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(E)-3-(2,2-difluoroethoxy)-N-(7-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-2-methylhept-5-en-2-yl)benzenesulfonamide
-
(E)-3-(cyclopentyloxy)-N-(7-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-2-methylhept-5-en-2-yl)benzenesulfonamide
-
(E)-3-(cyclopropylmethoxy)-N-(7-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-2-methylhept-5-en-2-yl)benzenesulfonamide
-
(E)-N-(7-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-2-methylhept-5-en-2-yl)-3-methoxybenzenesulfonamide
-
(E)-N-(7-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-2-methylhept-5-en-2-yl)benzenesulfonamide
-
(R)-1-(3-(2-(hydroxydiphenylmethyl)-pyrrolidin-1-ylsulfonyl)propyl)pyrimidine-2,4(1H,3H)-dione
-
(R)-1-(4-(2-(hydroxydiphenylmethyl)-pyrrolidin-1-yl)-4-oxobutyl)pyrimidine-2,4(1H,3H)-dione
-
(R)-N-(1-(3-(2,2-difluoroethoxy)phenyl)ethyl)-4-((2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl)benzenesulfonamide
-
(R)-N-(1-(3-(cyclopentyloxy)phenyl)ethyl)-4-((2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl)benzenesulfonamide
-
(R)-N-(1-(3-(cyclopropylmethoxy)phenyl)ethyl)-4-((2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl)-benzenesulfonamide
-
(R,E)-N-(1-(3-(2,2-difluoroethoxy)phenyl)ethyl)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)pent-3-ene-1-sulfonamide
-
(R,E)-N-(1-(3-(cyclopentyloxy)phenyl)ethyl)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)pent-3-ene-1-sulfonamide
-
(R,E)-N-(1-(3-(cyclopropylmethoxy)phenyl)ethyl)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)pent-3-ene-1-sulfonamide
-
(S)-1-(4-(2-(hydroxydiphenylmethyl)-pyrrolidin-1-yl)-4-oxobutyl)pyrimidine-2,4(1H,3H)-dione
-
1-(3-[[(2S)-2-[hydroxy[bis(2-methoxyphenyl)]methyl]pyrrolidin-1-yl]sulfonyl]propyl)pyrimidine-2,4(1H,3H)-dione
-
1-(3-[[(2S)-2-[hydroxy[bis(3-methoxyphenyl)]methyl]pyrrolidin-1-yl]sulfonyl]propyl)pyrimidine-2,4(1H,3H)-dione
-
1-(4-[(2S)-2-[bis(3-chlorophenyl)(hydroxy)methyl]pyrrolidin-1-yl]-4-oxobutyl)pyrimidine-2,4(1H,3H)-dione
-
1-(4-[(2S)-2-[bis(3-fluorophenyl)(hydroxy)methyl]pyrrolidin-1-yl]-4-oxobutyl)pyrimidine-2,4(1H,3H)-dione
-
1-(4-[(2S)-2-[bis(4-chlorophenyl)(hydroxy)methyl]pyrrolidin-1-yl]-4-oxobutyl)pyrimidine-2,4(1H,3H)-dione
-
1-(4-[(2S)-2-[bis(4-fluorophenyl)(hydroxy)methyl]pyrrolidin-1-yl]-4-oxobutyl)pyrimidine-2,4(1H,3H)-dione
-
1-[(1E,8E)-5-([[(E)-(3,4-dihydroxy-5-methoxybenzylidene)amino]oxy]methyl)-1-(3,4-dihydroxy-5-methoxyphenyl)-3,7-dioxa-2,8-diazadeca-1,8-dien-10-yl]pyrimidine-2,4(1H,3H)-dione
-
1-[(1Z,8E)-5-([[(E)-(3,4-dihydroxy-5-methoxybenzylidene)amino]oxy]methyl)-1-(3,4-dihydroxy-5-methoxyphenyl)-3,7-dioxa-2,8-diazadeca-1,8-dien-10-yl]pyrimidine-2,4(1H,3H)-dione
-
1-[3-(4-benzylpiperidin-1-yl)-3-oxopropyl]pyrimidine-2,4(1H,3H)-dione
-
1-[3-([(2R)-2-[hydroxy(diphenyl)methyl]pyrrolidin-1-yl]sulfonyl)propyl]pyrimidine-2,4(1H,3H)-dione
-
1-[3-([(2S)-2-[bis(3-fluorophenyl)(hydroxy)methyl]pyrrolidin-1-yl]sulfonyl)propyl]pyrimidine-2,4(1H,3H)-dione
-
1-[3-([(2S)-2-[bis(4-fluorophenyl)(hydroxy)methyl]pyrrolidin-1-yl]sulfonyl)propyl]pyrimidine-2,4(1H,3H)-dione
-
1-[3-[(2S)-2-(diphenylmethyl)pyrrolidin-1-yl]-3-oxopropyl]pyrimidine-2,4(1H,3H)-dione
-
1-[4-[(2S)-2-(diphenylmethyl)pyrrolidin-1-yl]-4-oxobutyl]pyrimidine-2,4(1H,3H)-dione
-
1-[4-[(2S)-2-[bis[2-(benzyloxy)phenyl](hydroxy)methyl]pyrrolidin-1-yl]-4-oxobutyl]pyrimidine-2,4(1H,3H)-dione
-
1-[4-[(2S)-2-[bis[3-(benzyloxy)phenyl](hydroxy)methyl]pyrrolidin-1-yl]-4-oxobutyl]pyrimidine-2,4(1H,3H)-dione
-
1-[4-[(2S)-2-[bis[4-(benzyloxy)phenyl](hydroxy)methyl]pyrrolidin-1-yl]-4-oxobutyl]pyrimidine-2,4(1H,3H)-dione
-
1-[4-[(2S)-2-[hydroxy[di(thiophen-3-yl)]methyl]pyrrolidin-1-yl]-4-oxobutyl]pyrimidine-2,4(1H,3H)-dione
-
1-[[2-(trityloxy)ethoxy]methyl]pyrimidine-2,4(1H,3H)-dione
2'-deoxy-5'-O-trityluridine
-
2'-deoxyuridine 5'-(alpha,beta-imido)triphosphate
3'-deoxy-5'-O-(hydroxy{[hydroxy(phosphonooxy)phosphoryl]amino}phosphoryl)uridine
-
3-(2,2-difluoroethoxy)-N-(2-(4-((2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl)phenyl)propan-2-yl)-benzenesulfonamide
-
3-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(2,4,4-trimethylpentan-2-yl)propanamide
-
3-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(2-methylbutan-2-yl)propanamide
-
3-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(2-phenylethyl)propanamide
-
3-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(3-ethylhexan-3-yl)propanamide
-
3-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(3-phenylpropyl)propanamide
-
3-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(diphenylmethyl)propanamide
-
3-(cyclopentyloxy)-N-(2-(4-((2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl)phenyl)propan-2-yl)-benzenesulfonamide
-
3-(cyclopropylmethoxy)-N-(2-(4-((2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl)phenyl)propan-2-yl)-benzenesulfonamide
-
3-(cyclopropylmethoxy)-N-[5-[(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methoxy]-2-methylpentan-2-yl]benzenesulfonamide
-
4-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(1-hydroxy-2-methyl-1,1-diphenylpropan-2-yl)butanamide
-
4-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(1-hydroxy-2-methylpropan-2-yl)butanamide
-
4-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(2,2-diphenylethyl)-N-methylbutanamide
-
4-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(2,2-diphenylethyl)butanamide
-
4-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(2,4,4-trimethylpentan-2-yl)butanamide
-
4-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(2-hydroxy-2,2-diphenylethyl)-N-methylbutanamide
-
4-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(2-methyl-1-phenylpropan-2-yl)butanamide
-
4-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(2-methyl-4-phenylbutan-2-yl)butanamide
-
4-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(2-phenylpropan-2-yl)butanamide
-
4-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(3-ethylpentan-3-yl)butanamide
-
4-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(diphenylmethyl)butanamide
-
4-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-phenylbutanamide
-
4-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-[2-methyl-1-(naphthalen-2-yl)propan-2-yl]butanamide
-
5'-(P3-benzyl-alpha,beta-methylene)-2'deoxyuridine
-
beta-hydroxyisovalerylshikonin
an ATP-noncompetitive inhibitor of protein tyrosine kinases, induces apoptosis in human lung cancer DMS114 cells through reduction of dUTP nucleotidohydrolase activity, acts synergistically with 5-fluorouracil, overview
N,N-dibenzyl-3-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)propanamide
-
N-(2-(4-((2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl)-phenyl)propan-2-yl)-3-methoxybenzenesulfonamide
-
N-(2-(4-((2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl)-phenyl)propan-2-yl)benzenesulfonamide
-
N-benzyl-4-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)butanamide
-
N-tert-butyl-4-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)butanamide
-
N-[(1R)-1-[3-(cyclopropylmethoxy)-4-fluorophenyl]ethyl]-3-[(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methoxy]propane-1-sulfonamide
-
N-[(1R)-1-[3-(cyclopropylmethoxy)phenyl]ethyl]-3-[(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methoxy]propane-1-sulfonamide
-
N-[2-[3-(cyclopropylmethoxy)phenyl]propan-2-yl]-3-[(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methoxy]propane-1-sulfonamide
-
N-[5-[(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methoxy]-2-methylpentan-2-yl]benzenesulfonamide
-
siRNAdUT3
a 21 base-pair double-stranded RNA molecule targeted against the motif 3 of the enzyme, time- and dose-dependent decrease in the dUTPase activity in transfected cells
-
1,10-phenanthroline
-
50 mM, 30% inhibition
1-(3-tert-butyldimethylsilyloxypropyl)uracil
-
-
1-(3-triphenylsilyloxypropyl)uracil
-
-
1-(3-tritylaminopropyl)uracil
-
-
1-(3-trityloxypropyl)uracil
-
-
1-(5-triphenylsilyloxypentyl)uracil
-
-
1-(5-tritylaminopentyl)uracil
-
-
1-(5-trityloxypentyl)uracil
-
-
1-[(E)-4-trityloxy-2-butenyl]uracil
-
-
1-[(Z)-4-trityloxy-2-butenyl]uracil
-
-
1-[2-(azidomethyl)-4-(trityloxy)butyl]uracil
-
-
1-[2-(hydroxymethyl)-4-(trityloxy)butyl]uracil
-
-
1-[2-(trityloxy)ethoxymethyl]uracil
-
-
1-[4-(tert-butoxycarbonylamino)-3-(trityloxymethyl)butyl]uracil
-
-
1-[4-acetoxy-3-(tritylaminomethyl)butyl]uracil
-
-
1-[4-hydroxy-2-(trityloxymethyl)butyl]uracil
-
-
1-[4-hydroxy-3-(tritylaminomethyl)butyl]uracil
-
-
2',3'-didehydro-2',3'-dideoxyuridine 5'-diphenyl phosphate
-
-
2',5'-dideoxyuridine 5'-N-diphenylphosphoramidate
-
-
2'-deoxy-5'-phenylmethylaminouracil
-
-
2'-deoxy-5'-triphenylmethanyluracil
-
-
2'-deoxyuracil 5'-diphenyl phosphate
-
-
3'-O-tert-butyldimethylsilyl-2',5'-dideoxyuridine 5'-N-diphenylphosphoramidate
-
-
3'-O-tert-butyldimethylsilyl-5'-O-sulfamoyl-2'-deoxyuridine
-
-
3-[5-(trityloxy)tetrahydrofuran-2-yl]pyridine-2,6(1H,3H)-dione
-
-
4-hydroxymercuribenzoate
-
5 mM, complete inhibition
5'-(2,2-dimethyl-1,1-diphenylpropan-1-yl)-2',3'-dideoxyuracil
-
-
5'-(2,2-dimethyl-1,1-diphenylpropan-1-yl)-2'-deoxyuracil
-
-
5'-(2,2-dimethyl-1,1-diphenylpropan-1-yl)-3'-methyl-2',3'-dideoxyuracil
-
-
5'-(2,3,3-trimethylbutan-2-yl)-3'-methyl-2',3'-dideoxyuracil
-
-
5'-(2,4-dimethyl-3-(1-methylethyl)pentan-3-yl)-2'-deoxyuracil
-
-
5'-adamantoyl-3'-methyl-2',3'-dideoxyuracil
-
-
5'-hexadecanoyl-3'-methyl-2',3'-dideoxyuracil
-
-
5'-O-(1-adamantoyl)-2',3'-didehydro-2',3'-dideoxyuridine
-
-
5'-O-sulfamoylcarbamoyl-2',3'-didehydro-2',3'-dideoxyuridine
-
-
5'-O-triphenylsilyl-2',3'-didehydro-2',3'-dideoxyuridine
-
-
5'-O-triphenylsilyl-2',3'-dideoxy-3'-fluorouridine
-
-
5'-O-triphenylsilyl-2'-deoxyuridine
-
-
5'-pentanoylamino-2',5'-dideoxyuridine
-
-
5'-tert-butyldiphenylsilyloxy-2',3'-dideoxy-3'-fluorouridine
-
-
5'-tritylamino-2',5'-dideoxyuridine
-
-
5'-tritylamino-3'-fluoro-2',3',5'-trideoxyuridine
-
-
alpha,beta-imido-dUTP
-
-
dUMP
-
product inhibition
staphylococcal repressor protein StlSaPIBov1
-
highly potent inhibitor
-
1-[[2-(trityloxy)ethoxy]methyl]pyrimidine-2,4(1H,3H)-dione
-
1-[[2-(trityloxy)ethoxy]methyl]pyrimidine-2,4(1H,3H)-dione
-
-
2'-deoxyuridine 5'-(alpha,beta-imido)triphosphate
-
2'-deoxyuridine 5'-(alpha,beta-imido)triphosphate
-
-
Cu2+
-
-
Cu2+
-
0.5 mM, 50% inhibition
EDTA
-
-
EDTA
-
reversed by Mg2+ or Zn2+
EDTA
-
dissociation of the enzyme into its monomeric form
EDTA
-
reversed by Mg2+, Co2+ or Mn2+
EDTA
-
0.5 mM, more than 90% inhibition
EGTA
-
-
EGTA
-
10 mM, more than 90% inhibition
additional information
-
inhibitor in vivo activity against the parasite, overview
-
additional information
-
enzyme inhibitor development by high-throughput screening of triskelion libraries, a uracil-aldehyde ligand is covalently tethered to one position of a trivalent alkyloxyamine linker via an oxime linkage, and then the vacant linker positions are derivatized with a library of aldehydes, screening of triskelion oximes for inhibitory potency, overview
-
additional information
-
programmed cell death protein 4 downregulates dUTPase in certain cell types, overview
-
additional information
-
the enzyme is not inhibited by 3'-azido-2',3'-dideoxy-UTP
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Adenocarcinoma
Expression of deoxyuridine triphosphatase (dUTPase) in colorectal tumours.
Adenoma
Expression of deoxyuridine triphosphatase (dUTPase) in colorectal tumours.
African Swine Fever
African swine fever virus dUTPase is a highly specific enzyme required for efficient replication in swine macrophages.
African Swine Fever
Crystal Structure of African Swine Fever Virus dUTPase Reveals a Potential Drug Target.
African Swine Fever
Orf virus encodes a functional dUTPase gene.
African Swine Fever
Structural Insight into African Swine Fever Virus dUTPase Reveals a Novel Folding Pattern in the dUTPase Family.
Alzheimer Disease
[Molecular cloning and identification and biological activity of GIF-interacting protein(s)]
Anemia
"Hidden" dUTPase sequence in human immunodeficiency virus type 1 gp120.
Anemia
Characterization and mutational studies of equine infectious anemia virus dUTPase.
Anemia
Characterization of equine infectious anemia virus dUTPase: growth properties of a dUTPase-deficient mutant.
Anemia
Crystal structure of dUTPase from equine infectious anaemia virus; active site metal binding in a substrate analogue complex.
Anemia
dUTPase from the retrovirus equine infectious anemia virus: high-level expression in Escherichia coli and purification.
Anemia
dUTPase from the retrovirus equine infectious anemia virus: specificity, turnover and inhibition.
Anemia
Incorporation of uracil into viral DNA correlates with reduced replication of EIAV in macrophages.
Anemia
Replication in vitro and in vivo of an equine infectious anemia virus mutant deficient in dUTPase activity.
Anemia
Specific derivatization of the active site tyrosine in dUTPase perturbs ligand binding to the active site.
Anemia
The dUTPase-related gene of bovine immunodeficiency virus is critical for viral replication, despite the lack of dUTPase activity of the encoded protein.
Anemia
The role of retroviral dUTPases in replication and virulence.
Anemia
Transient kinetics of ligand binding and role of the C-terminus in the dUTPase from equine infectious anemia virus.
Anemia, Megaloblastic
Elevated deoxyuridine triphosphate nucleotidohydrolase (dUTPase) activity in the cobalamin-deficient megaloblastic bone marrow cells.
Astrocytoma
Immunohistochemical detection of dUTPase in intracranial tumors.
Bone Marrow Failure Disorders
dUTPase (DUT) Is Mutated in a Novel Monogenic Syndrome With Diabetes and Bone Marrow Failure.
Breast Neoplasms
Novel opportunities for thymidylate metabolism as a therapeutic target.
Breast Neoplasms
The Impact of dUTPase on Ribonucleotide Reductase-Induced Genome Instability in Cancer Cells.
Burkitt Lymphoma
Expression of viral and human dUTPase in Epstein-Barr virus-associated diseases.
Carcinogenesis
Epstein-Barr virus encoded dUTPase containing exosomes modulate innate and adaptive immune responses in human dendritic cells and peripheral blood mononuclear cells.
Carcinoma
CKS2 modulates cell-cycle progression of tongue squamous cell carcinoma cells partly via modulating the cellular distribution of DUTPase.
Carcinoma
Expression of deoxyuridine triphosphatase (dUTPase) in colorectal tumours.
Carcinoma
Immunohistochemical detection of dUTPase in intracranial tumors.
Carcinoma
Phosphorylation of herpes simplex virus 1 dUTPase upregulated viral dUTPase activity to compensate for low cellular dUTPase activity for efficient viral replication.
Carcinoma
Synergy between the NAMPT inhibitor GMX1777(8) and pemetrexed in non-small cell lung cancer cells is mediated by PARP activation and enhanced NAD consumption.
Carcinoma, Hepatocellular
Characterization and functional studies of fowl adenovirus 9 dUTPase.
Carcinoma, Hepatocellular
Deoxyuridine triphosphatase in human hepatoma.
Carcinoma, Hepatocellular
dUTP pyrophosphatase and uracil-DNA glycosylase in rat liver and hepatomas.
Carcinoma, Hepatocellular
dUTP pyrophosphatase expression correlates with a poor prognosis in hepatocellular carcinoma.
Carcinoma, Hepatocellular
The reduction of uridine 5'-diphosphate and uridine 5'-triphosphate in some transplantable rat hepatomas.
Carcinoma, Non-Small-Cell Lung
Inhibition of dUTPase Induces Synthetic Lethality with Thymidylate Synthase-Targeted Therapies in Non-Small Cell Lung Cancer.
Carcinoma, Non-Small-Cell Lung
Synergy between the NAMPT inhibitor GMX1777(8) and pemetrexed in non-small cell lung cancer cells is mediated by PARP activation and enhanced NAD consumption.
Carcinoma, Squamous Cell
CKS2 modulates cell-cycle progression of tongue squamous cell carcinoma cells partly via modulating the cellular distribution of DUTPase.
Chagas Disease
The crystal structure of Trypanosoma cruzi dUTPase reveals a novel dUTP/dUDP binding fold.
Chickenpox
Nationwide distribution of varicella-zoster virus clades in China.
Chickenpox
The simian varicella virus uracil DNA glycosylase and dUTPase genes are expressed in vivo, but are non-essential for replication in cell culture.
Colonic Neoplasms
dUTP nucleotidohydrolase isoform expression in normal and neoplastic tissues: association with survival and response to 5-fluorouracil in colorectal cancer.
Colonic Neoplasms
Lack of dependence of 5-fluorodeoxyuridine-mediated radiosensitization on cytotoxicity.
Colonic Neoplasms
Macrophages from cancer patients: analysis of TRAIL, TRAIL receptors, and colon tumor cell apoptosis.
Colonic Neoplasms
The role of dUTPase and uracil-DNA repair in cancer chemotherapy.
Colorectal Neoplasms
dUTP nucleotidohydrolase isoform expression in normal and neoplastic tissues: association with survival and response to 5-fluorouracil in colorectal cancer.
Colorectal Neoplasms
Expression of deoxyuridine triphosphatase (dUTPase) in colorectal tumours.
Colorectal Neoplasms
Higher expression of deoxyuridine triphosphatase (dUTPase) may predict the metastasis potential of colorectal cancer.
Colorectal Neoplasms
Induction of resistance to fluorodeoxyuridine cytotoxicity and DNA damage in human tumor cells by expression of Escherichia coli deoxyuridinetriphosphatase.
Colorectal Neoplasms
The 1,2-Diaminocyclohexane Carrier Ligand in Oxaliplatin Induces p53-Dependent Transcriptional Repression of Factors Involved in Thymidylate Biosynthesis.
Communicable Diseases
Keeping Uracil Out of DNA: Physiological Role, Structure and Catalytic Mechanism of dUTPases.
Cysticercosis
Taenia solium dUTPase: A potential target for anti-human cysticercosis.
dutp diphosphatase deficiency
Description of a novel eukaryotic deoxyuridine 5'-triphosphate nucleotidohydrolase in Leishmania major.
dutp diphosphatase deficiency
Pyrimidine requirements in deoxyuridine triphosphate nucleotidohydrolase deficient Trypanosoma brucei mutants.
Ectromelia
The genome of swinepox virus.
Encephalitis
"Hidden" dUTPase sequence in human immunodeficiency virus type 1 gp120.
Enteritis
Identification and characterization of duck enteritis virus dUTPase gene.
Ependymoma
Immunohistochemical detection of dUTPase in intracranial tumors.
Epstein-Barr Virus Infections
Expression of viral and human dUTPase in Epstein-Barr virus-associated diseases.
Epstein-Barr Virus Infections
The EBV-encoded dUTPase activates NF-kappa B through the TLR2 and MyD88-dependent signaling pathway.
Equine Infectious Anemia
"Hidden" dUTPase sequence in human immunodeficiency virus type 1 gp120.
Equine Infectious Anemia
Characterization and mutational studies of equine infectious anemia virus dUTPase.
Equine Infectious Anemia
Characterization of equine infectious anemia virus dUTPase: growth properties of a dUTPase-deficient mutant.
Equine Infectious Anemia
Crystal structure of dUTPase from equine infectious anaemia virus; active site metal binding in a substrate analogue complex.
Equine Infectious Anemia
dUTPase from the retrovirus equine infectious anemia virus: high-level expression in Escherichia coli and purification.
Equine Infectious Anemia
dUTPase from the retrovirus equine infectious anemia virus: specificity, turnover and inhibition.
Equine Infectious Anemia
Incorporation of uracil into viral DNA correlates with reduced replication of EIAV in macrophages.
Equine Infectious Anemia
Replication in vitro and in vivo of an equine infectious anemia virus mutant deficient in dUTPase activity.
Equine Infectious Anemia
Specific derivatization of the active site tyrosine in dUTPase perturbs ligand binding to the active site.
Equine Infectious Anemia
The dUTPase-related gene of bovine immunodeficiency virus is critical for viral replication, despite the lack of dUTPase activity of the encoded protein.
Equine Infectious Anemia
The role of retroviral dUTPases in replication and virulence.
Equine Infectious Anemia
Transient kinetics of ligand binding and role of the C-terminus in the dUTPase from equine infectious anemia virus.
Fatigue Syndrome, Chronic
Antibody to Epstein-Barr virus deoxyuridine triphosphate nucleotidohydrolase and deoxyribonucleotide polymerase in a chronic fatigue syndrome subset.
Fragile X Syndrome
Antifolate-induced misincorporation of deoxyuridine monophosphate into DNA by cells from patients with the fragile X syndrome.
Herpes Simplex
Analysis of cyclin-dependent kinase activity after herpes simplex virus type 2 infection.
Herpes Simplex
Characterization of a herpes simplex virus type 2 deoxyuridine triphosphate nucleotidohydrolase and mapping of a gene conferring type specificity for the enzyme.
Herpes Simplex
Demonstration of a herpes simplex virus type 2-induced deoxyuridine triphosphate nucleotidohydrolase in infected KB cells and in biochemically transformed HeLa cells.
Herpes Simplex
Deoxyuridine triphosphate nucleotidohydrolase induced by herpes simplex virus type 1. Purification and characterization of induced enzyme.
Herpes Simplex
dUTPase from herpes simplex virus type 1; purification from infected green monkey kidney (Vero) cells and from an overproducing Escherichia coli strain.
Herpes Simplex
Effects of mercury (II) compounds on the activity of dUTPases from various sources.
Herpes Simplex
Herpes simplex virus 1 protein kinase Us3 phosphorylates viral dUTPase and regulates its catalytic activity in infected cells.
Herpes Simplex
Herpes simplex virus type 1 dUTPase mutants are attenuated for neurovirulence, neuroinvasiveness, and reactivation from latency.
Herpes Simplex
Herpes simplex virus-induced dUTPase: target site for antiviral chemotherapy.
Herpes Simplex
Identification and deletion mutagenesis of the bovine herpesvirus 1 dUTPase gene and a gene homologous to herpes simplex virus UL49.5.
Herpes Simplex
Identification of the herpes simplex virus type 1 gene encoding the dUTPase.
Herpes Simplex
Induction of uracil-DNA glycosylase and dUTP nucleotidohydrolase activity in herpes simplex virus-infected human cells.
Herpes Simplex
Inhibition of phosphorylation of cellular dUTP nucleotidohydrolase as a consequence of herpes simplex virus infection.
Herpes Simplex
Isolation and characterisation of herpes simplex virus type 1 mutants which fail to induce dUTPase activity.
Herpes Simplex
Kinetic properties and stereospecificity of the monomeric dUTPase from herpes simplex virus type 1.
Herpes Simplex
Mutations in accessory DNA replicating functions alter the relative mutation frequency of herpes simplex virus type 1 strains in cultured murine cells.
Herpes Simplex
Nucleotide sequence of a 55 kbp region from the right end of the genome of a pathogenic African swine fever virus isolate (Malawi LIL20/1).
Herpes Simplex
Phosphorylation of a herpes simplex virus 1 dUTPase by a viral protein kinase, Us3, dictates viral pathogenicity in the central nervous system but not at the periphery.
Herpes Simplex
Phosphorylation of herpes simplex virus 1 dUTPase regulates viral virulence and genome integrity by compensating for low cellular dUTPase activity in the central nervous system.
Herpes Simplex
Phosphorylation of herpes simplex virus 1 dUTPase upregulated viral dUTPase activity to compensate for low cellular dUTPase activity for efficient viral replication.
Herpes Simplex
Purification and properties of the deoxyuridine triphosphate nucleotidohydrolase enzyme derived from HeLa S3 cells. Comparison to a distinct dUTP nucleotidohydrolase induced in herpes simplex virus-infected HeLa S3 cells.
Herpes Simplex
[The relationship between gene function and virulence in alpha-herpesviruses]
HIV Infections
Expression and cytoplasmic localisation of deoxyuridine triphosphate pyrophosphatase encoded by a human endogenous retrovirus.
HIV Infections
Structure/function analysis of a dUTPase: catalytic mechanism of a potential chemotherapeutic target.
Hodgkin Disease
Expression of viral and human dUTPase in Epstein-Barr virus-associated diseases.
Hypertension
Monocyte-released HERV-K dUTPase engages TLR4 and MCAM causing endothelial mesenchymal transition.
Hypertension, Pulmonary
Monocyte-released HERV-K dUTPase engages TLR4 and MCAM causing endothelial mesenchymal transition.
Hypertension, Pulmonary
Upregulation of HERV-K is Linked to Immunity and Inflammation in Pulmonary Arterial Hypertension.
Infections
African swine fever virus dUTPase is a highly specific enzyme required for efficient replication in swine macrophages.
Infections
Analysis of cyclin-dependent kinase activity after herpes simplex virus type 2 infection.
Infections
Bacillus subtilis deoxyuridinetriphosphatase and its bacteriophage PBS2-induced inhibitor.
Infections
Crystal structure of the Mycobacterium tuberculosis dUTPase: insights into the catalytic mechanism.
Infections
Human herpesviruses-encoded dUTPases: a family of proteins that modulate dendritic cell function and innate immunity.
Infections
Identification and characterization of a baculovirus structural protein, VP1054, required for nucleocapsid formation.
Infections
Identification and characterization of duck enteritis virus dUTPase gene.
Infections
Immunological parameters in goats experimentally infected with SRLV genotype E, strain Roccaverano.
Infections
Inhibition of phosphorylation of cellular dUTP nucleotidohydrolase as a consequence of herpes simplex virus infection.
Infections
Insights into the molecular and biological features of the dUTPase-related gene of bovine immunodeficiency virus.
Infections
Murine cytomegalovirus M72 promotes acute virus replication in vivo and is a substrate of the TRiC/CCT complex.
Infections
New dUTPase and dUDPase activites after infection of Escherichia coli by T2 bacteriophage.
Infections
Nuclear-export-signal-dependent protein translocation of dUTPase encoded by Singapore grouper iridovirus.
Infections
Purification and properties of the deoxyuridine triphosphate nucleotidohydrolase enzyme derived from HeLa S3 cells. Comparison to a distinct dUTP nucleotidohydrolase induced in herpes simplex virus-infected HeLa S3 cells.
Infections
Structural Insight into African Swine Fever Virus dUTPase Reveals a Novel Folding Pattern in the dUTPase Family.
Infections
The anti-interferon activity of conserved viral dUTPase ORF54 is essential for an effective MHV-68 infection.
Infections
The EBV-encoded dUTPase activates NF-kappa B through the TLR2 and MyD88-dependent signaling pathway.
Infections
The properties of a bacteriophage T5 mutant unable to induce deoxyuridine 5'-triphosphate nucleotidohydrolase. Synthesis of uracil-containing T5 deoxyribonucleic acid.
Infectious Mononucleosis
Expression of viral and human dUTPase in Epstein-Barr virus-associated diseases.
Influenza in Birds
Live vaccination with an H5-hemagglutinin-expressing infectious laryngotracheitis virus recombinant protects chickens against different highly pathogenic avian influenza viruses of the H5 subtype.
Leukemia
Human deoxyuridine triphosphate nucleotidohydrolase. Purification and characterization of the deoxyuridine triphosphate nucleotidohydrolase from acute lymphocytic leukemia.
Leukemia, Lymphoid
Human deoxyuridine triphosphate nucleotidohydrolase. Purification and characterization of the deoxyuridine triphosphate nucleotidohydrolase from acute lymphocytic leukemia.
Leukoplakia, Hairy
Expression of viral and human dUTPase in Epstein-Barr virus-associated diseases.
Lung Neoplasms
A randomized, phase 2 study of deoxyuridine triphosphatase inhibitor, TAS-114, in combination with S-1 versus S-1 alone in patients with advanced non-small-cell lung cancer.
Lung Neoplasms
A tyrosine kinase inhibitor, beta-hydroxyisovalerylshikonin, induced apoptosis in human lung cancer DMS114 cells through reduction of dUTP nucleotidohydrolase activity.
Lung Neoplasms
Inhibition of dUTPase Induces Synthetic Lethality with Thymidylate Synthase-Targeted Therapies in Non-Small Cell Lung Cancer.
Malaria
Design, synthesis, and evaluation of 5'-diphenyl nucleoside analogues as inhibitors of the Plasmodium falciparum dUTPase.
Malaria
dUTPase as a platform for antimalarial drug design: structural basis for the selectivity of a class of nucleoside inhibitors.
Malaria
Functional genetic evaluation of DNA house-cleaning enzymes in the malaria parasite: dUTPase and Ap4AH are essential in Plasmodium berghei but ITPase and NDH are dispensable.
Malaria
Keeping Uracil Out of DNA: Physiological Role, Structure and Catalytic Mechanism of dUTPases.
Malaria
Kinetic and thermodynamic characterization of dUTP hydrolysis by Plasmodium falciparum dUTPase.
Melanoma
Monocyte-released HERV-K dUTPase engages TLR4 and MCAM causing endothelial mesenchymal transition.
Meningioma
Immunohistochemical detection of dUTPase in intracranial tumors.
Myxoma
The genome of swinepox virus.
Nasopharyngeal Carcinoma
A new lytic antibody, 7D6, detects Epstein-Barr virus dUTPase in nonkeratinizing undifferentiated nasopharyngeal carcinomas.
Nasopharyngeal Carcinoma
Expression of viral and human dUTPase in Epstein-Barr virus-associated diseases.
Neoplasm Metastasis
Expression of deoxyuridine triphosphatase (dUTPase) in colorectal tumours.
Neoplasm Metastasis
Higher expression of deoxyuridine triphosphatase (dUTPase) may predict the metastasis potential of colorectal cancer.
Neoplasms
A Human Endogenous Retrovirus K dUTPase Triggers a T(H)1, T(H)17 Cytokine Response: Does It Have a Role in Psoriasis?
Neoplasms
A multicenter phase II study of TAS-114 in combination with S-1 in patients with pretreated advanced gastric cancer (EPOC1604).
Neoplasms
Active site closure facilitates juxtaposition of reactant atoms for initiation of catalysis by human dUTPase.
Neoplasms
ATP-Linked Chimeric Nucleotide as a Specific Luminescence Reporter of Deoxyuridine Triphosphatase.
Neoplasms
Backbone nuclear magnetic resonance assignment of human deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTPase).
Neoplasms
Characterization of an integrated, endogenous mouse mammary tumor virus-like (MMTV) betaretrovirus genome in a black Syrian hamster (Mesocricetus auratus).
Neoplasms
Deoxyuridine triphosphatase (dUTPase) expression and sensitivity to the thymidylate synthase (TS) inhibitor ZD9331.
Neoplasms
Differentially expressed genes in multidrug resistant variants of U-2 OS human osteosarcoma cells.
Neoplasms
Dimeric dUTPases, HisE, and MazG belong to a new superfamily of all-alpha NTP pyrophosphohydrolases with potential "house-cleaning" functions.
Neoplasms
dUTP nucleotidohydrolase isoform expression in normal and neoplastic tissues: association with survival and response to 5-fluorouracil in colorectal cancer.
Neoplasms
dUTPase inhibition confers susceptibility to a thymidylate synthase inhibitor in DNA-repair-defective human cancer cells.
Neoplasms
Expression and purification of the mouse mammary tumor virus gag-pro transframe protein p30 and characterization of its dUTPase activity.
Neoplasms
Expression of deoxyuridine triphosphatase (dUTPase) in colorectal tumours.
Neoplasms
Expression of viral and human dUTPase in Epstein-Barr virus-associated diseases.
Neoplasms
First-in-human phase 1 study of novel dUTPase inhibitor TAS-114 in combination with S-1 in Japanese patients with advanced solid tumors.
Neoplasms
Higher expression of deoxyuridine triphosphatase (dUTPase) may predict the metastasis potential of colorectal cancer.
Neoplasms
Identification of potential pharmacogenomic markers of clinical efficacy of 5-fluorouracil in colorectal cancer.
Neoplasms
Identification of sequence determinants of human nuclear dUTPase isoform localization.
Neoplasms
Immunohistochemical detection of dUTPase in intracranial tumors.
Neoplasms
Induction of resistance to fluorodeoxyuridine cytotoxicity and DNA damage in human tumor cells by expression of Escherichia coli deoxyuridinetriphosphatase.
Neoplasms
Inhibition of dUTPase Induces Synthetic Lethality with Thymidylate Synthase-Targeted Therapies in Non-Small Cell Lung Cancer.
Neoplasms
Inhibition of the proliferation of human cancer cells in-vitro by substrate-analogous inhibitors of dUTPase.
Neoplasms
Keeping Uracil Out of DNA: Physiological Role, Structure and Catalytic Mechanism of dUTPases.
Neoplasms
New Challenges and Inspired Answers for Anticancer Drug Discovery and Development.
Neoplasms
Novel gain of function activity of p53 mutants: activation of the dUTPase gene expression leading to resistance to 5-fluorouracil.
Neoplasms
Novel opportunities for thymidylate metabolism as a therapeutic target.
Neoplasms
Regulation of human dUTPase gene expression and p53-mediated transcriptional repression in response to oxaliplatin-induced DNA damage.
Neoplasms
Role of Microglia Autophagy in Microglia Activation After Traumatic Brain Injury.
Neoplasms
Small interfering RNA-mediated suppression of dUTPase sensitizes cancer cell lines to thymidylate synthase inhibition.
Neoplasms
Structural insights into the mechanism defining substrate affinity in Arabidopsis thaliana dUTPase: the role of tryptophan 93 in ligand orientation.
Neoplasms
Structural model of human dUTPase in complex with a novel proteinaceous inhibitor.
Neoplasms
Targeting nucleotide metabolism enhances the efficacy of anthracyclines and anti-metabolites in triple-negative breast cancer.
Neoplasms
TAS-114, a First-in-Class Dual dUTPase/DPD Inhibitor, Demonstrates Potential to Improve Therapeutic Efficacy of Fluoropyrimidine-Based Chemotherapy.
Neoplasms
The ability to accumulate deoxyuridine triphosphate and cellular response to thymidylate synthase (TS) inhibition.
Neoplasms
The action of Pdcd4 may be cell type specific: evidence that reduction of dUTPase levels might contribute to its tumor suppressor activity in Bon-1 cells.
Neoplasms
The contribution of DNA base damage to human cancer is modulated by the base excision repair interaction network.
Neoplasms
The Impact of dUTPase on Ribonucleotide Reductase-Induced Genome Instability in Cancer Cells.
Neoplasms
The protein p30, encoded at the gag-pro junction of mouse mammary tumor virus, is a dUTPase fused with a nucleocapsid protein.
Neoplasms
The role of deoxyuridine triphosphate nucleotidohydrolase, uracil-DNA glycosylase, and DNA polymerase alpha in the metabolism of FUdR in human tumor cells.
Neoplasms
The role of dUTPase and uracil-DNA repair in cancer chemotherapy.
Neuroblastoma
Phosphorylation of herpes simplex virus 1 dUTPase upregulated viral dUTPase activity to compensate for low cellular dUTPase activity for efficient viral replication.
Neuroinflammatory Diseases
Epstein-Barr Virus dUTPase Induces Neuroinflammatory Mediators: Implications for Myalgic Encephalomyelitis/Chronic Fatigue Syndrome.
Oligodendroglioma
Immunohistochemical detection of dUTPase in intracranial tumors.
Osteosarcoma
Combining Non-reducing SDS-PAGE Analysis and Chemical Crosslinking to Detect Multimeric Complexes Stabilized by Disulfide Linkages in Mammalian Cells in Culture.
Persistent Infection
The anti-interferon activity of conserved viral dUTPase ORF54 is essential for an effective MHV-68 infection.
Precursor Cell Lymphoblastic Leukemia-Lymphoma
Human deoxyuridine triphosphate nucleotidohydrolase. Purification and characterization of the deoxyuridine triphosphate nucleotidohydrolase from acute lymphocytic leukemia.
Pseudorabies
Identification and characterization of pseudorabies virus dUTPase.
Pseudorabies
Pseudorabies Virus dUTPase UL50 Induces Lysosomal Degradation of Type I Interferon Receptor 1 and Antagonizes the Alpha Interferon Response.
Pseudorabies
The UL49.5 gene of pseudorabies virus codes for an O-glycosylated structural protein of the viral envelope.
Psoriasis
A Human Endogenous Retrovirus K dUTPase Triggers a T(H)1, T(H)17 Cytokine Response: Does It Have a Role in Psoriasis?
Psoriasis
Haplotype sharing analysis identifies a retroviral dUTPase as candidate susceptibility gene for psoriasis.
Psoriasis
Protective effect of human endogenous retrovirus K dUTPase variants on psoriasis susceptibility.
Retinoblastoma
Identification of candidate growth-regulating genes that are overexpressed in late gestation fetal liver in the rat.
Sarcoma, Kaposi
Kaposi's sarcoma-associated herpesvirus (human herpesvirus-8) ORF54 encodes a functional dUTPase expressed in the lytic replication cycle.
Sarcoma, Yoshida
A new deoxyuridine-5'-triphosphatase in Yoshida sarcoma cells involved in deoxyuridine 5'-triphosphate metabolism.
Smallpox
The genome of swinepox virus.
Stomach Neoplasms
A multicenter phase II study of TAS-114 in combination with S-1 in patients with pretreated advanced gastric cancer (EPOC1604).
Stomach Neoplasms
Loss of RUNX3 expression correlates with differentiation, nodal metastasis, and poor prognosis of gastric cancer.
Superinfection
Induction of a deoxyuridine triphosphate nucleotidohydrolase activity in Epstein-Barr virus-infected cells.
Tuberculosis
A Hidden Active Site in the Potential Drug Target Mycobacterium tuberculosis dUTPase Is Accessible through Small Amplitude Protein Conformational Changes.
Tuberculosis
Active site of mycobacterial dUTPase: structural characteristics and a built-in sensor.
Tuberculosis
Antimycobacterial activity of peptide conjugate of pyridopyrimidine derivative against Mycobacterium tuberculosis in a series of in vitro and in vivo models.
Tuberculosis
Cross-species inhibition of dUTPase via the Staphylococcal Stl protein perturbs dNTP pool and colony formation in Mycobacterium.
Tuberculosis
Crystal Structure of African Swine Fever Virus dUTPase Reveals a Potential Drug Target.
Tuberculosis
Crystal structure of the Mycobacterium tuberculosis dUTPase: insights into the catalytic mechanism.
Tuberculosis
Enhanced Cellular Uptake of a New, in Silico Identified Antitubercular Candidate by Peptide Conjugation.
Tuberculosis
Keeping Uracil Out of DNA: Physiological Role, Structure and Catalytic Mechanism of dUTPases.
Tuberculosis
Molecular Modeling of Mycobacterium Tuberculosis dUTpase: Docking and Catalytic Mechanism Studies.
Tuberculosis
Structural insights into the mechanism defining substrate affinity in Arabidopsis thaliana dUTPase: the role of tryptophan 93 in ligand orientation.
Tuberculosis
The dUTPase enzyme is essential in Mycobacterium smegmatis.
Uterine Cervical Neoplasms
Genetic variations in the SULF1 gene alter the risk of cervical cancer and precancerous lesions.
Vaccinia
Effects of vaccinia virus uracil DNA glycosylase catalytic site and deoxyuridine triphosphatase deletion mutations individually and together on replication in active and quiescent cells and pathogenesis in mice.
Vaccinia
Genomic analysis of a transposition-deletion variant of orf virus reveals a 3.3 kbp region of non-essential DNA.
Vaccinia
Orf virus encodes a functional dUTPase gene.
Vaccinia
Purification and characterization of the vaccinia virus deoxyuridine triphosphatase expressed in Escherichia coli.
Vaccinia
Structures of vaccinia virus dUTPase and its nucleotide complexes.
Vaccinia
The genome of swinepox virus.
Vaccinia
Vaccinia virus encodes a functional dUTPase.
Vaccinia
Vaccinia virus lacking the deoxyuridine triphosphatase gene (F2L) replicates well in vitro and in vivo, but is hypersensitive to the antiviral drug (N)-methanocarbathymidine.
Virus Diseases
Characterization and functional studies of fowl adenovirus 9 dUTPase.
Virus Diseases
Cloning and expression of the Epstein-Barr virus-encoded dUTPase: patients with acute, reactivated or chronic virus infection develop antibodies against the enzyme.
Virus Diseases
Inhibition of phosphorylation of cellular dUTP nucleotidohydrolase as a consequence of herpes simplex virus infection.
Virus Diseases
Vaccinia virus encodes a functional dUTPase.
Visna
"Hidden" dUTPase sequence in human immunodeficiency virus type 1 gp120.
Visna
Replication properties of dUTPase-deficient mutants of caprine and ovine lentiviruses.
Visna
The role of retroviral dUTPases in replication and virulence.
Visna
Visna virus dUTPase is dispensable for neuropathogenicity.
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0.0033
1-[(1Z,8E)-5-([[(E)-(3,4-dihydroxy-5-methoxybenzylidene)amino]oxy]methyl)-1-(3,4-dihydroxy-5-methoxyphenyl)-3,7-dioxa-2,8-diazadeca-1,8-dien-10-yl]pyrimidine-2,4(1H,3H)-dione
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.017
1-[[2-(trityloxy)ethoxy]methyl]pyrimidine-2,4(1H,3H)-dione
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.018
2'-deoxyuridine 5'-(alpha,beta-imido)triphosphate
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.000021
N-[(1R)-1-[3-(cyclopropylmethoxy)-4-fluorophenyl]ethyl]-3-[(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methoxy]propane-1-sulfonamide
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.073
1-(3-tert-butyldimethylsilyloxypropyl)uracil
-
-
0.025
1-(3-triphenylsilyloxypropyl)uracil
-
-
0.0014
1-(3-tritylaminopropyl)uracil
-
-
0.313
1-(3-trityloxypropyl)uracil
-
-
1
1-(5-triphenylsilyloxypentyl)uracil
-
above
1
1-(5-tritylaminopentyl)uracil
-
above
1
1-(5-trityloxypentyl)uracil
-
above
1
1-[(E)-4-trityloxy-2-butenyl]uracil
-
above
0.0052
1-[(Z)-4-trityloxy-2-butenyl]uracil
-
-
1
1-[2-(azidomethyl)-4-(trityloxy)butyl]uracil
-
above
0.26
1-[2-(hydroxymethyl)-4-(trityloxy)butyl]uracil
-
-
0.017
1-[2-(trityloxy)ethoxymethyl]uracil
-
-
1
1-[4-(tert-butoxycarbonylamino)-3-(trityloxymethyl)butyl]uracil
-
above
0.074
1-[4-acetoxy-3-(tritylaminomethyl)butyl]uracil
-
-
0.021
1-[4-hydroxy-2-(trityloxymethyl)butyl]uracil
-
-
0.0057
1-[4-hydroxy-3-(tritylaminomethyl)butyl]uracil
-
-
1
2',3'-didehydro-2',3'-dideoxyuridine 5'-diphenyl phosphate
-
above
1
2',5'-dideoxyuridine 5'-N-diphenylphosphoramidate
-
above
0.908
2'-deoxy-5'-triphenylmethanyluracil
-
pH 8.0, 25°C
0.135
2'-deoxyuracil 5'-diphenyl phosphate
-
pH 8.0, 25°C
0.232
3'-O-tert-butyldimethylsilyl-2',5'-dideoxyuridine 5'-N-diphenylphosphoramidate
-
-
0.324
3'-O-tert-butyldimethylsilyl-5'-O-sulfamoyl-2'-deoxyuridine
-
-
0.156
3-[5-(trityloxy)tetrahydrofuran-2-yl]pyridine-2,6(1H,3H)-dione
-
pH 8.0, 25°C
0.805
5'-(2,2-dimethyl-1,1-diphenylpropan-1-yl)-2'-deoxyuracil
-
pH 8.0, 25°C
0.807
5'-(2,2-dimethyl-1,1-diphenylpropan-1-yl)-3'-methyl-2',3'-dideoxyuracil
-
pH 8.0, 25°C
0.298 - 0.547
5'-adamantoyl-3'-methyl-2',3'-dideoxyuracil
0.35
5'-hexadecanoyl-3'-methyl-2',3'-dideoxyuracil
-
pH 8.0, 25°C
0.298
5'-O-(1-adamantoyl)-2',3'-didehydro-2',3'-dideoxyuridine
-
-
0.799
5'-O-sulfamoylcarbamoyl-2',3'-didehydro-2',3'-dideoxyuridine
-
-
1
5'-O-triphenylsilyl-2',3'-didehydro-2',3'-dideoxyuridine
-
above
1
5'-O-triphenylsilyl-2',3'-dideoxy-3'-fluorouridine
-
above
0.909
5'-O-triphenylsilyl-2'-deoxyuridine
-
-
1
5'-pentanoylamino-2',5'-dideoxyuridine
-
above
0.808
5'-tert-butyldiphenylsilyloxy-2',3'-dideoxy-3'-fluorouridine
-
-
0.046
5'-tritylamino-2',5'-dideoxyuridine
-
-
1
5'-tritylamino-3'-fluoro-2',3',5'-trideoxyuridine
-
above
0.0000067
staphylococcal repressor protein StlSaPIBov1
-
at pH 7.5 and 20°C
-
additional information
2'-deoxy-5'-phenylmethylaminouracil
0.298
5'-adamantoyl-3'-methyl-2',3'-dideoxyuracil
-
pH 8.0, 25°C
0.547
5'-adamantoyl-3'-methyl-2',3'-dideoxyuracil
-
pH 8.0, 25°C, recombinant enzyme
additional information
2'-deoxy-5'-phenylmethylaminouracil
-
above 1 mM, pH 8.0, 25°C
additional information
5'-(2,2-dimethyl-1,1-diphenylpropan-1-yl)-2',3'-dideoxyuracil
-
above 1 mM, pH 8.0, 25°C
additional information
5'-(2,3,3-trimethylbutan-2-yl)-3'-methyl-2',3'-dideoxyuracil
-
above 1 mM, pH 8.0, 25°C
additional information
5'-(2,4-dimethyl-3-(1-methylethyl)pentan-3-yl)-2'-deoxyuracil
-
above 1 mM, pH 8.0, 25°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.000026
(E)-3-(2,2-difluoroethoxy)-N-(7-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-2-methylhept-5-en-2-yl)benzenesulfonamide
Homo sapiens
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.000033
(E)-3-(cyclopentyloxy)-N-(7-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-2-methylhept-5-en-2-yl)benzenesulfonamide
Homo sapiens
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.000028
(E)-3-(cyclopropylmethoxy)-N-(7-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-2-methylhept-5-en-2-yl)benzenesulfonamide
Homo sapiens
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.00034
(E)-N-(7-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-2-methylhept-5-en-2-yl)-3-methoxybenzenesulfonamide
Homo sapiens
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.0016
(E)-N-(7-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-2-methylhept-5-en-2-yl)benzenesulfonamide
Homo sapiens
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.01
(R)-1-(4-(2-(hydroxydiphenylmethyl)-pyrrolidin-1-yl)-4-oxobutyl)pyrimidine-2,4(1H,3H)-dione
Homo sapiens
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.00041
(R)-N-(1-(3-(2,2-difluoroethoxy)phenyl)ethyl)-4-((2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl)benzenesulfonamide
Homo sapiens
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.00043
(R)-N-(1-(3-(cyclopentyloxy)phenyl)ethyl)-4-((2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl)benzenesulfonamide
Homo sapiens
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.00082
(R)-N-(1-(3-(cyclopropylmethoxy)phenyl)ethyl)-4-((2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl)-benzenesulfonamide
Homo sapiens
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.000082
(R,E)-N-(1-(3-(2,2-difluoroethoxy)phenyl)ethyl)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)pent-3-ene-1-sulfonamide
Homo sapiens
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.000041
(R,E)-N-(1-(3-(cyclopentyloxy)phenyl)ethyl)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)pent-3-ene-1-sulfonamide
Homo sapiens
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.000039
(R,E)-N-(1-(3-(cyclopropylmethoxy)phenyl)ethyl)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)pent-3-ene-1-sulfonamide
Homo sapiens
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.001
1-(3-[[(2S)-2-[hydroxy[bis(2-methoxyphenyl)]methyl]pyrrolidin-1-yl]sulfonyl]propyl)pyrimidine-2,4(1H,3H)-dione
Homo sapiens
IC50 above 0.001 mM, in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.001
1-(3-[[(2S)-2-[hydroxy[bis(3-methoxyphenyl)]methyl]pyrrolidin-1-yl]sulfonyl]propyl)pyrimidine-2,4(1H,3H)-dione
Homo sapiens
IC50 above 0.001 mM, in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.00058
1-(4-[(2S)-2-[bis(3-chlorophenyl)(hydroxy)methyl]pyrrolidin-1-yl]-4-oxobutyl)pyrimidine-2,4(1H,3H)-dione
Homo sapiens
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.00035
1-(4-[(2S)-2-[bis(3-fluorophenyl)(hydroxy)methyl]pyrrolidin-1-yl]-4-oxobutyl)pyrimidine-2,4(1H,3H)-dione
Homo sapiens
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.001
1-(4-[(2S)-2-[bis(4-chlorophenyl)(hydroxy)methyl]pyrrolidin-1-yl]-4-oxobutyl)pyrimidine-2,4(1H,3H)-dione
Homo sapiens
IC50 above 0.001 mM, in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.0006
1-(4-[(2S)-2-[bis(4-fluorophenyl)(hydroxy)methyl]pyrrolidin-1-yl]-4-oxobutyl)pyrimidine-2,4(1H,3H)-dione
Homo sapiens
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.0073 - 0.03
1-[3-(4-benzylpiperidin-1-yl)-3-oxopropyl]pyrimidine-2,4(1H,3H)-dione
0.0094
1-[3-([(2R)-2-[hydroxy(diphenyl)methyl]pyrrolidin-1-yl]sulfonyl)propyl]pyrimidine-2,4(1H,3H)-dione
Homo sapiens
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.00028
1-[3-([(2S)-2-[bis(3-fluorophenyl)(hydroxy)methyl]pyrrolidin-1-yl]sulfonyl)propyl]pyrimidine-2,4(1H,3H)-dione
Homo sapiens
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.00031
1-[3-([(2S)-2-[bis(4-fluorophenyl)(hydroxy)methyl]pyrrolidin-1-yl]sulfonyl)propyl]pyrimidine-2,4(1H,3H)-dione
Homo sapiens
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.001
1-[3-[(2S)-2-(diphenylmethyl)pyrrolidin-1-yl]-3-oxopropyl]pyrimidine-2,4(1H,3H)-dione
Homo sapiens
IC50 above 0.001 mM, in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.00015
1-[4-[(2S)-2-(diphenylmethyl)pyrrolidin-1-yl]-4-oxobutyl]pyrimidine-2,4(1H,3H)-dione
Homo sapiens
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.001
1-[4-[(2S)-2-[bis[2-(benzyloxy)phenyl](hydroxy)methyl]pyrrolidin-1-yl]-4-oxobutyl]pyrimidine-2,4(1H,3H)-dione
Homo sapiens
IC50 above 0.001 mM, in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.001
1-[4-[(2S)-2-[bis[3-(benzyloxy)phenyl](hydroxy)methyl]pyrrolidin-1-yl]-4-oxobutyl]pyrimidine-2,4(1H,3H)-dione
Homo sapiens
IC50 above 0.001 mM, in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.001
1-[4-[(2S)-2-[bis[4-(benzyloxy)phenyl](hydroxy)methyl]pyrrolidin-1-yl]-4-oxobutyl]pyrimidine-2,4(1H,3H)-dione
Homo sapiens
IC50 above 0.001 mM, in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.00023
1-[4-[(2S)-2-[hydroxy[di(thiophen-3-yl)]methyl]pyrrolidin-1-yl]-4-oxobutyl]pyrimidine-2,4(1H,3H)-dione
Homo sapiens
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.3
1-[[2-(trityloxy)ethoxy]methyl]pyrimidine-2,4(1H,3H)-dione
Homo sapiens
IC50 above 0.3 mM, in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.015
2'-deoxyuridine 5'-(alpha,beta-imido)triphosphate
Homo sapiens
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.000073
3-(2,2-difluoroethoxy)-N-(2-(4-((2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl)phenyl)propan-2-yl)-benzenesulfonamide
Homo sapiens
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.03
3-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(2,4,4-trimethylpentan-2-yl)propanamide
Homo sapiens
IC50 above 0.03 mM, in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.03
3-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(2-methylbutan-2-yl)propanamide
Homo sapiens
IC50 above 0.03 mM, in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.03
3-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(2-phenylethyl)propanamide
Homo sapiens
IC50 above 0.03 mM, in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.022
3-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(3-ethylhexan-3-yl)propanamide
Homo sapiens
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.03
3-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(3-phenylpropyl)propanamide
Homo sapiens
IC50 above 0.03 mM, in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.03
3-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(diphenylmethyl)propanamide
Homo sapiens
IC50 above 0.03 mM, in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.000031
3-(cyclopentyloxy)-N-(2-(4-((2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl)phenyl)propan-2-yl)-benzenesulfonamide
Homo sapiens
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.000073
3-(cyclopropylmethoxy)-N-(2-(4-((2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl)phenyl)propan-2-yl)-benzenesulfonamide
Homo sapiens
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.000035
3-(cyclopropylmethoxy)-N-[5-[(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methoxy]-2-methylpentan-2-yl]benzenesulfonamide
Homo sapiens
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.0025
4-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(1-hydroxy-2-methyl-1,1-diphenylpropan-2-yl)butanamide
Homo sapiens
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.03
4-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(1-hydroxy-2-methylpropan-2-yl)butanamide
Homo sapiens
IC50 above 0.03 mM, in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.0013
4-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(2,2-diphenylethyl)-N-methylbutanamide
Homo sapiens
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.016
4-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(2,2-diphenylethyl)butanamide
Homo sapiens
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.03
4-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(2,4,4-trimethylpentan-2-yl)butanamide
Homo sapiens
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.0011
4-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(2-hydroxy-2,2-diphenylethyl)-N-methylbutanamide
Homo sapiens
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.03
4-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(2-methyl-1-phenylpropan-2-yl)butanamide
Homo sapiens
IC50 above 0.03 mM, in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.021
4-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(2-methyl-4-phenylbutan-2-yl)butanamide
Homo sapiens
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.03
4-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(2-phenylpropan-2-yl)butanamide
Homo sapiens
IC50 above 0.03 mM, in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.03
4-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(3-ethylpentan-3-yl)butanamide
Homo sapiens
IC50 above 0.03 mM, in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.03
4-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(diphenylmethyl)butanamide
Homo sapiens
IC50 above 0.03 mM, in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.03
4-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-phenylbutanamide
Homo sapiens
IC50 above 0.03 mM, in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.03
4-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-[2-methyl-1-(naphthalen-2-yl)propan-2-yl]butanamide
Homo sapiens
IC50 above 0.03 mM, in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.03
N,N-dibenzyl-3-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)propanamide
Homo sapiens
IC50 above 0.03 mM, in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.00127
N-(2-(4-((2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl)-phenyl)propan-2-yl)-3-methoxybenzenesulfonamide
Homo sapiens
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.0018
N-(2-(4-((2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl)-phenyl)propan-2-yl)benzenesulfonamide
Homo sapiens
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.03
N-benzyl-4-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)butanamide
Homo sapiens
IC50 above 0.03 mM, in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.00004
N-[(1R)-1-[3-(cyclopropylmethoxy)phenyl]ethyl]-3-[(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methoxy]propane-1-sulfonamide
Homo sapiens
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.00034
N-[2-[3-(cyclopropylmethoxy)phenyl]propan-2-yl]-3-[(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methoxy]propane-1-sulfonamide
Homo sapiens
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.0039
N-[5-[(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methoxy]-2-methylpentan-2-yl]benzenesulfonamide
Homo sapiens
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.0073
1-[3-(4-benzylpiperidin-1-yl)-3-oxopropyl]pyrimidine-2,4(1H,3H)-dione
Homo sapiens
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.03
1-[3-(4-benzylpiperidin-1-yl)-3-oxopropyl]pyrimidine-2,4(1H,3H)-dione
Homo sapiens
IC50 above 0.03 mM, in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
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Williams, M.V.; Cheng, Y.
Human deoxyuridine triphosphate nucleotidohydrolase. Purification and characterization of the deoxyuridine triphosphate nucleotidohydrolase from acute lymphocytic leukemia
J. Biol. Chem.
254
2897-2901
1979
Homo sapiens
brenda
Wist, E.
Partial purification of deoxyuridine triphosphate nucleotidohydrolase and its effect on DNA synthesis in isolated HeLa cell nuclei
Biochim. Biophys. Acta
565
98-106
1979
Homo sapiens
brenda
Ingraham, H.A.; Goulian, M.
Deoxyuridine triphosphatase: a potential site of interaction with pyrimidine nucleotide analogues
Biochem. Biophys. Res. Commun.
109
746-752
1982
Homo sapiens
brenda
Caradonna, S.J.; Adamkiewicz, D.M.
Purification and properties of the deoxyuridine triphosphate nucleotidohydrolase enzyme derived from HeLa S3 cells. Comparison to a distinct dUTP nucleotidohydrolase induced in herpes simplex virus-infected HeLa S3 cells
J. Biol. Chem.
259
5459-5464
1984
Human alphaherpesvirus 1, Homo sapiens
brenda
Williams, M.V.
Deoxyuridine triphosphate nucleotidohydrolase induced by herpes simplex virus type 1. Purification and characterization of induced enzyme
J. Biol. Chem.
259
10080-10084
1984
Human alphaherpesvirus 1, Homo sapiens
brenda
Ladner, R.D.; McNulty, D.E.; Carr, S.A.; Roberts, G.D.; Caradonna, S.J.
Characterization of distinct nuclear and mitochondrial forms of human deoxyuridine triphosphate nucleotidohydrolase
J. Biol. Chem.
271
7745-7751
1996
Homo sapiens (P33316), Homo sapiens
brenda
McIntosh, E.M.; Ager, D.D.; Gadsen, M.H.; Haynes, R.H.
Human dUTP pyrophosphatase: cDNA sequence and potential biological importance of the enzyme
Proc. Natl. Acad. Sci. USA
89
8020-8024
1992
Homo sapiens
brenda
Studebaker, A.W.; Lafuse, W.P.; Kloesel, R.; Williams, M.V.
Modulation of human dUTPase using small interfering RNA
Biochem. Biophys. Res. Commun.
327
306-310
2005
Homo sapiens (P33316), Homo sapiens
brenda
Nguyen, C.; Kasinathan, G.; Leal-Cortijo, I.; Musso-Buendia, A.; Kaiser, M.; Brun, R.; Ruiz-Perez, L.M.; Johansson, N.G.; Gonzalez-Pacanowska, D.; Gilbert, I.H.
Deoxyuridine triphosphate nucleotidohydrolase as a potential antiparasitic drug target
J. Med. Chem.
48
5942-5954
2005
Homo sapiens, Leishmania donovani, Leishmania major, Plasmodium falciparum
brenda
Nguyen, C.; Ruda, G.F.; Schipani, A.; Kasinathan, G.; Leal, I.; Musso-Buendia, A.; Kaiser, M.; Brun, R.; Ruiz-Perez, L.M.; Sahlberg, B.L.; Johansson, N.G.; Gonzalez-Pacanowska, D.; Gilbert, I.H.
Acyclic nucleoside analogues as inhibitors of Plasmodium falciparum dUTPase
J. Med. Chem.
49
4183-4195
2006
Homo sapiens, Plasmodium falciparum
brenda
Romeike, B.F.; Boeckeler, A.; Kremmer, E.; Sommer, P.; Krick, C.; Graesser, F.
Immunohistochemical detection of dUTPase in intracranial tumors
Pathol. Res. Pract.
201
727-732
2005
Homo sapiens
brenda
Wu, M.; Shen, J.; Zhan, J.; Yu, Y.
dUTP pyrophosphatase, its appearance in extracellular compartment may serve as a potential biomarker for N-methyl-N-nitro-N-nitrosoguanidine exposure in mammalian cells
Proteomics
6
3001-3007
2006
Homo sapiens
brenda
Lankat-Buttgereit, B.; Lenschen, B.; Schmidt, H.; Goeke, R.
The action of Pdcd4 may be cell type specific: evidence that reduction of dUTPase levels might contribute to its tumor suppressor activity in Bon-1 cells
Apoptosis
13
157-164
2008
Homo sapiens
brenda
Kajimoto, S.; Horie, M.; Manabe, H.; Masuda, Y.; Shibayama-Imazu, T.; Nakajo, S.; Gong, X.F.; Obama, T.; Itabe, H.; Nakaya, K.
A tyrosine kinase inhibitor, beta-hydroxyisovalerylshikonin, induced apoptosis in human lung cancer DMS114 cells through reduction of dUTP nucleotidohydrolase activity
Biochim. Biophys. Acta
1782
41-50
2008
Homo sapiens (P33316), Homo sapiens
brenda
Jiang, Y.L.; Chung, S.; Krosky, D.J.; Stivers, J.T.
Synthesis and high-throughput evaluation of triskelion uracil libraries for inhibition of human dUTPase and UNG2
Bioorg. Med. Chem.
14
5666-5672
2006
Homo sapiens
brenda
Varga, B.; Barabas, O.; Kovari, J.; Toth, J.; Hunyadi-Gulyas, E.; Klement, E.; Medzihradszky, K.F.; Toelgyesi, F.; Fidy, J.; Vertessy, B.G.
Active site closure facilitates juxtaposition of reactant atoms for initiation of catalysis by human dUTPase
FEBS Lett.
581
4783-4788
2007
Homo sapiens (P33316), Homo sapiens
brenda
Toth, J.; Varga, B.; Kovacs, M.; Malnasi-Csizmadia, A.; Vertessy, B.G.
Kinetic mechanism of human dUTPase, an essential nucleotide pyrophosphatase enzyme
J. Biol. Chem.
282
33572-33582
2007
Homo sapiens (P33316), Homo sapiens
brenda
Vertessy, B.G.; Toth, J.
Keeping uracil out of DNA: physiological role, structure and catalytic mechanism of dUTPases
Acc. Chem. Res.
42
97-106
2009
Homo sapiens (P33316), Homo sapiens
brenda
Takacs, E.; Barabas, O.; Petoukhov, M.V.; Svergun, D.I.; Vertessy, B.G.
Molecular shape and prominent role of beta-strand swapping in organization of dUTPase oligomers
FEBS Lett.
583
865-871
2009
Escherichia coli (P06968), Escherichia coli, Homo sapiens (P33316), Homo sapiens, Drosophila melanogaster (Q9V3I1)
brenda
Kawahara, A.; Akagi, Y.; Hattori, S.; Mizobe, T.; Shirouzu, K.; Ono, M.; Yanagawa, T.; Kuwano, M.; Kage, M.
Higher expression of deoxyuridine triphosphatase (dUTPase) may predict the metastasis potential of colorectal cancer
J. Clin. Pathol.
62
364-369
2009
Homo sapiens
brenda
Musso-Buendia, J.A.; Vidal, A.E.; Kasinthan, G.; Nguyen, C.; Carrero-Lerida, J.; Ruiz-Perez, L.M.; Wilson, K.; Johansson, N.G.; Gilbert, I.H.; Gonzalez-Pacanowska, D.
Kinetic properties and inhibition of the dimeric dUTPase-dUDPase from Campylobacter jejuni
J. Enzyme Inhib. Med. Chem.
24
111-116
2009
Campylobacter jejuni, Homo sapiens
brenda
Quesada-Soriano, I.; Casas-Solvas, J.M.; Recio, E.; Ruiz-Perez, L.M.; Vargas-Berenguel, A.; Gonzalez-Pacanowska, D.; Garcia-Fuentes, L.
Kinetic properties and specificity of trimeric Plasmodium falciparum and human dUTPases
Biochimie
92
178-186
2010
Homo sapiens, Plasmodium falciparum
brenda
Takacs, E.; Nagy, G.; Leveles, I.; Harmat, V.; Lopata, A.; Toth, J.; Vertessy, B.G.
Direct contacts between conserved motifs of different subunits provide major contribution to active site organization in human and mycobacterial dUTPases
FEBS Lett.
584
3047-3054
2010
Homo sapiens, Mycobacterium tuberculosis (P9WNS5), Mycobacterium tuberculosis H37Rv (P9WNS5)
brenda
Palmen, L.G.; Kvassman, J.O.
Differential inhibition of homotrimeric dUTPases by the 3-azido derivative of dideoxy-UTP
J. Enzyme Inhib. Med. Chem.
25
146-150
2010
Escherichia coli, equine infectious anemia virus, Homo sapiens
brenda
Pecsi, I.; Leveles, I.; Harmat, V.; Vertessy, B.G.; Toth, J.
Aromatic stacking between nucleobase and enzyme promotes phosphate ester hydrolysis in dUTPase
Nucleic Acids Res.
38
7179-7186
2010
Homo sapiens, Mycobacterium tuberculosis (P9WNS5), Mycobacterium tuberculosis H37Rv (P9WNS5)
brenda
Miyakoshi, H.; Miyahara, S.; Yokogawa, T.; Chong, K.T.; Taguchi, J.; Endoh, K.; Yano, W.; Wakasa, T.; Ueno, H.; Takao, Y.; Nomura, M.; Shuto, S.; Nagasawa, H.; Fukuoka, M.
Synthesis and discovery of N-carbonylpyrrolidine- or N-sulfonylpyrrolidine-containing uracil derivatives as potent human deoxyuridine triphosphatase inhibitors
J. Med. Chem.
55
2960-2969
2012
Homo sapiens (P33316), Homo sapiens
brenda
Miyahara, S.; Miyakoshi, H.; Yokogawa, T.; Chong, K.T.; Taguchi, J.; Muto, T.; Endoh, K.; Yano, W.; Wakasa, T.; Ueno, H.; Takao, Y.; Fujioka, A.; Hashimoto, A.; Itou, K.; Yamamura, K.; Nomura, M.; Nagasawa, H.; Shuto, S.; Fukuoka, M.
Discovery of highly potent human deoxyuridine triphosphatase inhibitors based on the conformation restriction strategy
J. Med. Chem.
55
5483-5496
2012
Homo sapiens (P33316), Homo sapiens
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Guiomar, P.; Andras, H.; Beata, G.; Luis, M.; Dolores, G.; Requena, C.; Vidal, A.
The nucleotidohydrolases DCTPP1 and dUTPase are involved in the cellular response to decitabine
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Homo sapiens, Homo sapiens (P33316)
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Rotoli, S.M.; Jones, J.L.; Caradonna, S.J.
Cysteine residues contribute to the dimerization and enzymatic activity of human nuclear dUTP nucleotidohydrolase (nDut)
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2018
Homo sapiens (P33316), Homo sapiens
brenda
Hizi, A.; Herzig, E.
dUTPase the frequently overlooked enzyme encoded by many retroviruses
Retrovirology
12
70
2015
bovine immunodeficiency virus, Caenorhabditis elegans, Caprine arthritis encephalitis virus, equine infectious anemia virus, Escherichia coli (P06968), feline immunodeficiency virus, Homo sapiens (P33316), Homo sapiens, Human endogenous retrovirus K, Human gammaherpesvirus 4, Human gammaherpesvirus 8, Jembrana disease virus, Mason-Pfizer monkey virus, mouse mammary tumor virus, Murid gammaherpesvirus 4, Mycobacterium tuberculosis, Plasmodium falciparum, Saccharomyces cerevisiae, Visna-maedi virus
brenda
Nyiri, K.; Mertens, H.D.T.; Tihanyi, B.; Nagy, G.N.; Kohegyi, B.; Matejka, J.; Harris, M.J.; Szabo, J.E.; Papp-Kadar, V.; Nemeth-Pongracz, V.; Ozohanics, O.; Vekey, K.; Svergun, D.I.; Borysik, A.J.; Vertessy, B.G.
Structural model of human dUTPase in complex with a novel proteinaceous inhibitor
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Homo sapiens
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