu Study, a population-based cohort, were recruited.	Uric Acid	236-245	xanthine dehydrogenase	Homo sapiens	73-76
29643318-3	2018	We investigated the associations between metabolic parameters and plasma XOR activity measured by a sensitive and accurate assay using a combination of liquid chromatography and triple quadrupole mass spectrometry to detect [13C2,15N2]-uric acid using [13C2,15N2]-xanthine as a substrate.Methods and Results:A total of 627 Japanese subjects (M/F, 292/335) from the Tanno-Sobetsu Study, a population-based cohort, were recruited.	[13c2,15n2]-	224-236	xanthine dehydrogenase	Homo sapiens	73-76
29643318-3	2018	We investigated the associations between metabolic parameters and plasma XOR activity measured by a sensitive and accurate assay using a combination of liquid chromatography and triple quadrupole mass spectrometry to detect [13C2,15N2]-uric acid using [13C2,15N2]-xanthine as a substrate.Methods and Results:A total of 627 Japanese subjects (M/F, 292/335) from the Tanno-Sobetsu Study, a population-based cohort, were recruited.	Xanthine	264-272	xanthine dehydrogenase	Homo sapiens	73-76
29643318-6	2018	On stepwise and multivariate regression analyses, BMI, smoking and levels of alanine transaminase, uric acid, triglycerides and HOMA-R were independent predictors of plasma XOR activity after adjustment for age and gender.	Uric Acid	99-108	xanthine dehydrogenase	Homo sapiens	173-176
29643318-6	2018	On stepwise and multivariate regression analyses, BMI, smoking and levels of alanine transaminase, uric acid, triglycerides and HOMA-R were independent predictors of plasma XOR activity after adjustment for age and gender.	Triglycerides	110-123	xanthine dehydrogenase	Homo sapiens	173-176
29931553-1	2018	PURPOSE OF REVIEW: To review the extent of treatment success or failure with the xanthine oxidoreductase inhibitors allopurinol and febuxostat and indicate how the dosage of urate-lowering therapy (ULT) may be modified to increase the response in the majority of patients with gout.	Allopurinol	116-127	xanthine dehydrogenase	Homo sapiens	81-104
29931553-1	2018	PURPOSE OF REVIEW: To review the extent of treatment success or failure with the xanthine oxidoreductase inhibitors allopurinol and febuxostat and indicate how the dosage of urate-lowering therapy (ULT) may be modified to increase the response in the majority of patients with gout.	Febuxostat	132-142	xanthine dehydrogenase	Homo sapiens	81-104
29644146-6	2018	Recent Advances and Critical Issues: Xanthine oxidoreductase (XOR), a molybdoflavin enzyme, is emerging as an important source of reactive oxygen species (ROS) in various pathologies, including diabetes and chronic wounds.	molybdoflavin	70-83	xanthine dehydrogenase	Homo sapiens	37-60
29644146-6	2018	Recent Advances and Critical Issues: Xanthine oxidoreductase (XOR), a molybdoflavin enzyme, is emerging as an important source of reactive oxygen species (ROS) in various pathologies, including diabetes and chronic wounds.	molybdoflavin	70-83	xanthine dehydrogenase	Homo sapiens	62-65
29644146-6	2018	Recent Advances and Critical Issues: Xanthine oxidoreductase (XOR), a molybdoflavin enzyme, is emerging as an important source of reactive oxygen species (ROS) in various pathologies, including diabetes and chronic wounds.	Reactive Oxygen Species	130-153	xanthine dehydrogenase	Homo sapiens	37-60
29644146-6	2018	Recent Advances and Critical Issues: Xanthine oxidoreductase (XOR), a molybdoflavin enzyme, is emerging as an important source of reactive oxygen species (ROS) in various pathologies, including diabetes and chronic wounds.	Reactive Oxygen Species	130-153	xanthine dehydrogenase	Homo sapiens	62-65
29644146-6	2018	Recent Advances and Critical Issues: Xanthine oxidoreductase (XOR), a molybdoflavin enzyme, is emerging as an important source of reactive oxygen species (ROS) in various pathologies, including diabetes and chronic wounds.	Reactive Oxygen Species	155-158	xanthine dehydrogenase	Homo sapiens	37-60
29644146-6	2018	Recent Advances and Critical Issues: Xanthine oxidoreductase (XOR), a molybdoflavin enzyme, is emerging as an important source of reactive oxygen species (ROS) in various pathologies, including diabetes and chronic wounds.	Reactive Oxygen Species	155-158	xanthine dehydrogenase	Homo sapiens	62-65
29644146-7	2018	XOR has recently been shown to be upregulated in chronic wounds, stimulating the overproduction of ROS during dysfunctional wound healing.	Reactive Oxygen Species	99-102	xanthine dehydrogenase	Homo sapiens	0-3
29644146-8	2018	XOR-induced ROS can amplify and potentiate inflammation in the wound environment further delaying wound closure.	Reactive Oxygen Species	12-15	xanthine dehydrogenase	Homo sapiens	0-3
29372470-0	2018	Uric acid-lowering and renoprotective effects of topiroxostat, a selective xanthine oxidoreductase inhibitor, in patients with diabetic nephropathy and hyperuricemia: a randomized, double-blind, placebo-controlled, parallel-group study (UPWARD study).	FYX-051	49-61	xanthine dehydrogenase	Homo sapiens	75-98
29615789-8	2018	In addition, the two enzymes adenosine monophosphate deaminase-1 (AMPD1) and xanthine dehydrogenase (XDH), which are involved in purine metabolism, were identified as SRC-3 targets that may or may not be directly involved in purine synthesis.	purine	129-135	xanthine dehydrogenase	Homo sapiens	77-99
29615789-8	2018	In addition, the two enzymes adenosine monophosphate deaminase-1 (AMPD1) and xanthine dehydrogenase (XDH), which are involved in purine metabolism, were identified as SRC-3 targets that may or may not be directly involved in purine synthesis.	purine	129-135	xanthine dehydrogenase	Homo sapiens	101-104
29615789-8	2018	In addition, the two enzymes adenosine monophosphate deaminase-1 (AMPD1) and xanthine dehydrogenase (XDH), which are involved in purine metabolism, were identified as SRC-3 targets that may or may not be directly involved in purine synthesis.	purine	225-231	xanthine dehydrogenase	Homo sapiens	77-99
29615789-8	2018	In addition, the two enzymes adenosine monophosphate deaminase-1 (AMPD1) and xanthine dehydrogenase (XDH), which are involved in purine metabolism, were identified as SRC-3 targets that may or may not be directly involved in purine synthesis.	purine	225-231	xanthine dehydrogenase	Homo sapiens	101-104
29241594-3	2018	The purpose of this pilot study was to compare the effect of the xanthine oxidoreductase inhibitors allopurinol and febuxostat on urinary 2,8-dihydroxyadenine (DHA) excretion in APRT deficiency patients.	Allopurinol	100-111	xanthine dehydrogenase	Homo sapiens	65-88
29342419-3	2018	A recent genome wide association study suggested that allopurinol, a serum uric acid-lowering drug that inhibits xanthine dehydrogenase, is a potent substrate of ABCG2.	Allopurinol	54-65	xanthine dehydrogenase	Homo sapiens	113-135
29342419-3	2018	A recent genome wide association study suggested that allopurinol, a serum uric acid-lowering drug that inhibits xanthine dehydrogenase, is a potent substrate of ABCG2.	Uric Acid	75-84	xanthine dehydrogenase	Homo sapiens	113-135
29342419-5	2018	Our results show that ABCG2 transports oxypurinol, an active metabolite of allopurinol, whereas allopurinol and febuxostat, a new xanthine dehydrogenase inhibitor, are not substrates of ABCG2.	Febuxostat	112-122	xanthine dehydrogenase	Homo sapiens	130-152
29342419-7	2018	Since the half-life of oxypurinol is longer than that of allopurinol, the xanthine dehydrogenase-inhibiting effect of allopurinol mainly depends on its metabolite, oxypurinol.	Oxypurinol	23-33	xanthine dehydrogenase	Homo sapiens	74-96
29342419-7	2018	Since the half-life of oxypurinol is longer than that of allopurinol, the xanthine dehydrogenase-inhibiting effect of allopurinol mainly depends on its metabolite, oxypurinol.	Allopurinol	57-68	xanthine dehydrogenase	Homo sapiens	74-96
29342419-7	2018	Since the half-life of oxypurinol is longer than that of allopurinol, the xanthine dehydrogenase-inhibiting effect of allopurinol mainly depends on its metabolite, oxypurinol.	Allopurinol	118-129	xanthine dehydrogenase	Homo sapiens	74-96
29342419-7	2018	Since the half-life of oxypurinol is longer than that of allopurinol, the xanthine dehydrogenase-inhibiting effect of allopurinol mainly depends on its metabolite, oxypurinol.	Oxypurinol	164-174	xanthine dehydrogenase	Homo sapiens	74-96
29241594-3	2018	The purpose of this pilot study was to compare the effect of the xanthine oxidoreductase inhibitors allopurinol and febuxostat on urinary 2,8-dihydroxyadenine (DHA) excretion in APRT deficiency patients.	2,8-dihydroxyadenine	138-158	xanthine dehydrogenase	Homo sapiens	65-88
29241594-3	2018	The purpose of this pilot study was to compare the effect of the xanthine oxidoreductase inhibitors allopurinol and febuxostat on urinary 2,8-dihydroxyadenine (DHA) excretion in APRT deficiency patients.	2,8-dihydroxyadenine	160-163	xanthine dehydrogenase	Homo sapiens	65-88
28839105-0	2017	Alcohol abuse is associated with enhanced pulmonary and systemic xanthine oxidoreductase activity.	Alcohols	0-7	xanthine dehydrogenase	Homo sapiens	65-88
29723117-1	2018	Hereditary xanthinuria (type I) is caused by an inherited deficiency of the xanthine oxidorectase (XDH/XO), and is characterized by very low concentration of uric acid in blood and urine and high concentration of urinary xanthine, leading to urolithiasis.	Xanthine	76-84	xanthine dehydrogenase	Homo sapiens	99-102
29197117-4	2018	Coupled with the fact that certain thiopurine metabolites, notably 6-thioguanine nucleotide and 6-methylmercaptopurine, are associated with antiinflammatory effects and adverse effects, respectively, some investigators have examined intentionally shunting the metabolism of azathioprine toward increasing 6-thioguanine nucleotide levels by using low doses of the xanthine oxidoreductase inhibitor allopurinol to improve efficacy and decrease toxicity of azathioprine in patients with inflammatory bowel disease.	2-mercaptopyrazine	35-45	xanthine dehydrogenase	Homo sapiens	363-386
29197117-4	2018	Coupled with the fact that certain thiopurine metabolites, notably 6-thioguanine nucleotide and 6-methylmercaptopurine, are associated with antiinflammatory effects and adverse effects, respectively, some investigators have examined intentionally shunting the metabolism of azathioprine toward increasing 6-thioguanine nucleotide levels by using low doses of the xanthine oxidoreductase inhibitor allopurinol to improve efficacy and decrease toxicity of azathioprine in patients with inflammatory bowel disease.	6-thioguanylic acid	67-91	xanthine dehydrogenase	Homo sapiens	363-386
28839105-3	2017	Alcohol consumption increases activity of the enzyme xanthine oxidoreductase (XOR) that contributes to production of both reactive oxygen species (ROS) and uric acid, a damage-associated molecular pattern.	Alcohols	0-7	xanthine dehydrogenase	Homo sapiens	53-76
28839105-3	2017	Alcohol consumption increases activity of the enzyme xanthine oxidoreductase (XOR) that contributes to production of both reactive oxygen species (ROS) and uric acid, a damage-associated molecular pattern.	Alcohols	0-7	xanthine dehydrogenase	Homo sapiens	78-81
28839105-3	2017	Alcohol consumption increases activity of the enzyme xanthine oxidoreductase (XOR) that contributes to production of both reactive oxygen species (ROS) and uric acid, a damage-associated molecular pattern.	Reactive Oxygen Species	122-145	xanthine dehydrogenase	Homo sapiens	53-76
28839105-3	2017	Alcohol consumption increases activity of the enzyme xanthine oxidoreductase (XOR) that contributes to production of both reactive oxygen species (ROS) and uric acid, a damage-associated molecular pattern.	Reactive Oxygen Species	122-145	xanthine dehydrogenase	Homo sapiens	78-81
28839105-3	2017	Alcohol consumption increases activity of the enzyme xanthine oxidoreductase (XOR) that contributes to production of both reactive oxygen species (ROS) and uric acid, a damage-associated molecular pattern.	Reactive Oxygen Species	147-150	xanthine dehydrogenase	Homo sapiens	53-76
28839105-3	2017	Alcohol consumption increases activity of the enzyme xanthine oxidoreductase (XOR) that contributes to production of both reactive oxygen species (ROS) and uric acid, a damage-associated molecular pattern.	Reactive Oxygen Species	147-150	xanthine dehydrogenase	Homo sapiens	78-81
28839105-3	2017	Alcohol consumption increases activity of the enzyme xanthine oxidoreductase (XOR) that contributes to production of both reactive oxygen species (ROS) and uric acid, a damage-associated molecular pattern.	Uric Acid	156-165	xanthine dehydrogenase	Homo sapiens	53-76
28839105-3	2017	Alcohol consumption increases activity of the enzyme xanthine oxidoreductase (XOR) that contributes to production of both reactive oxygen species (ROS) and uric acid, a damage-associated molecular pattern.	Uric Acid	156-165	xanthine dehydrogenase	Homo sapiens	78-81
28839105-10	2017	Our data suggest that AUDs augment pulmonary and systemic XOR activity that may contribute to ROS and uric acid generation, promoting inflammation.	Reactive Oxygen Species	94-97	xanthine dehydrogenase	Homo sapiens	58-61
28839105-10	2017	Our data suggest that AUDs augment pulmonary and systemic XOR activity that may contribute to ROS and uric acid generation, promoting inflammation.	Uric Acid	102-111	xanthine dehydrogenase	Homo sapiens	58-61
28839105-11	2017	Further investigations will be necessary to determine if XOR inhibition can mitigate alcohol-associated pulmonary oxidative stress, diminish inflammation, and improve ARDS outcomes.	Alcohols	85-92	xanthine dehydrogenase	Homo sapiens	57-60
28945217-1	2017	Xanthine dehydrogenase (XDH), a rate-limiting enzyme involved in purine metabolism, has an essential role in inflammatory cascades.	purine	65-71	xanthine dehydrogenase	Homo sapiens	0-22
29133805-0	2017	Xanthine oxidoreductase activity is associated with serum uric acid and glycemic control in hemodialysis patients.	Uric Acid	58-67	xanthine dehydrogenase	Homo sapiens	0-23
29133805-1	2017	Xanthine oxidoreductase activity (XOR-a) plays an important role as a pivotal source of reactive oxygen species.	Reactive Oxygen Species	88-111	xanthine dehydrogenase	Homo sapiens	0-23
29133805-1	2017	Xanthine oxidoreductase activity (XOR-a) plays an important role as a pivotal source of reactive oxygen species.	Reactive Oxygen Species	88-111	xanthine dehydrogenase	Homo sapiens	34-37
29133805-3	2017	Plasma glucose and serum uric acid levels correlated significantly and positively with plasma XOR-a.	Glucose	7-14	xanthine dehydrogenase	Homo sapiens	94-97
29133805-3	2017	Plasma glucose and serum uric acid levels correlated significantly and positively with plasma XOR-a.	Uric Acid	25-34	xanthine dehydrogenase	Homo sapiens	94-97
29133805-4	2017	In multiple regression analyses, the presence of type 2 diabetes mellitus (T2DM) and plasma glucose were associated significantly, independently, and positively with plasma XOR-a.	Glucose	92-99	xanthine dehydrogenase	Homo sapiens	173-176
29133805-5	2017	While serum uric acid correlated significantly and positively with plasma XOR-a in hemodialysis patients without T2DM, plasma glucose and serum glycated albumin, a new marker of glycemic control in diabetic hemodialysis patients, correlated significantly and positively with plasma XOR-a in those with T2DM.	Uric Acid	12-21	xanthine dehydrogenase	Homo sapiens	74-77
29133805-6	2017	Multivariate analyses in those with T2DM revealed that plasma glucose and serum glycated albumin were associated significantly and independently with plasma XOR-a, and that serum uric acid was associated significantly and independently with XOR-a in those without T2DM.	Glucose	62-69	xanthine dehydrogenase	Homo sapiens	157-160
29133805-6	2017	Multivariate analyses in those with T2DM revealed that plasma glucose and serum glycated albumin were associated significantly and independently with plasma XOR-a, and that serum uric acid was associated significantly and independently with XOR-a in those without T2DM.	Uric Acid	179-188	xanthine dehydrogenase	Homo sapiens	241-244
29133805-7	2017	Our results suggested that glycemic control in hemodialysis patients may be important in regard to a decrease in ROS induced by XOR.	Reactive Oxygen Species	113-116	xanthine dehydrogenase	Homo sapiens	128-131
27447713-6	2017	Allopurinol, a xanthine dehydrogenase inhibitor, is the mainstay of treatment, supported by high fluid intake and dietary modifications.	Allopurinol	0-11	xanthine dehydrogenase	Homo sapiens	15-37
28945217-1	2017	Xanthine dehydrogenase (XDH), a rate-limiting enzyme involved in purine metabolism, has an essential role in inflammatory cascades.	purine	65-71	xanthine dehydrogenase	Homo sapiens	24-27
28797123-1	2017	BACKGROUND AND PURPOSE: Xanthine oxidoreductase (XOR), which catalyzes purine catabolism, has two interconvertible forms, xanthine dehydrogenase and xanthine oxidase, the latter of which produces superoxide during uric acid (UA) synthesis.	purine	71-77	xanthine dehydrogenase	Homo sapiens	24-47
28863172-11	2017	In HBEC-6KT, production of uric acid was sensitive to the xanthine dehydrogenase (XDH) inhibitor, allopurinol, and the ATP Binding Cassette C4 (ABCC4) inhibitor, MK-571.	Uric Acid	27-36	xanthine dehydrogenase	Homo sapiens	58-80
28863172-11	2017	In HBEC-6KT, production of uric acid was sensitive to the xanthine dehydrogenase (XDH) inhibitor, allopurinol, and the ATP Binding Cassette C4 (ABCC4) inhibitor, MK-571.	Uric Acid	27-36	xanthine dehydrogenase	Homo sapiens	82-85
28797123-1	2017	BACKGROUND AND PURPOSE: Xanthine oxidoreductase (XOR), which catalyzes purine catabolism, has two interconvertible forms, xanthine dehydrogenase and xanthine oxidase, the latter of which produces superoxide during uric acid (UA) synthesis.	purine	71-77	xanthine dehydrogenase	Homo sapiens	49-52
28797123-1	2017	BACKGROUND AND PURPOSE: Xanthine oxidoreductase (XOR), which catalyzes purine catabolism, has two interconvertible forms, xanthine dehydrogenase and xanthine oxidase, the latter of which produces superoxide during uric acid (UA) synthesis.	purine	71-77	xanthine dehydrogenase	Homo sapiens	122-144
28797123-1	2017	BACKGROUND AND PURPOSE: Xanthine oxidoreductase (XOR), which catalyzes purine catabolism, has two interconvertible forms, xanthine dehydrogenase and xanthine oxidase, the latter of which produces superoxide during uric acid (UA) synthesis.	Superoxides	196-206	xanthine dehydrogenase	Homo sapiens	24-47
28797123-1	2017	BACKGROUND AND PURPOSE: Xanthine oxidoreductase (XOR), which catalyzes purine catabolism, has two interconvertible forms, xanthine dehydrogenase and xanthine oxidase, the latter of which produces superoxide during uric acid (UA) synthesis.	Superoxides	196-206	xanthine dehydrogenase	Homo sapiens	49-52
28797123-1	2017	BACKGROUND AND PURPOSE: Xanthine oxidoreductase (XOR), which catalyzes purine catabolism, has two interconvertible forms, xanthine dehydrogenase and xanthine oxidase, the latter of which produces superoxide during uric acid (UA) synthesis.	Superoxides	196-206	xanthine dehydrogenase	Homo sapiens	122-144
28797123-1	2017	BACKGROUND AND PURPOSE: Xanthine oxidoreductase (XOR), which catalyzes purine catabolism, has two interconvertible forms, xanthine dehydrogenase and xanthine oxidase, the latter of which produces superoxide during uric acid (UA) synthesis.	Uric Acid	214-223	xanthine dehydrogenase	Homo sapiens	24-47
28797123-1	2017	BACKGROUND AND PURPOSE: Xanthine oxidoreductase (XOR), which catalyzes purine catabolism, has two interconvertible forms, xanthine dehydrogenase and xanthine oxidase, the latter of which produces superoxide during uric acid (UA) synthesis.	Uric Acid	214-223	xanthine dehydrogenase	Homo sapiens	49-52
28797123-1	2017	BACKGROUND AND PURPOSE: Xanthine oxidoreductase (XOR), which catalyzes purine catabolism, has two interconvertible forms, xanthine dehydrogenase and xanthine oxidase, the latter of which produces superoxide during uric acid (UA) synthesis.	Uric Acid	214-223	xanthine dehydrogenase	Homo sapiens	122-144
28797123-1	2017	BACKGROUND AND PURPOSE: Xanthine oxidoreductase (XOR), which catalyzes purine catabolism, has two interconvertible forms, xanthine dehydrogenase and xanthine oxidase, the latter of which produces superoxide during uric acid (UA) synthesis.	Uric Acid	225-227	xanthine dehydrogenase	Homo sapiens	24-47
28797123-1	2017	BACKGROUND AND PURPOSE: Xanthine oxidoreductase (XOR), which catalyzes purine catabolism, has two interconvertible forms, xanthine dehydrogenase and xanthine oxidase, the latter of which produces superoxide during uric acid (UA) synthesis.	Uric Acid	225-227	xanthine dehydrogenase	Homo sapiens	49-52
28797123-1	2017	BACKGROUND AND PURPOSE: Xanthine oxidoreductase (XOR), which catalyzes purine catabolism, has two interconvertible forms, xanthine dehydrogenase and xanthine oxidase, the latter of which produces superoxide during uric acid (UA) synthesis.	Uric Acid	225-227	xanthine dehydrogenase	Homo sapiens	122-144
28797123-4	2017	METHODS AND RESULTS: Plasma XOR activity was measured by [13C2,15N2]xanthine coupled with liquid chromatography/triplequadrupole mass spectrometry.	[13c2,15n2]xanthine	57-76	xanthine dehydrogenase	Homo sapiens	28-31
28797123-5	2017	Among 270 patients who were not taking UA-lowering drugs, XOR activity was associated with body mass index (BMI), alanine aminotransferase (ALT), HbA1c and renal function.	Uric Acid	39-41	xanthine dehydrogenase	Homo sapiens	58-61
28797123-6	2017	Although XOR activity was not associated with serum UA overall, patients with chronic kidney disease (CKD), those with higher XOR activity had higher serum UA among patients without CKD.	Uric Acid	156-158	xanthine dehydrogenase	Homo sapiens	126-129
28702574-5	2017	Inspired by this, these sensing systems can be utilized to design OR, XOR and INHIBIT logic gates, which would be used for the determination of dopamine, proline and ethylene blue via logic outputs.	Dopamine	144-152	xanthine dehydrogenase	Homo sapiens	70-73
28861423-3	2017	Sources of ROS are mitochondrial respiration, NADH/NADPH oxidase, xanthine oxidoreductase or the uncoupling of nitric oxide synthase (NOS) in vascular cells.	Reactive Oxygen Species	11-14	xanthine dehydrogenase	Homo sapiens	66-89
28702574-5	2017	Inspired by this, these sensing systems can be utilized to design OR, XOR and INHIBIT logic gates, which would be used for the determination of dopamine, proline and ethylene blue via logic outputs.	Proline	154-161	xanthine dehydrogenase	Homo sapiens	70-73
28702574-5	2017	Inspired by this, these sensing systems can be utilized to design OR, XOR and INHIBIT logic gates, which would be used for the determination of dopamine, proline and ethylene blue via logic outputs.	3,7-Bis(diethylamino)phenothiazin-5-ium	166-179	xanthine dehydrogenase	Homo sapiens	70-73
28590138-4	2017	Here, we use resonance Raman (rR) spectroscopy to probe Moco-protein interactions using heavy-atom congeners of lumazine, molecules that bind tightly to both wild-type xanthine dehydrogenase (wt-XDH) and its Q102G and Q197A variants following enzymatic hydroxylation to the corresponding violapterin product molecules.	lumazine	112-120	xanthine dehydrogenase	Homo sapiens	195-198
28403945-1	2017	BACKGROUND AND AIMS: The enzyme xanthine oxidoreductase (XOR) catalyzes the formation of uric acid (UA) from hypoxanthine and xanthine, which in turn are products of purine metabolism starting from ribose-5-phosphate.	Uric Acid	89-98	xanthine dehydrogenase	Homo sapiens	32-55
28403945-1	2017	BACKGROUND AND AIMS: The enzyme xanthine oxidoreductase (XOR) catalyzes the formation of uric acid (UA) from hypoxanthine and xanthine, which in turn are products of purine metabolism starting from ribose-5-phosphate.	Uric Acid	89-98	xanthine dehydrogenase	Homo sapiens	57-60
28403945-2	2017	Besides the synthesis of UA, basic research has suggested that XOR is involved in the regulation of reactive oxygen species, adipogenesis, and peroxisome proliferator-activated receptor-gamma (PPAR-gamma).	Reactive Oxygen Species	100-123	xanthine dehydrogenase	Homo sapiens	63-66
28403945-1	2017	BACKGROUND AND AIMS: The enzyme xanthine oxidoreductase (XOR) catalyzes the formation of uric acid (UA) from hypoxanthine and xanthine, which in turn are products of purine metabolism starting from ribose-5-phosphate.	Uric Acid	100-102	xanthine dehydrogenase	Homo sapiens	32-55
28403945-1	2017	BACKGROUND AND AIMS: The enzyme xanthine oxidoreductase (XOR) catalyzes the formation of uric acid (UA) from hypoxanthine and xanthine, which in turn are products of purine metabolism starting from ribose-5-phosphate.	Uric Acid	100-102	xanthine dehydrogenase	Homo sapiens	57-60
28403945-1	2017	BACKGROUND AND AIMS: The enzyme xanthine oxidoreductase (XOR) catalyzes the formation of uric acid (UA) from hypoxanthine and xanthine, which in turn are products of purine metabolism starting from ribose-5-phosphate.	Hypoxanthine	109-121	xanthine dehydrogenase	Homo sapiens	32-55
28403945-4	2017	Recently, a novel human plasma XOR activity assay has been established using a combination of liquid chromatography (LC) and triple quadrupole mass spectrometry (TQMS) to detect [13C2,15N2]UA using [13C2,15N2]xanthine as a substrate.	[13c2,15n2]xanthine	198-217	xanthine dehydrogenase	Homo sapiens	31-34
28403945-1	2017	BACKGROUND AND AIMS: The enzyme xanthine oxidoreductase (XOR) catalyzes the formation of uric acid (UA) from hypoxanthine and xanthine, which in turn are products of purine metabolism starting from ribose-5-phosphate.	Hypoxanthine	109-121	xanthine dehydrogenase	Homo sapiens	57-60
28403945-11	2017	CONCLUSIONS: The present study has shown that XOR activity is correlated with serum UA levels in humans.	Uric Acid	84-86	xanthine dehydrogenase	Homo sapiens	46-49
28403945-1	2017	BACKGROUND AND AIMS: The enzyme xanthine oxidoreductase (XOR) catalyzes the formation of uric acid (UA) from hypoxanthine and xanthine, which in turn are products of purine metabolism starting from ribose-5-phosphate.	Xanthine	32-40	xanthine dehydrogenase	Homo sapiens	57-60
28403945-1	2017	BACKGROUND AND AIMS: The enzyme xanthine oxidoreductase (XOR) catalyzes the formation of uric acid (UA) from hypoxanthine and xanthine, which in turn are products of purine metabolism starting from ribose-5-phosphate.	purine	166-172	xanthine dehydrogenase	Homo sapiens	32-55
28403945-1	2017	BACKGROUND AND AIMS: The enzyme xanthine oxidoreductase (XOR) catalyzes the formation of uric acid (UA) from hypoxanthine and xanthine, which in turn are products of purine metabolism starting from ribose-5-phosphate.	purine	166-172	xanthine dehydrogenase	Homo sapiens	57-60
28403945-1	2017	BACKGROUND AND AIMS: The enzyme xanthine oxidoreductase (XOR) catalyzes the formation of uric acid (UA) from hypoxanthine and xanthine, which in turn are products of purine metabolism starting from ribose-5-phosphate.	ribose-5-phosphate	198-216	xanthine dehydrogenase	Homo sapiens	32-55
28403945-1	2017	BACKGROUND AND AIMS: The enzyme xanthine oxidoreductase (XOR) catalyzes the formation of uric acid (UA) from hypoxanthine and xanthine, which in turn are products of purine metabolism starting from ribose-5-phosphate.	ribose-5-phosphate	198-216	xanthine dehydrogenase	Homo sapiens	57-60
28403945-2	2017	Besides the synthesis of UA, basic research has suggested that XOR is involved in the regulation of reactive oxygen species, adipogenesis, and peroxisome proliferator-activated receptor-gamma (PPAR-gamma).	Uric Acid	25-27	xanthine dehydrogenase	Homo sapiens	63-66
28389481-1	2017	OBJECTIVES: Uric acid (UA) is the product of purine or nucleotide metabolism via the pathway of xanthine oxidase or xanthine dehydrogenase.	Uric Acid	12-21	xanthine dehydrogenase	Homo sapiens	116-138
28389481-1	2017	OBJECTIVES: Uric acid (UA) is the product of purine or nucleotide metabolism via the pathway of xanthine oxidase or xanthine dehydrogenase.	Uric Acid	23-25	xanthine dehydrogenase	Homo sapiens	116-138
28389481-1	2017	OBJECTIVES: Uric acid (UA) is the product of purine or nucleotide metabolism via the pathway of xanthine oxidase or xanthine dehydrogenase.	purine	45-51	xanthine dehydrogenase	Homo sapiens	116-138
28017872-6	2017	Allopurinol (100 muM), an inhibitor of xanthine oxidoreductase, was added both alone and in combination with NaNO2 to cells exposed to hypoxia.	Allopurinol	0-11	xanthine dehydrogenase	Homo sapiens	39-62
28247173-0	2017	Effect of switching xanthine oxidoreductase inhibitor from febuxostat to topiroxostat on urinary protein excretion.	Febuxostat	59-69	xanthine dehydrogenase	Homo sapiens	20-43
28299863-5	2017	Expression analysis by cDNA microarray showed that xanthine dehydrogenase (XDH) expression was significantly lower in Li21 and tPH5CHDKK3-over-expressing cells in response to H2 O2 treatment when compared to that in their respective mock-transfected controls, whereas a marked increase was observed in H2 O2 -treated DKK3 knockdown cells.	Hydrogen Peroxide	175-180	xanthine dehydrogenase	Homo sapiens	51-73
28299863-5	2017	Expression analysis by cDNA microarray showed that xanthine dehydrogenase (XDH) expression was significantly lower in Li21 and tPH5CHDKK3-over-expressing cells in response to H2 O2 treatment when compared to that in their respective mock-transfected controls, whereas a marked increase was observed in H2 O2 -treated DKK3 knockdown cells.	Hydrogen Peroxide	175-180	xanthine dehydrogenase	Homo sapiens	75-78
28299863-5	2017	Expression analysis by cDNA microarray showed that xanthine dehydrogenase (XDH) expression was significantly lower in Li21 and tPH5CHDKK3-over-expressing cells in response to H2 O2 treatment when compared to that in their respective mock-transfected controls, whereas a marked increase was observed in H2 O2 -treated DKK3 knockdown cells.	Hydrogen Peroxide	302-307	xanthine dehydrogenase	Homo sapiens	51-73
28299863-5	2017	Expression analysis by cDNA microarray showed that xanthine dehydrogenase (XDH) expression was significantly lower in Li21 and tPH5CHDKK3-over-expressing cells in response to H2 O2 treatment when compared to that in their respective mock-transfected controls, whereas a marked increase was observed in H2 O2 -treated DKK3 knockdown cells.	Hydrogen Peroxide	302-307	xanthine dehydrogenase	Homo sapiens	75-78
28299863-6	2017	Thus, these data suggest that DKK3 promotes cell survival during oxidative stress by suppressing the expression of the superoxide-producing enzyme XDH.	Superoxides	119-129	xanthine dehydrogenase	Homo sapiens	147-150
28017872-13	2017	Treatment of cells with the xanthine oxidoreductase inhibitor allopurinol, in addition to NaNO2 attenuated the NaNO2-attributed suppression of hypoxia-mediated EV release.	Allopurinol	62-73	xanthine dehydrogenase	Homo sapiens	28-51
28017872-16	2017	Furthermore, the reduction of NO2- to NO via xanthine oxidoreductase during hypoxia appears to inhibit HIF-1alpha-mediated EV production.	Nitrogen Dioxide	30-33	xanthine dehydrogenase	Homo sapiens	45-68
27865177-2	2017	Xanthine oxidoreductase (XOR) is a rate-limiting enzyme of purine degradation that plays a key role in uric acid (UA) production with a resultant increase in reactive oxygen species.	purine	59-65	xanthine dehydrogenase	Homo sapiens	0-23
29379265-1	2017	An array of four independently wired indium tin oxide (ITO) electrodes was used for electrochemically stimulated DNA release and activation of DNA-based Identity, AND and XOR logic gates.	indium tin oxide	37-53	xanthine dehydrogenase	Homo sapiens	171-174
29379265-1	2017	An array of four independently wired indium tin oxide (ITO) electrodes was used for electrochemically stimulated DNA release and activation of DNA-based Identity, AND and XOR logic gates.	indium tin oxide	55-58	xanthine dehydrogenase	Homo sapiens	171-174
27865177-2	2017	Xanthine oxidoreductase (XOR) is a rate-limiting enzyme of purine degradation that plays a key role in uric acid (UA) production with a resultant increase in reactive oxygen species.	purine	59-65	xanthine dehydrogenase	Homo sapiens	25-28
27865177-2	2017	Xanthine oxidoreductase (XOR) is a rate-limiting enzyme of purine degradation that plays a key role in uric acid (UA) production with a resultant increase in reactive oxygen species.	Uric Acid	103-112	xanthine dehydrogenase	Homo sapiens	0-23
27865177-2	2017	Xanthine oxidoreductase (XOR) is a rate-limiting enzyme of purine degradation that plays a key role in uric acid (UA) production with a resultant increase in reactive oxygen species.	Uric Acid	103-112	xanthine dehydrogenase	Homo sapiens	25-28
27865177-2	2017	Xanthine oxidoreductase (XOR) is a rate-limiting enzyme of purine degradation that plays a key role in uric acid (UA) production with a resultant increase in reactive oxygen species.	Uric Acid	114-116	xanthine dehydrogenase	Homo sapiens	0-23
27865177-2	2017	Xanthine oxidoreductase (XOR) is a rate-limiting enzyme of purine degradation that plays a key role in uric acid (UA) production with a resultant increase in reactive oxygen species.	Uric Acid	114-116	xanthine dehydrogenase	Homo sapiens	25-28
27865177-2	2017	Xanthine oxidoreductase (XOR) is a rate-limiting enzyme of purine degradation that plays a key role in uric acid (UA) production with a resultant increase in reactive oxygen species.	Reactive Oxygen Species	158-181	xanthine dehydrogenase	Homo sapiens	0-23
27865177-2	2017	Xanthine oxidoreductase (XOR) is a rate-limiting enzyme of purine degradation that plays a key role in uric acid (UA) production with a resultant increase in reactive oxygen species.	Reactive Oxygen Species	158-181	xanthine dehydrogenase	Homo sapiens	25-28
27816314-3	2016	We developed a highly sensitive assay for XOR activity utilizing a combination of [13C2,15N2] xanthine and liquid chromatography/triple quadrupole mass spectrometry.	[13c2,15n2] xanthine	82-102	xanthine dehydrogenase	Homo sapiens	42-45
27997561-7	2016	In numerical model of BZ medium we show that functions of key flueric devices are implemented in the excitable chemical system: signal generator, and, xor, not and nor Boolean gates, delay elements, diodes and sensors.	bz medium	22-31	xanthine dehydrogenase	Homo sapiens	151-154
28413972-4	2017	The xanthine oxidoreductase (XOR) is an essential enzyme for the generation of uric acid.	Uric Acid	79-88	xanthine dehydrogenase	Homo sapiens	4-27
28413972-4	2017	The xanthine oxidoreductase (XOR) is an essential enzyme for the generation of uric acid.	Uric Acid	79-88	xanthine dehydrogenase	Homo sapiens	29-32
28413972-5	2017	A typical pharmacological therapy to reduce the uric acid amounts is inhibition of XOR.	Uric Acid	48-57	xanthine dehydrogenase	Homo sapiens	83-86
28413972-7	2017	The question arises if XOR inhibition might be an attractive target to reduce cardiovascular events in patients with high or even normal uric acid levels.	Uric Acid	137-146	xanthine dehydrogenase	Homo sapiens	23-26
27816314-5	2016	The calibration curve of [13C2,15N2]uric acid showed linearity over the range of 4-4000nM (r2>0.995) with a lower limit of quantitation of 4nM which corresponds to an XOR activity of 6.67pmol/h/mL plasma.	[13c2,15n2]uric acid	25-45	xanthine dehydrogenase	Homo sapiens	170-173
27816314-7	2016	Plasma XOR activities of 20 healthy volunteers ranged from 32.8 to 227pmol/h/mL (mean+-SD=89.1+-55.1, n=20), which correlated with alanine transaminase (r=0.827), aspartate transaminase (r=0.487), and uric acid (r=0.502).	Uric Acid	201-210	xanthine dehydrogenase	Homo sapiens	7-10
27798228-1	2016	Xanthine oxidoreductase (XOR) is the rate-limiting enzyme in purine catabolism and converts hypoxanthine to xanthine, and xanthine into uric acid.	purine	61-67	xanthine dehydrogenase	Homo sapiens	0-23
27798228-1	2016	Xanthine oxidoreductase (XOR) is the rate-limiting enzyme in purine catabolism and converts hypoxanthine to xanthine, and xanthine into uric acid.	purine	61-67	xanthine dehydrogenase	Homo sapiens	25-28
27798228-1	2016	Xanthine oxidoreductase (XOR) is the rate-limiting enzyme in purine catabolism and converts hypoxanthine to xanthine, and xanthine into uric acid.	Hypoxanthine	92-104	xanthine dehydrogenase	Homo sapiens	0-23
27798228-1	2016	Xanthine oxidoreductase (XOR) is the rate-limiting enzyme in purine catabolism and converts hypoxanthine to xanthine, and xanthine into uric acid.	Hypoxanthine	92-104	xanthine dehydrogenase	Homo sapiens	25-28
27798228-1	2016	Xanthine oxidoreductase (XOR) is the rate-limiting enzyme in purine catabolism and converts hypoxanthine to xanthine, and xanthine into uric acid.	Xanthine	96-104	xanthine dehydrogenase	Homo sapiens	0-23
27798228-1	2016	Xanthine oxidoreductase (XOR) is the rate-limiting enzyme in purine catabolism and converts hypoxanthine to xanthine, and xanthine into uric acid.	Xanthine	96-104	xanthine dehydrogenase	Homo sapiens	25-28
27798228-1	2016	Xanthine oxidoreductase (XOR) is the rate-limiting enzyme in purine catabolism and converts hypoxanthine to xanthine, and xanthine into uric acid.	Xanthine	108-116	xanthine dehydrogenase	Homo sapiens	0-23
27798228-1	2016	Xanthine oxidoreductase (XOR) is the rate-limiting enzyme in purine catabolism and converts hypoxanthine to xanthine, and xanthine into uric acid.	Xanthine	108-116	xanthine dehydrogenase	Homo sapiens	25-28
27798228-1	2016	Xanthine oxidoreductase (XOR) is the rate-limiting enzyme in purine catabolism and converts hypoxanthine to xanthine, and xanthine into uric acid.	Uric Acid	136-145	xanthine dehydrogenase	Homo sapiens	0-23
27798228-1	2016	Xanthine oxidoreductase (XOR) is the rate-limiting enzyme in purine catabolism and converts hypoxanthine to xanthine, and xanthine into uric acid.	Uric Acid	136-145	xanthine dehydrogenase	Homo sapiens	25-28
27798228-3	2016	XOR inhibitors are primarily used in the treatment of gout, reducing the formation of uric acid and thereby, preventing the formation of monosodium urate crystals.	Uric Acid	86-95	xanthine dehydrogenase	Homo sapiens	0-3
27798228-3	2016	XOR inhibitors are primarily used in the treatment of gout, reducing the formation of uric acid and thereby, preventing the formation of monosodium urate crystals.	Uric Acid	137-153	xanthine dehydrogenase	Homo sapiens	0-3
27607461-1	2016	OBJECTIVE: The enzyme xanthine oxidoreductase (XOR) generates uric acid in the terminal steps of the purine metabolism; meanwhile reactive oxygen species are formed.	Uric Acid	62-71	xanthine dehydrogenase	Homo sapiens	22-45
27743800-0	2016	Corrigendum to "Extended-release naltrexone opioid treatment at jail reentry (XOR)" [Contemp.	Naltrexone	33-43	xanthine dehydrogenase	Homo sapiens	78-81
27607461-1	2016	OBJECTIVE: The enzyme xanthine oxidoreductase (XOR) generates uric acid in the terminal steps of the purine metabolism; meanwhile reactive oxygen species are formed.	Uric Acid	62-71	xanthine dehydrogenase	Homo sapiens	47-50
27607461-1	2016	OBJECTIVE: The enzyme xanthine oxidoreductase (XOR) generates uric acid in the terminal steps of the purine metabolism; meanwhile reactive oxygen species are formed.	purine	101-107	xanthine dehydrogenase	Homo sapiens	22-45
27607461-1	2016	OBJECTIVE: The enzyme xanthine oxidoreductase (XOR) generates uric acid in the terminal steps of the purine metabolism; meanwhile reactive oxygen species are formed.	purine	101-107	xanthine dehydrogenase	Homo sapiens	47-50
27607461-1	2016	OBJECTIVE: The enzyme xanthine oxidoreductase (XOR) generates uric acid in the terminal steps of the purine metabolism; meanwhile reactive oxygen species are formed.	Reactive Oxygen Species	130-153	xanthine dehydrogenase	Homo sapiens	22-45
27607461-1	2016	OBJECTIVE: The enzyme xanthine oxidoreductase (XOR) generates uric acid in the terminal steps of the purine metabolism; meanwhile reactive oxygen species are formed.	Reactive Oxygen Species	130-153	xanthine dehydrogenase	Homo sapiens	47-50
27607461-2	2016	We hypothesized that uric acid production, as assessed indirectly from XOR variants, is associated with hypertension.	Uric Acid	21-30	xanthine dehydrogenase	Homo sapiens	71-74
27607461-9	2016	CONCLUSION: Pending confirmation, our findings suggest that variation in uric acid production, as captured by genetic variation in XOR, might be a predictor of changes in BP and in the risk of hypertension.	Uric Acid	73-82	xanthine dehydrogenase	Homo sapiens	131-134
27521759-0	2016	Omeprazole impairs vascular redox biology and causes xanthine oxidoreductase-mediated endothelial dysfunction.	Omeprazole	0-10	xanthine dehydrogenase	Homo sapiens	53-76
27021957-1	2016	Human xanthine oxidoreductase (XOR), which is responsible for the final steps of the purine metabolism pathway and involved in oxidative drug metabolism, was successfully expressed in Escherichia coli BL21(DE3) Gold.	purine	85-91	xanthine dehydrogenase	Homo sapiens	31-34
27021957-3	2016	Induction of XOR expression with lactose or IPTG resulted in complete loss of activity whereas shake flasks cultures using media rather poor in nutrients resulted in functional XOR expression in the stationary phase.	Lactose	33-40	xanthine dehydrogenase	Homo sapiens	13-16
27021957-3	2016	Induction of XOR expression with lactose or IPTG resulted in complete loss of activity whereas shake flasks cultures using media rather poor in nutrients resulted in functional XOR expression in the stationary phase.	Isopropyl Thiogalactoside	44-48	xanthine dehydrogenase	Homo sapiens	13-16
27521759-8	2016	The selective XOR inhibitor febuxostat blunted both effects induced by omeprazole.	Omeprazole	71-81	xanthine dehydrogenase	Homo sapiens	14-17
27521759-9	2016	Treatment with omeprazole increased plasma ADMA concentrations, XOR activity and systemic markers of oxidative stress.	Omeprazole	15-25	xanthine dehydrogenase	Homo sapiens	64-67
27521759-10	2016	Incubation of aortic rings with ADMA increased XOR activity, DHE fluorescence and lucigenin chemiluminescence signals, and febuxostat blunted these effects.	N,N-dimethylarginine	32-36	xanthine dehydrogenase	Homo sapiens	47-50
27521759-11	2016	Providing functional evidence that omeprazole causes ED by XOR-mediated mechanisms, we found that febuxostat blunted the ED caused by omeprazole treatment.	Omeprazole	35-45	xanthine dehydrogenase	Homo sapiens	59-62
27521759-11	2016	Providing functional evidence that omeprazole causes ED by XOR-mediated mechanisms, we found that febuxostat blunted the ED caused by omeprazole treatment.	Febuxostat	98-108	xanthine dehydrogenase	Homo sapiens	59-62
27521759-11	2016	Providing functional evidence that omeprazole causes ED by XOR-mediated mechanisms, we found that febuxostat blunted the ED caused by omeprazole treatment.	Omeprazole	134-144	xanthine dehydrogenase	Homo sapiens	59-62
27521759-12	2016	This study shows that treatment with omeprazole impairs the vascular redox biology by XOR-mediated mechanisms leading to ED.	Omeprazole	37-47	xanthine dehydrogenase	Homo sapiens	86-89
26887821-7	2016	(3) The inhibition of xanthine oxidoreductase leading to modulation of intracellular superoxide and plasma uric acid, a risk factor for developing type 2 diabetes.	Superoxides	85-95	xanthine dehydrogenase	Homo sapiens	22-45
26887821-7	2016	(3) The inhibition of xanthine oxidoreductase leading to modulation of intracellular superoxide and plasma uric acid, a risk factor for developing type 2 diabetes.	Uric Acid	107-116	xanthine dehydrogenase	Homo sapiens	22-45
27078869-15	2016	Our results show that XOR is important to the cardiovascular responses to nitrite in 2K1C hypertension, and XOR inhibitors commonly used by patients may cancel this effect.	Nitrites	74-81	xanthine dehydrogenase	Homo sapiens	22-25
27129464-3	2016	Hemoglobin, xanthine oxidoreductase and carbonic anhydrase (CA) have been reported to reduce/convert nitrite to NO.	Nitrites	101-108	xanthine dehydrogenase	Homo sapiens	12-35
27423335-2	2016	Xanthine oxidoreductase (XOR) catalyzes oxidative hydroxylation of hypoxanthine to xanthine to uric acid, accompanying the production of reactive oxygen species (ROS).	Hypoxanthine	67-79	xanthine dehydrogenase	Homo sapiens	0-23
27423335-2	2016	Xanthine oxidoreductase (XOR) catalyzes oxidative hydroxylation of hypoxanthine to xanthine to uric acid, accompanying the production of reactive oxygen species (ROS).	Hypoxanthine	67-79	xanthine dehydrogenase	Homo sapiens	25-28
27423335-2	2016	Xanthine oxidoreductase (XOR) catalyzes oxidative hydroxylation of hypoxanthine to xanthine to uric acid, accompanying the production of reactive oxygen species (ROS).	Xanthine	71-79	xanthine dehydrogenase	Homo sapiens	0-23
27423335-2	2016	Xanthine oxidoreductase (XOR) catalyzes oxidative hydroxylation of hypoxanthine to xanthine to uric acid, accompanying the production of reactive oxygen species (ROS).	Xanthine	71-79	xanthine dehydrogenase	Homo sapiens	25-28
27423335-2	2016	Xanthine oxidoreductase (XOR) catalyzes oxidative hydroxylation of hypoxanthine to xanthine to uric acid, accompanying the production of reactive oxygen species (ROS).	Uric Acid	95-104	xanthine dehydrogenase	Homo sapiens	0-23
27423335-2	2016	Xanthine oxidoreductase (XOR) catalyzes oxidative hydroxylation of hypoxanthine to xanthine to uric acid, accompanying the production of reactive oxygen species (ROS).	Uric Acid	95-104	xanthine dehydrogenase	Homo sapiens	25-28
27423335-2	2016	Xanthine oxidoreductase (XOR) catalyzes oxidative hydroxylation of hypoxanthine to xanthine to uric acid, accompanying the production of reactive oxygen species (ROS).	Reactive Oxygen Species	137-160	xanthine dehydrogenase	Homo sapiens	0-23
27423335-2	2016	Xanthine oxidoreductase (XOR) catalyzes oxidative hydroxylation of hypoxanthine to xanthine to uric acid, accompanying the production of reactive oxygen species (ROS).	Reactive Oxygen Species	137-160	xanthine dehydrogenase	Homo sapiens	25-28
27423335-2	2016	Xanthine oxidoreductase (XOR) catalyzes oxidative hydroxylation of hypoxanthine to xanthine to uric acid, accompanying the production of reactive oxygen species (ROS).	Reactive Oxygen Species	162-165	xanthine dehydrogenase	Homo sapiens	0-23
27423335-2	2016	Xanthine oxidoreductase (XOR) catalyzes oxidative hydroxylation of hypoxanthine to xanthine to uric acid, accompanying the production of reactive oxygen species (ROS).	Reactive Oxygen Species	162-165	xanthine dehydrogenase	Homo sapiens	25-28
27423335-5	2016	Accordingly, urate-lowering drugs such as allopurinol, an XOR-inhibitor, are extensively used for the treatment of gout.	Uric Acid	13-18	xanthine dehydrogenase	Homo sapiens	58-61
27423335-5	2016	Accordingly, urate-lowering drugs such as allopurinol, an XOR-inhibitor, are extensively used for the treatment of gout.	Allopurinol	42-53	xanthine dehydrogenase	Homo sapiens	58-61
27423335-8	2016	However, current XOR-inhibitor drugs such as allopurinol and febuxostat may have significant adverse effects.	Allopurinol	45-56	xanthine dehydrogenase	Homo sapiens	17-20
27423335-8	2016	However, current XOR-inhibitor drugs such as allopurinol and febuxostat may have significant adverse effects.	Febuxostat	61-71	xanthine dehydrogenase	Homo sapiens	17-20
26663724-10	2016	Treatment with etaftorone decreased expression of inducible NOS and XOR in kidneys, whereas it increased the expression of endothelial NOS.	etaftorone	15-25	xanthine dehydrogenase	Homo sapiens	68-71
27178765-0	2016	Extended-release naltrexone opioid treatment at jail reentry (XOR).	Naltrexone	17-27	xanthine dehydrogenase	Homo sapiens	62-65
27038523-1	2016	Topiroxostat, a xanthine oxidoreductase (XOR) inhibitor, has been shown to decrease the urinary albumin-to-creatinine ratio compared with placebo in hyperuricemic patients with stage 3 chronic kidney disease.	FYX-051	0-12	xanthine dehydrogenase	Homo sapiens	16-39
26320372-4	2016	Recently, evidence has been accumulated suggesting that chronic urate deposition requires a correct treatment not limited to acute episodes based on the modulation of the activity of key enzymes involved in metabolism and excretion of urate including xanthine oxidoreductase (XO) and URAT1.	Uric Acid	64-69	xanthine dehydrogenase	Homo sapiens	251-274
26320372-4	2016	Recently, evidence has been accumulated suggesting that chronic urate deposition requires a correct treatment not limited to acute episodes based on the modulation of the activity of key enzymes involved in metabolism and excretion of urate including xanthine oxidoreductase (XO) and URAT1.	Uric Acid	64-69	xanthine dehydrogenase	Homo sapiens	276-278
26320372-5	2016	The present review article will try to summarize the most recent evidences on the efficacy of XO inhibitors and uricosuric compounds in lowering uric acid levels in both the bloodstream and peripheral tissues.	Uric Acid	145-154	xanthine dehydrogenase	Homo sapiens	94-96
26320372-6	2016	In particular, we will focus on the effect of novel XO inhibitors in counteracting uric acid overproduction.	Uric Acid	83-92	xanthine dehydrogenase	Homo sapiens	52-54
26320372-7	2016	On the other hand, the effect of lowering uric acid levels via XO inhibition will be correlated with attenuation oxidative stress which leads to endothelial dysfunction thereby contributing to the pathophysiology of diabetes, hypertension, arteriosclerosis, and chronic heart failure.	Uric Acid	42-51	xanthine dehydrogenase	Homo sapiens	63-65
26320372-8	2016	Hence, scavenging and prevention of the XO generated oxygen radical accumulation emerge as an intriguing novel treatment option to counteract uric acid-induced tissue damages.	Reactive Oxygen Species	53-67	xanthine dehydrogenase	Homo sapiens	40-42
26320372-8	2016	Hence, scavenging and prevention of the XO generated oxygen radical accumulation emerge as an intriguing novel treatment option to counteract uric acid-induced tissue damages.	Uric Acid	142-151	xanthine dehydrogenase	Homo sapiens	40-42
27038523-1	2016	Topiroxostat, a xanthine oxidoreductase (XOR) inhibitor, has been shown to decrease the urinary albumin-to-creatinine ratio compared with placebo in hyperuricemic patients with stage 3 chronic kidney disease.	FYX-051	0-12	xanthine dehydrogenase	Homo sapiens	41-44
27038523-1	2016	Topiroxostat, a xanthine oxidoreductase (XOR) inhibitor, has been shown to decrease the urinary albumin-to-creatinine ratio compared with placebo in hyperuricemic patients with stage 3 chronic kidney disease.	Creatinine	107-117	xanthine dehydrogenase	Homo sapiens	41-44
27166140-0	2016	Opposing Functions for Plant Xanthine Dehydrogenase in Response to Powdery Mildew Infection: Production and Scavenging of Reactive Oxygen Species.	Reactive Oxygen Species	122-145	xanthine dehydrogenase	Homo sapiens	29-51
27006202-2	2016	In this assay, the amount of [(13) C2 ,(15) N2 ]uric acid (UA) produced by XOR was determined by using LC/TQMS.	[(13) c2 ,(15) n2 ]uric acid	29-57	xanthine dehydrogenase	Homo sapiens	75-78
27006202-2	2016	In this assay, the amount of [(13) C2 ,(15) N2 ]uric acid (UA) produced by XOR was determined by using LC/TQMS.	Uric Acid	59-61	xanthine dehydrogenase	Homo sapiens	75-78
27285897-8	2016	Xanthine oxidoreductase (XOR), aldehyde oxidase (SsAOX1), carbonyl reductase (CBR1) and cytochrome P450 (CYP) enzymes were involved in the QdNOs metabolism.	qdnos	139-144	xanthine dehydrogenase	Homo sapiens	0-23
27285897-8	2016	Xanthine oxidoreductase (XOR), aldehyde oxidase (SsAOX1), carbonyl reductase (CBR1) and cytochrome P450 (CYP) enzymes were involved in the QdNOs metabolism.	qdnos	139-144	xanthine dehydrogenase	Homo sapiens	25-28
26976364-4	2016	Hemoglobin, xanthine oxidoreductase and carbonic anhydrase (CA) have been reported to convert nitrite to NO.	Nitrites	94-101	xanthine dehydrogenase	Homo sapiens	12-35
26596572-5	2016	In this review, the impacts of metabolic perturbations including medium supplementation with glycerol; furfural and 5-hydroxymethyl furfural; allopurinol, an inhibitor of xanthine dehydrogenase; calcium (Ca(2+)) and zinc (Zn(2+)) ions); and artificial electron carriers, methyl viologen and neutral red, on butanol production are discussed.	Allopurinol	142-153	xanthine dehydrogenase	Homo sapiens	171-193
26390063-6	2016	Here, we demonstrate that both the activity of xanthine oxidoreductase (XOR), a superoxide-generating enzyme obligatory for CS-induced DNA damage and EndoC apoptosis, and superoxide concentrations are increased after CS exposure in the absence of MIF.	Superoxides	80-90	xanthine dehydrogenase	Homo sapiens	47-70
26390063-6	2016	Here, we demonstrate that both the activity of xanthine oxidoreductase (XOR), a superoxide-generating enzyme obligatory for CS-induced DNA damage and EndoC apoptosis, and superoxide concentrations are increased after CS exposure in the absence of MIF.	Superoxides	80-90	xanthine dehydrogenase	Homo sapiens	72-75
26390063-6	2016	Here, we demonstrate that both the activity of xanthine oxidoreductase (XOR), a superoxide-generating enzyme obligatory for CS-induced DNA damage and EndoC apoptosis, and superoxide concentrations are increased after CS exposure in the absence of MIF.	Cesium	124-126	xanthine dehydrogenase	Homo sapiens	47-70
26390063-6	2016	Here, we demonstrate that both the activity of xanthine oxidoreductase (XOR), a superoxide-generating enzyme obligatory for CS-induced DNA damage and EndoC apoptosis, and superoxide concentrations are increased after CS exposure in the absence of MIF.	Cesium	124-126	xanthine dehydrogenase	Homo sapiens	72-75
26390063-6	2016	Here, we demonstrate that both the activity of xanthine oxidoreductase (XOR), a superoxide-generating enzyme obligatory for CS-induced DNA damage and EndoC apoptosis, and superoxide concentrations are increased after CS exposure in the absence of MIF.	Cesium	217-219	xanthine dehydrogenase	Homo sapiens	47-70
26390063-6	2016	Here, we demonstrate that both the activity of xanthine oxidoreductase (XOR), a superoxide-generating enzyme obligatory for CS-induced DNA damage and EndoC apoptosis, and superoxide concentrations are increased after CS exposure in the absence of MIF.	Cesium	217-219	xanthine dehydrogenase	Homo sapiens	72-75
26390063-10	2016	Taken together, MIF suppresses CS-mediated cytotoxicity in the lung, in part by antagonizing ASK1-p38-XOR-dependent apoptosis.	Cesium	31-33	xanthine dehydrogenase	Homo sapiens	102-105
26687331-1	2016	Human xanthine oxidoreductase (XOR) catalyzes the last two steps of purine catabolism and is present in two interconvertible forms, which may utilize O2 or NAD(+) as electron acceptors.	purine	68-74	xanthine dehydrogenase	Homo sapiens	6-29
26687331-1	2016	Human xanthine oxidoreductase (XOR) catalyzes the last two steps of purine catabolism and is present in two interconvertible forms, which may utilize O2 or NAD(+) as electron acceptors.	purine	68-74	xanthine dehydrogenase	Homo sapiens	31-34
26687331-1	2016	Human xanthine oxidoreductase (XOR) catalyzes the last two steps of purine catabolism and is present in two interconvertible forms, which may utilize O2 or NAD(+) as electron acceptors.	Oxygen	150-152	xanthine dehydrogenase	Homo sapiens	6-29
26687331-1	2016	Human xanthine oxidoreductase (XOR) catalyzes the last two steps of purine catabolism and is present in two interconvertible forms, which may utilize O2 or NAD(+) as electron acceptors.	Oxygen	150-152	xanthine dehydrogenase	Homo sapiens	31-34
26687331-1	2016	Human xanthine oxidoreductase (XOR) catalyzes the last two steps of purine catabolism and is present in two interconvertible forms, which may utilize O2 or NAD(+) as electron acceptors.	NAD	156-162	xanthine dehydrogenase	Homo sapiens	6-29
26687331-1	2016	Human xanthine oxidoreductase (XOR) catalyzes the last two steps of purine catabolism and is present in two interconvertible forms, which may utilize O2 or NAD(+) as electron acceptors.	NAD	156-162	xanthine dehydrogenase	Homo sapiens	31-34
26687331-2	2016	In addition to uric acid, XOR products may comprise reactive oxygen and nitrogen species that have many biologic effects, including inflammation, endothelial dysfunction, and cytotoxicity, as well as mutagenesis and induction of proliferation.	reactive oxygen and nitrogen species	52-88	xanthine dehydrogenase	Homo sapiens	26-29
26687331-6	2016	Xanthine oxidoreductase (XOR) has been implicated in the process of oncogenesis either directly because it is able to catalyze the metabolic activation of carcinogenic substances or indirectly through the action of XOR-derived reactive oxygen and nitrogen species.	reactive oxygen and nitrogen species	227-263	xanthine dehydrogenase	Homo sapiens	0-23
26687331-6	2016	Xanthine oxidoreductase (XOR) has been implicated in the process of oncogenesis either directly because it is able to catalyze the metabolic activation of carcinogenic substances or indirectly through the action of XOR-derived reactive oxygen and nitrogen species.	reactive oxygen and nitrogen species	227-263	xanthine dehydrogenase	Homo sapiens	25-28
26687331-6	2016	Xanthine oxidoreductase (XOR) has been implicated in the process of oncogenesis either directly because it is able to catalyze the metabolic activation of carcinogenic substances or indirectly through the action of XOR-derived reactive oxygen and nitrogen species.	reactive oxygen and nitrogen species	227-263	xanthine dehydrogenase	Homo sapiens	215-218
26823950-1	2016	Xanthine oxidoreductase (XOR) is the enzyme that catalyzes the oxidation of hypoxanthine to xanthine and xanthine to uric acid and is widely distributed among species.	Hypoxanthine	76-88	xanthine dehydrogenase	Homo sapiens	0-23
27458036-1	2016	The enzyme xanthine oxidoreductase (XOR) catalyzes the last two steps of purine catabolism in the highest uricotelic primates.	purine	73-79	xanthine dehydrogenase	Homo sapiens	11-34
27458036-1	2016	The enzyme xanthine oxidoreductase (XOR) catalyzes the last two steps of purine catabolism in the highest uricotelic primates.	purine	73-79	xanthine dehydrogenase	Homo sapiens	36-39
27458036-3	2016	XOR activity is highly regulated at the transcriptional and post-translational levels and may generate reactive oxygen and nitrogen species, which trigger different consequences, ranging from cytotoxicity to inflammation.	reactive oxygen and nitrogen species	103-139	xanthine dehydrogenase	Homo sapiens	0-3
27458036-6	2016	XOR has an activating role that is essential to the pharmacological action of quinone drugs, cyadox, antiviral nucleoside analogues, allopurinol, nitrate and nitrite.	quinone	78-85	xanthine dehydrogenase	Homo sapiens	0-3
27458036-6	2016	XOR has an activating role that is essential to the pharmacological action of quinone drugs, cyadox, antiviral nucleoside analogues, allopurinol, nitrate and nitrite.	cyadox	93-99	xanthine dehydrogenase	Homo sapiens	0-3
27458036-6	2016	XOR has an activating role that is essential to the pharmacological action of quinone drugs, cyadox, antiviral nucleoside analogues, allopurinol, nitrate and nitrite.	Nucleosides	111-121	xanthine dehydrogenase	Homo sapiens	0-3
27458036-6	2016	XOR has an activating role that is essential to the pharmacological action of quinone drugs, cyadox, antiviral nucleoside analogues, allopurinol, nitrate and nitrite.	Allopurinol	133-144	xanthine dehydrogenase	Homo sapiens	0-3
27458036-6	2016	XOR has an activating role that is essential to the pharmacological action of quinone drugs, cyadox, antiviral nucleoside analogues, allopurinol, nitrate and nitrite.	Nitrates	146-153	xanthine dehydrogenase	Homo sapiens	0-3
27458036-6	2016	XOR has an activating role that is essential to the pharmacological action of quinone drugs, cyadox, antiviral nucleoside analogues, allopurinol, nitrate and nitrite.	Nitrites	158-165	xanthine dehydrogenase	Homo sapiens	0-3
27458036-7	2016	XOR activity has a degradation function toward thiopurine nucleotides, pyrazinoic acid, methylxanthines and tolbutamide, whose half-life may be prolonged by the use of XOR inhibitors.	thiopurine nucleotides	47-69	xanthine dehydrogenase	Homo sapiens	0-3
27458036-7	2016	XOR activity has a degradation function toward thiopurine nucleotides, pyrazinoic acid, methylxanthines and tolbutamide, whose half-life may be prolonged by the use of XOR inhibitors.	thiopurine nucleotides	47-69	xanthine dehydrogenase	Homo sapiens	168-171
27458036-7	2016	XOR activity has a degradation function toward thiopurine nucleotides, pyrazinoic acid, methylxanthines and tolbutamide, whose half-life may be prolonged by the use of XOR inhibitors.	pyrazinoic acid	71-86	xanthine dehydrogenase	Homo sapiens	0-3
27458036-7	2016	XOR activity has a degradation function toward thiopurine nucleotides, pyrazinoic acid, methylxanthines and tolbutamide, whose half-life may be prolonged by the use of XOR inhibitors.	pyrazinoic acid	71-86	xanthine dehydrogenase	Homo sapiens	168-171
27458036-7	2016	XOR activity has a degradation function toward thiopurine nucleotides, pyrazinoic acid, methylxanthines and tolbutamide, whose half-life may be prolonged by the use of XOR inhibitors.	methylxanthine	88-103	xanthine dehydrogenase	Homo sapiens	0-3
27458036-7	2016	XOR activity has a degradation function toward thiopurine nucleotides, pyrazinoic acid, methylxanthines and tolbutamide, whose half-life may be prolonged by the use of XOR inhibitors.	methylxanthine	88-103	xanthine dehydrogenase	Homo sapiens	168-171
27458036-7	2016	XOR activity has a degradation function toward thiopurine nucleotides, pyrazinoic acid, methylxanthines and tolbutamide, whose half-life may be prolonged by the use of XOR inhibitors.	Tolbutamide	108-119	xanthine dehydrogenase	Homo sapiens	0-3
27458036-7	2016	XOR activity has a degradation function toward thiopurine nucleotides, pyrazinoic acid, methylxanthines and tolbutamide, whose half-life may be prolonged by the use of XOR inhibitors.	Tolbutamide	108-119	xanthine dehydrogenase	Homo sapiens	168-171
26942273-1	2016	Febuxostat is a non-purine, selective inhibitor of both isoforms of xanthine oxido-reductase (XOR), and a major alternative to the scarce number of urate-lowering medications available in the last decades.	Febuxostat	0-10	xanthine dehydrogenase	Homo sapiens	68-92
26942273-1	2016	Febuxostat is a non-purine, selective inhibitor of both isoforms of xanthine oxido-reductase (XOR), and a major alternative to the scarce number of urate-lowering medications available in the last decades.	Febuxostat	0-10	xanthine dehydrogenase	Homo sapiens	94-97
26942273-2	2016	Its inhibition of XOR is more potent than allopurinol in a mg to mg comparison, what is associated to achievement of serum urate target more frequently than allopurinol at doses tested in clinical trials, especially in patients with the highest baseline serum urate levels.	Uric Acid	123-128	xanthine dehydrogenase	Homo sapiens	18-21
26942273-2	2016	Its inhibition of XOR is more potent than allopurinol in a mg to mg comparison, what is associated to achievement of serum urate target more frequently than allopurinol at doses tested in clinical trials, especially in patients with the highest baseline serum urate levels.	Uric Acid	260-265	xanthine dehydrogenase	Homo sapiens	18-21
26823950-1	2016	Xanthine oxidoreductase (XOR) is the enzyme that catalyzes the oxidation of hypoxanthine to xanthine and xanthine to uric acid and is widely distributed among species.	Hypoxanthine	76-88	xanthine dehydrogenase	Homo sapiens	25-28
26823950-1	2016	Xanthine oxidoreductase (XOR) is the enzyme that catalyzes the oxidation of hypoxanthine to xanthine and xanthine to uric acid and is widely distributed among species.	Xanthine	80-88	xanthine dehydrogenase	Homo sapiens	0-23
26823950-1	2016	Xanthine oxidoreductase (XOR) is the enzyme that catalyzes the oxidation of hypoxanthine to xanthine and xanthine to uric acid and is widely distributed among species.	Xanthine	80-88	xanthine dehydrogenase	Homo sapiens	25-28
26823950-1	2016	Xanthine oxidoreductase (XOR) is the enzyme that catalyzes the oxidation of hypoxanthine to xanthine and xanthine to uric acid and is widely distributed among species.	Xanthine	92-100	xanthine dehydrogenase	Homo sapiens	0-23
26823950-1	2016	Xanthine oxidoreductase (XOR) is the enzyme that catalyzes the oxidation of hypoxanthine to xanthine and xanthine to uric acid and is widely distributed among species.	Xanthine	92-100	xanthine dehydrogenase	Homo sapiens	25-28
26823950-1	2016	Xanthine oxidoreductase (XOR) is the enzyme that catalyzes the oxidation of hypoxanthine to xanthine and xanthine to uric acid and is widely distributed among species.	Uric Acid	117-126	xanthine dehydrogenase	Homo sapiens	0-23
26823950-1	2016	Xanthine oxidoreductase (XOR) is the enzyme that catalyzes the oxidation of hypoxanthine to xanthine and xanthine to uric acid and is widely distributed among species.	Uric Acid	117-126	xanthine dehydrogenase	Homo sapiens	25-28
26823950-2	2016	In addition to this housekeeping function, mammalian XOR is a physiological source of superoxide ion, hydrogen peroxide, and nitric oxide, which can function as second messengers in the activation of various pathways.	Superoxides	86-96	xanthine dehydrogenase	Homo sapiens	53-56
26823950-2	2016	In addition to this housekeeping function, mammalian XOR is a physiological source of superoxide ion, hydrogen peroxide, and nitric oxide, which can function as second messengers in the activation of various pathways.	Hydrogen Peroxide	102-119	xanthine dehydrogenase	Homo sapiens	53-56
26823950-2	2016	In addition to this housekeeping function, mammalian XOR is a physiological source of superoxide ion, hydrogen peroxide, and nitric oxide, which can function as second messengers in the activation of various pathways.	Nitric Oxide	125-137	xanthine dehydrogenase	Homo sapiens	53-56
26823950-8	2016	In conclusion, XOR activity generates free radicals and other oxidant reactive species that may result in either harmful or beneficial outcomes.	Free Radicals	38-51	xanthine dehydrogenase	Homo sapiens	15-18
26480148-1	2015	We report an electro-optic photonic integrated circuit which can perform the exclusive (XOR) logic operation based on two silicon parallel-cascaded microring resonators (MRRs) fabricated on the silicon-on-insulator (SOI) platform.	Silicon	122-129	xanthine dehydrogenase	Homo sapiens	88-91
26863601-0	2016	Influences of XDH genotype by gene-gene interactions with SUCLA2 for thiopurine-induced leukopenia in Korean patients with Crohn"s disease.	2-mercaptopyrazine	69-79	xanthine dehydrogenase	Homo sapiens	14-17
26863601-2	2016	Although xanthine dehydrogenase (XDH) is the second major contributor to azathioprine breakdown, polymorphisms in XDH have rarely been studied in IBD patients.	Azathioprine	73-85	xanthine dehydrogenase	Homo sapiens	9-31
26863601-2	2016	Although xanthine dehydrogenase (XDH) is the second major contributor to azathioprine breakdown, polymorphisms in XDH have rarely been studied in IBD patients.	Azathioprine	73-85	xanthine dehydrogenase	Homo sapiens	33-36
26863601-3	2016	We aim to access association between XDH variants and thiopurine-induced leukopenia by gene-gene interaction in a Crohn"s disease (CD) population.	2-mercaptopyrazine	54-64	xanthine dehydrogenase	Homo sapiens	37-40
26863601-5	2016	The association between four XDH variants (p.Gly172Arg, p.Asn1109Thr, p.Arg149Cys, and p.Thr910Lys) and thiopurine-induced leukopenia was analyzed in cases with early leukopenia (n = 66), late leukopenia (n = 264), and in controls without leukopenia (n = 632).	2-mercaptopyrazine	104-114	xanthine dehydrogenase	Homo sapiens	29-32
26863601-11	2016	Further studies are warranted to explore the mechanisms underlying the effects of the combination of XDH (p.Asn1109Thr) and SUCLA2 (199Ser) on thiopurine-induced leukopenia.	2-mercaptopyrazine	143-153	xanthine dehydrogenase	Homo sapiens	101-104
26342297-0	2015	Increase in thyroid stimulating hormone levels in patients with gout treated with inhibitors of xanthine oxidoreductase.	Thyrotropin	12-39	xanthine dehydrogenase	Homo sapiens	96-119
26480148-1	2015	We report an electro-optic photonic integrated circuit which can perform the exclusive (XOR) logic operation based on two silicon parallel-cascaded microring resonators (MRRs) fabricated on the silicon-on-insulator (SOI) platform.	Silicon	194-201	xanthine dehydrogenase	Homo sapiens	88-91
25995007-1	2015	Xanthine oxidoreductase (XOR), the molybdoflavin enzyme responsible for the terminal steps of purine degradation in humans, is also recognized as a significant source of reactive species contributory to inflammatory disease.	molybdoflavin	35-48	xanthine dehydrogenase	Homo sapiens	0-23
25995007-1	2015	Xanthine oxidoreductase (XOR), the molybdoflavin enzyme responsible for the terminal steps of purine degradation in humans, is also recognized as a significant source of reactive species contributory to inflammatory disease.	molybdoflavin	35-48	xanthine dehydrogenase	Homo sapiens	25-28
25995007-1	2015	Xanthine oxidoreductase (XOR), the molybdoflavin enzyme responsible for the terminal steps of purine degradation in humans, is also recognized as a significant source of reactive species contributory to inflammatory disease.	purine	94-100	xanthine dehydrogenase	Homo sapiens	0-23
25995007-1	2015	Xanthine oxidoreductase (XOR), the molybdoflavin enzyme responsible for the terminal steps of purine degradation in humans, is also recognized as a significant source of reactive species contributory to inflammatory disease.	purine	94-100	xanthine dehydrogenase	Homo sapiens	25-28
25995007-3	2015	For decades, XOR involvement in pathologic processes has been established by salutary outcomes attained from treatment with the XOR inhibitor allopurinol.	Allopurinol	142-153	xanthine dehydrogenase	Homo sapiens	13-16
25995007-3	2015	For decades, XOR involvement in pathologic processes has been established by salutary outcomes attained from treatment with the XOR inhibitor allopurinol.	Allopurinol	142-153	xanthine dehydrogenase	Homo sapiens	128-131
25995007-6	2015	This is exemplified by recent reports: (1) identifying XOR as a nitrite reductase and thus a source of beneficial nitric oxide (( )NO) under in vivo conditions similar to those where XOR inhibition has been assumed an optimal treatment choice, (2) describing XOR-derived uric acid (UA) as a critical pro-inflammatory mediator in vascular and metabolic disease and (3) ascribing an antioxidant/protective role for XOR-derived UA.	Nitric Oxide	114-126	xanthine dehydrogenase	Homo sapiens	55-58
25995007-6	2015	This is exemplified by recent reports: (1) identifying XOR as a nitrite reductase and thus a source of beneficial nitric oxide (( )NO) under in vivo conditions similar to those where XOR inhibition has been assumed an optimal treatment choice, (2) describing XOR-derived uric acid (UA) as a critical pro-inflammatory mediator in vascular and metabolic disease and (3) ascribing an antioxidant/protective role for XOR-derived UA.	Uric Acid	271-280	xanthine dehydrogenase	Homo sapiens	55-58
25995007-6	2015	This is exemplified by recent reports: (1) identifying XOR as a nitrite reductase and thus a source of beneficial nitric oxide (( )NO) under in vivo conditions similar to those where XOR inhibition has been assumed an optimal treatment choice, (2) describing XOR-derived uric acid (UA) as a critical pro-inflammatory mediator in vascular and metabolic disease and (3) ascribing an antioxidant/protective role for XOR-derived UA.	Uric Acid	282-284	xanthine dehydrogenase	Homo sapiens	55-58
25995007-6	2015	This is exemplified by recent reports: (1) identifying XOR as a nitrite reductase and thus a source of beneficial nitric oxide (( )NO) under in vivo conditions similar to those where XOR inhibition has been assumed an optimal treatment choice, (2) describing XOR-derived uric acid (UA) as a critical pro-inflammatory mediator in vascular and metabolic disease and (3) ascribing an antioxidant/protective role for XOR-derived UA.	Uric Acid	425-427	xanthine dehydrogenase	Homo sapiens	55-58
25995007-8	2015	As such, this review will critically evaluate XOR-catalyzed oxidant, ( )NO and UA formation as well as identify factors that mediate their production, inhibition and the resultant impact on inflammatory disease.	Uric Acid	79-81	xanthine dehydrogenase	Homo sapiens	46-49
26321266-2	2015	A critical source of these reactive species is the purine catabolizing enzyme xanthine oxidoreductase (XOR) as numerous reports over the past 30 years have demonstrated XOR inhibition to be salutary.	purine	51-57	xanthine dehydrogenase	Homo sapiens	78-101
26321266-2	2015	A critical source of these reactive species is the purine catabolizing enzyme xanthine oxidoreductase (XOR) as numerous reports over the past 30 years have demonstrated XOR inhibition to be salutary.	purine	51-57	xanthine dehydrogenase	Homo sapiens	103-106
26321266-2	2015	A critical source of these reactive species is the purine catabolizing enzyme xanthine oxidoreductase (XOR) as numerous reports over the past 30 years have demonstrated XOR inhibition to be salutary.	purine	51-57	xanthine dehydrogenase	Homo sapiens	169-172
26321266-3	2015	Despite this long standing association between increased vascular XOR activity and negative clinical outcomes, recent reports reveal a new paradigm whereby the enzymatic activity of XOR mediates beneficial outcomes by catalyzing the one electron reduction of nitrite (NO2(-)) to nitric oxide (NO) when NO2(-) and/or nitrate (NO3(-)) levels are enhanced either via dietary or pharmacologic means.	Nitrites	259-266	xanthine dehydrogenase	Homo sapiens	66-69
26321266-3	2015	Despite this long standing association between increased vascular XOR activity and negative clinical outcomes, recent reports reveal a new paradigm whereby the enzymatic activity of XOR mediates beneficial outcomes by catalyzing the one electron reduction of nitrite (NO2(-)) to nitric oxide (NO) when NO2(-) and/or nitrate (NO3(-)) levels are enhanced either via dietary or pharmacologic means.	Nitrites	259-266	xanthine dehydrogenase	Homo sapiens	182-185
26321266-3	2015	Despite this long standing association between increased vascular XOR activity and negative clinical outcomes, recent reports reveal a new paradigm whereby the enzymatic activity of XOR mediates beneficial outcomes by catalyzing the one electron reduction of nitrite (NO2(-)) to nitric oxide (NO) when NO2(-) and/or nitrate (NO3(-)) levels are enhanced either via dietary or pharmacologic means.	Nitrogen Dioxide	268-271	xanthine dehydrogenase	Homo sapiens	66-69
26321266-3	2015	Despite this long standing association between increased vascular XOR activity and negative clinical outcomes, recent reports reveal a new paradigm whereby the enzymatic activity of XOR mediates beneficial outcomes by catalyzing the one electron reduction of nitrite (NO2(-)) to nitric oxide (NO) when NO2(-) and/or nitrate (NO3(-)) levels are enhanced either via dietary or pharmacologic means.	Nitrogen Dioxide	268-271	xanthine dehydrogenase	Homo sapiens	182-185
26321266-3	2015	Despite this long standing association between increased vascular XOR activity and negative clinical outcomes, recent reports reveal a new paradigm whereby the enzymatic activity of XOR mediates beneficial outcomes by catalyzing the one electron reduction of nitrite (NO2(-)) to nitric oxide (NO) when NO2(-) and/or nitrate (NO3(-)) levels are enhanced either via dietary or pharmacologic means.	Nitric Oxide	279-291	xanthine dehydrogenase	Homo sapiens	182-185
26321266-3	2015	Despite this long standing association between increased vascular XOR activity and negative clinical outcomes, recent reports reveal a new paradigm whereby the enzymatic activity of XOR mediates beneficial outcomes by catalyzing the one electron reduction of nitrite (NO2(-)) to nitric oxide (NO) when NO2(-) and/or nitrate (NO3(-)) levels are enhanced either via dietary or pharmacologic means.	Nitrogen Dioxide	302-305	xanthine dehydrogenase	Homo sapiens	182-185
26321266-3	2015	Despite this long standing association between increased vascular XOR activity and negative clinical outcomes, recent reports reveal a new paradigm whereby the enzymatic activity of XOR mediates beneficial outcomes by catalyzing the one electron reduction of nitrite (NO2(-)) to nitric oxide (NO) when NO2(-) and/or nitrate (NO3(-)) levels are enhanced either via dietary or pharmacologic means.	Nitrates	316-323	xanthine dehydrogenase	Homo sapiens	182-185
26321266-3	2015	Despite this long standing association between increased vascular XOR activity and negative clinical outcomes, recent reports reveal a new paradigm whereby the enzymatic activity of XOR mediates beneficial outcomes by catalyzing the one electron reduction of nitrite (NO2(-)) to nitric oxide (NO) when NO2(-) and/or nitrate (NO3(-)) levels are enhanced either via dietary or pharmacologic means.	punky blue	325-328	xanthine dehydrogenase	Homo sapiens	182-185
25939710-1	2015	BACKGROUND: Xanthine oxidase (XO) is one of the two interconvertible forms of xanthine oxidoreductase and well-studied for its role in purine catabolism and that of other purine analogues, drugs especially.	purine	135-141	xanthine dehydrogenase	Homo sapiens	78-101
25841777-10	2015	However, inhibition of xanthine oxidoreductase (XOR; febuxostat or allopurinol) abolished the sensitized response to nitrite during hypoxia and acidosis.	Febuxostat	53-63	xanthine dehydrogenase	Homo sapiens	23-46
25841777-10	2015	However, inhibition of xanthine oxidoreductase (XOR; febuxostat or allopurinol) abolished the sensitized response to nitrite during hypoxia and acidosis.	Febuxostat	53-63	xanthine dehydrogenase	Homo sapiens	48-51
25841777-10	2015	However, inhibition of xanthine oxidoreductase (XOR; febuxostat or allopurinol) abolished the sensitized response to nitrite during hypoxia and acidosis.	Allopurinol	67-78	xanthine dehydrogenase	Homo sapiens	23-46
25841777-10	2015	However, inhibition of xanthine oxidoreductase (XOR; febuxostat or allopurinol) abolished the sensitized response to nitrite during hypoxia and acidosis.	Allopurinol	67-78	xanthine dehydrogenase	Homo sapiens	48-51
25841777-10	2015	However, inhibition of xanthine oxidoreductase (XOR; febuxostat or allopurinol) abolished the sensitized response to nitrite during hypoxia and acidosis.	Nitrites	117-124	xanthine dehydrogenase	Homo sapiens	23-46
25841777-10	2015	However, inhibition of xanthine oxidoreductase (XOR; febuxostat or allopurinol) abolished the sensitized response to nitrite during hypoxia and acidosis.	Nitrites	117-124	xanthine dehydrogenase	Homo sapiens	48-51
25939710-1	2015	BACKGROUND: Xanthine oxidase (XO) is one of the two interconvertible forms of xanthine oxidoreductase and well-studied for its role in purine catabolism and that of other purine analogues, drugs especially.	purine	171-177	xanthine dehydrogenase	Homo sapiens	78-101
25740261-0	2015	CGRP mediate the isosorbide-5-mononitrate cardiovascular response in healthy Chinese male volunteers through a XOR-independent pathway.	isosorbide-5-mononitrate	17-41	xanthine dehydrogenase	Homo sapiens	111-114
25727730-10	2015	Although the nitrate reductase activity of xanthine oxidoreductase in muscle is less than that of liver, the residual activity in muscle could be very important in view of its total mass and the high basal level of nitrate.	Nitrates	13-20	xanthine dehydrogenase	Homo sapiens	43-66
25879627-3	2015	Xanthine oxidoreductase (XOR) has the unique capacity to produce both ROS and NO.	Reactive Oxygen Species	70-73	xanthine dehydrogenase	Homo sapiens	0-23
25879627-3	2015	Xanthine oxidoreductase (XOR) has the unique capacity to produce both ROS and NO.	Reactive Oxygen Species	70-73	xanthine dehydrogenase	Homo sapiens	25-28
25879627-6	2015	XOR was inhibited with dietary tungsten or allopurinol.	Tungsten	31-39	xanthine dehydrogenase	Homo sapiens	0-3
25879627-6	2015	XOR was inhibited with dietary tungsten or allopurinol.	Allopurinol	43-54	xanthine dehydrogenase	Homo sapiens	0-3
25879627-12	2015	Tungsten significantly inhibited XOR activity and impaired healing with reduced ROS production with reduced angiogenesis and KC proliferation.	Tungsten	0-8	xanthine dehydrogenase	Homo sapiens	33-36
25879627-14	2015	Oral allopurinol did not reduce XOR activity or alter wound healing but topical allopurinol significantly reduced XOR activity and delayed healing.	Allopurinol	80-91	xanthine dehydrogenase	Homo sapiens	114-117
25879627-17	2015	These studies demonstrate for the first time that XOR is abundant in wounds and participates in normal wound healing through effects on ROS production.	Reactive Oxygen Species	136-139	xanthine dehydrogenase	Homo sapiens	50-53
25732085-2	2015	nNOS was reported to decrease superoxide production in the myocardium by inhibiting the function of xanthine oxidoreductase.	Superoxides	30-40	xanthine dehydrogenase	Homo sapiens	100-123
25740261-1	2015	OBJECTIVES: This study was designed to determine whether xanthine oxidoreductase (XOR) is involved in Isosorbide- 5-mononitrate (IS-5-MN) metabolism, and to elucidate the role of the neuropeptide calcitonin gene-related peptide (CGRP) in the IS-5-MN response.	isosorbide-5-mononitrate	102-127	xanthine dehydrogenase	Homo sapiens	57-80
25740261-1	2015	OBJECTIVES: This study was designed to determine whether xanthine oxidoreductase (XOR) is involved in Isosorbide- 5-mononitrate (IS-5-MN) metabolism, and to elucidate the role of the neuropeptide calcitonin gene-related peptide (CGRP) in the IS-5-MN response.	isosorbide-5-mononitrate	102-127	xanthine dehydrogenase	Homo sapiens	82-85
25740261-1	2015	OBJECTIVES: This study was designed to determine whether xanthine oxidoreductase (XOR) is involved in Isosorbide- 5-mononitrate (IS-5-MN) metabolism, and to elucidate the role of the neuropeptide calcitonin gene-related peptide (CGRP) in the IS-5-MN response.	isosorbide-5-mononitrate	129-136	xanthine dehydrogenase	Homo sapiens	57-80
25740261-1	2015	OBJECTIVES: This study was designed to determine whether xanthine oxidoreductase (XOR) is involved in Isosorbide- 5-mononitrate (IS-5-MN) metabolism, and to elucidate the role of the neuropeptide calcitonin gene-related peptide (CGRP) in the IS-5-MN response.	isosorbide-5-mononitrate	129-136	xanthine dehydrogenase	Homo sapiens	82-85
25740261-1	2015	OBJECTIVES: This study was designed to determine whether xanthine oxidoreductase (XOR) is involved in Isosorbide- 5-mononitrate (IS-5-MN) metabolism, and to elucidate the role of the neuropeptide calcitonin gene-related peptide (CGRP) in the IS-5-MN response.	Iodine	129-131	xanthine dehydrogenase	Homo sapiens	57-80
25740261-1	2015	OBJECTIVES: This study was designed to determine whether xanthine oxidoreductase (XOR) is involved in Isosorbide- 5-mononitrate (IS-5-MN) metabolism, and to elucidate the role of the neuropeptide calcitonin gene-related peptide (CGRP) in the IS-5-MN response.	Iodine	129-131	xanthine dehydrogenase	Homo sapiens	82-85
25740261-1	2015	OBJECTIVES: This study was designed to determine whether xanthine oxidoreductase (XOR) is involved in Isosorbide- 5-mononitrate (IS-5-MN) metabolism, and to elucidate the role of the neuropeptide calcitonin gene-related peptide (CGRP) in the IS-5-MN response.	5-mn	132-136	xanthine dehydrogenase	Homo sapiens	57-80
25740261-1	2015	OBJECTIVES: This study was designed to determine whether xanthine oxidoreductase (XOR) is involved in Isosorbide- 5-mononitrate (IS-5-MN) metabolism, and to elucidate the role of the neuropeptide calcitonin gene-related peptide (CGRP) in the IS-5-MN response.	5-mn	132-136	xanthine dehydrogenase	Homo sapiens	82-85
25740261-4	2015	RESULTS: Individuals with a lower baseline XOR-mRNA expression showed lower plasma XOR activity and significantly greater changes in SBP (DeltaSBP) after IS-5-MN administration.	Iodine	154-156	xanthine dehydrogenase	Homo sapiens	43-46
25800347-2	2015	We present evidence that macrophage secretion of IL1beta upon stimulation with ATP, crystals or LPS is mediated by a rapid increase in the activity of xanthine oxidase (XO), the oxidized form of xanthine dehydrogenase, resulting in the formation of uric acid as well as ROS.	Adenosine Triphosphate	79-82	xanthine dehydrogenase	Homo sapiens	195-217
25800347-2	2015	We present evidence that macrophage secretion of IL1beta upon stimulation with ATP, crystals or LPS is mediated by a rapid increase in the activity of xanthine oxidase (XO), the oxidized form of xanthine dehydrogenase, resulting in the formation of uric acid as well as ROS.	Uric Acid	249-258	xanthine dehydrogenase	Homo sapiens	195-217
25800347-2	2015	We present evidence that macrophage secretion of IL1beta upon stimulation with ATP, crystals or LPS is mediated by a rapid increase in the activity of xanthine oxidase (XO), the oxidized form of xanthine dehydrogenase, resulting in the formation of uric acid as well as ROS.	Reactive Oxygen Species	270-273	xanthine dehydrogenase	Homo sapiens	195-217
25634685-12	2015	Xanthine dehydrogenase (XDH), which plays an important role in uric acid synthesis, was up-regulated by the high-fat diet (p < 0.05).	Uric Acid	63-72	xanthine dehydrogenase	Homo sapiens	0-22
25501928-1	2015	Xanthine oxidoreductase (XOR), which is widely distributed from humans to bacteria, has a key role in purine catabolism, catalyzing two steps of sequential hydroxylation from hypoxanthine to xanthine and from xanthine to urate at its molybdenum cofactor (Moco).	purine	102-108	xanthine dehydrogenase	Homo sapiens	0-23
25501928-1	2015	Xanthine oxidoreductase (XOR), which is widely distributed from humans to bacteria, has a key role in purine catabolism, catalyzing two steps of sequential hydroxylation from hypoxanthine to xanthine and from xanthine to urate at its molybdenum cofactor (Moco).	purine	102-108	xanthine dehydrogenase	Homo sapiens	25-28
25501928-1	2015	Xanthine oxidoreductase (XOR), which is widely distributed from humans to bacteria, has a key role in purine catabolism, catalyzing two steps of sequential hydroxylation from hypoxanthine to xanthine and from xanthine to urate at its molybdenum cofactor (Moco).	Hypoxanthine	175-187	xanthine dehydrogenase	Homo sapiens	0-23
25501928-1	2015	Xanthine oxidoreductase (XOR), which is widely distributed from humans to bacteria, has a key role in purine catabolism, catalyzing two steps of sequential hydroxylation from hypoxanthine to xanthine and from xanthine to urate at its molybdenum cofactor (Moco).	Hypoxanthine	175-187	xanthine dehydrogenase	Homo sapiens	25-28
25501928-1	2015	Xanthine oxidoreductase (XOR), which is widely distributed from humans to bacteria, has a key role in purine catabolism, catalyzing two steps of sequential hydroxylation from hypoxanthine to xanthine and from xanthine to urate at its molybdenum cofactor (Moco).	Xanthine	179-187	xanthine dehydrogenase	Homo sapiens	0-23
25501928-1	2015	Xanthine oxidoreductase (XOR), which is widely distributed from humans to bacteria, has a key role in purine catabolism, catalyzing two steps of sequential hydroxylation from hypoxanthine to xanthine and from xanthine to urate at its molybdenum cofactor (Moco).	Xanthine	179-187	xanthine dehydrogenase	Homo sapiens	25-28
25501928-1	2015	Xanthine oxidoreductase (XOR), which is widely distributed from humans to bacteria, has a key role in purine catabolism, catalyzing two steps of sequential hydroxylation from hypoxanthine to xanthine and from xanthine to urate at its molybdenum cofactor (Moco).	Xanthine	191-199	xanthine dehydrogenase	Homo sapiens	0-23
25501928-1	2015	Xanthine oxidoreductase (XOR), which is widely distributed from humans to bacteria, has a key role in purine catabolism, catalyzing two steps of sequential hydroxylation from hypoxanthine to xanthine and from xanthine to urate at its molybdenum cofactor (Moco).	Xanthine	191-199	xanthine dehydrogenase	Homo sapiens	25-28
25267303-2	2015	Enzyme families containing a single pyranopterin dithiolene chelate have been demonstrated to have reactivity towards two (sulfite oxidase, SUOX-fold) and five (xanthine dehydrogenase, XDH-fold) types of substrate, whereas the major family of enzymes containing a bis-pyranopterin dithiolene chelate (dimethylsulfoxide reductase, DMSOR-fold) is reactive towards eight types of substrate.	pyranopterin dithiolene	36-59	xanthine dehydrogenase	Homo sapiens	161-183
25267303-2	2015	Enzyme families containing a single pyranopterin dithiolene chelate have been demonstrated to have reactivity towards two (sulfite oxidase, SUOX-fold) and five (xanthine dehydrogenase, XDH-fold) types of substrate, whereas the major family of enzymes containing a bis-pyranopterin dithiolene chelate (dimethylsulfoxide reductase, DMSOR-fold) is reactive towards eight types of substrate.	pyranopterin dithiolene	36-59	xanthine dehydrogenase	Homo sapiens	185-188
25634685-12	2015	Xanthine dehydrogenase (XDH), which plays an important role in uric acid synthesis, was up-regulated by the high-fat diet (p < 0.05).	Uric Acid	63-72	xanthine dehydrogenase	Homo sapiens	24-27
24506204-2	2014	In the present study, we investigated the potential role of xanthine dehydrogenase (XDH) in retinoic acid biosynthesis in human thyroid glandular cells (HTGC).	Tretinoin	92-105	xanthine dehydrogenase	Homo sapiens	60-82
25370766-2	2015	Missing XDH/XO activity leads to undetectable levels of uric acid excessively replaced by xanthine in serum/urine.	Uric Acid	56-65	xanthine dehydrogenase	Homo sapiens	8-11
25370766-2	2015	Missing XDH/XO activity leads to undetectable levels of uric acid excessively replaced by xanthine in serum/urine.	Xanthine	90-98	xanthine dehydrogenase	Homo sapiens	8-11
25571764-4	2015	Treatment of diabetic wounds with siXDH (xanthine dehydrogenase siRNA) decreased XDH mRNA expression by 51.6%, XO activity by 35.9%, ROS levels by 78.1%, pathologic wound burden by 31.5%, and accelerated wound healing by 7 days (23.3%).	Reactive Oxygen Species	133-136	xanthine dehydrogenase	Homo sapiens	36-39
25463089-4	2014	In particular, uric acid may have a protective as well as a detrimental role in vascular alterations, thus justifying the multi-directional effects of XOR inhibition.	Uric Acid	15-24	xanthine dehydrogenase	Homo sapiens	151-154
24997452-4	2015	Hyperglycemia triggers formation of advanced glycosylation end products (AGEs), activates protein kinase C, enhances polyol pathway, glucose autoxidation, which coupled with elevated levels of free fatty acids, and leptin have been implicated in increased generation of superoxide anion by mitochondria, NADPH oxidases and xanthine oxidoreductase in diabetic vasculature and myocardium.	Fatty Acids, Nonesterified	193-209	xanthine dehydrogenase	Homo sapiens	323-346
26353707-9	2015	By combining the photoconductive response of two different carbon nanotubes thin film samples, a straightforward XOR encryption was performed.	Carbon	59-65	xanthine dehydrogenase	Homo sapiens	113-116
26451288-3	2015	Recently, we employed a combined histological, metabolomics, and transcriptional and protein analysis approach to establish that nitrate promoted the "browning" of white adipose tissue via the xanthine oxidoreductase catalyzed reductive nitrate-nitrite-nitric oxide pathway.	Nitrates	129-136	xanthine dehydrogenase	Homo sapiens	193-216
26451288-3	2015	Recently, we employed a combined histological, metabolomics, and transcriptional and protein analysis approach to establish that nitrate promoted the "browning" of white adipose tissue via the xanthine oxidoreductase catalyzed reductive nitrate-nitrite-nitric oxide pathway.	Nitrates	237-244	xanthine dehydrogenase	Homo sapiens	193-216
26451288-3	2015	Recently, we employed a combined histological, metabolomics, and transcriptional and protein analysis approach to establish that nitrate promoted the "browning" of white adipose tissue via the xanthine oxidoreductase catalyzed reductive nitrate-nitrite-nitric oxide pathway.	Nitrites	245-252	xanthine dehydrogenase	Homo sapiens	193-216
26451288-3	2015	Recently, we employed a combined histological, metabolomics, and transcriptional and protein analysis approach to establish that nitrate promoted the "browning" of white adipose tissue via the xanthine oxidoreductase catalyzed reductive nitrate-nitrite-nitric oxide pathway.	Nitric Oxide	253-265	xanthine dehydrogenase	Homo sapiens	193-216
25512781-2	2014	Xanthine dehydrogenase/xanthine oxidase (XDH/XO) is rate-limiting enzyme of uric acid generation, and allopurinol was developed as a uric acid (UA) generation inhibitor in the 1950s and has been routinely used for gout prevention since then.	Uric Acid	76-85	xanthine dehydrogenase	Homo sapiens	0-22
25512781-2	2014	Xanthine dehydrogenase/xanthine oxidase (XDH/XO) is rate-limiting enzyme of uric acid generation, and allopurinol was developed as a uric acid (UA) generation inhibitor in the 1950s and has been routinely used for gout prevention since then.	Uric Acid	76-85	xanthine dehydrogenase	Homo sapiens	41-44
25512781-2	2014	Xanthine dehydrogenase/xanthine oxidase (XDH/XO) is rate-limiting enzyme of uric acid generation, and allopurinol was developed as a uric acid (UA) generation inhibitor in the 1950s and has been routinely used for gout prevention since then.	Allopurinol	102-113	xanthine dehydrogenase	Homo sapiens	0-22
25512781-2	2014	Xanthine dehydrogenase/xanthine oxidase (XDH/XO) is rate-limiting enzyme of uric acid generation, and allopurinol was developed as a uric acid (UA) generation inhibitor in the 1950s and has been routinely used for gout prevention since then.	Allopurinol	102-113	xanthine dehydrogenase	Homo sapiens	41-44
25512781-2	2014	Xanthine dehydrogenase/xanthine oxidase (XDH/XO) is rate-limiting enzyme of uric acid generation, and allopurinol was developed as a uric acid (UA) generation inhibitor in the 1950s and has been routinely used for gout prevention since then.	Uric Acid	133-142	xanthine dehydrogenase	Homo sapiens	0-22
25512781-2	2014	Xanthine dehydrogenase/xanthine oxidase (XDH/XO) is rate-limiting enzyme of uric acid generation, and allopurinol was developed as a uric acid (UA) generation inhibitor in the 1950s and has been routinely used for gout prevention since then.	Uric Acid	133-142	xanthine dehydrogenase	Homo sapiens	41-44
25512781-2	2014	Xanthine dehydrogenase/xanthine oxidase (XDH/XO) is rate-limiting enzyme of uric acid generation, and allopurinol was developed as a uric acid (UA) generation inhibitor in the 1950s and has been routinely used for gout prevention since then.	Uric Acid	144-146	xanthine dehydrogenase	Homo sapiens	0-22
25512781-2	2014	Xanthine dehydrogenase/xanthine oxidase (XDH/XO) is rate-limiting enzyme of uric acid generation, and allopurinol was developed as a uric acid (UA) generation inhibitor in the 1950s and has been routinely used for gout prevention since then.	Uric Acid	144-146	xanthine dehydrogenase	Homo sapiens	41-44
25512781-8	2014	Many in vitro and animal studies have implicated inflammation and oxidative stress in UA metabolism and vascular injury because XDH/XO act as one of the major source of reactive oxygen species Many studies on UA levels and associated diseases implicate involvement of UA generation in disease onset and/or progression.	Uric Acid	86-88	xanthine dehydrogenase	Homo sapiens	128-131
25512781-8	2014	Many in vitro and animal studies have implicated inflammation and oxidative stress in UA metabolism and vascular injury because XDH/XO act as one of the major source of reactive oxygen species Many studies on UA levels and associated diseases implicate involvement of UA generation in disease onset and/or progression.	Reactive Oxygen Species	169-192	xanthine dehydrogenase	Homo sapiens	128-131
25512781-8	2014	Many in vitro and animal studies have implicated inflammation and oxidative stress in UA metabolism and vascular injury because XDH/XO act as one of the major source of reactive oxygen species Many studies on UA levels and associated diseases implicate involvement of UA generation in disease onset and/or progression.	Uric Acid	209-211	xanthine dehydrogenase	Homo sapiens	128-131
25512781-8	2014	Many in vitro and animal studies have implicated inflammation and oxidative stress in UA metabolism and vascular injury because XDH/XO act as one of the major source of reactive oxygen species Many studies on UA levels and associated diseases implicate involvement of UA generation in disease onset and/or progression.	Uric Acid	209-211	xanthine dehydrogenase	Homo sapiens	128-131
25512781-9	2014	Interventional studies for UA generation, not UA excretion revealed XDH/XO can be the therapeutic target for vascular injury and renal dysfunction.	Uric Acid	27-29	xanthine dehydrogenase	Homo sapiens	68-71
25015064-1	2014	Uric acid (UA) is generalized as a byproduct the terminal steps of purine catabolism, which are catalyzed by xanthine oxidoreductase.	Uric Acid	0-9	xanthine dehydrogenase	Homo sapiens	109-132
25015064-1	2014	Uric acid (UA) is generalized as a byproduct the terminal steps of purine catabolism, which are catalyzed by xanthine oxidoreductase.	Uric Acid	11-13	xanthine dehydrogenase	Homo sapiens	109-132
25015064-1	2014	Uric acid (UA) is generalized as a byproduct the terminal steps of purine catabolism, which are catalyzed by xanthine oxidoreductase.	purine	67-73	xanthine dehydrogenase	Homo sapiens	109-132
24687403-8	2014	In addition, a newer xanthine oxidoreductase inhibitor, febuxostat, may also be effective in the prevention of calcium stones, as it reduces urinary uric acid excretion.	Febuxostat	56-66	xanthine dehydrogenase	Homo sapiens	21-44
24687403-8	2014	In addition, a newer xanthine oxidoreductase inhibitor, febuxostat, may also be effective in the prevention of calcium stones, as it reduces urinary uric acid excretion.	Calcium	111-118	xanthine dehydrogenase	Homo sapiens	21-44
24687403-8	2014	In addition, a newer xanthine oxidoreductase inhibitor, febuxostat, may also be effective in the prevention of calcium stones, as it reduces urinary uric acid excretion.	Uric Acid	149-158	xanthine dehydrogenase	Homo sapiens	21-44
24506204-2	2014	In the present study, we investigated the potential role of xanthine dehydrogenase (XDH) in retinoic acid biosynthesis in human thyroid glandular cells (HTGC).	Tretinoin	92-105	xanthine dehydrogenase	Homo sapiens	84-87
24506204-4	2014	After partial protein purification, the enzyme responsible for retinoic acid biosynthesis was identified and quantified as XDH by immunoassay, by its ability to oxidize xanthine to uric acid and its sensitivity to the inhibitory effect of oxypurinol.	Tretinoin	63-76	xanthine dehydrogenase	Homo sapiens	123-126
24506204-4	2014	After partial protein purification, the enzyme responsible for retinoic acid biosynthesis was identified and quantified as XDH by immunoassay, by its ability to oxidize xanthine to uric acid and its sensitivity to the inhibitory effect of oxypurinol.	Xanthine	169-177	xanthine dehydrogenase	Homo sapiens	123-126
24506204-4	2014	After partial protein purification, the enzyme responsible for retinoic acid biosynthesis was identified and quantified as XDH by immunoassay, by its ability to oxidize xanthine to uric acid and its sensitivity to the inhibitory effect of oxypurinol.	Uric Acid	181-190	xanthine dehydrogenase	Homo sapiens	123-126
24506204-4	2014	After partial protein purification, the enzyme responsible for retinoic acid biosynthesis was identified and quantified as XDH by immunoassay, by its ability to oxidize xanthine to uric acid and its sensitivity to the inhibitory effect of oxypurinol.	Oxypurinol	239-249	xanthine dehydrogenase	Homo sapiens	123-126
24506204-5	2014	The evidence of XDH-driven formation of retinoic acid in HTGC cultures further corroborates the potential role of XDH in retinoic acid biosynthesis in the epithelia.	Tretinoin	40-53	xanthine dehydrogenase	Homo sapiens	16-19
24506204-5	2014	The evidence of XDH-driven formation of retinoic acid in HTGC cultures further corroborates the potential role of XDH in retinoic acid biosynthesis in the epithelia.	Tretinoin	40-53	xanthine dehydrogenase	Homo sapiens	114-117
24506204-5	2014	The evidence of XDH-driven formation of retinoic acid in HTGC cultures further corroborates the potential role of XDH in retinoic acid biosynthesis in the epithelia.	Tretinoin	121-134	xanthine dehydrogenase	Homo sapiens	16-19
24506204-5	2014	The evidence of XDH-driven formation of retinoic acid in HTGC cultures further corroborates the potential role of XDH in retinoic acid biosynthesis in the epithelia.	Tretinoin	121-134	xanthine dehydrogenase	Homo sapiens	114-117
25478314-0	2014	Rhodamine-Appended Bipyridine: XOR and OR Logic Operations Integrated in an Example of Controlled Metal Migration.	Rhodamines	0-9	xanthine dehydrogenase	Homo sapiens	31-34
25478314-0	2014	Rhodamine-Appended Bipyridine: XOR and OR Logic Operations Integrated in an Example of Controlled Metal Migration.	2,2'-Dipyridyl	19-29	xanthine dehydrogenase	Homo sapiens	31-34
25478314-0	2014	Rhodamine-Appended Bipyridine: XOR and OR Logic Operations Integrated in an Example of Controlled Metal Migration.	Metals	98-103	xanthine dehydrogenase	Homo sapiens	31-34
24127160-7	2014	An interesting exception is the xanthine oxido-reductase produced ROS and their role in cardiovascular disease.	Reactive Oxygen Species	66-69	xanthine dehydrogenase	Homo sapiens	32-56
24092361-1	2014	It is known that xanthine oxidoreductase contributes significantly to ischemia/reperfusion injury by generating reactive oxygen species.	Reactive Oxygen Species	112-135	xanthine dehydrogenase	Homo sapiens	17-40
24824603-9	2014	Xanthine dehydrogenase (XDH), which belongs to the family of xanthine oxidoreductases and preferentially reduces nicotinamide adenine dinucleotide (NAD(+)), was shown to contribute to the overall production of the 6TX intermediate as well as the final product 6TUA in the presence of NAD(+) in human liver cytosol.	NAD	113-146	xanthine dehydrogenase	Homo sapiens	0-22
24824603-9	2014	Xanthine dehydrogenase (XDH), which belongs to the family of xanthine oxidoreductases and preferentially reduces nicotinamide adenine dinucleotide (NAD(+)), was shown to contribute to the overall production of the 6TX intermediate as well as the final product 6TUA in the presence of NAD(+) in human liver cytosol.	NAD	113-146	xanthine dehydrogenase	Homo sapiens	24-27
24824603-9	2014	Xanthine dehydrogenase (XDH), which belongs to the family of xanthine oxidoreductases and preferentially reduces nicotinamide adenine dinucleotide (NAD(+)), was shown to contribute to the overall production of the 6TX intermediate as well as the final product 6TUA in the presence of NAD(+) in human liver cytosol.	NAD	148-154	xanthine dehydrogenase	Homo sapiens	0-22
24824603-9	2014	Xanthine dehydrogenase (XDH), which belongs to the family of xanthine oxidoreductases and preferentially reduces nicotinamide adenine dinucleotide (NAD(+)), was shown to contribute to the overall production of the 6TX intermediate as well as the final product 6TUA in the presence of NAD(+) in human liver cytosol.	NAD	148-154	xanthine dehydrogenase	Homo sapiens	24-27
24824603-9	2014	Xanthine dehydrogenase (XDH), which belongs to the family of xanthine oxidoreductases and preferentially reduces nicotinamide adenine dinucleotide (NAD(+)), was shown to contribute to the overall production of the 6TX intermediate as well as the final product 6TUA in the presence of NAD(+) in human liver cytosol.	NAD	284-290	xanthine dehydrogenase	Homo sapiens	0-22
24824603-9	2014	Xanthine dehydrogenase (XDH), which belongs to the family of xanthine oxidoreductases and preferentially reduces nicotinamide adenine dinucleotide (NAD(+)), was shown to contribute to the overall production of the 6TX intermediate as well as the final product 6TUA in the presence of NAD(+) in human liver cytosol.	NAD	284-290	xanthine dehydrogenase	Homo sapiens	24-27
24824603-10	2014	In conclusion, we present evidence that three enzymes, AO, XO, and XDH, contribute to the production of 6TX intermediate, whereas only XO and XDH are involved in the conversion of 6TX to 6TUA in pooled HLC.	6-thioxanthine	104-107	xanthine dehydrogenase	Homo sapiens	67-70
24824603-10	2014	In conclusion, we present evidence that three enzymes, AO, XO, and XDH, contribute to the production of 6TX intermediate, whereas only XO and XDH are involved in the conversion of 6TX to 6TUA in pooled HLC.	6-thioxanthine	180-183	xanthine dehydrogenase	Homo sapiens	142-145
24824603-10	2014	In conclusion, we present evidence that three enzymes, AO, XO, and XDH, contribute to the production of 6TX intermediate, whereas only XO and XDH are involved in the conversion of 6TX to 6TUA in pooled HLC.	6-thiouric acid	187-191	xanthine dehydrogenase	Homo sapiens	142-145
25185415-2	2014	Xanthine oxidoreductase (XOR) is the key enzyme that catalyzes the formation of uric acid.	Uric Acid	80-89	xanthine dehydrogenase	Homo sapiens	0-23
25185415-2	2014	Xanthine oxidoreductase (XOR) is the key enzyme that catalyzes the formation of uric acid.	Uric Acid	80-89	xanthine dehydrogenase	Homo sapiens	25-28
24882753-1	2014	The enzyme xanthine oxidoreductase (XOR) catalyses the last step of purine degradation in the highest uricotelic primates as a rate-limiting enzyme in nucleic acid catabolism.	purine	68-74	xanthine dehydrogenase	Homo sapiens	11-34
24882753-1	2014	The enzyme xanthine oxidoreductase (XOR) catalyses the last step of purine degradation in the highest uricotelic primates as a rate-limiting enzyme in nucleic acid catabolism.	purine	68-74	xanthine dehydrogenase	Homo sapiens	36-39
24603754-2	2014	Reversible conversion of NAD(+) and NADH cofactors was used to perform a XOR logic operation, while biocatalytic hydrolysis of p-nitrophenyl phosphate resulted in an Identity operation working in parallel.	NAD	25-31	xanthine dehydrogenase	Homo sapiens	73-76
24603754-2	2014	Reversible conversion of NAD(+) and NADH cofactors was used to perform a XOR logic operation, while biocatalytic hydrolysis of p-nitrophenyl phosphate resulted in an Identity operation working in parallel.	NAD	36-40	xanthine dehydrogenase	Homo sapiens	73-76
24406683-2	2014	For example, capacity to catalyze the one electron reduction of nitrite (NO2-) to  NO has been reported for hemoglobin, myoglobin and molybdopterin-containing enzymes including xanthine oxidoreductase (XOR) and aldehyde oxidase (AO).	Nitrites	64-71	xanthine dehydrogenase	Homo sapiens	177-200
24406683-2	2014	For example, capacity to catalyze the one electron reduction of nitrite (NO2-) to  NO has been reported for hemoglobin, myoglobin and molybdopterin-containing enzymes including xanthine oxidoreductase (XOR) and aldehyde oxidase (AO).	Nitrites	64-71	xanthine dehydrogenase	Homo sapiens	202-205
24406683-2	2014	For example, capacity to catalyze the one electron reduction of nitrite (NO2-) to  NO has been reported for hemoglobin, myoglobin and molybdopterin-containing enzymes including xanthine oxidoreductase (XOR) and aldehyde oxidase (AO).	Nitrogen Dioxide	73-76	xanthine dehydrogenase	Homo sapiens	177-200
24406683-2	2014	For example, capacity to catalyze the one electron reduction of nitrite (NO2-) to  NO has been reported for hemoglobin, myoglobin and molybdopterin-containing enzymes including xanthine oxidoreductase (XOR) and aldehyde oxidase (AO).	Nitrogen Dioxide	73-76	xanthine dehydrogenase	Homo sapiens	202-205
24406683-4	2014	To this end, XOR inhibition has been accomplished with application of classic pyrazolopyrimidine-based inhibitors allo/oxypurinol or the newly FDA-approved XOR-specific inhibitor, Uloric  (febuxostat).	1H-pyrazolo[4,3-d]pyrimidine	78-96	xanthine dehydrogenase	Homo sapiens	13-16
24406683-4	2014	To this end, XOR inhibition has been accomplished with application of classic pyrazolopyrimidine-based inhibitors allo/oxypurinol or the newly FDA-approved XOR-specific inhibitor, Uloric  (febuxostat).	Oxypurinol	119-129	xanthine dehydrogenase	Homo sapiens	13-16
24406683-4	2014	To this end, XOR inhibition has been accomplished with application of classic pyrazolopyrimidine-based inhibitors allo/oxypurinol or the newly FDA-approved XOR-specific inhibitor, Uloric  (febuxostat).	Febuxostat	189-199	xanthine dehydrogenase	Homo sapiens	13-16
24406683-6	2014	Herein, we characterize the inhibition kinetics of raloxifene for XOR and describe the resultant effects on inhibiting XO-catalyzed  NO formation.	Raloxifene Hydrochloride	51-61	xanthine dehydrogenase	Homo sapiens	66-69
24663591-1	2014	We report the implementation of the XOR and XNOR logical operations using an electro-optic circuit, which is fabricated by CMOS-compatible process in the silicon-on-insulator (SOI) platform.	Silicon	154-161	xanthine dehydrogenase	Homo sapiens	36-39
24357442-7	2014	Further, we have revealed that xanthine oxidoreductase, the enzyme that catalyses the production of uric acid, is present at elevated levels in wound fluid.	Uric Acid	100-109	xanthine dehydrogenase	Homo sapiens	31-54
24127160-8	2014	Allopurinol inhibition of xanthine oxido-reductase was shown to be efficient in some cases of cardiovascular diseases.	Allopurinol	0-11	xanthine dehydrogenase	Homo sapiens	26-50
24127160-9	2014	Another important aspect of xanthine oxido-reductase produced ROS is their antibacterial capacity considered to be of importance with newborns fed on milk rich in this enzyme as well as at the gastrointestinal barrier.	Reactive Oxygen Species	62-65	xanthine dehydrogenase	Homo sapiens	28-52
24127160-10	2014	This ambivalent role of xanthine oxido-reductase justifies this review on the basic enzymatic mechanisms involved, derived ROS production, their role in the above mentioned biological processes and especially the interest of the inhibition of this enzyme as a preventive or curative measure in some cardiovascular pathologies.	Reactive Oxygen Species	123-126	xanthine dehydrogenase	Homo sapiens	24-48
26328123-1	2013	Xanthine dehydrogenase catalyzes the oxidation of hypoxanthine to xanthine and xanthine to uric acid in the final two steps of the purine degradation process.	Hypoxanthine	50-62	xanthine dehydrogenase	Homo sapiens	0-22
26328123-1	2013	Xanthine dehydrogenase catalyzes the oxidation of hypoxanthine to xanthine and xanthine to uric acid in the final two steps of the purine degradation process.	Xanthine	54-62	xanthine dehydrogenase	Homo sapiens	0-22
26328123-1	2013	Xanthine dehydrogenase catalyzes the oxidation of hypoxanthine to xanthine and xanthine to uric acid in the final two steps of the purine degradation process.	Xanthine	66-74	xanthine dehydrogenase	Homo sapiens	0-22
26328123-1	2013	Xanthine dehydrogenase catalyzes the oxidation of hypoxanthine to xanthine and xanthine to uric acid in the final two steps of the purine degradation process.	Uric Acid	91-100	xanthine dehydrogenase	Homo sapiens	0-22
26328123-1	2013	Xanthine dehydrogenase catalyzes the oxidation of hypoxanthine to xanthine and xanthine to uric acid in the final two steps of the purine degradation process.	purine	131-137	xanthine dehydrogenase	Homo sapiens	0-22
23860719-1	2013	In this study we employed self-deposition and competitive or synergistic interactions between metal ions and gold nanoparticles (Au NPs) to develop OR, AND, INHIBIT, and XOR logic gates through regulation of the enzyme-like activity of Au NPs.	Metals	94-99	xanthine dehydrogenase	Homo sapiens	170-173
24206286-3	2013	Generally good performances have been obtained with all three DH functionals, in particular, with xDH-PBE0.	2-(3,5-dihydroxyphenyl)-6-hydroxybenzothiazole	62-64	xanthine dehydrogenase	Homo sapiens	98-101
23929928-2	2013	Febuxostat, a xanthine oxidoreductase inhibitor, is effective in lowering serum urate concentration and urinary uric acid excretion in healthy volunteers and people with gout.	Febuxostat	0-10	xanthine dehydrogenase	Homo sapiens	14-37
23454592-0	2013	Xanthine oxidoreductase-catalyzed reduction of nitrite to nitric oxide: insights regarding where, when and how.	Nitrites	47-54	xanthine dehydrogenase	Homo sapiens	0-23
23454592-0	2013	Xanthine oxidoreductase-catalyzed reduction of nitrite to nitric oxide: insights regarding where, when and how.	Nitric Oxide	58-70	xanthine dehydrogenase	Homo sapiens	0-23
23454592-2	2013	Despite a long standing association between increased XOR activity and negative clinical outcomes, recent reports describe a paradigm shift where XOR mediates beneficial actions by catalyzing the reduction of NO2(-) to NO.	Nitrogen Dioxide	209-212	xanthine dehydrogenase	Homo sapiens	54-57
23454592-2	2013	Despite a long standing association between increased XOR activity and negative clinical outcomes, recent reports describe a paradigm shift where XOR mediates beneficial actions by catalyzing the reduction of NO2(-) to NO.	Nitrogen Dioxide	209-212	xanthine dehydrogenase	Homo sapiens	146-149
23454592-5	2013	As such, information herein serves to link recent reports in which XOR activity has been identified as mediating the beneficial outcomes resulting from nitrite supplementation to a microenvironmental setting where XOR can serve as substantial source of NO.	Nitrites	152-159	xanthine dehydrogenase	Homo sapiens	67-70
23963312-2	2013	The system contains an Au-surface immobilized molecular-beacon molecule that serves as a dual-gate molecule and outputs two series of fluorescence signals following Boolean INH and XOR patterns after interacting with one or two single-stranded DNA molecules as input.	Gold	23-25	xanthine dehydrogenase	Homo sapiens	181-184
23860719-5	2013	Taking advantage of this behavior, we constructed multiplex logic operations-OR, AND, INHIBIT, and XOR logic gates-through regulation of the enzyme-like activity after the introduction of metal ions into the Au NP solution.	Metals	188-193	xanthine dehydrogenase	Homo sapiens	99-102
23772834-1	2013	Utilizing the principles of metal-ion-mediated base pairs (C-Ag-C and T-Hg-T), the pH-sensitive conformational transition of C-rich DNA strand, and the ligand-exchange process triggered by DL-dithiothreitol (DTT), a system of colorimetric logic gates (YES, AND, INHIBIT, and XOR) can be rationally constructed based on the aggregation of the DNA-modified Au NPs.	Dithiothreitol	189-206	xanthine dehydrogenase	Homo sapiens	275-278
23897071-0	2013	Hypertension, nitrate-nitrite, and xanthine oxidoreductase catalyzed nitric oxide generation: pros and cons.	Nitric Oxide	69-81	xanthine dehydrogenase	Homo sapiens	35-58
23681975-3	2013	Thus, the xDH functionals are nonvariational in both the hybrid density functional part and the second-order perturbation part, each of which requires formally to solve a coupled-perturbed KS equation.	ks	189-191	xanthine dehydrogenase	Homo sapiens	10-13
23681975-7	2013	Satisfactory performance of the xDH functionals demonstrates that the extra computer time on top of the conventional KS procedure is well-invested, in particular, when the standard KS functionals and MP2 as well, are problematic.	ks	117-119	xanthine dehydrogenase	Homo sapiens	32-35
23681975-7	2013	Satisfactory performance of the xDH functionals demonstrates that the extra computer time on top of the conventional KS procedure is well-invested, in particular, when the standard KS functionals and MP2 as well, are problematic.	ks	181-183	xanthine dehydrogenase	Homo sapiens	32-35
23380026-4	2013	The enzyme xanthine oxidoreductase (XOR) has been shown to be a source of reactive oxygen species (ROS) in a multitude of diseases (S. Sakao et al., FASEB J.21, 3640-3652; 2007).	Reactive Oxygen Species	74-97	xanthine dehydrogenase	Homo sapiens	36-39
23380026-4	2013	The enzyme xanthine oxidoreductase (XOR) has been shown to be a source of reactive oxygen species (ROS) in a multitude of diseases (S. Sakao et al., FASEB J.21, 3640-3652; 2007).	Reactive Oxygen Species	99-102	xanthine dehydrogenase	Homo sapiens	11-34
23380026-4	2013	The enzyme xanthine oxidoreductase (XOR) has been shown to be a source of reactive oxygen species (ROS) in a multitude of diseases (S. Sakao et al., FASEB J.21, 3640-3652; 2007).	Reactive Oxygen Species	74-97	xanthine dehydrogenase	Homo sapiens	11-34
23380026-4	2013	The enzyme xanthine oxidoreductase (XOR) has been shown to be a source of reactive oxygen species (ROS) in a multitude of diseases (S. Sakao et al., FASEB J.21, 3640-3652; 2007).	Reactive Oxygen Species	99-102	xanthine dehydrogenase	Homo sapiens	36-39
23380026-5	2013	The contribution of XOR to CS-induced apoptosis is not well defined.	Cesium	27-29	xanthine dehydrogenase	Homo sapiens	20-23
23380026-8	2013	We also demonstrate that exogenous XOR is sufficient to increase p53 expression and induce apoptosis, suggesting that XOR is an upstream mediator of p53 in CS-induced EC apoptosis.	Cesium	156-158	xanthine dehydrogenase	Homo sapiens	35-38
23380026-8	2013	We also demonstrate that exogenous XOR is sufficient to increase p53 expression and induce apoptosis, suggesting that XOR is an upstream mediator of p53 in CS-induced EC apoptosis.	Cesium	156-158	xanthine dehydrogenase	Homo sapiens	118-121
23380026-10	2013	In conclusion, CS increases XOR expression, and the enzyme is both sufficient and necessary for p53 induction and CS-induced EC apoptosis.	Cesium	15-17	xanthine dehydrogenase	Homo sapiens	28-31
24024171-1	2013	Nearly 30 years have passed since the discovery of xanthine oxidoreductase (XOR) as a critical source of reactive species in ischemia/reperfusion injury.	reactive species	105-121	xanthine dehydrogenase	Homo sapiens	51-74
23425554-0	2013	Direct energy conversion from xylose using xylose dehydrogenase surface displayed bacteria based enzymatic biofuel cell.	Xylose	30-36	xanthine dehydrogenase	Homo sapiens	43-63
23425554-2	2013	Here we present the first report on the direct energy conversion from xylose achieved by using novel xylose dehydrogenase (XDH) surface displayed bacteria (XDH-bacteria) based enzymatic biofuel cell.	Xylose	70-76	xanthine dehydrogenase	Homo sapiens	101-121
23425554-2	2013	Here we present the first report on the direct energy conversion from xylose achieved by using novel xylose dehydrogenase (XDH) surface displayed bacteria (XDH-bacteria) based enzymatic biofuel cell.	Xylose	70-76	xanthine dehydrogenase	Homo sapiens	123-126
24024171-1	2013	Nearly 30 years have passed since the discovery of xanthine oxidoreductase (XOR) as a critical source of reactive species in ischemia/reperfusion injury.	reactive species	105-121	xanthine dehydrogenase	Homo sapiens	76-79
23685841-4	2013	We found that type I IFN supports the upregulation of xanthine dehydrogenase, which metabolizes the xanthine accumulating in infected erythrocytes to uric acid.	Uric Acid	150-159	xanthine dehydrogenase	Homo sapiens	54-76
23589565-5	2013	This effect was virtually abolished by the xanthine oxidoreductase (XOR) inhibitor, allopurinol, and associated with hypertension-specific XOR-dependent nitrite reductase activity localized to the erythrocyte but not the blood vessel wall.	Allopurinol	84-95	xanthine dehydrogenase	Homo sapiens	43-66
23589565-5	2013	This effect was virtually abolished by the xanthine oxidoreductase (XOR) inhibitor, allopurinol, and associated with hypertension-specific XOR-dependent nitrite reductase activity localized to the erythrocyte but not the blood vessel wall.	Allopurinol	84-95	xanthine dehydrogenase	Homo sapiens	68-71
23589565-9	2013	Our observations demonstrate the improved efficacy of inorganic nitrate and nitrite in hypertension as a consequence of increased erythrocytic XOR nitrite reductase activity and support the concept of dietary nitrate supplementation as an effective, but simple and inexpensive, antihypertensive strategy.	punky blue	54-71	xanthine dehydrogenase	Homo sapiens	143-146
23589565-9	2013	Our observations demonstrate the improved efficacy of inorganic nitrate and nitrite in hypertension as a consequence of increased erythrocytic XOR nitrite reductase activity and support the concept of dietary nitrate supplementation as an effective, but simple and inexpensive, antihypertensive strategy.	Nitrites	76-83	xanthine dehydrogenase	Homo sapiens	143-146
23589565-9	2013	Our observations demonstrate the improved efficacy of inorganic nitrate and nitrite in hypertension as a consequence of increased erythrocytic XOR nitrite reductase activity and support the concept of dietary nitrate supplementation as an effective, but simple and inexpensive, antihypertensive strategy.	Nitrates	64-71	xanthine dehydrogenase	Homo sapiens	143-146
22900756-9	2013	In particular, ROS production by the mitochondrial electron transport chain, NADPH oxidase, xanthine oxidoreductase, and cytochrome P450 will be addressed.	Reactive Oxygen Species	15-18	xanthine dehydrogenase	Homo sapiens	92-115
23202346-1	2013	In this paper, we first report the construction of Nafion/glucose oxidase (GOD)/xylose dehydrogenase displayed bacteria (XDH-bacteria)/multiwalled carbon nanotubes (MWNTs) modified electrode for simultaneous voltammetric determination of D-glucose and D-xylose.	Glucose	238-247	xanthine dehydrogenase	Homo sapiens	121-124
23202346-1	2013	In this paper, we first report the construction of Nafion/glucose oxidase (GOD)/xylose dehydrogenase displayed bacteria (XDH-bacteria)/multiwalled carbon nanotubes (MWNTs) modified electrode for simultaneous voltammetric determination of D-glucose and D-xylose.	Xylose	252-260	xanthine dehydrogenase	Homo sapiens	121-124
23202346-4	2013	In the mixture solution of D-glucose and D-xylose containing coenzyme NAD+ (the oxidized form of nicotinamide adenine dinucleotide), the Nafion/GOD/XDH-bacteria/MWNTs modified electrode exhibited quasi-reversible oxidation-reduction peak at -0.5 V (vs. saturated calomel electrode, SCE) originating from the catalytic oxidation of D-glucose, and oxidation peak at +0.55 V(vs. SCE) responding to the oxidation of NADH (the reduced form of nicotinamide adenine dinucleotide) by the carbon nanotubes, where NADH is the resultant product of coenzyme NAD+ involved in the catalysis of D-xylose by XDH-displayed bacteria.	Glucose	27-36	xanthine dehydrogenase	Homo sapiens	148-151
23202346-4	2013	In the mixture solution of D-glucose and D-xylose containing coenzyme NAD+ (the oxidized form of nicotinamide adenine dinucleotide), the Nafion/GOD/XDH-bacteria/MWNTs modified electrode exhibited quasi-reversible oxidation-reduction peak at -0.5 V (vs. saturated calomel electrode, SCE) originating from the catalytic oxidation of D-glucose, and oxidation peak at +0.55 V(vs. SCE) responding to the oxidation of NADH (the reduced form of nicotinamide adenine dinucleotide) by the carbon nanotubes, where NADH is the resultant product of coenzyme NAD+ involved in the catalysis of D-xylose by XDH-displayed bacteria.	Xylose	41-49	xanthine dehydrogenase	Homo sapiens	148-151
23202346-4	2013	In the mixture solution of D-glucose and D-xylose containing coenzyme NAD+ (the oxidized form of nicotinamide adenine dinucleotide), the Nafion/GOD/XDH-bacteria/MWNTs modified electrode exhibited quasi-reversible oxidation-reduction peak at -0.5 V (vs. saturated calomel electrode, SCE) originating from the catalytic oxidation of D-glucose, and oxidation peak at +0.55 V(vs. SCE) responding to the oxidation of NADH (the reduced form of nicotinamide adenine dinucleotide) by the carbon nanotubes, where NADH is the resultant product of coenzyme NAD+ involved in the catalysis of D-xylose by XDH-displayed bacteria.	NAD	97-130	xanthine dehydrogenase	Homo sapiens	148-151
23202346-4	2013	In the mixture solution of D-glucose and D-xylose containing coenzyme NAD+ (the oxidized form of nicotinamide adenine dinucleotide), the Nafion/GOD/XDH-bacteria/MWNTs modified electrode exhibited quasi-reversible oxidation-reduction peak at -0.5 V (vs. saturated calomel electrode, SCE) originating from the catalytic oxidation of D-glucose, and oxidation peak at +0.55 V(vs. SCE) responding to the oxidation of NADH (the reduced form of nicotinamide adenine dinucleotide) by the carbon nanotubes, where NADH is the resultant product of coenzyme NAD+ involved in the catalysis of D-xylose by XDH-displayed bacteria.	NAD	97-130	xanthine dehydrogenase	Homo sapiens	592-595
23086295-9	2013	While vibroX increased the expression of hexokinase II, xanthine dehydrogenase, and manganese superoxide dismutase mRNA, there were no changes in these transcripts after RES.	vibrox	6-12	xanthine dehydrogenase	Homo sapiens	56-78
23116398-1	2013	Xanthine oxidoreductase (XOR), a complex flavoprotein, catalyzes the metabolic reactions leading from hypoxanthine to xanthine and from xanthine to urate, and both reactions take place at the molybdenum cofactor.	Uric Acid	148-153	xanthine dehydrogenase	Homo sapiens	25-28
23116398-1	2013	Xanthine oxidoreductase (XOR), a complex flavoprotein, catalyzes the metabolic reactions leading from hypoxanthine to xanthine and from xanthine to urate, and both reactions take place at the molybdenum cofactor.	Hypoxanthine	102-114	xanthine dehydrogenase	Homo sapiens	0-23
23116398-1	2013	Xanthine oxidoreductase (XOR), a complex flavoprotein, catalyzes the metabolic reactions leading from hypoxanthine to xanthine and from xanthine to urate, and both reactions take place at the molybdenum cofactor.	Hypoxanthine	102-114	xanthine dehydrogenase	Homo sapiens	25-28
23116398-1	2013	Xanthine oxidoreductase (XOR), a complex flavoprotein, catalyzes the metabolic reactions leading from hypoxanthine to xanthine and from xanthine to urate, and both reactions take place at the molybdenum cofactor.	Xanthine	106-114	xanthine dehydrogenase	Homo sapiens	0-23
23116398-1	2013	Xanthine oxidoreductase (XOR), a complex flavoprotein, catalyzes the metabolic reactions leading from hypoxanthine to xanthine and from xanthine to urate, and both reactions take place at the molybdenum cofactor.	Xanthine	106-114	xanthine dehydrogenase	Homo sapiens	25-28
23116398-1	2013	Xanthine oxidoreductase (XOR), a complex flavoprotein, catalyzes the metabolic reactions leading from hypoxanthine to xanthine and from xanthine to urate, and both reactions take place at the molybdenum cofactor.	Xanthine	118-126	xanthine dehydrogenase	Homo sapiens	0-23
23116398-1	2013	Xanthine oxidoreductase (XOR), a complex flavoprotein, catalyzes the metabolic reactions leading from hypoxanthine to xanthine and from xanthine to urate, and both reactions take place at the molybdenum cofactor.	Xanthine	118-126	xanthine dehydrogenase	Homo sapiens	25-28
23116398-1	2013	Xanthine oxidoreductase (XOR), a complex flavoprotein, catalyzes the metabolic reactions leading from hypoxanthine to xanthine and from xanthine to urate, and both reactions take place at the molybdenum cofactor.	Uric Acid	148-153	xanthine dehydrogenase	Homo sapiens	0-23
23286293-1	2013	Xanthine oxidoreductase (XOR) catalyzes the final two reactions that lead to uric acid formation.	Uric Acid	77-86	xanthine dehydrogenase	Homo sapiens	0-23
23286293-1	2013	Xanthine oxidoreductase (XOR) catalyzes the final two reactions that lead to uric acid formation.	Uric Acid	77-86	xanthine dehydrogenase	Homo sapiens	25-28
23116398-3	2013	We review the chemical nature and reaction mechanisms of the molybdenum cofactor of XOR, focusing on molybdenum-dependent reactions of actual or potential medical importance, including nitric oxide (NO) synthesis.	Nitric Oxide	185-197	xanthine dehydrogenase	Homo sapiens	84-87
23116398-4	2013	It is now generally accepted that XOR transfers the water-exchangeable -OH ligand of the molybdenum atom to the substrate.	Water	52-57	xanthine dehydrogenase	Homo sapiens	34-37
23116398-4	2013	It is now generally accepted that XOR transfers the water-exchangeable -OH ligand of the molybdenum atom to the substrate.	Molybdenum	89-99	xanthine dehydrogenase	Homo sapiens	34-37
23116398-6	2013	Although formation of NO from nitrite or formation of xanthine from urate by XOR ischemically feasible, it is not yet clear whether these reactions have any physiological significance since the reactions are catalyzed at a slow rate even under anaerobic conditions.	Xanthine	54-62	xanthine dehydrogenase	Homo sapiens	77-80
23116398-6	2013	Although formation of NO from nitrite or formation of xanthine from urate by XOR ischemically feasible, it is not yet clear whether these reactions have any physiological significance since the reactions are catalyzed at a slow rate even under anaerobic conditions.	Uric Acid	68-73	xanthine dehydrogenase	Homo sapiens	77-80
22401856-7	2012	Many canonical ROS and NO signaling pathways are simultaneously disrupted in PAH, with increased expression of nicotinamide adenine dinucleotide phosphate (NADPH) oxidases and xanthine oxidoreductase, uncoupling of endothelial NO synthase (eNOS), and reduction in mitochondrial number, as well as impaired mitochondrial function.	Reactive Oxygen Species	15-18	xanthine dehydrogenase	Homo sapiens	176-199
23203137-1	2012	Xanthine oxidoreductase (XOR) catalyzes the conversion of hypoxanthine to xanthine and xanthine to uric acid with concomitant reduction of either NAD+ or O(2).	Hypoxanthine	58-70	xanthine dehydrogenase	Homo sapiens	0-23
23203137-1	2012	Xanthine oxidoreductase (XOR) catalyzes the conversion of hypoxanthine to xanthine and xanthine to uric acid with concomitant reduction of either NAD+ or O(2).	Hypoxanthine	58-70	xanthine dehydrogenase	Homo sapiens	25-28
23203137-1	2012	Xanthine oxidoreductase (XOR) catalyzes the conversion of hypoxanthine to xanthine and xanthine to uric acid with concomitant reduction of either NAD+ or O(2).	Xanthine	62-70	xanthine dehydrogenase	Homo sapiens	0-23
23203137-1	2012	Xanthine oxidoreductase (XOR) catalyzes the conversion of hypoxanthine to xanthine and xanthine to uric acid with concomitant reduction of either NAD+ or O(2).	Xanthine	62-70	xanthine dehydrogenase	Homo sapiens	25-28
23203137-1	2012	Xanthine oxidoreductase (XOR) catalyzes the conversion of hypoxanthine to xanthine and xanthine to uric acid with concomitant reduction of either NAD+ or O(2).	Xanthine	74-82	xanthine dehydrogenase	Homo sapiens	0-23
23203137-1	2012	Xanthine oxidoreductase (XOR) catalyzes the conversion of hypoxanthine to xanthine and xanthine to uric acid with concomitant reduction of either NAD+ or O(2).	Xanthine	74-82	xanthine dehydrogenase	Homo sapiens	25-28
23203137-1	2012	Xanthine oxidoreductase (XOR) catalyzes the conversion of hypoxanthine to xanthine and xanthine to uric acid with concomitant reduction of either NAD+ or O(2).	Uric Acid	99-108	xanthine dehydrogenase	Homo sapiens	0-23
23203137-1	2012	Xanthine oxidoreductase (XOR) catalyzes the conversion of hypoxanthine to xanthine and xanthine to uric acid with concomitant reduction of either NAD+ or O(2).	Uric Acid	99-108	xanthine dehydrogenase	Homo sapiens	25-28
23203137-1	2012	Xanthine oxidoreductase (XOR) catalyzes the conversion of hypoxanthine to xanthine and xanthine to uric acid with concomitant reduction of either NAD+ or O(2).	NAD	146-150	xanthine dehydrogenase	Homo sapiens	0-23
23203137-1	2012	Xanthine oxidoreductase (XOR) catalyzes the conversion of hypoxanthine to xanthine and xanthine to uric acid with concomitant reduction of either NAD+ or O(2).	NAD	146-150	xanthine dehydrogenase	Homo sapiens	25-28
23203137-1	2012	Xanthine oxidoreductase (XOR) catalyzes the conversion of hypoxanthine to xanthine and xanthine to uric acid with concomitant reduction of either NAD+ or O(2).	o(2)	154-158	xanthine dehydrogenase	Homo sapiens	0-23
23203137-1	2012	Xanthine oxidoreductase (XOR) catalyzes the conversion of hypoxanthine to xanthine and xanthine to uric acid with concomitant reduction of either NAD+ or O(2).	o(2)	154-158	xanthine dehydrogenase	Homo sapiens	25-28
23203137-3	2012	Human diseases associated with genetically determined dysfunction of XOR are termed xanthinuria, because of the excretion of xanthine in urine.	Xanthine	125-133	xanthine dehydrogenase	Homo sapiens	69-72
22927383-5	2012	Enzymes containing a single pyranopterin belong to either the xanthine dehydrogenase (XDH) or sulfite oxidase (SUOX) families, and these have pyranopterin conformations similar to those predicted for tetrahydro and dihydro forms, respectively.	pyranopterin	28-40	xanthine dehydrogenase	Homo sapiens	62-84
22927383-5	2012	Enzymes containing a single pyranopterin belong to either the xanthine dehydrogenase (XDH) or sulfite oxidase (SUOX) families, and these have pyranopterin conformations similar to those predicted for tetrahydro and dihydro forms, respectively.	pyranopterin	28-40	xanthine dehydrogenase	Homo sapiens	86-89
22927383-5	2012	Enzymes containing a single pyranopterin belong to either the xanthine dehydrogenase (XDH) or sulfite oxidase (SUOX) families, and these have pyranopterin conformations similar to those predicted for tetrahydro and dihydro forms, respectively.	pyranopterin	142-154	xanthine dehydrogenase	Homo sapiens	62-84
22927383-5	2012	Enzymes containing a single pyranopterin belong to either the xanthine dehydrogenase (XDH) or sulfite oxidase (SUOX) families, and these have pyranopterin conformations similar to those predicted for tetrahydro and dihydro forms, respectively.	pyranopterin	142-154	xanthine dehydrogenase	Homo sapiens	86-89
22798524-8	2012	Xanthine oxidoreductase inhibition abolished the difference in superoxide production but did not affect myocardial function in either group.	Superoxides	63-73	xanthine dehydrogenase	Homo sapiens	0-23
22495427-0	2012	Polymorphism of genes involved in purine metabolism (XDH, AOX1, MOCOS) in kidney transplant recipients receiving azathioprine.	purine	34-40	xanthine dehydrogenase	Homo sapiens	53-56
22495427-0	2012	Polymorphism of genes involved in purine metabolism (XDH, AOX1, MOCOS) in kidney transplant recipients receiving azathioprine.	Azathioprine	113-125	xanthine dehydrogenase	Homo sapiens	53-56
22495427-1	2012	BACKGROUND: Xanthine dehydrogenase (XDH), aldehyde oxidase1 (AOX1), and molybdenum cofactor sulfurase (MOCOS) are enzymes involved in purine metabolism.	purine	134-140	xanthine dehydrogenase	Homo sapiens	12-34
22495427-1	2012	BACKGROUND: Xanthine dehydrogenase (XDH), aldehyde oxidase1 (AOX1), and molybdenum cofactor sulfurase (MOCOS) are enzymes involved in purine metabolism.	purine	134-140	xanthine dehydrogenase	Homo sapiens	36-39
22495427-2	2012	The aim of this study was to investigate single nucleotide polymorphisms (SNPs) in XDH, AOX1, and MOCOS genes in relation to clinical parameters and risk of drug side effects in a cohort of kidney transplant recipients treated with azathioprine (AZA) as a part of standard immunosuppressive regimen.	Azathioprine	232-244	xanthine dehydrogenase	Homo sapiens	83-86
22495427-2	2012	The aim of this study was to investigate single nucleotide polymorphisms (SNPs) in XDH, AOX1, and MOCOS genes in relation to clinical parameters and risk of drug side effects in a cohort of kidney transplant recipients treated with azathioprine (AZA) as a part of standard immunosuppressive regimen.	Azathioprine	246-249	xanthine dehydrogenase	Homo sapiens	83-86
22425780-3	2012	Nitrite signaling has been described as NO dependent activation mediated by reactions with deoxygenated redox active hemoproteins, such as hemoglobin, myoglobin, neuroglobin, xanthine oxidoreductase (XO) and NO synthase at low pH and oxygen tension.	Nitrites	0-7	xanthine dehydrogenase	Homo sapiens	175-198
23091148-0	2012	The effects of allopurinol, uric acid, and inosine administration on xanthine oxidoreductase activity and uric acid concentrations in broilers.	Inosine	43-50	xanthine dehydrogenase	Homo sapiens	69-92
23091148-1	2012	The purpose of these studies was to determine the effects of uric acid (UA) and inosine administration on xanthine oxidoreductase activity in broilers.	Uric Acid	61-70	xanthine dehydrogenase	Homo sapiens	106-129
23091148-1	2012	The purpose of these studies was to determine the effects of uric acid (UA) and inosine administration on xanthine oxidoreductase activity in broilers.	Uric Acid	72-74	xanthine dehydrogenase	Homo sapiens	106-129
23091148-1	2012	The purpose of these studies was to determine the effects of uric acid (UA) and inosine administration on xanthine oxidoreductase activity in broilers.	Inosine	80-87	xanthine dehydrogenase	Homo sapiens	106-129
23091148-5	2012	Whereas xanthine oxidoreductase (XOR) activity in the liver (LXOR) was reduced (P < 0.05) by allopurinol treatment, XOR activity in the kidney (KXOR) was not affected (P = 0.05).	Allopurinol	96-107	xanthine dehydrogenase	Homo sapiens	8-31
23091148-5	2012	Whereas xanthine oxidoreductase (XOR) activity in the liver (LXOR) was reduced (P < 0.05) by allopurinol treatment, XOR activity in the kidney (KXOR) was not affected (P = 0.05).	Allopurinol	96-107	xanthine dehydrogenase	Homo sapiens	33-36
23091148-5	2012	Whereas xanthine oxidoreductase (XOR) activity in the liver (LXOR) was reduced (P < 0.05) by allopurinol treatment, XOR activity in the kidney (KXOR) was not affected (P = 0.05).	Allopurinol	96-107	xanthine dehydrogenase	Homo sapiens	62-65
22678977-1	2012	Xanthine dehydrogenase (XDH), also known as xanthine oxidoreductase (XOR), has long been recognized as the key enzyme in the catabolism of purines, oxidizing hypoxanthine into xanthine and then xanthine into uric acid.	Purines	139-146	xanthine dehydrogenase	Homo sapiens	0-22
22678977-1	2012	Xanthine dehydrogenase (XDH), also known as xanthine oxidoreductase (XOR), has long been recognized as the key enzyme in the catabolism of purines, oxidizing hypoxanthine into xanthine and then xanthine into uric acid.	Purines	139-146	xanthine dehydrogenase	Homo sapiens	24-27
22678977-1	2012	Xanthine dehydrogenase (XDH), also known as xanthine oxidoreductase (XOR), has long been recognized as the key enzyme in the catabolism of purines, oxidizing hypoxanthine into xanthine and then xanthine into uric acid.	Purines	139-146	xanthine dehydrogenase	Homo sapiens	44-67
22678977-1	2012	Xanthine dehydrogenase (XDH), also known as xanthine oxidoreductase (XOR), has long been recognized as the key enzyme in the catabolism of purines, oxidizing hypoxanthine into xanthine and then xanthine into uric acid.	Purines	139-146	xanthine dehydrogenase	Homo sapiens	69-72
22678977-1	2012	Xanthine dehydrogenase (XDH), also known as xanthine oxidoreductase (XOR), has long been recognized as the key enzyme in the catabolism of purines, oxidizing hypoxanthine into xanthine and then xanthine into uric acid.	Hypoxanthine	158-170	xanthine dehydrogenase	Homo sapiens	0-22
22678977-1	2012	Xanthine dehydrogenase (XDH), also known as xanthine oxidoreductase (XOR), has long been recognized as the key enzyme in the catabolism of purines, oxidizing hypoxanthine into xanthine and then xanthine into uric acid.	Hypoxanthine	158-170	xanthine dehydrogenase	Homo sapiens	24-27
22678977-1	2012	Xanthine dehydrogenase (XDH), also known as xanthine oxidoreductase (XOR), has long been recognized as the key enzyme in the catabolism of purines, oxidizing hypoxanthine into xanthine and then xanthine into uric acid.	Hypoxanthine	158-170	xanthine dehydrogenase	Homo sapiens	44-67
22678977-1	2012	Xanthine dehydrogenase (XDH), also known as xanthine oxidoreductase (XOR), has long been recognized as the key enzyme in the catabolism of purines, oxidizing hypoxanthine into xanthine and then xanthine into uric acid.	Hypoxanthine	158-170	xanthine dehydrogenase	Homo sapiens	69-72
22678977-1	2012	Xanthine dehydrogenase (XDH), also known as xanthine oxidoreductase (XOR), has long been recognized as the key enzyme in the catabolism of purines, oxidizing hypoxanthine into xanthine and then xanthine into uric acid.	Xanthine	44-52	xanthine dehydrogenase	Homo sapiens	0-22
22678977-1	2012	Xanthine dehydrogenase (XDH), also known as xanthine oxidoreductase (XOR), has long been recognized as the key enzyme in the catabolism of purines, oxidizing hypoxanthine into xanthine and then xanthine into uric acid.	Xanthine	44-52	xanthine dehydrogenase	Homo sapiens	24-27
22678977-1	2012	Xanthine dehydrogenase (XDH), also known as xanthine oxidoreductase (XOR), has long been recognized as the key enzyme in the catabolism of purines, oxidizing hypoxanthine into xanthine and then xanthine into uric acid.	Xanthine	44-52	xanthine dehydrogenase	Homo sapiens	69-72
22678977-1	2012	Xanthine dehydrogenase (XDH), also known as xanthine oxidoreductase (XOR), has long been recognized as the key enzyme in the catabolism of purines, oxidizing hypoxanthine into xanthine and then xanthine into uric acid.	Xanthine	162-170	xanthine dehydrogenase	Homo sapiens	0-22
22678977-1	2012	Xanthine dehydrogenase (XDH), also known as xanthine oxidoreductase (XOR), has long been recognized as the key enzyme in the catabolism of purines, oxidizing hypoxanthine into xanthine and then xanthine into uric acid.	Xanthine	162-170	xanthine dehydrogenase	Homo sapiens	24-27
22678977-1	2012	Xanthine dehydrogenase (XDH), also known as xanthine oxidoreductase (XOR), has long been recognized as the key enzyme in the catabolism of purines, oxidizing hypoxanthine into xanthine and then xanthine into uric acid.	Xanthine	162-170	xanthine dehydrogenase	Homo sapiens	44-67
22678977-1	2012	Xanthine dehydrogenase (XDH), also known as xanthine oxidoreductase (XOR), has long been recognized as the key enzyme in the catabolism of purines, oxidizing hypoxanthine into xanthine and then xanthine into uric acid.	Xanthine	162-170	xanthine dehydrogenase	Homo sapiens	69-72
22678977-1	2012	Xanthine dehydrogenase (XDH), also known as xanthine oxidoreductase (XOR), has long been recognized as the key enzyme in the catabolism of purines, oxidizing hypoxanthine into xanthine and then xanthine into uric acid.	Uric Acid	208-217	xanthine dehydrogenase	Homo sapiens	0-22
22678977-1	2012	Xanthine dehydrogenase (XDH), also known as xanthine oxidoreductase (XOR), has long been recognized as the key enzyme in the catabolism of purines, oxidizing hypoxanthine into xanthine and then xanthine into uric acid.	Uric Acid	208-217	xanthine dehydrogenase	Homo sapiens	24-27
22678977-1	2012	Xanthine dehydrogenase (XDH), also known as xanthine oxidoreductase (XOR), has long been recognized as the key enzyme in the catabolism of purines, oxidizing hypoxanthine into xanthine and then xanthine into uric acid.	Uric Acid	208-217	xanthine dehydrogenase	Homo sapiens	44-67
22678977-1	2012	Xanthine dehydrogenase (XDH), also known as xanthine oxidoreductase (XOR), has long been recognized as the key enzyme in the catabolism of purines, oxidizing hypoxanthine into xanthine and then xanthine into uric acid.	Uric Acid	208-217	xanthine dehydrogenase	Homo sapiens	69-72
22714146-1	2012	We report the implementation of the XOR and XNOR operations using an electro-optic directed logic circuit based on two cascaded silicon microring resonators (MRRs), which are both modulated through the plasma dispersion effect.	Silicon	128-135	xanthine dehydrogenase	Homo sapiens	36-39
22398104-2	2012	Its immediate precursor, xanthine, is converted to uric acid by an enzymatic reaction involving xanthine oxidoreductase.	Xanthine	25-33	xanthine dehydrogenase	Homo sapiens	96-119
22398104-2	2012	Its immediate precursor, xanthine, is converted to uric acid by an enzymatic reaction involving xanthine oxidoreductase.	Uric Acid	51-60	xanthine dehydrogenase	Homo sapiens	96-119
22398104-5	2012	In this paper, the molecular pattern of uric acid formation, its possible deleterious effects, as well as the involvement of xanthine oxidoreductase in reactive oxygen species generation are critically discussed.	Reactive Oxygen Species	152-175	xanthine dehydrogenase	Homo sapiens	125-148
22398104-7	2012	Recent studies have renewed attention to the xanthine oxidoreductase system, since xanthine oxidoreductase inhibitors, such as allopurinol and oxypurinol, would be capable of preventing atherosclerosis progression by reducing endothelial dysfunction.	Allopurinol	127-138	xanthine dehydrogenase	Homo sapiens	45-68
22398104-7	2012	Recent studies have renewed attention to the xanthine oxidoreductase system, since xanthine oxidoreductase inhibitors, such as allopurinol and oxypurinol, would be capable of preventing atherosclerosis progression by reducing endothelial dysfunction.	Allopurinol	127-138	xanthine dehydrogenase	Homo sapiens	83-106
22398104-7	2012	Recent studies have renewed attention to the xanthine oxidoreductase system, since xanthine oxidoreductase inhibitors, such as allopurinol and oxypurinol, would be capable of preventing atherosclerosis progression by reducing endothelial dysfunction.	Oxypurinol	143-153	xanthine dehydrogenase	Homo sapiens	45-68
22398104-7	2012	Recent studies have renewed attention to the xanthine oxidoreductase system, since xanthine oxidoreductase inhibitors, such as allopurinol and oxypurinol, would be capable of preventing atherosclerosis progression by reducing endothelial dysfunction.	Oxypurinol	143-153	xanthine dehydrogenase	Homo sapiens	83-106
22404107-9	2012	From the kinetic data, and the levels of AO and NADH, O(2)( -) production was estimated to be ~89 and ~4 nM/s in liver and heart, respectively, much higher than that estimated for XOR under similar conditions.	Superoxides	54-62	xanthine dehydrogenase	Homo sapiens	180-183
22145797-3	2012	In spite of identical protein primary structures, the redox potential difference between XDH and XO for the flavin semiquinone/hydroquinone pair (E(sq/hq)) is ~170 mV, a striking difference.	flavin semiquinone	108-126	xanthine dehydrogenase	Homo sapiens	89-92
22044687-1	2012	OBJECTIVE: Xanthine oxidoreductase (XOR) is a key enzyme in the degradation of DNA, RNA and high-energy phosphates.	Phosphates	104-114	xanthine dehydrogenase	Homo sapiens	11-34
22044687-1	2012	OBJECTIVE: Xanthine oxidoreductase (XOR) is a key enzyme in the degradation of DNA, RNA and high-energy phosphates.	Phosphates	104-114	xanthine dehydrogenase	Homo sapiens	36-39
22145797-9	2012	Instead, the positive charge of the NAD(+) ring, deprotonation of Asp429, and capping of the bulk surface of the flavin by the NAD(+) molecule all contribute to altering E(sq/hq) upon NAD(+) binding to XDH.	4,6-dinitro-o-cresol	113-119	xanthine dehydrogenase	Homo sapiens	202-205
22145797-9	2012	Instead, the positive charge of the NAD(+) ring, deprotonation of Asp429, and capping of the bulk surface of the flavin by the NAD(+) molecule all contribute to altering E(sq/hq) upon NAD(+) binding to XDH.	NAD	127-133	xanthine dehydrogenase	Homo sapiens	202-205
22145797-3	2012	In spite of identical protein primary structures, the redox potential difference between XDH and XO for the flavin semiquinone/hydroquinone pair (E(sq/hq)) is ~170 mV, a striking difference.	hydroquinone	127-139	xanthine dehydrogenase	Homo sapiens	89-92
22145797-9	2012	Instead, the positive charge of the NAD(+) ring, deprotonation of Asp429, and capping of the bulk surface of the flavin by the NAD(+) molecule all contribute to altering E(sq/hq) upon NAD(+) binding to XDH.	NAD	127-133	xanthine dehydrogenase	Homo sapiens	202-205
22145797-5	2012	In XDH (without NAD(+)), however, the redox potential of the electron donor FeS-II is 180 mV higher than that for the acceptor flavin, yielding an energetically uphill ET.	fes-ii	76-82	xanthine dehydrogenase	Homo sapiens	3-6
22145797-5	2012	In XDH (without NAD(+)), however, the redox potential of the electron donor FeS-II is 180 mV higher than that for the acceptor flavin, yielding an energetically uphill ET.	4,6-dinitro-o-cresol	127-133	xanthine dehydrogenase	Homo sapiens	3-6
22145797-6	2012	On the basis of new 1.65, 2.3, 1.9, and 2.2 A resolution crystal structures for XDH, XO, the NAD(+)- and NADH-complexed XDH, E(sq/hq) were calculated to better understand how the enzyme activates an ET from FeS-II to flavin.	NAD	93-99	xanthine dehydrogenase	Homo sapiens	80-83
22145797-6	2012	On the basis of new 1.65, 2.3, 1.9, and 2.2 A resolution crystal structures for XDH, XO, the NAD(+)- and NADH-complexed XDH, E(sq/hq) were calculated to better understand how the enzyme activates an ET from FeS-II to flavin.	NAD	93-99	xanthine dehydrogenase	Homo sapiens	120-123
22145797-6	2012	On the basis of new 1.65, 2.3, 1.9, and 2.2 A resolution crystal structures for XDH, XO, the NAD(+)- and NADH-complexed XDH, E(sq/hq) were calculated to better understand how the enzyme activates an ET from FeS-II to flavin.	NAD	105-109	xanthine dehydrogenase	Homo sapiens	80-83
22145797-6	2012	On the basis of new 1.65, 2.3, 1.9, and 2.2 A resolution crystal structures for XDH, XO, the NAD(+)- and NADH-complexed XDH, E(sq/hq) were calculated to better understand how the enzyme activates an ET from FeS-II to flavin.	NAD	105-109	xanthine dehydrogenase	Homo sapiens	120-123
22145797-6	2012	On the basis of new 1.65, 2.3, 1.9, and 2.2 A resolution crystal structures for XDH, XO, the NAD(+)- and NADH-complexed XDH, E(sq/hq) were calculated to better understand how the enzyme activates an ET from FeS-II to flavin.	fes-ii	207-213	xanthine dehydrogenase	Homo sapiens	80-83
22145797-6	2012	On the basis of new 1.65, 2.3, 1.9, and 2.2 A resolution crystal structures for XDH, XO, the NAD(+)- and NADH-complexed XDH, E(sq/hq) were calculated to better understand how the enzyme activates an ET from FeS-II to flavin.	fes-ii	207-213	xanthine dehydrogenase	Homo sapiens	120-123
22145797-6	2012	On the basis of new 1.65, 2.3, 1.9, and 2.2 A resolution crystal structures for XDH, XO, the NAD(+)- and NADH-complexed XDH, E(sq/hq) were calculated to better understand how the enzyme activates an ET from FeS-II to flavin.	4,6-dinitro-o-cresol	217-223	xanthine dehydrogenase	Homo sapiens	80-83
22145797-6	2012	On the basis of new 1.65, 2.3, 1.9, and 2.2 A resolution crystal structures for XDH, XO, the NAD(+)- and NADH-complexed XDH, E(sq/hq) were calculated to better understand how the enzyme activates an ET from FeS-II to flavin.	4,6-dinitro-o-cresol	217-223	xanthine dehydrogenase	Homo sapiens	120-123
22145797-7	2012	The majority of the E(sq/hq) difference between XDH and XO originates from a conformational change in the loop at positions 423-433 near the flavin binding site, causing the differences in stability of the semiquinone state.	4,6-dinitro-o-cresol	141-147	xanthine dehydrogenase	Homo sapiens	48-51
22145797-7	2012	The majority of the E(sq/hq) difference between XDH and XO originates from a conformational change in the loop at positions 423-433 near the flavin binding site, causing the differences in stability of the semiquinone state.	semiquinone	206-217	xanthine dehydrogenase	Homo sapiens	48-51
22145797-9	2012	Instead, the positive charge of the NAD(+) ring, deprotonation of Asp429, and capping of the bulk surface of the flavin by the NAD(+) molecule all contribute to altering E(sq/hq) upon NAD(+) binding to XDH.	NAD	36-42	xanthine dehydrogenase	Homo sapiens	202-205
23024809-9	2012	XDH mutations in man cause xanthinuria with undetectable plasma uric acid levels and three RENF mice had plasma uric acid levels below the limit of detection.	Uric Acid	64-73	xanthine dehydrogenase	Homo sapiens	0-3
22821105-1	2012	Hereditary xanthinuria is an extremely rare purine metabolism disorder caused by a genetic abnormality in xanthine dehydrogenase.	purine	44-50	xanthine dehydrogenase	Homo sapiens	106-128
22821105-5	2012	Genetic analysis revealed a homozygous deletion of cytosine 2,567 in the xanthine dehydrogenase gene, and as a result, a stop codon was formed at position 928.	Cytosine	51-59	xanthine dehydrogenase	Homo sapiens	73-95
21997046-0	2011	All-optical XOR logic gate for 40Gb/s DPSK signals via FWM in a silicon nanowire.	Silicon	64-71	xanthine dehydrogenase	Homo sapiens	12-15
22167616-1	2011	Xanthinuria is a rare autosomal recessive disorder associated with a deficiency of xanthine oxidoreductase (XOR), which normally catalyzes the conversion of hypoxanthine to uric acid.	Hypoxanthine	157-169	xanthine dehydrogenase	Homo sapiens	108-111
22167616-1	2011	Xanthinuria is a rare autosomal recessive disorder associated with a deficiency of xanthine oxidoreductase (XOR), which normally catalyzes the conversion of hypoxanthine to uric acid.	Uric Acid	173-182	xanthine dehydrogenase	Homo sapiens	108-111
22048384-0	2011	All-optical multiple-channel logic XOR gate for NRZ-DPSK signals based on nondegenerate four-wave mixing in a silicon waveguide.	Silicon	110-117	xanthine dehydrogenase	Homo sapiens	35-38
22448318-1	2012	Febuxostat, a drug recently approved in the US, European Union and Japan for treatment of gout, inhibits xanthine oxidoreductase (XOR)-mediated generation of uric acid during purine catabolism.	Febuxostat	0-10	xanthine dehydrogenase	Homo sapiens	105-128
22448318-1	2012	Febuxostat, a drug recently approved in the US, European Union and Japan for treatment of gout, inhibits xanthine oxidoreductase (XOR)-mediated generation of uric acid during purine catabolism.	Febuxostat	0-10	xanthine dehydrogenase	Homo sapiens	130-133
22448318-1	2012	Febuxostat, a drug recently approved in the US, European Union and Japan for treatment of gout, inhibits xanthine oxidoreductase (XOR)-mediated generation of uric acid during purine catabolism.	Uric Acid	158-167	xanthine dehydrogenase	Homo sapiens	105-128
22448318-1	2012	Febuxostat, a drug recently approved in the US, European Union and Japan for treatment of gout, inhibits xanthine oxidoreductase (XOR)-mediated generation of uric acid during purine catabolism.	Uric Acid	158-167	xanthine dehydrogenase	Homo sapiens	130-133
22448318-1	2012	Febuxostat, a drug recently approved in the US, European Union and Japan for treatment of gout, inhibits xanthine oxidoreductase (XOR)-mediated generation of uric acid during purine catabolism.	purine	175-181	xanthine dehydrogenase	Homo sapiens	105-128
22448318-1	2012	Febuxostat, a drug recently approved in the US, European Union and Japan for treatment of gout, inhibits xanthine oxidoreductase (XOR)-mediated generation of uric acid during purine catabolism.	purine	175-181	xanthine dehydrogenase	Homo sapiens	130-133
21480532-1	2011	Nonpurine xanthine oxidoreductase (XOR) inhibitors represent important alternatives to the purine analogue allopurinol, which is still the most widely used drug in the treatment of conditions associated with elevated uric acid levels in the blood.	purine	3-9	xanthine dehydrogenase	Homo sapiens	10-33
21959625-3	2011	Xanthine oxidoreductase (XOR) has been previously characterized as a housekeeping enzyme responsible for cellular uric acid formation via enzymatic conversion of hypoxanthine and xanthine.	Uric Acid	114-123	xanthine dehydrogenase	Homo sapiens	0-23
21959625-3	2011	Xanthine oxidoreductase (XOR) has been previously characterized as a housekeeping enzyme responsible for cellular uric acid formation via enzymatic conversion of hypoxanthine and xanthine.	Uric Acid	114-123	xanthine dehydrogenase	Homo sapiens	25-28
21959625-3	2011	Xanthine oxidoreductase (XOR) has been previously characterized as a housekeeping enzyme responsible for cellular uric acid formation via enzymatic conversion of hypoxanthine and xanthine.	Hypoxanthine	162-174	xanthine dehydrogenase	Homo sapiens	0-23
21959625-3	2011	Xanthine oxidoreductase (XOR) has been previously characterized as a housekeeping enzyme responsible for cellular uric acid formation via enzymatic conversion of hypoxanthine and xanthine.	Hypoxanthine	162-174	xanthine dehydrogenase	Homo sapiens	25-28
21959625-3	2011	Xanthine oxidoreductase (XOR) has been previously characterized as a housekeeping enzyme responsible for cellular uric acid formation via enzymatic conversion of hypoxanthine and xanthine.	Xanthine	166-174	xanthine dehydrogenase	Homo sapiens	0-23
21959625-3	2011	Xanthine oxidoreductase (XOR) has been previously characterized as a housekeeping enzyme responsible for cellular uric acid formation via enzymatic conversion of hypoxanthine and xanthine.	Xanthine	166-174	xanthine dehydrogenase	Homo sapiens	25-28
21959625-4	2011	It has become apparent that XOR possesses multi-functional enzymatic activities outside the realm of xanthine metabolism and a small but significant literature also established a compelling functional association between administered sodium nitrite, XOR activation, and pharmacologically characterized NO transductive effects in positive cardiovascular function enhanced pulmonary perfusion, and protection against ischemia/reperfusion injury and hypoxic damage and oxidative stress.	Xanthine	101-109	xanthine dehydrogenase	Homo sapiens	28-31
21959625-4	2011	It has become apparent that XOR possesses multi-functional enzymatic activities outside the realm of xanthine metabolism and a small but significant literature also established a compelling functional association between administered sodium nitrite, XOR activation, and pharmacologically characterized NO transductive effects in positive cardiovascular function enhanced pulmonary perfusion, and protection against ischemia/reperfusion injury and hypoxic damage and oxidative stress.	Sodium Nitrite	234-248	xanthine dehydrogenase	Homo sapiens	28-31
21774633-0	2011	Xanthine oxidoreductase: a journey from purine metabolism to cardiovascular excitation-contraction coupling.	purine	40-46	xanthine dehydrogenase	Homo sapiens	0-23
21774633-1	2011	Xanthine oxidoreductase (XOR) is a ubiquitous complex cytosolic molybdoflavoprotein which controls the rate limiting step of purine catabolism by converting xanthine to uric acid.	purine	125-131	xanthine dehydrogenase	Homo sapiens	0-23
21774633-1	2011	Xanthine oxidoreductase (XOR) is a ubiquitous complex cytosolic molybdoflavoprotein which controls the rate limiting step of purine catabolism by converting xanthine to uric acid.	purine	125-131	xanthine dehydrogenase	Homo sapiens	25-28
21774633-1	2011	Xanthine oxidoreductase (XOR) is a ubiquitous complex cytosolic molybdoflavoprotein which controls the rate limiting step of purine catabolism by converting xanthine to uric acid.	Xanthine	157-165	xanthine dehydrogenase	Homo sapiens	0-23
21774633-1	2011	Xanthine oxidoreductase (XOR) is a ubiquitous complex cytosolic molybdoflavoprotein which controls the rate limiting step of purine catabolism by converting xanthine to uric acid.	Xanthine	157-165	xanthine dehydrogenase	Homo sapiens	25-28
21774633-1	2011	Xanthine oxidoreductase (XOR) is a ubiquitous complex cytosolic molybdoflavoprotein which controls the rate limiting step of purine catabolism by converting xanthine to uric acid.	Uric Acid	169-178	xanthine dehydrogenase	Homo sapiens	0-23
21774633-1	2011	Xanthine oxidoreductase (XOR) is a ubiquitous complex cytosolic molybdoflavoprotein which controls the rate limiting step of purine catabolism by converting xanthine to uric acid.	Uric Acid	169-178	xanthine dehydrogenase	Homo sapiens	25-28
21774633-3	2011	The ability of XOR to perform detoxification reactions, and to synthesize UA and reactive oxygen species (ROS) makes it a versatile intra- and extra-cellular protective "housekeeping enzyme".	Uric Acid	74-76	xanthine dehydrogenase	Homo sapiens	15-18
21774633-3	2011	The ability of XOR to perform detoxification reactions, and to synthesize UA and reactive oxygen species (ROS) makes it a versatile intra- and extra-cellular protective "housekeeping enzyme".	Reactive Oxygen Species	81-104	xanthine dehydrogenase	Homo sapiens	15-18
21774633-3	2011	The ability of XOR to perform detoxification reactions, and to synthesize UA and reactive oxygen species (ROS) makes it a versatile intra- and extra-cellular protective "housekeeping enzyme".	Reactive Oxygen Species	106-109	xanthine dehydrogenase	Homo sapiens	15-18
21774633-6	2011	Xanthine oxidoreductase in conjugation with antibodies has been shown to have an anti-tumor effect due to its ability to produce ROS, which in turn reduces the growth of cancer tissues.	Reactive Oxygen Species	129-132	xanthine dehydrogenase	Homo sapiens	0-23
21766873-2	2011	In this work, we demonstrate that the electrostatic and chemical (complexing and gold-thiol bonding) interactions existing in a gold nanoparticle/Zn(2+)/dithiothreitol-based ternary chemical system is "programmable" and can be utilized to regulate the aggregation and dispersion of nanoparticles via XOR and INHIBIT logics.	Sulfhydryl Compounds	86-91	xanthine dehydrogenase	Homo sapiens	300-303
21766873-2	2011	In this work, we demonstrate that the electrostatic and chemical (complexing and gold-thiol bonding) interactions existing in a gold nanoparticle/Zn(2+)/dithiothreitol-based ternary chemical system is "programmable" and can be utilized to regulate the aggregation and dispersion of nanoparticles via XOR and INHIBIT logics.	Zinc	146-152	xanthine dehydrogenase	Homo sapiens	300-303
21766873-2	2011	In this work, we demonstrate that the electrostatic and chemical (complexing and gold-thiol bonding) interactions existing in a gold nanoparticle/Zn(2+)/dithiothreitol-based ternary chemical system is "programmable" and can be utilized to regulate the aggregation and dispersion of nanoparticles via XOR and INHIBIT logics.	Dithiothreitol	153-167	xanthine dehydrogenase	Homo sapiens	300-303
21757641-5	2011	Febuxostat, a nonpurine inhibitor of xanthine oxidase (also known as xanthine dehydrogenase or xanthine oxidoreductase) may have advantages over allopurinol and is being tested in a similar protocol, with the eventual goal of determining whether urate-lowering therapy prevents recurrent calcium stones.	Febuxostat	0-10	xanthine dehydrogenase	Homo sapiens	69-91
21757641-5	2011	Febuxostat, a nonpurine inhibitor of xanthine oxidase (also known as xanthine dehydrogenase or xanthine oxidoreductase) may have advantages over allopurinol and is being tested in a similar protocol, with the eventual goal of determining whether urate-lowering therapy prevents recurrent calcium stones.	Febuxostat	0-10	xanthine dehydrogenase	Homo sapiens	95-118
21757641-5	2011	Febuxostat, a nonpurine inhibitor of xanthine oxidase (also known as xanthine dehydrogenase or xanthine oxidoreductase) may have advantages over allopurinol and is being tested in a similar protocol, with the eventual goal of determining whether urate-lowering therapy prevents recurrent calcium stones.	Uric Acid	246-251	xanthine dehydrogenase	Homo sapiens	69-91
21480532-1	2011	Nonpurine xanthine oxidoreductase (XOR) inhibitors represent important alternatives to the purine analogue allopurinol, which is still the most widely used drug in the treatment of conditions associated with elevated uric acid levels in the blood.	purine	3-9	xanthine dehydrogenase	Homo sapiens	35-38
21480532-1	2011	Nonpurine xanthine oxidoreductase (XOR) inhibitors represent important alternatives to the purine analogue allopurinol, which is still the most widely used drug in the treatment of conditions associated with elevated uric acid levels in the blood.	Allopurinol	107-118	xanthine dehydrogenase	Homo sapiens	10-33
21480532-1	2011	Nonpurine xanthine oxidoreductase (XOR) inhibitors represent important alternatives to the purine analogue allopurinol, which is still the most widely used drug in the treatment of conditions associated with elevated uric acid levels in the blood.	Allopurinol	107-118	xanthine dehydrogenase	Homo sapiens	35-38
21480532-1	2011	Nonpurine xanthine oxidoreductase (XOR) inhibitors represent important alternatives to the purine analogue allopurinol, which is still the most widely used drug in the treatment of conditions associated with elevated uric acid levels in the blood.	Uric Acid	217-226	xanthine dehydrogenase	Homo sapiens	10-33
21480532-1	2011	Nonpurine xanthine oxidoreductase (XOR) inhibitors represent important alternatives to the purine analogue allopurinol, which is still the most widely used drug in the treatment of conditions associated with elevated uric acid levels in the blood.	Uric Acid	217-226	xanthine dehydrogenase	Homo sapiens	35-38
21480532-2	2011	By condensing mono-, di- and trihydroxybenzaldehydes with aromatic thiosemicarbazides, aryl hydrazides and dithiocarbazates, three series of structurally related Schiff bases were synthesised, characterised and tested for XOR inhibitory activity.	mono-, di- and trihydroxybenzaldehydes	14-52	xanthine dehydrogenase	Homo sapiens	222-225
21480532-2	2011	By condensing mono-, di- and trihydroxybenzaldehydes with aromatic thiosemicarbazides, aryl hydrazides and dithiocarbazates, three series of structurally related Schiff bases were synthesised, characterised and tested for XOR inhibitory activity.	dithiocarbazates	107-123	xanthine dehydrogenase	Homo sapiens	222-225
21480532-2	2011	By condensing mono-, di- and trihydroxybenzaldehydes with aromatic thiosemicarbazides, aryl hydrazides and dithiocarbazates, three series of structurally related Schiff bases were synthesised, characterised and tested for XOR inhibitory activity.	Schiff Bases	162-174	xanthine dehydrogenase	Homo sapiens	222-225
20570389-1	2011	BACKGROUND: Xanthine oxidoreductase (XOR) is a rate-limiting enzyme in the purine metabolism pathway.	purine	75-81	xanthine dehydrogenase	Homo sapiens	12-35
21368957-1	2011	We demonstrate a photonic chip-based all-optical exclusive-OR (XOR) gate for phase-encoded optical signals via four-wave mixing in a highly nonlinear, dispersion-engineered chalcogenide (As2S3) planar waveguide.	chalcogenide	173-185	xanthine dehydrogenase	Homo sapiens	63-66
25961263-2	2011	Recently, we have demonstrated that estradiol (E2) induces a significant decrease of the expression and activity of XDH and of its conversion to XO in human mammary epithelial cells.	Estradiol	36-45	xanthine dehydrogenase	Homo sapiens	116-119
25961263-4	2011	Because the XO-derived O2 - combines with  NO to yield ONOO-, and considering that ONOO- converts XDH to XO, the resulting increase of XO activity and reactive oxygen species production would eventually lead to a further increase of ONOO- production, thus creating a vicious cycle of oxidative stress.	onoo	55-59	xanthine dehydrogenase	Homo sapiens	98-101
25961263-4	2011	Because the XO-derived O2 - combines with  NO to yield ONOO-, and considering that ONOO- converts XDH to XO, the resulting increase of XO activity and reactive oxygen species production would eventually lead to a further increase of ONOO- production, thus creating a vicious cycle of oxidative stress.	onoo	83-87	xanthine dehydrogenase	Homo sapiens	98-101
25961263-4	2011	Because the XO-derived O2 - combines with  NO to yield ONOO-, and considering that ONOO- converts XDH to XO, the resulting increase of XO activity and reactive oxygen species production would eventually lead to a further increase of ONOO- production, thus creating a vicious cycle of oxidative stress.	Reactive Oxygen Species	151-174	xanthine dehydrogenase	Homo sapiens	98-101
25961263-4	2011	Because the XO-derived O2 - combines with  NO to yield ONOO-, and considering that ONOO- converts XDH to XO, the resulting increase of XO activity and reactive oxygen species production would eventually lead to a further increase of ONOO- production, thus creating a vicious cycle of oxidative stress.	onoo	83-87	xanthine dehydrogenase	Homo sapiens	98-101
21605422-10	2011	Allopurinol, an inhibitor of xanthine oxidoreductase that converts xanthine to uric acid, blocked uric acid production, MICA/B expression, and sensitivity to NK-92 cell killing toward a PANC-1 cancer cell line exposed to radiation and two genotoxic drugs, gemcitabine and 5-fluorouracil.	Allopurinol	0-11	xanthine dehydrogenase	Homo sapiens	29-52
21605422-10	2011	Allopurinol, an inhibitor of xanthine oxidoreductase that converts xanthine to uric acid, blocked uric acid production, MICA/B expression, and sensitivity to NK-92 cell killing toward a PANC-1 cancer cell line exposed to radiation and two genotoxic drugs, gemcitabine and 5-fluorouracil.	Uric Acid	79-88	xanthine dehydrogenase	Homo sapiens	29-52
21605422-10	2011	Allopurinol, an inhibitor of xanthine oxidoreductase that converts xanthine to uric acid, blocked uric acid production, MICA/B expression, and sensitivity to NK-92 cell killing toward a PANC-1 cancer cell line exposed to radiation and two genotoxic drugs, gemcitabine and 5-fluorouracil.	Uric Acid	98-107	xanthine dehydrogenase	Homo sapiens	29-52
21605422-10	2011	Allopurinol, an inhibitor of xanthine oxidoreductase that converts xanthine to uric acid, blocked uric acid production, MICA/B expression, and sensitivity to NK-92 cell killing toward a PANC-1 cancer cell line exposed to radiation and two genotoxic drugs, gemcitabine and 5-fluorouracil.	gemcitabine	256-267	xanthine dehydrogenase	Homo sapiens	29-52
21605422-10	2011	Allopurinol, an inhibitor of xanthine oxidoreductase that converts xanthine to uric acid, blocked uric acid production, MICA/B expression, and sensitivity to NK-92 cell killing toward a PANC-1 cancer cell line exposed to radiation and two genotoxic drugs, gemcitabine and 5-fluorouracil.	Fluorouracil	272-286	xanthine dehydrogenase	Homo sapiens	29-52
21177703-8	2011	Multiple nitrite reductases have been shown to be relevant in the conversion of nitrite to metabolically active NO, including deoxy-haemoglobin and myoglobin in the circulation and heart, respectively, and xanthine oxidoreductase in the lung parenchyma.	Nitrites	9-16	xanthine dehydrogenase	Homo sapiens	206-229
20570389-1	2011	BACKGROUND: Xanthine oxidoreductase (XOR) is a rate-limiting enzyme in the purine metabolism pathway.	purine	75-81	xanthine dehydrogenase	Homo sapiens	37-40
20077140-2	2010	BACKGROUND: Xanthinuria type I is a rare disorder of purine metabolism caused by xanthine dehydrogenase (XDH) deficiency; fewer than 150 cases have been described in the literature so far.	purine	53-59	xanthine dehydrogenase	Homo sapiens	81-103
20083360-3	2010	Nox2- and Nox4-dependent NADPH oxidase activity appears to be a major source of this oxidative stress, and oxidants can induce conformational changes in xanthine dehydrogenase, nitric oxide synthase, and the mitochondrial respiratory chain which increase their capacity to generate superoxide as well.	Superoxides	282-292	xanthine dehydrogenase	Homo sapiens	153-175
19109252-1	2009	Xanthine oxidoreductase is a ubiquitous cytoplasmic protein that catalyzes the final two steps in purine catabolism.	purine	98-104	xanthine dehydrogenase	Homo sapiens	0-23
20527878-1	2010	An "XOR" gate built using label-free, dual-analyte electrochemical sensors and the activation of this logic gate via changing concentrations of cocaine and the relevant cDNA as inputs are described.	Cocaine	144-151	xanthine dehydrogenase	Homo sapiens	4-7
20479828-1	2010	We have designed and fabricated a directed logic architecture consisting of two silicon microring resonators that can perform XOR and XNOR operations.	Silicon	80-87	xanthine dehydrogenase	Homo sapiens	126-129
19685356-1	2010	CONCLUSIONS: The results reported here provide the first evidence of the production of superoxide, a biologically relevant reactive oxygen species (ROS), in human inner ear perilymph (hIP) in pathological conditions, by the activity of the xanthine dehydrogenase/xanthine oxidase (XA/XO) enzyme system.	Superoxides	87-97	xanthine dehydrogenase	Homo sapiens	240-262
19685356-1	2010	CONCLUSIONS: The results reported here provide the first evidence of the production of superoxide, a biologically relevant reactive oxygen species (ROS), in human inner ear perilymph (hIP) in pathological conditions, by the activity of the xanthine dehydrogenase/xanthine oxidase (XA/XO) enzyme system.	Reactive Oxygen Species	123-146	xanthine dehydrogenase	Homo sapiens	240-262
19685356-1	2010	CONCLUSIONS: The results reported here provide the first evidence of the production of superoxide, a biologically relevant reactive oxygen species (ROS), in human inner ear perilymph (hIP) in pathological conditions, by the activity of the xanthine dehydrogenase/xanthine oxidase (XA/XO) enzyme system.	Reactive Oxygen Species	148-151	xanthine dehydrogenase	Homo sapiens	240-262
20377513-4	2010	In mammalian blood, nitrite, present at nanomolar concentrations, can be reduced to bioactive NO along a physiological oxygen and pH gradient either non-enzymatically (acidic disproportionation) or by a number of enzymes including xanthine oxidoreductase, NOS, mitochondrial cytochromes and deoxygenated haemoglobin and myoglobin.	Nitrites	20-27	xanthine dehydrogenase	Homo sapiens	231-254
20109996-0	2009	Febuxostat: a selective xanthine-oxidase/xanthine-dehydrogenase inhibitor for the management of hyperuricemia in adults with gout.	Febuxostat	0-10	xanthine dehydrogenase	Homo sapiens	41-63
19997154-0	2009	Optical polarization based logic functions (XOR or XNOR) with nonlinear Gallium nitride nanoslab.	gallium nitride	72-87	xanthine dehydrogenase	Homo sapiens	44-47
19997154-1	2009	We present a scheme of XOR/XNOR logic gate, based on non phase-matched noncollinear second harmonic generation from a medium of suitable crystalline symmetry, Gallium nitride.	gallium nitride	159-174	xanthine dehydrogenase	Homo sapiens	23-26
19441809-8	2009	The OR logic gate was fabricated by connecting the anodic and cathodic QS-PNP in a series; XOR logic was fabricated by connecting two anodic QS-PNPs in series.	qs-pnps	141-148	xanthine dehydrogenase	Homo sapiens	91-94
19500084-3	2009	Xanthine oxidase/dehydrogenase (XDH) and aldehyde oxidase (AO) compete with TPMT to inactivate AZA.	Azathioprine	95-98	xanthine dehydrogenase	Homo sapiens	0-30
19500084-3	2009	Xanthine oxidase/dehydrogenase (XDH) and aldehyde oxidase (AO) compete with TPMT to inactivate AZA.	Azathioprine	95-98	xanthine dehydrogenase	Homo sapiens	32-35
19500084-4	2009	AIM: To assess whether genetic polymorphism in AOX1, XDH and MOCOS (the product of which activates the essential cofactor for AO and XDH) is associated with AZA treatment outcome in IBD.	Azathioprine	157-160	xanthine dehydrogenase	Homo sapiens	133-136
19450565-1	2009	The oxidation of xanthine by xanthine oxidase (XO) or xanthine dehydrogenase represents an important source of reactive oxygen species (ROS), which contribute to the damaging consequences of cerebral ischemia, inflammation, and neurodegenerative disorders.	Xanthine	17-25	xanthine dehydrogenase	Homo sapiens	54-76
19450565-1	2009	The oxidation of xanthine by xanthine oxidase (XO) or xanthine dehydrogenase represents an important source of reactive oxygen species (ROS), which contribute to the damaging consequences of cerebral ischemia, inflammation, and neurodegenerative disorders.	Reactive Oxygen Species	111-134	xanthine dehydrogenase	Homo sapiens	54-76
19450565-1	2009	The oxidation of xanthine by xanthine oxidase (XO) or xanthine dehydrogenase represents an important source of reactive oxygen species (ROS), which contribute to the damaging consequences of cerebral ischemia, inflammation, and neurodegenerative disorders.	Reactive Oxygen Species	136-139	xanthine dehydrogenase	Homo sapiens	54-76
19584965-1	2009	Allopurinol is an inhibitor of xanthine oxidoreductase (XOR) and inhibits the generation of uric acid (UA) as the final product of purine catabolism, as well as the resulting generation of superoxide (O2(-)), in humans.	Allopurinol	0-11	xanthine dehydrogenase	Homo sapiens	31-54
19584965-1	2009	Allopurinol is an inhibitor of xanthine oxidoreductase (XOR) and inhibits the generation of uric acid (UA) as the final product of purine catabolism, as well as the resulting generation of superoxide (O2(-)), in humans.	Allopurinol	0-11	xanthine dehydrogenase	Homo sapiens	56-59
19584965-1	2009	Allopurinol is an inhibitor of xanthine oxidoreductase (XOR) and inhibits the generation of uric acid (UA) as the final product of purine catabolism, as well as the resulting generation of superoxide (O2(-)), in humans.	Uric Acid	92-101	xanthine dehydrogenase	Homo sapiens	56-59
19584965-1	2009	Allopurinol is an inhibitor of xanthine oxidoreductase (XOR) and inhibits the generation of uric acid (UA) as the final product of purine catabolism, as well as the resulting generation of superoxide (O2(-)), in humans.	Uric Acid	103-105	xanthine dehydrogenase	Homo sapiens	56-59
19693777-0	2009	Estradiol decreases xanthine dehydrogenase enzyme activity and protein expression in non-tumorigenic and malignant human mammary epithelial cells.	Estradiol	0-9	xanthine dehydrogenase	Homo sapiens	20-42
19693777-4	2009	In these latter two cell lines, as opposed to HMEC cells, we observe a residual ability of XDH to produce retinoic acid from retinaldehyde and the inability to use retinol, as a consequence of a deficit in CRBP.	Tretinoin	106-119	xanthine dehydrogenase	Homo sapiens	91-94
19693777-4	2009	In these latter two cell lines, as opposed to HMEC cells, we observe a residual ability of XDH to produce retinoic acid from retinaldehyde and the inability to use retinol, as a consequence of a deficit in CRBP.	Retinaldehyde	125-138	xanthine dehydrogenase	Homo sapiens	91-94
19584965-1	2009	Allopurinol is an inhibitor of xanthine oxidoreductase (XOR) and inhibits the generation of uric acid (UA) as the final product of purine catabolism, as well as the resulting generation of superoxide (O2(-)), in humans.	purine	131-137	xanthine dehydrogenase	Homo sapiens	56-59
19584965-1	2009	Allopurinol is an inhibitor of xanthine oxidoreductase (XOR) and inhibits the generation of uric acid (UA) as the final product of purine catabolism, as well as the resulting generation of superoxide (O2(-)), in humans.	Superoxides	189-199	xanthine dehydrogenase	Homo sapiens	31-54
19584965-1	2009	Allopurinol is an inhibitor of xanthine oxidoreductase (XOR) and inhibits the generation of uric acid (UA) as the final product of purine catabolism, as well as the resulting generation of superoxide (O2(-)), in humans.	Superoxides	189-199	xanthine dehydrogenase	Homo sapiens	56-59
19584965-1	2009	Allopurinol is an inhibitor of xanthine oxidoreductase (XOR) and inhibits the generation of uric acid (UA) as the final product of purine catabolism, as well as the resulting generation of superoxide (O2(-)), in humans.	Superoxides	201-203	xanthine dehydrogenase	Homo sapiens	56-59
19412257-2	2009	The scheme explores dual-pump four-wave mixing in a 35 cm highly nonlinear bismuth oxide fiber to achieve XOR operation of the plaintext and the encryption key.	bismuth oxide	75-88	xanthine dehydrogenase	Homo sapiens	106-109
19191374-4	2009	The properties of the complex at its equilibrium geometry with applied field have been calculated, showing that dependencies between hydrogen bond distance, dissociation energy, and properties derived from the topological analysis of the electron distribution are analogous to those observed in families of XDH...AY complexes.	Hydrogen	133-141	xanthine dehydrogenase	Homo sapiens	307-310
19250215-2	2009	In a previous study we indicated that xanthine dehydrogenase (XDH) is able to oxidize actively both all-trans-retinol (t-ROL) bound to the CRBP (holo-CRBP) and all-trans-retinaldehyde (t-RAL) to all-trans-retinoic acid (t-RA) in human mammary epithelial cells (HMEC).	Vitamin A	100-117	xanthine dehydrogenase	Homo sapiens	38-60
19250215-2	2009	In a previous study we indicated that xanthine dehydrogenase (XDH) is able to oxidize actively both all-trans-retinol (t-ROL) bound to the CRBP (holo-CRBP) and all-trans-retinaldehyde (t-RAL) to all-trans-retinoic acid (t-RA) in human mammary epithelial cells (HMEC).	Vitamin A	100-117	xanthine dehydrogenase	Homo sapiens	62-65
19250215-2	2009	In a previous study we indicated that xanthine dehydrogenase (XDH) is able to oxidize actively both all-trans-retinol (t-ROL) bound to the CRBP (holo-CRBP) and all-trans-retinaldehyde (t-RAL) to all-trans-retinoic acid (t-RA) in human mammary epithelial cells (HMEC).	Vitamin A	119-124	xanthine dehydrogenase	Homo sapiens	38-60
19250215-2	2009	In a previous study we indicated that xanthine dehydrogenase (XDH) is able to oxidize actively both all-trans-retinol (t-ROL) bound to the CRBP (holo-CRBP) and all-trans-retinaldehyde (t-RAL) to all-trans-retinoic acid (t-RA) in human mammary epithelial cells (HMEC).	Vitamin A	119-124	xanthine dehydrogenase	Homo sapiens	62-65
19250215-2	2009	In a previous study we indicated that xanthine dehydrogenase (XDH) is able to oxidize actively both all-trans-retinol (t-ROL) bound to the CRBP (holo-CRBP) and all-trans-retinaldehyde (t-RAL) to all-trans-retinoic acid (t-RA) in human mammary epithelial cells (HMEC).	Retinaldehyde	160-183	xanthine dehydrogenase	Homo sapiens	38-60
19250215-2	2009	In a previous study we indicated that xanthine dehydrogenase (XDH) is able to oxidize actively both all-trans-retinol (t-ROL) bound to the CRBP (holo-CRBP) and all-trans-retinaldehyde (t-RAL) to all-trans-retinoic acid (t-RA) in human mammary epithelial cells (HMEC).	Retinaldehyde	160-183	xanthine dehydrogenase	Homo sapiens	62-65
19250215-2	2009	In a previous study we indicated that xanthine dehydrogenase (XDH) is able to oxidize actively both all-trans-retinol (t-ROL) bound to the CRBP (holo-CRBP) and all-trans-retinaldehyde (t-RAL) to all-trans-retinoic acid (t-RA) in human mammary epithelial cells (HMEC).	Tretinoin	195-218	xanthine dehydrogenase	Homo sapiens	38-60
19250215-2	2009	In a previous study we indicated that xanthine dehydrogenase (XDH) is able to oxidize actively both all-trans-retinol (t-ROL) bound to the CRBP (holo-CRBP) and all-trans-retinaldehyde (t-RAL) to all-trans-retinoic acid (t-RA) in human mammary epithelial cells (HMEC).	Tretinoin	195-218	xanthine dehydrogenase	Homo sapiens	62-65
19250215-2	2009	In a previous study we indicated that xanthine dehydrogenase (XDH) is able to oxidize actively both all-trans-retinol (t-ROL) bound to the CRBP (holo-CRBP) and all-trans-retinaldehyde (t-RAL) to all-trans-retinoic acid (t-RA) in human mammary epithelial cells (HMEC).	Tretinoin	185-189	xanthine dehydrogenase	Homo sapiens	38-60
19250215-2	2009	In a previous study we indicated that xanthine dehydrogenase (XDH) is able to oxidize actively both all-trans-retinol (t-ROL) bound to the CRBP (holo-CRBP) and all-trans-retinaldehyde (t-RAL) to all-trans-retinoic acid (t-RA) in human mammary epithelial cells (HMEC).	Tretinoin	185-189	xanthine dehydrogenase	Homo sapiens	62-65
19250215-3	2009	Since both XDH and CRBP are required for the biosynthesis of t-RA, we have inspected their bioavailability in both estrogen-responsive and nonresponsive human mammary epithelial cancer cells.	Tretinoin	61-65	xanthine dehydrogenase	Homo sapiens	11-14
19250215-4	2009	The XDH activity, as assessed in the crude and purified extracts of both MCF7 and MDA-MB 231 cells by measuring the substrate t-RAL (that unlike t-ROL does not need CRBP), was 6 to 10 times lower than that previously encountered in normal HMEC.	-rol	146-150	xanthine dehydrogenase	Homo sapiens	4-7
19158351-2	2009	Once in the cell, fructose is phosphorylated by ketohexokinase (KHK), leading to consumption of ATP, formation of AMP, and generation of uric acid through xanthine oxidoreductase (XOR).	Fructose	18-26	xanthine dehydrogenase	Homo sapiens	155-178
19158351-2	2009	Once in the cell, fructose is phosphorylated by ketohexokinase (KHK), leading to consumption of ATP, formation of AMP, and generation of uric acid through xanthine oxidoreductase (XOR).	Fructose	18-26	xanthine dehydrogenase	Homo sapiens	180-183
19158351-2	2009	Once in the cell, fructose is phosphorylated by ketohexokinase (KHK), leading to consumption of ATP, formation of AMP, and generation of uric acid through xanthine oxidoreductase (XOR).	Adenosine Triphosphate	96-99	xanthine dehydrogenase	Homo sapiens	155-178
19158351-2	2009	Once in the cell, fructose is phosphorylated by ketohexokinase (KHK), leading to consumption of ATP, formation of AMP, and generation of uric acid through xanthine oxidoreductase (XOR).	Uric Acid	137-146	xanthine dehydrogenase	Homo sapiens	155-178
19158351-2	2009	Once in the cell, fructose is phosphorylated by ketohexokinase (KHK), leading to consumption of ATP, formation of AMP, and generation of uric acid through xanthine oxidoreductase (XOR).	Uric Acid	137-146	xanthine dehydrogenase	Homo sapiens	180-183
19158351-7	2009	We detected XOR mRNA in HK-2 cells and confirmed its activity by identifying uric acid by mass spectrometry.	Uric Acid	77-86	xanthine dehydrogenase	Homo sapiens	12-15
18772145-1	2008	The xanthine oxidoreductase gene (XOR) encodes an important source of reactive oxygen species and uric acid, and its expression is associated with various human diseases including several forms of cancer.	Reactive Oxygen Species	70-93	xanthine dehydrogenase	Homo sapiens	4-27
19273066-2	2009	Xanthine oxidoreductase (XOR) is a major oxidative enzyme and increased XOR activity, leading to both increased production of reactive oxygen species and uric acid, is implicated in heart failure.	Reactive Oxygen Species	126-149	xanthine dehydrogenase	Homo sapiens	0-23
19273066-2	2009	Xanthine oxidoreductase (XOR) is a major oxidative enzyme and increased XOR activity, leading to both increased production of reactive oxygen species and uric acid, is implicated in heart failure.	Reactive Oxygen Species	126-149	xanthine dehydrogenase	Homo sapiens	25-28
19273066-2	2009	Xanthine oxidoreductase (XOR) is a major oxidative enzyme and increased XOR activity, leading to both increased production of reactive oxygen species and uric acid, is implicated in heart failure.	Reactive Oxygen Species	126-149	xanthine dehydrogenase	Homo sapiens	72-75
19273066-2	2009	Xanthine oxidoreductase (XOR) is a major oxidative enzyme and increased XOR activity, leading to both increased production of reactive oxygen species and uric acid, is implicated in heart failure.	Uric Acid	154-163	xanthine dehydrogenase	Homo sapiens	0-23
19273066-2	2009	Xanthine oxidoreductase (XOR) is a major oxidative enzyme and increased XOR activity, leading to both increased production of reactive oxygen species and uric acid, is implicated in heart failure.	Uric Acid	154-163	xanthine dehydrogenase	Homo sapiens	25-28
19273066-2	2009	Xanthine oxidoreductase (XOR) is a major oxidative enzyme and increased XOR activity, leading to both increased production of reactive oxygen species and uric acid, is implicated in heart failure.	Uric Acid	154-163	xanthine dehydrogenase	Homo sapiens	72-75
19273066-5	2009	In this regard, XOR interacts with nitric oxide signaling at numerous levels, including a direct protein-protein interaction with neuronal nitric oxide synthase (NOS1) in the sarcoplasmic reticulum.	Nitric Oxide	35-47	xanthine dehydrogenase	Homo sapiens	16-19
19273066-6	2009	Deficiency or translocation of NOS1 away from this microdomain leads to increased activity of XOR, which in turn impairs excitation-contraction coupling and myofilament calcium sensitivity.	Calcium	169-176	xanthine dehydrogenase	Homo sapiens	94-97
20877801-0	2009	The reaction mechanism of the molybdenum hydroxylase xanthine oxidoreductase: evidence against the formation of intermediates having metal-carbon bonds.	Metals	133-138	xanthine dehydrogenase	Homo sapiens	53-76
20877801-0	2009	The reaction mechanism of the molybdenum hydroxylase xanthine oxidoreductase: evidence against the formation of intermediates having metal-carbon bonds.	Carbon	139-145	xanthine dehydrogenase	Homo sapiens	53-76
18974051-0	2008	Nitro-oleic acid, a novel and irreversible inhibitor of xanthine oxidoreductase.	nitro-oleic acid	0-16	xanthine dehydrogenase	Homo sapiens	56-79
18974051-3	2008	Nitro-oleic acid inhibits XOR activity in a concentration-dependent manner with an IC50 of 0.6 microM, limiting both purine oxidation and formation of superoxide (O2.).	nitro-oleic acid	0-16	xanthine dehydrogenase	Homo sapiens	26-29
18974051-3	2008	Nitro-oleic acid inhibits XOR activity in a concentration-dependent manner with an IC50 of 0.6 microM, limiting both purine oxidation and formation of superoxide (O2.).	purine	117-123	xanthine dehydrogenase	Homo sapiens	26-29
18974051-3	2008	Nitro-oleic acid inhibits XOR activity in a concentration-dependent manner with an IC50 of 0.6 microM, limiting both purine oxidation and formation of superoxide (O2.).	Superoxides	151-161	xanthine dehydrogenase	Homo sapiens	26-29
18974051-3	2008	Nitro-oleic acid inhibits XOR activity in a concentration-dependent manner with an IC50 of 0.6 microM, limiting both purine oxidation and formation of superoxide (O2.).	Superoxides	163-165	xanthine dehydrogenase	Homo sapiens	26-29
18974051-5	2008	Structure-function studies indicate that the carboxylic acid moiety, nitration at the 9 or 10 olefinic carbon, and unsaturation is required for XOR inhibition.	Carboxylic Acids	45-60	xanthine dehydrogenase	Homo sapiens	144-147
18974051-5	2008	Structure-function studies indicate that the carboxylic acid moiety, nitration at the 9 or 10 olefinic carbon, and unsaturation is required for XOR inhibition.	Carbon	103-109	xanthine dehydrogenase	Homo sapiens	144-147
18974051-7	2008	Importantly, OA-NO2 more potently inhibits cell-associated XOR-dependent O2.	Nitrogen Dioxide	16-19	xanthine dehydrogenase	Homo sapiens	59-62
19000269-2	2008	In the present study we aimed to evaluate placental transfer of allopurinol, an inhibitor of XOR.	Allopurinol	64-75	xanthine dehydrogenase	Homo sapiens	93-96
18767115-9	2008	Further experiments suggested that XOR derived ROS mediated this effect and also modulated COX-2 and MMP levels and function.	ros	47-50	xanthine dehydrogenase	Homo sapiens	35-38
18772145-1	2008	The xanthine oxidoreductase gene (XOR) encodes an important source of reactive oxygen species and uric acid, and its expression is associated with various human diseases including several forms of cancer.	Reactive Oxygen Species	70-93	xanthine dehydrogenase	Homo sapiens	34-37
18772145-1	2008	The xanthine oxidoreductase gene (XOR) encodes an important source of reactive oxygen species and uric acid, and its expression is associated with various human diseases including several forms of cancer.	Uric Acid	98-107	xanthine dehydrogenase	Homo sapiens	4-27
18772145-1	2008	The xanthine oxidoreductase gene (XOR) encodes an important source of reactive oxygen species and uric acid, and its expression is associated with various human diseases including several forms of cancer.	Uric Acid	98-107	xanthine dehydrogenase	Homo sapiens	34-37
18669934-5	2008	The reactive oxygen species (ROS)-producing enzyme xanthine oxidoreductase (XOR) is activated in a p38 MAP kinase-dependent manner following HVt MV.	Reactive Oxygen Species	4-27	xanthine dehydrogenase	Homo sapiens	51-74
18818408-3	2008	Herein, we have demonstrated that conversion of nitrite to NO by blood vessels and RBCs was enhanced in the presence of the XOR substrate xanthine (10 micromol/L) and attenuated by the XOR inhibitor allopurinol (100 micromol/L) in acidic and hypoxic conditions only.	Nitrites	48-55	xanthine dehydrogenase	Homo sapiens	124-127
18818408-3	2008	Herein, we have demonstrated that conversion of nitrite to NO by blood vessels and RBCs was enhanced in the presence of the XOR substrate xanthine (10 micromol/L) and attenuated by the XOR inhibitor allopurinol (100 micromol/L) in acidic and hypoxic conditions only.	Nitrites	48-55	xanthine dehydrogenase	Homo sapiens	185-188
18818408-3	2008	Herein, we have demonstrated that conversion of nitrite to NO by blood vessels and RBCs was enhanced in the presence of the XOR substrate xanthine (10 micromol/L) and attenuated by the XOR inhibitor allopurinol (100 micromol/L) in acidic and hypoxic conditions only.	Xanthine	138-146	xanthine dehydrogenase	Homo sapiens	124-127
18818408-3	2008	Herein, we have demonstrated that conversion of nitrite to NO by blood vessels and RBCs was enhanced in the presence of the XOR substrate xanthine (10 micromol/L) and attenuated by the XOR inhibitor allopurinol (100 micromol/L) in acidic and hypoxic conditions only.	Allopurinol	199-210	xanthine dehydrogenase	Homo sapiens	124-127
18818408-3	2008	Herein, we have demonstrated that conversion of nitrite to NO by blood vessels and RBCs was enhanced in the presence of the XOR substrate xanthine (10 micromol/L) and attenuated by the XOR inhibitor allopurinol (100 micromol/L) in acidic and hypoxic conditions only.	Allopurinol	199-210	xanthine dehydrogenase	Homo sapiens	185-188
18678861-4	2008	Here we found that the proteolytic activation of the xanthine dehydrogenase/xanthine oxidase (XD/XO) system was required because pretreatment with serine protease inhibitors abolished rhinovirus-induced superoxide generation in primary bronchial and A549 respiratory epithelial cells.	Superoxides	203-213	xanthine dehydrogenase	Homo sapiens	53-75
18818408-6	2008	Thus, XOR and eNOS are ideally situated on the membranes of RBCs and blood vessels to generate intravascular vasodilator NO from nitrite during ischemic episodes.	Nitrites	129-136	xanthine dehydrogenase	Homo sapiens	6-9
18669934-5	2008	The reactive oxygen species (ROS)-producing enzyme xanthine oxidoreductase (XOR) is activated in a p38 MAP kinase-dependent manner following HVt MV.	Reactive Oxygen Species	4-27	xanthine dehydrogenase	Homo sapiens	76-79
18669934-5	2008	The reactive oxygen species (ROS)-producing enzyme xanthine oxidoreductase (XOR) is activated in a p38 MAP kinase-dependent manner following HVt MV.	Reactive Oxygen Species	29-32	xanthine dehydrogenase	Homo sapiens	51-74
18669934-5	2008	The reactive oxygen species (ROS)-producing enzyme xanthine oxidoreductase (XOR) is activated in a p38 MAP kinase-dependent manner following HVt MV.	Reactive Oxygen Species	29-32	xanthine dehydrogenase	Homo sapiens	76-79
18669934-6	2008	Allopurinol, a XOR inhibitor, also suppresses HVt MV-induced apoptosis, implicating HVt MV-induced ROS in the induction of alveolar cell apoptosis.	Allopurinol	0-11	xanthine dehydrogenase	Homo sapiens	15-18
18513323-1	2008	Reactive oxygen species are generated by various biological systems, including NADPH oxidases, xanthine oxidoreductase, and mitochondrial respiratory enzymes, and contribute to many physiological and pathological phenomena.	Reactive Oxygen Species	0-23	xanthine dehydrogenase	Homo sapiens	95-118
18328088-1	2008	Xanthine dehydrogenase/xanthine oxidase (XDH/XO) catalyses the hydroxylation of hypoxanthine to xanthine and finally to uric acid in purine degradation.	Hypoxanthine	80-92	xanthine dehydrogenase	Homo sapiens	41-47
18328088-1	2008	Xanthine dehydrogenase/xanthine oxidase (XDH/XO) catalyses the hydroxylation of hypoxanthine to xanthine and finally to uric acid in purine degradation.	Xanthine	23-31	xanthine dehydrogenase	Homo sapiens	41-47
18328088-1	2008	Xanthine dehydrogenase/xanthine oxidase (XDH/XO) catalyses the hydroxylation of hypoxanthine to xanthine and finally to uric acid in purine degradation.	Uric Acid	120-129	xanthine dehydrogenase	Homo sapiens	41-47
18328088-1	2008	Xanthine dehydrogenase/xanthine oxidase (XDH/XO) catalyses the hydroxylation of hypoxanthine to xanthine and finally to uric acid in purine degradation.	purine	133-139	xanthine dehydrogenase	Homo sapiens	41-47
18513323-2	2008	Mammalian xanthine dehydrogenase (XDH) can be converted to xanthine oxidase (XO), which produces both superoxide anion and hydrogen peroxide.	Superoxides	102-118	xanthine dehydrogenase	Homo sapiens	10-32
18513323-2	2008	Mammalian xanthine dehydrogenase (XDH) can be converted to xanthine oxidase (XO), which produces both superoxide anion and hydrogen peroxide.	Superoxides	102-118	xanthine dehydrogenase	Homo sapiens	34-37
18513323-2	2008	Mammalian xanthine dehydrogenase (XDH) can be converted to xanthine oxidase (XO), which produces both superoxide anion and hydrogen peroxide.	Hydrogen Peroxide	123-140	xanthine dehydrogenase	Homo sapiens	10-32
18513323-2	2008	Mammalian xanthine dehydrogenase (XDH) can be converted to xanthine oxidase (XO), which produces both superoxide anion and hydrogen peroxide.	Hydrogen Peroxide	123-140	xanthine dehydrogenase	Homo sapiens	34-37
18513323-4	2008	Furthermore, this transition seems to involve a thermodynamic equilibrium between XDH and XO; disulfide bond formation or proteolysis can then lock the enzyme in the XO form.	Disulfides	94-103	xanthine dehydrogenase	Homo sapiens	82-85
18594651-0	2008	Ultrafast all-optical three-input Boolean XOR operation for differential phase-shift keying signals using periodically poled lithium niobate.	lithium niobate	125-140	xanthine dehydrogenase	Homo sapiens	42-45
18516050-3	2008	Here we report on nitrate reductase activity in rodent and human tissues that results in formation of nitrite and nitric oxide (NO) and is attenuated by the xanthine oxidoreductase inhibitor allopurinol.	Nitrites	102-109	xanthine dehydrogenase	Homo sapiens	157-180
18516050-3	2008	Here we report on nitrate reductase activity in rodent and human tissues that results in formation of nitrite and nitric oxide (NO) and is attenuated by the xanthine oxidoreductase inhibitor allopurinol.	Nitric Oxide	114-126	xanthine dehydrogenase	Homo sapiens	157-180
18516050-3	2008	Here we report on nitrate reductase activity in rodent and human tissues that results in formation of nitrite and nitric oxide (NO) and is attenuated by the xanthine oxidoreductase inhibitor allopurinol.	Allopurinol	191-202	xanthine dehydrogenase	Homo sapiens	157-180
18594651-1	2008	We propose and demonstrate that periodically poled lithium niobate (PPLN) can act as an ultrafast three-input XOR gate for differential phase-shift keying (DPSK) signals based on cascaded sum- and difference-frequency generation.	lithium niobate	51-66	xanthine dehydrogenase	Homo sapiens	110-113
18594651-1	2008	We propose and demonstrate that periodically poled lithium niobate (PPLN) can act as an ultrafast three-input XOR gate for differential phase-shift keying (DPSK) signals based on cascaded sum- and difference-frequency generation.	ppln	68-72	xanthine dehydrogenase	Homo sapiens	110-113
18600557-0	2008	Mechanism of transition from xanthine dehydrogenase to xanthine oxidase: effect of guanidine-HCL or urea on the activity.	Guanidine	83-96	xanthine dehydrogenase	Homo sapiens	29-51
18569334-0	2008	Xanthine dehydrogenase processes retinol to retinoic acid in human mammary epithelial cells.	Vitamin A	33-40	xanthine dehydrogenase	Homo sapiens	0-22
18569334-0	2008	Xanthine dehydrogenase processes retinol to retinoic acid in human mammary epithelial cells.	Tretinoin	44-57	xanthine dehydrogenase	Homo sapiens	0-22
18569334-7	2008	To get further knowledge regarding this process we have evaluated the biosynthetic pathway of retinoic acid in a human mammary epithelial cell line (HMEC) in which xanthine dehydrogenase (E.C.	Tretinoin	94-107	xanthine dehydrogenase	Homo sapiens	164-186
18569334-11	2008	After isolation and immunoassay of the cytosolic protein showing retinol oxidizing activity we identified it with the well-known enzyme xanthine dehydrogenase.	Vitamin A	65-72	xanthine dehydrogenase	Homo sapiens	136-158
18569334-12	2008	The NAD+ dependent retinol oxidation catalyzed by xanthine dehydrogenase is strictly dependent on cellular retinol binding proteins and is inhibited by oxypurinol.	NAD	4-8	xanthine dehydrogenase	Homo sapiens	50-72
18569334-12	2008	The NAD+ dependent retinol oxidation catalyzed by xanthine dehydrogenase is strictly dependent on cellular retinol binding proteins and is inhibited by oxypurinol.	Vitamin A	19-26	xanthine dehydrogenase	Homo sapiens	50-72
18569334-12	2008	The NAD+ dependent retinol oxidation catalyzed by xanthine dehydrogenase is strictly dependent on cellular retinol binding proteins and is inhibited by oxypurinol.	Vitamin A	107-114	xanthine dehydrogenase	Homo sapiens	50-72
18569334-12	2008	The NAD+ dependent retinol oxidation catalyzed by xanthine dehydrogenase is strictly dependent on cellular retinol binding proteins and is inhibited by oxypurinol.	Oxypurinol	152-162	xanthine dehydrogenase	Homo sapiens	50-72
18390908-6	2008	Amino acid substitutions at two cysteine residues coordinating FeSI of the two [2Fe-2S] clusters of the enzyme demonstrate that an incomplete assembly of FeSI impairs the formation of the XDH (alphabeta)(2) heterotetramer and, thus, insertion of Moco into the enzyme.	Cysteine	32-40	xanthine dehydrogenase	Homo sapiens	188-191
18600557-0	2008	Mechanism of transition from xanthine dehydrogenase to xanthine oxidase: effect of guanidine-HCL or urea on the activity.	Urea	100-104	xanthine dehydrogenase	Homo sapiens	29-51
18600557-1	2008	Mammalian xanthine oxidoreductase can be converted from the dehydrogenase to the oxidase form, either reversibly by formation of disulfide bridges or irreversibly by proteolytic cleavage within the xanthine oxidoreductase protein molecule.	Disulfides	129-138	xanthine dehydrogenase	Homo sapiens	10-33
18330493-10	2008	CONCLUSION: Xanthine oxidoreductase inhibition by allopurinol in patients with metabolic syndrome reduces oxidative stress, improves endothelial function, ameliorates myeloperoxidase levels and does not have any effect on CRP and fibrinogen levels.	Allopurinol	50-61	xanthine dehydrogenase	Homo sapiens	12-35
18344415-1	2008	In addition to its critical role in purine metabolism, xanthine oxidoreductase (XOR) has been implicated in the development of tissue oxidative damage in a wide variety of respiratory and cardiovascular disorders such as acute lung injury, ischemia-reperfusion injury, atherosclerosis, heart failure, and arterial hypertension.	purine	36-42	xanthine dehydrogenase	Homo sapiens	55-78
18344415-1	2008	In addition to its critical role in purine metabolism, xanthine oxidoreductase (XOR) has been implicated in the development of tissue oxidative damage in a wide variety of respiratory and cardiovascular disorders such as acute lung injury, ischemia-reperfusion injury, atherosclerosis, heart failure, and arterial hypertension.	purine	36-42	xanthine dehydrogenase	Homo sapiens	80-83
18409526-1	2008	Inhibitors of xanthine oxidoreductase decrease production of uric acid, thus they act as hypouricemic drugs.	Uric Acid	61-70	xanthine dehydrogenase	Homo sapiens	14-37
18712049-2	2008	Xanthine dehydrogenase (XDH) produces urate and, in its oxidase isoform, reactive oxygen species.	Uric Acid	38-43	xanthine dehydrogenase	Homo sapiens	0-22
18712049-2	2008	Xanthine dehydrogenase (XDH) produces urate and, in its oxidase isoform, reactive oxygen species.	Uric Acid	38-43	xanthine dehydrogenase	Homo sapiens	24-27
18712049-2	2008	Xanthine dehydrogenase (XDH) produces urate and, in its oxidase isoform, reactive oxygen species.	Reactive Oxygen Species	73-96	xanthine dehydrogenase	Homo sapiens	0-22
18712049-2	2008	Xanthine dehydrogenase (XDH) produces urate and, in its oxidase isoform, reactive oxygen species.	Reactive Oxygen Species	73-96	xanthine dehydrogenase	Homo sapiens	24-27
18409526-2	2008	Allopurinol, a prototypical xanthine oxidoreductase inhibitor, has been widely prescribed for treatment of gout and hyperuricemia.	Allopurinol	0-11	xanthine dehydrogenase	Homo sapiens	28-51
18409526-4	2008	Recently, novel nonpurine selective inhibitors of xanthine oxidoreductase have been developed as potential alternatives to allopurinol.	Allopurinol	123-134	xanthine dehydrogenase	Homo sapiens	50-73
18409528-1	2008	An inhibitor of xanthine dehydrogenase (XDH), allopurinol, and uricosuric agents, probenecid and benzbromarone, have been used for more than 20 years in the treatment of hyperuricemia and gout.	Probenecid	82-92	xanthine dehydrogenase	Homo sapiens	16-38
18409528-1	2008	An inhibitor of xanthine dehydrogenase (XDH), allopurinol, and uricosuric agents, probenecid and benzbromarone, have been used for more than 20 years in the treatment of hyperuricemia and gout.	Benzbromarone	97-110	xanthine dehydrogenase	Homo sapiens	16-38
18409528-6	2008	The dosage reduction of the new XDH inhibitors, febuxostat and FYX-051, is not necessary in patients with renal insufficiency because renal excretion is not main excretory pathway.	Febuxostat	48-58	xanthine dehydrogenase	Homo sapiens	32-35
18409528-6	2008	The dosage reduction of the new XDH inhibitors, febuxostat and FYX-051, is not necessary in patients with renal insufficiency because renal excretion is not main excretory pathway.	FYX-051	63-70	xanthine dehydrogenase	Homo sapiens	32-35
18409529-6	2008	Xanthine oxido-reductase, a key enzyme of uric acid metabolism was indicated as one of regulatory factors in adipocyte differentiation.	Uric Acid	42-51	xanthine dehydrogenase	Homo sapiens	0-24
18344696-3	2008	Its activity is largely the result of the inhibition of xanthine oxidoreductase by oxypurinol, the active metabolite of allopurinol.	Oxypurinol	83-93	xanthine dehydrogenase	Homo sapiens	56-79
18344696-3	2008	Its activity is largely the result of the inhibition of xanthine oxidoreductase by oxypurinol, the active metabolite of allopurinol.	Allopurinol	120-131	xanthine dehydrogenase	Homo sapiens	56-79
18379995-11	2008	But, in inflammatory conditions, xanthine oxidoreductase is expressed leading to detrimentally reduce O(2) and NO(3) (-) into O(2) (*) (-) and NO(*) that may interact, reconstituting the ONOO(-) pool.	o(2)	102-106	xanthine dehydrogenase	Homo sapiens	33-56
18360072-0	2008	Crystal structures of mammalian xanthine oxidoreductase bound with various inhibitors: allopurinol, febuxostat, and FYX-051.	Allopurinol	87-98	xanthine dehydrogenase	Homo sapiens	32-55
18360072-0	2008	Crystal structures of mammalian xanthine oxidoreductase bound with various inhibitors: allopurinol, febuxostat, and FYX-051.	Febuxostat	100-110	xanthine dehydrogenase	Homo sapiens	32-55
18360072-0	2008	Crystal structures of mammalian xanthine oxidoreductase bound with various inhibitors: allopurinol, febuxostat, and FYX-051.	FYX-051	116-123	xanthine dehydrogenase	Homo sapiens	32-55
18360072-1	2008	Xanthine oxidoreductase (XOR) catalyzes the reaction of hypoxanthine to xanthine and of xanthine to uric acid.	Hypoxanthine	56-68	xanthine dehydrogenase	Homo sapiens	0-23
18360072-1	2008	Xanthine oxidoreductase (XOR) catalyzes the reaction of hypoxanthine to xanthine and of xanthine to uric acid.	Hypoxanthine	56-68	xanthine dehydrogenase	Homo sapiens	25-28
18360072-1	2008	Xanthine oxidoreductase (XOR) catalyzes the reaction of hypoxanthine to xanthine and of xanthine to uric acid.	Xanthine	60-68	xanthine dehydrogenase	Homo sapiens	0-23
18360072-1	2008	Xanthine oxidoreductase (XOR) catalyzes the reaction of hypoxanthine to xanthine and of xanthine to uric acid.	Xanthine	60-68	xanthine dehydrogenase	Homo sapiens	25-28
18360072-1	2008	Xanthine oxidoreductase (XOR) catalyzes the reaction of hypoxanthine to xanthine and of xanthine to uric acid.	Xanthine	72-80	xanthine dehydrogenase	Homo sapiens	0-23
18360072-1	2008	Xanthine oxidoreductase (XOR) catalyzes the reaction of hypoxanthine to xanthine and of xanthine to uric acid.	Xanthine	72-80	xanthine dehydrogenase	Homo sapiens	25-28
18360072-1	2008	Xanthine oxidoreductase (XOR) catalyzes the reaction of hypoxanthine to xanthine and of xanthine to uric acid.	Uric Acid	100-109	xanthine dehydrogenase	Homo sapiens	0-23
18360072-1	2008	Xanthine oxidoreductase (XOR) catalyzes the reaction of hypoxanthine to xanthine and of xanthine to uric acid.	Uric Acid	100-109	xanthine dehydrogenase	Homo sapiens	25-28
18360072-2	2008	Inhibitors of XOR can thus decrease the concentration of uric acid in serum.	Uric Acid	57-66	xanthine dehydrogenase	Homo sapiens	14-17
18067304-1	2008	The electrode functionalized with glucose oxidase (GOx) and microperoxidase-11 (MP-11) performs various Boolean logic operations (OR, XOR, AND-OR) upon addition of glucose and/or H2O2 and application of different potentials.	Glucose	34-41	xanthine dehydrogenase	Homo sapiens	134-137
19096112-4	2008	However its formation is connected to the conversion of Xanthine dehydrogenase (XDH) to Xanthine oxidase (XO) which leads to concomitant production of free radicals.	Free Radicals	151-164	xanthine dehydrogenase	Homo sapiens	56-78
19096112-4	2008	However its formation is connected to the conversion of Xanthine dehydrogenase (XDH) to Xanthine oxidase (XO) which leads to concomitant production of free radicals.	Free Radicals	151-164	xanthine dehydrogenase	Homo sapiens	80-83
18636784-20	2008	Febuxostat is a new xanthine oxidoreductase inhibitor, which is still in clinical trials, but abnormal liver function is the most commonly reported adverse reaction.Even assuming a causal relationship between benzbromarone and hepatotoxicity in the identified cases, benefit-risk assessment based on total exposure to the drug does not support the decision by the drug company to withdraw benzbromarone from the market given the paucity of alternative options.	Febuxostat	0-10	xanthine dehydrogenase	Homo sapiens	20-43
18379995-11	2008	But, in inflammatory conditions, xanthine oxidoreductase is expressed leading to detrimentally reduce O(2) and NO(3) (-) into O(2) (*) (-) and NO(*) that may interact, reconstituting the ONOO(-) pool.	o(2)	126-130	xanthine dehydrogenase	Homo sapiens	33-56
18379995-11	2008	But, in inflammatory conditions, xanthine oxidoreductase is expressed leading to detrimentally reduce O(2) and NO(3) (-) into O(2) (*) (-) and NO(*) that may interact, reconstituting the ONOO(-) pool.	onoo	187-191	xanthine dehydrogenase	Homo sapiens	33-56
17761779-0	2007	Characterization of N-glucuronidation of 4-(5-pyridin-4-yl-1H-[1,2,4]triazol-3-yl) pyridine-2-carbonitrile (FYX-051): a new xanthine oxidoreductase inhibitor.	Nitrogen	20-21	xanthine dehydrogenase	Homo sapiens	124-147
17761779-0	2007	Characterization of N-glucuronidation of 4-(5-pyridin-4-yl-1H-[1,2,4]triazol-3-yl) pyridine-2-carbonitrile (FYX-051): a new xanthine oxidoreductase inhibitor.	FYX-051	41-106	xanthine dehydrogenase	Homo sapiens	124-147
17761779-0	2007	Characterization of N-glucuronidation of 4-(5-pyridin-4-yl-1H-[1,2,4]triazol-3-yl) pyridine-2-carbonitrile (FYX-051): a new xanthine oxidoreductase inhibitor.	FYX-051	108-115	xanthine dehydrogenase	Homo sapiens	124-147
18039602-3	2007	APRT deficiency results in adenine accumulation with oxidation by xanthine dehydrogenase (XDH; EC 1.1.1.204) to 2,8-dihydroxyadenine (2,8-DHA) then excreted in urine.	Adenine	27-34	xanthine dehydrogenase	Homo sapiens	90-93
17569214-1	2007	Curcumin possesses anti-inflammatory activity and is a potent inhibitor of reactive-oxygen-generating enzymes such as lipoxygenase/cyclooxygenase, xanthine dehydrogenase/oxidase, and inducible nitric oxide synthase (iNOS); it is an effective inducer of heme oxygenase-1.	Curcumin	0-8	xanthine dehydrogenase	Homo sapiens	147-177
18039602-3	2007	APRT deficiency results in adenine accumulation with oxidation by xanthine dehydrogenase (XDH; EC 1.1.1.204) to 2,8-dihydroxyadenine (2,8-DHA) then excreted in urine.	2,8-dihydroxyadenine	112-132	xanthine dehydrogenase	Homo sapiens	90-93
17704913-1	2007	Molybdenum cofactor is essential for the function of three human enzymes: sulphite oxidase, xanthine dehydrogenase, and aldehyde oxidase.	Molybdenum	0-10	xanthine dehydrogenase	Homo sapiens	92-114
17523077-2	2007	The aim of the present paper was to investigate whether the enzymes xanthine oxidoreductase/xanthine oxidase known to generate reactive oxygen species contribute to oxidative reactions on the ocular surface.	Reactive Oxygen Species	127-150	xanthine dehydrogenase	Homo sapiens	68-91
17370312-0	2007	PD98059 enhanced insulin, cytokine, and growth factor activation of xanthine oxidoreductase in epithelial cells involves STAT3 and the glucocorticoid receptor.	2-(2-amino-3-methoxyphenyl)-4H-1-benzopyran-4-one	0-7	xanthine dehydrogenase	Homo sapiens	68-91
17370312-4	2007	The XOR reporter gene was activated by the epidermal growth factors (EGF), prolactin, and dexamethasone and by the acute phase cytokines (APC) IL-1, IL-6, and TNFalpha as previously reported for its native gene, and insulin further stimulated activation induced with acute phase cytokines or growth factors.	Dexamethasone	90-103	xanthine dehydrogenase	Homo sapiens	4-7
17370312-7	2007	Analysis of the XOR upstream DNA and proximal promoter revealed primary roles for the GR and STAT3 in mediating the effects of PD98059 on XOR activation and protein complex formation with the promoter.	2-(2-amino-3-methoxyphenyl)-4H-1-benzopyran-4-one	127-134	xanthine dehydrogenase	Homo sapiens	16-19
17370312-7	2007	Analysis of the XOR upstream DNA and proximal promoter revealed primary roles for the GR and STAT3 in mediating the effects of PD98059 on XOR activation and protein complex formation with the promoter.	2-(2-amino-3-methoxyphenyl)-4H-1-benzopyran-4-one	127-134	xanthine dehydrogenase	Homo sapiens	138-141
17370312-9	2007	XOR activation by PD98059, dexamethasone, or insulin was superinduced by a constitutively active derivative of STAT3, while a dominant negative derivative of STAT3 blocked the enhancing effect of PD98059 on XOR activation.	2-(2-amino-3-methoxyphenyl)-4H-1-benzopyran-4-one	18-25	xanthine dehydrogenase	Homo sapiens	0-3
17370312-9	2007	XOR activation by PD98059, dexamethasone, or insulin was superinduced by a constitutively active derivative of STAT3, while a dominant negative derivative of STAT3 blocked the enhancing effect of PD98059 on XOR activation.	Dexamethasone	27-40	xanthine dehydrogenase	Homo sapiens	0-3
17370312-9	2007	XOR activation by PD98059, dexamethasone, or insulin was superinduced by a constitutively active derivative of STAT3, while a dominant negative derivative of STAT3 blocked the enhancing effect of PD98059 on XOR activation.	Dexamethasone	27-40	xanthine dehydrogenase	Homo sapiens	207-210
17370312-9	2007	XOR activation by PD98059, dexamethasone, or insulin was superinduced by a constitutively active derivative of STAT3, while a dominant negative derivative of STAT3 blocked the enhancing effect of PD98059 on XOR activation.	2-(2-amino-3-methoxyphenyl)-4H-1-benzopyran-4-one	196-203	xanthine dehydrogenase	Homo sapiens	0-3
17370312-9	2007	XOR activation by PD98059, dexamethasone, or insulin was superinduced by a constitutively active derivative of STAT3, while a dominant negative derivative of STAT3 blocked the enhancing effect of PD98059 on XOR activation.	2-(2-amino-3-methoxyphenyl)-4H-1-benzopyran-4-one	196-203	xanthine dehydrogenase	Homo sapiens	207-210
17440754-0	2007	NADH oxidase activity of rat and human liver xanthine oxidoreductase: potential role in superoxide production.	Superoxides	88-98	xanthine dehydrogenase	Homo sapiens	45-68
17622935-2	2007	Xanthine oxidoreductase is one of the enzymes producing free radicals in the cardiovascular system, and it can contribute to the increment of the oxidative stress and, consequently, blood pressure.	Free Radicals	56-69	xanthine dehydrogenase	Homo sapiens	0-23
17362040-5	2007	This behavior of dyad 9 could be interpreted by a two-input INH logic gate, while in the presence of Fe(III), the ion complex of 9 could execute a two-input XOR logic gate.	ferric sulfate	101-108	xanthine dehydrogenase	Homo sapiens	157-160
17301076-0	2007	Two mutations convert mammalian xanthine oxidoreductase to highly superoxide-productive xanthine oxidase.	Superoxides	66-76	xanthine dehydrogenase	Homo sapiens	32-55
17301076-1	2007	Reactive oxygen species are generated by various systems, including NADPH oxidases, xanthine oxidoreductase (XOR) and mitochondrial respiratory enzymes, and contribute to many physiological and pathological phenomena.	Reactive Oxygen Species	0-23	xanthine dehydrogenase	Homo sapiens	84-107
17301076-1	2007	Reactive oxygen species are generated by various systems, including NADPH oxidases, xanthine oxidoreductase (XOR) and mitochondrial respiratory enzymes, and contribute to many physiological and pathological phenomena.	Reactive Oxygen Species	0-23	xanthine dehydrogenase	Homo sapiens	109-112
17301076-2	2007	Mammalian xanthine dehydrogenase (XDH) can be converted to xanthine oxidase (XO), which produces both superoxide anion and hydrogen peroxide in a molar ratio of about 1:3, depending upon the conditions.	Superoxides	102-118	xanthine dehydrogenase	Homo sapiens	10-32
17301076-2	2007	Mammalian xanthine dehydrogenase (XDH) can be converted to xanthine oxidase (XO), which produces both superoxide anion and hydrogen peroxide in a molar ratio of about 1:3, depending upon the conditions.	Superoxides	102-118	xanthine dehydrogenase	Homo sapiens	34-37
17301076-2	2007	Mammalian xanthine dehydrogenase (XDH) can be converted to xanthine oxidase (XO), which produces both superoxide anion and hydrogen peroxide in a molar ratio of about 1:3, depending upon the conditions.	Hydrogen Peroxide	123-140	xanthine dehydrogenase	Homo sapiens	10-32
17301076-2	2007	Mammalian xanthine dehydrogenase (XDH) can be converted to xanthine oxidase (XO), which produces both superoxide anion and hydrogen peroxide in a molar ratio of about 1:3, depending upon the conditions.	Hydrogen Peroxide	123-140	xanthine dehydrogenase	Homo sapiens	34-37
17301076-4	2007	In the mutant, tryptophan 335, which is a component of the amino acid cluster crucial for switching from the XDH to the XO conformation, was replaced with alanine, and phenylalanine 336, which modulates FAD"s redox potential through stacking interactions with the flavin cofactor, was changed to leucine.	Tryptophan	15-25	xanthine dehydrogenase	Homo sapiens	109-112
17301076-8	2007	These results are consistent with the idea that the XDH and XO forms of the mutant are in an equilibrium that greatly favours the XO form, but the equilibrium is partly shifted towards the XDH form upon incubation with dithiothreitol.	Dithiothreitol	219-233	xanthine dehydrogenase	Homo sapiens	52-55
17301076-8	2007	These results are consistent with the idea that the XDH and XO forms of the mutant are in an equilibrium that greatly favours the XO form, but the equilibrium is partly shifted towards the XDH form upon incubation with dithiothreitol.	Dithiothreitol	219-233	xanthine dehydrogenase	Homo sapiens	189-192
17301077-2	2007	Here we show that mutation of two amino acid residues in the active site of human XOR for purine substrates results in conversion of the substrate preference to AO type.	purine	90-96	xanthine dehydrogenase	Homo sapiens	82-85
17569214-1	2007	Curcumin possesses anti-inflammatory activity and is a potent inhibitor of reactive-oxygen-generating enzymes such as lipoxygenase/cyclooxygenase, xanthine dehydrogenase/oxidase, and inducible nitric oxide synthase (iNOS); it is an effective inducer of heme oxygenase-1.	reactive-oxygen	75-90	xanthine dehydrogenase	Homo sapiens	147-177
16540390-1	2006	Xanthine oxidoreductase (XOR) activity has been previously noted to be responsive to changes in O2 tension.	Oxygen	96-98	xanthine dehydrogenase	Homo sapiens	0-23
17590984-5	2007	Additional sources of acetaldehyde include other minor enzymes (nitric oxide synthase, other cytochrome P450s, P450 reductase, xanthine oxidoreductase) as well as non-enzymatic pathways (formation of hydroxyethyl radicals from the reaction of ethanol with hydroxyl radical, and its subsequent decomposition to acetaldehyde).	Acetaldehyde	22-34	xanthine dehydrogenase	Homo sapiens	127-150
16935971-1	2006	BACKGROUND: Xanthine oxidoreductase (XOR) is a key enzyme in the degradation of DNA, RNA and high-energy phosphates.	Phosphates	105-115	xanthine dehydrogenase	Homo sapiens	12-35
16935971-1	2006	BACKGROUND: Xanthine oxidoreductase (XOR) is a key enzyme in the degradation of DNA, RNA and high-energy phosphates.	Phosphates	105-115	xanthine dehydrogenase	Homo sapiens	37-40
16572497-0	2006	TiO2-based light-driven XOR/INH logic gates.	titanium dioxide	0-4	xanthine dehydrogenase	Homo sapiens	24-27
16540390-1	2006	Xanthine oxidoreductase (XOR) activity has been previously noted to be responsive to changes in O2 tension.	Oxygen	96-98	xanthine dehydrogenase	Homo sapiens	25-28
16540390-2	2006	While prior studies have focused on the extremes (0-3% and 95-100%) of O2 tensions, we report the influence of 10% O2 on endothelial cell XOR, a concentration resembling modest arterial hypoxia commonly found in patients with chronic cardiopulmonary diseases.	Oxygen	115-117	xanthine dehydrogenase	Homo sapiens	138-141
16540390-4	2006	Concomitantly, there was a 3-fold increase in XOR activity, XOR-dependent reactive oxygen species production, and cellular export of active enzyme.	Reactive Oxygen Species	74-97	xanthine dehydrogenase	Homo sapiens	60-63
16540390-7	2006	Treatment of control cells with adenosine resulted in increased XOR activity similar to hypoxia.	Adenosine	32-41	xanthine dehydrogenase	Homo sapiens	64-67
16540390-9	2006	Combined, these data reveal that moderate hypoxia significantly enhances endothelial XOR specific activity, release, and XOR-derived reactive oxygen species generation.	Reactive Oxygen Species	133-156	xanthine dehydrogenase	Homo sapiens	121-124
15958620-1	2005	PURPOSE: Xanthine oxidoreductase (XOR) is a key enzyme in the degradation of DNA, RNA, and high-energy phosphates and also plays a role in milk lipid globule secretion.	Phosphates	103-113	xanthine dehydrogenase	Homo sapiens	9-32
16572688-2	2006	Using the XOR interferometer, we measure the refractive indices of silicon and ruthenium, essential materials for extreme-ultraviolet lithography.	Silicon	67-74	xanthine dehydrogenase	Homo sapiens	10-13
16572688-2	2006	Using the XOR interferometer, we measure the refractive indices of silicon and ruthenium, essential materials for extreme-ultraviolet lithography.	Ruthenium	79-88	xanthine dehydrogenase	Homo sapiens	10-13
16669776-6	2006	(3) Aldehyde oxidase catalyzes the last step of abscisic acid biosynthesis, and (4) xanthine dehydrogenase is essential for purine degradation and stress response.	Abscisic Acid	48-61	xanthine dehydrogenase	Homo sapiens	84-106
16669776-6	2006	(3) Aldehyde oxidase catalyzes the last step of abscisic acid biosynthesis, and (4) xanthine dehydrogenase is essential for purine degradation and stress response.	purine	124-130	xanthine dehydrogenase	Homo sapiens	84-106
16382292-2	2005	The transformation of hypoxanthine to xanthine and the conversion of the latter into uric acid, which occur in purine catabolism, are catalysed by xanthine oxidoreductase.	Hypoxanthine	22-34	xanthine dehydrogenase	Homo sapiens	147-170
16382292-2	2005	The transformation of hypoxanthine to xanthine and the conversion of the latter into uric acid, which occur in purine catabolism, are catalysed by xanthine oxidoreductase.	Xanthine	26-34	xanthine dehydrogenase	Homo sapiens	147-170
16382292-2	2005	The transformation of hypoxanthine to xanthine and the conversion of the latter into uric acid, which occur in purine catabolism, are catalysed by xanthine oxidoreductase.	Uric Acid	85-94	xanthine dehydrogenase	Homo sapiens	147-170
16382292-2	2005	The transformation of hypoxanthine to xanthine and the conversion of the latter into uric acid, which occur in purine catabolism, are catalysed by xanthine oxidoreductase.	purine	111-117	xanthine dehydrogenase	Homo sapiens	147-170
16382292-3	2005	The constitutive xanthine dehydrogenase form of this enzyme generally uses NAD(+) as an electron acceptor, whereas the post-translational xanthine oxidase form uses molecular oxygen and yields four units of reactive oxygen species per unit of transformed substrate.	NAD	75-81	xanthine dehydrogenase	Homo sapiens	17-39
16382292-3	2005	The constitutive xanthine dehydrogenase form of this enzyme generally uses NAD(+) as an electron acceptor, whereas the post-translational xanthine oxidase form uses molecular oxygen and yields four units of reactive oxygen species per unit of transformed substrate.	Reactive Oxygen Species	207-230	xanthine dehydrogenase	Homo sapiens	17-39
16382292-4	2005	Allopurinol and oxypurinol inhibit xanthine oxidoreductase and thus diminish the generation of reactive species and decrease plasma uric acid.	Allopurinol	0-11	xanthine dehydrogenase	Homo sapiens	35-58
16382292-4	2005	Allopurinol and oxypurinol inhibit xanthine oxidoreductase and thus diminish the generation of reactive species and decrease plasma uric acid.	Oxypurinol	16-26	xanthine dehydrogenase	Homo sapiens	35-58
16382292-4	2005	Allopurinol and oxypurinol inhibit xanthine oxidoreductase and thus diminish the generation of reactive species and decrease plasma uric acid.	Uric Acid	132-141	xanthine dehydrogenase	Homo sapiens	35-58
15932950-1	2005	Molybdenum hydroxylases, aldehyde oxidase and xanthine oxidoreductase, were shown to be involved in the nitroreduction of 2-nitrofluorene (NF), 1-nitropyrene, and 4-nitrobiphenyl, environmental pollutants, in the skin of various mammalian species.	2-nitrofluorene	122-137	xanthine dehydrogenase	Homo sapiens	46-69
15932950-1	2005	Molybdenum hydroxylases, aldehyde oxidase and xanthine oxidoreductase, were shown to be involved in the nitroreduction of 2-nitrofluorene (NF), 1-nitropyrene, and 4-nitrobiphenyl, environmental pollutants, in the skin of various mammalian species.	1-nitropyrene	144-157	xanthine dehydrogenase	Homo sapiens	46-69
15932950-3	2005	Inhibitors of aldehyde oxidase markedly inhibited these nitroreductase activities, but oxypurinol, an inhibitor of xanthine oxidoreductase, had little effect.	Oxypurinol	87-97	xanthine dehydrogenase	Homo sapiens	115-138
15932950-10	2005	These skin cytosols of various mammals also exhibited significant 2-hydroxypyrimidine-linked nitroreductase activities toward 1-nitropyrene and 4-nitrobiphenyl catalyzed by aldehyde oxidase and xanthine oxidoreductase.	1-nitropyrene	126-139	xanthine dehydrogenase	Homo sapiens	194-217
16602626-1	2005	Reactive oxygen species (ROS) generated by xanthine oxidoreductase (XOR) were toxic to B lymphoma-derived Raji cells (positive for 8A monoclonal antibody, mAb).	Reactive Oxygen Species	0-23	xanthine dehydrogenase	Homo sapiens	43-66
16602626-1	2005	Reactive oxygen species (ROS) generated by xanthine oxidoreductase (XOR) were toxic to B lymphoma-derived Raji cells (positive for 8A monoclonal antibody, mAb).	Reactive Oxygen Species	0-23	xanthine dehydrogenase	Homo sapiens	68-71
16602626-1	2005	Reactive oxygen species (ROS) generated by xanthine oxidoreductase (XOR) were toxic to B lymphoma-derived Raji cells (positive for 8A monoclonal antibody, mAb).	Reactive Oxygen Species	25-28	xanthine dehydrogenase	Homo sapiens	43-66
16602626-1	2005	Reactive oxygen species (ROS) generated by xanthine oxidoreductase (XOR) were toxic to B lymphoma-derived Raji cells (positive for 8A monoclonal antibody, mAb).	Reactive Oxygen Species	25-28	xanthine dehydrogenase	Homo sapiens	68-71
16602626-3	2005	The understanding of the mechanisms of cytotoxicity induced by XOR-produced ROS is essential in view of a possible clinical application.	Reactive Oxygen Species	76-79	xanthine dehydrogenase	Homo sapiens	63-66
16602626-5	2005	Catalase, but not superoxide dismutase, protected cells from the toxicity of XOR, thus indicating that cell damage depended on the production of hydrogen peroxide.	Hydrogen Peroxide	145-162	xanthine dehydrogenase	Homo sapiens	77-80
16602626-6	2005	The toxicity of ROS was selectively targeted to malignant Raji cells by antibody-XOR conjugation, either directly, with an 8A-XOR conjugate, or indirectly, with an 8A mAb plus an anti-mouse IgG-XOR.	Reactive Oxygen Species	16-19	xanthine dehydrogenase	Homo sapiens	81-84
16602626-6	2005	The toxicity of ROS was selectively targeted to malignant Raji cells by antibody-XOR conjugation, either directly, with an 8A-XOR conjugate, or indirectly, with an 8A mAb plus an anti-mouse IgG-XOR.	Reactive Oxygen Species	16-19	xanthine dehydrogenase	Homo sapiens	126-129
16602626-6	2005	The toxicity of ROS was selectively targeted to malignant Raji cells by antibody-XOR conjugation, either directly, with an 8A-XOR conjugate, or indirectly, with an 8A mAb plus an anti-mouse IgG-XOR.	Reactive Oxygen Species	16-19	xanthine dehydrogenase	Homo sapiens	126-129
15958620-1	2005	PURPOSE: Xanthine oxidoreductase (XOR) is a key enzyme in the degradation of DNA, RNA, and high-energy phosphates and also plays a role in milk lipid globule secretion.	Phosphates	103-113	xanthine dehydrogenase	Homo sapiens	34-37
16128162-5	2005	The Authors briefly review the xanthine oxido-reductase enzyme system and in particular analyse the latest evidence reported in the literature on allopurinol in the treatment of heart failure.	Allopurinol	146-157	xanthine dehydrogenase	Homo sapiens	31-55
15679468-0	2005	Molecular characterization of human xanthine oxidoreductase: the enzyme is grossly deficient in molybdenum and substantially deficient in iron-sulphur centres.	Iron	138-142	xanthine dehydrogenase	Homo sapiens	36-59
15788238-2	2005	The only enzymatic source of urate is xanthine oxidoreductase.	Uric Acid	29-34	xanthine dehydrogenase	Homo sapiens	38-61
15788238-3	2005	If a major purpose of xanthine oxidoreductase is the production of urate to function as an iron chelator and antioxidant, a system for coupling the activity of this enzyme to the availability of catalytically-active metal would be required.	Uric Acid	67-72	xanthine dehydrogenase	Homo sapiens	22-45
15788238-3	2005	If a major purpose of xanthine oxidoreductase is the production of urate to function as an iron chelator and antioxidant, a system for coupling the activity of this enzyme to the availability of catalytically-active metal would be required.	Iron	91-95	xanthine dehydrogenase	Homo sapiens	22-45
15788238-3	2005	If a major purpose of xanthine oxidoreductase is the production of urate to function as an iron chelator and antioxidant, a system for coupling the activity of this enzyme to the availability of catalytically-active metal would be required.	Metals	216-221	xanthine dehydrogenase	Homo sapiens	22-45
16375736-2	2005	The final two reactions of its production catalyzing the conversion of hypoxanthine to xanthine and the latter to uric acid are catalysed by the enzyme xanthine oxidoreductase, which may attain two inter-convertible forms, namely xanthine dehydrogenase or xanthine oxidase.	Hypoxanthine	71-83	xanthine dehydrogenase	Homo sapiens	152-175
16375736-2	2005	The final two reactions of its production catalyzing the conversion of hypoxanthine to xanthine and the latter to uric acid are catalysed by the enzyme xanthine oxidoreductase, which may attain two inter-convertible forms, namely xanthine dehydrogenase or xanthine oxidase.	Hypoxanthine	71-83	xanthine dehydrogenase	Homo sapiens	230-252
16375736-2	2005	The final two reactions of its production catalyzing the conversion of hypoxanthine to xanthine and the latter to uric acid are catalysed by the enzyme xanthine oxidoreductase, which may attain two inter-convertible forms, namely xanthine dehydrogenase or xanthine oxidase.	Xanthine	75-83	xanthine dehydrogenase	Homo sapiens	152-175
16375736-2	2005	The final two reactions of its production catalyzing the conversion of hypoxanthine to xanthine and the latter to uric acid are catalysed by the enzyme xanthine oxidoreductase, which may attain two inter-convertible forms, namely xanthine dehydrogenase or xanthine oxidase.	Xanthine	75-83	xanthine dehydrogenase	Homo sapiens	230-252
16375736-2	2005	The final two reactions of its production catalyzing the conversion of hypoxanthine to xanthine and the latter to uric acid are catalysed by the enzyme xanthine oxidoreductase, which may attain two inter-convertible forms, namely xanthine dehydrogenase or xanthine oxidase.	Uric Acid	114-123	xanthine dehydrogenase	Homo sapiens	152-175
16375736-2	2005	The final two reactions of its production catalyzing the conversion of hypoxanthine to xanthine and the latter to uric acid are catalysed by the enzyme xanthine oxidoreductase, which may attain two inter-convertible forms, namely xanthine dehydrogenase or xanthine oxidase.	Uric Acid	114-123	xanthine dehydrogenase	Homo sapiens	230-252
16375736-6	2005	Also, allopurinol, a xanthine oxidoreductase inhibitor that lowers serum levels of uric acid exerts protective effects in situations associated with oxidative stress (e.g. ischaemia-reperfusion injury, cardiovascular disease).	Allopurinol	6-17	xanthine dehydrogenase	Homo sapiens	21-44
16375736-6	2005	Also, allopurinol, a xanthine oxidoreductase inhibitor that lowers serum levels of uric acid exerts protective effects in situations associated with oxidative stress (e.g. ischaemia-reperfusion injury, cardiovascular disease).	Uric Acid	83-92	xanthine dehydrogenase	Homo sapiens	21-44
15148401-3	2004	Here, we present the crystal structure of the key intermediate in the hydroxylation reaction of xanthine oxidoreductase with a slow substrate, in which the carbon-oxygen bond of the product is formed, yet the product remains complexed to the molybdenum.	Carbon	156-162	xanthine dehydrogenase	Homo sapiens	96-119
15486091-2	2004	Here, we demonstrate that xanthine oxidoreductase (XOR), a prototypic superoxide O(2)(.-) -producing enzyme, and neuronal nitric oxide synthase (NOS1) coimmunoprecipitate and colocalize in the sarcoplasmic reticulum of cardiac myocytes.	superoxide o(2)	70-85	xanthine dehydrogenase	Homo sapiens	26-49
15486091-2	2004	Here, we demonstrate that xanthine oxidoreductase (XOR), a prototypic superoxide O(2)(.-) -producing enzyme, and neuronal nitric oxide synthase (NOS1) coimmunoprecipitate and colocalize in the sarcoplasmic reticulum of cardiac myocytes.	superoxide o(2)	70-85	xanthine dehydrogenase	Homo sapiens	51-54
15486091-3	2004	Deficiency of NOS1 (but not endothelial NOS, NOS3) leads to profound increases in XOR-mediated O(2)(.-) production, which in turn depresses myocardial excitation-contraction coupling in a manner reversible by XOR inhibition with allopurinol.	Superoxides	95-99	xanthine dehydrogenase	Homo sapiens	82-85
15486091-3	2004	Deficiency of NOS1 (but not endothelial NOS, NOS3) leads to profound increases in XOR-mediated O(2)(.-) production, which in turn depresses myocardial excitation-contraction coupling in a manner reversible by XOR inhibition with allopurinol.	Allopurinol	229-240	xanthine dehydrogenase	Homo sapiens	82-85
15486091-4	2004	These data demonstrate a unique interaction between a nitric oxide and an O(2)(.-) -generating enzyme that accounts for crosstalk between these signaling pathways; these findings demonstrate a direct antioxidant mechanism for NOS1 and have pathophysiologic implications for the growing number of disease states in which increased XOR activity plays a role.	Nitric Oxide	54-66	xanthine dehydrogenase	Homo sapiens	330-333
15486091-4	2004	These data demonstrate a unique interaction between a nitric oxide and an O(2)(.-) -generating enzyme that accounts for crosstalk between these signaling pathways; these findings demonstrate a direct antioxidant mechanism for NOS1 and have pathophysiologic implications for the growing number of disease states in which increased XOR activity plays a role.	Superoxides	74-82	xanthine dehydrogenase	Homo sapiens	330-333
15600349-12	2004	(2H+).2] exhibit two distinct optical outputs (a naphthalene-based and a Ru(bpy)-based emission) that behave according to an XOR and an XNOR logic, respectively.	Deuterium	1-3	xanthine dehydrogenase	Homo sapiens	125-128
15600349-12	2004	(2H+).2] exhibit two distinct optical outputs (a naphthalene-based and a Ru(bpy)-based emission) that behave according to an XOR and an XNOR logic, respectively.	naphthalene	49-60	xanthine dehydrogenase	Homo sapiens	125-128
15451061-1	2004	Xanthine oxidoreductase (XOR) is a widely distributed enzyme, involved in the metabolism of purines, which generates superoxide and is thought to be involved in free radical-generated tissue injury.	Purines	92-99	xanthine dehydrogenase	Homo sapiens	0-23
15451061-1	2004	Xanthine oxidoreductase (XOR) is a widely distributed enzyme, involved in the metabolism of purines, which generates superoxide and is thought to be involved in free radical-generated tissue injury.	Purines	92-99	xanthine dehydrogenase	Homo sapiens	25-28
15451061-1	2004	Xanthine oxidoreductase (XOR) is a widely distributed enzyme, involved in the metabolism of purines, which generates superoxide and is thought to be involved in free radical-generated tissue injury.	Superoxides	117-127	xanthine dehydrogenase	Homo sapiens	0-23
15451061-1	2004	Xanthine oxidoreductase (XOR) is a widely distributed enzyme, involved in the metabolism of purines, which generates superoxide and is thought to be involved in free radical-generated tissue injury.	Superoxides	117-127	xanthine dehydrogenase	Homo sapiens	25-28
15451061-1	2004	Xanthine oxidoreductase (XOR) is a widely distributed enzyme, involved in the metabolism of purines, which generates superoxide and is thought to be involved in free radical-generated tissue injury.	Free Radicals	161-173	xanthine dehydrogenase	Homo sapiens	0-23
15451061-1	2004	Xanthine oxidoreductase (XOR) is a widely distributed enzyme, involved in the metabolism of purines, which generates superoxide and is thought to be involved in free radical-generated tissue injury.	Free Radicals	161-173	xanthine dehydrogenase	Homo sapiens	25-28
15201667-2	2004	Xanthine oxidoreductase (XOR) may constitute a relevant reactive oxygen species (ROS) source.	Reactive Oxygen Species	56-79	xanthine dehydrogenase	Homo sapiens	0-23
15201667-2	2004	Xanthine oxidoreductase (XOR) may constitute a relevant reactive oxygen species (ROS) source.	Reactive Oxygen Species	56-79	xanthine dehydrogenase	Homo sapiens	25-28
15201667-2	2004	Xanthine oxidoreductase (XOR) may constitute a relevant reactive oxygen species (ROS) source.	Reactive Oxygen Species	81-84	xanthine dehydrogenase	Homo sapiens	0-23
15201667-2	2004	Xanthine oxidoreductase (XOR) may constitute a relevant reactive oxygen species (ROS) source.	Reactive Oxygen Species	81-84	xanthine dehydrogenase	Homo sapiens	25-28
15201667-5	2004	to modulate acute rejection by tungsten administration, a specific inhibitor of XOR.	Tungsten	31-39	xanthine dehydrogenase	Homo sapiens	80-83
15201667-9	2004	Oxygen radicals were generated to a significant degree by enhanced XOR activity, which increased more than 10-fold in renal allografts at day 9 posttransplantation; XOR protein in glomeruli and tubulointerstitium was also elevated in allo-grafts.	Reactive Oxygen Species	0-15	xanthine dehydrogenase	Homo sapiens	67-70
15201667-9	2004	Oxygen radicals were generated to a significant degree by enhanced XOR activity, which increased more than 10-fold in renal allografts at day 9 posttransplantation; XOR protein in glomeruli and tubulointerstitium was also elevated in allo-grafts.	Reactive Oxygen Species	0-15	xanthine dehydrogenase	Homo sapiens	165-168
15201667-12	2004	Tungsten treatment resulted in a pronounced reduction of XOR activity and ROS production, without any effect on NADPH-oxidase activity; mononuclear cell infiltration and rejection signs were significantly ameliorated at day 9 post-transplantation by selective inhibition of XOR.	Tungsten	0-8	xanthine dehydrogenase	Homo sapiens	57-60
15201667-12	2004	Tungsten treatment resulted in a pronounced reduction of XOR activity and ROS production, without any effect on NADPH-oxidase activity; mononuclear cell infiltration and rejection signs were significantly ameliorated at day 9 post-transplantation by selective inhibition of XOR.	Tungsten	0-8	xanthine dehydrogenase	Homo sapiens	274-277
15201667-13	2004	CONCLUSIONS: A major part of ROS generation in acute rejection was contributed by XOR.	Reactive Oxygen Species	29-32	xanthine dehydrogenase	Homo sapiens	82-85
15201667-14	2004	ROS are not only associated with but also contribute to acute allograft rejection because inhibition of XOR alleviated rejection phenomena.	Reactive Oxygen Species	0-3	xanthine dehydrogenase	Homo sapiens	104-107
15148401-3	2004	Here, we present the crystal structure of the key intermediate in the hydroxylation reaction of xanthine oxidoreductase with a slow substrate, in which the carbon-oxygen bond of the product is formed, yet the product remains complexed to the molybdenum.	Oxygen	163-169	xanthine dehydrogenase	Homo sapiens	96-119
16220932-1	2003	Spectroscopic changes from a solution of the amphophile 5,10,15,20-tetraphenylporphyrin in N,N-dimethylformamide using inputs of acid (HClaq) and base (KOBut) are interpreted as XOR and INHIBIT logic operations.	amphophile	45-55	xanthine dehydrogenase	Homo sapiens	178-181
15237859-5	2004	It is argued here that XOR-derived ROS and RNS play a role in innate immunity, specifically in the inflammatory response and in anti-microbial defense of the gastrointestinal tract.	Reactive Oxygen Species	35-38	xanthine dehydrogenase	Homo sapiens	23-26
15114092-3	2004	Xanthine oxidoreductase (XOR) and neutrophil activation, two sources of reactive oxygen species, could play a role in the development of graft dysfunction.	Reactive Oxygen Species	72-95	xanthine dehydrogenase	Homo sapiens	0-23
15114092-3	2004	Xanthine oxidoreductase (XOR) and neutrophil activation, two sources of reactive oxygen species, could play a role in the development of graft dysfunction.	Reactive Oxygen Species	72-95	xanthine dehydrogenase	Homo sapiens	25-28
14694147-2	2004	Biochemical, molecular and pharmacological studies further implicate xanthine oxidoreductase (XOR) as a source of reactive oxygen species in the cardiovascular system.	Reactive Oxygen Species	114-137	xanthine dehydrogenase	Homo sapiens	69-92
14694147-2	2004	Biochemical, molecular and pharmacological studies further implicate xanthine oxidoreductase (XOR) as a source of reactive oxygen species in the cardiovascular system.	Reactive Oxygen Species	114-137	xanthine dehydrogenase	Homo sapiens	94-97
14694147-3	2004	XOR is a member of the molybdoenzyme family and is best known for its catalytic role in purine degradation, metabolizing hypoxanthine and xanthine to uric acid with concomitant generation of superoxide.	purine	88-94	xanthine dehydrogenase	Homo sapiens	0-3
15032331-1	2004	We have previously found that xanthine oxidase (one form of xanthine oxidoreductase that generates reactive oxygen species, such as superoxide radicals and hydrogen peroxide) is present in corneal epithelium of normal rabbit eye.	Reactive Oxygen Species	99-122	xanthine dehydrogenase	Homo sapiens	60-83
15032331-1	2004	We have previously found that xanthine oxidase (one form of xanthine oxidoreductase that generates reactive oxygen species, such as superoxide radicals and hydrogen peroxide) is present in corneal epithelium of normal rabbit eye.	Superoxides	132-142	xanthine dehydrogenase	Homo sapiens	60-83
15032331-1	2004	We have previously found that xanthine oxidase (one form of xanthine oxidoreductase that generates reactive oxygen species, such as superoxide radicals and hydrogen peroxide) is present in corneal epithelium of normal rabbit eye.	Hydrogen Peroxide	156-173	xanthine dehydrogenase	Homo sapiens	60-83
14664579-1	2003	Xanthine dehydrogenase (XDH) from the bacterium Rhodobacter capsulatus catalyzes the hydroxylation of xanthine to uric acid with NAD(+) as the electron acceptor.	Xanthine	102-110	xanthine dehydrogenase	Homo sapiens	24-27
14664579-1	2003	Xanthine dehydrogenase (XDH) from the bacterium Rhodobacter capsulatus catalyzes the hydroxylation of xanthine to uric acid with NAD(+) as the electron acceptor.	Uric Acid	114-123	xanthine dehydrogenase	Homo sapiens	24-27
14664579-1	2003	Xanthine dehydrogenase (XDH) from the bacterium Rhodobacter capsulatus catalyzes the hydroxylation of xanthine to uric acid with NAD(+) as the electron acceptor.	NAD	129-135	xanthine dehydrogenase	Homo sapiens	24-27
14694147-3	2004	XOR is a member of the molybdoenzyme family and is best known for its catalytic role in purine degradation, metabolizing hypoxanthine and xanthine to uric acid with concomitant generation of superoxide.	Hypoxanthine	121-133	xanthine dehydrogenase	Homo sapiens	0-3
14694147-3	2004	XOR is a member of the molybdoenzyme family and is best known for its catalytic role in purine degradation, metabolizing hypoxanthine and xanthine to uric acid with concomitant generation of superoxide.	Xanthine	125-133	xanthine dehydrogenase	Homo sapiens	0-3
14694147-3	2004	XOR is a member of the molybdoenzyme family and is best known for its catalytic role in purine degradation, metabolizing hypoxanthine and xanthine to uric acid with concomitant generation of superoxide.	Uric Acid	150-159	xanthine dehydrogenase	Homo sapiens	0-3
14694147-3	2004	XOR is a member of the molybdoenzyme family and is best known for its catalytic role in purine degradation, metabolizing hypoxanthine and xanthine to uric acid with concomitant generation of superoxide.	Superoxides	191-201	xanthine dehydrogenase	Homo sapiens	0-3
14694147-5	2004	XOR requires molybdopterin, iron-sulphur centres, and FAD as cofactors and has two interconvertible forms, xanthine oxidase and xanthine dehydrogenase, which transfer electrons from xanthine to oxygen and NAD(+), respectively, yielding superoxide, hydrogen peroxide and NADH.	Iron	28-32	xanthine dehydrogenase	Homo sapiens	0-3
14694147-5	2004	XOR requires molybdopterin, iron-sulphur centres, and FAD as cofactors and has two interconvertible forms, xanthine oxidase and xanthine dehydrogenase, which transfer electrons from xanthine to oxygen and NAD(+), respectively, yielding superoxide, hydrogen peroxide and NADH.	Iron	28-32	xanthine dehydrogenase	Homo sapiens	128-150
14694147-5	2004	XOR requires molybdopterin, iron-sulphur centres, and FAD as cofactors and has two interconvertible forms, xanthine oxidase and xanthine dehydrogenase, which transfer electrons from xanthine to oxygen and NAD(+), respectively, yielding superoxide, hydrogen peroxide and NADH.	Sulfur	33-40	xanthine dehydrogenase	Homo sapiens	0-3
14694147-5	2004	XOR requires molybdopterin, iron-sulphur centres, and FAD as cofactors and has two interconvertible forms, xanthine oxidase and xanthine dehydrogenase, which transfer electrons from xanthine to oxygen and NAD(+), respectively, yielding superoxide, hydrogen peroxide and NADH.	Sulfur	33-40	xanthine dehydrogenase	Homo sapiens	128-150
14694147-5	2004	XOR requires molybdopterin, iron-sulphur centres, and FAD as cofactors and has two interconvertible forms, xanthine oxidase and xanthine dehydrogenase, which transfer electrons from xanthine to oxygen and NAD(+), respectively, yielding superoxide, hydrogen peroxide and NADH.	Flavin-Adenine Dinucleotide	54-57	xanthine dehydrogenase	Homo sapiens	0-3
14694147-5	2004	XOR requires molybdopterin, iron-sulphur centres, and FAD as cofactors and has two interconvertible forms, xanthine oxidase and xanthine dehydrogenase, which transfer electrons from xanthine to oxygen and NAD(+), respectively, yielding superoxide, hydrogen peroxide and NADH.	Flavin-Adenine Dinucleotide	54-57	xanthine dehydrogenase	Homo sapiens	128-150
14694147-5	2004	XOR requires molybdopterin, iron-sulphur centres, and FAD as cofactors and has two interconvertible forms, xanthine oxidase and xanthine dehydrogenase, which transfer electrons from xanthine to oxygen and NAD(+), respectively, yielding superoxide, hydrogen peroxide and NADH.	Xanthine	107-115	xanthine dehydrogenase	Homo sapiens	0-3
14694147-5	2004	XOR requires molybdopterin, iron-sulphur centres, and FAD as cofactors and has two interconvertible forms, xanthine oxidase and xanthine dehydrogenase, which transfer electrons from xanthine to oxygen and NAD(+), respectively, yielding superoxide, hydrogen peroxide and NADH.	Xanthine	107-115	xanthine dehydrogenase	Homo sapiens	128-150
14694147-5	2004	XOR requires molybdopterin, iron-sulphur centres, and FAD as cofactors and has two interconvertible forms, xanthine oxidase and xanthine dehydrogenase, which transfer electrons from xanthine to oxygen and NAD(+), respectively, yielding superoxide, hydrogen peroxide and NADH.	Oxygen	194-200	xanthine dehydrogenase	Homo sapiens	0-3
14694147-5	2004	XOR requires molybdopterin, iron-sulphur centres, and FAD as cofactors and has two interconvertible forms, xanthine oxidase and xanthine dehydrogenase, which transfer electrons from xanthine to oxygen and NAD(+), respectively, yielding superoxide, hydrogen peroxide and NADH.	Oxygen	194-200	xanthine dehydrogenase	Homo sapiens	128-150
14694147-5	2004	XOR requires molybdopterin, iron-sulphur centres, and FAD as cofactors and has two interconvertible forms, xanthine oxidase and xanthine dehydrogenase, which transfer electrons from xanthine to oxygen and NAD(+), respectively, yielding superoxide, hydrogen peroxide and NADH.	NAD	205-211	xanthine dehydrogenase	Homo sapiens	0-3
14694147-5	2004	XOR requires molybdopterin, iron-sulphur centres, and FAD as cofactors and has two interconvertible forms, xanthine oxidase and xanthine dehydrogenase, which transfer electrons from xanthine to oxygen and NAD(+), respectively, yielding superoxide, hydrogen peroxide and NADH.	NAD	205-211	xanthine dehydrogenase	Homo sapiens	128-150
14694147-5	2004	XOR requires molybdopterin, iron-sulphur centres, and FAD as cofactors and has two interconvertible forms, xanthine oxidase and xanthine dehydrogenase, which transfer electrons from xanthine to oxygen and NAD(+), respectively, yielding superoxide, hydrogen peroxide and NADH.	Superoxides	236-246	xanthine dehydrogenase	Homo sapiens	0-3
14694147-5	2004	XOR requires molybdopterin, iron-sulphur centres, and FAD as cofactors and has two interconvertible forms, xanthine oxidase and xanthine dehydrogenase, which transfer electrons from xanthine to oxygen and NAD(+), respectively, yielding superoxide, hydrogen peroxide and NADH.	Superoxides	236-246	xanthine dehydrogenase	Homo sapiens	128-150
14694147-5	2004	XOR requires molybdopterin, iron-sulphur centres, and FAD as cofactors and has two interconvertible forms, xanthine oxidase and xanthine dehydrogenase, which transfer electrons from xanthine to oxygen and NAD(+), respectively, yielding superoxide, hydrogen peroxide and NADH.	Hydrogen Peroxide	248-265	xanthine dehydrogenase	Homo sapiens	0-3
14694147-5	2004	XOR requires molybdopterin, iron-sulphur centres, and FAD as cofactors and has two interconvertible forms, xanthine oxidase and xanthine dehydrogenase, which transfer electrons from xanthine to oxygen and NAD(+), respectively, yielding superoxide, hydrogen peroxide and NADH.	Hydrogen Peroxide	248-265	xanthine dehydrogenase	Homo sapiens	128-150
14694147-5	2004	XOR requires molybdopterin, iron-sulphur centres, and FAD as cofactors and has two interconvertible forms, xanthine oxidase and xanthine dehydrogenase, which transfer electrons from xanthine to oxygen and NAD(+), respectively, yielding superoxide, hydrogen peroxide and NADH.	NAD	270-274	xanthine dehydrogenase	Homo sapiens	0-3
14694147-5	2004	XOR requires molybdopterin, iron-sulphur centres, and FAD as cofactors and has two interconvertible forms, xanthine oxidase and xanthine dehydrogenase, which transfer electrons from xanthine to oxygen and NAD(+), respectively, yielding superoxide, hydrogen peroxide and NADH.	NAD	270-274	xanthine dehydrogenase	Homo sapiens	128-150
14694147-6	2004	Additionally, XOR can generate superoxide via NADH oxidase activity and can produce nitric oxide via nitrate and nitrite reductase activities.	Superoxides	31-41	xanthine dehydrogenase	Homo sapiens	14-17
14694147-6	2004	Additionally, XOR can generate superoxide via NADH oxidase activity and can produce nitric oxide via nitrate and nitrite reductase activities.	Nitric Oxide	84-96	xanthine dehydrogenase	Homo sapiens	14-17
14694147-8	2004	Importantly, the XOR inhibitors allopurinol and oxypurinol attenuate dysfunction caused by XOR in these disease states.	Allopurinol	32-43	xanthine dehydrogenase	Homo sapiens	17-20
14694147-8	2004	Importantly, the XOR inhibitors allopurinol and oxypurinol attenuate dysfunction caused by XOR in these disease states.	Allopurinol	32-43	xanthine dehydrogenase	Homo sapiens	91-94
14694147-8	2004	Importantly, the XOR inhibitors allopurinol and oxypurinol attenuate dysfunction caused by XOR in these disease states.	Oxypurinol	48-58	xanthine dehydrogenase	Homo sapiens	17-20
14694147-8	2004	Importantly, the XOR inhibitors allopurinol and oxypurinol attenuate dysfunction caused by XOR in these disease states.	Oxypurinol	48-58	xanthine dehydrogenase	Homo sapiens	91-94
14551354-10	2003	Within the entire coding region of the XDH gene, an A to T base change at nucleotide position 2164 was identified in the siblings, indicating a nonsense substitution from AAG (Lys) to TAG (Tyr) at codon 722.	Adenosine Diphosphate Glucose	171-174	xanthine dehydrogenase	Homo sapiens	39-42
14551354-10	2003	Within the entire coding region of the XDH gene, an A to T base change at nucleotide position 2164 was identified in the siblings, indicating a nonsense substitution from AAG (Lys) to TAG (Tyr) at codon 722.	Lysine	176-179	xanthine dehydrogenase	Homo sapiens	39-42
14551354-10	2003	Within the entire coding region of the XDH gene, an A to T base change at nucleotide position 2164 was identified in the siblings, indicating a nonsense substitution from AAG (Lys) to TAG (Tyr) at codon 722.	Tyrosine	189-192	xanthine dehydrogenase	Homo sapiens	39-42
16220932-1	2003	Spectroscopic changes from a solution of the amphophile 5,10,15,20-tetraphenylporphyrin in N,N-dimethylformamide using inputs of acid (HClaq) and base (KOBut) are interpreted as XOR and INHIBIT logic operations.	5,10,15,20-tetraphenylporphyrin	56-87	xanthine dehydrogenase	Homo sapiens	178-181
16220932-1	2003	Spectroscopic changes from a solution of the amphophile 5,10,15,20-tetraphenylporphyrin in N,N-dimethylformamide using inputs of acid (HClaq) and base (KOBut) are interpreted as XOR and INHIBIT logic operations.	Dimethylformamide	91-112	xanthine dehydrogenase	Homo sapiens	178-181
12637268-7	2003	Hydrogen peroxide partially inactivated the molybdenum center of XOR, as shown by a parallel decrease in XOR-catalyzed xanthine oxidation and dichlorophenolindophenol reduction.	Hydrogen Peroxide	0-17	xanthine dehydrogenase	Homo sapiens	105-108
12637268-0	2003	Posttranslational inactivation of human xanthine oxidoreductase by oxygen under standard cell culture conditions.	Oxygen	67-73	xanthine dehydrogenase	Homo sapiens	40-63
12637268-1	2003	Xanthine oxidoreductase (XOR) catalyzes the final reactions of purine catabolism and may account for cell damage by producing reactive oxygen metabolites in cells reoxygenated after hypoxia.	purine	63-69	xanthine dehydrogenase	Homo sapiens	0-23
12637268-7	2003	Hydrogen peroxide partially inactivated the molybdenum center of XOR, as shown by a parallel decrease in XOR-catalyzed xanthine oxidation and dichlorophenolindophenol reduction.	Xanthine	119-127	xanthine dehydrogenase	Homo sapiens	65-68
12637268-1	2003	Xanthine oxidoreductase (XOR) catalyzes the final reactions of purine catabolism and may account for cell damage by producing reactive oxygen metabolites in cells reoxygenated after hypoxia.	purine	63-69	xanthine dehydrogenase	Homo sapiens	25-28
12637268-1	2003	Xanthine oxidoreductase (XOR) catalyzes the final reactions of purine catabolism and may account for cell damage by producing reactive oxygen metabolites in cells reoxygenated after hypoxia.	Oxygen	135-141	xanthine dehydrogenase	Homo sapiens	0-23
12637268-7	2003	Hydrogen peroxide partially inactivated the molybdenum center of XOR, as shown by a parallel decrease in XOR-catalyzed xanthine oxidation and dichlorophenolindophenol reduction.	Xanthine	119-127	xanthine dehydrogenase	Homo sapiens	105-108
12637268-1	2003	Xanthine oxidoreductase (XOR) catalyzes the final reactions of purine catabolism and may account for cell damage by producing reactive oxygen metabolites in cells reoxygenated after hypoxia.	Oxygen	135-141	xanthine dehydrogenase	Homo sapiens	25-28
12637268-2	2003	We found a three- to eightfold higher XOR activity in cultured human bronchial epithelial cells exposed to hypoxia (0.5-3% O2) compared with cells grown in normoxia (21% O2) but no difference in XOR protein or mRNA.	Oxygen	123-125	xanthine dehydrogenase	Homo sapiens	38-41
12637268-7	2003	Hydrogen peroxide partially inactivated the molybdenum center of XOR, as shown by a parallel decrease in XOR-catalyzed xanthine oxidation and dichlorophenolindophenol reduction.	2,6-Dichloroindophenol	142-166	xanthine dehydrogenase	Homo sapiens	65-68
12637268-2	2003	We found a three- to eightfold higher XOR activity in cultured human bronchial epithelial cells exposed to hypoxia (0.5-3% O2) compared with cells grown in normoxia (21% O2) but no difference in XOR protein or mRNA.	Oxygen	170-172	xanthine dehydrogenase	Homo sapiens	38-41
12637268-4	2003	The cellular XOR activity at 3% O2 returned to basal levels when the cells were returned to 21% O2, and hyperoxia (95% O2) abolished enzyme activity with no change in XOR protein.	Oxygen	32-34	xanthine dehydrogenase	Homo sapiens	13-16
12637268-4	2003	The cellular XOR activity at 3% O2 returned to basal levels when the cells were returned to 21% O2, and hyperoxia (95% O2) abolished enzyme activity with no change in XOR protein.	Oxygen	96-98	xanthine dehydrogenase	Homo sapiens	13-16
12637268-4	2003	The cellular XOR activity at 3% O2 returned to basal levels when the cells were returned to 21% O2, and hyperoxia (95% O2) abolished enzyme activity with no change in XOR protein.	Oxygen	96-98	xanthine dehydrogenase	Homo sapiens	13-16
12637268-9	2003	Instead, the molybdenum center of XOR is posttranslationally inactivated by oxygen metabolites in "normal" (21% O2) cell culture atmosphere.	Oxygen	76-82	xanthine dehydrogenase	Homo sapiens	34-37
12637268-7	2003	Hydrogen peroxide partially inactivated the molybdenum center of XOR, as shown by a parallel decrease in XOR-catalyzed xanthine oxidation and dichlorophenolindophenol reduction.	Hydrogen Peroxide	0-17	xanthine dehydrogenase	Homo sapiens	65-68
12637268-9	2003	Instead, the molybdenum center of XOR is posttranslationally inactivated by oxygen metabolites in "normal" (21% O2) cell culture atmosphere.	Oxygen	112-114	xanthine dehydrogenase	Homo sapiens	34-37
12742114-1	2003	Caffeine is metabolised in humans primarily by cytochromes P450 1A2 and 2A6, xanthine dehydrogenase/oxidase, and N-acetyltransferase 2.	Caffeine	0-8	xanthine dehydrogenase	Homo sapiens	77-134
12535843-1	2003	The XOR activity in human plasma was measured by quantifying the XOR-derived uric acid (UA) in plasma using the high-performance liquid chromatography (HPLC) equipped with a UV detector.	Uric Acid	77-86	xanthine dehydrogenase	Homo sapiens	4-7
12578558-9	2003	Xanthine oxidoreductase is the key enzyme in the catabolism of purines, although recent data suggest that the physiological function of this enzyme is more complex than previously assumed.	Purines	63-70	xanthine dehydrogenase	Homo sapiens	0-23
12689826-3	2003	The hypoxanthine is oxidized to uric acid by xanthine oxidase/xanthine dehydrogenase and can be measured by formation of formazan when a tetrazolium salt is used as the oxidant.	Hypoxanthine	4-16	xanthine dehydrogenase	Homo sapiens	62-84
12689826-3	2003	The hypoxanthine is oxidized to uric acid by xanthine oxidase/xanthine dehydrogenase and can be measured by formation of formazan when a tetrazolium salt is used as the oxidant.	Uric Acid	32-41	xanthine dehydrogenase	Homo sapiens	62-84
12689826-3	2003	The hypoxanthine is oxidized to uric acid by xanthine oxidase/xanthine dehydrogenase and can be measured by formation of formazan when a tetrazolium salt is used as the oxidant.	Formazans	121-129	xanthine dehydrogenase	Homo sapiens	62-84
12535843-1	2003	The XOR activity in human plasma was measured by quantifying the XOR-derived uric acid (UA) in plasma using the high-performance liquid chromatography (HPLC) equipped with a UV detector.	Uric Acid	77-86	xanthine dehydrogenase	Homo sapiens	65-68
12535843-1	2003	The XOR activity in human plasma was measured by quantifying the XOR-derived uric acid (UA) in plasma using the high-performance liquid chromatography (HPLC) equipped with a UV detector.	Uric Acid	88-90	xanthine dehydrogenase	Homo sapiens	4-7
12535843-1	2003	The XOR activity in human plasma was measured by quantifying the XOR-derived uric acid (UA) in plasma using the high-performance liquid chromatography (HPLC) equipped with a UV detector.	Uric Acid	88-90	xanthine dehydrogenase	Homo sapiens	65-68
12535843-3	2003	Deproteinization with heat-treatment of plasma samples after the reaction was used in the assay to avoid splitting of the UA and xanthine peaks caused by acid deproteinization that could interfere the accurate determination of human plasma XOR activity in our case.	Xanthine	129-137	xanthine dehydrogenase	Homo sapiens	240-243
12535843-4	2003	Based on the examination of the dependence of XOR activity on added amounts of xanthine and reaction times, the amount of xanthine and reaction time for XOR activity assay were determined to prevent the errors caused by the limiting effect of substrates and plateau phase of the reaction.	Xanthine	79-87	xanthine dehydrogenase	Homo sapiens	46-49
12535843-4	2003	Based on the examination of the dependence of XOR activity on added amounts of xanthine and reaction times, the amount of xanthine and reaction time for XOR activity assay were determined to prevent the errors caused by the limiting effect of substrates and plateau phase of the reaction.	Xanthine	122-130	xanthine dehydrogenase	Homo sapiens	153-156
12549937-10	2003	Thus, XOR catalyzed nitrate reduction to nitrite and NO occurs and can be an important source of NO production in ischemic tissues.	Nitrates	20-27	xanthine dehydrogenase	Homo sapiens	6-9
12549937-10	2003	Thus, XOR catalyzed nitrate reduction to nitrite and NO occurs and can be an important source of NO production in ischemic tissues.	Nitrites	41-48	xanthine dehydrogenase	Homo sapiens	6-9
12208366-3	2002	The publication, just over 20 years ago, of a hypothesis implicating XOR in ischemia-reperfusion injury focused research attention on the enzyme and its ability to generate reactive oxygen species (ROS).	Reactive Oxygen Species	173-196	xanthine dehydrogenase	Homo sapiens	69-72
12502743-1	2002	Xanthine oxidoreductase (XOR) is the rate-limiting enzyme in purine catabolism occurring in most cell types.	purine	61-67	xanthine dehydrogenase	Homo sapiens	0-23
12502743-1	2002	Xanthine oxidoreductase (XOR) is the rate-limiting enzyme in purine catabolism occurring in most cell types.	purine	61-67	xanthine dehydrogenase	Homo sapiens	25-28
12388055-0	2002	Regulation of xanthine oxidoreductase by intracellular iron.	Iron	55-59	xanthine dehydrogenase	Homo sapiens	14-37
12388055-1	2002	Xanthine oxidoreductase (XOR) may produce reactive oxygen species and play a role in ischemia-reperfusion injury.	Reactive Oxygen Species	42-65	xanthine dehydrogenase	Homo sapiens	0-23
12388055-1	2002	Xanthine oxidoreductase (XOR) may produce reactive oxygen species and play a role in ischemia-reperfusion injury.	Reactive Oxygen Species	42-65	xanthine dehydrogenase	Homo sapiens	25-28
12388055-2	2002	Because tissue iron levels increase after ischemia, and because XOR contains functionally critical iron-sulfur clusters, we studied the effects of intracellular iron on XOR expression.	Iron	99-103	xanthine dehydrogenase	Homo sapiens	64-67
12388055-2	2002	Because tissue iron levels increase after ischemia, and because XOR contains functionally critical iron-sulfur clusters, we studied the effects of intracellular iron on XOR expression.	Sulfur	104-110	xanthine dehydrogenase	Homo sapiens	64-67
12388055-2	2002	Because tissue iron levels increase after ischemia, and because XOR contains functionally critical iron-sulfur clusters, we studied the effects of intracellular iron on XOR expression.	Iron	99-103	xanthine dehydrogenase	Homo sapiens	64-67
12388055-4	2002	Iron increased XOR protein and mRNA levels, whereas protein and RNA synthesis inhibitors abolished the induction of XOR activity.	Iron	0-4	xanthine dehydrogenase	Homo sapiens	15-18
12388055-7	2002	Iron chelation by deferoxamine (DFO) decreased XOR activity but did not lower endogenous XOR protein or mRNA levels.	Iron	0-4	xanthine dehydrogenase	Homo sapiens	47-50
12421831-2	2003	TEI-6720 (2-(3-cyano-4-isobutoxyphenyl)-4-methyl-5-thiazolecarboxylic acid) is an extremely potent inhibitor of xanthine oxidoreductase.	Febuxostat	0-8	xanthine dehydrogenase	Homo sapiens	112-135
12421831-2	2003	TEI-6720 (2-(3-cyano-4-isobutoxyphenyl)-4-methyl-5-thiazolecarboxylic acid) is an extremely potent inhibitor of xanthine oxidoreductase.	Febuxostat	10-74	xanthine dehydrogenase	Homo sapiens	112-135
12388055-7	2002	Iron chelation by deferoxamine (DFO) decreased XOR activity but did not lower endogenous XOR protein or mRNA levels.	Deferoxamine	18-30	xanthine dehydrogenase	Homo sapiens	47-50
12388055-7	2002	Iron chelation by deferoxamine (DFO) decreased XOR activity but did not lower endogenous XOR protein or mRNA levels.	Deferoxamine	32-35	xanthine dehydrogenase	Homo sapiens	47-50
12388055-8	2002	Furthermore, DFO reduced the activity of overexpressed human XOR but not the amount of immunoreactive protein.	Deferoxamine	13-16	xanthine dehydrogenase	Homo sapiens	61-64
12388055-9	2002	Our data show that XOR activity is transcriptionally induced by iron but posttranslationally inactivated by iron chelation.	Iron	64-68	xanthine dehydrogenase	Homo sapiens	19-22
12388055-9	2002	Our data show that XOR activity is transcriptionally induced by iron but posttranslationally inactivated by iron chelation.	Iron	108-112	xanthine dehydrogenase	Homo sapiens	19-22
12208366-3	2002	The publication, just over 20 years ago, of a hypothesis implicating XOR in ischemia-reperfusion injury focused research attention on the enzyme and its ability to generate reactive oxygen species (ROS).	Reactive Oxygen Species	198-201	xanthine dehydrogenase	Homo sapiens	69-72
12208366-6	2002	Of special interest has been the finding that XOR can catalyze the reduction of nitrates and nitrites to nitric oxide (NO), acting as a source of both NO and peroxynitrite.	Nitrates	80-88	xanthine dehydrogenase	Homo sapiens	46-49
12208366-6	2002	Of special interest has been the finding that XOR can catalyze the reduction of nitrates and nitrites to nitric oxide (NO), acting as a source of both NO and peroxynitrite.	Nitrites	93-101	xanthine dehydrogenase	Homo sapiens	46-49
12208366-6	2002	Of special interest has been the finding that XOR can catalyze the reduction of nitrates and nitrites to nitric oxide (NO), acting as a source of both NO and peroxynitrite.	Nitric Oxide	105-117	xanthine dehydrogenase	Homo sapiens	46-49
12208366-6	2002	Of special interest has been the finding that XOR can catalyze the reduction of nitrates and nitrites to nitric oxide (NO), acting as a source of both NO and peroxynitrite.	Peroxynitrous Acid	158-171	xanthine dehydrogenase	Homo sapiens	46-49
11801171-4	2002	We show that the dipole-dipole interaction leads only to very small errors in the XOR gate.	dipole-dipole	17-30	xanthine dehydrogenase	Homo sapiens	82-85
12190180-6	2002	The percentage of XOR oxidase activity in cirrhotic liver, regardless of virus infection, correlated positively with aspartate amino-transferase, bilirubin concentration, and partial thromboplastin time, and negatively with prothrombin time.	Bilirubin	146-155	xanthine dehydrogenase	Homo sapiens	18-21
12147719-2	2002	(1) Nitrate reductase catalyses the key step in inorganic nitrogen assimilation, (2) aldehyde oxidase(s) have been shown to catalyse the last step in the biosynthesis of the phytohormone abscisic acid, (3) xanthine dehydrogenase is involved in purine catabolism and stress reactions, and (4) sulphite oxidase is probably involved in detoxifying excess sulphite.	Nitrogen	58-66	xanthine dehydrogenase	Homo sapiens	206-228
12147719-2	2002	(1) Nitrate reductase catalyses the key step in inorganic nitrogen assimilation, (2) aldehyde oxidase(s) have been shown to catalyse the last step in the biosynthesis of the phytohormone abscisic acid, (3) xanthine dehydrogenase is involved in purine catabolism and stress reactions, and (4) sulphite oxidase is probably involved in detoxifying excess sulphite.	Abscisic Acid	187-200	xanthine dehydrogenase	Homo sapiens	206-228
12147719-2	2002	(1) Nitrate reductase catalyses the key step in inorganic nitrogen assimilation, (2) aldehyde oxidase(s) have been shown to catalyse the last step in the biosynthesis of the phytohormone abscisic acid, (3) xanthine dehydrogenase is involved in purine catabolism and stress reactions, and (4) sulphite oxidase is probably involved in detoxifying excess sulphite.	purine	244-250	xanthine dehydrogenase	Homo sapiens	206-228
12147719-2	2002	(1) Nitrate reductase catalyses the key step in inorganic nitrogen assimilation, (2) aldehyde oxidase(s) have been shown to catalyse the last step in the biosynthesis of the phytohormone abscisic acid, (3) xanthine dehydrogenase is involved in purine catabolism and stress reactions, and (4) sulphite oxidase is probably involved in detoxifying excess sulphite.	Sulfites	292-300	xanthine dehydrogenase	Homo sapiens	206-228
11961098-7	2002	It is also argued that the high concentration of uric acid in the blood of humans and nonhuman primates has developed molecular coevolution with the xanthine oxidoreductase in purine metabolism.	Uric Acid	49-58	xanthine dehydrogenase	Homo sapiens	149-172
11961098-7	2002	It is also argued that the high concentration of uric acid in the blood of humans and nonhuman primates has developed molecular coevolution with the xanthine oxidoreductase in purine metabolism.	purine	176-182	xanthine dehydrogenase	Homo sapiens	149-172
11905046-9	2002	We have shown that peroxynitrite (a reactive nitrogen species) has the potential to convert xanthine dehydrogenase to oxidase.	Peroxynitrous Acid	19-32	xanthine dehydrogenase	Homo sapiens	92-114
11905046-9	2002	We have shown that peroxynitrite (a reactive nitrogen species) has the potential to convert xanthine dehydrogenase to oxidase.	Reactive Nitrogen Species	36-61	xanthine dehydrogenase	Homo sapiens	92-114
11914370-1	2002	Xanthine oxidoreductase (XOR) is a 300-kDa homodimer that can exist as an NAD+-dependent dehydrogenase (XD) or as an O2-dependent oxidase (XO) depending on the oxidation state of its cysteine thiols.	cysteine thiols	183-198	xanthine dehydrogenase	Homo sapiens	0-23
11914370-1	2002	Xanthine oxidoreductase (XOR) is a 300-kDa homodimer that can exist as an NAD+-dependent dehydrogenase (XD) or as an O2-dependent oxidase (XO) depending on the oxidation state of its cysteine thiols.	cysteine thiols	183-198	xanthine dehydrogenase	Homo sapiens	25-28
11914370-5	2002	Size exclusion chromatography showed that disulfide bond formation reduced the hydrodynamic volume of the enzyme, and two-dimensional gel electrophoresis of chymotrypsin-digested XO showed significant, disulfide bond-mediated, conformational heterogeneity in the N-terminal third of the enzyme but no evidence of disulfide bonds between the N-terminal and C-terminal regions or between XOR subunits.	Disulfides	42-51	xanthine dehydrogenase	Homo sapiens	386-389
11914370-5	2002	Size exclusion chromatography showed that disulfide bond formation reduced the hydrodynamic volume of the enzyme, and two-dimensional gel electrophoresis of chymotrypsin-digested XO showed significant, disulfide bond-mediated, conformational heterogeneity in the N-terminal third of the enzyme but no evidence of disulfide bonds between the N-terminal and C-terminal regions or between XOR subunits.	Disulfides	202-211	xanthine dehydrogenase	Homo sapiens	386-389
11914370-5	2002	Size exclusion chromatography showed that disulfide bond formation reduced the hydrodynamic volume of the enzyme, and two-dimensional gel electrophoresis of chymotrypsin-digested XO showed significant, disulfide bond-mediated, conformational heterogeneity in the N-terminal third of the enzyme but no evidence of disulfide bonds between the N-terminal and C-terminal regions or between XOR subunits.	Disulfides	202-211	xanthine dehydrogenase	Homo sapiens	386-389
11914370-6	2002	These results indicate that intrasubunit disulfide bond formation leads to a global conformational change in XOR that results in the exposure of the region surrounding Phe560.	Disulfides	41-50	xanthine dehydrogenase	Homo sapiens	109-112
11811520-1	2001	The in vitro toxicity of the reactive oxygen species generating enzyme xanthine oxidoreductase (XOR) to human peripheral blood lymphocytes was studied after stimulation with phytohaemoagglutinin or anti-CD3/CD28 antibodies.	Reactive Oxygen Species	29-52	xanthine dehydrogenase	Homo sapiens	71-94
12168784-1	2002	Xanthine oxidoreductase (xanthine dehydrogenase + xanthine oxidase) is a complex enzyme that catalyzes the oxidation of hypoxanthine to xanthine, subsequently producing uric acid.	Hypoxanthine	120-132	xanthine dehydrogenase	Homo sapiens	0-23
12168784-1	2002	Xanthine oxidoreductase (xanthine dehydrogenase + xanthine oxidase) is a complex enzyme that catalyzes the oxidation of hypoxanthine to xanthine, subsequently producing uric acid.	Hypoxanthine	120-132	xanthine dehydrogenase	Homo sapiens	25-47
12168784-1	2002	Xanthine oxidoreductase (xanthine dehydrogenase + xanthine oxidase) is a complex enzyme that catalyzes the oxidation of hypoxanthine to xanthine, subsequently producing uric acid.	Xanthine	25-33	xanthine dehydrogenase	Homo sapiens	0-23
12168784-1	2002	Xanthine oxidoreductase (xanthine dehydrogenase + xanthine oxidase) is a complex enzyme that catalyzes the oxidation of hypoxanthine to xanthine, subsequently producing uric acid.	Uric Acid	169-178	xanthine dehydrogenase	Homo sapiens	0-23
12168784-1	2002	Xanthine oxidoreductase (xanthine dehydrogenase + xanthine oxidase) is a complex enzyme that catalyzes the oxidation of hypoxanthine to xanthine, subsequently producing uric acid.	Uric Acid	169-178	xanthine dehydrogenase	Homo sapiens	25-47
12168784-2	2002	The enzyme complex exists in separate but interconvertible forms, xanthine dehydrogenase and xanthine oxidase, which generate reactive oxygen species (ROS), a well known causative factor in ischemia/reperfusion injury and also in some other pathological states and diseases.	Reactive Oxygen Species	126-149	xanthine dehydrogenase	Homo sapiens	66-88
12168784-2	2002	The enzyme complex exists in separate but interconvertible forms, xanthine dehydrogenase and xanthine oxidase, which generate reactive oxygen species (ROS), a well known causative factor in ischemia/reperfusion injury and also in some other pathological states and diseases.	Reactive Oxygen Species	151-154	xanthine dehydrogenase	Homo sapiens	66-88
12168784-4	2002	Xanthine oxidoreductase activity was demonstrated by the tetrazolium salt reduction method and xanthine oxidase activity was detected by methods based on cerium ion capture of hydrogen peroxide.	Tetrazolium Salts	57-73	xanthine dehydrogenase	Homo sapiens	0-23
12168784-10	2002	Based on the findings obtained in this study (xanthine oxidoreductase/xanthine oxidase activities are present in normal human corneas), we hypothesize that during various pathological states, xanthine oxidase-generated ROS might be involved in oxidative eye injury.	Reactive Oxygen Species	219-222	xanthine dehydrogenase	Homo sapiens	46-69
12632927-1	2002	Ethanol ingestion causes an increase in free radical generation in the liver mainly by induction of microsomal cytochrome P-450, conversion of xanthine dehydrogenase into xanthine oxidase in cytosol and increased one electron oxygen reduction in mitochondria.	Ethanol	0-7	xanthine dehydrogenase	Homo sapiens	143-165
11811520-1	2001	The in vitro toxicity of the reactive oxygen species generating enzyme xanthine oxidoreductase (XOR) to human peripheral blood lymphocytes was studied after stimulation with phytohaemoagglutinin or anti-CD3/CD28 antibodies.	Reactive Oxygen Species	29-52	xanthine dehydrogenase	Homo sapiens	96-99
11811520-3	2001	CD8+ lymphocytes showed a higher sensitivity than CD4+ cells to the XOR/hypoxanthine system.	Hypoxanthine	72-84	xanthine dehydrogenase	Homo sapiens	68-71
11811520-6	2001	Apoptosis was induced by XOR activity proportionally to substrate concentration and was prevented by the competitive enzyme inhibitor, allopurinol.	Allopurinol	135-146	xanthine dehydrogenase	Homo sapiens	25-28
11811520-7	2001	The hydrogen peroxide scavenging enzyme, catalase, gave a higher protection than superoxide dismutase from the toxicity caused by the XOR/hypoxanthine system.	Hydrogen Peroxide	4-21	xanthine dehydrogenase	Homo sapiens	134-137
11811520-7	2001	The hydrogen peroxide scavenging enzyme, catalase, gave a higher protection than superoxide dismutase from the toxicity caused by the XOR/hypoxanthine system.	Hypoxanthine	138-150	xanthine dehydrogenase	Homo sapiens	134-137
11811520-8	2001	Necrosis occurs in a variable percentage indicating that reactive oxygen species may trigger both apoptosis and necrosis in proliferating human lymphocytes, mostly depending on XOR concentration.	Reactive Oxygen Species	57-80	xanthine dehydrogenase	Homo sapiens	177-180
11601679-9	2001	It is known that diabetic patients produce more TBARS as a result of enhanced free radical generation the source of which may also be the large amounts of XO produced following the conversion of xanthine dehydrogenase in hypoxic diabetic tissues.	Thiobarbituric Acid Reactive Substances	48-53	xanthine dehydrogenase	Homo sapiens	195-217
11513730-0	2001	Suicide inactivation of xanthine oxidoreductase during reduction of inorganic nitrite to nitric oxide.	inorganic nitrite	68-85	xanthine dehydrogenase	Homo sapiens	24-47
11513730-0	2001	Suicide inactivation of xanthine oxidoreductase during reduction of inorganic nitrite to nitric oxide.	Nitric Oxide	89-101	xanthine dehydrogenase	Homo sapiens	24-47
11513730-1	2001	Xanthine oxidoreductase (XOR) is progressively inactivated while catalysing the reduction of inorganic nitrite to NO by xanthine.	inorganic nitrite	93-110	xanthine dehydrogenase	Homo sapiens	0-23
11513730-1	2001	Xanthine oxidoreductase (XOR) is progressively inactivated while catalysing the reduction of inorganic nitrite to NO by xanthine.	inorganic nitrite	93-110	xanthine dehydrogenase	Homo sapiens	25-28
11513730-1	2001	Xanthine oxidoreductase (XOR) is progressively inactivated while catalysing the reduction of inorganic nitrite to NO by xanthine.	Xanthine	120-128	xanthine dehydrogenase	Homo sapiens	0-23
11513730-1	2001	Xanthine oxidoreductase (XOR) is progressively inactivated while catalysing the reduction of inorganic nitrite to NO by xanthine.	Xanthine	120-128	xanthine dehydrogenase	Homo sapiens	25-28
11513730-7	2001	Inorganic nitrate, like nitrite, was shown to be reduced at the molybdenum site of XOR.	punky blue	0-17	xanthine dehydrogenase	Homo sapiens	83-86
11513730-7	2001	Inorganic nitrate, like nitrite, was shown to be reduced at the molybdenum site of XOR.	Nitrites	24-31	xanthine dehydrogenase	Homo sapiens	83-86
11302742-7	2001	These results indicate that a functional defect of the HMCS gene is responsible for classical xanthinuria type II, and that HMCS protein functions to provide a sulfur atom for the molybdenum cofactor of XDH and AO.	Sulfur	160-166	xanthine dehydrogenase	Homo sapiens	203-206
11579333-12	2001	CONCLUSIONS: These results suggest that CLS could act by interfering with the conversion of xanthine dehydrogenase into superoxide-producing xanthine oxidase.	calusterone	40-43	xanthine dehydrogenase	Homo sapiens	92-114
11579333-12	2001	CONCLUSIONS: These results suggest that CLS could act by interfering with the conversion of xanthine dehydrogenase into superoxide-producing xanthine oxidase.	Superoxides	120-130	xanthine dehydrogenase	Homo sapiens	92-114
11404767-0	2001	[Crystal structures of heme binding protein 23 and xanthine dehydrogenase].	Heme	23-27	xanthine dehydrogenase	Homo sapiens	51-73
12549228-1	2001	Xanthine Oxidoreductase (XOR) is the key enzyme in purine metabolism and also produces oxygen free radicals.	purine	51-57	xanthine dehydrogenase	Homo sapiens	0-23
12549228-1	2001	Xanthine Oxidoreductase (XOR) is the key enzyme in purine metabolism and also produces oxygen free radicals.	purine	51-57	xanthine dehydrogenase	Homo sapiens	25-28
12549228-1	2001	Xanthine Oxidoreductase (XOR) is the key enzyme in purine metabolism and also produces oxygen free radicals.	oxygen free radicals	87-107	xanthine dehydrogenase	Homo sapiens	0-23
12549228-1	2001	Xanthine Oxidoreductase (XOR) is the key enzyme in purine metabolism and also produces oxygen free radicals.	oxygen free radicals	87-107	xanthine dehydrogenase	Homo sapiens	25-28
11334804-6	2001	Treatment with the xanthine oxidoreductase inhibitor allopurinol inhibited CSF urate levels earlier than those in blood plasma, supporting the notion that urate was produced within the brain.	Allopurinol	53-64	xanthine dehydrogenase	Homo sapiens	19-42
11334804-6	2001	Treatment with the xanthine oxidoreductase inhibitor allopurinol inhibited CSF urate levels earlier than those in blood plasma, supporting the notion that urate was produced within the brain.	Uric Acid	79-84	xanthine dehydrogenase	Homo sapiens	19-42
11334804-6	2001	Treatment with the xanthine oxidoreductase inhibitor allopurinol inhibited CSF urate levels earlier than those in blood plasma, supporting the notion that urate was produced within the brain.	Uric Acid	155-160	xanthine dehydrogenase	Homo sapiens	19-42
11334804-8	2001	Together with data from the literature, the results strongly suggest that xanthine oxidase is not a major cause of oxidative stress in bacterial meningitis and that urate formation due to induction of xanthine oxidoreductase in the brain may in fact represent a protective response.	Uric Acid	165-170	xanthine dehydrogenase	Homo sapiens	201-224
11278616-3	2001	Posttranslational modification of the protein, for example through thiol oxidation or proteolysis, has been shown to be important in converting XDH to XO.	Sulfhydryl Compounds	67-72	xanthine dehydrogenase	Homo sapiens	144-147
11230310-6	2001	In dTGR, serum 8-isoprostaglandin F(2alpha), a vasoconstrictor and antinatriuretic arachidonic acid metabolite produced by oxidative stress, was increased by 100%, and the activity of XOR in the kidney was increased by 40%.	8-isoprostaglandin f	15-35	xanthine dehydrogenase	Homo sapiens	184-187
11165212-1	2001	To investigate the properties of xanthine dehydrogenase/xanthine oxidase (XDH/XO) deficiency in a patient with atypical type I xanthinuria, as indicated by oxypurine data, a cDNA sequence encoding XDH, XDH/XO immunoblot analysis and a competitive PCR assay were performed, and the results were compared with those of normal subjects.	2-Hydroxypurine	156-165	xanthine dehydrogenase	Homo sapiens	33-55
11165212-1	2001	To investigate the properties of xanthine dehydrogenase/xanthine oxidase (XDH/XO) deficiency in a patient with atypical type I xanthinuria, as indicated by oxypurine data, a cDNA sequence encoding XDH, XDH/XO immunoblot analysis and a competitive PCR assay were performed, and the results were compared with those of normal subjects.	2-Hydroxypurine	156-165	xanthine dehydrogenase	Homo sapiens	74-77
11230310-4	2001	Preincubation with the XOR inhibitor oxypurinol also improved endothelium-dependent vascular relaxation.	Oxypurinol	37-47	xanthine dehydrogenase	Homo sapiens	23-26
11230310-10	2001	Valsartan also normalized serum 8-isoprostaglandin F(2alpha) levels, renal XOR activity, and, to a degree, NO(x) excretion.	Valsartan	0-9	xanthine dehydrogenase	Homo sapiens	75-78
10801779-1	2000	Defective xanthine dehydrogenase (XDH) activity in humans results in xanthinuria and xanthine calculus accumulation in kidneys.	Xanthine	10-18	xanthine dehydrogenase	Homo sapiens	34-37
11163031-7	2001	We conclude that elimination of the reaction products (NADH, H(2)O(2) and O(2)) from the reaction mixture, and short incubation times, are necessary for accurate measurement of the XOR activities.	NAD	55-59	xanthine dehydrogenase	Homo sapiens	181-184
11163031-7	2001	We conclude that elimination of the reaction products (NADH, H(2)O(2) and O(2)) from the reaction mixture, and short incubation times, are necessary for accurate measurement of the XOR activities.	Hydrogen Peroxide	61-69	xanthine dehydrogenase	Homo sapiens	181-184
11163031-7	2001	We conclude that elimination of the reaction products (NADH, H(2)O(2) and O(2)) from the reaction mixture, and short incubation times, are necessary for accurate measurement of the XOR activities.	o(2)	65-69	xanthine dehydrogenase	Homo sapiens	181-184
11163031-3	2001	We studied the effect of the assay conditions on the xanthine oxidation rate catalysed by the XOR forms.	Xanthine	53-61	xanthine dehydrogenase	Homo sapiens	94-97
11154741-4	2000	Physiologically, XOR is known as the rate-limiting enzyme in purine catabolism but has also been shown to be able to metabolize a number of other physiological compounds.	purine	61-67	xanthine dehydrogenase	Homo sapiens	17-20
11132637-2	2000	The mammalian enzymes exist originally as the dehydrogenase form (XDH) but can be converted to the oxidase form (XO) either reversibly by oxidation of sulfhydryl residues of the protein molecule or irreversibly by proteolysis.	Sulfhydryl Compounds	151-161	xanthine dehydrogenase	Homo sapiens	66-69
10858495-2	2000	We show that peroxynitrite can be produced by the action of a single enzyme, xanthine oxidoreductase (XOR), in the presence of inorganic nitrite, molecular oxygen and a reducing agent, such as pterin.	Oxygen	156-162	xanthine dehydrogenase	Homo sapiens	77-100
10858495-0	2000	A new route to peroxynitrite: a role for xanthine oxidoreductase.	Peroxynitrous Acid	15-28	xanthine dehydrogenase	Homo sapiens	41-64
10999428-0	2000	Study of the effect of the administration of Cd(II), cysteine, methionine, and Cd(II) together with cysteine or methionine on the conversion of xanthine dehydrogenase into xanthine oxidase.	cd(ii)	45-51	xanthine dehydrogenase	Homo sapiens	144-166
10999428-0	2000	Study of the effect of the administration of Cd(II), cysteine, methionine, and Cd(II) together with cysteine or methionine on the conversion of xanthine dehydrogenase into xanthine oxidase.	Cysteine	53-61	xanthine dehydrogenase	Homo sapiens	144-166
10999428-0	2000	Study of the effect of the administration of Cd(II), cysteine, methionine, and Cd(II) together with cysteine or methionine on the conversion of xanthine dehydrogenase into xanthine oxidase.	Methionine	63-73	xanthine dehydrogenase	Homo sapiens	144-166
10999428-0	2000	Study of the effect of the administration of Cd(II), cysteine, methionine, and Cd(II) together with cysteine or methionine on the conversion of xanthine dehydrogenase into xanthine oxidase.	cd(ii)	79-85	xanthine dehydrogenase	Homo sapiens	144-166
10999428-0	2000	Study of the effect of the administration of Cd(II), cysteine, methionine, and Cd(II) together with cysteine or methionine on the conversion of xanthine dehydrogenase into xanthine oxidase.	Cysteine	100-108	xanthine dehydrogenase	Homo sapiens	144-166
10999428-0	2000	Study of the effect of the administration of Cd(II), cysteine, methionine, and Cd(II) together with cysteine or methionine on the conversion of xanthine dehydrogenase into xanthine oxidase.	Methionine	112-122	xanthine dehydrogenase	Homo sapiens	144-166
10858495-2	2000	We show that peroxynitrite can be produced by the action of a single enzyme, xanthine oxidoreductase (XOR), in the presence of inorganic nitrite, molecular oxygen and a reducing agent, such as pterin.	Peroxynitrous Acid	13-26	xanthine dehydrogenase	Homo sapiens	77-100
10858495-2	2000	We show that peroxynitrite can be produced by the action of a single enzyme, xanthine oxidoreductase (XOR), in the presence of inorganic nitrite, molecular oxygen and a reducing agent, such as pterin.	Peroxynitrous Acid	13-26	xanthine dehydrogenase	Homo sapiens	102-105
10858495-2	2000	We show that peroxynitrite can be produced by the action of a single enzyme, xanthine oxidoreductase (XOR), in the presence of inorganic nitrite, molecular oxygen and a reducing agent, such as pterin.	inorganic nitrite	127-144	xanthine dehydrogenase	Homo sapiens	77-100
10858495-2	2000	We show that peroxynitrite can be produced by the action of a single enzyme, xanthine oxidoreductase (XOR), in the presence of inorganic nitrite, molecular oxygen and a reducing agent, such as pterin.	inorganic nitrite	127-144	xanthine dehydrogenase	Homo sapiens	102-105
10858495-2	2000	We show that peroxynitrite can be produced by the action of a single enzyme, xanthine oxidoreductase (XOR), in the presence of inorganic nitrite, molecular oxygen and a reducing agent, such as pterin.	Oxygen	156-162	xanthine dehydrogenase	Homo sapiens	102-105
10858495-2	2000	We show that peroxynitrite can be produced by the action of a single enzyme, xanthine oxidoreductase (XOR), in the presence of inorganic nitrite, molecular oxygen and a reducing agent, such as pterin.	Pterins	193-199	xanthine dehydrogenase	Homo sapiens	77-100
10858495-2	2000	We show that peroxynitrite can be produced by the action of a single enzyme, xanthine oxidoreductase (XOR), in the presence of inorganic nitrite, molecular oxygen and a reducing agent, such as pterin.	Pterins	193-199	xanthine dehydrogenase	Homo sapiens	102-105
11200484-0	2000	[Role of xanthine oxidase and xanthine dehydrogenase systems in thymocyte apoptosis, induced by papaverine].	Papaverine	96-106	xanthine dehydrogenase	Homo sapiens	30-52
11200484-3	2000	In papaverine-induced process of thymocyte apoptosis the total activity of xanthine oxidase in thymocytes strongly elevated long before their death, the conversion of xanthine dehydrogenase (D-form) to xanthinoxidase (O-form) and accumulation of O-form in the cultural medium took place.	Papaverine	3-13	xanthine dehydrogenase	Homo sapiens	167-189
10713088-0	2000	Reduction of nitrite to nitric oxide catalyzed by xanthine oxidoreductase.	Nitrites	13-20	xanthine dehydrogenase	Homo sapiens	50-73
10713088-0	2000	Reduction of nitrite to nitric oxide catalyzed by xanthine oxidoreductase.	Nitric Oxide	24-36	xanthine dehydrogenase	Homo sapiens	50-73
10822909-2	2000	During sustained physical exercise, reactive oxygen species (ROS) production increase through several mechanism; one of them is the purine nucleotide cycle activation by shifting xanthine-dehydrogenase to xanthine-oxidase during AMP breakdown.	Reactive Oxygen Species	36-59	xanthine dehydrogenase	Homo sapiens	179-201
10879682-2	2000	Three enzyme systems produce reactive oxygen species in the vascular wall: NADH/NADPH oxidase, xanthine oxidoreductase, and endothelial nitric oxide synthase.	Reactive Oxygen Species	29-52	xanthine dehydrogenase	Homo sapiens	95-118
10822909-2	2000	During sustained physical exercise, reactive oxygen species (ROS) production increase through several mechanism; one of them is the purine nucleotide cycle activation by shifting xanthine-dehydrogenase to xanthine-oxidase during AMP breakdown.	Reactive Oxygen Species	61-64	xanthine dehydrogenase	Homo sapiens	179-201
10822909-2	2000	During sustained physical exercise, reactive oxygen species (ROS) production increase through several mechanism; one of them is the purine nucleotide cycle activation by shifting xanthine-dehydrogenase to xanthine-oxidase during AMP breakdown.	Purine Nucleotides	132-149	xanthine dehydrogenase	Homo sapiens	179-201
10822909-2	2000	During sustained physical exercise, reactive oxygen species (ROS) production increase through several mechanism; one of them is the purine nucleotide cycle activation by shifting xanthine-dehydrogenase to xanthine-oxidase during AMP breakdown.	Adenosine Monophosphate	229-232	xanthine dehydrogenase	Homo sapiens	179-201
10554121-1	1999	BACKGROUND: The xanthine oxidoreductase system has been identified as one of the main sources of free radicals responsible for various forms of tissue injury.	Free Radicals	97-110	xanthine dehydrogenase	Homo sapiens	16-39
10620355-3	2000	XOR was purified as the NAD(+)-dependent dehydrogenase by benzamidine-Sepharose chromatography and was shown to be intact and to have biochemical properties similar to those of enzyme from other sources.	benzamidine	58-69	xanthine dehydrogenase	Homo sapiens	0-3
10620355-3	2000	XOR was purified as the NAD(+)-dependent dehydrogenase by benzamidine-Sepharose chromatography and was shown to be intact and to have biochemical properties similar to those of enzyme from other sources.	Sepharose	70-79	xanthine dehydrogenase	Homo sapiens	0-3
10620355-7	2000	Further, hormonal stimulation of XOR was inhibited by genistein (a protein tyrosine kinase inhibitor) and by PD 98059 (a specific inhibitor of the MAP kinase cascade).	Genistein	54-63	xanthine dehydrogenase	Homo sapiens	33-36
10623681-5	2000	The expression of xanthine dehydrogenase/xanthine oxidase holoenzyme and the activity of xanthine oxidase, the isoform known to generate reactive oxygen species, were increased in a subpopulation of cytotrophoblasts of preeclamptic women.	Reactive Oxygen Species	137-160	xanthine dehydrogenase	Homo sapiens	18-40
10604966-1	2000	Xanthine oxidoreductase (XOR) is a mammalian enzyme that possesses a series of redox centers, which use either NAD(+) or molecular oxygen for oxidation of the purines xanthine and hypoxanthine to uric acid.	NAD	111-117	xanthine dehydrogenase	Homo sapiens	0-23
10604966-1	2000	Xanthine oxidoreductase (XOR) is a mammalian enzyme that possesses a series of redox centers, which use either NAD(+) or molecular oxygen for oxidation of the purines xanthine and hypoxanthine to uric acid.	NAD	111-117	xanthine dehydrogenase	Homo sapiens	25-28
10604966-1	2000	Xanthine oxidoreductase (XOR) is a mammalian enzyme that possesses a series of redox centers, which use either NAD(+) or molecular oxygen for oxidation of the purines xanthine and hypoxanthine to uric acid.	Oxygen	131-137	xanthine dehydrogenase	Homo sapiens	0-23
10604966-1	2000	Xanthine oxidoreductase (XOR) is a mammalian enzyme that possesses a series of redox centers, which use either NAD(+) or molecular oxygen for oxidation of the purines xanthine and hypoxanthine to uric acid.	Oxygen	131-137	xanthine dehydrogenase	Homo sapiens	25-28
10604966-1	2000	Xanthine oxidoreductase (XOR) is a mammalian enzyme that possesses a series of redox centers, which use either NAD(+) or molecular oxygen for oxidation of the purines xanthine and hypoxanthine to uric acid.	Purines	159-166	xanthine dehydrogenase	Homo sapiens	0-23
10604966-1	2000	Xanthine oxidoreductase (XOR) is a mammalian enzyme that possesses a series of redox centers, which use either NAD(+) or molecular oxygen for oxidation of the purines xanthine and hypoxanthine to uric acid.	Purines	159-166	xanthine dehydrogenase	Homo sapiens	25-28
10604966-1	2000	Xanthine oxidoreductase (XOR) is a mammalian enzyme that possesses a series of redox centers, which use either NAD(+) or molecular oxygen for oxidation of the purines xanthine and hypoxanthine to uric acid.	Xanthine	167-175	xanthine dehydrogenase	Homo sapiens	0-23
10604966-1	2000	Xanthine oxidoreductase (XOR) is a mammalian enzyme that possesses a series of redox centers, which use either NAD(+) or molecular oxygen for oxidation of the purines xanthine and hypoxanthine to uric acid.	Xanthine	167-175	xanthine dehydrogenase	Homo sapiens	25-28
10604966-1	2000	Xanthine oxidoreductase (XOR) is a mammalian enzyme that possesses a series of redox centers, which use either NAD(+) or molecular oxygen for oxidation of the purines xanthine and hypoxanthine to uric acid.	Hypoxanthine	180-192	xanthine dehydrogenase	Homo sapiens	0-23
10604966-1	2000	Xanthine oxidoreductase (XOR) is a mammalian enzyme that possesses a series of redox centers, which use either NAD(+) or molecular oxygen for oxidation of the purines xanthine and hypoxanthine to uric acid.	Hypoxanthine	180-192	xanthine dehydrogenase	Homo sapiens	25-28
10604966-1	2000	Xanthine oxidoreductase (XOR) is a mammalian enzyme that possesses a series of redox centers, which use either NAD(+) or molecular oxygen for oxidation of the purines xanthine and hypoxanthine to uric acid.	Uric Acid	196-205	xanthine dehydrogenase	Homo sapiens	0-23
10604966-1	2000	Xanthine oxidoreductase (XOR) is a mammalian enzyme that possesses a series of redox centers, which use either NAD(+) or molecular oxygen for oxidation of the purines xanthine and hypoxanthine to uric acid.	Uric Acid	196-205	xanthine dehydrogenase	Homo sapiens	25-28
10604966-2	2000	The ability of XOR to act as an NADH oxidase is a less well recognized function of the enzyme, and it is this function that we used to explore the metabolism of glyceryl trinitrate.	Nitroglycerin	161-180	xanthine dehydrogenase	Homo sapiens	15-18
10604966-3	2000	The antiplatelet effect of nitric oxide (NO) on platelet aggregation was used as a bioassay to assess the bioconversion of glyceryl trinitrate to NO by XOR.	Nitroglycerin	123-142	xanthine dehydrogenase	Homo sapiens	152-155
10604966-6	2000	XOR produced a dose-dependent antiaggregant effect when incubated with glyceryl trinitrate (GTN), 220 microM.	Nitroglycerin	71-90	xanthine dehydrogenase	Homo sapiens	0-3
10604966-6	2000	XOR produced a dose-dependent antiaggregant effect when incubated with glyceryl trinitrate (GTN), 220 microM.	Nitroglycerin	92-95	xanthine dehydrogenase	Homo sapiens	0-3
10604966-8	2000	The antiaggregant effect of XOR plus GTN was dose dependently inhibited by allopurinol, with an IC(50) of 100 microM.	Allopurinol	75-86	xanthine dehydrogenase	Homo sapiens	28-31
10604966-12	2000	These findings suggest that GTN may be reduced to NO in vitro by the enzyme XOR in sufficient amounts to inhibit platelet aggregation.	Nitroglycerin	28-31	xanthine dehydrogenase	Homo sapiens	76-79
10506947-15	1999	Xanthine oxidase has been suggested to be involved in the pathogenesis of post-ischemic reperfusion tissue injury through the generation of reactive oxygen species, while the extensive tissue localization of xanthine dehydrogenase/oxidase suggests several other roles for this enzyme, including a protective barrier against bacterial infection by producing either superoxide radicals or uric acid.	Superoxides	364-383	xanthine dehydrogenase	Homo sapiens	208-238
11229448-6	1999	Xanthine dehydrogenase from mammalian sources can be converted to an oxidase form that readily donates electrons to molecular oxygen, but does not reduce NAD+.	Oxygen	126-132	xanthine dehydrogenase	Homo sapiens	0-22
10506947-15	1999	Xanthine oxidase has been suggested to be involved in the pathogenesis of post-ischemic reperfusion tissue injury through the generation of reactive oxygen species, while the extensive tissue localization of xanthine dehydrogenase/oxidase suggests several other roles for this enzyme, including a protective barrier against bacterial infection by producing either superoxide radicals or uric acid.	Uric Acid	387-396	xanthine dehydrogenase	Homo sapiens	208-238
10462034-1	1999	Xanthine oxidoreductase is an important cytoplasmic source of reactive oxygen species, and has been implicated in the pathogenesis of ischemia-reperfusion damage.	Reactive Oxygen Species	62-85	xanthine dehydrogenase	Homo sapiens	0-23
9895226-6	1999	Recently, hepatic XOR and AOX were found to generate ROS in two ways from alcohol metabolism: by acetaldehyde consumption and by the intrinsic NADH oxidase activity of both XOR and AOX.	Alcohols	74-81	xanthine dehydrogenase	Homo sapiens	18-21
10075667-0	1999	Inhibition of xanthine oxidase and xanthine dehydrogenase by nitric oxide.	Nitric Oxide	61-73	xanthine dehydrogenase	Homo sapiens	35-57
10075667-2	1999	Xanthine oxidase (XO) and xanthine dehydrogenase (XDH) were inactivated by incubation with nitric oxide under anaerobic conditions in the presence of xanthine or allopurinol.	Nitric Oxide	91-103	xanthine dehydrogenase	Homo sapiens	26-48
10075667-2	1999	Xanthine oxidase (XO) and xanthine dehydrogenase (XDH) were inactivated by incubation with nitric oxide under anaerobic conditions in the presence of xanthine or allopurinol.	Nitric Oxide	91-103	xanthine dehydrogenase	Homo sapiens	50-53
10075667-2	1999	Xanthine oxidase (XO) and xanthine dehydrogenase (XDH) were inactivated by incubation with nitric oxide under anaerobic conditions in the presence of xanthine or allopurinol.	Xanthine	26-34	xanthine dehydrogenase	Homo sapiens	50-53
10075667-2	1999	Xanthine oxidase (XO) and xanthine dehydrogenase (XDH) were inactivated by incubation with nitric oxide under anaerobic conditions in the presence of xanthine or allopurinol.	Allopurinol	162-173	xanthine dehydrogenase	Homo sapiens	26-48
10075667-2	1999	Xanthine oxidase (XO) and xanthine dehydrogenase (XDH) were inactivated by incubation with nitric oxide under anaerobic conditions in the presence of xanthine or allopurinol.	Allopurinol	162-173	xanthine dehydrogenase	Homo sapiens	50-53
10075667-6	1999	The flavin and iron-sulfur centers of inactivated XO were reduced by dithionite and reoxidized readily with oxygen, and inactivated XDH retained electron transfer activities from NADH to electron acceptors, consistent with the conclusion that the flavin and iron-sulfur centers of the inactivated enzyme both remained intact.	NAD	179-183	xanthine dehydrogenase	Homo sapiens	132-135
10075667-6	1999	The flavin and iron-sulfur centers of inactivated XO were reduced by dithionite and reoxidized readily with oxygen, and inactivated XDH retained electron transfer activities from NADH to electron acceptors, consistent with the conclusion that the flavin and iron-sulfur centers of the inactivated enzyme both remained intact.	4,6-dinitro-o-cresol	247-253	xanthine dehydrogenase	Homo sapiens	132-135
10075667-6	1999	The flavin and iron-sulfur centers of inactivated XO were reduced by dithionite and reoxidized readily with oxygen, and inactivated XDH retained electron transfer activities from NADH to electron acceptors, consistent with the conclusion that the flavin and iron-sulfur centers of the inactivated enzyme both remained intact.	Iron	258-262	xanthine dehydrogenase	Homo sapiens	132-135
10075667-6	1999	The flavin and iron-sulfur centers of inactivated XO were reduced by dithionite and reoxidized readily with oxygen, and inactivated XDH retained electron transfer activities from NADH to electron acceptors, consistent with the conclusion that the flavin and iron-sulfur centers of the inactivated enzyme both remained intact.	Sulfur	263-269	xanthine dehydrogenase	Homo sapiens	132-135
10075667-11	1999	It is concluded that nitric oxide reacts with an essential sulfur of the reduced molybdenum center of XO and XDH to produce desulfo-type inactive enzymes.	Nitric Oxide	21-33	xanthine dehydrogenase	Homo sapiens	109-112
10075667-11	1999	It is concluded that nitric oxide reacts with an essential sulfur of the reduced molybdenum center of XO and XDH to produce desulfo-type inactive enzymes.	Sulfur	59-65	xanthine dehydrogenase	Homo sapiens	109-112
9895226-5	1999	Mammary gland XOR is an efficient source of ROS.	Reactive Oxygen Species	44-47	xanthine dehydrogenase	Homo sapiens	14-17
9895226-6	1999	Recently, hepatic XOR and AOX were found to generate ROS in two ways from alcohol metabolism: by acetaldehyde consumption and by the intrinsic NADH oxidase activity of both XOR and AOX.	Reactive Oxygen Species	53-56	xanthine dehydrogenase	Homo sapiens	18-21
9895226-6	1999	Recently, hepatic XOR and AOX were found to generate ROS in two ways from alcohol metabolism: by acetaldehyde consumption and by the intrinsic NADH oxidase activity of both XOR and AOX.	Reactive Oxygen Species	53-56	xanthine dehydrogenase	Homo sapiens	173-176
9895226-6	1999	Recently, hepatic XOR and AOX were found to generate ROS in two ways from alcohol metabolism: by acetaldehyde consumption and by the intrinsic NADH oxidase activity of both XOR and AOX.	Alcohols	74-81	xanthine dehydrogenase	Homo sapiens	173-176
9895226-6	1999	Recently, hepatic XOR and AOX were found to generate ROS in two ways from alcohol metabolism: by acetaldehyde consumption and by the intrinsic NADH oxidase activity of both XOR and AOX.	Acetaldehyde	97-109	xanthine dehydrogenase	Homo sapiens	18-21
9895226-7	1999	The data obtained suggests that: (1) expression of ADH and XOR or AOX in breast tissue provides the enzymes that generate ROS; (2) metabolism of alcohol produces acetaldehyde and NADH that can both be substrates for XOR or AOX and thereby result in ROS formation; and (3) ROS generated by XOR or AOX can induce the carcinogenic mutations and DNA damage found in breast cancer.	Reactive Oxygen Species	122-125	xanthine dehydrogenase	Homo sapiens	59-62
9895226-7	1999	The data obtained suggests that: (1) expression of ADH and XOR or AOX in breast tissue provides the enzymes that generate ROS; (2) metabolism of alcohol produces acetaldehyde and NADH that can both be substrates for XOR or AOX and thereby result in ROS formation; and (3) ROS generated by XOR or AOX can induce the carcinogenic mutations and DNA damage found in breast cancer.	Reactive Oxygen Species	122-125	xanthine dehydrogenase	Homo sapiens	216-219
9895226-7	1999	The data obtained suggests that: (1) expression of ADH and XOR or AOX in breast tissue provides the enzymes that generate ROS; (2) metabolism of alcohol produces acetaldehyde and NADH that can both be substrates for XOR or AOX and thereby result in ROS formation; and (3) ROS generated by XOR or AOX can induce the carcinogenic mutations and DNA damage found in breast cancer.	Reactive Oxygen Species	122-125	xanthine dehydrogenase	Homo sapiens	216-219
9895226-7	1999	The data obtained suggests that: (1) expression of ADH and XOR or AOX in breast tissue provides the enzymes that generate ROS; (2) metabolism of alcohol produces acetaldehyde and NADH that can both be substrates for XOR or AOX and thereby result in ROS formation; and (3) ROS generated by XOR or AOX can induce the carcinogenic mutations and DNA damage found in breast cancer.	Alcohols	145-152	xanthine dehydrogenase	Homo sapiens	59-62
9895226-7	1999	The data obtained suggests that: (1) expression of ADH and XOR or AOX in breast tissue provides the enzymes that generate ROS; (2) metabolism of alcohol produces acetaldehyde and NADH that can both be substrates for XOR or AOX and thereby result in ROS formation; and (3) ROS generated by XOR or AOX can induce the carcinogenic mutations and DNA damage found in breast cancer.	Alcohols	145-152	xanthine dehydrogenase	Homo sapiens	216-219
9895226-7	1999	The data obtained suggests that: (1) expression of ADH and XOR or AOX in breast tissue provides the enzymes that generate ROS; (2) metabolism of alcohol produces acetaldehyde and NADH that can both be substrates for XOR or AOX and thereby result in ROS formation; and (3) ROS generated by XOR or AOX can induce the carcinogenic mutations and DNA damage found in breast cancer.	Alcohols	145-152	xanthine dehydrogenase	Homo sapiens	216-219
9895226-7	1999	The data obtained suggests that: (1) expression of ADH and XOR or AOX in breast tissue provides the enzymes that generate ROS; (2) metabolism of alcohol produces acetaldehyde and NADH that can both be substrates for XOR or AOX and thereby result in ROS formation; and (3) ROS generated by XOR or AOX can induce the carcinogenic mutations and DNA damage found in breast cancer.	Acetaldehyde	162-174	xanthine dehydrogenase	Homo sapiens	59-62
9895226-7	1999	The data obtained suggests that: (1) expression of ADH and XOR or AOX in breast tissue provides the enzymes that generate ROS; (2) metabolism of alcohol produces acetaldehyde and NADH that can both be substrates for XOR or AOX and thereby result in ROS formation; and (3) ROS generated by XOR or AOX can induce the carcinogenic mutations and DNA damage found in breast cancer.	Acetaldehyde	162-174	xanthine dehydrogenase	Homo sapiens	216-219
9895226-7	1999	The data obtained suggests that: (1) expression of ADH and XOR or AOX in breast tissue provides the enzymes that generate ROS; (2) metabolism of alcohol produces acetaldehyde and NADH that can both be substrates for XOR or AOX and thereby result in ROS formation; and (3) ROS generated by XOR or AOX can induce the carcinogenic mutations and DNA damage found in breast cancer.	Acetaldehyde	162-174	xanthine dehydrogenase	Homo sapiens	216-219
9895226-7	1999	The data obtained suggests that: (1) expression of ADH and XOR or AOX in breast tissue provides the enzymes that generate ROS; (2) metabolism of alcohol produces acetaldehyde and NADH that can both be substrates for XOR or AOX and thereby result in ROS formation; and (3) ROS generated by XOR or AOX can induce the carcinogenic mutations and DNA damage found in breast cancer.	NAD	179-183	xanthine dehydrogenase	Homo sapiens	59-62
9895226-7	1999	The data obtained suggests that: (1) expression of ADH and XOR or AOX in breast tissue provides the enzymes that generate ROS; (2) metabolism of alcohol produces acetaldehyde and NADH that can both be substrates for XOR or AOX and thereby result in ROS formation; and (3) ROS generated by XOR or AOX can induce the carcinogenic mutations and DNA damage found in breast cancer.	NAD	179-183	xanthine dehydrogenase	Homo sapiens	216-219
9895226-7	1999	The data obtained suggests that: (1) expression of ADH and XOR or AOX in breast tissue provides the enzymes that generate ROS; (2) metabolism of alcohol produces acetaldehyde and NADH that can both be substrates for XOR or AOX and thereby result in ROS formation; and (3) ROS generated by XOR or AOX can induce the carcinogenic mutations and DNA damage found in breast cancer.	NAD	179-183	xanthine dehydrogenase	Homo sapiens	216-219
9895226-7	1999	The data obtained suggests that: (1) expression of ADH and XOR or AOX in breast tissue provides the enzymes that generate ROS; (2) metabolism of alcohol produces acetaldehyde and NADH that can both be substrates for XOR or AOX and thereby result in ROS formation; and (3) ROS generated by XOR or AOX can induce the carcinogenic mutations and DNA damage found in breast cancer.	Reactive Oxygen Species	249-252	xanthine dehydrogenase	Homo sapiens	59-62
9895226-7	1999	The data obtained suggests that: (1) expression of ADH and XOR or AOX in breast tissue provides the enzymes that generate ROS; (2) metabolism of alcohol produces acetaldehyde and NADH that can both be substrates for XOR or AOX and thereby result in ROS formation; and (3) ROS generated by XOR or AOX can induce the carcinogenic mutations and DNA damage found in breast cancer.	Reactive Oxygen Species	249-252	xanthine dehydrogenase	Homo sapiens	216-219
9895226-7	1999	The data obtained suggests that: (1) expression of ADH and XOR or AOX in breast tissue provides the enzymes that generate ROS; (2) metabolism of alcohol produces acetaldehyde and NADH that can both be substrates for XOR or AOX and thereby result in ROS formation; and (3) ROS generated by XOR or AOX can induce the carcinogenic mutations and DNA damage found in breast cancer.	Reactive Oxygen Species	249-252	xanthine dehydrogenase	Homo sapiens	216-219
9895226-7	1999	The data obtained suggests that: (1) expression of ADH and XOR or AOX in breast tissue provides the enzymes that generate ROS; (2) metabolism of alcohol produces acetaldehyde and NADH that can both be substrates for XOR or AOX and thereby result in ROS formation; and (3) ROS generated by XOR or AOX can induce the carcinogenic mutations and DNA damage found in breast cancer.	Reactive Oxygen Species	249-252	xanthine dehydrogenase	Homo sapiens	59-62
9895226-7	1999	The data obtained suggests that: (1) expression of ADH and XOR or AOX in breast tissue provides the enzymes that generate ROS; (2) metabolism of alcohol produces acetaldehyde and NADH that can both be substrates for XOR or AOX and thereby result in ROS formation; and (3) ROS generated by XOR or AOX can induce the carcinogenic mutations and DNA damage found in breast cancer.	Reactive Oxygen Species	249-252	xanthine dehydrogenase	Homo sapiens	216-219
9895226-7	1999	The data obtained suggests that: (1) expression of ADH and XOR or AOX in breast tissue provides the enzymes that generate ROS; (2) metabolism of alcohol produces acetaldehyde and NADH that can both be substrates for XOR or AOX and thereby result in ROS formation; and (3) ROS generated by XOR or AOX can induce the carcinogenic mutations and DNA damage found in breast cancer.	Reactive Oxygen Species	249-252	xanthine dehydrogenase	Homo sapiens	216-219
9989587-1	1999	Irreversible conversion of xanthine dehydrogenase (XDH) to its oxygen free radical producing oxidase (XO) form occurs through an uncharacterized proteolytic process, which was studied in human liver.	Oxygen	63-69	xanthine dehydrogenase	Homo sapiens	27-49
9989587-1	1999	Irreversible conversion of xanthine dehydrogenase (XDH) to its oxygen free radical producing oxidase (XO) form occurs through an uncharacterized proteolytic process, which was studied in human liver.	Oxygen	63-69	xanthine dehydrogenase	Homo sapiens	51-54
9607316-0	1998	Xanthine oxidoreductase catalyses the reduction of nitrates and nitrite to nitric oxide under hypoxic conditions.	Nitrates	51-59	xanthine dehydrogenase	Homo sapiens	0-23
9701649-1	1998	Xanthine oxidoreductase (XOR) has been implicated in tissue injury following ischemia-reperfusion because of its ability to generate reactive oxygen species under these conditions.	Reactive Oxygen Species	133-156	xanthine dehydrogenase	Homo sapiens	0-23
9701649-1	1998	Xanthine oxidoreductase (XOR) has been implicated in tissue injury following ischemia-reperfusion because of its ability to generate reactive oxygen species under these conditions.	Reactive Oxygen Species	133-156	xanthine dehydrogenase	Homo sapiens	25-28
10888479-0	1999	Modulation of renal xanthine oxidoreductase in aging: gene expression and reactive oxygen species generation.	Reactive Oxygen Species	74-97	xanthine dehydrogenase	Homo sapiens	20-43
10888479-1	1999	Xanthine oxidoreductase (XD: xanthine dehydrogenase + xanthine oxidase) is a complex enzyme that catalyzes oxidation of hypoxathine to xanthine, subsequently producing uric acid.	hypoxathine	120-131	xanthine dehydrogenase	Homo sapiens	0-23
10888479-1	1999	Xanthine oxidoreductase (XD: xanthine dehydrogenase + xanthine oxidase) is a complex enzyme that catalyzes oxidation of hypoxathine to xanthine, subsequently producing uric acid.	hypoxathine	120-131	xanthine dehydrogenase	Homo sapiens	29-51
10888479-1	1999	Xanthine oxidoreductase (XD: xanthine dehydrogenase + xanthine oxidase) is a complex enzyme that catalyzes oxidation of hypoxathine to xanthine, subsequently producing uric acid.	Xanthine	29-37	xanthine dehydrogenase	Homo sapiens	0-23
10888479-1	1999	Xanthine oxidoreductase (XD: xanthine dehydrogenase + xanthine oxidase) is a complex enzyme that catalyzes oxidation of hypoxathine to xanthine, subsequently producing uric acid.	Uric Acid	168-177	xanthine dehydrogenase	Homo sapiens	0-23
10888479-1	1999	Xanthine oxidoreductase (XD: xanthine dehydrogenase + xanthine oxidase) is a complex enzyme that catalyzes oxidation of hypoxathine to xanthine, subsequently producing uric acid.	Uric Acid	168-177	xanthine dehydrogenase	Homo sapiens	29-51
9788904-5	1998	We observe that gene expression of XDH/XO is regulatory in a cell-specific manner and is markedly affected by inflammatory cytokines, steroids, and physiologic events such as hypoxia.	Steroids	134-142	xanthine dehydrogenase	Homo sapiens	35-38
9607316-0	1998	Xanthine oxidoreductase catalyses the reduction of nitrates and nitrite to nitric oxide under hypoxic conditions.	Nitrites	64-71	xanthine dehydrogenase	Homo sapiens	0-23
9607316-0	1998	Xanthine oxidoreductase catalyses the reduction of nitrates and nitrite to nitric oxide under hypoxic conditions.	Nitric Oxide	75-87	xanthine dehydrogenase	Homo sapiens	0-23
9607316-1	1998	Xanthine oxidoreductase (XOR) catalyses the reduction of the therapeutic organic nitrate, nitroglycerin (glyceryl trinitrate, GTN), as well as inorganic nitrate and nitrite, to nitric oxide (NO) under hypoxic conditions in the presence of NADH.	Nitrates	81-88	xanthine dehydrogenase	Homo sapiens	0-23
9607316-1	1998	Xanthine oxidoreductase (XOR) catalyses the reduction of the therapeutic organic nitrate, nitroglycerin (glyceryl trinitrate, GTN), as well as inorganic nitrate and nitrite, to nitric oxide (NO) under hypoxic conditions in the presence of NADH.	Nitrates	81-88	xanthine dehydrogenase	Homo sapiens	25-28
9607316-1	1998	Xanthine oxidoreductase (XOR) catalyses the reduction of the therapeutic organic nitrate, nitroglycerin (glyceryl trinitrate, GTN), as well as inorganic nitrate and nitrite, to nitric oxide (NO) under hypoxic conditions in the presence of NADH.	Nitroglycerin	90-103	xanthine dehydrogenase	Homo sapiens	0-23
9607316-1	1998	Xanthine oxidoreductase (XOR) catalyses the reduction of the therapeutic organic nitrate, nitroglycerin (glyceryl trinitrate, GTN), as well as inorganic nitrate and nitrite, to nitric oxide (NO) under hypoxic conditions in the presence of NADH.	Nitroglycerin	90-103	xanthine dehydrogenase	Homo sapiens	25-28
9607316-1	1998	Xanthine oxidoreductase (XOR) catalyses the reduction of the therapeutic organic nitrate, nitroglycerin (glyceryl trinitrate, GTN), as well as inorganic nitrate and nitrite, to nitric oxide (NO) under hypoxic conditions in the presence of NADH.	Nitroglycerin	105-124	xanthine dehydrogenase	Homo sapiens	0-23
9607316-1	1998	Xanthine oxidoreductase (XOR) catalyses the reduction of the therapeutic organic nitrate, nitroglycerin (glyceryl trinitrate, GTN), as well as inorganic nitrate and nitrite, to nitric oxide (NO) under hypoxic conditions in the presence of NADH.	Nitroglycerin	105-124	xanthine dehydrogenase	Homo sapiens	25-28
9607316-1	1998	Xanthine oxidoreductase (XOR) catalyses the reduction of the therapeutic organic nitrate, nitroglycerin (glyceryl trinitrate, GTN), as well as inorganic nitrate and nitrite, to nitric oxide (NO) under hypoxic conditions in the presence of NADH.	Nitroglycerin	126-129	xanthine dehydrogenase	Homo sapiens	0-23
9607316-1	1998	Xanthine oxidoreductase (XOR) catalyses the reduction of the therapeutic organic nitrate, nitroglycerin (glyceryl trinitrate, GTN), as well as inorganic nitrate and nitrite, to nitric oxide (NO) under hypoxic conditions in the presence of NADH.	Nitroglycerin	126-129	xanthine dehydrogenase	Homo sapiens	25-28
9607316-1	1998	Xanthine oxidoreductase (XOR) catalyses the reduction of the therapeutic organic nitrate, nitroglycerin (glyceryl trinitrate, GTN), as well as inorganic nitrate and nitrite, to nitric oxide (NO) under hypoxic conditions in the presence of NADH.	Nitrates	117-124	xanthine dehydrogenase	Homo sapiens	0-23
9607316-1	1998	Xanthine oxidoreductase (XOR) catalyses the reduction of the therapeutic organic nitrate, nitroglycerin (glyceryl trinitrate, GTN), as well as inorganic nitrate and nitrite, to nitric oxide (NO) under hypoxic conditions in the presence of NADH.	Nitrates	117-124	xanthine dehydrogenase	Homo sapiens	25-28
9607316-1	1998	Xanthine oxidoreductase (XOR) catalyses the reduction of the therapeutic organic nitrate, nitroglycerin (glyceryl trinitrate, GTN), as well as inorganic nitrate and nitrite, to nitric oxide (NO) under hypoxic conditions in the presence of NADH.	Nitrites	165-172	xanthine dehydrogenase	Homo sapiens	0-23
9607316-1	1998	Xanthine oxidoreductase (XOR) catalyses the reduction of the therapeutic organic nitrate, nitroglycerin (glyceryl trinitrate, GTN), as well as inorganic nitrate and nitrite, to nitric oxide (NO) under hypoxic conditions in the presence of NADH.	Nitrites	165-172	xanthine dehydrogenase	Homo sapiens	25-28
9607316-1	1998	Xanthine oxidoreductase (XOR) catalyses the reduction of the therapeutic organic nitrate, nitroglycerin (glyceryl trinitrate, GTN), as well as inorganic nitrate and nitrite, to nitric oxide (NO) under hypoxic conditions in the presence of NADH.	Nitric Oxide	177-189	xanthine dehydrogenase	Homo sapiens	0-23
9607316-1	1998	Xanthine oxidoreductase (XOR) catalyses the reduction of the therapeutic organic nitrate, nitroglycerin (glyceryl trinitrate, GTN), as well as inorganic nitrate and nitrite, to nitric oxide (NO) under hypoxic conditions in the presence of NADH.	Nitric Oxide	177-189	xanthine dehydrogenase	Homo sapiens	25-28
9607316-1	1998	Xanthine oxidoreductase (XOR) catalyses the reduction of the therapeutic organic nitrate, nitroglycerin (glyceryl trinitrate, GTN), as well as inorganic nitrate and nitrite, to nitric oxide (NO) under hypoxic conditions in the presence of NADH.	NAD	239-243	xanthine dehydrogenase	Homo sapiens	0-23
9607316-1	1998	Xanthine oxidoreductase (XOR) catalyses the reduction of the therapeutic organic nitrate, nitroglycerin (glyceryl trinitrate, GTN), as well as inorganic nitrate and nitrite, to nitric oxide (NO) under hypoxic conditions in the presence of NADH.	NAD	239-243	xanthine dehydrogenase	Homo sapiens	25-28
21528298-1	1997	Xanthine oxidase (XO) and xanthine dehydrogenase (XDH) are alternate enzymatic forms of the XO/XDH protein that catalyzes the oxidation of hypoxanthine to xanthine, and xanthine to uric acid, and in the process XO/XDH generates reactive oxygen species (ROS) such as superoxide, hydrogen peroxide, and hydroxyl radicals.	Hypoxanthine	139-151	xanthine dehydrogenase	Homo sapiens	26-48
9730249-11	1998	Elevations of intracellular calcium above a threshold are involved in: the stimulation of Ca2+-sensitive enzymes such as phospholipase A2, endonucleases and proteases, the conversion of xanthine dehydrogenase to xanthine oxidase and the formation of free radicals, all of which disturb biomembranes.	Calcium	28-35	xanthine dehydrogenase	Homo sapiens	186-208
9730249-11	1998	Elevations of intracellular calcium above a threshold are involved in: the stimulation of Ca2+-sensitive enzymes such as phospholipase A2, endonucleases and proteases, the conversion of xanthine dehydrogenase to xanthine oxidase and the formation of free radicals, all of which disturb biomembranes.	Free Radicals	250-263	xanthine dehydrogenase	Homo sapiens	186-208
9367530-6	1997	In the present investigation, the potential for drug activation of doxorubicin (DOX), streptonigrin (STN), and menadione (MD) by XO and XDH was assessed through oxygen consumption studies.	Doxorubicin	67-78	xanthine dehydrogenase	Homo sapiens	136-139
9367530-6	1997	In the present investigation, the potential for drug activation of doxorubicin (DOX), streptonigrin (STN), and menadione (MD) by XO and XDH was assessed through oxygen consumption studies.	Doxorubicin	80-83	xanthine dehydrogenase	Homo sapiens	136-139
9367530-6	1997	In the present investigation, the potential for drug activation of doxorubicin (DOX), streptonigrin (STN), and menadione (MD) by XO and XDH was assessed through oxygen consumption studies.	Streptonigrin	86-99	xanthine dehydrogenase	Homo sapiens	136-139
9367530-6	1997	In the present investigation, the potential for drug activation of doxorubicin (DOX), streptonigrin (STN), and menadione (MD) by XO and XDH was assessed through oxygen consumption studies.	Streptonigrin	101-104	xanthine dehydrogenase	Homo sapiens	136-139
9367530-6	1997	In the present investigation, the potential for drug activation of doxorubicin (DOX), streptonigrin (STN), and menadione (MD) by XO and XDH was assessed through oxygen consumption studies.	Vitamin K 3	111-120	xanthine dehydrogenase	Homo sapiens	136-139
9367530-6	1997	In the present investigation, the potential for drug activation of doxorubicin (DOX), streptonigrin (STN), and menadione (MD) by XO and XDH was assessed through oxygen consumption studies.	Oxygen	161-167	xanthine dehydrogenase	Homo sapiens	136-139
9367530-8	1997	Apparent kinetic constants were determined for DOX, STN, and MD activation by XO and XDH at both pH levels.	Doxorubicin	47-50	xanthine dehydrogenase	Homo sapiens	85-88
9367530-9	1997	Higher oxygen consumption was observed for XDH drug activation in comparison to XO drug activation at equivalent enzyme activity for both pH levels.	Oxygen	7-13	xanthine dehydrogenase	Homo sapiens	43-46
21528298-1	1997	Xanthine oxidase (XO) and xanthine dehydrogenase (XDH) are alternate enzymatic forms of the XO/XDH protein that catalyzes the oxidation of hypoxanthine to xanthine, and xanthine to uric acid, and in the process XO/XDH generates reactive oxygen species (ROS) such as superoxide, hydrogen peroxide, and hydroxyl radicals.	Reactive Oxygen Species	253-256	xanthine dehydrogenase	Homo sapiens	50-53
21528298-1	1997	Xanthine oxidase (XO) and xanthine dehydrogenase (XDH) are alternate enzymatic forms of the XO/XDH protein that catalyzes the oxidation of hypoxanthine to xanthine, and xanthine to uric acid, and in the process XO/XDH generates reactive oxygen species (ROS) such as superoxide, hydrogen peroxide, and hydroxyl radicals.	Reactive Oxygen Species	253-256	xanthine dehydrogenase	Homo sapiens	92-98
21528298-1	1997	Xanthine oxidase (XO) and xanthine dehydrogenase (XDH) are alternate enzymatic forms of the XO/XDH protein that catalyzes the oxidation of hypoxanthine to xanthine, and xanthine to uric acid, and in the process XO/XDH generates reactive oxygen species (ROS) such as superoxide, hydrogen peroxide, and hydroxyl radicals.	Reactive Oxygen Species	253-256	xanthine dehydrogenase	Homo sapiens	95-98
21528298-1	1997	Xanthine oxidase (XO) and xanthine dehydrogenase (XDH) are alternate enzymatic forms of the XO/XDH protein that catalyzes the oxidation of hypoxanthine to xanthine, and xanthine to uric acid, and in the process XO/XDH generates reactive oxygen species (ROS) such as superoxide, hydrogen peroxide, and hydroxyl radicals.	Superoxides	266-276	xanthine dehydrogenase	Homo sapiens	26-48
21528298-1	1997	Xanthine oxidase (XO) and xanthine dehydrogenase (XDH) are alternate enzymatic forms of the XO/XDH protein that catalyzes the oxidation of hypoxanthine to xanthine, and xanthine to uric acid, and in the process XO/XDH generates reactive oxygen species (ROS) such as superoxide, hydrogen peroxide, and hydroxyl radicals.	Superoxides	266-276	xanthine dehydrogenase	Homo sapiens	50-53
21528298-1	1997	Xanthine oxidase (XO) and xanthine dehydrogenase (XDH) are alternate enzymatic forms of the XO/XDH protein that catalyzes the oxidation of hypoxanthine to xanthine, and xanthine to uric acid, and in the process XO/XDH generates reactive oxygen species (ROS) such as superoxide, hydrogen peroxide, and hydroxyl radicals.	Superoxides	266-276	xanthine dehydrogenase	Homo sapiens	92-98
21528298-1	1997	Xanthine oxidase (XO) and xanthine dehydrogenase (XDH) are alternate enzymatic forms of the XO/XDH protein that catalyzes the oxidation of hypoxanthine to xanthine, and xanthine to uric acid, and in the process XO/XDH generates reactive oxygen species (ROS) such as superoxide, hydrogen peroxide, and hydroxyl radicals.	Superoxides	266-276	xanthine dehydrogenase	Homo sapiens	95-98
21528298-1	1997	Xanthine oxidase (XO) and xanthine dehydrogenase (XDH) are alternate enzymatic forms of the XO/XDH protein that catalyzes the oxidation of hypoxanthine to xanthine, and xanthine to uric acid, and in the process XO/XDH generates reactive oxygen species (ROS) such as superoxide, hydrogen peroxide, and hydroxyl radicals.	Hydrogen Peroxide	278-295	xanthine dehydrogenase	Homo sapiens	26-48
21528298-1	1997	Xanthine oxidase (XO) and xanthine dehydrogenase (XDH) are alternate enzymatic forms of the XO/XDH protein that catalyzes the oxidation of hypoxanthine to xanthine, and xanthine to uric acid, and in the process XO/XDH generates reactive oxygen species (ROS) such as superoxide, hydrogen peroxide, and hydroxyl radicals.	Hydrogen Peroxide	278-295	xanthine dehydrogenase	Homo sapiens	50-53
21528298-1	1997	Xanthine oxidase (XO) and xanthine dehydrogenase (XDH) are alternate enzymatic forms of the XO/XDH protein that catalyzes the oxidation of hypoxanthine to xanthine, and xanthine to uric acid, and in the process XO/XDH generates reactive oxygen species (ROS) such as superoxide, hydrogen peroxide, and hydroxyl radicals.	Hypoxanthine	139-151	xanthine dehydrogenase	Homo sapiens	50-53
21528298-1	1997	Xanthine oxidase (XO) and xanthine dehydrogenase (XDH) are alternate enzymatic forms of the XO/XDH protein that catalyzes the oxidation of hypoxanthine to xanthine, and xanthine to uric acid, and in the process XO/XDH generates reactive oxygen species (ROS) such as superoxide, hydrogen peroxide, and hydroxyl radicals.	Hydrogen Peroxide	278-295	xanthine dehydrogenase	Homo sapiens	92-98
21528298-1	1997	Xanthine oxidase (XO) and xanthine dehydrogenase (XDH) are alternate enzymatic forms of the XO/XDH protein that catalyzes the oxidation of hypoxanthine to xanthine, and xanthine to uric acid, and in the process XO/XDH generates reactive oxygen species (ROS) such as superoxide, hydrogen peroxide, and hydroxyl radicals.	Hydrogen Peroxide	278-295	xanthine dehydrogenase	Homo sapiens	95-98
21528298-1	1997	Xanthine oxidase (XO) and xanthine dehydrogenase (XDH) are alternate enzymatic forms of the XO/XDH protein that catalyzes the oxidation of hypoxanthine to xanthine, and xanthine to uric acid, and in the process XO/XDH generates reactive oxygen species (ROS) such as superoxide, hydrogen peroxide, and hydroxyl radicals.	Hypoxanthine	139-151	xanthine dehydrogenase	Homo sapiens	92-98
21528298-1	1997	Xanthine oxidase (XO) and xanthine dehydrogenase (XDH) are alternate enzymatic forms of the XO/XDH protein that catalyzes the oxidation of hypoxanthine to xanthine, and xanthine to uric acid, and in the process XO/XDH generates reactive oxygen species (ROS) such as superoxide, hydrogen peroxide, and hydroxyl radicals.	Hydroxyl Radical	301-318	xanthine dehydrogenase	Homo sapiens	26-48
21528298-1	1997	Xanthine oxidase (XO) and xanthine dehydrogenase (XDH) are alternate enzymatic forms of the XO/XDH protein that catalyzes the oxidation of hypoxanthine to xanthine, and xanthine to uric acid, and in the process XO/XDH generates reactive oxygen species (ROS) such as superoxide, hydrogen peroxide, and hydroxyl radicals.	Hydroxyl Radical	301-318	xanthine dehydrogenase	Homo sapiens	50-53
21528298-1	1997	Xanthine oxidase (XO) and xanthine dehydrogenase (XDH) are alternate enzymatic forms of the XO/XDH protein that catalyzes the oxidation of hypoxanthine to xanthine, and xanthine to uric acid, and in the process XO/XDH generates reactive oxygen species (ROS) such as superoxide, hydrogen peroxide, and hydroxyl radicals.	Hydroxyl Radical	301-318	xanthine dehydrogenase	Homo sapiens	92-98
21528298-1	1997	Xanthine oxidase (XO) and xanthine dehydrogenase (XDH) are alternate enzymatic forms of the XO/XDH protein that catalyzes the oxidation of hypoxanthine to xanthine, and xanthine to uric acid, and in the process XO/XDH generates reactive oxygen species (ROS) such as superoxide, hydrogen peroxide, and hydroxyl radicals.	Hydroxyl Radical	301-318	xanthine dehydrogenase	Homo sapiens	95-98
21528298-2	1997	We hypothesize that XO/XDH, which is expressed in mammary epithelium, contributes to the development of breast cancers by virtue of its ability to generate genotoxic ROS.	Reactive Oxygen Species	166-169	xanthine dehydrogenase	Homo sapiens	20-26
21528298-1	1997	Xanthine oxidase (XO) and xanthine dehydrogenase (XDH) are alternate enzymatic forms of the XO/XDH protein that catalyzes the oxidation of hypoxanthine to xanthine, and xanthine to uric acid, and in the process XO/XDH generates reactive oxygen species (ROS) such as superoxide, hydrogen peroxide, and hydroxyl radicals.	Hypoxanthine	139-151	xanthine dehydrogenase	Homo sapiens	95-98
21528298-1	1997	Xanthine oxidase (XO) and xanthine dehydrogenase (XDH) are alternate enzymatic forms of the XO/XDH protein that catalyzes the oxidation of hypoxanthine to xanthine, and xanthine to uric acid, and in the process XO/XDH generates reactive oxygen species (ROS) such as superoxide, hydrogen peroxide, and hydroxyl radicals.	Xanthine	26-34	xanthine dehydrogenase	Homo sapiens	50-53
21528298-1	1997	Xanthine oxidase (XO) and xanthine dehydrogenase (XDH) are alternate enzymatic forms of the XO/XDH protein that catalyzes the oxidation of hypoxanthine to xanthine, and xanthine to uric acid, and in the process XO/XDH generates reactive oxygen species (ROS) such as superoxide, hydrogen peroxide, and hydroxyl radicals.	Xanthine	26-34	xanthine dehydrogenase	Homo sapiens	92-98
21528298-1	1997	Xanthine oxidase (XO) and xanthine dehydrogenase (XDH) are alternate enzymatic forms of the XO/XDH protein that catalyzes the oxidation of hypoxanthine to xanthine, and xanthine to uric acid, and in the process XO/XDH generates reactive oxygen species (ROS) such as superoxide, hydrogen peroxide, and hydroxyl radicals.	Xanthine	26-34	xanthine dehydrogenase	Homo sapiens	95-98
21528298-1	1997	Xanthine oxidase (XO) and xanthine dehydrogenase (XDH) are alternate enzymatic forms of the XO/XDH protein that catalyzes the oxidation of hypoxanthine to xanthine, and xanthine to uric acid, and in the process XO/XDH generates reactive oxygen species (ROS) such as superoxide, hydrogen peroxide, and hydroxyl radicals.	Xanthine	143-151	xanthine dehydrogenase	Homo sapiens	26-48
21528298-1	1997	Xanthine oxidase (XO) and xanthine dehydrogenase (XDH) are alternate enzymatic forms of the XO/XDH protein that catalyzes the oxidation of hypoxanthine to xanthine, and xanthine to uric acid, and in the process XO/XDH generates reactive oxygen species (ROS) such as superoxide, hydrogen peroxide, and hydroxyl radicals.	Xanthine	143-151	xanthine dehydrogenase	Homo sapiens	50-53
21528298-1	1997	Xanthine oxidase (XO) and xanthine dehydrogenase (XDH) are alternate enzymatic forms of the XO/XDH protein that catalyzes the oxidation of hypoxanthine to xanthine, and xanthine to uric acid, and in the process XO/XDH generates reactive oxygen species (ROS) such as superoxide, hydrogen peroxide, and hydroxyl radicals.	Xanthine	143-151	xanthine dehydrogenase	Homo sapiens	92-98
21528298-1	1997	Xanthine oxidase (XO) and xanthine dehydrogenase (XDH) are alternate enzymatic forms of the XO/XDH protein that catalyzes the oxidation of hypoxanthine to xanthine, and xanthine to uric acid, and in the process XO/XDH generates reactive oxygen species (ROS) such as superoxide, hydrogen peroxide, and hydroxyl radicals.	Xanthine	143-151	xanthine dehydrogenase	Homo sapiens	95-98
21528298-1	1997	Xanthine oxidase (XO) and xanthine dehydrogenase (XDH) are alternate enzymatic forms of the XO/XDH protein that catalyzes the oxidation of hypoxanthine to xanthine, and xanthine to uric acid, and in the process XO/XDH generates reactive oxygen species (ROS) such as superoxide, hydrogen peroxide, and hydroxyl radicals.	Uric Acid	181-190	xanthine dehydrogenase	Homo sapiens	26-48
21528298-1	1997	Xanthine oxidase (XO) and xanthine dehydrogenase (XDH) are alternate enzymatic forms of the XO/XDH protein that catalyzes the oxidation of hypoxanthine to xanthine, and xanthine to uric acid, and in the process XO/XDH generates reactive oxygen species (ROS) such as superoxide, hydrogen peroxide, and hydroxyl radicals.	Uric Acid	181-190	xanthine dehydrogenase	Homo sapiens	50-53
21528298-1	1997	Xanthine oxidase (XO) and xanthine dehydrogenase (XDH) are alternate enzymatic forms of the XO/XDH protein that catalyzes the oxidation of hypoxanthine to xanthine, and xanthine to uric acid, and in the process XO/XDH generates reactive oxygen species (ROS) such as superoxide, hydrogen peroxide, and hydroxyl radicals.	Uric Acid	181-190	xanthine dehydrogenase	Homo sapiens	92-98
21528298-1	1997	Xanthine oxidase (XO) and xanthine dehydrogenase (XDH) are alternate enzymatic forms of the XO/XDH protein that catalyzes the oxidation of hypoxanthine to xanthine, and xanthine to uric acid, and in the process XO/XDH generates reactive oxygen species (ROS) such as superoxide, hydrogen peroxide, and hydroxyl radicals.	Uric Acid	181-190	xanthine dehydrogenase	Homo sapiens	95-98
21528298-1	1997	Xanthine oxidase (XO) and xanthine dehydrogenase (XDH) are alternate enzymatic forms of the XO/XDH protein that catalyzes the oxidation of hypoxanthine to xanthine, and xanthine to uric acid, and in the process XO/XDH generates reactive oxygen species (ROS) such as superoxide, hydrogen peroxide, and hydroxyl radicals.	Reactive Oxygen Species	228-251	xanthine dehydrogenase	Homo sapiens	26-48
21528298-1	1997	Xanthine oxidase (XO) and xanthine dehydrogenase (XDH) are alternate enzymatic forms of the XO/XDH protein that catalyzes the oxidation of hypoxanthine to xanthine, and xanthine to uric acid, and in the process XO/XDH generates reactive oxygen species (ROS) such as superoxide, hydrogen peroxide, and hydroxyl radicals.	Reactive Oxygen Species	228-251	xanthine dehydrogenase	Homo sapiens	50-53
21528298-1	1997	Xanthine oxidase (XO) and xanthine dehydrogenase (XDH) are alternate enzymatic forms of the XO/XDH protein that catalyzes the oxidation of hypoxanthine to xanthine, and xanthine to uric acid, and in the process XO/XDH generates reactive oxygen species (ROS) such as superoxide, hydrogen peroxide, and hydroxyl radicals.	Reactive Oxygen Species	228-251	xanthine dehydrogenase	Homo sapiens	92-98
21528298-1	1997	Xanthine oxidase (XO) and xanthine dehydrogenase (XDH) are alternate enzymatic forms of the XO/XDH protein that catalyzes the oxidation of hypoxanthine to xanthine, and xanthine to uric acid, and in the process XO/XDH generates reactive oxygen species (ROS) such as superoxide, hydrogen peroxide, and hydroxyl radicals.	Reactive Oxygen Species	228-251	xanthine dehydrogenase	Homo sapiens	95-98
21528298-1	1997	Xanthine oxidase (XO) and xanthine dehydrogenase (XDH) are alternate enzymatic forms of the XO/XDH protein that catalyzes the oxidation of hypoxanthine to xanthine, and xanthine to uric acid, and in the process XO/XDH generates reactive oxygen species (ROS) such as superoxide, hydrogen peroxide, and hydroxyl radicals.	Reactive Oxygen Species	253-256	xanthine dehydrogenase	Homo sapiens	26-48
9364609-1	1997	Xanthine dehydrogenase/oxidase (XDH/XO) produces uric acid.	Uric Acid	49-58	xanthine dehydrogenase	Homo sapiens	0-30
9364609-1	1997	Xanthine dehydrogenase/oxidase (XDH/XO) produces uric acid.	Uric Acid	49-58	xanthine dehydrogenase	Homo sapiens	32-35
9364609-5	1997	It was found that XO activity was higher in the placentae of labouring women (P = 0.003), which suggests that labour enhances conversion of XDH to XO, facilitating free radical production.	Free Radicals	164-176	xanthine dehydrogenase	Homo sapiens	140-143
23604305-3	1997	XDH acts on these same substrates but utilizes NAD as a cofactor to produce NADH instead of  O2 (-) and uric acid.	NAD	47-50	xanthine dehydrogenase	Homo sapiens	0-3
9388747-0	1997	Elevated circulating plasma NADH oxidising activity of xanthine oxidoreductase in plasma.	NAD	28-32	xanthine dehydrogenase	Homo sapiens	55-78
23604305-3	1997	XDH acts on these same substrates but utilizes NAD as a cofactor to produce NADH instead of  O2 (-) and uric acid.	NAD	76-80	xanthine dehydrogenase	Homo sapiens	0-3
23604305-3	1997	XDH acts on these same substrates but utilizes NAD as a cofactor to produce NADH instead of  O2 (-) and uric acid.	Superoxides	93-99	xanthine dehydrogenase	Homo sapiens	0-3
23604305-3	1997	XDH acts on these same substrates but utilizes NAD as a cofactor to produce NADH instead of  O2 (-) and uric acid.	Uric Acid	104-113	xanthine dehydrogenase	Homo sapiens	0-3
9182988-0	1997	NADH oxidase activity of human xanthine oxidoreductase--generation of superoxide anion.	Superoxides	70-86	xanthine dehydrogenase	Homo sapiens	31-54
9182988-7	1997	The potential involvement of reactive oxygen species arising from NADH oxidation by xanthine oxidoreductase in ischaemia-reperfusion injury and other disease states, as well as in normal signal transduction, is discusssed.	Reactive Oxygen Species	29-52	xanthine dehydrogenase	Homo sapiens	84-107
9182988-7	1997	The potential involvement of reactive oxygen species arising from NADH oxidation by xanthine oxidoreductase in ischaemia-reperfusion injury and other disease states, as well as in normal signal transduction, is discusssed.	NAD	66-70	xanthine dehydrogenase	Homo sapiens	84-107
9031292-0	1997	Possible association of xanthine dehydrogenase/xanthine oxidase activity with nitric oxide in vivo.	Nitric Oxide	78-90	xanthine dehydrogenase	Homo sapiens	24-46
9128279-2	1997	Experimental studies have revealed two main sources of these metabolites: 1) the oxidation of hypoxanthine to xanthine and on to uric acid by the oxidase form of xanthine oxidoreductase and 2) neutrophils accumulating in ischemic and reperfused tissue.	Hypoxanthine	94-106	xanthine dehydrogenase	Homo sapiens	162-185
9128279-2	1997	Experimental studies have revealed two main sources of these metabolites: 1) the oxidation of hypoxanthine to xanthine and on to uric acid by the oxidase form of xanthine oxidoreductase and 2) neutrophils accumulating in ischemic and reperfused tissue.	Xanthine	98-106	xanthine dehydrogenase	Homo sapiens	162-185
9128279-2	1997	Experimental studies have revealed two main sources of these metabolites: 1) the oxidation of hypoxanthine to xanthine and on to uric acid by the oxidase form of xanthine oxidoreductase and 2) neutrophils accumulating in ischemic and reperfused tissue.	Uric Acid	129-138	xanthine dehydrogenase	Homo sapiens	162-185
8824513-3	1996	The G418-resistant clone XAN1 was isolated and its DNA repair phenotype compared with XP12BE-SV cells transformed with a cosmid containing a human chromosome 8 gene and a neo(r) cassette and selected for G418 resistance (2-0-A2), DNA repair-normal human fibroblasts and untransfected XP12BE-SV cells.	antibiotic G 418	4-8	xanthine dehydrogenase	Homo sapiens	25-29
8569197-1	1996	Xanthine dehydrogenase/xanthine oxidase (XDH/XO) is a major cytoplasmic source of superoxide radicals and hydrogen peroxide, and it is considered important in the pathogenesis of ischemia-reperfusion damage.	Superoxides	82-92	xanthine dehydrogenase	Homo sapiens	0-22
8829220-1	1996	Xanthine dehydrogenase/oxidase (XDH, EC 1.1.1.204, XO, EC 1.2.3.2) produces uric acid, and in the oxidase form also generates the free radical superoxide.	Uric Acid	76-85	xanthine dehydrogenase	Homo sapiens	0-30
8829220-1	1996	Xanthine dehydrogenase/oxidase (XDH, EC 1.1.1.204, XO, EC 1.2.3.2) produces uric acid, and in the oxidase form also generates the free radical superoxide.	Uric Acid	76-85	xanthine dehydrogenase	Homo sapiens	32-35
8829220-1	1996	Xanthine dehydrogenase/oxidase (XDH, EC 1.1.1.204, XO, EC 1.2.3.2) produces uric acid, and in the oxidase form also generates the free radical superoxide.	Free Radicals	130-142	xanthine dehydrogenase	Homo sapiens	0-30
8829220-1	1996	Xanthine dehydrogenase/oxidase (XDH, EC 1.1.1.204, XO, EC 1.2.3.2) produces uric acid, and in the oxidase form also generates the free radical superoxide.	Free Radicals	130-142	xanthine dehydrogenase	Homo sapiens	32-35
8829220-1	1996	Xanthine dehydrogenase/oxidase (XDH, EC 1.1.1.204, XO, EC 1.2.3.2) produces uric acid, and in the oxidase form also generates the free radical superoxide.	Superoxides	143-153	xanthine dehydrogenase	Homo sapiens	0-30
8829220-1	1996	Xanthine dehydrogenase/oxidase (XDH, EC 1.1.1.204, XO, EC 1.2.3.2) produces uric acid, and in the oxidase form also generates the free radical superoxide.	Superoxides	143-153	xanthine dehydrogenase	Homo sapiens	32-35
8661045-1	1996	Xanthine dehydrogenase (XDH, EC 1.1.1.204) is a rate-limiting enzyme in the oxidative metabolism of purines and is thought to play a key role in a variety of pathophysiologic processes including ischemiasolidusreperfusion injury, viral pneumonia, and renal failure.	Purines	100-107	xanthine dehydrogenase	Homo sapiens	0-22
8661045-1	1996	Xanthine dehydrogenase (XDH, EC 1.1.1.204) is a rate-limiting enzyme in the oxidative metabolism of purines and is thought to play a key role in a variety of pathophysiologic processes including ischemiasolidusreperfusion injury, viral pneumonia, and renal failure.	Purines	100-107	xanthine dehydrogenase	Homo sapiens	24-27
8812740-0	1996	Tetrahydrobiopterin loading test in xanthine dehydrogenase and molybdenum cofactor deficiencies.	sapropterin	0-19	xanthine dehydrogenase	Homo sapiens	36-58
8812740-7	1996	Evidence was obtained for the in vivo involvement of xanthine dehydrogenase in the conversion of pterin to isoxanthopterin.	Pterins	97-103	xanthine dehydrogenase	Homo sapiens	53-75
8812740-7	1996	Evidence was obtained for the in vivo involvement of xanthine dehydrogenase in the conversion of pterin to isoxanthopterin.	isoxanthopterin	107-122	xanthine dehydrogenase	Homo sapiens	53-75
8567127-9	1996	This activity was also distinct from xanthine oxidoreductase and NADH-cytochrome b5 reductase, 2 other enzymes that catalyze metabolic activation of MMC, because the unique activity was not inhibited by allopurinol (an inhibitor of xanthine oxidoreductase) and its activity was the same with NADH and NADPH (cytochrome b5 reductase is specific to NADH).	Mitomycin	149-152	xanthine dehydrogenase	Homo sapiens	37-60
8567127-9	1996	This activity was also distinct from xanthine oxidoreductase and NADH-cytochrome b5 reductase, 2 other enzymes that catalyze metabolic activation of MMC, because the unique activity was not inhibited by allopurinol (an inhibitor of xanthine oxidoreductase) and its activity was the same with NADH and NADPH (cytochrome b5 reductase is specific to NADH).	Mitomycin	149-152	xanthine dehydrogenase	Homo sapiens	232-255
8567127-9	1996	This activity was also distinct from xanthine oxidoreductase and NADH-cytochrome b5 reductase, 2 other enzymes that catalyze metabolic activation of MMC, because the unique activity was not inhibited by allopurinol (an inhibitor of xanthine oxidoreductase) and its activity was the same with NADH and NADPH (cytochrome b5 reductase is specific to NADH).	Allopurinol	203-214	xanthine dehydrogenase	Homo sapiens	37-60
8567127-9	1996	This activity was also distinct from xanthine oxidoreductase and NADH-cytochrome b5 reductase, 2 other enzymes that catalyze metabolic activation of MMC, because the unique activity was not inhibited by allopurinol (an inhibitor of xanthine oxidoreductase) and its activity was the same with NADH and NADPH (cytochrome b5 reductase is specific to NADH).	NAD	65-69	xanthine dehydrogenase	Homo sapiens	232-255
8567127-9	1996	This activity was also distinct from xanthine oxidoreductase and NADH-cytochrome b5 reductase, 2 other enzymes that catalyze metabolic activation of MMC, because the unique activity was not inhibited by allopurinol (an inhibitor of xanthine oxidoreductase) and its activity was the same with NADH and NADPH (cytochrome b5 reductase is specific to NADH).	NADP	301-306	xanthine dehydrogenase	Homo sapiens	37-60
8567127-9	1996	This activity was also distinct from xanthine oxidoreductase and NADH-cytochrome b5 reductase, 2 other enzymes that catalyze metabolic activation of MMC, because the unique activity was not inhibited by allopurinol (an inhibitor of xanthine oxidoreductase) and its activity was the same with NADH and NADPH (cytochrome b5 reductase is specific to NADH).	NAD	292-296	xanthine dehydrogenase	Homo sapiens	37-60
8572024-4	1996	Xanthine dehydrogenase/oxidase produces uric acid.	Uric Acid	40-49	xanthine dehydrogenase	Homo sapiens	0-30
8569197-1	1996	Xanthine dehydrogenase/xanthine oxidase (XDH/XO) is a major cytoplasmic source of superoxide radicals and hydrogen peroxide, and it is considered important in the pathogenesis of ischemia-reperfusion damage.	Superoxides	82-92	xanthine dehydrogenase	Homo sapiens	41-47
8569197-1	1996	Xanthine dehydrogenase/xanthine oxidase (XDH/XO) is a major cytoplasmic source of superoxide radicals and hydrogen peroxide, and it is considered important in the pathogenesis of ischemia-reperfusion damage.	Hydrogen Peroxide	106-123	xanthine dehydrogenase	Homo sapiens	0-22
8569197-1	1996	Xanthine dehydrogenase/xanthine oxidase (XDH/XO) is a major cytoplasmic source of superoxide radicals and hydrogen peroxide, and it is considered important in the pathogenesis of ischemia-reperfusion damage.	Hydrogen Peroxide	106-123	xanthine dehydrogenase	Homo sapiens	41-47
7642590-5	1995	Application of the double-difference protocol to the respective circular dichroism spectra of xanthine oxidase and xanthine dehydrogenase reveals appreciable CD changes at 420 and 580 nm associated with the reduction of the molybdenum center.	Cadmium	158-160	xanthine dehydrogenase	Homo sapiens	115-137
7888480-1	1994	The aim of this study was the elucidation of the role of the xanthine oxidoreductase in the purine metabolism in ischaemic diseases of man.	purine	92-98	xanthine dehydrogenase	Homo sapiens	61-84
7649415-3	1995	Xanthine oxidase and xanthine dehydrogenase are enzymes involved in the metabolism of purines and pyrimidines in various organisms.	Purines	86-93	xanthine dehydrogenase	Homo sapiens	21-43
7649415-3	1995	Xanthine oxidase and xanthine dehydrogenase are enzymes involved in the metabolism of purines and pyrimidines in various organisms.	Pyrimidines	98-109	xanthine dehydrogenase	Homo sapiens	21-43
7622587-2	1995	Reactive O2 species (ROS) have been implicated in the pathogenesis of hypoxic and reoxygenation lung injury, and xanthine dehydrogenase/oxidase (XDH/XO) is a major generator of the ROS.	ros	21-24	xanthine dehydrogenase	Homo sapiens	145-148
7622587-2	1995	Reactive O2 species (ROS) have been implicated in the pathogenesis of hypoxic and reoxygenation lung injury, and xanthine dehydrogenase/oxidase (XDH/XO) is a major generator of the ROS.	ros	181-184	xanthine dehydrogenase	Homo sapiens	113-143
7622587-2	1995	Reactive O2 species (ROS) have been implicated in the pathogenesis of hypoxic and reoxygenation lung injury, and xanthine dehydrogenase/oxidase (XDH/XO) is a major generator of the ROS.	ros	181-184	xanthine dehydrogenase	Homo sapiens	145-148
7622587-9	1995	The absence of XDH/XO may prevent porcine PAEC from developing injury and increased ROS production during reoxygenation.	ros	84-87	xanthine dehydrogenase	Homo sapiens	15-18
7713871-1	1995	The mechanism of inhibition of milk xanthine oxidase and xanthine dehydrogenase by the tight binding inhibitor, sodium-8-(3-methoxy-4-phenylsulfinylphenyl)pyrazolo[1,5-a]-1,3,5- triazine-4-olate monohydrate (BOF-4272), was studied after separation of the two isomers.	BOF 4272	112-206	xanthine dehydrogenase	Homo sapiens	57-79
7713871-1	1995	The mechanism of inhibition of milk xanthine oxidase and xanthine dehydrogenase by the tight binding inhibitor, sodium-8-(3-methoxy-4-phenylsulfinylphenyl)pyrazolo[1,5-a]-1,3,5- triazine-4-olate monohydrate (BOF-4272), was studied after separation of the two isomers.	BOF 4272	208-216	xanthine dehydrogenase	Homo sapiens	57-79
7956361-1	1995	Mutations in the xanthine dehydrogenase gene (XDH), which codes for the last enzyme of the purine catabolic pathway in man, cause the autosomal recessive disease xanthinuria.	purine	91-97	xanthine dehydrogenase	Homo sapiens	17-39
7956361-1	1995	Mutations in the xanthine dehydrogenase gene (XDH), which codes for the last enzyme of the purine catabolic pathway in man, cause the autosomal recessive disease xanthinuria.	purine	91-97	xanthine dehydrogenase	Homo sapiens	46-49
7783663-0	1995	Ethanol as a xanthine dehydrogenase inhibitor.	Ethanol	0-7	xanthine dehydrogenase	Homo sapiens	13-35
7783663-1	1995	In the present study, we investigated whether ethanol inhibits the activity of xanthine dehydrogenase.	Ethanol	46-53	xanthine dehydrogenase	Homo sapiens	79-101
7783663-6	1995	These results suggest that ethanol inhibits xanthine dehydrogenase presumably by an ethanol-induced increase in the cytosolic concentration of NADH in the liver.	Ethanol	27-34	xanthine dehydrogenase	Homo sapiens	44-66
7783663-6	1995	These results suggest that ethanol inhibits xanthine dehydrogenase presumably by an ethanol-induced increase in the cytosolic concentration of NADH in the liver.	Ethanol	84-91	xanthine dehydrogenase	Homo sapiens	44-66
7783663-6	1995	These results suggest that ethanol inhibits xanthine dehydrogenase presumably by an ethanol-induced increase in the cytosolic concentration of NADH in the liver.	NAD	143-147	xanthine dehydrogenase	Homo sapiens	44-66
7896566-1	1994	Xanthine oxidoreductase is an enzyme which has the unusual property that it can exist in a dehydrogenase form which uses NAD+ and an oxidase form which uses oxygen as electron acceptor.	NAD	121-125	xanthine dehydrogenase	Homo sapiens	0-23
7896566-1	1994	Xanthine oxidoreductase is an enzyme which has the unusual property that it can exist in a dehydrogenase form which uses NAD+ and an oxidase form which uses oxygen as electron acceptor.	Oxygen	157-163	xanthine dehydrogenase	Homo sapiens	0-23
7888480-4	1994	An increase of the serum xanthine concentration in patients with myocardial infarction indicates a significant metabolic involvement of xanthine oxidoreductase in this disease and therefore a possible role in the development of tissue damage in the postischaemic phase due to oxygen radicals generated by the oxidase activity of this enzyme.	Xanthine	25-33	xanthine dehydrogenase	Homo sapiens	136-159
7888480-4	1994	An increase of the serum xanthine concentration in patients with myocardial infarction indicates a significant metabolic involvement of xanthine oxidoreductase in this disease and therefore a possible role in the development of tissue damage in the postischaemic phase due to oxygen radicals generated by the oxidase activity of this enzyme.	Reactive Oxygen Species	276-291	xanthine dehydrogenase	Homo sapiens	136-159
7519008-4	1994	Xanthine-induced lipofuscin formation could be inhibited by oxypurinol, indicating that the pigment may be formed by free radicals generated by xanthine dehydrogenase.	Xanthine	0-8	xanthine dehydrogenase	Homo sapiens	144-166
7829092-1	1994	Xanthine dehydrogenase (XDH, EC 1.1.1.204) oxidizes a variety of purines, pterins, and other heterogenic nitrogen compounds, serving as a rate-limiting enzyme in nucleic acid degradation.	Purines	65-72	xanthine dehydrogenase	Homo sapiens	0-22
7829092-1	1994	Xanthine dehydrogenase (XDH, EC 1.1.1.204) oxidizes a variety of purines, pterins, and other heterogenic nitrogen compounds, serving as a rate-limiting enzyme in nucleic acid degradation.	Purines	65-72	xanthine dehydrogenase	Homo sapiens	24-27
7829092-1	1994	Xanthine dehydrogenase (XDH, EC 1.1.1.204) oxidizes a variety of purines, pterins, and other heterogenic nitrogen compounds, serving as a rate-limiting enzyme in nucleic acid degradation.	Pterins	74-81	xanthine dehydrogenase	Homo sapiens	0-22
7829092-1	1994	Xanthine dehydrogenase (XDH, EC 1.1.1.204) oxidizes a variety of purines, pterins, and other heterogenic nitrogen compounds, serving as a rate-limiting enzyme in nucleic acid degradation.	Pterins	74-81	xanthine dehydrogenase	Homo sapiens	24-27
7829092-1	1994	Xanthine dehydrogenase (XDH, EC 1.1.1.204) oxidizes a variety of purines, pterins, and other heterogenic nitrogen compounds, serving as a rate-limiting enzyme in nucleic acid degradation.	Nitrogen	105-113	xanthine dehydrogenase	Homo sapiens	0-22
7829092-1	1994	Xanthine dehydrogenase (XDH, EC 1.1.1.204) oxidizes a variety of purines, pterins, and other heterogenic nitrogen compounds, serving as a rate-limiting enzyme in nucleic acid degradation.	Nitrogen	105-113	xanthine dehydrogenase	Homo sapiens	24-27
7829092-2	1994	The genetic defect of XDH results in hereditary xanthinuria and other disorders in purine metabolism.	purine	83-89	xanthine dehydrogenase	Homo sapiens	22-25
8034647-1	1994	The reductive half-reaction of milk xanthine dehydrogenase (XDH) with NADH and with xanthine has been studied at pH 7.5, 25 degree C. NADH reduces XDH to the two-electron reduced form at a rate of 18 s-1, independent of NADH concentration over the range studied.	NAD	70-74	xanthine dehydrogenase	Homo sapiens	36-58
8034647-1	1994	The reductive half-reaction of milk xanthine dehydrogenase (XDH) with NADH and with xanthine has been studied at pH 7.5, 25 degree C. NADH reduces XDH to the two-electron reduced form at a rate of 18 s-1, independent of NADH concentration over the range studied.	NAD	70-74	xanthine dehydrogenase	Homo sapiens	60-63
8034647-1	1994	The reductive half-reaction of milk xanthine dehydrogenase (XDH) with NADH and with xanthine has been studied at pH 7.5, 25 degree C. NADH reduces XDH to the two-electron reduced form at a rate of 18 s-1, independent of NADH concentration over the range studied.	NAD	70-74	xanthine dehydrogenase	Homo sapiens	147-150
8034647-1	1994	The reductive half-reaction of milk xanthine dehydrogenase (XDH) with NADH and with xanthine has been studied at pH 7.5, 25 degree C. NADH reduces XDH to the two-electron reduced form at a rate of 18 s-1, independent of NADH concentration over the range studied.	Xanthine	36-44	xanthine dehydrogenase	Homo sapiens	60-63
8034647-1	1994	The reductive half-reaction of milk xanthine dehydrogenase (XDH) with NADH and with xanthine has been studied at pH 7.5, 25 degree C. NADH reduces XDH to the two-electron reduced form at a rate of 18 s-1, independent of NADH concentration over the range studied.	Xanthine	36-44	xanthine dehydrogenase	Homo sapiens	147-150
8034647-1	1994	The reductive half-reaction of milk xanthine dehydrogenase (XDH) with NADH and with xanthine has been studied at pH 7.5, 25 degree C. NADH reduces XDH to the two-electron reduced form at a rate of 18 s-1, independent of NADH concentration over the range studied.	NAD	134-138	xanthine dehydrogenase	Homo sapiens	36-58
8034647-1	1994	The reductive half-reaction of milk xanthine dehydrogenase (XDH) with NADH and with xanthine has been studied at pH 7.5, 25 degree C. NADH reduces XDH to the two-electron reduced form at a rate of 18 s-1, independent of NADH concentration over the range studied.	NAD	134-138	xanthine dehydrogenase	Homo sapiens	60-63
8034647-1	1994	The reductive half-reaction of milk xanthine dehydrogenase (XDH) with NADH and with xanthine has been studied at pH 7.5, 25 degree C. NADH reduces XDH to the two-electron reduced form at a rate of 18 s-1, independent of NADH concentration over the range studied.	NAD	134-138	xanthine dehydrogenase	Homo sapiens	147-150
8034647-1	1994	The reductive half-reaction of milk xanthine dehydrogenase (XDH) with NADH and with xanthine has been studied at pH 7.5, 25 degree C. NADH reduces XDH to the two-electron reduced form at a rate of 18 s-1, independent of NADH concentration over the range studied.	NAD	134-138	xanthine dehydrogenase	Homo sapiens	36-58
8034647-1	1994	The reductive half-reaction of milk xanthine dehydrogenase (XDH) with NADH and with xanthine has been studied at pH 7.5, 25 degree C. NADH reduces XDH to the two-electron reduced form at a rate of 18 s-1, independent of NADH concentration over the range studied.	NAD	134-138	xanthine dehydrogenase	Homo sapiens	60-63
8034647-1	1994	The reductive half-reaction of milk xanthine dehydrogenase (XDH) with NADH and with xanthine has been studied at pH 7.5, 25 degree C. NADH reduces XDH to the two-electron reduced form at a rate of 18 s-1, independent of NADH concentration over the range studied.	NAD	134-138	xanthine dehydrogenase	Homo sapiens	147-150
8034647-4	1994	The four-electron reduced species reached through reduction by NADH is the same as the species obtained upon reaction of NAD with fully reduced XDH.	NAD	63-67	xanthine dehydrogenase	Homo sapiens	144-147
8034647-4	1994	The four-electron reduced species reached through reduction by NADH is the same as the species obtained upon reaction of NAD with fully reduced XDH.	NAD	63-66	xanthine dehydrogenase	Homo sapiens	144-147
8034647-5	1994	In contrast, xanthine rapidly reduces XDH to the four-electron level; further reduction is comparatively slow and is inhibited by excess xanthine.	Xanthine	13-21	xanthine dehydrogenase	Homo sapiens	38-41
8034647-6	1994	Studies using substoichiometric xanthine show that the reaction of XDH with 1 equivalent of xanthine involves rapid substrate binding and rapid reduction of the molybdenum center of the enzyme.	Xanthine	32-40	xanthine dehydrogenase	Homo sapiens	67-70
8034647-6	1994	Studies using substoichiometric xanthine show that the reaction of XDH with 1 equivalent of xanthine involves rapid substrate binding and rapid reduction of the molybdenum center of the enzyme.	Xanthine	92-100	xanthine dehydrogenase	Homo sapiens	67-70
8034647-7	1994	Before the release of urate from the molybdenum active site, an electron is transferred at 15 s-1 from the reduced molybdenum center to one of the iron-sulfur centers of XDH.	Uric Acid	22-27	xanthine dehydrogenase	Homo sapiens	170-173
8034647-7	1994	Before the release of urate from the molybdenum active site, an electron is transferred at 15 s-1 from the reduced molybdenum center to one of the iron-sulfur centers of XDH.	Iron	147-151	xanthine dehydrogenase	Homo sapiens	170-173
8034647-7	1994	Before the release of urate from the molybdenum active site, an electron is transferred at 15 s-1 from the reduced molybdenum center to one of the iron-sulfur centers of XDH.	Sulfur	152-158	xanthine dehydrogenase	Homo sapiens	170-173
8034647-9	1994	The reductive half-reaction of XDH with xanthine is rate-limiting in xanthine/NAD turnover, which appears to occur between the two- and four-electron reduced enzyme species.	Xanthine	40-48	xanthine dehydrogenase	Homo sapiens	31-34
8034647-9	1994	The reductive half-reaction of XDH with xanthine is rate-limiting in xanthine/NAD turnover, which appears to occur between the two- and four-electron reduced enzyme species.	Xanthine	69-77	xanthine dehydrogenase	Homo sapiens	31-34
8034647-9	1994	The reductive half-reaction of XDH with xanthine is rate-limiting in xanthine/NAD turnover, which appears to occur between the two- and four-electron reduced enzyme species.	NAD	78-81	xanthine dehydrogenase	Homo sapiens	31-34
8034647-10	1994	The reduction of XDH by substoichiometric amounts of the fluorescent substrate xanthopterin was also studied.	Xanthopterin	79-91	xanthine dehydrogenase	Homo sapiens	17-20
8071837-1	1994	A novel pyrazolotriazine derivative [BOF-4272, sodium-(+-)-8-(3-methoxy-4-phenylsulfinylphenyl)pyrazolo[1,5-a]-1 ,3,5-triazine-4-olate monohydrate], which inhibits biosynthesis of uric acid (UA) by interfering with xanthine oxidase/xanthine dehydrogenase, was administered p.o.	pyrazolotriazine	8-24	xanthine dehydrogenase	Homo sapiens	232-254
8071837-1	1994	A novel pyrazolotriazine derivative [BOF-4272, sodium-(+-)-8-(3-methoxy-4-phenylsulfinylphenyl)pyrazolo[1,5-a]-1 ,3,5-triazine-4-olate monohydrate], which inhibits biosynthesis of uric acid (UA) by interfering with xanthine oxidase/xanthine dehydrogenase, was administered p.o.	BOF 4272	47-146	xanthine dehydrogenase	Homo sapiens	232-254
7519008-4	1994	Xanthine-induced lipofuscin formation could be inhibited by oxypurinol, indicating that the pigment may be formed by free radicals generated by xanthine dehydrogenase.	Lipofuscin	17-27	xanthine dehydrogenase	Homo sapiens	144-166
7519008-4	1994	Xanthine-induced lipofuscin formation could be inhibited by oxypurinol, indicating that the pigment may be formed by free radicals generated by xanthine dehydrogenase.	Oxypurinol	60-70	xanthine dehydrogenase	Homo sapiens	144-166
7519008-4	1994	Xanthine-induced lipofuscin formation could be inhibited by oxypurinol, indicating that the pigment may be formed by free radicals generated by xanthine dehydrogenase.	Free Radicals	117-130	xanthine dehydrogenase	Homo sapiens	144-166
8135849-1	1994	Xanthine dehydrogenase (XDH, EC 1.1.1.204) is a molybdenum iron-sulphur flavin hydroxylase which oxidizes a variety of purines, pterins and other heterogenic nitrogen compounds, serving as a rate-limiting enzyme in nucleic acid degradation.	Purines	119-126	xanthine dehydrogenase	Homo sapiens	0-22
7798166-5	1994	The flavin semiquinone is thermodynamically stable in xanthine dehydrogenase, but is unstable in xanthine oxidase.	flavin semiquinone	4-22	xanthine dehydrogenase	Homo sapiens	54-76
7798166-7	1994	Although xanthine dehydrogenase can produce greater amounts of superoxide anion than xanthine oxidase during xanthine-oxygen turnover, it seems to be physiologically insignificant because NAD inhibits almost completely the formation of superoxide anion.	Superoxides	63-79	xanthine dehydrogenase	Homo sapiens	9-31
7798166-7	1994	Although xanthine dehydrogenase can produce greater amounts of superoxide anion than xanthine oxidase during xanthine-oxygen turnover, it seems to be physiologically insignificant because NAD inhibits almost completely the formation of superoxide anion.	Oxygen	118-124	xanthine dehydrogenase	Homo sapiens	9-31
8038267-9	1994	Beside the well known regulation of the xanthine dehydrogenase/xanthine oxidase ratio by the redox status of SH-groups, substances reacting with NH2-groups of the xanthine oxidoreductase are also able to change the xanthine dehydrogenase/xanthine oxidase activity ratio, thereby influencing the potential to generate oxygen radicals by xanthine oxidoreductase.	Reactive Oxygen Species	317-332	xanthine dehydrogenase	Homo sapiens	215-237
8038267-9	1994	Beside the well known regulation of the xanthine dehydrogenase/xanthine oxidase ratio by the redox status of SH-groups, substances reacting with NH2-groups of the xanthine oxidoreductase are also able to change the xanthine dehydrogenase/xanthine oxidase activity ratio, thereby influencing the potential to generate oxygen radicals by xanthine oxidoreductase.	Reactive Oxygen Species	317-332	xanthine dehydrogenase	Homo sapiens	336-359
8038267-0	1994	Modulation of the xanthine oxidase/xanthine dehydrogenase ratio by reaction of malondialdehyde with NH2-groups.	Malondialdehyde	79-94	xanthine dehydrogenase	Homo sapiens	35-57
8038267-1	1994	The potential of xanthine oxidoreductase to generate oxygen radicals depends on the ratio of xanthine dehydrogenase and xanthine oxidase.	Reactive Oxygen Species	53-68	xanthine dehydrogenase	Homo sapiens	17-40
8038267-1	1994	The potential of xanthine oxidoreductase to generate oxygen radicals depends on the ratio of xanthine dehydrogenase and xanthine oxidase.	Reactive Oxygen Species	53-68	xanthine dehydrogenase	Homo sapiens	93-115
8038267-2	1994	Previous studies showed that the lipid peroxidation products, malondialdehyde and 4-hydroxynonenal have different effects on xanthine oxidoreductase activity.	Malondialdehyde	62-77	xanthine dehydrogenase	Homo sapiens	125-148
8038267-2	1994	Previous studies showed that the lipid peroxidation products, malondialdehyde and 4-hydroxynonenal have different effects on xanthine oxidoreductase activity.	4-hydroxy-2-nonenal	82-98	xanthine dehydrogenase	Homo sapiens	125-148
8038267-4	1994	We therefore investigated the influence of malondialdehyde on xanthine oxidoreductase.	Malondialdehyde	43-58	xanthine dehydrogenase	Homo sapiens	62-85
8038267-7	1994	The inhibited xanthine oxidase was converted to an active xanthine dehydrogenase by dithiothreitol treatment.	Dithiothreitol	84-98	xanthine dehydrogenase	Homo sapiens	58-80
8038267-9	1994	Beside the well known regulation of the xanthine dehydrogenase/xanthine oxidase ratio by the redox status of SH-groups, substances reacting with NH2-groups of the xanthine oxidoreductase are also able to change the xanthine dehydrogenase/xanthine oxidase activity ratio, thereby influencing the potential to generate oxygen radicals by xanthine oxidoreductase.	Reactive Oxygen Species	317-332	xanthine dehydrogenase	Homo sapiens	40-62
8038267-9	1994	Beside the well known regulation of the xanthine dehydrogenase/xanthine oxidase ratio by the redox status of SH-groups, substances reacting with NH2-groups of the xanthine oxidoreductase are also able to change the xanthine dehydrogenase/xanthine oxidase activity ratio, thereby influencing the potential to generate oxygen radicals by xanthine oxidoreductase.	Reactive Oxygen Species	317-332	xanthine dehydrogenase	Homo sapiens	163-186
8135849-1	1994	Xanthine dehydrogenase (XDH, EC 1.1.1.204) is a molybdenum iron-sulphur flavin hydroxylase which oxidizes a variety of purines, pterins and other heterogenic nitrogen compounds, serving as a rate-limiting enzyme in nucleic acid degradation.	Purines	119-126	xanthine dehydrogenase	Homo sapiens	24-27
8135849-1	1994	Xanthine dehydrogenase (XDH, EC 1.1.1.204) is a molybdenum iron-sulphur flavin hydroxylase which oxidizes a variety of purines, pterins and other heterogenic nitrogen compounds, serving as a rate-limiting enzyme in nucleic acid degradation.	Pterins	128-135	xanthine dehydrogenase	Homo sapiens	0-22
8135849-1	1994	Xanthine dehydrogenase (XDH, EC 1.1.1.204) is a molybdenum iron-sulphur flavin hydroxylase which oxidizes a variety of purines, pterins and other heterogenic nitrogen compounds, serving as a rate-limiting enzyme in nucleic acid degradation.	Pterins	128-135	xanthine dehydrogenase	Homo sapiens	24-27
8135849-1	1994	Xanthine dehydrogenase (XDH, EC 1.1.1.204) is a molybdenum iron-sulphur flavin hydroxylase which oxidizes a variety of purines, pterins and other heterogenic nitrogen compounds, serving as a rate-limiting enzyme in nucleic acid degradation.	Nitrogen	158-166	xanthine dehydrogenase	Homo sapiens	0-22
8135849-1	1994	Xanthine dehydrogenase (XDH, EC 1.1.1.204) is a molybdenum iron-sulphur flavin hydroxylase which oxidizes a variety of purines, pterins and other heterogenic nitrogen compounds, serving as a rate-limiting enzyme in nucleic acid degradation.	Nitrogen	158-166	xanthine dehydrogenase	Homo sapiens	24-27
8227023-1	1993	The reduction of milk xanthine dehydrogenase by salicylate anion radical (SL-), nicotinamide adenine dinucleotide radical (NAD.), and 1-methylnicotinamide (NMA) radicals was investigated by the use of pulse radiolysis.	salicylate anion radical	48-72	xanthine dehydrogenase	Homo sapiens	22-44
8304479-8	1994	Trifluoperazine also decreased superoxide radical production during H/R and was shown to inhibit the conversion of xanthine dehydrogenase to xanthine oxidase.	Trifluoperazine	0-15	xanthine dehydrogenase	Homo sapiens	115-137
8304479-12	1994	In summary, Ca2+ derived from extracellular sources promoted superoxide radical production and renal cell injury by a calmodulin-dependent conversion of xanthine dehydrogenase to xanthine oxidase, a major source of oxygen free radicals during H/R.	Superoxides	61-79	xanthine dehydrogenase	Homo sapiens	153-175
8304479-12	1994	In summary, Ca2+ derived from extracellular sources promoted superoxide radical production and renal cell injury by a calmodulin-dependent conversion of xanthine dehydrogenase to xanthine oxidase, a major source of oxygen free radicals during H/R.	oxygen free radicals	215-235	xanthine dehydrogenase	Homo sapiens	153-175
8227023-1	1993	The reduction of milk xanthine dehydrogenase by salicylate anion radical (SL-), nicotinamide adenine dinucleotide radical (NAD.), and 1-methylnicotinamide (NMA) radicals was investigated by the use of pulse radiolysis.	nicotinamide adenine dinucleotide radical	80-121	xanthine dehydrogenase	Homo sapiens	22-44
8227023-1	1993	The reduction of milk xanthine dehydrogenase by salicylate anion radical (SL-), nicotinamide adenine dinucleotide radical (NAD.), and 1-methylnicotinamide (NMA) radicals was investigated by the use of pulse radiolysis.	NAD	123-127	xanthine dehydrogenase	Homo sapiens	22-44
8227023-1	1993	The reduction of milk xanthine dehydrogenase by salicylate anion radical (SL-), nicotinamide adenine dinucleotide radical (NAD.), and 1-methylnicotinamide (NMA) radicals was investigated by the use of pulse radiolysis.	N(1)-methylnicotinamide	134-154	xanthine dehydrogenase	Homo sapiens	22-44
8227023-1	1993	The reduction of milk xanthine dehydrogenase by salicylate anion radical (SL-), nicotinamide adenine dinucleotide radical (NAD.), and 1-methylnicotinamide (NMA) radicals was investigated by the use of pulse radiolysis.	nma	156-159	xanthine dehydrogenase	Homo sapiens	22-44
8227023-10	1993	reacted predominantly with FAD of the dehydrogenase to form the neutral semiquinone of FAD with a second order rate constant of 1.4 x 10(7) M-1 s-1 at pH 7.5, whereas a similar reaction in the oxidase, which was converted from xanthine dehydrogenase by proteolytical cleavage, was not observed.	Flavin-Adenine Dinucleotide	27-30	xanthine dehydrogenase	Homo sapiens	227-249
8227023-10	1993	reacted predominantly with FAD of the dehydrogenase to form the neutral semiquinone of FAD with a second order rate constant of 1.4 x 10(7) M-1 s-1 at pH 7.5, whereas a similar reaction in the oxidase, which was converted from xanthine dehydrogenase by proteolytical cleavage, was not observed.	Flavin-Adenine Dinucleotide	87-90	xanthine dehydrogenase	Homo sapiens	227-249
8248161-3	1993	Human XD possessed many of the signature sequences typical of XDs from flies and rodents, including an unusual cysteine distribution, a potential 2Fe/2S binding site, and a putative molybdopterin cofactor binding domain.	Cysteine	111-119	xanthine dehydrogenase	Homo sapiens	6-8
8221687-0	1993	Kinetics and mechanism of mitomycin C bioactivation by xanthine dehydrogenase under aerobic and hypoxic conditions.	Mitomycin	26-37	xanthine dehydrogenase	Homo sapiens	55-77
8221687-1	1993	These studies examined the kinetic and mechanistic parameters of mitomycin C (MMC) bioreduction by xanthine dehydrogenase (XDH), an enzyme recently shown to be capable of MMC activation.	Mitomycin	65-76	xanthine dehydrogenase	Homo sapiens	99-121
8221687-1	1993	These studies examined the kinetic and mechanistic parameters of mitomycin C (MMC) bioreduction by xanthine dehydrogenase (XDH), an enzyme recently shown to be capable of MMC activation.	Mitomycin	65-76	xanthine dehydrogenase	Homo sapiens	123-126
8221687-1	1993	These studies examined the kinetic and mechanistic parameters of mitomycin C (MMC) bioreduction by xanthine dehydrogenase (XDH), an enzyme recently shown to be capable of MMC activation.	Mitomycin	78-81	xanthine dehydrogenase	Homo sapiens	99-121
8221687-1	1993	These studies examined the kinetic and mechanistic parameters of mitomycin C (MMC) bioreduction by xanthine dehydrogenase (XDH), an enzyme recently shown to be capable of MMC activation.	Mitomycin	78-81	xanthine dehydrogenase	Homo sapiens	123-126
8221687-2	1993	The bioreduction of MMC by XDH leads to the formation of 2,7-diaminomitosene (2,7-DM) under both aerobic and hypoxic conditions, with greater 2,7-DM formation observed under hypoxic conditions.	Mitomycin	20-23	xanthine dehydrogenase	Homo sapiens	27-30
8221687-2	1993	The bioreduction of MMC by XDH leads to the formation of 2,7-diaminomitosene (2,7-DM) under both aerobic and hypoxic conditions, with greater 2,7-DM formation observed under hypoxic conditions.	2,7-diaminomitosene	57-76	xanthine dehydrogenase	Homo sapiens	27-30
8221687-2	1993	The bioreduction of MMC by XDH leads to the formation of 2,7-diaminomitosene (2,7-DM) under both aerobic and hypoxic conditions, with greater 2,7-DM formation observed under hypoxic conditions.	2,7-diaminomitosene	78-84	xanthine dehydrogenase	Homo sapiens	27-30
8221687-2	1993	The bioreduction of MMC by XDH leads to the formation of 2,7-diaminomitosene (2,7-DM) under both aerobic and hypoxic conditions, with greater 2,7-DM formation observed under hypoxic conditions.	2,7-diaminomitosene	142-148	xanthine dehydrogenase	Homo sapiens	27-30
8221687-3	1993	The XDH-induced formation of 2,7-DM is pH dependent with increasing formation as the pH is varied from 7.4 to 6.0.	2,7-diaminomitosene	29-35	xanthine dehydrogenase	Homo sapiens	4-7
8221687-4	1993	In this study, the kinetics of MMC bioreduction by XDH was assessed under aerobic and hypoxic conditions and at pH 7.4 and 6.0.	Mitomycin	31-34	xanthine dehydrogenase	Homo sapiens	51-54
8221687-5	1993	MMC interaction with XDH was also assessed by monitoring the ability of MMC to inhibit XDH-mediated uric acid and NADH formation.	Uric Acid	100-109	xanthine dehydrogenase	Homo sapiens	87-90
8221687-5	1993	MMC interaction with XDH was also assessed by monitoring the ability of MMC to inhibit XDH-mediated uric acid and NADH formation.	NAD	114-118	xanthine dehydrogenase	Homo sapiens	87-90
8221687-7	1993	Aerobically but not hypoxically, MMC reduction by XDH followed Michaelis-Menten kinetics.	Mitomycin	33-36	xanthine dehydrogenase	Homo sapiens	50-53
8221687-9	1993	Stimulation of uric acid formation and decreases in NADH formation by XDH in the presence of MMC suggest that MMC interaction with XDH may occur at the NAD(+)-binding region of the enzyme.	Uric Acid	15-24	xanthine dehydrogenase	Homo sapiens	131-134
8221687-9	1993	Stimulation of uric acid formation and decreases in NADH formation by XDH in the presence of MMC suggest that MMC interaction with XDH may occur at the NAD(+)-binding region of the enzyme.	NAD	52-56	xanthine dehydrogenase	Homo sapiens	70-73
8221687-9	1993	Stimulation of uric acid formation and decreases in NADH formation by XDH in the presence of MMC suggest that MMC interaction with XDH may occur at the NAD(+)-binding region of the enzyme.	NAD	52-56	xanthine dehydrogenase	Homo sapiens	131-134
8221687-9	1993	Stimulation of uric acid formation and decreases in NADH formation by XDH in the presence of MMC suggest that MMC interaction with XDH may occur at the NAD(+)-binding region of the enzyme.	Mitomycin	93-96	xanthine dehydrogenase	Homo sapiens	131-134
8221687-9	1993	Stimulation of uric acid formation and decreases in NADH formation by XDH in the presence of MMC suggest that MMC interaction with XDH may occur at the NAD(+)-binding region of the enzyme.	Mitomycin	110-113	xanthine dehydrogenase	Homo sapiens	70-73
8221687-9	1993	Stimulation of uric acid formation and decreases in NADH formation by XDH in the presence of MMC suggest that MMC interaction with XDH may occur at the NAD(+)-binding region of the enzyme.	Mitomycin	110-113	xanthine dehydrogenase	Homo sapiens	131-134
8248161-4	1993	Analysis of potential NAD binding sites suggested a simple hypothesis for the conversion of human XD into the oxygen metabolite forming xanthine oxidase (XO; xanthine:oxygen oxidoreductase, EC 1.1.3.22).	NAD	22-25	xanthine dehydrogenase	Homo sapiens	98-100
8221687-9	1993	Stimulation of uric acid formation and decreases in NADH formation by XDH in the presence of MMC suggest that MMC interaction with XDH may occur at the NAD(+)-binding region of the enzyme.	NAD	152-158	xanthine dehydrogenase	Homo sapiens	70-73
8221687-9	1993	Stimulation of uric acid formation and decreases in NADH formation by XDH in the presence of MMC suggest that MMC interaction with XDH may occur at the NAD(+)-binding region of the enzyme.	NAD	152-158	xanthine dehydrogenase	Homo sapiens	131-134
8248161-4	1993	Analysis of potential NAD binding sites suggested a simple hypothesis for the conversion of human XD into the oxygen metabolite forming xanthine oxidase (XO; xanthine:oxygen oxidoreductase, EC 1.1.3.22).	Oxygen	110-116	xanthine dehydrogenase	Homo sapiens	98-100
8248161-6	1993	This RNA exhibited tissue-specific distribution that may be pertinent to XD- and XO-mediated oxygen radical injury in ischemia/reperfusion and inflammation.	Oxygen	93-99	xanthine dehydrogenase	Homo sapiens	73-75
8287417-10	1993	Apparent xanthine oxidoreductase was calculated as xanthine +2 x urate production.	Uric Acid	65-70	xanthine dehydrogenase	Homo sapiens	9-32
8123198-4	1993	A mechanism for ethanol-dependent liver damage is proposed which involves the CYP2E1-dependent lipid peroxide formation, either directly by its capability to induce NADPH-dependent peroxidation in the microsomal membranes or indirectly by a hypoxia-mediated transformation of xanthine dehydrogenase to xanthine oxidase, in activation of Ito cells and Kupffer cells to yield cytokine and collagen production.	Ethanol	16-23	xanthine dehydrogenase	Homo sapiens	276-298
8123198-4	1993	A mechanism for ethanol-dependent liver damage is proposed which involves the CYP2E1-dependent lipid peroxide formation, either directly by its capability to induce NADPH-dependent peroxidation in the microsomal membranes or indirectly by a hypoxia-mediated transformation of xanthine dehydrogenase to xanthine oxidase, in activation of Ito cells and Kupffer cells to yield cytokine and collagen production.	Lipid Peroxides	95-109	xanthine dehydrogenase	Homo sapiens	276-298
8344756-5	1993	Cytotoxic and biochemical effects of TR were enhanced by combining it with allopurinol (an inhibitor of xanthine dehydrogenase), and hypoxanthine (an alternate substrate for hypoxanthine-guanine phosphoribosyltransferase).	Allopurinol	75-86	xanthine dehydrogenase	Homo sapiens	104-126
1328233-1	1992	Milk xanthine oxidase (XO) has been prepared in a dehydrogenase form (XDH) by purifying the enzyme in the presence of 2.5 mM dithiothreitol.	Dithiothreitol	125-139	xanthine dehydrogenase	Homo sapiens	70-73
8439471-2	1993	Children and infants may present chronically with stones or acutely with renal failure from crystal nephropathy, as a result of inherited deficiencies of the purine salvage enzymes hypoxanthine-guanine phosphoribosyltransferase (HPRT) and adenine phosphoribosyltransferase (APRT) or of the catabolic enzyme xanthine dehydrogenase (XDH).	purine	158-164	xanthine dehydrogenase	Homo sapiens	307-329
8439471-2	1993	Children and infants may present chronically with stones or acutely with renal failure from crystal nephropathy, as a result of inherited deficiencies of the purine salvage enzymes hypoxanthine-guanine phosphoribosyltransferase (HPRT) and adenine phosphoribosyltransferase (APRT) or of the catabolic enzyme xanthine dehydrogenase (XDH).	purine	158-164	xanthine dehydrogenase	Homo sapiens	331-334
1281039-0	1992	Enhancement of xanthine dehydrogenase mediated mitomycin C metabolism by dicumarol.	Mitomycin	47-58	xanthine dehydrogenase	Homo sapiens	15-37
1281039-0	1992	Enhancement of xanthine dehydrogenase mediated mitomycin C metabolism by dicumarol.	Dicumarol	73-82	xanthine dehydrogenase	Homo sapiens	15-37
1281039-1	1992	These studies examined the effect of dicumarol on xanthine dehydrogenase (XDH), an enzyme recently shown to bioreduce mitomycin C.	Dicumarol	37-46	xanthine dehydrogenase	Homo sapiens	50-72
1281039-1	1992	These studies examined the effect of dicumarol on xanthine dehydrogenase (XDH), an enzyme recently shown to bioreduce mitomycin C.	Dicumarol	37-46	xanthine dehydrogenase	Homo sapiens	74-77
1281039-1	1992	These studies examined the effect of dicumarol on xanthine dehydrogenase (XDH), an enzyme recently shown to bioreduce mitomycin C.	Mitomycin	118-129	xanthine dehydrogenase	Homo sapiens	50-72
1281039-1	1992	These studies examined the effect of dicumarol on xanthine dehydrogenase (XDH), an enzyme recently shown to bioreduce mitomycin C.	Mitomycin	118-129	xanthine dehydrogenase	Homo sapiens	74-77
1281039-2	1992	Dicumarol, which has previously been shown to inhibit xanthine oxidase (XO), inhibited both XDH and XO mediated conversion of xanthine to uric acid but potentiated the metabolism of mitomycin C by XDH and XO.	Dicumarol	0-9	xanthine dehydrogenase	Homo sapiens	92-95
1281039-2	1992	Dicumarol, which has previously been shown to inhibit xanthine oxidase (XO), inhibited both XDH and XO mediated conversion of xanthine to uric acid but potentiated the metabolism of mitomycin C by XDH and XO.	Dicumarol	0-9	xanthine dehydrogenase	Homo sapiens	197-200
1281039-2	1992	Dicumarol, which has previously been shown to inhibit xanthine oxidase (XO), inhibited both XDH and XO mediated conversion of xanthine to uric acid but potentiated the metabolism of mitomycin C by XDH and XO.	Xanthine	54-62	xanthine dehydrogenase	Homo sapiens	92-95
1281039-2	1992	Dicumarol, which has previously been shown to inhibit xanthine oxidase (XO), inhibited both XDH and XO mediated conversion of xanthine to uric acid but potentiated the metabolism of mitomycin C by XDH and XO.	Uric Acid	138-147	xanthine dehydrogenase	Homo sapiens	92-95
1281039-2	1992	Dicumarol, which has previously been shown to inhibit xanthine oxidase (XO), inhibited both XDH and XO mediated conversion of xanthine to uric acid but potentiated the metabolism of mitomycin C by XDH and XO.	Mitomycin	182-193	xanthine dehydrogenase	Homo sapiens	197-200
1281039-3	1992	Formation of 2,7-diaminomitosene following mitomycin C bioactivation by XDH was increased 3-fold aerobically and 4-fold hypoxically when 20 microM dicumarol was included in the reaction mixture.	2,7-diaminomitosene	13-32	xanthine dehydrogenase	Homo sapiens	72-75
1281039-3	1992	Formation of 2,7-diaminomitosene following mitomycin C bioactivation by XDH was increased 3-fold aerobically and 4-fold hypoxically when 20 microM dicumarol was included in the reaction mixture.	Mitomycin	43-54	xanthine dehydrogenase	Homo sapiens	72-75
1281039-3	1992	Formation of 2,7-diaminomitosene following mitomycin C bioactivation by XDH was increased 3-fold aerobically and 4-fold hypoxically when 20 microM dicumarol was included in the reaction mixture.	Dicumarol	147-156	xanthine dehydrogenase	Homo sapiens	72-75
1328233-6	1992	XDH can be converted back to the XO form by the addition of three to four equivalents of the disulfide-forming reagent 4,4"-dithiodipyridine, suggesting that, in the XDH form of the enzyme, disulfide bonds are broken; this may cause a conformational change which creates a binding site for NAD and changes the protein structure near the flavin.	Disulfides	190-199	xanthine dehydrogenase	Homo sapiens	166-169
1328233-6	1992	XDH can be converted back to the XO form by the addition of three to four equivalents of the disulfide-forming reagent 4,4"-dithiodipyridine, suggesting that, in the XDH form of the enzyme, disulfide bonds are broken; this may cause a conformational change which creates a binding site for NAD and changes the protein structure near the flavin.	NAD	290-293	xanthine dehydrogenase	Homo sapiens	0-3
1328233-6	1992	XDH can be converted back to the XO form by the addition of three to four equivalents of the disulfide-forming reagent 4,4"-dithiodipyridine, suggesting that, in the XDH form of the enzyme, disulfide bonds are broken; this may cause a conformational change which creates a binding site for NAD and changes the protein structure near the flavin.	NAD	290-293	xanthine dehydrogenase	Homo sapiens	166-169
1328233-6	1992	XDH can be converted back to the XO form by the addition of three to four equivalents of the disulfide-forming reagent 4,4"-dithiodipyridine, suggesting that, in the XDH form of the enzyme, disulfide bonds are broken; this may cause a conformational change which creates a binding site for NAD and changes the protein structure near the flavin.	4,6-dinitro-o-cresol	337-343	xanthine dehydrogenase	Homo sapiens	0-3
1328233-6	1992	XDH can be converted back to the XO form by the addition of three to four equivalents of the disulfide-forming reagent 4,4"-dithiodipyridine, suggesting that, in the XDH form of the enzyme, disulfide bonds are broken; this may cause a conformational change which creates a binding site for NAD and changes the protein structure near the flavin.	4,6-dinitro-o-cresol	337-343	xanthine dehydrogenase	Homo sapiens	166-169
1328233-2	1992	Unlike XO, which reacts rapidly only with oxygen and not with NAD, the XDH form of the enzyme reacts rapidly with NAD.	Oxygen	42-48	xanthine dehydrogenase	Homo sapiens	71-74
1328233-2	1992	Unlike XO, which reacts rapidly only with oxygen and not with NAD, the XDH form of the enzyme reacts rapidly with NAD.	NAD	114-117	xanthine dehydrogenase	Homo sapiens	71-74
1328233-3	1992	XDH has a turnover number for the NAD-dependent conversion of xanthine to urate of 380 mol/min/mol at pH 7.5, 25 degrees C, with a Km = < or = 1 microM for xanthine and a Km = 7 microM for NAD, but has very little O2-dependent activity.	NAD	34-37	xanthine dehydrogenase	Homo sapiens	0-3
1328233-3	1992	XDH has a turnover number for the NAD-dependent conversion of xanthine to urate of 380 mol/min/mol at pH 7.5, 25 degrees C, with a Km = < or = 1 microM for xanthine and a Km = 7 microM for NAD, but has very little O2-dependent activity.	Xanthine	62-70	xanthine dehydrogenase	Homo sapiens	0-3
1328233-3	1992	XDH has a turnover number for the NAD-dependent conversion of xanthine to urate of 380 mol/min/mol at pH 7.5, 25 degrees C, with a Km = < or = 1 microM for xanthine and a Km = 7 microM for NAD, but has very little O2-dependent activity.	Uric Acid	74-79	xanthine dehydrogenase	Homo sapiens	0-3
1328233-3	1992	XDH has a turnover number for the NAD-dependent conversion of xanthine to urate of 380 mol/min/mol at pH 7.5, 25 degrees C, with a Km = < or = 1 microM for xanthine and a Km = 7 microM for NAD, but has very little O2-dependent activity.	Xanthine	159-167	xanthine dehydrogenase	Homo sapiens	0-3
1328233-3	1992	XDH has a turnover number for the NAD-dependent conversion of xanthine to urate of 380 mol/min/mol at pH 7.5, 25 degrees C, with a Km = < or = 1 microM for xanthine and a Km = 7 microM for NAD, but has very little O2-dependent activity.	NAD	192-195	xanthine dehydrogenase	Homo sapiens	0-3
1328233-3	1992	XDH has a turnover number for the NAD-dependent conversion of xanthine to urate of 380 mol/min/mol at pH 7.5, 25 degrees C, with a Km = < or = 1 microM for xanthine and a Km = 7 microM for NAD, but has very little O2-dependent activity.	Oxygen	217-219	xanthine dehydrogenase	Homo sapiens	0-3
1328233-4	1992	There is evidence that the two forms of the enzyme have different flavin environments: XDH stabilizes the neutral form of the flavin semiquinone and XO does not.	4,6-dinitro-o-cresol	66-72	xanthine dehydrogenase	Homo sapiens	87-90
1328233-4	1992	There is evidence that the two forms of the enzyme have different flavin environments: XDH stabilizes the neutral form of the flavin semiquinone and XO does not.	flavin semiquinone	126-144	xanthine dehydrogenase	Homo sapiens	87-90
1328233-5	1992	Further, XDH binds the artificial flavin 8-mercapto-FAD in its neutral form, shifting the pK of this flavin by 5 pH units, while XO binds 8-mercapto-FAD in its benzoquinoid anionic form.	4,6-dinitro-o-cresol	34-40	xanthine dehydrogenase	Homo sapiens	9-12
1328233-5	1992	Further, XDH binds the artificial flavin 8-mercapto-FAD in its neutral form, shifting the pK of this flavin by 5 pH units, while XO binds 8-mercapto-FAD in its benzoquinoid anionic form.	8-mercapto-FAD	41-55	xanthine dehydrogenase	Homo sapiens	9-12
1328233-5	1992	Further, XDH binds the artificial flavin 8-mercapto-FAD in its neutral form, shifting the pK of this flavin by 5 pH units, while XO binds 8-mercapto-FAD in its benzoquinoid anionic form.	4,6-dinitro-o-cresol	101-107	xanthine dehydrogenase	Homo sapiens	9-12
1328233-5	1992	Further, XDH binds the artificial flavin 8-mercapto-FAD in its neutral form, shifting the pK of this flavin by 5 pH units, while XO binds 8-mercapto-FAD in its benzoquinoid anionic form.	8-mercapto-FAD	138-152	xanthine dehydrogenase	Homo sapiens	9-12
1328233-5	1992	Further, XDH binds the artificial flavin 8-mercapto-FAD in its neutral form, shifting the pK of this flavin by 5 pH units, while XO binds 8-mercapto-FAD in its benzoquinoid anionic form.	benzoquinoid	160-172	xanthine dehydrogenase	Homo sapiens	9-12
1328233-6	1992	XDH can be converted back to the XO form by the addition of three to four equivalents of the disulfide-forming reagent 4,4"-dithiodipyridine, suggesting that, in the XDH form of the enzyme, disulfide bonds are broken; this may cause a conformational change which creates a binding site for NAD and changes the protein structure near the flavin.	Disulfides	93-102	xanthine dehydrogenase	Homo sapiens	0-3
1328233-6	1992	XDH can be converted back to the XO form by the addition of three to four equivalents of the disulfide-forming reagent 4,4"-dithiodipyridine, suggesting that, in the XDH form of the enzyme, disulfide bonds are broken; this may cause a conformational change which creates a binding site for NAD and changes the protein structure near the flavin.	Disulfides	93-102	xanthine dehydrogenase	Homo sapiens	166-169
1328233-6	1992	XDH can be converted back to the XO form by the addition of three to four equivalents of the disulfide-forming reagent 4,4"-dithiodipyridine, suggesting that, in the XDH form of the enzyme, disulfide bonds are broken; this may cause a conformational change which creates a binding site for NAD and changes the protein structure near the flavin.	4,4'-dipyridyl disulfide	119-140	xanthine dehydrogenase	Homo sapiens	0-3
1328233-6	1992	XDH can be converted back to the XO form by the addition of three to four equivalents of the disulfide-forming reagent 4,4"-dithiodipyridine, suggesting that, in the XDH form of the enzyme, disulfide bonds are broken; this may cause a conformational change which creates a binding site for NAD and changes the protein structure near the flavin.	4,4'-dipyridyl disulfide	119-140	xanthine dehydrogenase	Homo sapiens	166-169
1328233-6	1992	XDH can be converted back to the XO form by the addition of three to four equivalents of the disulfide-forming reagent 4,4"-dithiodipyridine, suggesting that, in the XDH form of the enzyme, disulfide bonds are broken; this may cause a conformational change which creates a binding site for NAD and changes the protein structure near the flavin.	Disulfides	190-199	xanthine dehydrogenase	Homo sapiens	0-3
1314387-1	1992	Exposure to decreasing oxygen tensions progressively increased xanthine dehydrogenase (XD) and xanthine oxidase (XO) activities over 48 hr in cultured pulmonary artery endothelial cells (EC) without altering XD/XO ratios.	Oxygen	23-29	xanthine dehydrogenase	Homo sapiens	63-85
1616255-4	1992	During ischaemia, adenosine triphosphate (ATP) is converted to hypoxanthine and xanthine, and endothelial xanthine dehydrogenase to xanthine oxidase (alcohol also mediates this change, a finding of particular relevance given the association of Dupuytren"s contracture with alcohol intake).	Alcohols	150-157	xanthine dehydrogenase	Homo sapiens	106-128
1616255-4	1992	During ischaemia, adenosine triphosphate (ATP) is converted to hypoxanthine and xanthine, and endothelial xanthine dehydrogenase to xanthine oxidase (alcohol also mediates this change, a finding of particular relevance given the association of Dupuytren"s contracture with alcohol intake).	Alcohols	273-280	xanthine dehydrogenase	Homo sapiens	106-128
1314387-1	1992	Exposure to decreasing oxygen tensions progressively increased xanthine dehydrogenase (XD) and xanthine oxidase (XO) activities over 48 hr in cultured pulmonary artery endothelial cells (EC) without altering XD/XO ratios.	Oxygen	23-29	xanthine dehydrogenase	Homo sapiens	87-89
1314387-2	1992	Increases in XD and XO activity in EC induced by hypoxia were associated upon reoxygenation with increased (P less than 0.05) extracellular superoxide anion (O2-.)	Superoxides	140-156	xanthine dehydrogenase	Homo sapiens	13-15
1314387-2	1992	Increases in XD and XO activity in EC induced by hypoxia were associated upon reoxygenation with increased (P less than 0.05) extracellular superoxide anion (O2-.)	Oxygen	158-160	xanthine dehydrogenase	Homo sapiens	13-15
1540391-2	1992	The elastase inhibitors, elastatinal, alpha 1-antitrypsin, and MeO-Suc-(Ala)2-Pro-Val-CH2Cl, significantly inhibited xanthine dehydrogenase to oxidase conversion by phorbol myristate acetate-stimulated neutrophils without inhibition of neutrophil adherence to the endothelial cell monolayer.	Tetradecanoylphorbol Acetate	165-190	xanthine dehydrogenase	Homo sapiens	117-139
1551461-0	1992	Involvement of histidine residues in catalytic activity of xanthine dehydrogenase from hen liver.	Histidine	15-24	xanthine dehydrogenase	Homo sapiens	59-81
1551461-2	1992	Modification of histidine residue(s) of xanthine dehydrogenase from hen liver by DEP and photooxidation results in loss of the ability to transfer electrons from xanthine to NAD+ and also from NADH to 2,6-dichlorophenolindophenol (DCIP).	Histidine	16-25	xanthine dehydrogenase	Homo sapiens	40-62
1551461-2	1992	Modification of histidine residue(s) of xanthine dehydrogenase from hen liver by DEP and photooxidation results in loss of the ability to transfer electrons from xanthine to NAD+ and also from NADH to 2,6-dichlorophenolindophenol (DCIP).	NAD	174-178	xanthine dehydrogenase	Homo sapiens	40-62
1551461-2	1992	Modification of histidine residue(s) of xanthine dehydrogenase from hen liver by DEP and photooxidation results in loss of the ability to transfer electrons from xanthine to NAD+ and also from NADH to 2,6-dichlorophenolindophenol (DCIP).	NAD	193-197	xanthine dehydrogenase	Homo sapiens	40-62
1551461-2	1992	Modification of histidine residue(s) of xanthine dehydrogenase from hen liver by DEP and photooxidation results in loss of the ability to transfer electrons from xanthine to NAD+ and also from NADH to 2,6-dichlorophenolindophenol (DCIP).	2,6-Dichloroindophenol	201-229	xanthine dehydrogenase	Homo sapiens	40-62
1551461-2	1992	Modification of histidine residue(s) of xanthine dehydrogenase from hen liver by DEP and photooxidation results in loss of the ability to transfer electrons from xanthine to NAD+ and also from NADH to 2,6-dichlorophenolindophenol (DCIP).	2,6-Dichloroindophenol	231-235	xanthine dehydrogenase	Homo sapiens	40-62
1362018-1	1992	Localization of the activity of both the dehydrogenase and oxidase forms of xanthine oxidoreductase were studied in biopsy and postmortem specimens of various human tissues with a recently developed histochemical method using unfixed cryostat sections, poly-(vinyl alcohol) as tissue stabilizator, 1-methoxyphenazine methosulphate as intermediate electron acceptor and Tetranitro BT as final electron acceptor.	tetranitrotetrazolium blue	369-382	xanthine dehydrogenase	Homo sapiens	76-99
1502213-0	1992	Oxygen radical generation and alkylating ability of mitomycin C bioactivated by xanthine dehydrogenase.	Reactive Oxygen Species	0-14	xanthine dehydrogenase	Homo sapiens	80-102
1502213-0	1992	Oxygen radical generation and alkylating ability of mitomycin C bioactivated by xanthine dehydrogenase.	Mitomycin	52-63	xanthine dehydrogenase	Homo sapiens	80-102
1362018-1	1992	Localization of the activity of both the dehydrogenase and oxidase forms of xanthine oxidoreductase were studied in biopsy and postmortem specimens of various human tissues with a recently developed histochemical method using unfixed cryostat sections, poly-(vinyl alcohol) as tissue stabilizator, 1-methoxyphenazine methosulphate as intermediate electron acceptor and Tetranitro BT as final electron acceptor.	Polyvinyl Alcohol	253-273	xanthine dehydrogenase	Homo sapiens	76-99
1362018-1	1992	Localization of the activity of both the dehydrogenase and oxidase forms of xanthine oxidoreductase were studied in biopsy and postmortem specimens of various human tissues with a recently developed histochemical method using unfixed cryostat sections, poly-(vinyl alcohol) as tissue stabilizator, 1-methoxyphenazine methosulphate as intermediate electron acceptor and Tetranitro BT as final electron acceptor.	1-methoxyphenazine methosulphate	298-330	xanthine dehydrogenase	Homo sapiens	76-99
1680657-10	1991	Both the xanthine dehydrogenase/oxidase and azoxy procarbazine oxidase activities of this protein fraction were inhibited by allopurinol, a specific inhibitor of xanthine dehydrogenase.	Allopurinol	125-136	xanthine dehydrogenase	Homo sapiens	9-39
1680657-11	1991	Xanthine dehydrogenase/oxidase was partially purified by an alternative procedure and was shown to metabolize both the azoxy 2 procarbazine isomer and ALD, ultimately producing N-isopropylterephthalamic acid.	methylazoxyprocarbazine	119-139	xanthine dehydrogenase	Homo sapiens	0-30
1680657-11	1991	Xanthine dehydrogenase/oxidase was partially purified by an alternative procedure and was shown to metabolize both the azoxy 2 procarbazine isomer and ALD, ultimately producing N-isopropylterephthalamic acid.	N-isopropylterephthalamic acid	177-207	xanthine dehydrogenase	Homo sapiens	0-30
1789243-0	1991	Lower xanthine oxidoreductase activity in isolated perfused hearts if xanthine replaces hypoxanthine as substrate.	Hypoxanthine	88-100	xanthine dehydrogenase	Homo sapiens	6-29
2087924-2	1990	These aspects exemplified by xanthine oxidoreductase from vertebrates of various type of nitrogen excretion are discussed.	Nitrogen	89-97	xanthine dehydrogenase	Homo sapiens	29-52
2021865-1	1991	Xanthine oxidase is the pathological form of xanthine oxidoreductase, which generates free oxygen radicals, when it converts (hypo)xanthine to urate.	free oxygen radicals	86-106	xanthine dehydrogenase	Homo sapiens	45-68
2021865-1	1991	Xanthine oxidase is the pathological form of xanthine oxidoreductase, which generates free oxygen radicals, when it converts (hypo)xanthine to urate.	Hypoxanthine	125-139	xanthine dehydrogenase	Homo sapiens	45-68
2021865-1	1991	Xanthine oxidase is the pathological form of xanthine oxidoreductase, which generates free oxygen radicals, when it converts (hypo)xanthine to urate.	Uric Acid	143-148	xanthine dehydrogenase	Homo sapiens	45-68
2374259-4	1990	In addition, we studied the rate of conversion of xanthine dehydrogenase to xanthine oxidase, a potential source of oxygen-free radicals, after controlled periods of total normothermic ischemia (4 hours and 5 hours) and during the reperfusion phase.	oxygen-free radicals	116-136	xanthine dehydrogenase	Homo sapiens	50-72
34496841-1	2021	BACKGROUND: Xanthine dehydrogenase (XDH) is a critical enzyme involved in the oxidative metabolism of purines, pterin and aldehydes and a central component of the innate immune system.	Purines	102-109	xanthine dehydrogenase	Homo sapiens	12-34
34884248-1	2021	Xanthine oxidoreductase (XOR) is the rate-limiting enzyme in uric acid (UA) production that plays a pivotal role in generating oxidative stress.	Uric Acid	61-70	xanthine dehydrogenase	Homo sapiens	0-23
34884248-1	2021	Xanthine oxidoreductase (XOR) is the rate-limiting enzyme in uric acid (UA) production that plays a pivotal role in generating oxidative stress.	Uric Acid	61-70	xanthine dehydrogenase	Homo sapiens	25-28
34884248-1	2021	Xanthine oxidoreductase (XOR) is the rate-limiting enzyme in uric acid (UA) production that plays a pivotal role in generating oxidative stress.	Uric Acid	72-74	xanthine dehydrogenase	Homo sapiens	0-23
34884248-1	2021	Xanthine oxidoreductase (XOR) is the rate-limiting enzyme in uric acid (UA) production that plays a pivotal role in generating oxidative stress.	Uric Acid	72-74	xanthine dehydrogenase	Homo sapiens	25-28
34884248-3	2021	We investigated plasma XOR activity in 132 patients suspected of having CAS (male, n = 78; female, n = 54) and who underwent an intracoronary acetylcholine provocation test.	Acetylcholine	142-155	xanthine dehydrogenase	Homo sapiens	23-26
34829959-1	2021	Xanthine oxidoreductase (XOR) is an enzyme that catalyzes the two-step reaction from hypoxanthine to xanthine and from xanthine to uric acid in purine metabolism.	Hypoxanthine	85-97	xanthine dehydrogenase	Homo sapiens	0-23
34829959-1	2021	Xanthine oxidoreductase (XOR) is an enzyme that catalyzes the two-step reaction from hypoxanthine to xanthine and from xanthine to uric acid in purine metabolism.	Hypoxanthine	85-97	xanthine dehydrogenase	Homo sapiens	25-28
34829959-1	2021	Xanthine oxidoreductase (XOR) is an enzyme that catalyzes the two-step reaction from hypoxanthine to xanthine and from xanthine to uric acid in purine metabolism.	Xanthine	101-109	xanthine dehydrogenase	Homo sapiens	0-23
34829959-1	2021	Xanthine oxidoreductase (XOR) is an enzyme that catalyzes the two-step reaction from hypoxanthine to xanthine and from xanthine to uric acid in purine metabolism.	Xanthine	101-109	xanthine dehydrogenase	Homo sapiens	25-28
34829959-1	2021	Xanthine oxidoreductase (XOR) is an enzyme that catalyzes the two-step reaction from hypoxanthine to xanthine and from xanthine to uric acid in purine metabolism.	Xanthine	119-127	xanthine dehydrogenase	Homo sapiens	0-23
34829959-1	2021	Xanthine oxidoreductase (XOR) is an enzyme that catalyzes the two-step reaction from hypoxanthine to xanthine and from xanthine to uric acid in purine metabolism.	Xanthine	119-127	xanthine dehydrogenase	Homo sapiens	25-28
34829959-1	2021	Xanthine oxidoreductase (XOR) is an enzyme that catalyzes the two-step reaction from hypoxanthine to xanthine and from xanthine to uric acid in purine metabolism.	Uric Acid	131-140	xanthine dehydrogenase	Homo sapiens	0-23
34829959-1	2021	Xanthine oxidoreductase (XOR) is an enzyme that catalyzes the two-step reaction from hypoxanthine to xanthine and from xanthine to uric acid in purine metabolism.	Uric Acid	131-140	xanthine dehydrogenase	Homo sapiens	25-28
34829959-1	2021	Xanthine oxidoreductase (XOR) is an enzyme that catalyzes the two-step reaction from hypoxanthine to xanthine and from xanthine to uric acid in purine metabolism.	purine	144-150	xanthine dehydrogenase	Homo sapiens	0-23
34829959-1	2021	Xanthine oxidoreductase (XOR) is an enzyme that catalyzes the two-step reaction from hypoxanthine to xanthine and from xanthine to uric acid in purine metabolism.	purine	144-150	xanthine dehydrogenase	Homo sapiens	25-28
34829959-4	2021	Three XOR inhibitors are currently used as hyperuricemia and gout therapeutics but are also expected to have potential effects other than uric acid reduction, such as suppressing XO-generating reactive oxygen species.	Uric Acid	138-147	xanthine dehydrogenase	Homo sapiens	6-9
34829959-4	2021	Three XOR inhibitors are currently used as hyperuricemia and gout therapeutics but are also expected to have potential effects other than uric acid reduction, such as suppressing XO-generating reactive oxygen species.	Oxygen	202-208	xanthine dehydrogenase	Homo sapiens	6-9
34619144-3	2022	Xanthine oxidoreductase (XOR) is an enzyme that catalyzes the oxidation of hypoxanthine to xanthine and xanthine to uric acid and is related to oxidative stress.	Hypoxanthine	75-87	xanthine dehydrogenase	Homo sapiens	0-23
34619144-3	2022	Xanthine oxidoreductase (XOR) is an enzyme that catalyzes the oxidation of hypoxanthine to xanthine and xanthine to uric acid and is related to oxidative stress.	Hypoxanthine	75-87	xanthine dehydrogenase	Homo sapiens	25-28
34619144-3	2022	Xanthine oxidoreductase (XOR) is an enzyme that catalyzes the oxidation of hypoxanthine to xanthine and xanthine to uric acid and is related to oxidative stress.	Xanthine	91-99	xanthine dehydrogenase	Homo sapiens	0-23
34619144-3	2022	Xanthine oxidoreductase (XOR) is an enzyme that catalyzes the oxidation of hypoxanthine to xanthine and xanthine to uric acid and is related to oxidative stress.	Xanthine	91-99	xanthine dehydrogenase	Homo sapiens	25-28
34619144-3	2022	Xanthine oxidoreductase (XOR) is an enzyme that catalyzes the oxidation of hypoxanthine to xanthine and xanthine to uric acid and is related to oxidative stress.	Xanthine	104-112	xanthine dehydrogenase	Homo sapiens	0-23
34619144-3	2022	Xanthine oxidoreductase (XOR) is an enzyme that catalyzes the oxidation of hypoxanthine to xanthine and xanthine to uric acid and is related to oxidative stress.	Xanthine	104-112	xanthine dehydrogenase	Homo sapiens	25-28
34619144-3	2022	Xanthine oxidoreductase (XOR) is an enzyme that catalyzes the oxidation of hypoxanthine to xanthine and xanthine to uric acid and is related to oxidative stress.	Uric Acid	116-125	xanthine dehydrogenase	Homo sapiens	0-23
34619144-3	2022	Xanthine oxidoreductase (XOR) is an enzyme that catalyzes the oxidation of hypoxanthine to xanthine and xanthine to uric acid and is related to oxidative stress.	Uric Acid	116-125	xanthine dehydrogenase	Homo sapiens	25-28
34273539-2	2021	Of these enzymes, XOR has been the most extensively studied and reported to be a substantive source of nitric oxide (NO) under inflammatory/hypoxic conditions that limit the catalytic activity of the canonical NOS pathway.	Nitric Oxide	103-115	xanthine dehydrogenase	Homo sapiens	18-21
33795813-2	2021	This cross-sectional study examined whether uric acid possesses effects on oxidative stress under physiological conditions independent of xanthine oxidoreductase (XOR), which is involved in uric acid and ROS production.	Uric Acid	190-199	xanthine dehydrogenase	Homo sapiens	138-161
33795813-2	2021	This cross-sectional study examined whether uric acid possesses effects on oxidative stress under physiological conditions independent of xanthine oxidoreductase (XOR), which is involved in uric acid and ROS production.	Uric Acid	190-199	xanthine dehydrogenase	Homo sapiens	163-166
33795813-2	2021	This cross-sectional study examined whether uric acid possesses effects on oxidative stress under physiological conditions independent of xanthine oxidoreductase (XOR), which is involved in uric acid and ROS production.	Reactive Oxygen Species	204-207	xanthine dehydrogenase	Homo sapiens	138-161
33795813-2	2021	This cross-sectional study examined whether uric acid possesses effects on oxidative stress under physiological conditions independent of xanthine oxidoreductase (XOR), which is involved in uric acid and ROS production.	Reactive Oxygen Species	204-207	xanthine dehydrogenase	Homo sapiens	163-166
34844041-7	2021	The inhibition of XOR activity appears more promising than just the control of uricemia level in preventing cardiovascular events, possibly because it also reduces the intracellular accumulation of urate, as well as the production of reactive oxygen species.	Uric Acid	198-203	xanthine dehydrogenase	Homo sapiens	18-21
34844041-7	2021	The inhibition of XOR activity appears more promising than just the control of uricemia level in preventing cardiovascular events, possibly because it also reduces the intracellular accumulation of urate, as well as the production of reactive oxygen species.	Oxygen	243-249	xanthine dehydrogenase	Homo sapiens	18-21
34844041-8	2021	However, XOR inhibition also reduces the availability of the multifaced mediator nitric oxide and, at present, can be recommended only in hyperuricemic patients.	Nitric Oxide	81-93	xanthine dehydrogenase	Homo sapiens	9-12
34811515-1	2021	Xanthine oxidoreductase (XOR) is a critical, rate-limiting enzyme that controls the last two steps of purine catabolism by converting hypoxanthine to xanthine and xanthine to uric acid.	purine	102-108	xanthine dehydrogenase	Homo sapiens	0-23
34811515-1	2021	Xanthine oxidoreductase (XOR) is a critical, rate-limiting enzyme that controls the last two steps of purine catabolism by converting hypoxanthine to xanthine and xanthine to uric acid.	purine	102-108	xanthine dehydrogenase	Homo sapiens	25-28
34811515-1	2021	Xanthine oxidoreductase (XOR) is a critical, rate-limiting enzyme that controls the last two steps of purine catabolism by converting hypoxanthine to xanthine and xanthine to uric acid.	Hypoxanthine	134-146	xanthine dehydrogenase	Homo sapiens	0-23
34811515-1	2021	Xanthine oxidoreductase (XOR) is a critical, rate-limiting enzyme that controls the last two steps of purine catabolism by converting hypoxanthine to xanthine and xanthine to uric acid.	Hypoxanthine	134-146	xanthine dehydrogenase	Homo sapiens	25-28
34811515-1	2021	Xanthine oxidoreductase (XOR) is a critical, rate-limiting enzyme that controls the last two steps of purine catabolism by converting hypoxanthine to xanthine and xanthine to uric acid.	Xanthine	150-158	xanthine dehydrogenase	Homo sapiens	0-23
34811515-1	2021	Xanthine oxidoreductase (XOR) is a critical, rate-limiting enzyme that controls the last two steps of purine catabolism by converting hypoxanthine to xanthine and xanthine to uric acid.	Xanthine	150-158	xanthine dehydrogenase	Homo sapiens	25-28
34811515-1	2021	Xanthine oxidoreductase (XOR) is a critical, rate-limiting enzyme that controls the last two steps of purine catabolism by converting hypoxanthine to xanthine and xanthine to uric acid.	Xanthine	163-171	xanthine dehydrogenase	Homo sapiens	0-23
34811515-1	2021	Xanthine oxidoreductase (XOR) is a critical, rate-limiting enzyme that controls the last two steps of purine catabolism by converting hypoxanthine to xanthine and xanthine to uric acid.	Xanthine	163-171	xanthine dehydrogenase	Homo sapiens	25-28
34811515-1	2021	Xanthine oxidoreductase (XOR) is a critical, rate-limiting enzyme that controls the last two steps of purine catabolism by converting hypoxanthine to xanthine and xanthine to uric acid.	Uric Acid	175-184	xanthine dehydrogenase	Homo sapiens	0-23
34811515-1	2021	Xanthine oxidoreductase (XOR) is a critical, rate-limiting enzyme that controls the last two steps of purine catabolism by converting hypoxanthine to xanthine and xanthine to uric acid.	Uric Acid	175-184	xanthine dehydrogenase	Homo sapiens	25-28
34626042-1	2022	INTRODUCTION: Xanthine oxidoreductase (XOR) is known as an enzyme related to purine metabolism, catalyzing the oxidation of hypoxanthine to xanthine and of xanthine to uric acid.	purine	77-83	xanthine dehydrogenase	Homo sapiens	14-37
34626042-1	2022	INTRODUCTION: Xanthine oxidoreductase (XOR) is known as an enzyme related to purine metabolism, catalyzing the oxidation of hypoxanthine to xanthine and of xanthine to uric acid.	purine	77-83	xanthine dehydrogenase	Homo sapiens	39-42
34626042-1	2022	INTRODUCTION: Xanthine oxidoreductase (XOR) is known as an enzyme related to purine metabolism, catalyzing the oxidation of hypoxanthine to xanthine and of xanthine to uric acid.	Hypoxanthine	124-136	xanthine dehydrogenase	Homo sapiens	14-37
34626042-1	2022	INTRODUCTION: Xanthine oxidoreductase (XOR) is known as an enzyme related to purine metabolism, catalyzing the oxidation of hypoxanthine to xanthine and of xanthine to uric acid.	Hypoxanthine	124-136	xanthine dehydrogenase	Homo sapiens	39-42
34626042-1	2022	INTRODUCTION: Xanthine oxidoreductase (XOR) is known as an enzyme related to purine metabolism, catalyzing the oxidation of hypoxanthine to xanthine and of xanthine to uric acid.	Xanthine	140-148	xanthine dehydrogenase	Homo sapiens	14-37
34626042-1	2022	INTRODUCTION: Xanthine oxidoreductase (XOR) is known as an enzyme related to purine metabolism, catalyzing the oxidation of hypoxanthine to xanthine and of xanthine to uric acid.	Xanthine	140-148	xanthine dehydrogenase	Homo sapiens	39-42
34626042-1	2022	INTRODUCTION: Xanthine oxidoreductase (XOR) is known as an enzyme related to purine metabolism, catalyzing the oxidation of hypoxanthine to xanthine and of xanthine to uric acid.	Xanthine	156-164	xanthine dehydrogenase	Homo sapiens	14-37
34626042-1	2022	INTRODUCTION: Xanthine oxidoreductase (XOR) is known as an enzyme related to purine metabolism, catalyzing the oxidation of hypoxanthine to xanthine and of xanthine to uric acid.	Xanthine	156-164	xanthine dehydrogenase	Homo sapiens	39-42
34626042-1	2022	INTRODUCTION: Xanthine oxidoreductase (XOR) is known as an enzyme related to purine metabolism, catalyzing the oxidation of hypoxanthine to xanthine and of xanthine to uric acid.	Uric Acid	168-177	xanthine dehydrogenase	Homo sapiens	14-37
34626042-1	2022	INTRODUCTION: Xanthine oxidoreductase (XOR) is known as an enzyme related to purine metabolism, catalyzing the oxidation of hypoxanthine to xanthine and of xanthine to uric acid.	Uric Acid	168-177	xanthine dehydrogenase	Homo sapiens	39-42
34520495-1	2021	OBJECTIVES: Reactive oxygen species generated by xanthine oxidoreductase (XOR) are associated with the progression of atherosclerosis.	Oxygen	21-27	xanthine dehydrogenase	Homo sapiens	49-72
34520495-1	2021	OBJECTIVES: Reactive oxygen species generated by xanthine oxidoreductase (XOR) are associated with the progression of atherosclerosis.	Oxygen	21-27	xanthine dehydrogenase	Homo sapiens	74-77
34496841-1	2021	BACKGROUND: Xanthine dehydrogenase (XDH) is a critical enzyme involved in the oxidative metabolism of purines, pterin and aldehydes and a central component of the innate immune system.	Pterins	111-117	xanthine dehydrogenase	Homo sapiens	12-34
34496841-1	2021	BACKGROUND: Xanthine dehydrogenase (XDH) is a critical enzyme involved in the oxidative metabolism of purines, pterin and aldehydes and a central component of the innate immune system.	Pterins	111-117	xanthine dehydrogenase	Homo sapiens	36-39
34496841-1	2021	BACKGROUND: Xanthine dehydrogenase (XDH) is a critical enzyme involved in the oxidative metabolism of purines, pterin and aldehydes and a central component of the innate immune system.	Aldehydes	122-131	xanthine dehydrogenase	Homo sapiens	12-34
34496841-1	2021	BACKGROUND: Xanthine dehydrogenase (XDH) is a critical enzyme involved in the oxidative metabolism of purines, pterin and aldehydes and a central component of the innate immune system.	Aldehydes	122-131	xanthine dehydrogenase	Homo sapiens	36-39
34496841-1	2021	BACKGROUND: Xanthine dehydrogenase (XDH) is a critical enzyme involved in the oxidative metabolism of purines, pterin and aldehydes and a central component of the innate immune system.	Purines	102-109	xanthine dehydrogenase	Homo sapiens	36-39
34171392-1	2021	In addition to its pivotal role in purine metabolism, xanthine oxidoreductase (XOR) is one of the key enzymes involved in superoxide radical generation.	purine	35-41	xanthine dehydrogenase	Homo sapiens	54-77
34171392-1	2021	In addition to its pivotal role in purine metabolism, xanthine oxidoreductase (XOR) is one of the key enzymes involved in superoxide radical generation.	purine	35-41	xanthine dehydrogenase	Homo sapiens	79-82
34171392-1	2021	In addition to its pivotal role in purine metabolism, xanthine oxidoreductase (XOR) is one of the key enzymes involved in superoxide radical generation.	Superoxides	122-132	xanthine dehydrogenase	Homo sapiens	54-77
34171392-7	2021	Mechanistically, TNFalpha may activate XOR transcription via activator protein-1 and, thus, promote endogenous hydrogen peroxide generation, resulting in oxidative DNA damage in colon cancer cells.	Hydrogen Peroxide	111-128	xanthine dehydrogenase	Homo sapiens	39-42
34494551-1	2021	Xanthine oxidoreductase (XOR) is an enzyme that catalyzes hypoxanthine to xanthine and xanthine to uric acid, respectively.	Hypoxanthine	58-70	xanthine dehydrogenase	Homo sapiens	0-23
34171392-1	2021	In addition to its pivotal role in purine metabolism, xanthine oxidoreductase (XOR) is one of the key enzymes involved in superoxide radical generation.	Superoxides	122-132	xanthine dehydrogenase	Homo sapiens	79-82
34494551-1	2021	Xanthine oxidoreductase (XOR) is an enzyme that catalyzes hypoxanthine to xanthine and xanthine to uric acid, respectively.	Hypoxanthine	58-70	xanthine dehydrogenase	Homo sapiens	25-28
34435469-3	2021	Febuxostat and rasburicase reduce the uric acid concentration by xanthine oxidoreductase inhibition and uric acid degradation into allantoin, respectively.	Uric Acid	38-47	xanthine dehydrogenase	Homo sapiens	65-88
34494551-1	2021	Xanthine oxidoreductase (XOR) is an enzyme that catalyzes hypoxanthine to xanthine and xanthine to uric acid, respectively.	Xanthine	74-82	xanthine dehydrogenase	Homo sapiens	0-23
34494551-1	2021	Xanthine oxidoreductase (XOR) is an enzyme that catalyzes hypoxanthine to xanthine and xanthine to uric acid, respectively.	Xanthine	74-82	xanthine dehydrogenase	Homo sapiens	25-28
34494551-1	2021	Xanthine oxidoreductase (XOR) is an enzyme that catalyzes hypoxanthine to xanthine and xanthine to uric acid, respectively.	Xanthine	87-95	xanthine dehydrogenase	Homo sapiens	0-23
34494551-1	2021	Xanthine oxidoreductase (XOR) is an enzyme that catalyzes hypoxanthine to xanthine and xanthine to uric acid, respectively.	Xanthine	87-95	xanthine dehydrogenase	Homo sapiens	25-28
34494551-1	2021	Xanthine oxidoreductase (XOR) is an enzyme that catalyzes hypoxanthine to xanthine and xanthine to uric acid, respectively.	Uric Acid	99-108	xanthine dehydrogenase	Homo sapiens	0-23
34494551-1	2021	Xanthine oxidoreductase (XOR) is an enzyme that catalyzes hypoxanthine to xanthine and xanthine to uric acid, respectively.	Uric Acid	99-108	xanthine dehydrogenase	Homo sapiens	25-28
34494551-5	2021	Besides, purine catabolism was accelerated in the plasma per se of NASH mice and human patients with high XOR activity.	purine	9-15	xanthine dehydrogenase	Homo sapiens	106-109
34494551-7	2021	In vitro, human liver S9-derived XOR promoted proliferation of SMCs with phenotypic modulation and induced ROS production by catabolizing hypoxanthine released from human endothelial cells.	ros	107-110	xanthine dehydrogenase	Homo sapiens	33-36
34494551-7	2021	In vitro, human liver S9-derived XOR promoted proliferation of SMCs with phenotypic modulation and induced ROS production by catabolizing hypoxanthine released from human endothelial cells.	Hypoxanthine	138-150	xanthine dehydrogenase	Homo sapiens	33-36
34117403-1	2021	Xanthine oxidoreductase (XOR), a rate-limiting and catalyzing enzyme of uric acid formation in purine metabolism, is involved in reactive oxygen species generation.	Uric Acid	72-81	xanthine dehydrogenase	Homo sapiens	0-23
34117403-1	2021	Xanthine oxidoreductase (XOR), a rate-limiting and catalyzing enzyme of uric acid formation in purine metabolism, is involved in reactive oxygen species generation.	Uric Acid	72-81	xanthine dehydrogenase	Homo sapiens	25-28
34117403-1	2021	Xanthine oxidoreductase (XOR), a rate-limiting and catalyzing enzyme of uric acid formation in purine metabolism, is involved in reactive oxygen species generation.	purine	95-101	xanthine dehydrogenase	Homo sapiens	0-23
34117403-1	2021	Xanthine oxidoreductase (XOR), a rate-limiting and catalyzing enzyme of uric acid formation in purine metabolism, is involved in reactive oxygen species generation.	purine	95-101	xanthine dehydrogenase	Homo sapiens	25-28
34117403-1	2021	Xanthine oxidoreductase (XOR), a rate-limiting and catalyzing enzyme of uric acid formation in purine metabolism, is involved in reactive oxygen species generation.	Reactive Oxygen Species	129-152	xanthine dehydrogenase	Homo sapiens	0-23
34117403-1	2021	Xanthine oxidoreductase (XOR), a rate-limiting and catalyzing enzyme of uric acid formation in purine metabolism, is involved in reactive oxygen species generation.	Reactive Oxygen Species	129-152	xanthine dehydrogenase	Homo sapiens	25-28
34117403-9	2021	Multivariable logistic regression analysis showed that plasma XOR activity (odds ratio: 1.091 (95% confidence interval: 1.023-1.177) per 10 pmol/h/mL, P = 0.007) was an independent determinant of the risk for hypertension after adjustment for age, sex, current smoking and alcohol consumption, estimated glomerular filtration rate, brain natriuretic peptide, and insulin resistance index.	Alcohols	273-280	xanthine dehydrogenase	Homo sapiens	62-65
34434930-11	2021	In summary, we observed an increased serum UA level in the early stage of women"s pregnancy, and proved that the increased level of UA results from the expressed XDH in decidualizing endometrium of both human and mouse, leading to the formation of MSU crystal.	Uric Acid	248-251	xanthine dehydrogenase	Homo sapiens	162-165
34440256-8	2021	The logarithmically transformed plasma XOR activity (ln-XOR) correlated positively with hypoxanthine, xanthine, visceral fatty area, and liver dysfunction but negatively with HDL cholesterol.	Hypoxanthine	88-100	xanthine dehydrogenase	Homo sapiens	39-42
34440256-8	2021	The logarithmically transformed plasma XOR activity (ln-XOR) correlated positively with hypoxanthine, xanthine, visceral fatty area, and liver dysfunction but negatively with HDL cholesterol.	Hypoxanthine	88-100	xanthine dehydrogenase	Homo sapiens	56-59
34440256-8	2021	The logarithmically transformed plasma XOR activity (ln-XOR) correlated positively with hypoxanthine, xanthine, visceral fatty area, and liver dysfunction but negatively with HDL cholesterol.	Xanthine	102-110	xanthine dehydrogenase	Homo sapiens	39-42
34440256-8	2021	The logarithmically transformed plasma XOR activity (ln-XOR) correlated positively with hypoxanthine, xanthine, visceral fatty area, and liver dysfunction but negatively with HDL cholesterol.	Cholesterol	179-190	xanthine dehydrogenase	Homo sapiens	39-42
34451714-5	2021	We found that treatment with Ci, Co, and FSU-CC suppressed the activity of xanthine oxidase and mRNA expression of xanthine dehydrogenase while inducing an increase in the expression levels of the organic anion transporter 1 (OAT1) and organic anion transporter 3 (OAT3) proteins and a decrease in the expression levels of glucose transporter 9 (GLUT9) and urate transporter 1 (URAT1) proteins.	Cobalt	33-35	xanthine dehydrogenase	Homo sapiens	115-137
34451714-5	2021	We found that treatment with Ci, Co, and FSU-CC suppressed the activity of xanthine oxidase and mRNA expression of xanthine dehydrogenase while inducing an increase in the expression levels of the organic anion transporter 1 (OAT1) and organic anion transporter 3 (OAT3) proteins and a decrease in the expression levels of glucose transporter 9 (GLUT9) and urate transporter 1 (URAT1) proteins.	fsu-cc	41-47	xanthine dehydrogenase	Homo sapiens	115-137
34356852-9	2021	As far as we are aware, this is the largest cohort of xanthinuria cases described so far, substantially expanding the repertoire of pathogenic variants, characterizing structurally and functionally essential amino acid residues in the XDH and MOCOS proteins and addressing the population genetic aspects of classical xanthinuria.	Amino Acids, Essential	198-218	xanthine dehydrogenase	Homo sapiens	235-238
34082427-1	2021	INTRODUCTION: Xanthine oxidoreductase (XOR) activity plays an important role as a pivotal source of reactive oxygen species, which is associated with cardiovascular disease (CVD) events.	reactive	100-108	xanthine dehydrogenase	Homo sapiens	14-37
34082427-1	2021	INTRODUCTION: Xanthine oxidoreductase (XOR) activity plays an important role as a pivotal source of reactive oxygen species, which is associated with cardiovascular disease (CVD) events.	reactive	100-108	xanthine dehydrogenase	Homo sapiens	39-42
34082427-1	2021	INTRODUCTION: Xanthine oxidoreductase (XOR) activity plays an important role as a pivotal source of reactive oxygen species, which is associated with cardiovascular disease (CVD) events.	oxygen species	109-123	xanthine dehydrogenase	Homo sapiens	14-37
34082427-1	2021	INTRODUCTION: Xanthine oxidoreductase (XOR) activity plays an important role as a pivotal source of reactive oxygen species, which is associated with cardiovascular disease (CVD) events.	oxygen species	109-123	xanthine dehydrogenase	Homo sapiens	39-42
34082427-5	2021	RESULTS: Plasma glucose, hemoglobin A1c, and estimated glomerular filtration (eGFR) were significantly and positively correlated with plasma logarithmically transformed XOR (ln-XOR) activity.	Glucose	16-23	xanthine dehydrogenase	Homo sapiens	169-172
34082427-5	2021	RESULTS: Plasma glucose, hemoglobin A1c, and estimated glomerular filtration (eGFR) were significantly and positively correlated with plasma logarithmically transformed XOR (ln-XOR) activity.	Glucose	16-23	xanthine dehydrogenase	Homo sapiens	177-180
34082427-6	2021	In multiple regression analyses, eGFR and hemoglobin A1c or plasma glucose were significantly, independently, and positively associated with plasma ln-XOR activity after adjusting for several confounders.	Glucose	67-74	xanthine dehydrogenase	Homo sapiens	148-154
35042470-1	2022	BACKGROUND: Xanthine oxidoreductase (XOR) is a hydroxylase enzyme involved in the metabolism of purines.	Purines	96-103	xanthine dehydrogenase	Homo sapiens	37-40
35467852-5	2022	It is shown here that the XYGJ-OS functional is able to give a mean absolute deviation (MAD) of ~3.0 ppm in the calculated shielding constants for 13C, 15N, 17O, 19F, while both XYGJ-OS and xDH-PBE0 functionals are able to provide a satisfactory estimation of chemical shifts with MADs of ~0.03 and 1.0 ppm for 1H and 13C, respectively.	Carbon-13	147-150	xanthine dehydrogenase	Homo sapiens	190-193
35298131-11	2022	Network pharmacology and molecular docking revealed that CYP1A2, CYP2A6, CYP2E1, MAOA, PLA2G2A, PTGS1, and XDH were critical targets for PBZ hepatorenal toxicity.	paclobutrazol	137-140	xanthine dehydrogenase	Homo sapiens	107-110
35192152-19	2022	Finally, concomitant therapies that inhibit the xanthine oxidase enzyme (XDH), such as allopurinol, predispose to ADRs.	Allopurinol	87-98	xanthine dehydrogenase	Homo sapiens	73-76
35192152-19	2022	Finally, concomitant therapies that inhibit the xanthine oxidase enzyme (XDH), such as allopurinol, predispose to ADRs.	adrs	114-118	xanthine dehydrogenase	Homo sapiens	73-76
35046512-7	2022	Accumulated studies have proposed mechanisms of renal damage and atherosclerosis in hyperuricemia, including inflammasome activation, decreased nitric oxide bioavailability and oxidative stress induced by uric acid, urate crystals and xanthine oxidoreductase (XOR)-mediated reactive oxygen species.	Oxygen	283-289	xanthine dehydrogenase	Homo sapiens	235-258
35194983-7	2022	Most intriguingly, we found that six unique substitutions in cetacean xanthine dehydrogenase (XDH), an enzyme that regulates the generation of the ROS precursor xanthine oxidase (XO) during ischemic/hypoxic conditions, show enhanced enzyme activity and thermal stability and diminished XO conversion activity.	Reactive Oxygen Species	147-150	xanthine dehydrogenase	Homo sapiens	70-92
35194983-7	2022	Most intriguingly, we found that six unique substitutions in cetacean xanthine dehydrogenase (XDH), an enzyme that regulates the generation of the ROS precursor xanthine oxidase (XO) during ischemic/hypoxic conditions, show enhanced enzyme activity and thermal stability and diminished XO conversion activity.	Reactive Oxygen Species	147-150	xanthine dehydrogenase	Homo sapiens	94-97
35608201-5	2022	Plasma XOR activity was evaluated using a highly sensitive assay utilizing a combination of (13C2,15N2) xanthine and liquid chromatography-triple quadrupole mass spectrometry.	(13c2,15n2) xanthine	92-112	xanthine dehydrogenase	Homo sapiens	7-10
35608201-8	2022	Immediately after the marathon, individual relative changes in plasma XOR activity were independently correlated with corresponding changes in serum creatinine and urinary L-FABP levels.	Creatinine	149-159	xanthine dehydrogenase	Homo sapiens	70-73
35608201-10	2022	These findings collectively suggest that marathon running substantially influences the purine metabolism pathway including XOR activity.	purine	87-93	xanthine dehydrogenase	Homo sapiens	123-126
35228125-6	2022	XOR, which catalyzes the terminal two steps of purine degradation, is the major source of both reactive oxygen species (O2.-, H2O2) and UA.	purine	47-53	xanthine dehydrogenase	Homo sapiens	0-3
35228125-6	2022	XOR, which catalyzes the terminal two steps of purine degradation, is the major source of both reactive oxygen species (O2.-, H2O2) and UA.	Reactive Oxygen Species	95-118	xanthine dehydrogenase	Homo sapiens	0-3
35228125-6	2022	XOR, which catalyzes the terminal two steps of purine degradation, is the major source of both reactive oxygen species (O2.-, H2O2) and UA.	Oxygen	120-122	xanthine dehydrogenase	Homo sapiens	0-3
35228125-6	2022	XOR, which catalyzes the terminal two steps of purine degradation, is the major source of both reactive oxygen species (O2.-, H2O2) and UA.	Hydrogen Peroxide	126-130	xanthine dehydrogenase	Homo sapiens	0-3
35356803-1	2022	Background and Aims: There are two types of serum uric acid-lowering agents, the xanthine oxidoreductase (XO) inhibitor and non-XO inhibitor.	Uric Acid	50-59	xanthine dehydrogenase	Homo sapiens	81-104
34998885-9	2022	The simple, newly designed Au-XOR/fMWCNT-PEDOT/GCE exhibited interference-free reproducibility and stability (~4 months) with excellent sensitivity of 16.075 microA.microM-1.cm-2for the quantification of xanthine in biological samples such as blood, tissue, urine.	Xanthine	204-212	xanthine dehydrogenase	Homo sapiens	27-33
35201174-2	2022	This study presents a plasmonic model that uses a Y-shaped metal-insulator-metal waveguide structure that realizes the ultrafast all-optical AND, XOR, and XNOR gate operation that is developed at a footprint of 6.6micromx3.4microm with a wavelength of 1.55 microm.	Metals	59-64	xanthine dehydrogenase	Homo sapiens	146-149
35201174-2	2022	This study presents a plasmonic model that uses a Y-shaped metal-insulator-metal waveguide structure that realizes the ultrafast all-optical AND, XOR, and XNOR gate operation that is developed at a footprint of 6.6micromx3.4microm with a wavelength of 1.55 microm.	Metals	75-80	xanthine dehydrogenase	Homo sapiens	146-149
35198574-1	2022	Background: Xanthine oxidoreductase (XOR) inhibition reduces reactive oxygen species (ROS) production and enhances adenosine triphosphate (ATP) synthesis.	Reactive Oxygen Species	61-84	xanthine dehydrogenase	Homo sapiens	12-35
35198574-1	2022	Background: Xanthine oxidoreductase (XOR) inhibition reduces reactive oxygen species (ROS) production and enhances adenosine triphosphate (ATP) synthesis.	Reactive Oxygen Species	61-84	xanthine dehydrogenase	Homo sapiens	37-40
35198574-1	2022	Background: Xanthine oxidoreductase (XOR) inhibition reduces reactive oxygen species (ROS) production and enhances adenosine triphosphate (ATP) synthesis.	Reactive Oxygen Species	86-89	xanthine dehydrogenase	Homo sapiens	12-35
35198574-1	2022	Background: Xanthine oxidoreductase (XOR) inhibition reduces reactive oxygen species (ROS) production and enhances adenosine triphosphate (ATP) synthesis.	Reactive Oxygen Species	86-89	xanthine dehydrogenase	Homo sapiens	37-40
35198574-1	2022	Background: Xanthine oxidoreductase (XOR) inhibition reduces reactive oxygen species (ROS) production and enhances adenosine triphosphate (ATP) synthesis.	Adenosine	115-124	xanthine dehydrogenase	Homo sapiens	12-35
35198574-1	2022	Background: Xanthine oxidoreductase (XOR) inhibition reduces reactive oxygen species (ROS) production and enhances adenosine triphosphate (ATP) synthesis.	Adenosine	115-124	xanthine dehydrogenase	Homo sapiens	37-40
35198574-1	2022	Background: Xanthine oxidoreductase (XOR) inhibition reduces reactive oxygen species (ROS) production and enhances adenosine triphosphate (ATP) synthesis.	Adenosine Triphosphate	139-142	xanthine dehydrogenase	Homo sapiens	12-35
35198574-1	2022	Background: Xanthine oxidoreductase (XOR) inhibition reduces reactive oxygen species (ROS) production and enhances adenosine triphosphate (ATP) synthesis.	Adenosine Triphosphate	139-142	xanthine dehydrogenase	Homo sapiens	37-40
35154100-0	2022	Purine-Induced IFN-gamma Promotes Uric Acid Production by Upregulating Xanthine Oxidoreductase Expression.	purine	0-6	xanthine dehydrogenase	Homo sapiens	71-94
35154100-0	2022	Purine-Induced IFN-gamma Promotes Uric Acid Production by Upregulating Xanthine Oxidoreductase Expression.	Uric Acid	34-43	xanthine dehydrogenase	Homo sapiens	71-94
35154100-1	2022	Objective: Limiting purine intake, inhibiting xanthine oxidoreductase (XOR) and inhibiting urate reabsorption in proximal tubule by uricosuric drugs, to reduce serum uric acid (UA) levels, are recognized treatments for gout.	Uric Acid	166-175	xanthine dehydrogenase	Homo sapiens	71-74
35154100-3	2022	This study aims to explore whether exogenous purines are responsible for increased XOR expression and activity.	Purines	45-52	xanthine dehydrogenase	Homo sapiens	83-86
35154100-8	2022	Results: Excess of purine was metabolized to UA in hepatocyte metabolism by XOR that was induced by IFN-gamma secreted in the conditioned growth medium of Jurkat cells in response to exogenous purine, but it did not directly induce XOR expression.	purine	19-25	xanthine dehydrogenase	Homo sapiens	76-79
35154100-8	2022	Results: Excess of purine was metabolized to UA in hepatocyte metabolism by XOR that was induced by IFN-gamma secreted in the conditioned growth medium of Jurkat cells in response to exogenous purine, but it did not directly induce XOR expression.	Uric Acid	45-47	xanthine dehydrogenase	Homo sapiens	76-79
35154100-8	2022	Results: Excess of purine was metabolized to UA in hepatocyte metabolism by XOR that was induced by IFN-gamma secreted in the conditioned growth medium of Jurkat cells in response to exogenous purine, but it did not directly induce XOR expression.	Uric Acid	45-47	xanthine dehydrogenase	Homo sapiens	232-235
35154100-8	2022	Results: Excess of purine was metabolized to UA in hepatocyte metabolism by XOR that was induced by IFN-gamma secreted in the conditioned growth medium of Jurkat cells in response to exogenous purine, but it did not directly induce XOR expression.	purine	193-199	xanthine dehydrogenase	Homo sapiens	76-79
35154100-11	2022	Conclusion: Purine not only acts as a metabolic substrate of XOR for UA production, but it induces inflammation through IFN-gamma secretion that stimulates UA production through elevation of XOR expression.	purine	12-18	xanthine dehydrogenase	Homo sapiens	61-64
35154100-11	2022	Conclusion: Purine not only acts as a metabolic substrate of XOR for UA production, but it induces inflammation through IFN-gamma secretion that stimulates UA production through elevation of XOR expression.	purine	12-18	xanthine dehydrogenase	Homo sapiens	191-194
35042470-1	2022	BACKGROUND: Xanthine oxidoreductase (XOR) is a hydroxylase enzyme involved in the metabolism of purines.	Purines	96-103	xanthine dehydrogenase	Homo sapiens	12-35
2516241-11	1989	Increased Ca2+ may affect proteases and may help in the conversion of xanthine dehydrogenase to xanthine oxidase, consequently increased production of super oxide radicals.	Superoxides	151-171	xanthine dehydrogenase	Homo sapiens	70-92
2612453-5	1989	Xanthine dehydrogenase was converted to xanthine oxidase during reperfusion and the activity of both enzymes were inhibited by allopurinol.	Allopurinol	127-138	xanthine dehydrogenase	Homo sapiens	0-22
2795662-5	1989	Urate is the end product of the reaction catalysed by xanthine oxidoreductase.	Uric Acid	0-5	xanthine dehydrogenase	Homo sapiens	54-77
2795662-8	1989	We conclude that xanthine oxidoreductase is probably present in the heart of patients, suffering from ischemic heart disease, and responsible for the increase in urate production during transient myocardial ischemia.	Uric Acid	162-167	xanthine dehydrogenase	Homo sapiens	17-40
2610113-0	1989	Mammalian xanthine oxidoreductase--a unique enzyme among hypoxanthine hydroxylating enzymes in vertebrates.	Hypoxanthine	57-69	xanthine dehydrogenase	Homo sapiens	10-33
2499318-1	1989	The purine oxidation via XOD formed from XDH in ischemia in an oxidative or proteolytic way is regarded as a source of reactive O2- species.	purine	4-10	xanthine dehydrogenase	Homo sapiens	41-44
2499318-1	1989	The purine oxidation via XOD formed from XDH in ischemia in an oxidative or proteolytic way is regarded as a source of reactive O2- species.	o2- species	128-139	xanthine dehydrogenase	Homo sapiens	41-44
2981404-3	1985	The primary source of superoxide in reperfused reoxygenated tissues appears to be the enzyme xanthine oxidase, released during ischemia by a calcium-triggered proteolytic attack on xanthine dehydrogenase.	Superoxides	22-32	xanthine dehydrogenase	Homo sapiens	181-203
2834709-3	1988	The activities of key enzymes involved in purine degradation and re-utilization (5"-nucleotidase; AMP-deaminase; hypoxanthine phosphoribosyltransferase (HPRT); xanthine dehydrogenase/oxidase) as well as the total activity of alkaline phosphatase were measured in the trophoblastic cells.	purine	42-48	xanthine dehydrogenase	Homo sapiens	160-190
3510480-3	1986	Moreover, trypsin can activate the conversion of xanthine dehydrogenase into superoxide radicals producing xanthine oxidase.	Superoxides	77-87	xanthine dehydrogenase	Homo sapiens	49-71
3935101-8	1985	In endothelial cells of microvascular origin uric acid predominates by far as the final purine degradative because of the presence of xanthine dehydrogenase in these cells; in the macrovascular endothelium purine breakdown proceeds only to hypoxanthine, since xanthine dehydrogenase is lacking.	Uric Acid	45-54	xanthine dehydrogenase	Homo sapiens	134-156
3935101-8	1985	In endothelial cells of microvascular origin uric acid predominates by far as the final purine degradative because of the presence of xanthine dehydrogenase in these cells; in the macrovascular endothelium purine breakdown proceeds only to hypoxanthine, since xanthine dehydrogenase is lacking.	Uric Acid	45-54	xanthine dehydrogenase	Homo sapiens	260-282
2753392-1	1989	The conversion of xanthine dehydrogenase to a free radical producing oxidase is an important component of oxygen-mediated tissue injury.	Oxygen	106-112	xanthine dehydrogenase	Homo sapiens	18-40
2753392-5	1989	Xanthine oxidase is assayed in the presence of pterin only, while combined xanthine dehydrogenase plus oxidase activity is determined with methylene blue which replaces NAD+ as an electron acceptor.	Methylene Blue	139-153	xanthine dehydrogenase	Homo sapiens	75-97
3059826-3	1988	The hypoxic stress also triggers the conversion of NAD-reducing xanthine dehydrogenase to the oxygen radical-producing xanthine oxidase.	Reactive Oxygen Species	94-108	xanthine dehydrogenase	Homo sapiens	64-86
3250538-3	1988	The hypoxic stress also triggers the conversion of NAD-reducing xanthine dehydrogenase to the oxygen radical-producing xanthine oxidase via a protease.	Reactive Oxygen Species	94-108	xanthine dehydrogenase	Homo sapiens	64-86
3032690-3	1987	The active oxygen species also have roles in postischemic injury brought about by the conversion during ischemia of the enzyme xanthine dehydrogenase (EC 1.1.1.204) to the radical-producing xanthine oxidase (EC 1.1.3.22).	Oxygen	11-17	xanthine dehydrogenase	Homo sapiens	127-149
2981404-3	1985	The primary source of superoxide in reperfused reoxygenated tissues appears to be the enzyme xanthine oxidase, released during ischemia by a calcium-triggered proteolytic attack on xanthine dehydrogenase.	Calcium	141-148	xanthine dehydrogenase	Homo sapiens	181-203
6357927-11	1983	There is evidence also that Se is an essential component of nicotinic acid hydroxylase, xanthine dehydrogenase, and a bacterial thiolase.	Selenium	28-30	xanthine dehydrogenase	Homo sapiens	88-110
6414723-0	1983	Activation of xanthine dehydrogenase during the prenatal period through L-thyroxine, thiourea and cycloheximide.	Thyroxine	72-83	xanthine dehydrogenase	Homo sapiens	14-36
6414723-0	1983	Activation of xanthine dehydrogenase during the prenatal period through L-thyroxine, thiourea and cycloheximide.	Thiourea	85-93	xanthine dehydrogenase	Homo sapiens	14-36
6414723-0	1983	Activation of xanthine dehydrogenase during the prenatal period through L-thyroxine, thiourea and cycloheximide.	Cycloheximide	98-111	xanthine dehydrogenase	Homo sapiens	14-36
6414723-1	1983	Xanthine dehydrogenase activity in the liver of embryonic chicks has been shown to be inducible by L-thyroxine, thiourea, and cycloheximide.	Thyroxine	99-110	xanthine dehydrogenase	Homo sapiens	0-22
6414723-1	1983	Xanthine dehydrogenase activity in the liver of embryonic chicks has been shown to be inducible by L-thyroxine, thiourea, and cycloheximide.	Thiourea	112-120	xanthine dehydrogenase	Homo sapiens	0-22
6414723-1	1983	Xanthine dehydrogenase activity in the liver of embryonic chicks has been shown to be inducible by L-thyroxine, thiourea, and cycloheximide.	Cycloheximide	126-139	xanthine dehydrogenase	Homo sapiens	0-22
6414723-3	1983	Using hepatocyte suspension and homogenized liver, it has been shown that prenatal activation of xanthine dehydrogenase results in increased rate of uric acid formation from nucleic acids and purine derivatives, but not from amino acids.	Uric Acid	149-158	xanthine dehydrogenase	Homo sapiens	97-119
6599141-0	1984	Effect of cold environment on the rat serum xanthine dehydrogenase in carbon tetrachloride poisoning.	Carbon Tetrachloride	70-90	xanthine dehydrogenase	Homo sapiens	44-66
6414723-3	1983	Using hepatocyte suspension and homogenized liver, it has been shown that prenatal activation of xanthine dehydrogenase results in increased rate of uric acid formation from nucleic acids and purine derivatives, but not from amino acids.	purine	192-198	xanthine dehydrogenase	Homo sapiens	97-119
612097-0	1977	Effect of large intraperitoneal doses of fatty acids on the rat blood serum xanthine dehydrogenase activity.	Fatty Acids	41-52	xanthine dehydrogenase	Homo sapiens	76-98
6301524-0	1983	Electron paramagnetic resonance and potentiometric studies of arsenite interaction with the molybdenum centers of xanthine oxidase, xanthine dehydrogenase, and aldehyde oxidase: a specific stabilization of the molybdenum(V) oxidation state.	arsenite	62-70	xanthine dehydrogenase	Homo sapiens	132-154
232388-0	1979	Kinetic studies of the blood serum xanthine dehydrogenase inhibition by alloxan (2,4,5,6-tetraoxypyrimidine 5,6-dioxyuracil).	Alloxan	72-79	xanthine dehydrogenase	Homo sapiens	35-57
232388-0	1979	Kinetic studies of the blood serum xanthine dehydrogenase inhibition by alloxan (2,4,5,6-tetraoxypyrimidine 5,6-dioxyuracil).	2,4,5,6-tetraoxypyrimidine 5,6-dioxyuracil	81-123	xanthine dehydrogenase	Homo sapiens	35-57
6244290-1	1980	The reduced forms of xanthine oxidase, xanthine dehydrogenase, aldehyde oxidase, and sulfite oxidase are inactivated by cyanide.	Cyanides	120-127	xanthine dehydrogenase	Homo sapiens	39-61
229850-0	1979	Observation of 17O effects on MoV EPR spectra in sulfite oxidase, xanthine dehydrogenase, and MoO(SC6H5)4-.	17o	15-18	xanthine dehydrogenase	Homo sapiens	66-88
92920-1	1979	The steady-state concentrations of glutamine, glutamate and ammonia in the kidney cells might regulate the rate of renal xanthine dehydrogenase activity.	Glutamine	35-44	xanthine dehydrogenase	Homo sapiens	121-143
92920-1	1979	The steady-state concentrations of glutamine, glutamate and ammonia in the kidney cells might regulate the rate of renal xanthine dehydrogenase activity.	Glutamic Acid	46-55	xanthine dehydrogenase	Homo sapiens	121-143
92920-1	1979	The steady-state concentrations of glutamine, glutamate and ammonia in the kidney cells might regulate the rate of renal xanthine dehydrogenase activity.	Ammonia	60-67	xanthine dehydrogenase	Homo sapiens	121-143
92920-2	1979	Both glutamate and glutamine were found to be effective inhibitors of the renal xanthine dehydrogenase activity in vivo.	Glutamic Acid	5-14	xanthine dehydrogenase	Homo sapiens	80-102
92920-2	1979	Both glutamate and glutamine were found to be effective inhibitors of the renal xanthine dehydrogenase activity in vivo.	Glutamine	19-28	xanthine dehydrogenase	Homo sapiens	80-102
232638-0	1979	Xanthine oxidoreductase inhibition by NADH as a regulatory factor of purine metabolism.	NAD	38-42	xanthine dehydrogenase	Homo sapiens	0-23
232638-0	1979	Xanthine oxidoreductase inhibition by NADH as a regulatory factor of purine metabolism.	purine	69-75	xanthine dehydrogenase	Homo sapiens	0-23
4366871-0	1972	[Actions induced by urea and guanidine on xanthine dehydrogenase].	Urea	20-24	xanthine dehydrogenase	Homo sapiens	42-64
135463-0	1975	Effect of nicotinamide on the serum xanthine dehydrogenase activity during fasting.	Niacinamide	10-22	xanthine dehydrogenase	Homo sapiens	36-58
4806470-0	1973	Differential effect of base purine analogs on levels of xanthine dehydrogenase.	purine	28-34	xanthine dehydrogenase	Homo sapiens	56-78
4790789-0	1973	Ethanol-induced inhibition in liver and blood serum xanthine dehydrogenase.	Ethanol	0-7	xanthine dehydrogenase	Homo sapiens	52-74
4366871-0	1972	[Actions induced by urea and guanidine on xanthine dehydrogenase].	Guanidine	29-38	xanthine dehydrogenase	Homo sapiens	42-64
4677279-0	1972	Inhibition of xanthine dehydrogenase by protracted ethanol uptake.	Ethanol	51-58	xanthine dehydrogenase	Homo sapiens	14-36
5377652-0	1969	Studies on the phosphate requirement for xanthine dehydrogenase activity.	Phosphates	15-24	xanthine dehydrogenase	Homo sapiens	41-63
5497992-0	1970	Studies on the phosphate requirement for xanthine dehydrogenase activity.	Phosphates	15-24	xanthine dehydrogenase	Homo sapiens	41-63
5381136-0	1969	Studies on the phosphate requirement for xanthine dehydrogenase activity.	Phosphates	15-24	xanthine dehydrogenase	Homo sapiens	41-63
5705175-0	1968	The relationship of phosphate and lipids to xanthine dehydrogenase.	Phosphates	20-29	xanthine dehydrogenase	Homo sapiens	44-66
5505815-0	1970	Studies on the phosphate requirement for xanthine dehydrogenase activity.	Phosphates	15-24	xanthine dehydrogenase	Homo sapiens	41-63
33578127-2	2021	The main XOR activities are: (i) xanthine dehydrogenase (XDH) activity that performs the last two steps of purine catabolism, from hypoxanthine to uric acid; (ii) xanthine oxidase (XO) activity that, besides purine catabolism, produces reactive oxygen species (ROS); (iii) nitrite reductase activity that generates nitric oxide, contributing to vasodilation and regulation of blood pressure; (iv) NADH oxidase activity that produces ROS.	purine	107-113	xanthine dehydrogenase	Homo sapiens	9-12
14263924-0	1964	XANTHINE DEHYDROGENASE OF HUMAN LIVER AND ITS INHIBITION BY COLCHICINE AND PHENYLBUTAZONE.	Colchicine	60-70	xanthine dehydrogenase	Homo sapiens	0-22
14263924-0	1964	XANTHINE DEHYDROGENASE OF HUMAN LIVER AND ITS INHIBITION BY COLCHICINE AND PHENYLBUTAZONE.	Phenylbutazone	75-89	xanthine dehydrogenase	Homo sapiens	0-22
33219412-2	2021	Xanthine oxidoreductase (XOR) is a rate-limiting enzyme in purine metabolism and believed to play an important role in coronary atherosclerosis.	purine	59-65	xanthine dehydrogenase	Homo sapiens	0-23
33219412-2	2021	Xanthine oxidoreductase (XOR) is a rate-limiting enzyme in purine metabolism and believed to play an important role in coronary atherosclerosis.	purine	59-65	xanthine dehydrogenase	Homo sapiens	25-28
4293483-0	1967	Comparative effects of carbon tetrachloride and colchicine on xanthine dehydrogenase.	Carbon Tetrachloride	23-43	xanthine dehydrogenase	Homo sapiens	62-84
4293483-0	1967	Comparative effects of carbon tetrachloride and colchicine on xanthine dehydrogenase.	Colchicine	48-58	xanthine dehydrogenase	Homo sapiens	62-84
4954639-0	1965	Molybdenum requirement for bacterial xanthine dehydrogenase activity.	Molybdenum	0-10	xanthine dehydrogenase	Homo sapiens	37-59
13478742-0	1957	Role of essential amino acids in the early formation of avian liver xanthine dehydrogenase activity.	Amino Acids, Essential	8-29	xanthine dehydrogenase	Homo sapiens	68-90
33578127-2	2021	The main XOR activities are: (i) xanthine dehydrogenase (XDH) activity that performs the last two steps of purine catabolism, from hypoxanthine to uric acid; (ii) xanthine oxidase (XO) activity that, besides purine catabolism, produces reactive oxygen species (ROS); (iii) nitrite reductase activity that generates nitric oxide, contributing to vasodilation and regulation of blood pressure; (iv) NADH oxidase activity that produces ROS.	purine	107-113	xanthine dehydrogenase	Homo sapiens	33-55
33578127-2	2021	The main XOR activities are: (i) xanthine dehydrogenase (XDH) activity that performs the last two steps of purine catabolism, from hypoxanthine to uric acid; (ii) xanthine oxidase (XO) activity that, besides purine catabolism, produces reactive oxygen species (ROS); (iii) nitrite reductase activity that generates nitric oxide, contributing to vasodilation and regulation of blood pressure; (iv) NADH oxidase activity that produces ROS.	purine	107-113	xanthine dehydrogenase	Homo sapiens	57-60
33578127-2	2021	The main XOR activities are: (i) xanthine dehydrogenase (XDH) activity that performs the last two steps of purine catabolism, from hypoxanthine to uric acid; (ii) xanthine oxidase (XO) activity that, besides purine catabolism, produces reactive oxygen species (ROS); (iii) nitrite reductase activity that generates nitric oxide, contributing to vasodilation and regulation of blood pressure; (iv) NADH oxidase activity that produces ROS.	Hypoxanthine	131-143	xanthine dehydrogenase	Homo sapiens	9-12
33578127-2	2021	The main XOR activities are: (i) xanthine dehydrogenase (XDH) activity that performs the last two steps of purine catabolism, from hypoxanthine to uric acid; (ii) xanthine oxidase (XO) activity that, besides purine catabolism, produces reactive oxygen species (ROS); (iii) nitrite reductase activity that generates nitric oxide, contributing to vasodilation and regulation of blood pressure; (iv) NADH oxidase activity that produces ROS.	Hypoxanthine	131-143	xanthine dehydrogenase	Homo sapiens	33-55
33578127-2	2021	The main XOR activities are: (i) xanthine dehydrogenase (XDH) activity that performs the last two steps of purine catabolism, from hypoxanthine to uric acid; (ii) xanthine oxidase (XO) activity that, besides purine catabolism, produces reactive oxygen species (ROS); (iii) nitrite reductase activity that generates nitric oxide, contributing to vasodilation and regulation of blood pressure; (iv) NADH oxidase activity that produces ROS.	Hypoxanthine	131-143	xanthine dehydrogenase	Homo sapiens	57-60
33578127-2	2021	The main XOR activities are: (i) xanthine dehydrogenase (XDH) activity that performs the last two steps of purine catabolism, from hypoxanthine to uric acid; (ii) xanthine oxidase (XO) activity that, besides purine catabolism, produces reactive oxygen species (ROS); (iii) nitrite reductase activity that generates nitric oxide, contributing to vasodilation and regulation of blood pressure; (iv) NADH oxidase activity that produces ROS.	Uric Acid	147-156	xanthine dehydrogenase	Homo sapiens	9-12
33578127-2	2021	The main XOR activities are: (i) xanthine dehydrogenase (XDH) activity that performs the last two steps of purine catabolism, from hypoxanthine to uric acid; (ii) xanthine oxidase (XO) activity that, besides purine catabolism, produces reactive oxygen species (ROS); (iii) nitrite reductase activity that generates nitric oxide, contributing to vasodilation and regulation of blood pressure; (iv) NADH oxidase activity that produces ROS.	Uric Acid	147-156	xanthine dehydrogenase	Homo sapiens	33-55
33578127-2	2021	The main XOR activities are: (i) xanthine dehydrogenase (XDH) activity that performs the last two steps of purine catabolism, from hypoxanthine to uric acid; (ii) xanthine oxidase (XO) activity that, besides purine catabolism, produces reactive oxygen species (ROS); (iii) nitrite reductase activity that generates nitric oxide, contributing to vasodilation and regulation of blood pressure; (iv) NADH oxidase activity that produces ROS.	Uric Acid	147-156	xanthine dehydrogenase	Homo sapiens	57-60
33578127-2	2021	The main XOR activities are: (i) xanthine dehydrogenase (XDH) activity that performs the last two steps of purine catabolism, from hypoxanthine to uric acid; (ii) xanthine oxidase (XO) activity that, besides purine catabolism, produces reactive oxygen species (ROS); (iii) nitrite reductase activity that generates nitric oxide, contributing to vasodilation and regulation of blood pressure; (iv) NADH oxidase activity that produces ROS.	purine	208-214	xanthine dehydrogenase	Homo sapiens	9-12
33578127-2	2021	The main XOR activities are: (i) xanthine dehydrogenase (XDH) activity that performs the last two steps of purine catabolism, from hypoxanthine to uric acid; (ii) xanthine oxidase (XO) activity that, besides purine catabolism, produces reactive oxygen species (ROS); (iii) nitrite reductase activity that generates nitric oxide, contributing to vasodilation and regulation of blood pressure; (iv) NADH oxidase activity that produces ROS.	purine	208-214	xanthine dehydrogenase	Homo sapiens	33-55
33578127-2	2021	The main XOR activities are: (i) xanthine dehydrogenase (XDH) activity that performs the last two steps of purine catabolism, from hypoxanthine to uric acid; (ii) xanthine oxidase (XO) activity that, besides purine catabolism, produces reactive oxygen species (ROS); (iii) nitrite reductase activity that generates nitric oxide, contributing to vasodilation and regulation of blood pressure; (iv) NADH oxidase activity that produces ROS.	purine	208-214	xanthine dehydrogenase	Homo sapiens	57-60
33578127-2	2021	The main XOR activities are: (i) xanthine dehydrogenase (XDH) activity that performs the last two steps of purine catabolism, from hypoxanthine to uric acid; (ii) xanthine oxidase (XO) activity that, besides purine catabolism, produces reactive oxygen species (ROS); (iii) nitrite reductase activity that generates nitric oxide, contributing to vasodilation and regulation of blood pressure; (iv) NADH oxidase activity that produces ROS.	Reactive Oxygen Species	236-259	xanthine dehydrogenase	Homo sapiens	9-12
33578127-2	2021	The main XOR activities are: (i) xanthine dehydrogenase (XDH) activity that performs the last two steps of purine catabolism, from hypoxanthine to uric acid; (ii) xanthine oxidase (XO) activity that, besides purine catabolism, produces reactive oxygen species (ROS); (iii) nitrite reductase activity that generates nitric oxide, contributing to vasodilation and regulation of blood pressure; (iv) NADH oxidase activity that produces ROS.	Reactive Oxygen Species	236-259	xanthine dehydrogenase	Homo sapiens	33-55
33578127-2	2021	The main XOR activities are: (i) xanthine dehydrogenase (XDH) activity that performs the last two steps of purine catabolism, from hypoxanthine to uric acid; (ii) xanthine oxidase (XO) activity that, besides purine catabolism, produces reactive oxygen species (ROS); (iii) nitrite reductase activity that generates nitric oxide, contributing to vasodilation and regulation of blood pressure; (iv) NADH oxidase activity that produces ROS.	Reactive Oxygen Species	236-259	xanthine dehydrogenase	Homo sapiens	57-60
33578127-2	2021	The main XOR activities are: (i) xanthine dehydrogenase (XDH) activity that performs the last two steps of purine catabolism, from hypoxanthine to uric acid; (ii) xanthine oxidase (XO) activity that, besides purine catabolism, produces reactive oxygen species (ROS); (iii) nitrite reductase activity that generates nitric oxide, contributing to vasodilation and regulation of blood pressure; (iv) NADH oxidase activity that produces ROS.	Reactive Oxygen Species	261-264	xanthine dehydrogenase	Homo sapiens	9-12
33578127-2	2021	The main XOR activities are: (i) xanthine dehydrogenase (XDH) activity that performs the last two steps of purine catabolism, from hypoxanthine to uric acid; (ii) xanthine oxidase (XO) activity that, besides purine catabolism, produces reactive oxygen species (ROS); (iii) nitrite reductase activity that generates nitric oxide, contributing to vasodilation and regulation of blood pressure; (iv) NADH oxidase activity that produces ROS.	Reactive Oxygen Species	261-264	xanthine dehydrogenase	Homo sapiens	33-55
33578127-2	2021	The main XOR activities are: (i) xanthine dehydrogenase (XDH) activity that performs the last two steps of purine catabolism, from hypoxanthine to uric acid; (ii) xanthine oxidase (XO) activity that, besides purine catabolism, produces reactive oxygen species (ROS); (iii) nitrite reductase activity that generates nitric oxide, contributing to vasodilation and regulation of blood pressure; (iv) NADH oxidase activity that produces ROS.	Reactive Oxygen Species	261-264	xanthine dehydrogenase	Homo sapiens	57-60
33578127-2	2021	The main XOR activities are: (i) xanthine dehydrogenase (XDH) activity that performs the last two steps of purine catabolism, from hypoxanthine to uric acid; (ii) xanthine oxidase (XO) activity that, besides purine catabolism, produces reactive oxygen species (ROS); (iii) nitrite reductase activity that generates nitric oxide, contributing to vasodilation and regulation of blood pressure; (iv) NADH oxidase activity that produces ROS.	Nitrites	273-280	xanthine dehydrogenase	Homo sapiens	9-12
33578127-2	2021	The main XOR activities are: (i) xanthine dehydrogenase (XDH) activity that performs the last two steps of purine catabolism, from hypoxanthine to uric acid; (ii) xanthine oxidase (XO) activity that, besides purine catabolism, produces reactive oxygen species (ROS); (iii) nitrite reductase activity that generates nitric oxide, contributing to vasodilation and regulation of blood pressure; (iv) NADH oxidase activity that produces ROS.	Nitrites	273-280	xanthine dehydrogenase	Homo sapiens	33-55
33578127-2	2021	The main XOR activities are: (i) xanthine dehydrogenase (XDH) activity that performs the last two steps of purine catabolism, from hypoxanthine to uric acid; (ii) xanthine oxidase (XO) activity that, besides purine catabolism, produces reactive oxygen species (ROS); (iii) nitrite reductase activity that generates nitric oxide, contributing to vasodilation and regulation of blood pressure; (iv) NADH oxidase activity that produces ROS.	Nitrites	273-280	xanthine dehydrogenase	Homo sapiens	57-60
33578127-2	2021	The main XOR activities are: (i) xanthine dehydrogenase (XDH) activity that performs the last two steps of purine catabolism, from hypoxanthine to uric acid; (ii) xanthine oxidase (XO) activity that, besides purine catabolism, produces reactive oxygen species (ROS); (iii) nitrite reductase activity that generates nitric oxide, contributing to vasodilation and regulation of blood pressure; (iv) NADH oxidase activity that produces ROS.	Nitric Oxide	315-327	xanthine dehydrogenase	Homo sapiens	9-12
33578127-2	2021	The main XOR activities are: (i) xanthine dehydrogenase (XDH) activity that performs the last two steps of purine catabolism, from hypoxanthine to uric acid; (ii) xanthine oxidase (XO) activity that, besides purine catabolism, produces reactive oxygen species (ROS); (iii) nitrite reductase activity that generates nitric oxide, contributing to vasodilation and regulation of blood pressure; (iv) NADH oxidase activity that produces ROS.	Nitric Oxide	315-327	xanthine dehydrogenase	Homo sapiens	33-55
33578127-2	2021	The main XOR activities are: (i) xanthine dehydrogenase (XDH) activity that performs the last two steps of purine catabolism, from hypoxanthine to uric acid; (ii) xanthine oxidase (XO) activity that, besides purine catabolism, produces reactive oxygen species (ROS); (iii) nitrite reductase activity that generates nitric oxide, contributing to vasodilation and regulation of blood pressure; (iv) NADH oxidase activity that produces ROS.	Nitric Oxide	315-327	xanthine dehydrogenase	Homo sapiens	57-60
33578127-2	2021	The main XOR activities are: (i) xanthine dehydrogenase (XDH) activity that performs the last two steps of purine catabolism, from hypoxanthine to uric acid; (ii) xanthine oxidase (XO) activity that, besides purine catabolism, produces reactive oxygen species (ROS); (iii) nitrite reductase activity that generates nitric oxide, contributing to vasodilation and regulation of blood pressure; (iv) NADH oxidase activity that produces ROS.	Reactive Oxygen Species	433-436	xanthine dehydrogenase	Homo sapiens	9-12
33578127-2	2021	The main XOR activities are: (i) xanthine dehydrogenase (XDH) activity that performs the last two steps of purine catabolism, from hypoxanthine to uric acid; (ii) xanthine oxidase (XO) activity that, besides purine catabolism, produces reactive oxygen species (ROS); (iii) nitrite reductase activity that generates nitric oxide, contributing to vasodilation and regulation of blood pressure; (iv) NADH oxidase activity that produces ROS.	Reactive Oxygen Species	433-436	xanthine dehydrogenase	Homo sapiens	33-55
33578127-2	2021	The main XOR activities are: (i) xanthine dehydrogenase (XDH) activity that performs the last two steps of purine catabolism, from hypoxanthine to uric acid; (ii) xanthine oxidase (XO) activity that, besides purine catabolism, produces reactive oxygen species (ROS); (iii) nitrite reductase activity that generates nitric oxide, contributing to vasodilation and regulation of blood pressure; (iv) NADH oxidase activity that produces ROS.	Reactive Oxygen Species	433-436	xanthine dehydrogenase	Homo sapiens	57-60
33578127-4	2021	About XOR products, it should be considered that (i) uric acid is not only a proinflammatory agent, but also a fundamental antioxidant molecule in serum and (ii) XOR-derived ROS are essential to the inflammatory defensive response.	Uric Acid	53-62	xanthine dehydrogenase	Homo sapiens	6-9
33578127-4	2021	About XOR products, it should be considered that (i) uric acid is not only a proinflammatory agent, but also a fundamental antioxidant molecule in serum and (ii) XOR-derived ROS are essential to the inflammatory defensive response.	Uric Acid	53-62	xanthine dehydrogenase	Homo sapiens	162-165
33578127-4	2021	About XOR products, it should be considered that (i) uric acid is not only a proinflammatory agent, but also a fundamental antioxidant molecule in serum and (ii) XOR-derived ROS are essential to the inflammatory defensive response.	Reactive Oxygen Species	174-177	xanthine dehydrogenase	Homo sapiens	6-9
33578127-4	2021	About XOR products, it should be considered that (i) uric acid is not only a proinflammatory agent, but also a fundamental antioxidant molecule in serum and (ii) XOR-derived ROS are essential to the inflammatory defensive response.	Reactive Oxygen Species	174-177	xanthine dehydrogenase	Homo sapiens	162-165
33854690-6	2021	In the human body, xanthine oxidoreductase (XOR) catalyzes the oxidative hydroxylation of hypoxanthine to xanthine to uric acid, with the accompanying production of ROS.	Hypoxanthine	90-102	xanthine dehydrogenase	Homo sapiens	19-42
33854690-6	2021	In the human body, xanthine oxidoreductase (XOR) catalyzes the oxidative hydroxylation of hypoxanthine to xanthine to uric acid, with the accompanying production of ROS.	Hypoxanthine	90-102	xanthine dehydrogenase	Homo sapiens	44-47
33854690-6	2021	In the human body, xanthine oxidoreductase (XOR) catalyzes the oxidative hydroxylation of hypoxanthine to xanthine to uric acid, with the accompanying production of ROS.	Xanthine	19-27	xanthine dehydrogenase	Homo sapiens	44-47
33854690-6	2021	In the human body, xanthine oxidoreductase (XOR) catalyzes the oxidative hydroxylation of hypoxanthine to xanthine to uric acid, with the accompanying production of ROS.	Uric Acid	118-127	xanthine dehydrogenase	Homo sapiens	19-42
33854690-6	2021	In the human body, xanthine oxidoreductase (XOR) catalyzes the oxidative hydroxylation of hypoxanthine to xanthine to uric acid, with the accompanying production of ROS.	Uric Acid	118-127	xanthine dehydrogenase	Homo sapiens	44-47
33854690-6	2021	In the human body, xanthine oxidoreductase (XOR) catalyzes the oxidative hydroxylation of hypoxanthine to xanthine to uric acid, with the accompanying production of ROS.	Reactive Oxygen Species	165-168	xanthine dehydrogenase	Homo sapiens	19-42
33854690-6	2021	In the human body, xanthine oxidoreductase (XOR) catalyzes the oxidative hydroxylation of hypoxanthine to xanthine to uric acid, with the accompanying production of ROS.	Reactive Oxygen Species	165-168	xanthine dehydrogenase	Homo sapiens	44-47
33580173-1	2021	Xanthine oxidoreductase (XOR) catalyzes the oxidation of hypoxanthine to xanthine, and of xanthine to uric acid.	Hypoxanthine	57-69	xanthine dehydrogenase	Homo sapiens	0-23
33689361-3	2021	By using the extensive and chemically diverse GMTKN55 database, we explore the limits of the XYG3-type DHAs using the B3LYP reference orbitals, namely, xDH@B3LYP, with a gradually relaxed constraint on the mixing parameters of DHAs.	dhas	103-107	xanthine dehydrogenase	Homo sapiens	152-155
33669298-5	2021	Multiple regression analysis demonstrated that XOR activity was independently associated with body mass index (beta = 0.26, p < 0.001), diabetes (beta = 0.09, p < 0.001), dyslipidemia (beta = 0.08, p = 0.001), and uric acid (beta = 0.13, p < 0.001).	Uric Acid	214-223	xanthine dehydrogenase	Homo sapiens	47-50
33580173-1	2021	Xanthine oxidoreductase (XOR) catalyzes the oxidation of hypoxanthine to xanthine, and of xanthine to uric acid.	Hypoxanthine	57-69	xanthine dehydrogenase	Homo sapiens	25-28
33580173-1	2021	Xanthine oxidoreductase (XOR) catalyzes the oxidation of hypoxanthine to xanthine, and of xanthine to uric acid.	Xanthine	61-69	xanthine dehydrogenase	Homo sapiens	0-23
33580173-1	2021	Xanthine oxidoreductase (XOR) catalyzes the oxidation of hypoxanthine to xanthine, and of xanthine to uric acid.	Xanthine	61-69	xanthine dehydrogenase	Homo sapiens	25-28
33580173-1	2021	Xanthine oxidoreductase (XOR) catalyzes the oxidation of hypoxanthine to xanthine, and of xanthine to uric acid.	Xanthine	73-81	xanthine dehydrogenase	Homo sapiens	0-23
33580173-1	2021	Xanthine oxidoreductase (XOR) catalyzes the oxidation of hypoxanthine to xanthine, and of xanthine to uric acid.	Xanthine	73-81	xanthine dehydrogenase	Homo sapiens	25-28
33580173-1	2021	Xanthine oxidoreductase (XOR) catalyzes the oxidation of hypoxanthine to xanthine, and of xanthine to uric acid.	Uric Acid	102-111	xanthine dehydrogenase	Homo sapiens	0-23
33580173-1	2021	Xanthine oxidoreductase (XOR) catalyzes the oxidation of hypoxanthine to xanthine, and of xanthine to uric acid.	Uric Acid	102-111	xanthine dehydrogenase	Homo sapiens	25-28
33580173-2	2021	XOR also enhances the production of reactive oxygen species and causes endothelial dysfunction.	Oxygen	45-51	xanthine dehydrogenase	Homo sapiens	0-3
33580173-5	2021	The plasma XOR activity also showed a positive correlation with the serum triglyceride.	Triglycerides	74-86	xanthine dehydrogenase	Homo sapiens	11-14
32789757-5	2021	XDH is initially synthesised as a 150-kDa protein from which XO is derived, e.g. under conditions of ischemia/hypoxia either reversibly by conformational changes (calcium or SH oxidation) or irreversibly by proteolysis, the latter leading to formation of a 130-kDa form of XO.	Calcium	163-170	xanthine dehydrogenase	Homo sapiens	0-3
33091574-3	2021	METHODS: Inhibition of adenosine deaminase (ADA), purine nucleoside phosphorylase (PNP) and xanthine oxidoreductase (XOR) activity by quercetin and metabolites was determined by HPLC.	Quercetin	134-143	xanthine dehydrogenase	Homo sapiens	92-115
33091574-3	2021	METHODS: Inhibition of adenosine deaminase (ADA), purine nucleoside phosphorylase (PNP) and xanthine oxidoreductase (XOR) activity by quercetin and metabolites was determined by HPLC.	Quercetin	134-143	xanthine dehydrogenase	Homo sapiens	117-120
33400348-2	2021	Xanthine oxidoreductase inhibitors (XORi) reduce serum uric acid levels and have several other potential effects.	Uric Acid	55-64	xanthine dehydrogenase	Homo sapiens	0-23
32789757-6	2021	Both, XO and XDH, catalyse the conversion of hypoxanthine via xanthine to uric acid, the former by using oxygen forming superoxide and hydrogen peroxide and the latter NAD+.	Hypoxanthine	45-57	xanthine dehydrogenase	Homo sapiens	13-16
32789757-6	2021	Both, XO and XDH, catalyse the conversion of hypoxanthine via xanthine to uric acid, the former by using oxygen forming superoxide and hydrogen peroxide and the latter NAD+.	Xanthine	49-57	xanthine dehydrogenase	Homo sapiens	13-16
32789757-6	2021	Both, XO and XDH, catalyse the conversion of hypoxanthine via xanthine to uric acid, the former by using oxygen forming superoxide and hydrogen peroxide and the latter NAD+.	Uric Acid	74-83	xanthine dehydrogenase	Homo sapiens	13-16
32789757-6	2021	Both, XO and XDH, catalyse the conversion of hypoxanthine via xanthine to uric acid, the former by using oxygen forming superoxide and hydrogen peroxide and the latter NAD+.	Oxygen	105-111	xanthine dehydrogenase	Homo sapiens	13-16
32789757-6	2021	Both, XO and XDH, catalyse the conversion of hypoxanthine via xanthine to uric acid, the former by using oxygen forming superoxide and hydrogen peroxide and the latter NAD+.	Superoxides	120-130	xanthine dehydrogenase	Homo sapiens	13-16
32789757-6	2021	Both, XO and XDH, catalyse the conversion of hypoxanthine via xanthine to uric acid, the former by using oxygen forming superoxide and hydrogen peroxide and the latter NAD+.	Hydrogen Peroxide	135-152	xanthine dehydrogenase	Homo sapiens	13-16
32789757-6	2021	Both, XO and XDH, catalyse the conversion of hypoxanthine via xanthine to uric acid, the former by using oxygen forming superoxide and hydrogen peroxide and the latter NAD+.	NAD	168-172	xanthine dehydrogenase	Homo sapiens	13-16
32789757-7	2021	However, XDH is in principle also able to generate ROS.	ros	51-54	xanthine dehydrogenase	Homo sapiens	9-12
32893671-8	2020	Treatment with an XOR inhibitor can decrease uric acid for preventing gout, reduce production of XO-related ROS, and promote reutilization of hypoxanthine and ATP production through the salvage pathway.	Reactive Oxygen Species	108-111	xanthine dehydrogenase	Homo sapiens	18-21
33096031-5	2020	Xanthine dehydrogenase converted the hypoxanthine to uric acid and yielded two molecules of NADH, which in turn reduced Fe3+ to Fe2+ (mediated by 1-methoxy-5-ethylphenazinium ethylsulfate).	Hypoxanthine	37-49	xanthine dehydrogenase	Homo sapiens	0-22
33096031-5	2020	Xanthine dehydrogenase converted the hypoxanthine to uric acid and yielded two molecules of NADH, which in turn reduced Fe3+ to Fe2+ (mediated by 1-methoxy-5-ethylphenazinium ethylsulfate).	Uric Acid	53-62	xanthine dehydrogenase	Homo sapiens	0-22
33096031-5	2020	Xanthine dehydrogenase converted the hypoxanthine to uric acid and yielded two molecules of NADH, which in turn reduced Fe3+ to Fe2+ (mediated by 1-methoxy-5-ethylphenazinium ethylsulfate).	NAD	92-96	xanthine dehydrogenase	Homo sapiens	0-22
33096031-5	2020	Xanthine dehydrogenase converted the hypoxanthine to uric acid and yielded two molecules of NADH, which in turn reduced Fe3+ to Fe2+ (mediated by 1-methoxy-5-ethylphenazinium ethylsulfate).	ferric sulfate	120-124	xanthine dehydrogenase	Homo sapiens	0-22
33096031-5	2020	Xanthine dehydrogenase converted the hypoxanthine to uric acid and yielded two molecules of NADH, which in turn reduced Fe3+ to Fe2+ (mediated by 1-methoxy-5-ethylphenazinium ethylsulfate).	ammonium ferrous sulfate	128-132	xanthine dehydrogenase	Homo sapiens	0-22
33096031-5	2020	Xanthine dehydrogenase converted the hypoxanthine to uric acid and yielded two molecules of NADH, which in turn reduced Fe3+ to Fe2+ (mediated by 1-methoxy-5-ethylphenazinium ethylsulfate).	1-methoxy-5-ethylphenazinium ethylsulfate	146-187	xanthine dehydrogenase	Homo sapiens	0-22
33211396-1	2021	AIMS: Xanthine oxidoreductase (XOR) is an enzyme that catalyzes hypoxanthine and xanthine to xanthine and uric acid, respectively.	Xanthine	68-76	xanthine dehydrogenase	Homo sapiens	6-29
33211396-1	2021	AIMS: Xanthine oxidoreductase (XOR) is an enzyme that catalyzes hypoxanthine and xanthine to xanthine and uric acid, respectively.	Xanthine	68-76	xanthine dehydrogenase	Homo sapiens	31-34
33211396-1	2021	AIMS: Xanthine oxidoreductase (XOR) is an enzyme that catalyzes hypoxanthine and xanthine to xanthine and uric acid, respectively.	Xanthine	81-89	xanthine dehydrogenase	Homo sapiens	6-29
33211396-1	2021	AIMS: Xanthine oxidoreductase (XOR) is an enzyme that catalyzes hypoxanthine and xanthine to xanthine and uric acid, respectively.	Xanthine	81-89	xanthine dehydrogenase	Homo sapiens	31-34
33211396-1	2021	AIMS: Xanthine oxidoreductase (XOR) is an enzyme that catalyzes hypoxanthine and xanthine to xanthine and uric acid, respectively.	Uric Acid	106-115	xanthine dehydrogenase	Homo sapiens	6-29
33211396-1	2021	AIMS: Xanthine oxidoreductase (XOR) is an enzyme that catalyzes hypoxanthine and xanthine to xanthine and uric acid, respectively.	Uric Acid	106-115	xanthine dehydrogenase	Homo sapiens	31-34
32893671-0	2020	New insights into purine metabolism in metabolic diseases: role of xanthine oxidoreductase activity.	purine	18-24	xanthine dehydrogenase	Homo sapiens	67-90
32893671-1	2020	Xanthine oxidoreductase (XOR) consists of two different forms, xanthine dehydrogenase and xanthine oxidase (XO), and is a rate-limiting enzyme of uric acid production from hypoxanthine and xanthine.	Uric Acid	146-155	xanthine dehydrogenase	Homo sapiens	0-23
32893671-1	2020	Xanthine oxidoreductase (XOR) consists of two different forms, xanthine dehydrogenase and xanthine oxidase (XO), and is a rate-limiting enzyme of uric acid production from hypoxanthine and xanthine.	Uric Acid	146-155	xanthine dehydrogenase	Homo sapiens	25-28
32893671-1	2020	Xanthine oxidoreductase (XOR) consists of two different forms, xanthine dehydrogenase and xanthine oxidase (XO), and is a rate-limiting enzyme of uric acid production from hypoxanthine and xanthine.	Uric Acid	146-155	xanthine dehydrogenase	Homo sapiens	63-85
32893671-8	2020	Treatment with an XOR inhibitor can decrease uric acid for preventing gout, reduce production of XO-related ROS, and promote reutilization of hypoxanthine and ATP production through the salvage pathway.	Uric Acid	45-54	xanthine dehydrogenase	Homo sapiens	18-21
32893671-8	2020	Treatment with an XOR inhibitor can decrease uric acid for preventing gout, reduce production of XO-related ROS, and promote reutilization of hypoxanthine and ATP production through the salvage pathway.	Hypoxanthine	142-154	xanthine dehydrogenase	Homo sapiens	18-21
32893671-8	2020	Treatment with an XOR inhibitor can decrease uric acid for preventing gout, reduce production of XO-related ROS, and promote reutilization of hypoxanthine and ATP production through the salvage pathway.	Adenosine Triphosphate	159-162	xanthine dehydrogenase	Homo sapiens	18-21
32893671-9	2020	It has recently been suggested that discontinuation of an XOR inhibitor causes adverse cardiovascular outcomes as XOR inhibitor withdrawal syndrome, possibly due to cardiac disturbance of conduction and contraction by reduced ATP production.	Adenosine Triphosphate	226-229	xanthine dehydrogenase	Homo sapiens	58-61
32893671-9	2020	It has recently been suggested that discontinuation of an XOR inhibitor causes adverse cardiovascular outcomes as XOR inhibitor withdrawal syndrome, possibly due to cardiac disturbance of conduction and contraction by reduced ATP production.	Adenosine Triphosphate	226-229	xanthine dehydrogenase	Homo sapiens	114-117
32893671-10	2020	New insights into purine metabolism, including the role of XOR activity in the past 5 yr, are mainly discussed in this review.	purine	18-24	xanthine dehydrogenase	Homo sapiens	59-62
32342210-6	2020	A multivariate logistic regression model showed that lactate (per 1.0 mmol/L increase, OR 1.326; 95%, CI 1.166-1.508, p < 0.001) and the Acute Physiology and Chronic Health Evaluation II score (per 1.0 point increase, OR 1.095, 95% CI 1.034-1.160, p = 0.002) were independently associated with the high-XOR group.	Lactic Acid	53-60	xanthine dehydrogenase	Homo sapiens	303-306
32996975-1	2020	In purine metabolism, the xanthine oxidoreductase enzyme converts hypoxanthine (HXN) to xanthine (XN) and XN to uric acid (UA).	purine	3-9	xanthine dehydrogenase	Homo sapiens	26-49
32996975-1	2020	In purine metabolism, the xanthine oxidoreductase enzyme converts hypoxanthine (HXN) to xanthine (XN) and XN to uric acid (UA).	Hypoxanthine	66-78	xanthine dehydrogenase	Homo sapiens	26-49
32996975-1	2020	In purine metabolism, the xanthine oxidoreductase enzyme converts hypoxanthine (HXN) to xanthine (XN) and XN to uric acid (UA).	Uric Acid	112-121	xanthine dehydrogenase	Homo sapiens	26-49
32996975-1	2020	In purine metabolism, the xanthine oxidoreductase enzyme converts hypoxanthine (HXN) to xanthine (XN) and XN to uric acid (UA).	Uric Acid	123-125	xanthine dehydrogenase	Homo sapiens	26-49
32955243-7	2020	Based on above results, we designed a XOR logic gate based on the biosensing interface for ATPA and ATP detection.	ATPA	91-95	xanthine dehydrogenase	Homo sapiens	38-41
32955243-7	2020	Based on above results, we designed a XOR logic gate based on the biosensing interface for ATPA and ATP detection.	Adenosine Triphosphate	91-94	xanthine dehydrogenase	Homo sapiens	38-41
32911634-3	2020	Xanthine oxidoreductase (XOR) activities produce uric acid, as well as reactive oxygen and nitrogen species, which all may be relevant to such equilibrium.	Uric Acid	49-58	xanthine dehydrogenase	Homo sapiens	0-23
32911634-3	2020	Xanthine oxidoreductase (XOR) activities produce uric acid, as well as reactive oxygen and nitrogen species, which all may be relevant to such equilibrium.	Uric Acid	49-58	xanthine dehydrogenase	Homo sapiens	25-28
32911634-5	2020	However, XOR activity contributes to a regular level of ROS and RNS, which appears essential for the proper functioning of many physiological pathways.	Radon	64-67	xanthine dehydrogenase	Homo sapiens	9-12
32911634-3	2020	Xanthine oxidoreductase (XOR) activities produce uric acid, as well as reactive oxygen and nitrogen species, which all may be relevant to such equilibrium.	Nitrogen	91-99	xanthine dehydrogenase	Homo sapiens	0-23
32911634-3	2020	Xanthine oxidoreductase (XOR) activities produce uric acid, as well as reactive oxygen and nitrogen species, which all may be relevant to such equilibrium.	Nitrogen	91-99	xanthine dehydrogenase	Homo sapiens	25-28
32911634-5	2020	However, XOR activity contributes to a regular level of ROS and RNS, which appears essential for the proper functioning of many physiological pathways.	ros	56-59	xanthine dehydrogenase	Homo sapiens	9-12
32432414-2	2020	Xanthine oxidoreductase (XOR), the rate-limiting enzyme of purine metabolism, plays an important role in uric acid production and generates reactive oxygen species.	purine	59-65	xanthine dehydrogenase	Homo sapiens	0-23
32434129-3	2020	It is well-known that uric acid is an organic compound and the water-soluble final product of purine catabolism, which is catalysed by xanthine oxidoreductase and excreted by kidneys.	Uric Acid	22-31	xanthine dehydrogenase	Homo sapiens	135-158
32434129-3	2020	It is well-known that uric acid is an organic compound and the water-soluble final product of purine catabolism, which is catalysed by xanthine oxidoreductase and excreted by kidneys.	Water	63-68	xanthine dehydrogenase	Homo sapiens	135-158
32434129-3	2020	It is well-known that uric acid is an organic compound and the water-soluble final product of purine catabolism, which is catalysed by xanthine oxidoreductase and excreted by kidneys.	purine	94-100	xanthine dehydrogenase	Homo sapiens	135-158
32613959-2	2020	Herein, a hybrid system comprising polyethylene glycerol swing-arm-tethered NAD+ and xylose dehydrogenase (XDH), coupled with platinum nanoparticles deposited on carbon nanotubes (PtNPs@MWCNTs), was constructed for the real-time sensing of xylose.	polyethylene glycerol	35-56	xanthine dehydrogenase	Homo sapiens	107-110
32759980-6	2020	Western blotting showed expression of sialin, a known nitrate transporter, in the lacrimal glands and other eye components, and also xanthine oxidoreductase, a nitrate and nitrite reductase, in cornea and sclera.	Nitrites	172-179	xanthine dehydrogenase	Homo sapiens	133-156
32432414-2	2020	Xanthine oxidoreductase (XOR), the rate-limiting enzyme of purine metabolism, plays an important role in uric acid production and generates reactive oxygen species.	purine	59-65	xanthine dehydrogenase	Homo sapiens	25-28
32432414-2	2020	Xanthine oxidoreductase (XOR), the rate-limiting enzyme of purine metabolism, plays an important role in uric acid production and generates reactive oxygen species.	Uric Acid	105-114	xanthine dehydrogenase	Homo sapiens	0-23
32432414-2	2020	Xanthine oxidoreductase (XOR), the rate-limiting enzyme of purine metabolism, plays an important role in uric acid production and generates reactive oxygen species.	Uric Acid	105-114	xanthine dehydrogenase	Homo sapiens	25-28
32432414-2	2020	Xanthine oxidoreductase (XOR), the rate-limiting enzyme of purine metabolism, plays an important role in uric acid production and generates reactive oxygen species.	Oxygen	149-155	xanthine dehydrogenase	Homo sapiens	0-23
32432414-2	2020	Xanthine oxidoreductase (XOR), the rate-limiting enzyme of purine metabolism, plays an important role in uric acid production and generates reactive oxygen species.	Oxygen	149-155	xanthine dehydrogenase	Homo sapiens	25-28
32699806-3	2020	In in vitro cell culture experiments Alternol inhibits prostate cancer cell proliferation by causing cell cycle arrest, reduces the expression of Bcl-2 and other pro-survival proteins, increases the level of radical oxygen species by activating xanthine dehydrogenase, blunts mitochondrial aerobic respiration and ATP production, and triggers autophagy flux.	Alternol	37-45	xanthine dehydrogenase	Homo sapiens	245-267
32380019-0	2020	Arabinogalactan and hyaluronic acid in ophthalmic solution: Experimental effect on xanthine oxidoreductase complex as key player in ocular inflammation (in vitro study).	arabinogalactan	0-15	xanthine dehydrogenase	Homo sapiens	83-106
32380019-0	2020	Arabinogalactan and hyaluronic acid in ophthalmic solution: Experimental effect on xanthine oxidoreductase complex as key player in ocular inflammation (in vitro study).	Hyaluronic Acid	20-35	xanthine dehydrogenase	Homo sapiens	83-106
32380019-2	2020	The enzymatic complex of xanthine oxidoreductase (XOR) is involved in the generation of reactive oxygen species (ROS) and uric acid that, in the end, can cause reperfusion injuries, irritation and pathological conditions.	Reactive Oxygen Species	88-111	xanthine dehydrogenase	Homo sapiens	25-48
32380019-2	2020	The enzymatic complex of xanthine oxidoreductase (XOR) is involved in the generation of reactive oxygen species (ROS) and uric acid that, in the end, can cause reperfusion injuries, irritation and pathological conditions.	Reactive Oxygen Species	88-111	xanthine dehydrogenase	Homo sapiens	50-53
32380019-2	2020	The enzymatic complex of xanthine oxidoreductase (XOR) is involved in the generation of reactive oxygen species (ROS) and uric acid that, in the end, can cause reperfusion injuries, irritation and pathological conditions.	Reactive Oxygen Species	113-116	xanthine dehydrogenase	Homo sapiens	25-48
32380019-2	2020	The enzymatic complex of xanthine oxidoreductase (XOR) is involved in the generation of reactive oxygen species (ROS) and uric acid that, in the end, can cause reperfusion injuries, irritation and pathological conditions.	Reactive Oxygen Species	113-116	xanthine dehydrogenase	Homo sapiens	50-53
32380019-2	2020	The enzymatic complex of xanthine oxidoreductase (XOR) is involved in the generation of reactive oxygen species (ROS) and uric acid that, in the end, can cause reperfusion injuries, irritation and pathological conditions.	Uric Acid	122-131	xanthine dehydrogenase	Homo sapiens	25-48
32380019-2	2020	The enzymatic complex of xanthine oxidoreductase (XOR) is involved in the generation of reactive oxygen species (ROS) and uric acid that, in the end, can cause reperfusion injuries, irritation and pathological conditions.	Uric Acid	122-131	xanthine dehydrogenase	Homo sapiens	50-53
31916414-1	2020	AIMS: Uric acid is synthesized by oxidation of hypoxanthine and xanthine using a catalyzing enzyme, xanthine oxidoreductase (XOR), which can be a source of reactive oxygen species.	Uric Acid	6-15	xanthine dehydrogenase	Homo sapiens	100-123
31916414-1	2020	AIMS: Uric acid is synthesized by oxidation of hypoxanthine and xanthine using a catalyzing enzyme, xanthine oxidoreductase (XOR), which can be a source of reactive oxygen species.	Uric Acid	6-15	xanthine dehydrogenase	Homo sapiens	125-128
31916414-1	2020	AIMS: Uric acid is synthesized by oxidation of hypoxanthine and xanthine using a catalyzing enzyme, xanthine oxidoreductase (XOR), which can be a source of reactive oxygen species.	Hypoxanthine	47-59	xanthine dehydrogenase	Homo sapiens	100-123
31916414-1	2020	AIMS: Uric acid is synthesized by oxidation of hypoxanthine and xanthine using a catalyzing enzyme, xanthine oxidoreductase (XOR), which can be a source of reactive oxygen species.	Hypoxanthine	47-59	xanthine dehydrogenase	Homo sapiens	125-128
31916414-1	2020	AIMS: Uric acid is synthesized by oxidation of hypoxanthine and xanthine using a catalyzing enzyme, xanthine oxidoreductase (XOR), which can be a source of reactive oxygen species.	Xanthine	51-59	xanthine dehydrogenase	Homo sapiens	100-123
31916414-1	2020	AIMS: Uric acid is synthesized by oxidation of hypoxanthine and xanthine using a catalyzing enzyme, xanthine oxidoreductase (XOR), which can be a source of reactive oxygen species.	Xanthine	51-59	xanthine dehydrogenase	Homo sapiens	125-128
31916414-1	2020	AIMS: Uric acid is synthesized by oxidation of hypoxanthine and xanthine using a catalyzing enzyme, xanthine oxidoreductase (XOR), which can be a source of reactive oxygen species.	Oxygen	165-171	xanthine dehydrogenase	Homo sapiens	100-123
31916414-1	2020	AIMS: Uric acid is synthesized by oxidation of hypoxanthine and xanthine using a catalyzing enzyme, xanthine oxidoreductase (XOR), which can be a source of reactive oxygen species.	Oxygen	165-171	xanthine dehydrogenase	Homo sapiens	125-128
31916414-6	2020	In 59 subjects with hyperuricemia, 11 (male/female: 11/0) subjects were being treated with an XOR inhibitor and had a significantly higher level of xanthine, but not hypoxanthine, than that in subjects without treatment.	Xanthine	148-156	xanthine dehydrogenase	Homo sapiens	94-97
31916414-9	2020	Whereas, alanine transaminase, hypoxanthine and plasma XOR activity were independent predictors for xanthine, and alanine transaminase, triglycerides and xanthine were independent predictors for plasma XOR activity.	Triglycerides	136-149	xanthine dehydrogenase	Homo sapiens	202-205
31916414-9	2020	Whereas, alanine transaminase, hypoxanthine and plasma XOR activity were independent predictors for xanthine, and alanine transaminase, triglycerides and xanthine were independent predictors for plasma XOR activity.	Xanthine	100-108	xanthine dehydrogenase	Homo sapiens	55-58
32735550-0	2021	Plasma xanthine oxidoreductase activity change over 12 months independently associated with change in serum uric acid level: MedCity21 health examination registry.	Uric Acid	108-117	xanthine dehydrogenase	Homo sapiens	7-30
31955828-2	2020	Xanthine oxidoreductase (XOR) is a rate-limiting enzyme in purine metabolism and is believed to play important roles in coronary atherosclerosis.	Purines	59-65	xanthine dehydrogenase	Homo sapiens	0-23
31578733-4	2020	Mechanistically, XOR physically interacts with USP15, thereby promoting deubiquitination of Kelch Like ECH Associated Protein 1 (KEAP1) to stabilize its expression, which leads to degradation of Nrf2 via ubiquitination and subsequently reactive oxygen species (ROS) accumulation in liver CSCs.	Oxygen	245-251	xanthine dehydrogenase	Homo sapiens	17-20
32404047-6	2020	Transcriptomic data revealed that purine metabolism have a substantial change in gene expression of OTLF and that xanthine dehydrogenase (XDH) is the key regulatory factor.	purine	34-40	xanthine dehydrogenase	Homo sapiens	114-136
32404047-6	2020	Transcriptomic data revealed that purine metabolism have a substantial change in gene expression of OTLF and that xanthine dehydrogenase (XDH) is the key regulatory factor.	purine	34-40	xanthine dehydrogenase	Homo sapiens	138-141
32404047-9	2020	XDH could affect purine metabolism by suppressing the expression of hypoxanthine and xanthine leading to low serum levels of uric acid in OTLF, which could be a focal point in developing new therapeutic methods for OTLF.	purine	17-23	xanthine dehydrogenase	Homo sapiens	0-3
32404047-9	2020	XDH could affect purine metabolism by suppressing the expression of hypoxanthine and xanthine leading to low serum levels of uric acid in OTLF, which could be a focal point in developing new therapeutic methods for OTLF.	Hypoxanthine	68-80	xanthine dehydrogenase	Homo sapiens	0-3
32404047-9	2020	XDH could affect purine metabolism by suppressing the expression of hypoxanthine and xanthine leading to low serum levels of uric acid in OTLF, which could be a focal point in developing new therapeutic methods for OTLF.	Xanthine	72-80	xanthine dehydrogenase	Homo sapiens	0-3
32404047-9	2020	XDH could affect purine metabolism by suppressing the expression of hypoxanthine and xanthine leading to low serum levels of uric acid in OTLF, which could be a focal point in developing new therapeutic methods for OTLF.	Uric Acid	125-134	xanthine dehydrogenase	Homo sapiens	0-3
32067994-1	2020	Xanthinuria is a rare genetic metabolic disorder, the biochemical mechanism of xanthinuria is the disturbance of purine to uric acid metabolism due to the deficiency of xanthine dehydrogenase/xanthine oxidase (XDH/XO) and aldehyde oxidase 1 (AOX1).	purine	113-119	xanthine dehydrogenase	Homo sapiens	210-216
32067994-1	2020	Xanthinuria is a rare genetic metabolic disorder, the biochemical mechanism of xanthinuria is the disturbance of purine to uric acid metabolism due to the deficiency of xanthine dehydrogenase/xanthine oxidase (XDH/XO) and aldehyde oxidase 1 (AOX1).	Uric Acid	123-132	xanthine dehydrogenase	Homo sapiens	210-216
31085741-0	2020	Independent association of plasma xanthine oxidoreductase activity with serum uric acid level based on stable isotope-labeled xanthine and liquid chromatography/triple quadrupole mass spectrometry: MedCity21 health examination registry.	Uric Acid	78-87	xanthine dehydrogenase	Homo sapiens	34-57
31085741-4	2020	Plasma XOR activity was determined using our assay for plasma XOR activity with [13C2,15N2] xanthine and liquid chromatography/triple quadrupole mass spectrometry.	[13c2,15n2] xanthine	80-100	xanthine dehydrogenase	Homo sapiens	7-10
31085741-4	2020	Plasma XOR activity was determined using our assay for plasma XOR activity with [13C2,15N2] xanthine and liquid chromatography/triple quadrupole mass spectrometry.	[13c2,15n2] xanthine	80-100	xanthine dehydrogenase	Homo sapiens	62-65
31085741-7	2020	Multivariable linear regression analysis showed a significant and positive association of serum uric acid level (coefficient: 26.503; 95% confidence interval: 2.06, 50.945; p = 0.035) with plasma XOR activity independent of VFA and HOMA-IR, and also age, gender, alcohol drinking habit, systolic blood pressure, estimated glomerular filtration rate (eGFR), glycated hemoglobin A1c, triglyceride, and adiponectin levels.	Uric Acid	96-105	xanthine dehydrogenase	Homo sapiens	196-199
31085741-7	2020	Multivariable linear regression analysis showed a significant and positive association of serum uric acid level (coefficient: 26.503; 95% confidence interval: 2.06, 50.945; p = 0.035) with plasma XOR activity independent of VFA and HOMA-IR, and also age, gender, alcohol drinking habit, systolic blood pressure, estimated glomerular filtration rate (eGFR), glycated hemoglobin A1c, triglyceride, and adiponectin levels.	Alcohols	263-270	xanthine dehydrogenase	Homo sapiens	196-199
31085741-7	2020	Multivariable linear regression analysis showed a significant and positive association of serum uric acid level (coefficient: 26.503; 95% confidence interval: 2.06, 50.945; p = 0.035) with plasma XOR activity independent of VFA and HOMA-IR, and also age, gender, alcohol drinking habit, systolic blood pressure, estimated glomerular filtration rate (eGFR), glycated hemoglobin A1c, triglyceride, and adiponectin levels.	Triglycerides	382-394	xanthine dehydrogenase	Homo sapiens	196-199
31085741-9	2020	Conclusions Plasma XOR activity was found to be positively associated with serum uric acid level independent of other known confounding factors affecting that level, including gender difference, eGFR, adiponectin level, VFA, and HOMA-IR.	Uric Acid	81-90	xanthine dehydrogenase	Homo sapiens	19-22
31955828-2	2020	Xanthine oxidoreductase (XOR) is a rate-limiting enzyme in purine metabolism and is believed to play important roles in coronary atherosclerosis.	Purines	59-65	xanthine dehydrogenase	Homo sapiens	25-28
32615578-7	2020	In particular, a low XOR activity with an increased serum creatinine level (>1.21 mg/dL) was independently associated with heart failure events (HR 1.937, 95% CI 1.199-3.130).	Creatinine	58-68	xanthine dehydrogenase	Homo sapiens	21-24
32157204-1	2020	Xanthine oxidoreductase (XOR) inhibitor administration reduces uric acid and reactive oxygen species (ROS) production, and also lowers blood pressure (BP).	Uric Acid	63-72	xanthine dehydrogenase	Homo sapiens	0-23
32157204-1	2020	Xanthine oxidoreductase (XOR) inhibitor administration reduces uric acid and reactive oxygen species (ROS) production, and also lowers blood pressure (BP).	Uric Acid	63-72	xanthine dehydrogenase	Homo sapiens	25-28
32157204-1	2020	Xanthine oxidoreductase (XOR) inhibitor administration reduces uric acid and reactive oxygen species (ROS) production, and also lowers blood pressure (BP).	Reactive Oxygen Species	77-100	xanthine dehydrogenase	Homo sapiens	0-23
32157204-1	2020	Xanthine oxidoreductase (XOR) inhibitor administration reduces uric acid and reactive oxygen species (ROS) production, and also lowers blood pressure (BP).	Reactive Oxygen Species	77-100	xanthine dehydrogenase	Homo sapiens	25-28
32157204-1	2020	Xanthine oxidoreductase (XOR) inhibitor administration reduces uric acid and reactive oxygen species (ROS) production, and also lowers blood pressure (BP).	Reactive Oxygen Species	102-105	xanthine dehydrogenase	Homo sapiens	0-23
32157204-1	2020	Xanthine oxidoreductase (XOR) inhibitor administration reduces uric acid and reactive oxygen species (ROS) production, and also lowers blood pressure (BP).	Reactive Oxygen Species	102-105	xanthine dehydrogenase	Homo sapiens	25-28
32157204-9	2020	XOR may contribute to the pathophysiology of higher BP through ROS but not uric acid production, especially in patients with lower oxidative stress.	Reactive Oxygen Species	63-66	xanthine dehydrogenase	Homo sapiens	0-3
31952182-0	2020	Inhibition of Xanthine Oxidoreductase Enhances the Potential of Tyrosine Kinase Inhibitors against Chronic Myeloid Leukemia.	Tyrosine	64-72	xanthine dehydrogenase	Homo sapiens	14-37
31952182-6	2020	To analyze the therapeutic potential of xanthine oxidoreductase (XOR) in CML, we tested the effect of XOR inhibitor allopurinol.	Allopurinol	116-127	xanthine dehydrogenase	Homo sapiens	102-105
33693215-7	2020	Plasma hydrogen peroxide was significantly higher in DM patients with high plasma XOR activity and obesity (>22 kg/m2) than in other patients.	Hydrogen Peroxide	7-24	xanthine dehydrogenase	Homo sapiens	82-85
33693215-9	2020	The increase of XOR is a possible pathway for the production of reactive oxygen species in obese cardiovascular disease patients with DM.	Reactive Oxygen Species	64-87	xanthine dehydrogenase	Homo sapiens	16-19
32108781-0	2020	All-optical neuromorphic XOR operation with inhibitory dynamics of a single photonic spiking neuron based on a VCSEL-SA.	vcsel-sa	111-119	xanthine dehydrogenase	Homo sapiens	25-28
31093763-1	2020	AIMS: Xanthine oxidoreductase (XOR) is an enzyme regulating uric acid synthesis and generation of reactive oxygen species.	Uric Acid	60-69	xanthine dehydrogenase	Homo sapiens	6-29
31093763-1	2020	AIMS: Xanthine oxidoreductase (XOR) is an enzyme regulating uric acid synthesis and generation of reactive oxygen species.	Uric Acid	60-69	xanthine dehydrogenase	Homo sapiens	31-34
31093763-1	2020	AIMS: Xanthine oxidoreductase (XOR) is an enzyme regulating uric acid synthesis and generation of reactive oxygen species.	reactive oxygen	98-113	xanthine dehydrogenase	Homo sapiens	6-29
31093763-1	2020	AIMS: Xanthine oxidoreductase (XOR) is an enzyme regulating uric acid synthesis and generation of reactive oxygen species.	reactive oxygen	98-113	xanthine dehydrogenase	Homo sapiens	31-34
31093763-7	2020	ln-XOR showed positive correlation with HbA1c (r = 0.292, P = 0.013), ALT (r = 0.658, P < 0.001), and ADMA (r = 0.363, P = 0.002).	N,N-dimethylarginine	102-106	xanthine dehydrogenase	Homo sapiens	3-6
31146669-2	2020	In hypertension, is well known the increase in ROS production, mainly by NADPH oxidases and xanthine oxidoreductase, among others, activated by a myriad of mechanisms.	ros	47-50	xanthine dehydrogenase	Homo sapiens	92-115
32071838-3	2020	Here we present two Israeli Arab families affected by type I xanthinuria in whom a c.2164A>T (Lys722Ter) variant in the XDH gene, previously reported in a Turkish family of Turkmen origin, was identified.	lys722ter	94-103	xanthine dehydrogenase	Homo sapiens	120-123
32082372-9	2019	Conclusions: Our results indicate that insulin resistance is associated with plasma XOR activity and that relationship is independent of visceral adiposity and adiponectin level, suggesting that the development of insulin resistance resulting from increased visceral adiposity and/or reduced serum adiponectin contributes to increased uric acid production by stimulating XOR activity.	Uric Acid	335-344	xanthine dehydrogenase	Homo sapiens	84-87
30739714-2	2019	In this study, we demonstrate co-immobilization of xylose dehydrogenase (XDH, EC 1.1.1.175) and alcohol dehydrogenase (ADH, EC 1.1.1.1) using magnetite-silica core-shell particles for simultaneous conversion of xylose into xylonic acid (XA) and in situ cofactor regeneration.	Ferrosoferric Oxide	142-151	xanthine dehydrogenase	Homo sapiens	51-71
30739714-2	2019	In this study, we demonstrate co-immobilization of xylose dehydrogenase (XDH, EC 1.1.1.175) and alcohol dehydrogenase (ADH, EC 1.1.1.1) using magnetite-silica core-shell particles for simultaneous conversion of xylose into xylonic acid (XA) and in situ cofactor regeneration.	Ferrosoferric Oxide	142-151	xanthine dehydrogenase	Homo sapiens	73-76
30739714-2	2019	In this study, we demonstrate co-immobilization of xylose dehydrogenase (XDH, EC 1.1.1.175) and alcohol dehydrogenase (ADH, EC 1.1.1.1) using magnetite-silica core-shell particles for simultaneous conversion of xylose into xylonic acid (XA) and in situ cofactor regeneration.	Silicon Dioxide	152-158	xanthine dehydrogenase	Homo sapiens	51-71
30739714-2	2019	In this study, we demonstrate co-immobilization of xylose dehydrogenase (XDH, EC 1.1.1.175) and alcohol dehydrogenase (ADH, EC 1.1.1.1) using magnetite-silica core-shell particles for simultaneous conversion of xylose into xylonic acid (XA) and in situ cofactor regeneration.	Silicon Dioxide	152-158	xanthine dehydrogenase	Homo sapiens	73-76
30739714-2	2019	In this study, we demonstrate co-immobilization of xylose dehydrogenase (XDH, EC 1.1.1.175) and alcohol dehydrogenase (ADH, EC 1.1.1.1) using magnetite-silica core-shell particles for simultaneous conversion of xylose into xylonic acid (XA) and in situ cofactor regeneration.	Xylose	51-57	xanthine dehydrogenase	Homo sapiens	73-76
31350908-7	2019	This muscle nitrate reservoir has been found to be an important source of nitrite and nitric oxide (NO) via its reduction by tissue xanthine oxidoreductase.	Nitrates	12-19	xanthine dehydrogenase	Homo sapiens	132-155
31350908-7	2019	This muscle nitrate reservoir has been found to be an important source of nitrite and nitric oxide (NO) via its reduction by tissue xanthine oxidoreductase.	Nitrites	74-81	xanthine dehydrogenase	Homo sapiens	132-155
31350908-7	2019	This muscle nitrate reservoir has been found to be an important source of nitrite and nitric oxide (NO) via its reduction by tissue xanthine oxidoreductase.	Nitric Oxide	86-98	xanthine dehydrogenase	Homo sapiens	132-155
31130575-1	2019	Xanthine oxidoreductase (XOR), an enzyme of uric acid formation from hypoxanthine and xanthine, is recognized as a source of oxidative stress.	Uric Acid	44-53	xanthine dehydrogenase	Homo sapiens	0-23
31754153-3	2019	In this study, we report that febuxostat, an inhibitor of XOR, suppressed NLRP3 inflammasome-mediated IL-1beta secretion and cell death by two mechanisms: in a mitochondrial ROS (mitoROS)-dependent and mitoROS-independent manner.	febuxostat	30-40	xanthine dehydrogenase	Homo sapiens	58-61
33693087-4	2019	XOR generates reactive oxygen species (ROS) that lead to atrial structural remodeling via inflammation.	Reactive Oxygen Species	14-37	xanthine dehydrogenase	Homo sapiens	0-3
33693087-4	2019	XOR generates reactive oxygen species (ROS) that lead to atrial structural remodeling via inflammation.	Reactive Oxygen Species	39-42	xanthine dehydrogenase	Homo sapiens	0-3
31496508-2	2019	Xanthine oxidoreductase (XOR) inhibitors inhibit uric acid (UA) production and may be treatment options for hyperuricemia patients.	Uric Acid	49-58	xanthine dehydrogenase	Homo sapiens	0-23
31496508-2	2019	Xanthine oxidoreductase (XOR) inhibitors inhibit uric acid (UA) production and may be treatment options for hyperuricemia patients.	Uric Acid	49-58	xanthine dehydrogenase	Homo sapiens	25-28
31496508-2	2019	Xanthine oxidoreductase (XOR) inhibitors inhibit uric acid (UA) production and may be treatment options for hyperuricemia patients.	Uric Acid	60-62	xanthine dehydrogenase	Homo sapiens	0-23
31496508-2	2019	Xanthine oxidoreductase (XOR) inhibitors inhibit uric acid (UA) production and may be treatment options for hyperuricemia patients.	Uric Acid	60-62	xanthine dehydrogenase	Homo sapiens	25-28
31556223-1	2019	Xanthine oxidoreductase (XOR) inhibitors, such as allopurinol and febuxostat, inhibit the catalysis of serum uric acid (SUA) synthesis.	Allopurinol	50-61	xanthine dehydrogenase	Homo sapiens	0-23
31556223-1	2019	Xanthine oxidoreductase (XOR) inhibitors, such as allopurinol and febuxostat, inhibit the catalysis of serum uric acid (SUA) synthesis.	febuxostat	66-76	xanthine dehydrogenase	Homo sapiens	0-23
31556223-1	2019	Xanthine oxidoreductase (XOR) inhibitors, such as allopurinol and febuxostat, inhibit the catalysis of serum uric acid (SUA) synthesis.	Uric Acid	109-118	xanthine dehydrogenase	Homo sapiens	0-23
31130575-1	2019	Xanthine oxidoreductase (XOR), an enzyme of uric acid formation from hypoxanthine and xanthine, is recognized as a source of oxidative stress.	Uric Acid	44-53	xanthine dehydrogenase	Homo sapiens	25-28
31130575-1	2019	Xanthine oxidoreductase (XOR), an enzyme of uric acid formation from hypoxanthine and xanthine, is recognized as a source of oxidative stress.	Hypoxanthine	69-81	xanthine dehydrogenase	Homo sapiens	0-23
31130575-1	2019	Xanthine oxidoreductase (XOR), an enzyme of uric acid formation from hypoxanthine and xanthine, is recognized as a source of oxidative stress.	Hypoxanthine	69-81	xanthine dehydrogenase	Homo sapiens	25-28
31130575-1	2019	Xanthine oxidoreductase (XOR), an enzyme of uric acid formation from hypoxanthine and xanthine, is recognized as a source of oxidative stress.	Xanthine	73-81	xanthine dehydrogenase	Homo sapiens	0-23
31130575-1	2019	Xanthine oxidoreductase (XOR), an enzyme of uric acid formation from hypoxanthine and xanthine, is recognized as a source of oxidative stress.	Xanthine	73-81	xanthine dehydrogenase	Homo sapiens	25-28
31130575-3	2019	We investigated longitudinal change in plasma XOR activity, which was determined by using mass spectrometry and liquid chromatography to detect [13C2, 15N2]-uric acid using [13C2, 15N2]-xanthine as a substrate, in 511 subjects (male/female: 244/267) of the Tanno-Sobetsu Study in the years 2016 and 2017.	[13c2, 15n2]-	144-157	xanthine dehydrogenase	Homo sapiens	46-49
31130575-3	2019	We investigated longitudinal change in plasma XOR activity, which was determined by using mass spectrometry and liquid chromatography to detect [13C2, 15N2]-uric acid using [13C2, 15N2]-xanthine as a substrate, in 511 subjects (male/female: 244/267) of the Tanno-Sobetsu Study in the years 2016 and 2017.	Uric Acid	157-166	xanthine dehydrogenase	Homo sapiens	46-49
31130575-3	2019	We investigated longitudinal change in plasma XOR activity, which was determined by using mass spectrometry and liquid chromatography to detect [13C2, 15N2]-uric acid using [13C2, 15N2]-xanthine as a substrate, in 511 subjects (male/female: 244/267) of the Tanno-Sobetsu Study in the years 2016 and 2017.	Xanthine	186-194	xanthine dehydrogenase	Homo sapiens	46-49
31569698-0	2019	Co-Immobilization of Glucose Dehydrogenase and Xylose Dehydrogenase as a New Approach for Simultaneous Production of Gluconic and Xylonic Acid.	gluconic acid	117-125	xanthine dehydrogenase	Homo sapiens	47-67
22934314-5	1993	MANAGEMENT: Treatment of manifestations: Treatment with the xanthine dehydrogenase (XDH) inhibitor allopurinol can prevent or dissolve kidney stones and improve kidney function, even in individuals with advanced CKD.	Allopurinol	99-110	xanthine dehydrogenase	Homo sapiens	84-87
22934314-6	1993	The XDH inhibitor febuxostat is an alternative option for those allergic to or intolerant of allopurinol.	Febuxostat	18-28	xanthine dehydrogenase	Homo sapiens	4-7
22934314-6	1993	The XDH inhibitor febuxostat is an alternative option for those allergic to or intolerant of allopurinol.	Allopurinol	93-104	xanthine dehydrogenase	Homo sapiens	4-7
22934314-13	1993	Agents/circumstances to avoid: Azathioprine should be avoided by individuals taking XDH inhibitors.	Azathioprine	31-43	xanthine dehydrogenase	Homo sapiens	84-87
22934314-5	1993	MANAGEMENT: Treatment of manifestations: Treatment with the xanthine dehydrogenase (XDH) inhibitor allopurinol can prevent or dissolve kidney stones and improve kidney function, even in individuals with advanced CKD.	Allopurinol	99-110	xanthine dehydrogenase	Homo sapiens	60-82
31569698-0	2019	Co-Immobilization of Glucose Dehydrogenase and Xylose Dehydrogenase as a New Approach for Simultaneous Production of Gluconic and Xylonic Acid.	carbamoylpolyoxamic acid	130-142	xanthine dehydrogenase	Homo sapiens	47-67
31569698-3	2019	Therefore, in this work we have undertaken a study focused on the co-immobilization of glucose dehydrogenase (GDH, EC 1.1.1.118) and xylose dehydrogenase (XDH, EC 1.1.1.175) using mesoporous Santa Barbara Amorphous silica (SBA 15) for the simultaneous production of gluconic acid and xylonic acid.	Silicon Dioxide	215-221	xanthine dehydrogenase	Homo sapiens	133-153
31569698-3	2019	Therefore, in this work we have undertaken a study focused on the co-immobilization of glucose dehydrogenase (GDH, EC 1.1.1.118) and xylose dehydrogenase (XDH, EC 1.1.1.175) using mesoporous Santa Barbara Amorphous silica (SBA 15) for the simultaneous production of gluconic acid and xylonic acid.	Silicon Dioxide	215-221	xanthine dehydrogenase	Homo sapiens	155-158
31569698-3	2019	Therefore, in this work we have undertaken a study focused on the co-immobilization of glucose dehydrogenase (GDH, EC 1.1.1.118) and xylose dehydrogenase (XDH, EC 1.1.1.175) using mesoporous Santa Barbara Amorphous silica (SBA 15) for the simultaneous production of gluconic acid and xylonic acid.	gluconic acid	266-279	xanthine dehydrogenase	Homo sapiens	133-153
31569698-3	2019	Therefore, in this work we have undertaken a study focused on the co-immobilization of glucose dehydrogenase (GDH, EC 1.1.1.118) and xylose dehydrogenase (XDH, EC 1.1.1.175) using mesoporous Santa Barbara Amorphous silica (SBA 15) for the simultaneous production of gluconic acid and xylonic acid.	gluconic acid	266-279	xanthine dehydrogenase	Homo sapiens	155-158
31569698-3	2019	Therefore, in this work we have undertaken a study focused on the co-immobilization of glucose dehydrogenase (GDH, EC 1.1.1.118) and xylose dehydrogenase (XDH, EC 1.1.1.175) using mesoporous Santa Barbara Amorphous silica (SBA 15) for the simultaneous production of gluconic acid and xylonic acid.	carbamoylpolyoxamic acid	284-296	xanthine dehydrogenase	Homo sapiens	133-153
31569698-3	2019	Therefore, in this work we have undertaken a study focused on the co-immobilization of glucose dehydrogenase (GDH, EC 1.1.1.118) and xylose dehydrogenase (XDH, EC 1.1.1.175) using mesoporous Santa Barbara Amorphous silica (SBA 15) for the simultaneous production of gluconic acid and xylonic acid.	carbamoylpolyoxamic acid	284-296	xanthine dehydrogenase	Homo sapiens	155-158
31569698-5	2019	A GDH:XDH ratio equal to 1:5 was the most suitable for the conversion of xylose and glucose, as the reaction yield reached over 90% for both monosaccharides after 45 min of the process.	Xylose	73-79	xanthine dehydrogenase	Homo sapiens	6-9
31569698-5	2019	A GDH:XDH ratio equal to 1:5 was the most suitable for the conversion of xylose and glucose, as the reaction yield reached over 90% for both monosaccharides after 45 min of the process.	Glucose	84-91	xanthine dehydrogenase	Homo sapiens	6-9
31569698-5	2019	A GDH:XDH ratio equal to 1:5 was the most suitable for the conversion of xylose and glucose, as the reaction yield reached over 90% for both monosaccharides after 45 min of the process.	Monosaccharides	141-156	xanthine dehydrogenase	Homo sapiens	6-9
30516339-1	2019	AIMS/INTRODUCTION: Xanthine oxidoreductase (XOR) is a rate-limiting enzyme that catalyzes uric acid formation in the purine metabolism, is involved in an increase in reactive oxygen species.	Uric Acid	90-99	xanthine dehydrogenase	Homo sapiens	19-42
31267233-4	2019	In addition to MDH, the other PDHs including RDH, GDH, ArDH, and XDH are also important tools for the production of rare sugars including D-tagatose, allitol, D-xylulose, and L-xylulose.	allitol	150-157	xanthine dehydrogenase	Homo sapiens	65-68
31267233-4	2019	In addition to MDH, the other PDHs including RDH, GDH, ArDH, and XDH are also important tools for the production of rare sugars including D-tagatose, allitol, D-xylulose, and L-xylulose.	L-xylulose	175-185	xanthine dehydrogenase	Homo sapiens	65-68
31103463-5	2019	However, XDH/XO inhibition by specific small chemical inhibitors or gene silencing reduced total ROS levels and protected cells from apoptosis induced by Alternol.	ros	97-100	xanthine dehydrogenase	Homo sapiens	9-12
31103463-5	2019	However, XDH/XO inhibition by specific small chemical inhibitors or gene silencing reduced total ROS levels and protected cells from apoptosis induced by Alternol.	Alternol	154-162	xanthine dehydrogenase	Homo sapiens	9-12
31103463-6	2019	Further analysis revealed that Alternol treatment significantly enhanced XDH oxidative activity and induced a strong protein oxidation-related damage in malignant but not benign cells.	Alternol	31-39	xanthine dehydrogenase	Homo sapiens	73-76
31103463-8	2019	Cell-based protein-ligand engagement and in-silicon docking analysis showed that Alternol interacts with XDH protein on the catalytic domain with two amino acid residues away from its substrate binding sites.	Silicon	44-51	xanthine dehydrogenase	Homo sapiens	105-108
31103463-8	2019	Cell-based protein-ligand engagement and in-silicon docking analysis showed that Alternol interacts with XDH protein on the catalytic domain with two amino acid residues away from its substrate binding sites.	Alternol	81-89	xanthine dehydrogenase	Homo sapiens	105-108
31103463-9	2019	Taken together, our data demonstrate that Alternol treatment enhances XDH oxidative activity, leading to ROS-dependent apoptotic cell death.	Alternol	42-50	xanthine dehydrogenase	Homo sapiens	70-73
31103463-9	2019	Taken together, our data demonstrate that Alternol treatment enhances XDH oxidative activity, leading to ROS-dependent apoptotic cell death.	ros	105-108	xanthine dehydrogenase	Homo sapiens	70-73
31116490-4	2019	We tested allopurinol, an FDA-approved drug that inhibits XDH, on human non-small-cell lung cancer (NSCLC) cell lines obtained from the Broad Institute Cancer Cell Line Encyclopedia and identified sensitive and resistant cell lines.	Allopurinol	10-21	xanthine dehydrogenase	Homo sapiens	58-61
31267233-4	2019	In addition to MDH, the other PDHs including RDH, GDH, ArDH, and XDH are also important tools for the production of rare sugars including D-tagatose, allitol, D-xylulose, and L-xylulose.	Sugars	121-127	xanthine dehydrogenase	Homo sapiens	65-68
31267233-4	2019	In addition to MDH, the other PDHs including RDH, GDH, ArDH, and XDH are also important tools for the production of rare sugars including D-tagatose, allitol, D-xylulose, and L-xylulose.	tagatose	138-148	xanthine dehydrogenase	Homo sapiens	65-68
30516339-1	2019	AIMS/INTRODUCTION: Xanthine oxidoreductase (XOR) is a rate-limiting enzyme that catalyzes uric acid formation in the purine metabolism, is involved in an increase in reactive oxygen species.	Uric Acid	90-99	xanthine dehydrogenase	Homo sapiens	44-47
30516339-1	2019	AIMS/INTRODUCTION: Xanthine oxidoreductase (XOR) is a rate-limiting enzyme that catalyzes uric acid formation in the purine metabolism, is involved in an increase in reactive oxygen species.	purine	117-123	xanthine dehydrogenase	Homo sapiens	19-42
30516339-1	2019	AIMS/INTRODUCTION: Xanthine oxidoreductase (XOR) is a rate-limiting enzyme that catalyzes uric acid formation in the purine metabolism, is involved in an increase in reactive oxygen species.	purine	117-123	xanthine dehydrogenase	Homo sapiens	44-47
30516339-1	2019	AIMS/INTRODUCTION: Xanthine oxidoreductase (XOR) is a rate-limiting enzyme that catalyzes uric acid formation in the purine metabolism, is involved in an increase in reactive oxygen species.	Reactive Oxygen Species	166-189	xanthine dehydrogenase	Homo sapiens	19-42
30516339-1	2019	AIMS/INTRODUCTION: Xanthine oxidoreductase (XOR) is a rate-limiting enzyme that catalyzes uric acid formation in the purine metabolism, is involved in an increase in reactive oxygen species.	Reactive Oxygen Species	166-189	xanthine dehydrogenase	Homo sapiens	44-47
30516339-6	2019	Plasma XOR activity was positively correlated with concentrations of FABP4 (r = 0.192, P &lt; 0.001) and FGF21 (r = 0.208, P &lt; 0.001), homeostasis model assessment of insulin resistance as an index of insulin resistance and uric acid, and was negatively correlated with adiponectin level (r = -0.243, P = 0.001).	Uric Acid	227-236	xanthine dehydrogenase	Homo sapiens	7-10
30516339-7	2019	Multivariate regression analyses showed that levels of adiponectin, FABP4 and FGF21 were independent determinants of plasma XOR activity after adjusting age, sex, uric acid and homeostasis model assessment of insulin resistance.	Uric Acid	163-172	xanthine dehydrogenase	Homo sapiens	124-127
31140171-4	2019	Herein, we describe the molecular aspects of nitrated fatty acid-associated inactivation of XOR, identify specificity via structure function relationships and discuss XOR as a crucial component of the anti-inflammatory portfolio of nitrated fatty acids.	nitrated fatty acids	232-252	xanthine dehydrogenase	Homo sapiens	167-170
31126092-5	2019	In addition, we investigated an association between xanthine dehydrogenase gene and sUA and their combined associations on the risk of hypertension.	sua	84-87	xanthine dehydrogenase	Homo sapiens	52-74
30837873-8	2019	Similarly, beneficial effects have been seen in heart, skeletal muscle, or brain after treatment with allopurinol or febuxostat to inhibit xanthine oxidoreductase, which catalyzes hypoxanthine -&gt; xanthine and xanthine -&gt; urate reactions.	Allopurinol	102-113	xanthine dehydrogenase	Homo sapiens	139-162
30837873-8	2019	Similarly, beneficial effects have been seen in heart, skeletal muscle, or brain after treatment with allopurinol or febuxostat to inhibit xanthine oxidoreductase, which catalyzes hypoxanthine -&gt; xanthine and xanthine -&gt; urate reactions.	Febuxostat	117-127	xanthine dehydrogenase	Homo sapiens	139-162
30837873-8	2019	Similarly, beneficial effects have been seen in heart, skeletal muscle, or brain after treatment with allopurinol or febuxostat to inhibit xanthine oxidoreductase, which catalyzes hypoxanthine -&gt; xanthine and xanthine -&gt; urate reactions.	Hypoxanthine	180-192	xanthine dehydrogenase	Homo sapiens	139-162
30837873-8	2019	Similarly, beneficial effects have been seen in heart, skeletal muscle, or brain after treatment with allopurinol or febuxostat to inhibit xanthine oxidoreductase, which catalyzes hypoxanthine -&gt; xanthine and xanthine -&gt; urate reactions.	Xanthine	184-192	xanthine dehydrogenase	Homo sapiens	139-162
30837873-8	2019	Similarly, beneficial effects have been seen in heart, skeletal muscle, or brain after treatment with allopurinol or febuxostat to inhibit xanthine oxidoreductase, which catalyzes hypoxanthine -&gt; xanthine and xanthine -&gt; urate reactions.	Uric Acid	227-232	xanthine dehydrogenase	Homo sapiens	139-162
30837873-10	2019	Recent clinical studies indicated that treatment with xanthine oxidoreductase inhibitors plus inosine had the strongest impact for increasing the pool of salvageable purines and leading to increased ATP levels in humans, thereby suggesting that this combination is more beneficial than a xanthine oxidoreductase inhibitor alone to treat disorders with ATP deficiency.	Inosine	94-101	xanthine dehydrogenase	Homo sapiens	288-311
30837873-10	2019	Recent clinical studies indicated that treatment with xanthine oxidoreductase inhibitors plus inosine had the strongest impact for increasing the pool of salvageable purines and leading to increased ATP levels in humans, thereby suggesting that this combination is more beneficial than a xanthine oxidoreductase inhibitor alone to treat disorders with ATP deficiency.	Purines	166-173	xanthine dehydrogenase	Homo sapiens	54-77
30837873-10	2019	Recent clinical studies indicated that treatment with xanthine oxidoreductase inhibitors plus inosine had the strongest impact for increasing the pool of salvageable purines and leading to increased ATP levels in humans, thereby suggesting that this combination is more beneficial than a xanthine oxidoreductase inhibitor alone to treat disorders with ATP deficiency.	Adenosine Triphosphate	199-202	xanthine dehydrogenase	Homo sapiens	54-77
30837873-10	2019	Recent clinical studies indicated that treatment with xanthine oxidoreductase inhibitors plus inosine had the strongest impact for increasing the pool of salvageable purines and leading to increased ATP levels in humans, thereby suggesting that this combination is more beneficial than a xanthine oxidoreductase inhibitor alone to treat disorders with ATP deficiency.	Adenosine Triphosphate	352-355	xanthine dehydrogenase	Homo sapiens	54-77
30576922-4	2019	The reactive oxygen and nitrogen species and the uric acid derived from XOR concur to the development of hypertension, dyslipidemia and insulin resistance and participate in both cell transformation and proliferation, as well as in the progression and metastasis process.	Uric Acid	49-58	xanthine dehydrogenase	Homo sapiens	72-75
31140171-0	2019	Diminishing Inflammation by Reducing Oxidant Generation: Nitrated Fatty Acid-Mediated Inactivation of Xanthine Oxidoreductase.	nitrated fatty acid	57-76	xanthine dehydrogenase	Homo sapiens	102-125
31140171-3	2019	An alternative process in which nitrated fatty acids may extend anti-inflammatory actions is via inactivation of XOR, a process that is more effective than allo/oxypurinol-mediated inhibition.	nitrated fatty acids	32-52	xanthine dehydrogenase	Homo sapiens	113-116
31140171-3	2019	An alternative process in which nitrated fatty acids may extend anti-inflammatory actions is via inactivation of XOR, a process that is more effective than allo/oxypurinol-mediated inhibition.	Oxypurinol	161-171	xanthine dehydrogenase	Homo sapiens	113-116
31140171-4	2019	Herein, we describe the molecular aspects of nitrated fatty acid-associated inactivation of XOR, identify specificity via structure function relationships and discuss XOR as a crucial component of the anti-inflammatory portfolio of nitrated fatty acids.	nitrated fatty acid	45-64	xanthine dehydrogenase	Homo sapiens	92-95
30620450-6	2019	The multivariate logistic regression model showed that serum uric acid (per 1.0 mg/dL increase, odds ratio: 1.280; 95% confidence interval: 1.066-1.536; P = 0.008) and lactate levels (per 1.0 mmol/L increase, odds ratio: 1.239; 95% confidence interval: 1.040-1.475; P = 0.016) were independently associated with high plasma XOR activity (&gt;300 pg/h/mL) during the acute phase of AHF.	Uric Acid	61-70	xanthine dehydrogenase	Homo sapiens	324-327
30769179-4	2019	Commercially, there are three kinds of agents targeting at urate-lowering, xanthine oxidoreductase inhibitor which prevents the production of UA, uricosuric which increases the concentration of UA in urine thus decreasing serum UA level, and uricase which converts UA to allantoin resulting in the dramatic decrement of serum UA.	Uric Acid	142-144	xanthine dehydrogenase	Homo sapiens	75-98
30559212-7	2019	Mechanistically, the salutary metabolic effects of nitrate and nitrite can be ascribed to nitrite-derived formation of NO species and activation of soluble guanylyl cyclase, where xanthine oxidoreductase is proposed to mediate the reduction of nitrite.	Nitrates	51-58	xanthine dehydrogenase	Homo sapiens	180-203
30559212-7	2019	Mechanistically, the salutary metabolic effects of nitrate and nitrite can be ascribed to nitrite-derived formation of NO species and activation of soluble guanylyl cyclase, where xanthine oxidoreductase is proposed to mediate the reduction of nitrite.	Nitrites	63-70	xanthine dehydrogenase	Homo sapiens	180-203
31805226-7	2019	XOR, activated after modification of the redox environment by either RBC-NOX or RBC-NOS activity, concurred to the overall oxidative/nitrosative stress by either oxysterols.	arthrofactin	162-172	xanthine dehydrogenase	Homo sapiens	0-3
31805226-4	2019	The activity of individual 7-KC (7 muM) and TRIOL (2, muM) on ROS-generating enzymes and relevant activation pathways was assayed in the presence of Diphenylene iodonium chloride (DPI), N-nitro-L-arginine methyl ester (L-NAME), allopurinol, NSC23766 and LY294002, inhibitors in this order of RBC-NOX, RBC-NOS, XOR and upstream regulatory proteins Rac GTPase and phosphoinositide3 Kinase (PI3K); hemoglobin oxidation from spectrophotometric analysis.	Cholesterol	27-31	xanthine dehydrogenase	Homo sapiens	310-313
29936631-2	2019	Xanthine oxidoreductase (XOR) plays a pivotal role in producing both uric acid and ROS.	Uric Acid	69-78	xanthine dehydrogenase	Homo sapiens	0-23
29936631-2	2019	Xanthine oxidoreductase (XOR) plays a pivotal role in producing both uric acid and ROS.	Uric Acid	69-78	xanthine dehydrogenase	Homo sapiens	25-28
29936631-2	2019	Xanthine oxidoreductase (XOR) plays a pivotal role in producing both uric acid and ROS.	Reactive Oxygen Species	83-86	xanthine dehydrogenase	Homo sapiens	0-23
29936631-2	2019	Xanthine oxidoreductase (XOR) plays a pivotal role in producing both uric acid and ROS.	Reactive Oxygen Species	83-86	xanthine dehydrogenase	Homo sapiens	25-28
29936631-5	2019	We measured XOR activity in 104 patients suspected for CAS, who presented without significant coronary artery stenosis and underwent intracoronary acetylcholine provocation tests.	Acetylcholine	147-160	xanthine dehydrogenase	Homo sapiens	12-15
30740729-2	2019	UA excess, causing renal failure, is commonly decreased by xanthine oxidoreductase (XOR) inhibitors, such as allopurinol, yielding a xanthine and hypoxanthine increase.	Uric Acid	0-2	xanthine dehydrogenase	Homo sapiens	59-82
30740729-2	2019	UA excess, causing renal failure, is commonly decreased by xanthine oxidoreductase (XOR) inhibitors, such as allopurinol, yielding a xanthine and hypoxanthine increase.	Uric Acid	0-2	xanthine dehydrogenase	Homo sapiens	84-87
30740729-2	2019	UA excess, causing renal failure, is commonly decreased by xanthine oxidoreductase (XOR) inhibitors, such as allopurinol, yielding a xanthine and hypoxanthine increase.	Allopurinol	109-120	xanthine dehydrogenase	Homo sapiens	59-82
30740729-2	2019	UA excess, causing renal failure, is commonly decreased by xanthine oxidoreductase (XOR) inhibitors, such as allopurinol, yielding a xanthine and hypoxanthine increase.	Allopurinol	109-120	xanthine dehydrogenase	Homo sapiens	84-87
30740729-2	2019	UA excess, causing renal failure, is commonly decreased by xanthine oxidoreductase (XOR) inhibitors, such as allopurinol, yielding a xanthine and hypoxanthine increase.	Xanthine	59-67	xanthine dehydrogenase	Homo sapiens	84-87
30740729-2	2019	UA excess, causing renal failure, is commonly decreased by xanthine oxidoreductase (XOR) inhibitors, such as allopurinol, yielding a xanthine and hypoxanthine increase.	Hypoxanthine	146-158	xanthine dehydrogenase	Homo sapiens	59-82
30740729-2	2019	UA excess, causing renal failure, is commonly decreased by xanthine oxidoreductase (XOR) inhibitors, such as allopurinol, yielding a xanthine and hypoxanthine increase.	Hypoxanthine	146-158	xanthine dehydrogenase	Homo sapiens	84-87
30740729-8	2019	The therapeutic aim is to limit the administration of XOR inhibitors to LND patients by supplying the PNP inhibitor in low doses, avoiding d-nucleoside toxicity.	d-nucleoside	139-151	xanthine dehydrogenase	Homo sapiens	54-57