PMID-sentid	Pub_year	Sent_text	compound_name	comp_offset	prot_official_name	organism	prot_offset
32663205-5	2020	Overexpression of human uracil DNA glycosylase in MDM prior to infection resulted in rapid removal of dUMP from HIV cDNA and near complete depletion of dUMP-containing viral copies.	2'-deoxyuridylic acid	102-106	uracil DNA glycosylase	Homo sapiens	24-46
32663626-6	2020	A better understanding of the pathological role of IL-1 family cytokines in autoimmunity involves a deeper evaluation, in the pathological situations, of the possible anomalies in the feed-back anti-inflammatory mechanisms that in physiological reactions control and dump IL-1-mediated inflammation.	2'-deoxyuridylic acid	267-271	interleukin 1 alpha	Homo sapiens	51-55
32663626-6	2020	A better understanding of the pathological role of IL-1 family cytokines in autoimmunity involves a deeper evaluation, in the pathological situations, of the possible anomalies in the feed-back anti-inflammatory mechanisms that in physiological reactions control and dump IL-1-mediated inflammation.	2'-deoxyuridylic acid	267-271	interleukin 1 alpha	Homo sapiens	272-276
32663205-5	2020	Overexpression of human uracil DNA glycosylase in MDM prior to infection resulted in rapid removal of dUMP from HIV cDNA and near complete depletion of dUMP-containing viral copies.	2'-deoxyuridylic acid	152-156	uracil DNA glycosylase	Homo sapiens	24-46
31662460-7	2019	Our crystallographic and biochemical studies reveal that ASFV E165R is a member of trimeric dUTP nucleotidohydrolase (dUTPase) family that catalyzes the hydrolysis of dUTP into dUMP.	2'-deoxyuridylic acid	177-181	Deoxyuridine triphosphatase	Drosophila melanogaster	118-125
32715203-0	2020	dUMP/F-dUMP Binding to Thymidylate Synthase: Human Versus Mycobacterium tuberculosis.	2'-deoxyuridylic acid	0-4	thymidylate synthetase	Homo sapiens	23-43
32715203-1	2020	Thymidylate synthase is an enzyme that catalyzes deoxythymidine monophosphate (dTMP) synthesis from substrate deoxyuridine monophosphate (dUMP).	2'-deoxyuridylic acid	110-136	thymidylate synthetase	Homo sapiens	0-20
32715203-1	2020	Thymidylate synthase is an enzyme that catalyzes deoxythymidine monophosphate (dTMP) synthesis from substrate deoxyuridine monophosphate (dUMP).	2'-deoxyuridylic acid	138-142	thymidylate synthetase	Homo sapiens	0-20
31748385-4	2020	Here, we present the crystal structures of the ASFV dUTPase in complex with the product dUMP and cofactor Mg2+ at a resolution of 2.2 A.	2'-deoxyuridylic acid	88-92	Deoxyuridine triphosphatase	Drosophila melanogaster	52-59
31748385-11	2020	Here, we solved the crystal structure of the ASFV dUTPase-dUMP-Mg2+ complex.	2'-deoxyuridylic acid	58-62	Deoxyuridine triphosphatase	Drosophila melanogaster	50-57
31910901-2	2020	To begin to investigate how the pyrimidine biosynthetic pathway fulfills the demand for dTTP, we determined the catalytic properties and structure of the key enzyme deoxyuridine triphosphate nucleotidohydrolase (dUTPase) that hydrolyzes dUTP to dUMP, the precursor of dTTP.	2'-deoxyuridylic acid	245-249	Deoxyuridine triphosphatase	Drosophila melanogaster	212-219
31796083-3	2019	Deoxyuridine 5"-triphosphate nucleotido-hydrolase (dUTPase) is responsible for the hydrolysis of dUTP to dUMP within the parasite and has been proposed as an essential step in pyrimidine metabolism by providing dUMP for thymidylate biosynthesis.	2'-deoxyuridylic acid	105-109	Deoxyuridine triphosphatase	Drosophila melanogaster	51-58
31796083-3	2019	Deoxyuridine 5"-triphosphate nucleotido-hydrolase (dUTPase) is responsible for the hydrolysis of dUTP to dUMP within the parasite and has been proposed as an essential step in pyrimidine metabolism by providing dUMP for thymidylate biosynthesis.	2'-deoxyuridylic acid	211-215	Deoxyuridine triphosphatase	Drosophila melanogaster	51-58
31391279-4	2019	This observation contrasts with the existence in T. brucei of a dimeric deoxyuridine 5"-triphosphate nucleotidohydrolase (dUTPase), an essential enzyme that can produce dUMP via the hydrolysis of dUTP/dUDP.	2'-deoxyuridylic acid	169-173	Deoxyuridine triphosphatase	Drosophila melanogaster	122-129
31500803-1	2019	Thymidylate synthase (TS) catalyzes the production of the nucleotide dTMP from deoxyuridine monophosphate (dUMP), making the enzyme necessary for DNA replication and consequently a target for cancer therapeutics.	2'-deoxyuridylic acid	79-105	thymidylate synthetase	Homo sapiens	0-20
31500803-1	2019	Thymidylate synthase (TS) catalyzes the production of the nucleotide dTMP from deoxyuridine monophosphate (dUMP), making the enzyme necessary for DNA replication and consequently a target for cancer therapeutics.	2'-deoxyuridylic acid	107-111	thymidylate synthetase	Homo sapiens	0-20
31391279-5	2019	Thus, T. brucei dUTPase-null mutants are thymidine auxotrophs, suggesting that dUTPase might have a role in providing dUMP for thymidylate biosynthesis.	2'-deoxyuridylic acid	118-122	Deoxyuridine triphosphatase	Drosophila melanogaster	16-23
31391279-5	2019	Thus, T. brucei dUTPase-null mutants are thymidine auxotrophs, suggesting that dUTPase might have a role in providing dUMP for thymidylate biosynthesis.	2'-deoxyuridylic acid	118-122	Deoxyuridine triphosphatase	Drosophila melanogaster	79-86
31391279-6	2019	We show that overexpression of human dCMP deaminase (DCTD), an enzyme that provides directly dUMP through dCMP deamination, does not reverse the lethal phenotype of dUTPase knockout cells, which further supports the notion that in T. brucei, CDA is uniquely involved in providing dUMP, while the main role of dUTPase would be the withdrawal of the excess of dUTP to avoid its incorporation into DNA.	2'-deoxyuridylic acid	93-97	dCMP deaminase	Homo sapiens	53-57
30987342-2	2019	Deoxyuridine 5"-triphosphate nucleotidohydrolase (dUTPase) is a key enzyme in this pathway since it catalyzes the cleavage of 2"-deoxyuridine 5"-triphosphate (dUTP) into 2"-deoxyuridine 5"-monophosphate (dUMP) and inorganic pyrophosphate.	2'-deoxyuridylic acid	170-202	Deoxyuridine triphosphatase	Drosophila melanogaster	50-57
31351608-0	2019	Management of municipal solid waste open dumps immediately after the collapse: An integrated approach from Meethotamulla open dump, Sri Lanka.	2'-deoxyuridylic acid	41-46	sorcin	Homo sapiens	132-135
31351608-1	2019	Meethotamulla open dump (MOD) of Sri Lanka that has received about 290,000 metric tons of mixed MSW annually collapsed on 14th April 2017 with massive devastation.	2'-deoxyuridylic acid	19-23	sorcin	Homo sapiens	33-36
31152062-4	2019	We found that the region spanning amino acids 106-123, namely the Ca-loop of C. albicans TMPK (CaTMPK), contributes to the hyperactivity of this enzyme compared with the human enzyme (hTMPK) and to the utilization of deoxyuridine monophosphate (dUMP)/deoxy-5-fluorouridine monophosphate (5-FdUMP) as a substrate.	2'-deoxyuridylic acid	217-243	deoxythymidylate kinase	Homo sapiens	89-93
31152062-4	2019	We found that the region spanning amino acids 106-123, namely the Ca-loop of C. albicans TMPK (CaTMPK), contributes to the hyperactivity of this enzyme compared with the human enzyme (hTMPK) and to the utilization of deoxyuridine monophosphate (dUMP)/deoxy-5-fluorouridine monophosphate (5-FdUMP) as a substrate.	2'-deoxyuridylic acid	217-243	deoxythymidylate kinase	Homo sapiens	184-189
31152062-4	2019	We found that the region spanning amino acids 106-123, namely the Ca-loop of C. albicans TMPK (CaTMPK), contributes to the hyperactivity of this enzyme compared with the human enzyme (hTMPK) and to the utilization of deoxyuridine monophosphate (dUMP)/deoxy-5-fluorouridine monophosphate (5-FdUMP) as a substrate.	2'-deoxyuridylic acid	245-249	deoxythymidylate kinase	Homo sapiens	89-93
31152062-4	2019	We found that the region spanning amino acids 106-123, namely the Ca-loop of C. albicans TMPK (CaTMPK), contributes to the hyperactivity of this enzyme compared with the human enzyme (hTMPK) and to the utilization of deoxyuridine monophosphate (dUMP)/deoxy-5-fluorouridine monophosphate (5-FdUMP) as a substrate.	2'-deoxyuridylic acid	245-249	deoxythymidylate kinase	Homo sapiens	184-189
31077566-2	2019	The enzyme dUTPase is a prime example of such coupling, as it generates dUMP for thymidylate biosynthesis and removes dUTP for synthesis of uracil-free DNA.	2'-deoxyuridylic acid	72-76	Deoxyuridine triphosphatase	Drosophila melanogaster	11-18
30987342-2	2019	Deoxyuridine 5"-triphosphate nucleotidohydrolase (dUTPase) is a key enzyme in this pathway since it catalyzes the cleavage of 2"-deoxyuridine 5"-triphosphate (dUTP) into 2"-deoxyuridine 5"-monophosphate (dUMP) and inorganic pyrophosphate.	2'-deoxyuridylic acid	204-208	Deoxyuridine triphosphatase	Drosophila melanogaster	50-57
30987342-3	2019	Through its action dUTPase efficiently prevents uracil misincorporation into DNA and at the same time provides dUMP, the substrate for de novo thymidylate biosynthesis.	2'-deoxyuridylic acid	111-115	Deoxyuridine triphosphatase	Drosophila melanogaster	19-26
28693108-0	2017	Nitrate release from waste rock dumps in the Elk Valley, British Columbia, Canada.	2'-deoxyuridylic acid	32-37	potassium voltage-gated channel subfamily H member 8	Homo sapiens	45-48
30935102-0	2019	Structural Comparison of Enterococcus faecalis and Human Thymidylate Synthase Complexes with the Substrate dUMP and Its Analogue FdUMP Provides Hints about Enzyme Conformational Variabilities.	2'-deoxyuridylic acid	107-111	thymidylate synthetase	Homo sapiens	57-77
30306346-2	2019	A garbage dump at Meethotamulla in Sri Lanka suddenly collapsed, resulting in the death of 32 individuals.	2'-deoxyuridylic acid	10-14	sorcin	Homo sapiens	35-38
30574873-3	2019	The cellular enzyme thymidylate synthase (TS) catalyses the conversion of dUMP to TMP, which is converted to TDP and ultimately to TTP, a building block in DNA synthesis.	2'-deoxyuridylic acid	74-78	thymidylate synthetase	Homo sapiens	20-40
29859430-2	2018	The decomposition and oxidation of undetonated explosives can result in high NO3- concentrations in waters emanating from waste rock dumps.	2'-deoxyuridylic acid	133-138	NBL1, DAN family BMP antagonist	Homo sapiens	77-80
29859430-3	2018	We used the stable isotopic composition of NO3- (delta15N- and delta18O-NO3-) to define and quantify the controls on NO3- composition in waste rock dumps by studying water-unsaturated and saturated conditions at nine coal waste rock dumps located in the Elk Valley, British Columbia, Canada.	2'-deoxyuridylic acid	148-153	NBL1, DAN family BMP antagonist	Homo sapiens	43-46
29946843-2	2018	The source of NO3 in groundwater includes surface leaching from wastewater and waste dump sites, animal excreta disposal, industrial effluents, and N-based fertilizers, etc.	2'-deoxyuridylic acid	85-89	NBL1, DAN family BMP antagonist	Homo sapiens	14-17
29258758-1	2018	Thymidylate synthase (TYMS) is a key enzyme in the de novo synthesis of 2"-deoxythymidine-5"-monophosphate (dTMP) from 2"-deoxyuridine-5"-monophosphate (dUMP).	2'-deoxyuridylic acid	119-151	thymidylate synthase	Mus musculus	0-20
29258758-1	2018	Thymidylate synthase (TYMS) is a key enzyme in the de novo synthesis of 2"-deoxythymidine-5"-monophosphate (dTMP) from 2"-deoxyuridine-5"-monophosphate (dUMP).	2'-deoxyuridylic acid	119-151	thymidylate synthase	Mus musculus	22-26
29258758-1	2018	Thymidylate synthase (TYMS) is a key enzyme in the de novo synthesis of 2"-deoxythymidine-5"-monophosphate (dTMP) from 2"-deoxyuridine-5"-monophosphate (dUMP).	2'-deoxyuridylic acid	153-157	thymidylate synthase	Mus musculus	0-20
29258758-1	2018	Thymidylate synthase (TYMS) is a key enzyme in the de novo synthesis of 2"-deoxythymidine-5"-monophosphate (dTMP) from 2"-deoxyuridine-5"-monophosphate (dUMP).	2'-deoxyuridylic acid	153-157	thymidylate synthase	Mus musculus	22-26
29258758-4	2018	TYMS activity was significantly inhibited with decreased dTMP and accumulation of dUMP after 5-FU injection.	2'-deoxyuridylic acid	82-86	thymidylate synthase	Mus musculus	0-4
30902068-3	2019	dUTPase catalyzes the hydrolysis of dUTP to dUMP and pyrophosphate.	2'-deoxyuridylic acid	44-48	Deoxyuridine triphosphatase	Drosophila melanogaster	0-7
30180988-2	2019	Thymidylate synthase (TYMS) is a key enzyme in DNA synthesis that catalyzes the conversion of deoxyuridine monophosphate to dTMP.	2'-deoxyuridylic acid	94-120	thymidylate synthetase	Homo sapiens	0-20
30180988-2	2019	Thymidylate synthase (TYMS) is a key enzyme in DNA synthesis that catalyzes the conversion of deoxyuridine monophosphate to dTMP.	2'-deoxyuridylic acid	94-120	thymidylate synthetase	Homo sapiens	22-26
29859430-4	2018	Estimates of the extent of nitrification of NH4NO3 in oxic zones in the dumps, initial NO3- concentrations prior to denitrification, and the extent of NO3- removal by denitrification in sub-oxic to anoxic zones are provided.	2'-deoxyuridylic acid	72-77	NBL1, DAN family BMP antagonist	Homo sapiens	47-50
29859430-5	2018	delta15N data from unsaturated waste rock dumps confirm NO3- is derived from blasting.	2'-deoxyuridylic acid	42-47	NBL1, DAN family BMP antagonist	Homo sapiens	56-59
29735940-2	2018	Although the physical structure of TYMS and the molecular mechanisms of TYMS catalyzing the conversion of deoxyuridine monophosphate (dUMP) to dTMP have been the subject of thorough studies, its oligomeric structure remains unclear.	2'-deoxyuridylic acid	106-132	thymidylate synthetase	Homo sapiens	72-76
29735940-2	2018	Although the physical structure of TYMS and the molecular mechanisms of TYMS catalyzing the conversion of deoxyuridine monophosphate (dUMP) to dTMP have been the subject of thorough studies, its oligomeric structure remains unclear.	2'-deoxyuridylic acid	134-138	thymidylate synthetase	Homo sapiens	35-39
29735940-2	2018	Although the physical structure of TYMS and the molecular mechanisms of TYMS catalyzing the conversion of deoxyuridine monophosphate (dUMP) to dTMP have been the subject of thorough studies, its oligomeric structure remains unclear.	2'-deoxyuridylic acid	134-138	thymidylate synthetase	Homo sapiens	72-76
28575832-0	2017	Estimates of water and solute release from a coal waste rock dump in the Elk Valley, British Columbia, Canada.	2'-deoxyuridylic acid	61-65	potassium voltage-gated channel subfamily H member 8	Homo sapiens	73-76
28796306-3	2017	Reconstitution of both flavin-dependent RNA methyltransferase and thymidylate synthase apoproteins with this synthetic compound led to active enzymes for the C5-uracil methylation within their respective transfer RNA and dUMP substrate.	2'-deoxyuridylic acid	221-225	thymidylate synthetase	Homo sapiens	66-86
28787572-1	2017	Nuclear human uracil-DNA glycosylase (hUNG2) initiates base excision repair (BER) of genomic uracils generated through misincorporation of dUMP or through deamination of cytosines.	2'-deoxyuridylic acid	139-143	uracil DNA glycosylase	Homo sapiens	14-36
28787572-1	2017	Nuclear human uracil-DNA glycosylase (hUNG2) initiates base excision repair (BER) of genomic uracils generated through misincorporation of dUMP or through deamination of cytosines.	2'-deoxyuridylic acid	139-143	uracil DNA glycosylase	Homo sapiens	38-43
28729658-1	2017	dUTPase superfamily enzymes generate dUMP, the obligate precursor for de novo dTTP biosynthesis, from either dUTP (monofunctional dUTPase, Dut) or dCTP (bifunctional dCTP deaminase/dUTPase, Dcd:dut).	2'-deoxyuridylic acid	37-41	Deoxyuridine triphosphatase	Drosophila melanogaster	0-7
28746850-1	2017	Uracil DNA Glycosylase (UNG2) is the primary enzyme in humans that prevents the stable incorporation of deoxyuridine monophosphate into DNA in the form of U/A basepairs.	2'-deoxyuridylic acid	104-130	uracil DNA glycosylase	Homo sapiens	0-22
28746850-1	2017	Uracil DNA Glycosylase (UNG2) is the primary enzyme in humans that prevents the stable incorporation of deoxyuridine monophosphate into DNA in the form of U/A basepairs.	2'-deoxyuridylic acid	104-130	uracil DNA glycosylase	Homo sapiens	24-28
28729658-1	2017	dUTPase superfamily enzymes generate dUMP, the obligate precursor for de novo dTTP biosynthesis, from either dUTP (monofunctional dUTPase, Dut) or dCTP (bifunctional dCTP deaminase/dUTPase, Dcd:dut).	2'-deoxyuridylic acid	37-41	Deoxyuridine triphosphatase	Drosophila melanogaster	130-137
28729658-1	2017	dUTPase superfamily enzymes generate dUMP, the obligate precursor for de novo dTTP biosynthesis, from either dUTP (monofunctional dUTPase, Dut) or dCTP (bifunctional dCTP deaminase/dUTPase, Dcd:dut).	2'-deoxyuridylic acid	37-41	deoxyuridine triphosphatase	Homo sapiens	139-142
28729658-1	2017	dUTPase superfamily enzymes generate dUMP, the obligate precursor for de novo dTTP biosynthesis, from either dUTP (monofunctional dUTPase, Dut) or dCTP (bifunctional dCTP deaminase/dUTPase, Dcd:dut).	2'-deoxyuridylic acid	37-41	Deoxyuridine triphosphatase	Drosophila melanogaster	130-137
28729658-1	2017	dUTPase superfamily enzymes generate dUMP, the obligate precursor for de novo dTTP biosynthesis, from either dUTP (monofunctional dUTPase, Dut) or dCTP (bifunctional dCTP deaminase/dUTPase, Dcd:dut).	2'-deoxyuridylic acid	37-41	dermcidin	Homo sapiens	190-193
28729658-1	2017	dUTPase superfamily enzymes generate dUMP, the obligate precursor for de novo dTTP biosynthesis, from either dUTP (monofunctional dUTPase, Dut) or dCTP (bifunctional dCTP deaminase/dUTPase, Dcd:dut).	2'-deoxyuridylic acid	37-41	deoxyuridine triphosphatase	Homo sapiens	194-197
28580921-3	2017	hTS binds 2"-deoxyuridine 5"-monophosphate (dUMP) and the folate co-substrate N5,N10-methylenetetrahydrofolate (meTHF) in a pocket near the catalytic residue Cys195.	2'-deoxyuridylic acid	10-42	APC down-regulated 1	Homo sapiens	0-3
28580921-8	2017	Here, the structure of apo hTS crystallized in the active form with sulfate ions coordinated by the arginine residue that binds dUMP is reported.	2'-deoxyuridylic acid	128-132	APC down-regulated 1	Homo sapiens	27-30
28580921-3	2017	hTS binds 2"-deoxyuridine 5"-monophosphate (dUMP) and the folate co-substrate N5,N10-methylenetetrahydrofolate (meTHF) in a pocket near the catalytic residue Cys195.	2'-deoxyuridylic acid	44-48	APC down-regulated 1	Homo sapiens	0-3
27936107-3	2016	Thymidylate synthase catalyzes the conversion of 2"-deoxyuridine-5"-monophosphate (dUMP) to thymidine-5"-monophosphate (dTMP) using 5,10-methylenetetrahydrofolate (mTHF) as a co-substrate.	2'-deoxyuridylic acid	49-81	thymidylate synthetase	Homo sapiens	0-20
27890409-9	2017	Secondary Fe oxyhydroxides act as a long-term sink for As under present day hydrologic settings in waste rock dumps in the Elk Valley.	2'-deoxyuridylic acid	110-115	potassium voltage-gated channel subfamily H member 8	Homo sapiens	123-126
27785684-0	2017	Erratum to: Investigation of the S1/ICT equilibrium in fucoxanthin by ultrafast pump-dump-probe and femtosecond stimulated Raman scattering spectroscopy.	2'-deoxyuridylic acid	85-89	proteasome 26S subunit, non-ATPase 1	Homo sapiens	33-39
27936107-3	2016	Thymidylate synthase catalyzes the conversion of 2"-deoxyuridine-5"-monophosphate (dUMP) to thymidine-5"-monophosphate (dTMP) using 5,10-methylenetetrahydrofolate (mTHF) as a co-substrate.	2'-deoxyuridylic acid	83-87	thymidylate synthetase	Homo sapiens	0-20
27936107-4	2016	The crystal structures of thymidylate synthase from KSHV (apo), complexes with dUMP (binary), and complexes with both dUMP and raltitrexed (ternary) were determined at 1.7 A, 2.0 A, and 2.4 A, respectively.	2'-deoxyuridylic acid	118-122	ORF70	Human gammaherpesvirus 8	26-46
27498408-1	2016	Deoxyuridine 5"-triphosphate pyrophosphatase (dUTPase), a ubiquitous enzyme that catalyzes the hydrolysis of dUTP to dUMP and found in many viruses, has yet to be identified in fowl adenovirus 9 (FAdV-9).	2'-deoxyuridylic acid	117-121	Deoxyuridine triphosphatase	Drosophila melanogaster	46-53
27575846-0	2016	Characterization of temporal variations in landfill gas components inside an open solid waste dump site in Sri Lanka.	2'-deoxyuridylic acid	94-98	sorcin	Homo sapiens	107-110
27820863-5	2016	Unlike humans, T. brucei and all other kinetoplastids lack dCMP deaminase (DCTD), which provides an alternative route to dUMP formation.	2'-deoxyuridylic acid	121-125	dCMP deaminase	Homo sapiens	75-79
27026843-8	2016	The drugs were superimposed on the resolved crystal structure (at 1.9 A) of ZD1694/dUMP/TYMS system to shed light on similarity of the binding of capecitabine, and its modifiers, to that of ZD1694.	2'-deoxyuridylic acid	83-87	thymidylate synthetase	Homo sapiens	88-92
27214228-1	2016	Many microorganisms use flavin-dependent thymidylate synthase (FDTS) to synthesize the essential nucleotide 2"-deoxythymidine 5"-monophosphate (dTMP) from 2"-deoxyuridine 5"-monophosphate (dUMP), 5,10-methylenetetrahydrofolate (CH2THF), and NADPH.	2'-deoxyuridylic acid	155-187	thymidylate synthetase	Homo sapiens	41-61
27214228-1	2016	Many microorganisms use flavin-dependent thymidylate synthase (FDTS) to synthesize the essential nucleotide 2"-deoxythymidine 5"-monophosphate (dTMP) from 2"-deoxyuridine 5"-monophosphate (dUMP), 5,10-methylenetetrahydrofolate (CH2THF), and NADPH.	2'-deoxyuridylic acid	189-193	thymidylate synthetase	Homo sapiens	41-61
26748441-4	2016	Here we report high to medium resolution structures of native porcine RNase 4 (PL3), a "substrate-specificity" determining mutant D80A and their respective complexes with deoxyuridine 5"-monophosphate (dUMP) and deoxycytidine 5"-monophosphate (dCMP).	2'-deoxyuridylic acid	171-200	ribonuclease A family member 4	Homo sapiens	70-77
26748441-4	2016	Here we report high to medium resolution structures of native porcine RNase 4 (PL3), a "substrate-specificity" determining mutant D80A and their respective complexes with deoxyuridine 5"-monophosphate (dUMP) and deoxycytidine 5"-monophosphate (dCMP).	2'-deoxyuridylic acid	202-206	ribonuclease A family member 4	Homo sapiens	70-77
26748441-7	2016	Compared to the previously reported structure of the human RNase 4 2"-deoxyuridine 3"-phosphate complex, the structure of PL3 dUMP complex shows additional hydrogen bonds between the ligand and the protein.	2'-deoxyuridylic acid	126-130	ribonuclease A family member 4	Homo sapiens	59-66
26742754-0	2016	Investigation of the S1/ICT equilibrium in fucoxanthin by ultrafast pump-dump-probe and femtosecond stimulated Raman scattering spectroscopy.	2'-deoxyuridylic acid	73-77	proteasome 26S subunit, non-ATPase 1	Homo sapiens	21-27
26208523-3	2015	In the p53-proficient colorectal cancer cell line HCT116, oxaliplatin represses the expression of deoxyuridine triphosphatase (dUTPase), a ubiquitous pyrophosphatase that catalyzes the hydrolysis of dUTP to dUMP and inhibits dUTP-mediated cytotoxicity.	2'-deoxyuridylic acid	207-211	deoxyuridine triphosphatase	Homo sapiens	98-125
25912171-2	2015	TSase catalyzes a multi-step mechanism that includes the abstraction of a proton from the C5 of the substrate 2"-deoxyuridine-5"-monophosphate (dUMP).	2'-deoxyuridylic acid	110-142	thymidylate synthetase	Homo sapiens	0-5
25912171-2	2015	TSase catalyzes a multi-step mechanism that includes the abstraction of a proton from the C5 of the substrate 2"-deoxyuridine-5"-monophosphate (dUMP).	2'-deoxyuridylic acid	144-148	thymidylate synthetase	Homo sapiens	0-5
26630264-2	2015	VZV encodes a functional thymidylate synthase (TS), which is the sole enzyme that produces dTMP from dUMP de novo.	2'-deoxyuridylic acid	101-105	thymidylate synthase	Human alphaherpesvirus 3	25-45
26443810-1	2015	Thymidylate synthase (TYMS; EC 2.1.1.15) catalyzes the reductive methylation of 2"-deoxyuridine-5"-monophosphate (dUMP) by N(5),N(10)-methyhlenetetrahydrofolate, forming dTMP for the maintenance of DNA replication and repair.	2'-deoxyuridylic acid	80-112	thymidylate synthetase	Homo sapiens	0-20
26443810-1	2015	Thymidylate synthase (TYMS; EC 2.1.1.15) catalyzes the reductive methylation of 2"-deoxyuridine-5"-monophosphate (dUMP) by N(5),N(10)-methyhlenetetrahydrofolate, forming dTMP for the maintenance of DNA replication and repair.	2'-deoxyuridylic acid	80-112	thymidylate synthetase	Homo sapiens	22-26
26443810-1	2015	Thymidylate synthase (TYMS; EC 2.1.1.15) catalyzes the reductive methylation of 2"-deoxyuridine-5"-monophosphate (dUMP) by N(5),N(10)-methyhlenetetrahydrofolate, forming dTMP for the maintenance of DNA replication and repair.	2'-deoxyuridylic acid	114-118	thymidylate synthetase	Homo sapiens	0-20
26443810-1	2015	Thymidylate synthase (TYMS; EC 2.1.1.15) catalyzes the reductive methylation of 2"-deoxyuridine-5"-monophosphate (dUMP) by N(5),N(10)-methyhlenetetrahydrofolate, forming dTMP for the maintenance of DNA replication and repair.	2'-deoxyuridylic acid	114-118	thymidylate synthetase	Homo sapiens	22-26
26666293-1	2015	BACKGROUND: Deoxyuridine triphosphate nucleotidohydrolase (dUTPase) hydrolyzes dUTP to dUMP and pyrophosphate to maintain the cellular thymine-uracil ratio.	2'-deoxyuridylic acid	87-91	Deoxyuridine triphosphatase	Drosophila melanogaster	59-66
26208523-3	2015	In the p53-proficient colorectal cancer cell line HCT116, oxaliplatin represses the expression of deoxyuridine triphosphatase (dUTPase), a ubiquitous pyrophosphatase that catalyzes the hydrolysis of dUTP to dUMP and inhibits dUTP-mediated cytotoxicity.	2'-deoxyuridylic acid	207-211	Deoxyuridine triphosphatase	Drosophila melanogaster	127-134
25997777-1	2015	Inspired by TSase catalysis for dUMP conversion to dTMP, a biomodel reagent is developed.	2'-deoxyuridylic acid	32-36	thymidylate synthetase	Homo sapiens	12-17
25663396-0	2015	Dioxin-like PCB levels in maternal and umbilical cord sera of people living near dump sites in southern Italy: a pilot study of biomonitoring.	2'-deoxyuridylic acid	81-85	pyruvate carboxylase	Homo sapiens	12-15
25581782-4	2015	TSase catalyzes the reductive methylation of 2"-deoxy-uridylate (dUMP) to dTMP using (R)-N(5),N(10)-methylene-5,6,7,8-tetrahydrofolate (MTHF) as a cofactor.	2'-deoxyuridylic acid	45-63	thymidylate synthetase	Homo sapiens	0-5
25562513-3	2015	Because of the structural similarity of one metabolite of dFdC, dFdUMP, with the natural substrate for thymidylate synthase (TS) dUMP, we investigated whether dFdC and its deamination product 2",2"-difluoro-2"-deoxyuridine (dFdU) would inhibit TS.	2'-deoxyuridylic acid	66-70	thymidylate synthetase	Homo sapiens	103-123
25581782-4	2015	TSase catalyzes the reductive methylation of 2"-deoxy-uridylate (dUMP) to dTMP using (R)-N(5),N(10)-methylene-5,6,7,8-tetrahydrofolate (MTHF) as a cofactor.	2'-deoxyuridylic acid	65-69	thymidylate synthetase	Homo sapiens	0-5
24321279-1	2014	Crystal structure is presented of the binary complex between potassium phosphoramidate-phosphorylated recombinant C. elegans thymidylate synthase and dUMP.	2'-deoxyuridylic acid	150-154	Thymidylate synthase	Caenorhabditis elegans	125-145
26745074-1	2015	BACKGROUND: Thymidylate synthase (TS) catalyzes the methylation of deoxyuridylate to deoxythymidylate and is involved in DNA methylation, synthesis and repair.	2'-deoxyuridylic acid	67-81	thymidylate synthetase	Homo sapiens	12-32
25537069-3	2015	Communities in close proximity to mine dumps had an increased likelihood of current wheeze OR 1.38 (95 % CI: 1.10-1.71), rhinoconjunctivitis OR 1.54 (95 % CI: 1.29-1.82), and a protective association with asthma OR 0.29 (95 % CI: 0.23-0.35).	2'-deoxyuridylic acid	39-44	olfactory receptor family 6 subfamily F member 1	Homo sapiens	91-98
25537069-3	2015	Communities in close proximity to mine dumps had an increased likelihood of current wheeze OR 1.38 (95 % CI: 1.10-1.71), rhinoconjunctivitis OR 1.54 (95 % CI: 1.29-1.82), and a protective association with asthma OR 0.29 (95 % CI: 0.23-0.35).	2'-deoxyuridylic acid	39-44	olfactory receptor family 2 subfamily M member 3	Homo sapiens	141-148
25415336-12	2014	IGFBP-3 was positively correlated with IGF-1 and house close to an e-waste dump.	2'-deoxyuridylic acid	75-79	insulin like growth factor binding protein 3	Homo sapiens	0-7
23726796-2	2013	In the folate pathway, TYMS catalyzes the methylation of deoxyuridylate to deoxythymidylate using 5,10-methylenetetrahydrofolate [5,10-CH2=THF, derived from tetrahydrofolate (THF)], as a cofactor.	2'-deoxyuridylic acid	57-71	thymidylate synthetase	Homo sapiens	23-27
24023064-9	2013	MALDI-TOF MS analysis of the reaction products demonstrated that APE1-catalyzed cleavage of a U G duplex generates the expected DNA fragments containing a 5"-terminal deoxyuridine monophosphate.	2'-deoxyuridylic acid	167-193	apurinic/apyrimidinic endodeoxyribonuclease 1	Homo sapiens	65-69
24995339-0	2014	Crystal structure of mouse thymidylate synthase in tertiary complex with dUMP and raltitrexed reveals N-terminus architecture and two different active site conformations.	2'-deoxyuridylic acid	73-77	thymidylate synthase	Mus musculus	27-47
24995339-1	2014	The crystal structure of mouse thymidylate synthase (mTS) in complex with substrate dUMP and antifolate inhibitor Raltitrexed is reported.	2'-deoxyuridylic acid	84-88	thymidylate synthase	Mus musculus	31-51
24995339-1	2014	The crystal structure of mouse thymidylate synthase (mTS) in complex with substrate dUMP and antifolate inhibitor Raltitrexed is reported.	2'-deoxyuridylic acid	84-88	tumor suppressor region 1	Mus musculus	53-56
24995339-5	2014	Conformational changes leading to a ligand-induced closing of the active site cleft are observed by comparing the crystal structures of mTS in three different states along the catalytic pathway: ligand-free, dUMP-bound, and dUMP- and Raltitrexed-bound.	2'-deoxyuridylic acid	208-212	tumor suppressor region 1	Mus musculus	136-139
24995339-5	2014	Conformational changes leading to a ligand-induced closing of the active site cleft are observed by comparing the crystal structures of mTS in three different states along the catalytic pathway: ligand-free, dUMP-bound, and dUMP- and Raltitrexed-bound.	2'-deoxyuridylic acid	224-228	tumor suppressor region 1	Mus musculus	136-139
24147825-0	2013	2"-Deoxyuridine 5"-monophosphate substrate displacement in thymidylate synthase through 6-hydroxy-2H-naphtho[1,8-bc]furan-2-one derivatives.	2'-deoxyuridylic acid	0-32	thymidylate synthetase	Homo sapiens	59-79
23239172-7	2013	The simulations were based on the crystal structure of hTS ternary complex with dUMP and Tomudex (PDB code: 1I00), with the Tomudex molecule replaced by the molecule of TS cofactor analogue, tetrahydrofolate.	2'-deoxyuridylic acid	80-84	thymidylate synthetase	Homo sapiens	56-58
23705822-0	2013	Effect of halogen substitutions on dUMP to stability of thymidylate synthase/dUMP/mTHF ternary complex using molecular dynamics simulation.	2'-deoxyuridylic acid	35-39	thymidylate synthetase	Homo sapiens	56-76
23705822-0	2013	Effect of halogen substitutions on dUMP to stability of thymidylate synthase/dUMP/mTHF ternary complex using molecular dynamics simulation.	2'-deoxyuridylic acid	77-81	thymidylate synthetase	Homo sapiens	56-76
23558980-4	2013	Among the PCB congeners, high relative similarity was observed between the e-waste dump site soil (EW1) and Aroclor 1254, implying that the technical product Aroclor 1254 was one of the major sources of PCB contamination.	2'-deoxyuridylic acid	83-87	pyruvate carboxylase	Homo sapiens	10-13
24563811-2	2013	In contrast to the human thymidylate synthase enzyme that utilizes methylene-tetrahydrofolate (CH2H4 folate) for the conversion of dUMP to dTMP, the microbial enzymes utilize an additional non-covalently bound FAD molecule for the hydride transfer from NAD(P)H.	2'-deoxyuridylic acid	131-135	thymidylate synthetase	Homo sapiens	25-45
23404871-2	2013	Thymidylate synthase (TYMS) is a folate-dependent enzyme that catalyzes reductive methylation of deoxyuridylate to thymidylate, thereby playing a central role in DNA synthesis and repair.	2'-deoxyuridylic acid	97-111	thymidylate synthetase	Homo sapiens	0-20
23404871-2	2013	Thymidylate synthase (TYMS) is a folate-dependent enzyme that catalyzes reductive methylation of deoxyuridylate to thymidylate, thereby playing a central role in DNA synthesis and repair.	2'-deoxyuridylic acid	97-111	thymidylate synthetase	Homo sapiens	22-26
23314484-1	2013	A simple, selective, and sensitive method utilizing tritium ((3)H) release from (3)H-deoxyuridine 5"-monophosphate (dUMP) substrate for accurate and precise determination of the low basal thymidylate synthase activity (TSA) in normal healthy peripheral blood mononuclear cells (PBMCs) was developed and validated.	2'-deoxyuridylic acid	85-114	thymidylate synthetase	Homo sapiens	188-208
23314484-1	2013	A simple, selective, and sensitive method utilizing tritium ((3)H) release from (3)H-deoxyuridine 5"-monophosphate (dUMP) substrate for accurate and precise determination of the low basal thymidylate synthase activity (TSA) in normal healthy peripheral blood mononuclear cells (PBMCs) was developed and validated.	2'-deoxyuridylic acid	116-120	thymidylate synthetase	Homo sapiens	188-208
24460328-1	2013	Thymidylate synthase (TS) catalyzes the transfer of a methyl group from methylenetetrahydrofolate to dUMP to form dTMP.	2'-deoxyuridylic acid	101-105	thymidylate synthetase	Homo sapiens	0-20
24460328-1	2013	Thymidylate synthase (TS) catalyzes the transfer of a methyl group from methylenetetrahydrofolate to dUMP to form dTMP.	2'-deoxyuridylic acid	101-105	APC down-regulated 1	Homo sapiens	22-24
23019356-1	2012	The DNA nucleotide thymidylate is synthesized by the enzyme thymidylate synthase, which catalyzes the reductive methylation of deoxyuridylate using the cofactor methylene-tetrahydrofolate (CH(2)H(4)folate).	2'-deoxyuridylic acid	127-141	thymidylate synthetase	Homo sapiens	60-80
22512654-1	2012	ThyX, a flavin-dependent thymidylate synthase that is involved in the synthesis of dTMP from dUMP, is a promising target for the development of novel antibacterial drugs that aimed at blocking the biosynthesis of dTMP, one of the building blocks of DNA.	2'-deoxyuridylic acid	93-97	FAD-dependent thymidylate synthase	Helicobacter pylori 26695	0-4
22512654-6	2012	Here we report the crystal structure of ThyX from Helicobacter pylori strain 26695 in complex with co-factor FAD and substrate dUMP at 2.5 A resolution, which consists of a 1.5 tetramer of ThyX with a total of 1248 residues, six FAD and six dUMP molecules in an asymmetric unit.	2'-deoxyuridylic acid	127-131	FAD-dependent thymidylate synthase	Helicobacter pylori 26695	40-44
22512654-6	2012	Here we report the crystal structure of ThyX from Helicobacter pylori strain 26695 in complex with co-factor FAD and substrate dUMP at 2.5 A resolution, which consists of a 1.5 tetramer of ThyX with a total of 1248 residues, six FAD and six dUMP molecules in an asymmetric unit.	2'-deoxyuridylic acid	127-131	FAD-dependent thymidylate synthase	Helicobacter pylori 26695	189-193
22512654-6	2012	Here we report the crystal structure of ThyX from Helicobacter pylori strain 26695 in complex with co-factor FAD and substrate dUMP at 2.5 A resolution, which consists of a 1.5 tetramer of ThyX with a total of 1248 residues, six FAD and six dUMP molecules in an asymmetric unit.	2'-deoxyuridylic acid	241-245	FAD-dependent thymidylate synthase	Helicobacter pylori 26695	40-44
22512654-7	2012	The structure revealed the key residues that are involved in co-factor FAD and substrate dUMP binding, site-directed mutagenesis were performed to analysis the importance of these residues on ThyX activity by genetic complementation and FAD binding assay.	2'-deoxyuridylic acid	89-93	FAD-dependent thymidylate synthase	Helicobacter pylori 26695	192-196
22307944-1	2012	Thymidylate synthase (TS) is an important enzyme involved in folate metabolism and catalyzes methylation of deoxyuridine monophosphate to deoxythymidine monophosphate, which is essential for DNA replication.	2'-deoxyuridylic acid	108-134	thymidylate synthetase	Homo sapiens	0-20
22307944-1	2012	Thymidylate synthase (TS) is an important enzyme involved in folate metabolism and catalyzes methylation of deoxyuridine monophosphate to deoxythymidine monophosphate, which is essential for DNA replication.	2'-deoxyuridylic acid	108-134	thymidylate synthetase	Homo sapiens	22-24
22224900-1	2012	Both ThyA and ThyX proteins catalyze the transfer of the methyl group from methylenetetrahydrofolate (CH(2) H(4) -folate) to dUMP, forming dTMP.	2'-deoxyuridylic acid	125-129	FAD-dependent thymidylate synthase	Corynebacterium glutamicum ATCC 13032	14-18
22093367-2	2012	This activity is compromised when vitamin B12 concentration is low because methionine synthase activity is reduced, lowering the concentration of S-adenosyl methionine (SAM) which in turn may diminish DNA methylation and cause folate to become unavailable for the conversion of dUMP to dTMP.	2'-deoxyuridylic acid	278-282	5-methyltetrahydrofolate-homocysteine methyltransferase	Homo sapiens	75-94
22809153-1	2012	We have examined the influence of centrin 2 (Cen2) on the interaction of nucleotide excision repair factors (XPC-HR23b, RPA, and XPA) with 48-mer DNA duplexes bearing the dUMP derivative 5-{3-[6-(carboxyamidofluoresceinyl)amidocapromoyl]allyl}-2"-deoxyuridine-5"-monophosphate.	2'-deoxyuridylic acid	171-175	centrin 2	Homo sapiens	34-43
22809153-1	2012	We have examined the influence of centrin 2 (Cen2) on the interaction of nucleotide excision repair factors (XPC-HR23b, RPA, and XPA) with 48-mer DNA duplexes bearing the dUMP derivative 5-{3-[6-(carboxyamidofluoresceinyl)amidocapromoyl]allyl}-2"-deoxyuridine-5"-monophosphate.	2'-deoxyuridylic acid	171-175	centrin 2	Homo sapiens	45-49
22809153-1	2012	We have examined the influence of centrin 2 (Cen2) on the interaction of nucleotide excision repair factors (XPC-HR23b, RPA, and XPA) with 48-mer DNA duplexes bearing the dUMP derivative 5-{3-[6-(carboxyamidofluoresceinyl)amidocapromoyl]allyl}-2"-deoxyuridine-5"-monophosphate.	2'-deoxyuridylic acid	171-175	XPC complex subunit, DNA damage recognition and repair factor	Homo sapiens	109-112
23056627-7	2012	Our data also suggest that the inhibition of the catalytic activity of hTS and the up-regulation of the hTS protein level are not causally linked, as the inactivated ternary complex, formed by hTS, deoxyuridine monophosphate and methylenetetrahydrofolate, was detected already 3 hours after 5-FU exposure, whereas substantial increase in global TS levels was detected only after 24 hours.	2'-deoxyuridylic acid	198-224	APC down-regulated 1	Homo sapiens	71-74
23056627-7	2012	Our data also suggest that the inhibition of the catalytic activity of hTS and the up-regulation of the hTS protein level are not causally linked, as the inactivated ternary complex, formed by hTS, deoxyuridine monophosphate and methylenetetrahydrofolate, was detected already 3 hours after 5-FU exposure, whereas substantial increase in global TS levels was detected only after 24 hours.	2'-deoxyuridylic acid	198-224	APC down-regulated 1	Homo sapiens	104-107
23056627-7	2012	Our data also suggest that the inhibition of the catalytic activity of hTS and the up-regulation of the hTS protein level are not causally linked, as the inactivated ternary complex, formed by hTS, deoxyuridine monophosphate and methylenetetrahydrofolate, was detected already 3 hours after 5-FU exposure, whereas substantial increase in global TS levels was detected only after 24 hours.	2'-deoxyuridylic acid	198-224	APC down-regulated 1	Homo sapiens	104-107
23056627-7	2012	Our data also suggest that the inhibition of the catalytic activity of hTS and the up-regulation of the hTS protein level are not causally linked, as the inactivated ternary complex, formed by hTS, deoxyuridine monophosphate and methylenetetrahydrofolate, was detected already 3 hours after 5-FU exposure, whereas substantial increase in global TS levels was detected only after 24 hours.	2'-deoxyuridylic acid	198-224	APC down-regulated 1	Homo sapiens	72-74
21647531-10	2011	For dUMP methylation, the highest level was observed with 25%, suggesting a low rate of dUMP methylation into dTMP with 25% of MTHFR activity.	2'-deoxyuridylic acid	4-8	methylenetetrahydrofolate reductase	Homo sapiens	127-132
22655049-3	2012	Due to its pivotal role in mycobacterial thymidylate synthesis dUTPase, which hydrolyzes dUTP into the dTTP precursor dUMP, has been suggested as a target for new antitubercular agents.	2'-deoxyuridylic acid	118-122	Deoxyuridine triphosphatase	Drosophila melanogaster	63-70
21876188-4	2011	Mitochondria purified from wild-type Chinese hamster ovary (CHO) cells and HepG2 cells converted dUMP to dTMP in the presence of NADPH and serine, through the activities of mitochondrial serine hydroxymethyltransferase (SHMT2), thymidylate synthase (TYMS), and a novel human mitochondrial dihydrofolate reductase (DHFR) previously thought to be a pseudogene known as dihydrofolate reductase-like protein 1 (DHFRL1).	2'-deoxyuridylic acid	97-101	serine hydroxymethyltransferase 2	Homo sapiens	173-218
21876188-4	2011	Mitochondria purified from wild-type Chinese hamster ovary (CHO) cells and HepG2 cells converted dUMP to dTMP in the presence of NADPH and serine, through the activities of mitochondrial serine hydroxymethyltransferase (SHMT2), thymidylate synthase (TYMS), and a novel human mitochondrial dihydrofolate reductase (DHFR) previously thought to be a pseudogene known as dihydrofolate reductase-like protein 1 (DHFRL1).	2'-deoxyuridylic acid	97-101	serine hydroxymethyltransferase 2	Homo sapiens	220-225
21876188-4	2011	Mitochondria purified from wild-type Chinese hamster ovary (CHO) cells and HepG2 cells converted dUMP to dTMP in the presence of NADPH and serine, through the activities of mitochondrial serine hydroxymethyltransferase (SHMT2), thymidylate synthase (TYMS), and a novel human mitochondrial dihydrofolate reductase (DHFR) previously thought to be a pseudogene known as dihydrofolate reductase-like protein 1 (DHFRL1).	2'-deoxyuridylic acid	97-101	thymidylate synthetase	Homo sapiens	228-248
21876188-4	2011	Mitochondria purified from wild-type Chinese hamster ovary (CHO) cells and HepG2 cells converted dUMP to dTMP in the presence of NADPH and serine, through the activities of mitochondrial serine hydroxymethyltransferase (SHMT2), thymidylate synthase (TYMS), and a novel human mitochondrial dihydrofolate reductase (DHFR) previously thought to be a pseudogene known as dihydrofolate reductase-like protein 1 (DHFRL1).	2'-deoxyuridylic acid	97-101	thymidylate synthetase	Homo sapiens	250-254
21876188-4	2011	Mitochondria purified from wild-type Chinese hamster ovary (CHO) cells and HepG2 cells converted dUMP to dTMP in the presence of NADPH and serine, through the activities of mitochondrial serine hydroxymethyltransferase (SHMT2), thymidylate synthase (TYMS), and a novel human mitochondrial dihydrofolate reductase (DHFR) previously thought to be a pseudogene known as dihydrofolate reductase-like protein 1 (DHFRL1).	2'-deoxyuridylic acid	97-101	dihydrofolate reductase	Homo sapiens	289-312
21876188-4	2011	Mitochondria purified from wild-type Chinese hamster ovary (CHO) cells and HepG2 cells converted dUMP to dTMP in the presence of NADPH and serine, through the activities of mitochondrial serine hydroxymethyltransferase (SHMT2), thymidylate synthase (TYMS), and a novel human mitochondrial dihydrofolate reductase (DHFR) previously thought to be a pseudogene known as dihydrofolate reductase-like protein 1 (DHFRL1).	2'-deoxyuridylic acid	97-101	dihydrofolate reductase	Homo sapiens	314-318
21876188-4	2011	Mitochondria purified from wild-type Chinese hamster ovary (CHO) cells and HepG2 cells converted dUMP to dTMP in the presence of NADPH and serine, through the activities of mitochondrial serine hydroxymethyltransferase (SHMT2), thymidylate synthase (TYMS), and a novel human mitochondrial dihydrofolate reductase (DHFR) previously thought to be a pseudogene known as dihydrofolate reductase-like protein 1 (DHFRL1).	2'-deoxyuridylic acid	97-101	dihydrofolate reductase 2	Homo sapiens	367-405
21876188-4	2011	Mitochondria purified from wild-type Chinese hamster ovary (CHO) cells and HepG2 cells converted dUMP to dTMP in the presence of NADPH and serine, through the activities of mitochondrial serine hydroxymethyltransferase (SHMT2), thymidylate synthase (TYMS), and a novel human mitochondrial dihydrofolate reductase (DHFR) previously thought to be a pseudogene known as dihydrofolate reductase-like protein 1 (DHFRL1).	2'-deoxyuridylic acid	97-101	dihydrofolate reductase 2	Homo sapiens	407-413
21832075-3	2011	Increased DNA replication in proliferating cancerous cells requires TSase activity, which catalyzes the reductive methylation of dUMP to dTMP using (R)-N(5),N(10)-methylene-5,6,7,8-tetrahydrofolate (MTHF) as a cofactor.	2'-deoxyuridylic acid	129-133	thymidylate synthetase	Homo sapiens	68-73
21647531-10	2011	For dUMP methylation, the highest level was observed with 25%, suggesting a low rate of dUMP methylation into dTMP with 25% of MTHFR activity.	2'-deoxyuridylic acid	88-92	methylenetetrahydrofolate reductase	Homo sapiens	127-132
21064161-4	2011	Inclusion of the substrate dUMP was without effect on M190K but induced structural changes in A191K that are unique, relative to hTS.	2'-deoxyuridylic acid	27-31	APC down-regulated 1	Homo sapiens	129-132
21548881-6	2011	The crystal structure of DUT1 was solved at 2 A resolution (1 A=0.1 nm) in an apo state and in complex with the non-hydrolysable substrate alpha,beta-imido dUTP or dUMP product.	2'-deoxyuridylic acid	164-168	bifunctional dITP/dUTP diphosphatase	Saccharomyces cerevisiae S288C	25-29
21188629-1	2011	Thymidylate synthase (TYMS), which catalyzes the conversion of deoxyuridine monophosphate to deoxythymidine monophosphate, is a central enzyme in the folate metabolic pathway.	2'-deoxyuridylic acid	63-89	thymidylate synthetase	Homo sapiens	0-20
21188629-1	2011	Thymidylate synthase (TYMS), which catalyzes the conversion of deoxyuridine monophosphate to deoxythymidine monophosphate, is a central enzyme in the folate metabolic pathway.	2'-deoxyuridylic acid	63-89	thymidylate synthetase	Homo sapiens	22-26
21567966-7	2011	Among the series of pyrimidine analogues, one derivative was shown to be phosphorylated by human UMP-CMP kinase, with rates similar to those of dUMP and even better than dCMP.	2'-deoxyuridylic acid	144-148	cytidine/uridine monophosphate kinase 1	Homo sapiens	97-111
21742238-1	2011	Thymidylate synthase (TS) is an enzyme, which catalyzes the methylation of deoxyuridylate to deoxythymidylate using 5.10-methylenetetrahydrofolate as a cofactor.	2'-deoxyuridylic acid	75-89	thymidylate synthetase	Homo sapiens	0-20
21742238-1	2011	Thymidylate synthase (TS) is an enzyme, which catalyzes the methylation of deoxyuridylate to deoxythymidylate using 5.10-methylenetetrahydrofolate as a cofactor.	2'-deoxyuridylic acid	75-89	thymidylate synthetase	Homo sapiens	22-24
21454646-4	2011	Here, we present crystal structures of the Leishmania major dUTPase in complex with substrate analogues, the product dUMP and a substrate fragment, and of the homologous Campylobacter jejuni dUTPase in complex with a triphosphate substrate analogue.	2'-deoxyuridylic acid	117-121	Deoxyuridine triphosphatase	Drosophila melanogaster	60-67
21222484-1	2011	5-Fluorouracil (5-FU), 5-fluorodeoxyuridine (5-dUrd), and raltitrixed (RTX) are anticancer agents that target thymidylate synthase (TS), thereby blocking the conversion of dUMP into dTMP.	2'-deoxyuridylic acid	172-176	thymidylate synthetase	Homo sapiens	110-130
21222484-2	2011	In budding yeast, 5-FU promotes a large increase in the dUMP/dTMP ratio leading to massive polymerase-catalyzed incorporation of uracil (U) into genomic DNA, and to a lesser extent 5-FU, which are both excised by yeast uracil DNA glycosylase (UNG), leading to DNA fragmentation and cell death.	2'-deoxyuridylic acid	56-60	uracil-DNA glycosylase	Saccharomyces cerevisiae S288C	219-241
21222484-2	2011	In budding yeast, 5-FU promotes a large increase in the dUMP/dTMP ratio leading to massive polymerase-catalyzed incorporation of uracil (U) into genomic DNA, and to a lesser extent 5-FU, which are both excised by yeast uracil DNA glycosylase (UNG), leading to DNA fragmentation and cell death.	2'-deoxyuridylic acid	56-60	uracil DNA glycosylase	Gallus gallus	243-246
21206062-0	2011	Structures of human thymidylate synthase R163K with dUMP, FdUMP and glutathione show asymmetric ligand binding.	2'-deoxyuridylic acid	52-56	thymidylate synthetase	Homo sapiens	20-40
21206062-4	2011	Using this approach, crystal structures of hTS complexes with FdUMP and dUMP were obtained, indicating that this form should facilitate high-throughput analysis of hTS complexes with drug candidates.	2'-deoxyuridylic acid	63-67	APC down-regulated 1	Homo sapiens	43-46
21206062-4	2011	Using this approach, crystal structures of hTS complexes with FdUMP and dUMP were obtained, indicating that this form should facilitate high-throughput analysis of hTS complexes with drug candidates.	2'-deoxyuridylic acid	63-67	APC down-regulated 1	Homo sapiens	164-167
21064161-7	2011	dUMP had no detectable effect on phosphorylation of M190K; however, dUMP inhibited phosphorylation of hTS and R163K.	2'-deoxyuridylic acid	68-72	APC down-regulated 1	Homo sapiens	102-105
20580582-1	2010	BACKGROUND: Thymidylate synthase (TS) is a key enzyme that regulates the production of nucleotide synthesis by catalyzing the conversion of deoxyuridylate to thymidylate.	2'-deoxyuridylic acid	140-154	thymidylate synthetase	Homo sapiens	12-32
22049707-0	2011	Research of waste dump water mutagenicity of bacterial detection system SOS chromotest.	2'-deoxyuridylic acid	18-22	xylosyltransferase 2	Homo sapiens	72-75
22049707-1	2011	The paper deals with a possible use of the bacterial detection system of SOS chromotest to test mutagenicity of waste dump water checking the mutagenicity degree on real samples from Praksice waste dump, which is a controlled waste dump with mixed industrial, municipal and inert wastes.	2'-deoxyuridylic acid	118-122	xylosyltransferase 2	Homo sapiens	73-76
22049707-1	2011	The paper deals with a possible use of the bacterial detection system of SOS chromotest to test mutagenicity of waste dump water checking the mutagenicity degree on real samples from Praksice waste dump, which is a controlled waste dump with mixed industrial, municipal and inert wastes.	2'-deoxyuridylic acid	198-202	xylosyltransferase 2	Homo sapiens	73-76
22049707-1	2011	The paper deals with a possible use of the bacterial detection system of SOS chromotest to test mutagenicity of waste dump water checking the mutagenicity degree on real samples from Praksice waste dump, which is a controlled waste dump with mixed industrial, municipal and inert wastes.	2'-deoxyuridylic acid	198-202	xylosyltransferase 2	Homo sapiens	73-76
21131780-2	2010	Inhibition of thymidylate synthetase (TS) leads to a decrease in cellular TTP levels, replication stress and increased genomic incorporation of uridine (dUMP).	2'-deoxyuridylic acid	153-157	thymidylate synthetase	Homo sapiens	14-36
21131780-11	2010	These data suggest Neil1 may be a critical mediator of BER of incorporated dUMP following TS pathway inhibition.	2'-deoxyuridylic acid	75-79	nei like DNA glycosylase 1	Homo sapiens	19-24
20580582-1	2010	BACKGROUND: Thymidylate synthase (TS) is a key enzyme that regulates the production of nucleotide synthesis by catalyzing the conversion of deoxyuridylate to thymidylate.	2'-deoxyuridylic acid	140-154	thymidylate synthetase	Homo sapiens	34-36
19879316-1	2010	Deoxyuridine 5"-triphosphate nucleotidohydrolase (dUTPase, EC 3.6.1.23) catalyzes the hydrolysis of dUTP to dUMP and pyrophosphate, and plays important roles in nucleotide metabolism and DNA replication.	2'-deoxyuridylic acid	108-112	Deoxyuridine triphosphatase	Drosophila melanogaster	50-57
20651387-1	2010	BACKGROUND: Thymidylate synthase (TS) plays an important role in the conversion of dUMP to dTMP.	2'-deoxyuridylic acid	83-87	thymidylate synthetase	Homo sapiens	12-32
20651387-1	2010	BACKGROUND: Thymidylate synthase (TS) plays an important role in the conversion of dUMP to dTMP.	2'-deoxyuridylic acid	83-87	thymidylate synthetase	Homo sapiens	34-36
20430630-6	2010	Computed free energies, in agreement with structural analysis, predict that the binding of dUMP and THF to hTS is favored in the native compared to phosphorylated state of the enzyme.	2'-deoxyuridylic acid	91-95	APC down-regulated 1	Homo sapiens	107-110
20485548-1	2010	Thymidylate synthase (TS), which catalyzes the de novo synthesis of dUMP, is an important target for cancer therapy.	2'-deoxyuridylic acid	68-72	thymidylate synthetase	Danio rerio	0-20
20485548-1	2010	Thymidylate synthase (TS), which catalyzes the de novo synthesis of dUMP, is an important target for cancer therapy.	2'-deoxyuridylic acid	68-72	thymidylate synthetase	Danio rerio	22-24
20056608-7	2010	AtUNG-deficient plants do not display any apparent phenotype, but show increased resistance to 5-fluorouracil (5-FU), a cytostatic drug that favors dUMP misincorporation into DNA.	2'-deoxyuridylic acid	148-152	uracil dna glycosylase	Arabidopsis thaliana	0-5
19370033-1	2009	Biosynthesis of the DNA base thymine depends on activity of the enzyme thymidylate synthase to catalyse the methylation of the uracil moiety of 2"-deoxyuridine-5"-monophosphate.	2'-deoxyuridylic acid	144-176	thymidylate synthetase	Homo sapiens	71-91
19797058-2	2009	One substrate of this pathway is the pyrimidine biosynthetic enzyme thymidylate synthase (TS; EC 2.1.1.45), which catalyzes the reductive methylation of dUMP to form dTMP and is essential for DNA replication during cell growth and proliferation.	2'-deoxyuridylic acid	153-157	thymidylate synthetase	Homo sapiens	68-88
19797058-2	2009	One substrate of this pathway is the pyrimidine biosynthetic enzyme thymidylate synthase (TS; EC 2.1.1.45), which catalyzes the reductive methylation of dUMP to form dTMP and is essential for DNA replication during cell growth and proliferation.	2'-deoxyuridylic acid	153-157	thymidylate synthetase	Homo sapiens	90-92
20725619-1	2010	Thymidylate synthase (TS) catalyzes methylation of dUMP to dTMP and it is the target for the 5-Fluorouracil (5-FU) activity.	2'-deoxyuridylic acid	51-55	thymidylate synthetase	Homo sapiens	0-20
19362086-4	2009	Here we used a yeast cdc21-1 mutant to demonstrate that the mutant cells accumulated dUMP in the mitochondrial genome.	2'-deoxyuridylic acid	85-89	thymidylate synthase	Saccharomyces cerevisiae S288C	21-26
19342774-1	2009	All organisms examined to date possess a dUTPase that performs the important function of efficiently hydrolyzing dUTP to dUMP in order to prevent the incorporation of dUTP into DNA.	2'-deoxyuridylic acid	121-125	Deoxyuridine triphosphatase	Drosophila melanogaster	41-48
19374805-1	2009	OBJECTIVE: Thymidylate synthase (TS) catalyses the conversion of deoxy-uridylate to deoxy-thymidylate and is a key enzyme for DNA synthesis.	2'-deoxyuridylic acid	65-80	thymidylate synthetase	Homo sapiens	11-31
19374805-1	2009	OBJECTIVE: Thymidylate synthase (TS) catalyses the conversion of deoxy-uridylate to deoxy-thymidylate and is a key enzyme for DNA synthesis.	2'-deoxyuridylic acid	65-80	thymidylate synthetase	Homo sapiens	33-35
18619713-1	2009	The ubiquitous enzyme dUTP nucleotidohydrolase (dUTPase) catalyses the hydrolysis of dUTP to dUMP and can be considered as the first line of defence against incorporation of uracil into DNA.	2'-deoxyuridylic acid	93-97	Deoxyuridine triphosphatase	Drosophila melanogaster	48-55
18646465-1	2008	Deoxyuridine triphosphatase (dUTPase) is a ubiquitous and important enzyme that hydrolyzes dUTP to dUMP.	2'-deoxyuridylic acid	99-103	Deoxyuridine triphosphatase	Drosophila melanogaster	29-36
18608754-1	2009	The enzyme deoxyuridine 5"-triphosphate nucleotidohydrolase (dUTPase) catalyses the hydrolysis of dUTP to dUMP and PPi thus controlling the incorporation of uracil into DNA genomes.	2'-deoxyuridylic acid	106-110	Deoxyuridine triphosphatase	Drosophila melanogaster	61-68
18586121-1	2008	Deoxyuridine 5"-triphosphate nucleotidohydrolase (dUTPase) catalyzes the hydrolysis of dUTP to dUMP and pyrophosphate and plays an important role in nucleotide metabolism and DNA replication controlling relative cellular levels of dTTP/dUTP, both of which can be incorporated into DNA.	2'-deoxyuridylic acid	95-99	Deoxyuridine triphosphatase	Drosophila melanogaster	50-57
21479480-1	2008	Thymidylate synthase, as a rate-limiting step in DNA synthesis, catalyses the conversion of dUMP into dTMP using 5,10-methylenotetrahydrofolate as the methyl donor.	2'-deoxyuridylic acid	92-96	thymidylate synthetase	Homo sapiens	0-20
19015155-1	2009	Deoxyuridine triphosphate nucleotidohydrolase (dUTPase) catalyzes the hydrolysis of dUTP to dUMP and PPi.	2'-deoxyuridylic acid	92-96	Deoxyuridine triphosphatase	Drosophila melanogaster	47-54
19055736-3	2008	Deoxyuridine triphosphatase (dUTPase) hydrolyzes dUTP, generating dUMP for biosynthesis of thymidine nucleotides while decreasing the availability of dUTP for misincorporation; uracil DNA glycosylase (UNG) cleaves uracil N-glycosylic bonds in DNA initiating base excision repair.	2'-deoxyuridylic acid	66-70	deoxyuridine triphosphatase	Homo sapiens	0-27
19055736-3	2008	Deoxyuridine triphosphatase (dUTPase) hydrolyzes dUTP, generating dUMP for biosynthesis of thymidine nucleotides while decreasing the availability of dUTP for misincorporation; uracil DNA glycosylase (UNG) cleaves uracil N-glycosylic bonds in DNA initiating base excision repair.	2'-deoxyuridylic acid	66-70	Deoxyuridine triphosphatase	Drosophila melanogaster	29-36
19055736-3	2008	Deoxyuridine triphosphatase (dUTPase) hydrolyzes dUTP, generating dUMP for biosynthesis of thymidine nucleotides while decreasing the availability of dUTP for misincorporation; uracil DNA glycosylase (UNG) cleaves uracil N-glycosylic bonds in DNA initiating base excision repair.	2'-deoxyuridylic acid	66-70	uracil DNA glycosylase	Homo sapiens	177-199
19055736-3	2008	Deoxyuridine triphosphatase (dUTPase) hydrolyzes dUTP, generating dUMP for biosynthesis of thymidine nucleotides while decreasing the availability of dUTP for misincorporation; uracil DNA glycosylase (UNG) cleaves uracil N-glycosylic bonds in DNA initiating base excision repair.	2'-deoxyuridylic acid	66-70	uracil DNA glycosylase	Homo sapiens	201-204
18790783-3	2008	dUTP nucleotidohydrolase (dUTPase) catalyzes the hydrolysis of dUTP to dUMP and PPi, providing substrate for thymidylate synthase (TS) and DNA synthesis and repair.	2'-deoxyuridylic acid	71-75	Deoxyuridine triphosphatase	Drosophila melanogaster	26-33
18790783-3	2008	dUTP nucleotidohydrolase (dUTPase) catalyzes the hydrolysis of dUTP to dUMP and PPi, providing substrate for thymidylate synthase (TS) and DNA synthesis and repair.	2'-deoxyuridylic acid	71-75	thymidylate synthetase	Homo sapiens	109-129
18804702-3	2008	Methylenetetrahydrofolate reductase (MTHFR) is an important folate metabolizing enzyme that catalyzes the irreversible conversion of 5,10-methylenetretrahydrofolate, which is the methyl donor for the conversion of dUMP to dTMP, into 5-methyltetrahydrofolate, which is the methyl donor for remethylation of homocysteine to methionine.	2'-deoxyuridylic acid	214-218	methylenetetrahydrofolate reductase	Homo sapiens	0-35
18706203-8	2008	The dump reflux and delayed clearance were more significant in patients in the HH2 group than those in the HH1 group (P < 0.05).	2'-deoxyuridylic acid	4-8	fibroblast growth factor receptor 1	Homo sapiens	79-82
18362071-0	2008	A molecular modeling study of the interaction of 2"-fluoro-substituted analogues of dUMP/FdUMP with thymidylate synthase.	2'-deoxyuridylic acid	84-88	thymidylate synthetase	Homo sapiens	100-120
18362071-1	2008	Molecular dynamics simulations and free energy calculations are presented, exploring previously described experimentally studied interactions of a series of 2"-fluoro-substituted dUMP/FdUMP analogues with thymidylate synthase (TS).	2'-deoxyuridylic acid	179-183	thymidylate synthetase	Homo sapiens	205-225
18321387-1	2008	BACKGROUND: The vaccinia virus (VV) F2L gene encodes a functional deoxyuridine triphosphatase (dUTPase) that catalyzes the conversion of dUTP to dUMP and is thought to minimize the incorporation of deoxyuridine residues into the viral genome.	2'-deoxyuridylic acid	145-149	dUTPase	Vaccinia virus	36-39
18321387-1	2008	BACKGROUND: The vaccinia virus (VV) F2L gene encodes a functional deoxyuridine triphosphatase (dUTPase) that catalyzes the conversion of dUTP to dUMP and is thought to minimize the incorporation of deoxyuridine residues into the viral genome.	2'-deoxyuridylic acid	145-149	deoxyuridine triphosphatase	Homo sapiens	66-93
18321387-1	2008	BACKGROUND: The vaccinia virus (VV) F2L gene encodes a functional deoxyuridine triphosphatase (dUTPase) that catalyzes the conversion of dUTP to dUMP and is thought to minimize the incorporation of deoxyuridine residues into the viral genome.	2'-deoxyuridylic acid	145-149	Deoxyuridine triphosphatase	Drosophila melanogaster	95-102
18321387-10	2008	The absence of dUTPase should reduce cellular dUMP pools and may result in a reduced conversion to dTMP by thymidylate synthetase or an increased reliance on the salvage of thymidine by the viral thymidine kinase.	2'-deoxyuridylic acid	46-50	Deoxyuridine triphosphatase	Drosophila melanogaster	15-22
17999954-6	2008	The enzyme was able to phosphorylate dUMP, dCMP, CMP, and UMP with ATP as phosphate donor, but the kinetic properties were different compared with the cytosolic UMP-CMPK.	2'-deoxyuridylic acid	37-41	cytidine/uridine monophosphate kinase 2	Homo sapiens	161-169
18589584-1	2008	Thymidylate synthase (TYMS) converts dUMP to dTMP, the rate-limiting nucleotide in DNA synthesis.	2'-deoxyuridylic acid	37-41	thymidylate synthetase	Homo sapiens	0-20
18589584-1	2008	Thymidylate synthase (TYMS) converts dUMP to dTMP, the rate-limiting nucleotide in DNA synthesis.	2'-deoxyuridylic acid	37-41	thymidylate synthetase	Homo sapiens	22-26
18804702-3	2008	Methylenetetrahydrofolate reductase (MTHFR) is an important folate metabolizing enzyme that catalyzes the irreversible conversion of 5,10-methylenetretrahydrofolate, which is the methyl donor for the conversion of dUMP to dTMP, into 5-methyltetrahydrofolate, which is the methyl donor for remethylation of homocysteine to methionine.	2'-deoxyuridylic acid	214-218	methylenetetrahydrofolate reductase	Homo sapiens	37-42
17985935-3	2007	To understand the relatively narrow substrate specificity of these two enzymes and their ability to use nucleotide analogues as substrates, we determined the crystal structures of human cdN in complex with deoxyuridine, murine cdN in complex with dUMP and dGMP, and human mdN in complex with the nucleotide analogues AZTMP and BVdUMP.	2'-deoxyuridylic acid	247-251	5', 3'-nucleotidase, cytosolic	Homo sapiens	227-230
17459559-0	2007	Effect of an Asp80Ala substitution on the binding of dUTP and dUMP to Trypanosoma cruzi dUTPase.	2'-deoxyuridylic acid	62-66	Deoxyuridine triphosphatase	Drosophila melanogaster	88-95
17692822-0	2007	Interactions of 2"-fluoro-substituted dUMP analogues with thymidylate synthase.	2'-deoxyuridylic acid	38-42	thymidylate synthetase	Homo sapiens	58-78
17692822-1	2007	A series of 2"-fluoro-substituted dUMP/FdUMP analogues were synthesized, their interaction with human recombinant thymidylate synthase investigated, and structural (1)H and (19)F NMR study of the corresponding nucleosides performed.	2'-deoxyuridylic acid	34-38	thymidylate synthetase	Homo sapiens	114-134
17870091-1	2007	Uracil-DNA glycosylase (UDG) removes uracil generated by the deamination of cytosine or misincorporation of deoxyuridine monophosphate.	2'-deoxyuridylic acid	108-134	uracil-DNA glycosylase	Thermus thermophilus HB8	0-22
17870091-1	2007	Uracil-DNA glycosylase (UDG) removes uracil generated by the deamination of cytosine or misincorporation of deoxyuridine monophosphate.	2'-deoxyuridylic acid	108-134	uracil-DNA glycosylase	Thermus thermophilus HB8	24-27
17459559-2	2007	The thermodynamics of binding for both dUTP and dUMP (deoxyuridine 5"-monophosphate) to the D80A mutant form of Trypanosoma cruzi dUTPase have been investigated by fluorescence spectroscopy and high-sensitivity isothermal titration calorimetry.	2'-deoxyuridylic acid	48-52	Deoxyuridine triphosphatase	Drosophila melanogaster	130-137
17459559-2	2007	The thermodynamics of binding for both dUTP and dUMP (deoxyuridine 5"-monophosphate) to the D80A mutant form of Trypanosoma cruzi dUTPase have been investigated by fluorescence spectroscopy and high-sensitivity isothermal titration calorimetry.	2'-deoxyuridylic acid	54-83	Deoxyuridine triphosphatase	Drosophila melanogaster	130-137
17452782-1	2007	Deoxyuridine triphosphate nucleotidohydrolase (dUTPase) catalyzes the hydrolysis of dUTP to dUMP and pyrophosphate in the presence of Mg(2+) ions.	2'-deoxyuridylic acid	92-96	Deoxyuridine triphosphatase	Drosophila melanogaster	47-54
17544982-2	2007	The interaction of Plasmodium falciparum dUTPase (PfdUTPase) with deoxyuridine derivatives (dU, dUMP, dUDP and dUpNHpp) has been studied thermodynamically by both isothermal titration and differential scanning calorimetry.	2'-deoxyuridylic acid	96-100	Deoxyuridine triphosphatase	Drosophila melanogaster	41-48
17452782-4	2007	The crystal structure of vaccinia virus dUTPase has been solved and the active site has been mapped by crystallographic analysis of the apo enzyme and of complexes with the substrate-analog dUMPNPP, with the product dUMP and with dUDP, which acts as an inhibitor.	2'-deoxyuridylic acid	190-194	Deoxyuridine triphosphatase	Drosophila melanogaster	40-47
16723031-3	2006	Thymidylate synthase (TYMS) is a key enzyme that participates in folate metabolism and catalyzes the conversion of dUMP to dTMP in the process of DNA synthesis.	2'-deoxyuridylic acid	115-119	thymidylate synthetase	Homo sapiens	0-20
17626051-8	2007	The stereopreference was conserved with the 2"-azido derivatives of dUMP and dUMP while, unexpectedly, the 2"-azido-D-dCMP was a 4-fold better substrate for UMP-CMP kinase than was CMP.	2'-deoxyuridylic acid	68-72	cytidine/uridine monophosphate kinase 2	Homo sapiens	157-171
17626051-8	2007	The stereopreference was conserved with the 2"-azido derivatives of dUMP and dUMP while, unexpectedly, the 2"-azido-D-dCMP was a 4-fold better substrate for UMP-CMP kinase than was CMP.	2'-deoxyuridylic acid	77-81	cytidine/uridine monophosphate kinase 2	Homo sapiens	157-171
17275316-0	2007	The effect of 5-substitution in the pyrimidine ring of dUMP on the interaction with thymidylate synthase: molecular modeling and QSAR.	2'-deoxyuridylic acid	55-59	thymidylate synthetase	Homo sapiens	84-104
17380903-6	2007	The apyrimidinic sites were formed when DNA fragment containing dTMP and dUMP residues in various ratios was treated with uracil-DNA-glycosylase (UDG).	2'-deoxyuridylic acid	73-77	uracil DNA glycosylase	Homo sapiens	122-144
17380903-6	2007	The apyrimidinic sites were formed when DNA fragment containing dTMP and dUMP residues in various ratios was treated with uracil-DNA-glycosylase (UDG).	2'-deoxyuridylic acid	73-77	uracil DNA glycosylase	Homo sapiens	146-149
17004711-1	2006	Thymidylate synthase (TS, ThyA) catalyzes the reductive methylation of 2"-deoxyuridine 5"-monophosphate to 2"-deoxythymidine 5"-monophosphate, an essential precursor for DNA synthesis.	2'-deoxyuridylic acid	71-103	thymidylate synthetase	Homo sapiens	0-20
17004711-1	2006	Thymidylate synthase (TS, ThyA) catalyzes the reductive methylation of 2"-deoxyuridine 5"-monophosphate to 2"-deoxythymidine 5"-monophosphate, an essential precursor for DNA synthesis.	2'-deoxyuridylic acid	71-103	APC down-regulated 1	Homo sapiens	22-24
16723031-3	2006	Thymidylate synthase (TYMS) is a key enzyme that participates in folate metabolism and catalyzes the conversion of dUMP to dTMP in the process of DNA synthesis.	2'-deoxyuridylic acid	115-119	thymidylate synthetase	Homo sapiens	22-26
16617146-7	2006	These data strongly suggest that the phenotypes of the dut1-1 mutant result from the incorporation of dUMPs into DNA subsequently converted into AP sites.	2'-deoxyuridylic acid	102-107	bifunctional dITP/dUTP diphosphatase	Saccharomyces cerevisiae S288C	55-59
16685161-1	2006	UNLABELLED: During DNA synthesis in tumors, fluoropyrimidine anticancer agents target thymidylate synthase (TS) that catalyze the synthesis of dTMP from dUMP and are metabolized by dihydropyrimidine dehydrogenase (DPD).	2'-deoxyuridylic acid	153-157	thymidylate synthetase	Homo sapiens	86-106
16685161-1	2006	UNLABELLED: During DNA synthesis in tumors, fluoropyrimidine anticancer agents target thymidylate synthase (TS) that catalyze the synthesis of dTMP from dUMP and are metabolized by dihydropyrimidine dehydrogenase (DPD).	2'-deoxyuridylic acid	153-157	dihydropyrimidine dehydrogenase	Homo sapiens	181-212
16685161-1	2006	UNLABELLED: During DNA synthesis in tumors, fluoropyrimidine anticancer agents target thymidylate synthase (TS) that catalyze the synthesis of dTMP from dUMP and are metabolized by dihydropyrimidine dehydrogenase (DPD).	2'-deoxyuridylic acid	153-157	dihydropyrimidine dehydrogenase	Homo sapiens	214-217
16489621-1	2006	BACKGROUND: Thymidylate synthase (TS) catalyzes the methylation of deoxyuridine monophosphate (dUMP) to deoxythymidine monophosphate (dTMP) and is a key enzyme for DNA synthesis.	2'-deoxyuridylic acid	67-93	thymidylate synthetase	Homo sapiens	12-32
16489621-1	2006	BACKGROUND: Thymidylate synthase (TS) catalyzes the methylation of deoxyuridine monophosphate (dUMP) to deoxythymidine monophosphate (dTMP) and is a key enzyme for DNA synthesis.	2'-deoxyuridylic acid	67-93	thymidylate synthetase	Homo sapiens	34-36
16489621-1	2006	BACKGROUND: Thymidylate synthase (TS) catalyzes the methylation of deoxyuridine monophosphate (dUMP) to deoxythymidine monophosphate (dTMP) and is a key enzyme for DNA synthesis.	2'-deoxyuridylic acid	95-99	thymidylate synthetase	Homo sapiens	12-32
16489621-1	2006	BACKGROUND: Thymidylate synthase (TS) catalyzes the methylation of deoxyuridine monophosphate (dUMP) to deoxythymidine monophosphate (dTMP) and is a key enzyme for DNA synthesis.	2'-deoxyuridylic acid	95-99	thymidylate synthetase	Homo sapiens	34-36
16259621-1	2006	Thymidylate synthase (TS) catalyses the reductive methylation of dUMP to form dTMP, a reaction that is essential for maintenance of nucleotide pools during cell growth.	2'-deoxyuridylic acid	65-69	thymidylate synthetase	Homo sapiens	0-20
16259621-1	2006	Thymidylate synthase (TS) catalyses the reductive methylation of dUMP to form dTMP, a reaction that is essential for maintenance of nucleotide pools during cell growth.	2'-deoxyuridylic acid	65-69	thymidylate synthetase	Homo sapiens	22-24
16154087-5	2005	Here, we describe the crystal structures of EBV dUTPase in complex with the product dUMP and a substrate analog alpha,beta-imino-dUTP.	2'-deoxyuridylic acid	84-88	Deoxyuridine triphosphatase	Drosophila melanogaster	48-55
16615178-14	2006	DNA increased virus antigen-induced immune cell secretion of IFN-gamma only, whereas dUMP significantly increased secretion of IL-10 only.	2'-deoxyuridylic acid	85-89	interleukin 10	Homo sapiens	127-132
16157237-14	2005	DNA increased virus antigen-induced immune cell secretion of IFN-gamma only, whereas deoxyuridine monophosphate significantly increased secretion of interleukin-10 only.	2'-deoxyuridylic acid	85-111	interleukin 10	Homo sapiens	149-163
16428394-4	2006	The B. hermsii thyX gene complemented the thyA mutation in E. coli, and purified B. hermsii ThyX protein catalyzed the conversion of dTMP from dUMP.	2'-deoxyuridylic acid	143-147	thyX	Borrelia hermsii	15-19
16428394-4	2006	The B. hermsii thyX gene complemented the thyA mutation in E. coli, and purified B. hermsii ThyX protein catalyzed the conversion of dTMP from dUMP.	2'-deoxyuridylic acid	143-147	thyX	Borrelia hermsii	92-96
16505899-1	2006	Thymidylate synthase purified from 5-fluoro-dUrd-resistant mouse leukemia L1210 cells (TSr) was less sensitive to slow-binding inhibition by 5-fluoro-dUMP than the enzyme from the parental cells (TSp), both enzyme forms differing also in sensitivity to several other dump analogues, apparent molecular weights of monomer and dimer, and temperature dependence of the catalyzed reaction.	2'-deoxyuridylic acid	267-271	thymidylate synthase	Mus musculus	0-20
15598787-1	2004	Thymidylate synthase (TS), a key one-carbon metabolizing gene, encodes an enzyme that converts dUMP to dTMP, the rate-limiting nucleotide in DNA synthesis.	2'-deoxyuridylic acid	95-99	thymidylate synthetase	Homo sapiens	0-20
15897250-6	2005	Studies with inside-out membrane vesicles prepared from transfected cells showed that MRP5 mediates ATP-dependent transport of 5 micromol/L [(3)H]5-FdUMP, [(3)H]5-FUMP, [(3)H]dUMP, and not [(3)H]5-FUdR, or [(3)H]5-FU.	2'-deoxyuridylic acid	149-153	ATP binding cassette subfamily C member 5	Homo sapiens	86-90
15670155-4	2005	The three-dimensional structures of the crystalline complexes of RNase A with dUMP, dU(F)MP and araUMP were determined at < 1.7 A resolution by X-ray diffraction analysis.	2'-deoxyuridylic acid	78-82	ribonuclease A family member 1, pancreatic	Homo sapiens	65-72
16381716-0	2005	Beam dumps design and local radiation protection at TERA synchrotron.	2'-deoxyuridylic acid	5-10	SIN3-HDAC complex associated factor	Homo sapiens	52-56
15817609-1	2005	Thymidylate synthase (TS) catalyzes the 5,10-methylene-tetrahydrofolate-mediated conversion of deoxyuridine monophosphate to deoxythymydine monophosphate, a nucleotide required for DNA synthesis and repair.	2'-deoxyuridylic acid	95-121	thymidylate synthetase	Homo sapiens	0-20
15817609-1	2005	Thymidylate synthase (TS) catalyzes the 5,10-methylene-tetrahydrofolate-mediated conversion of deoxyuridine monophosphate to deoxythymydine monophosphate, a nucleotide required for DNA synthesis and repair.	2'-deoxyuridylic acid	95-121	thymidylate synthetase	Homo sapiens	22-24
15939294-1	2005	The cDNA encoding dUTPase, an enzyme catalysing the hydrolysis of dUTP to dUMP and pyrophosphate, from the integrated Bacillus subtilis temperate bacteriophage SPbeta has been cloned and over-expressed at high levels in Escherichia coli.	2'-deoxyuridylic acid	74-78	Deoxyuridine triphosphatase	Drosophila melanogaster	18-25
15550676-8	2005	The differential regulation of dCMPK versus CMPK activities by ATP or magnesium was also seen in other 2"-deoxypyrimidine analog monophosphates (deoxyuridine monophosphate, 5-fluorodeoxyuridine monophosphate, 1-beta-D-arabinofuranosylcytosine monophosphate, and gemcitabine monophosphate) versus their ribose-counterparts (UMP and 5-fluorouridine monophosphate), in a similar manner.	2'-deoxyuridylic acid	145-171	cytidine/uridine monophosphate kinase 1	Homo sapiens	32-36
15598787-1	2004	Thymidylate synthase (TS), a key one-carbon metabolizing gene, encodes an enzyme that converts dUMP to dTMP, the rate-limiting nucleotide in DNA synthesis.	2'-deoxyuridylic acid	95-99	thymidylate synthetase	Homo sapiens	22-24
14967037-1	2004	Thymidylate synthase (EC 2.1.1.45) (TS) catalyzes the conversion of dUMP to dTMP and is therefore indispensable for DNA replication in actively dividing cells.	2'-deoxyuridylic acid	68-72	thymidylate synthetase	Homo sapiens	0-20
15479784-1	2004	Nuclear uracil-DNA glycosylase UNG2 has an established role in repair of U/A pairs resulting from misincorporation of dUMP during replication.	2'-deoxyuridylic acid	118-122	uracil DNA glycosylase	Homo sapiens	31-35
15044615-3	2004	The human mitochondrial deoxyribonucleotidase (dNT-2) dephosphorylates thymidine and deoxyuridine monophosphates.	2'-deoxyuridylic acid	85-112	spatzle 5	Drosophila melanogaster	47-52
15450848-0	2004	Calorimetric determination of thermodynamic parameters of 2"-dUMP binding to Leishmania major dUTPase.	2'-deoxyuridylic acid	58-65	Deoxyuridine triphosphatase	Drosophila melanogaster	94-101
15450848-1	2004	We have investigated the binding of 2"-deoxyuridine 5"-monophosphate (2"-dUMP) to Leishmania major deoxyuridine 5"-triphosphate nucleotide hydrolase (dUTPase) by isothermal titration microcalorimetry under different experimental conditions.	2'-deoxyuridylic acid	36-68	Deoxyuridine triphosphatase	Drosophila melanogaster	150-157
15450848-1	2004	We have investigated the binding of 2"-deoxyuridine 5"-monophosphate (2"-dUMP) to Leishmania major deoxyuridine 5"-triphosphate nucleotide hydrolase (dUTPase) by isothermal titration microcalorimetry under different experimental conditions.	2'-deoxyuridylic acid	70-77	Deoxyuridine triphosphatase	Drosophila melanogaster	150-157
15450848-2	2004	Binding to dimeric L. major dUTPase is a non-cooperative process, with a stoichiometry of 1 molecule of 2"-dUMP per subunit.	2'-deoxyuridylic acid	104-111	Deoxyuridine triphosphatase	Drosophila melanogaster	28-35
15475457-8	2004	Thymidylate synthase activity was determined in vitro in tumors from untreated mice by [3H] release from [3H]dUMP.	2'-deoxyuridylic acid	109-113	thymidylate synthase	Mus musculus	0-20
14724274-8	2004	In fly, but not in bacterial dUTPase, binding of the product dUMP induces protection against proteolysis at the tryptic site reflecting formation of the catalytically competent closed conformer.	2'-deoxyuridylic acid	61-65	Deoxyuridine triphosphatase	Drosophila melanogaster	29-36
14578129-1	2003	Thymidylate synthase (TS) converts dUMP to dTMP, the rate-limiting nucleotide in DNA synthesis.	2'-deoxyuridylic acid	35-39	thymidylate synthetase	Homo sapiens	0-20
14578129-1	2003	Thymidylate synthase (TS) converts dUMP to dTMP, the rate-limiting nucleotide in DNA synthesis.	2'-deoxyuridylic acid	35-39	thymidylate synthetase	Homo sapiens	22-24
12948860-4	2003	5-Fluorouracil is known to inhibit thymidylate synthase (TS), a key enzyme that transfers a methyl group from 5,10-methylene-tetrahydrofolate to dUMP during nucleotide biosynthesis.	2'-deoxyuridylic acid	145-149	thymidylate synthetase	Homo sapiens	35-55
12948860-4	2003	5-Fluorouracil is known to inhibit thymidylate synthase (TS), a key enzyme that transfers a methyl group from 5,10-methylene-tetrahydrofolate to dUMP during nucleotide biosynthesis.	2'-deoxyuridylic acid	145-149	thymidylate synthetase	Homo sapiens	57-59
12756253-1	2003	The bifunctional dCTP deaminase-dUTPase (DCD-DUT) from Methanocaldococcus jannaschii catalyzes the deamination of the cytosine moiety in dCTP and the hydrolysis of the triphosphate moiety forming dUMP, thereby preventing uracil from being incorporated into DNA.	2'-deoxyuridylic acid	196-200	Deoxyuridine triphosphatase	Drosophila melanogaster	32-39
12934097-1	2003	Mice deficient in the Ung uracil-DNA glycosylase have an increased level of uracil in their genome, consistent with a major role of Ung counteracting U:A base pairs arising by misincorporation of dUMP during DNA replication.	2'-deoxyuridylic acid	196-200	uracil DNA glycosylase	Mus musculus	22-25
12934097-1	2003	Mice deficient in the Ung uracil-DNA glycosylase have an increased level of uracil in their genome, consistent with a major role of Ung counteracting U:A base pairs arising by misincorporation of dUMP during DNA replication.	2'-deoxyuridylic acid	196-200	uracil DNA glycosylase	Mus musculus	132-135
12791246-1	2003	The structure of thymidylate synthase complementing protein with substrates dUMP and FAD, presented in this issue of Structure, sheds light on a fascinating new catalytic mechanism, suggests a strategy for the design of new antimicrobial compounds, and highlights the promise of proteomics in medicine.	2'-deoxyuridylic acid	76-80	thymidylate synthetase	Homo sapiens	17-37
12819937-1	2003	Thymidylate synthase (TS) is a folate-dependent enzyme that catalyzes the reductive methylation of 2"-deoxyuridine-5"-monophosphate to 2"-deoxythymidine-5"-monophosphate.	2'-deoxyuridylic acid	99-131	thymidylate synthetase	Homo sapiens	0-20
12819937-1	2003	Thymidylate synthase (TS) is a folate-dependent enzyme that catalyzes the reductive methylation of 2"-deoxyuridine-5"-monophosphate to 2"-deoxythymidine-5"-monophosphate.	2'-deoxyuridylic acid	99-131	thymidylate synthetase	Homo sapiens	22-24
12859954-1	2003	We have determined the kinetic parameters of human recombinant thymidylate synthase (hrTS) with its natural substrate, dUMP, and E-5-(2-bromovinyl)-2(")-deoxyuridine monophosphate (BVdUMP), a nucleotide derivative believed to be the active species of the novel anticancer drug NB1011.	2'-deoxyuridylic acid	119-123	thymidylate synthetase	Homo sapiens	63-83
12799180-1	2003	dUTP nucleotidohydrolase (dUTPase) catalyzes the hydrolysis of dUTP to dUMP and pyrophosphate and is the central regulator of cellular dUTP pools.	2'-deoxyuridylic acid	71-75	Deoxyuridine triphosphatase	Drosophila melanogaster	26-33
12670946-1	2003	By the sequential action of dCTP deaminase and dUTPase, dCTP is converted to dUMP, the precursor of thymidine nucleotides.	2'-deoxyuridylic acid	77-81	Deoxyuridine triphosphatase	Drosophila melanogaster	28-54
12670946-1	2003	By the sequential action of dCTP deaminase and dUTPase, dCTP is converted to dUMP, the precursor of thymidine nucleotides.	2'-deoxyuridylic acid	77-81	cut up	Drosophila melanogaster	28-32
12670946-5	2003	When the reaction was followed by thin layer chromatography using [3H]dCTP as substrate, dUMP and not dUTP was identified as a reaction product.	2'-deoxyuridylic acid	89-93	cut up	Drosophila melanogaster	70-74
12771412-2	2003	Here, we have demonstrated that HCMV increases expression of the cellular deoxycytidylate deaminase (dCMP deaminase), which provides the substrate for TS by converting dCMP to dUMP.	2'-deoxyuridylic acid	176-180	dCMP deaminase	Homo sapiens	74-99
12666783-0	2003	Numerical and experimental studies of CCl4 destruction in a dump incinerator.	2'-deoxyuridylic acid	60-64	C-C motif chemokine ligand 4	Homo sapiens	38-42
12565992-2	2003	Inhibition of thymidylate synthase (TS), an important target for cancer chemotherapy, leads to deoxythymidine triphosphate (dTTP) pool depletion and elevation of deoxyuridine monophosphate (dUMP) pools which may also result in the accumulation of deoxyuridine triphosphate (dUTP).	2'-deoxyuridylic acid	162-188	thymidylate synthetase	Homo sapiens	14-34
12565992-2	2003	Inhibition of thymidylate synthase (TS), an important target for cancer chemotherapy, leads to deoxythymidine triphosphate (dTTP) pool depletion and elevation of deoxyuridine monophosphate (dUMP) pools which may also result in the accumulation of deoxyuridine triphosphate (dUTP).	2'-deoxyuridylic acid	190-194	thymidylate synthetase	Homo sapiens	14-34
12684419-3	2003	TS is the key enzyme in the catalysis of the methylation from dUMP to dTMP in the DNA synthetic process.	2'-deoxyuridylic acid	62-66	thymidylate synthetase	Homo sapiens	0-2
12536082-2	2003	A critical step in the de novo pathway of DNA synthesis is the production of the pyrimidine nucleotide dTMP from dump and this reaction is catalyzed by thymidylate synthase (TS).	2'-deoxyuridylic acid	113-117	thymidylate synthetase	Homo sapiens	152-172
12536082-2	2003	A critical step in the de novo pathway of DNA synthesis is the production of the pyrimidine nucleotide dTMP from dump and this reaction is catalyzed by thymidylate synthase (TS).	2'-deoxyuridylic acid	113-117	thymidylate synthetase	Homo sapiens	174-176
12483510-5	2002	UNG2 is a major nuclear uracil-DNA glycosylase central in removal of misincorporated dUMP in replication foci, but recent evidence also indicates an important role in repair of U : G mispairs and possibly U in single-stranded DNA.	2'-deoxyuridylic acid	85-89	uracil DNA glycosylase	Homo sapiens	0-4
12488549-1	2003	Thymidylate synthase (TS), a key cancer chemotherapeutic target, catalyzes the conversion of deoxyuridylate to thymidylate.	2'-deoxyuridylic acid	93-107	thymidylate synthetase	Homo sapiens	0-20
12488549-1	2003	Thymidylate synthase (TS), a key cancer chemotherapeutic target, catalyzes the conversion of deoxyuridylate to thymidylate.	2'-deoxyuridylic acid	93-107	thymidylate synthetase	Homo sapiens	22-24
12616366-3	2003	METHODS: To predict tumor sensitivity to 5-fluorouracil (5-FU) in thymoma, we investigated the mRNA levels of thymidylate synthase (TS), the key enzyme that catalyzes the methylation of deoxyuridine monophosphate, and correlates with the resistance of 5-FU and dihydropyrimidine dehydrogenase (DPD), which degrades 5-FU in thymoma.	2'-deoxyuridylic acid	186-212	thymidylate synthetase	Homo sapiens	110-130
12616366-3	2003	METHODS: To predict tumor sensitivity to 5-fluorouracil (5-FU) in thymoma, we investigated the mRNA levels of thymidylate synthase (TS), the key enzyme that catalyzes the methylation of deoxyuridine monophosphate, and correlates with the resistance of 5-FU and dihydropyrimidine dehydrogenase (DPD), which degrades 5-FU in thymoma.	2'-deoxyuridylic acid	186-212	thymidylate synthetase	Homo sapiens	132-134
12488542-1	2003	Deoxycytidylate deaminase, catalyzing the conversion of dCMP to dUMP, is an important enzyme in the de novo synthesis of thymidine nucleotides.	2'-deoxyuridylic acid	64-68	dCMP deaminase	Homo sapiens	0-25
12147691-1	2002	Thymidylate synthase (TS) catalyzes methylation of dUMP to dTMP and is the target of cancer chemotherapeutic agents (e.g. 5-fluorouracil).	2'-deoxyuridylic acid	51-55	thymidylate synthetase	Homo sapiens	0-20
12376965-1	2002	Deoxyuridine triphosphatase (dUTPase) catalyses the hydrolysis of dUTP to dUMP and pyrophosphate thus preventing the incorporation of uracil into replicating DNA.	2'-deoxyuridylic acid	74-78	Deoxyuridine triphosphatase	Drosophila melanogaster	29-36
12147691-1	2002	Thymidylate synthase (TS) catalyzes methylation of dUMP to dTMP and is the target of cancer chemotherapeutic agents (e.g. 5-fluorouracil).	2'-deoxyuridylic acid	51-55	thymidylate synthetase	Homo sapiens	22-24
12084461-1	2002	Thymidylate synthase (TS) is a key enzyme in the de novo synthesis of 2"-deoxythymidine-5"-monophosphate (dTMP) from 2"-deoxyuridine-5"-monophosphate (dUMP), for which 5,10-methylene-tetrahydrofolate (CH(2)-THF) is the methyl donor.	2'-deoxyuridylic acid	117-149	thymidylate synthetase	Homo sapiens	0-20
12124385-3	2002	We earlier obtained evidence for a mitochondrial 5"-nucleotidase (dNT2) with a pronounced specificity for dUMP and dTMP and suggested that the enzyme protects mitochondrial DNA replication from excess dTTP.	2'-deoxyuridylic acid	106-110	5',3'-nucleotidase, mitochondrial	Homo sapiens	35-64
12124385-3	2002	We earlier obtained evidence for a mitochondrial 5"-nucleotidase (dNT2) with a pronounced specificity for dUMP and dTMP and suggested that the enzyme protects mitochondrial DNA replication from excess dTTP.	2'-deoxyuridylic acid	106-110	spatzle 5	Drosophila melanogaster	66-70
12215845-1	2002	The thymidylate synthase gene ( TYMS or TS) encodes a tightly regulated enzyme that catalyzes the conversion of deoxyuridylate to thymidylate, and contains a tandem repeat polymorphism that affects expression of the enzyme.	2'-deoxyuridylic acid	112-126	thymidylate synthetase	Homo sapiens	4-24
12215845-1	2002	The thymidylate synthase gene ( TYMS or TS) encodes a tightly regulated enzyme that catalyzes the conversion of deoxyuridylate to thymidylate, and contains a tandem repeat polymorphism that affects expression of the enzyme.	2'-deoxyuridylic acid	112-126	thymidylate synthetase	Homo sapiens	32-36
12084461-1	2002	Thymidylate synthase (TS) is a key enzyme in the de novo synthesis of 2"-deoxythymidine-5"-monophosphate (dTMP) from 2"-deoxyuridine-5"-monophosphate (dUMP), for which 5,10-methylene-tetrahydrofolate (CH(2)-THF) is the methyl donor.	2'-deoxyuridylic acid	117-149	thymidylate synthetase	Homo sapiens	22-24
12084461-1	2002	Thymidylate synthase (TS) is a key enzyme in the de novo synthesis of 2"-deoxythymidine-5"-monophosphate (dTMP) from 2"-deoxyuridine-5"-monophosphate (dUMP), for which 5,10-methylene-tetrahydrofolate (CH(2)-THF) is the methyl donor.	2'-deoxyuridylic acid	151-155	thymidylate synthetase	Homo sapiens	0-20
12084461-1	2002	Thymidylate synthase (TS) is a key enzyme in the de novo synthesis of 2"-deoxythymidine-5"-monophosphate (dTMP) from 2"-deoxyuridine-5"-monophosphate (dUMP), for which 5,10-methylene-tetrahydrofolate (CH(2)-THF) is the methyl donor.	2'-deoxyuridylic acid	151-155	thymidylate synthetase	Homo sapiens	22-24
11914638-2	2002	NB1011 is converted intracellularly to bromovinyldeoxyuridine monophosphate (BVdUMP) which competes with the natural substrate, deoxyuridine monophosphate, for binding to TS.	2'-deoxyuridylic acid	49-75	thymidylate synthetase	Homo sapiens	171-173
12124583-0	2002	Senate nod prompts fresh analysis of nuclear waste dump.	2'-deoxyuridylic acid	51-55	atrophin 1	Homo sapiens	7-10
12422235-3	2002	The reaction catalyzed by the R209K enzyme (studied in a crude extract), compared to that catalyzed by purified wild-type recombinant mouse thymidylate synthase, showed the K(m) value for dUMP 571-fold higher and V(max) value over 50-fold (assuming that the mutated enzyme constituted 20% of total crude extract protein) lower.	2'-deoxyuridylic acid	188-192	thymidylate synthase	Mus musculus	140-160
11605654-2	2001	Molecular design was performed on the human TS complex model built on the basis of the reported structure of TS-deoxyuridinemonophosphate (dUMP)-CB3717 ternary complex.	2'-deoxyuridylic acid	112-137	thymidylate synthetase	Homo sapiens	44-46
12369927-1	2001	Deoxyuridine pyrophosphatase (dUTPase) cleaves the alpha-beta phosphodiester bond of dUTP to form pyrophosphate and dUMP, preventing incorporation of uracil into DNA and providing the substrate for dTTP synthesis.	2'-deoxyuridylic acid	116-120	Deoxyuridine triphosphatase	Drosophila melanogaster	30-37
12374095-2	2001	Therapeutic strategies applied to this pathway target the thymidylate synthase (TS) reaction that catalyzes the reductive methylation of deoxyuridylate (dUMP) to form thymidylate (TMP).	2'-deoxyuridylic acid	137-151	thymidylate synthetase	Homo sapiens	58-78
12374095-2	2001	Therapeutic strategies applied to this pathway target the thymidylate synthase (TS) reaction that catalyzes the reductive methylation of deoxyuridylate (dUMP) to form thymidylate (TMP).	2'-deoxyuridylic acid	153-157	thymidylate synthetase	Homo sapiens	58-78
12374095-10	2001	dUTPase catalyzes the hydrolysis of dUTP to form dUMP and pyrophosphate thereby eliminating dUTP and preventing its utilization by DNA polymerases during replication and repair.	2'-deoxyuridylic acid	49-53	Deoxyuridine triphosphatase	Drosophila melanogaster	0-7
11605654-2	2001	Molecular design was performed on the human TS complex model built on the basis of the reported structure of TS-deoxyuridinemonophosphate (dUMP)-CB3717 ternary complex.	2'-deoxyuridylic acid	139-143	thymidylate synthetase	Homo sapiens	44-46
11487279-1	2001	Thymidylate synthase (TS) is an important enzyme catalysing the reductive methylation of dUMP to dTMP that is further metabolized to dTTP for DNA synthesis.	2'-deoxyuridylic acid	89-93	thymidylate synthetase	Homo sapiens	0-20
11605536-3	2001	A photoreactive dUMP derivative was added to the 3" end of a gap-flanking oligonucleotide with DNA polymerase beta, and an oligonucleotide containing a 5"-photoreactive group was chemically synthesized.	2'-deoxyuridylic acid	16-20	DNA polymerase beta	Homo sapiens	95-114
11487279-1	2001	Thymidylate synthase (TS) is an important enzyme catalysing the reductive methylation of dUMP to dTMP that is further metabolized to dTTP for DNA synthesis.	2'-deoxyuridylic acid	89-93	thymidylate synthetase	Homo sapiens	22-24
11483530-6	2001	We propose a model in which SMUG1 has evolved in higher eukaryotes as an anti-mutator distinct from the UNG enzyme, the latter being largely localized to replication foci in mammalian cells to counteract de novo dUMP incorporation into DNA.	2'-deoxyuridylic acid	212-216	single-strand-selective monofunctional uracil-DNA glycosylase 1	Homo sapiens	28-33
11505394-3	2001	TS is the key enzyme in the catalysis of the methylation from deoxyuridine monophosphate (dUMP) to deoxythymidine monophosphate.	2'-deoxyuridylic acid	62-88	thymidylate synthetase	Homo sapiens	0-2
11505394-3	2001	TS is the key enzyme in the catalysis of the methylation from deoxyuridine monophosphate (dUMP) to deoxythymidine monophosphate.	2'-deoxyuridylic acid	90-94	thymidylate synthetase	Homo sapiens	0-2
11483530-6	2001	We propose a model in which SMUG1 has evolved in higher eukaryotes as an anti-mutator distinct from the UNG enzyme, the latter being largely localized to replication foci in mammalian cells to counteract de novo dUMP incorporation into DNA.	2'-deoxyuridylic acid	212-216	uracil DNA glycosylase	Homo sapiens	104-107
11316879-0	2001	Crystal structure of a deletion mutant of human thymidylate synthase Delta (7-29) and its ternary complex with Tomudex and dUMP.	2'-deoxyuridylic acid	123-127	thymidylate synthetase	Homo sapiens	48-68
11316879-1	2001	The crystal structures of a deletion mutant of human thymidylate synthase (TS) and its ternary complex with dUMP and Tomudex have been determined at 2.0 A and 2.5 A resolution, respectively.	2'-deoxyuridylic acid	108-112	thymidylate synthetase	Homo sapiens	53-73
11316879-1	2001	The crystal structures of a deletion mutant of human thymidylate synthase (TS) and its ternary complex with dUMP and Tomudex have been determined at 2.0 A and 2.5 A resolution, respectively.	2'-deoxyuridylic acid	108-112	thymidylate synthetase	Homo sapiens	75-77
11329255-0	2001	Human thymidylate synthase is in the closed conformation when complexed with dUMP and raltitrexed, an antifolate drug.	2'-deoxyuridylic acid	77-81	thymidylate synthetase	Homo sapiens	6-26
11295154-2	2001	This activity is compromised when Vitamin B12 (B12) concentration is low because methionine synthase activity is reduced, lowering the concentration of S-adenosyl methionine (SAM) which in turn may diminish DNA methylation and cause folate to become unavailable for the conversion of dUMP to dTMP.	2'-deoxyuridylic acid	284-288	5-methyltetrahydrofolate-homocysteine methyltransferase	Homo sapiens	81-100
11278511-8	2001	Thus, TS inhibition via stabilization of the inactive conformation should lead to less resistance than is observed with presently used drugs, which are analogs of its substrates, dUMP and CH(2)H(4)folate, and bind in the active site, promoting the active conformation.	2'-deoxyuridylic acid	179-183	thymidylate synthetase	Homo sapiens	6-8
11554311-8	2001	However, one major role of UNG2 is to remove misincorporated dUMP residues.	2'-deoxyuridylic acid	61-65	uracil DNA glycosylase	Homo sapiens	27-31
11212266-1	2001	Thymidylate synthase catalyzes the reductive methylation of dUMP to dTMP and is essential for the synthesis of DNA.	2'-deoxyuridylic acid	60-64	thymidylate synthetase	Homo sapiens	0-20
11913730-1	2001	Thymidylate synthase (TS) catalyses the conversion of deoxy-uridylate to deoxy-thymidylate and is essential for DNA synthesis.	2'-deoxyuridylic acid	54-69	thymidylate synthetase	Homo sapiens	0-20
11913730-1	2001	Thymidylate synthase (TS) catalyses the conversion of deoxy-uridylate to deoxy-thymidylate and is essential for DNA synthesis.	2'-deoxyuridylic acid	54-69	thymidylate synthetase	Homo sapiens	22-24
10915553-1	2000	In order to explain different activities shown by 5-hydroxy-dUMP (substrate) and its close analogue 5-hydroxymethyl-dUMP (slow-binding inhibitor) in the reaction catalyzed by thymidylate synthase, studies have been undertaken involving (i) ab initio RHF simulations, (ii) comparative analysis of crystallographic structures available from CSD, and (iii) QSAR analysis of experimental results describing thymidylate synthase interaction with various 5-substituted dUMP analogues.	2'-deoxyuridylic acid	60-64	thymidylate synthetase	Homo sapiens	175-195
10957629-1	2000	dUTP pyrophosphatase (dUTPase) cleaves the alpha-beta phosphodiester of dUTP to form pyrophosphate and dUMP, preventing incorporation of uracil into DNA and providing the substrate for thymine synthesis.	2'-deoxyuridylic acid	103-107	Deoxyuridine triphosphatase	Drosophila melanogaster	22-29
10957629-2	2000	Seven crystal structures of feline immunodeficiency virus (FIV) dUTPase in three crystal forms have been determined, including complexes with substrate (dUTP), product (dUMP) or inhibitor (dUDP) bound.	2'-deoxyuridylic acid	169-173	Deoxyuridine triphosphatase	Drosophila melanogaster	64-71
10952785-2	2000	dUTPase catalyses the hydrolysis of dUTP to dUMP, thereby maintaining low intracellular dUTP.	2'-deoxyuridylic acid	44-48	Deoxyuridine triphosphatase	Drosophila melanogaster	0-7
10915553-1	2000	In order to explain different activities shown by 5-hydroxy-dUMP (substrate) and its close analogue 5-hydroxymethyl-dUMP (slow-binding inhibitor) in the reaction catalyzed by thymidylate synthase, studies have been undertaken involving (i) ab initio RHF simulations, (ii) comparative analysis of crystallographic structures available from CSD, and (iii) QSAR analysis of experimental results describing thymidylate synthase interaction with various 5-substituted dUMP analogues.	2'-deoxyuridylic acid	60-64	thymidylate synthetase	Homo sapiens	403-423
10915553-3	2000	The results indicate the 5-hydroxyl deprotonation to be easier and supported by resonance electronic effect, pointing to a probable mechanism of different activities of the two dUMP analogues in thymidylate synthase reaction.	2'-deoxyuridylic acid	177-181	thymidylate synthetase	Homo sapiens	195-215
10653645-1	2000	In thymidylate synthase, four conserved arginines provide two hydrogen bonds each to the oxygens of the phosphate group of the substrate, 2"-deoxyuridine-5"-monophosphate.	2'-deoxyuridylic acid	138-170	thymidylate synthetase	Homo sapiens	3-23
10536004-1	1999	Reduction of 5,10-methylenetetrahydrofolate (methyleneTHF), a donor for methylating dUMP to dTMP in DNA synthesis, to 5-methyltetrahydrofolate (methylTHF), the primary methyl donor for methionine synthesis, is catalyzed by 5,10-methylenetetrahydrofolate reductase (MTHFR).	2'-deoxyuridylic acid	84-88	methylenetetrahydrofolate reductase	Homo sapiens	223-263
10536004-1	1999	Reduction of 5,10-methylenetetrahydrofolate (methyleneTHF), a donor for methylating dUMP to dTMP in DNA synthesis, to 5-methyltetrahydrofolate (methylTHF), the primary methyl donor for methionine synthesis, is catalyzed by 5,10-methylenetetrahydrofolate reductase (MTHFR).	2'-deoxyuridylic acid	84-88	methylenetetrahydrofolate reductase	Homo sapiens	265-270
10509749-3	1999	Although the kcat/Km of the mutant protein for the substrate, dUMP, is 10(3) lower than that of wild-type TS, the mutant TS confers thymidine prototrophy on a TS-deficient bacterial strain when expressed at high levels.	2'-deoxyuridylic acid	62-66	thymidylate synthetase	Homo sapiens	106-108
10509749-3	1999	Although the kcat/Km of the mutant protein for the substrate, dUMP, is 10(3) lower than that of wild-type TS, the mutant TS confers thymidine prototrophy on a TS-deficient bacterial strain when expressed at high levels.	2'-deoxyuridylic acid	62-66	thymidylate synthetase	Homo sapiens	121-123
10509749-3	1999	Although the kcat/Km of the mutant protein for the substrate, dUMP, is 10(3) lower than that of wild-type TS, the mutant TS confers thymidine prototrophy on a TS-deficient bacterial strain when expressed at high levels.	2'-deoxyuridylic acid	62-66	thymidylate synthetase	Homo sapiens	121-123
10462544-4	1999	We showed that the recombinant UMP-CMP kinase phosphorylated CMP, dCMP, and UMP with highest efficiency and dUMP, AMP, and dAMP with lower efficiency.	2'-deoxyuridylic acid	108-112	cytidine/uridine monophosphate kinase 1	Homo sapiens	31-45
9894005-1	1999	Two crystal structures of rat thymidylate synthase (TS) complexed with dUMP and the anticancer drug Tomudex (ZD1694) have been determined to resolutions of 3.3 and 2.6 A. Tomudex is one of several new antifolates targeted to TS and the first to be approved for clinical use.	2'-deoxyuridylic acid	71-75	thymidylate synthetase	Rattus norvegicus	30-50
10220346-9	1999	In addition, the binding of the folate analogue, CB3717, to dUMP binary complexes of mutant enzymes was characterized by a slow isomerization phase that was not detected in binding studies utilizing wild-type hTS.	2'-deoxyuridylic acid	60-64	APC down-regulated 1	Homo sapiens	209-212
9894005-1	1999	Two crystal structures of rat thymidylate synthase (TS) complexed with dUMP and the anticancer drug Tomudex (ZD1694) have been determined to resolutions of 3.3 and 2.6 A. Tomudex is one of several new antifolates targeted to TS and the first to be approved for clinical use.	2'-deoxyuridylic acid	71-75	thymidylate synthetase	Rattus norvegicus	52-54
9894005-1	1999	Two crystal structures of rat thymidylate synthase (TS) complexed with dUMP and the anticancer drug Tomudex (ZD1694) have been determined to resolutions of 3.3 and 2.6 A. Tomudex is one of several new antifolates targeted to TS and the first to be approved for clinical use.	2'-deoxyuridylic acid	71-75	thymidylate synthetase	Rattus norvegicus	225-227
10794525-8	1999	These observations suggest the existence of variants of dUTPase, some of which may influence nuclear receptor function during development and differentiation, in addition to catalyzing the hydrolysis of dUTP to dUMP.	2'-deoxyuridylic acid	211-215	Deoxyuridine triphosphatase	Drosophila melanogaster	56-63
10698291-4	1999	The new assay was tested to show comparable results with a previously described assay, based on measuring dUTPase-catalyzed [5-(3)H]dUMP production.	2'-deoxyuridylic acid	132-136	Deoxyuridine triphosphatase	Drosophila melanogaster	106-113
21374032-4	1999	Most investigations into cellular resistance factors regulating 5-FU activity have focused on alterations in (TS) levels and reduced folate pools, the required cofactor for binding dUMP to thymidylate synthase (1).	2'-deoxyuridylic acid	181-185	thymidylate synthase	Mus musculus	189-209
9821803-1	1998	Thymidylate synthase (TS) catalyzes the conversion of deoxyuridylate to thymidylate.	2'-deoxyuridylic acid	54-68	thymidylate synthetase	Homo sapiens	0-20
9748254-1	1998	Thymidylate synthase (TS) catalyzes the methylation of dUMP to dTMP and is the target for the widely used chemotherapeutic agent 5-fluorouracil.	2'-deoxyuridylic acid	55-59	thymidylate synthetase	Homo sapiens	0-20
9821803-1	1998	Thymidylate synthase (TS) catalyzes the conversion of deoxyuridylate to thymidylate.	2'-deoxyuridylic acid	54-68	thymidylate synthetase	Homo sapiens	22-24
9990482-3	1998	This allowed linear extension from an allele-specific primer and the incorporation of digoxigenin-labeled deoxyuridine monophosphate from digoxigenin-11-deoxyuridine triphosphate in the presence of the appropriate K-ras allele.	2'-deoxyuridylic acid	106-132	KRAS proto-oncogene, GTPase	Homo sapiens	214-219
9668195-1	1998	Thymidylate synthase (TS), an enzyme that catalyses the conversion of dUMP to dTMP, has been the focus of interest as a target in cancer chemotherapy for more than two decades.	2'-deoxyuridylic acid	70-74	thymidylate synthetase	Homo sapiens	0-20
9668195-1	1998	Thymidylate synthase (TS), an enzyme that catalyses the conversion of dUMP to dTMP, has been the focus of interest as a target in cancer chemotherapy for more than two decades.	2'-deoxyuridylic acid	70-74	thymidylate synthetase	Homo sapiens	22-24
9463483-8	1998	FUra-mediated thymidylate synthase inhibition was accompanied by a 124-fold increase in total deoxyuridylate immunoreactivity and a 31-fold increase in dUTP pools, but the addition of IFN-alpha + gamma attenuated the accumulation.	2'-deoxyuridylic acid	94-108	thymidylate synthetase	Homo sapiens	14-34
9497317-2	1998	The putative gene was expressed in Escherichia coli, and dUTPase activity of the recombinant enzyme was demonstrated by hydrolysis of dUTP to dUMP.	2'-deoxyuridylic acid	142-146	Deoxyuridine triphosphatase	Drosophila melanogaster	57-64
9540799-1	1998	In order to understand the influence on thymidylate synthase interactions with dUMP analogues of the pyrimidine ring 2- and/or 4-thio, and 5-fluoro substitutions, X-ray diffractions by crystals of 5-fluoro-dUrd and its 2- and 4-thio, and 2,4-dithio analogues were measured, the four structures solved and refined.	2'-deoxyuridylic acid	79-83	thymidylate synthetase	Homo sapiens	40-60
9398324-2	1997	As a result, the cytosine moiety of dCMP is displaced from the active site and the catalytic thiol is moved from the C6 of the substrate about 0.5 A further than in the wild-type TS-dUMP complex.	2'-deoxyuridylic acid	182-186	cmp	Drosophila melanogaster	36-40
9398324-6	1997	The structures of TS H199A/N229D in complex with dCMP and dUMP confirmed that the position and orientation of bound dCMP closely approaches that of dUMP in wild-type TS, whereas dUMP was displaced from the optimal catalytic binding site.	2'-deoxyuridylic acid	58-62	cmp	Drosophila melanogaster	116-120
9398324-1	1997	X-ray crystal structures of binary complexes of dUMP or dCMP with the Lactobacillus caseiTS mutant N229D, a dCMP methylase, revealed that there is a steric clash between the 4-NH2 of dCMP and His 199, a residue which normally H-bonds to the 4-O of dUMP but is not essential for activity.	2'-deoxyuridylic acid	48-52	cmp	Drosophila melanogaster	108-112
9398324-6	1997	The structures of TS H199A/N229D in complex with dCMP and dUMP confirmed that the position and orientation of bound dCMP closely approaches that of dUMP in wild-type TS, whereas dUMP was displaced from the optimal catalytic binding site.	2'-deoxyuridylic acid	148-152	cmp	Drosophila melanogaster	49-53
9398324-1	1997	X-ray crystal structures of binary complexes of dUMP or dCMP with the Lactobacillus caseiTS mutant N229D, a dCMP methylase, revealed that there is a steric clash between the 4-NH2 of dCMP and His 199, a residue which normally H-bonds to the 4-O of dUMP but is not essential for activity.	2'-deoxyuridylic acid	48-52	cmp	Drosophila melanogaster	108-112
9398324-1	1997	X-ray crystal structures of binary complexes of dUMP or dCMP with the Lactobacillus caseiTS mutant N229D, a dCMP methylase, revealed that there is a steric clash between the 4-NH2 of dCMP and His 199, a residue which normally H-bonds to the 4-O of dUMP but is not essential for activity.	2'-deoxyuridylic acid	248-252	cmp	Drosophila melanogaster	56-60
9398324-6	1997	The structures of TS H199A/N229D in complex with dCMP and dUMP confirmed that the position and orientation of bound dCMP closely approaches that of dUMP in wild-type TS, whereas dUMP was displaced from the optimal catalytic binding site.	2'-deoxyuridylic acid	148-152	cmp	Drosophila melanogaster	116-120
9398324-1	1997	X-ray crystal structures of binary complexes of dUMP or dCMP with the Lactobacillus caseiTS mutant N229D, a dCMP methylase, revealed that there is a steric clash between the 4-NH2 of dCMP and His 199, a residue which normally H-bonds to the 4-O of dUMP but is not essential for activity.	2'-deoxyuridylic acid	248-252	cmp	Drosophila melanogaster	108-112
9398324-6	1997	The structures of TS H199A/N229D in complex with dCMP and dUMP confirmed that the position and orientation of bound dCMP closely approaches that of dUMP in wild-type TS, whereas dUMP was displaced from the optimal catalytic binding site.	2'-deoxyuridylic acid	148-152	cmp	Drosophila melanogaster	49-53
9398324-1	1997	X-ray crystal structures of binary complexes of dUMP or dCMP with the Lactobacillus caseiTS mutant N229D, a dCMP methylase, revealed that there is a steric clash between the 4-NH2 of dCMP and His 199, a residue which normally H-bonds to the 4-O of dUMP but is not essential for activity.	2'-deoxyuridylic acid	248-252	cmp	Drosophila melanogaster	108-112
9398324-6	1997	The structures of TS H199A/N229D in complex with dCMP and dUMP confirmed that the position and orientation of bound dCMP closely approaches that of dUMP in wild-type TS, whereas dUMP was displaced from the optimal catalytic binding site.	2'-deoxyuridylic acid	148-152	cmp	Drosophila melanogaster	116-120
9535167-2	1997	The reaction catalyzed by TS is the methylation of dUMP, with the transferred methyl group provided by the cofactor methylenetetrahydrofolate (CH2THF).	2'-deoxyuridylic acid	51-55	thymidylate synthetase	Homo sapiens	26-28
9535167-4	1997	Included among these structures are complexes of TS bound to substrate dUMP; cofactor CH2THF; the nucleotide analogs 5-fluoro-dUMP, 5-nitro-dUMP and dGMP; and the promising antifolates BW1843, ZD1694, and AG337.	2'-deoxyuridylic acid	71-75	thymidylate synthetase	Homo sapiens	49-51
8805593-2	1996	dUTPase hydrolyzes dUTP to dUMP and pyrophosphate, simultaneously reducing dUTP levels and providing the dUMP for dTTP biosynthesis.	2'-deoxyuridylic acid	27-31	Deoxyuridine triphosphatase	Drosophila melanogaster	0-7
9171083-7	1997	Chemical probing with KMnO4showed that the presence of SSB resulted in the reduction of cleavage of the nucleotides in the vicinity of dUMP residue in single stranded substrates but their increased susceptibility in the hairpin substrates.	2'-deoxyuridylic acid	135-139	single-stranded DNA-binding protein	Escherichia coli	55-58
9000104-1	1996	The enzyme dUTPase catalyses the hydrolysis of dUTP to dUMP and pyrophosphate, thereby suppressing incorporation of uracil into DNA and providing a pool of dUMP, the precursor of dTTP.	2'-deoxyuridylic acid	55-59	Deoxyuridine triphosphatase	Drosophila melanogaster	11-18
9000104-1	1996	The enzyme dUTPase catalyses the hydrolysis of dUTP to dUMP and pyrophosphate, thereby suppressing incorporation of uracil into DNA and providing a pool of dUMP, the precursor of dTTP.	2'-deoxyuridylic acid	156-160	Deoxyuridine triphosphatase	Drosophila melanogaster	11-18
8798636-1	1996	The enzyme dUTPase catalyzes the hydrolysis of dUTP to dUMP and pyrophosphate, thereby preventing a deleterious incorporation of uracil into DNA.	2'-deoxyuridylic acid	55-59	Deoxyuridine triphosphatase	Drosophila melanogaster	11-18
9256160-7	1997	This study showed changes in the TS enzyme kinetics during the induction of doxorubicin resistance in both SW-1573 variants, resulting in 2-fold lower Km values for 2"-deoxyuridine-5"-monophosphate (dUMP) in both resistant variants compared to the parental cell line.	2'-deoxyuridylic acid	165-197	thymidylate synthetase	Homo sapiens	33-35
9256160-7	1997	This study showed changes in the TS enzyme kinetics during the induction of doxorubicin resistance in both SW-1573 variants, resulting in 2-fold lower Km values for 2"-deoxyuridine-5"-monophosphate (dUMP) in both resistant variants compared to the parental cell line.	2'-deoxyuridylic acid	199-203	thymidylate synthetase	Homo sapiens	33-35
9048572-1	1997	Several steps of the reaction catalyzed by thymidylate synthase (TS) require proton transfers to and from O-4 and C-5 of the pyrimidine moiety of substrate dUMP.	2'-deoxyuridylic acid	156-160	thymidylate synthetase	Homo sapiens	43-63
9048572-1	1997	Several steps of the reaction catalyzed by thymidylate synthase (TS) require proton transfers to and from O-4 and C-5 of the pyrimidine moiety of substrate dUMP.	2'-deoxyuridylic acid	156-160	thymidylate synthetase	Homo sapiens	65-67
9048572-1	1997	Several steps of the reaction catalyzed by thymidylate synthase (TS) require proton transfers to and from O-4 and C-5 of the pyrimidine moiety of substrate dUMP.	2'-deoxyuridylic acid	156-160	immunoglobulin kappa variable 1D-37 (non-functional)	Homo sapiens	106-109
8805593-2	1996	dUTPase hydrolyzes dUTP to dUMP and pyrophosphate, simultaneously reducing dUTP levels and providing the dUMP for dTTP biosynthesis.	2'-deoxyuridylic acid	105-109	Deoxyuridine triphosphatase	Drosophila melanogaster	0-7
8805593-4	1996	We report the first detailed atomic-resolution structure of a eukaryotic dUTPase, human dUTPase, and complexes with the uracil-containing deoxyribonucleotides, dUMP, dUDP and dUTP.	2'-deoxyuridylic acid	160-164	Deoxyuridine triphosphatase	Drosophila melanogaster	73-80
8805593-4	1996	We report the first detailed atomic-resolution structure of a eukaryotic dUTPase, human dUTPase, and complexes with the uracil-containing deoxyribonucleotides, dUMP, dUDP and dUTP.	2'-deoxyuridylic acid	160-164	Deoxyuridine triphosphatase	Drosophila melanogaster	88-95
8672425-1	1996	The conserved Asn 229 of thymidylate synthase (TS) forms a cyclic hydrogen bond network with the 3-NH and 4-O of the nucleotide substrate 2"-deoxyuridine 5"-monophosphate (dUMP).	2'-deoxyuridylic acid	138-170	thymidylate synthetase	Homo sapiens	25-45
8787551-1	1996	ZD1694 (Tomudex; TDX) is a quinazoline antifolate that, when polyglutamated, is a potent inhibitor of thymidylate synthase (TS), the enzyme that converts dUMP to dTMP.	2'-deoxyuridylic acid	154-158	thymidylate synthetase	Homo sapiens	102-122
8787551-1	1996	ZD1694 (Tomudex; TDX) is a quinazoline antifolate that, when polyglutamated, is a potent inhibitor of thymidylate synthase (TS), the enzyme that converts dUMP to dTMP.	2'-deoxyuridylic acid	154-158	thymidylate synthetase	Homo sapiens	124-126
8611496-1	1996	Thymidylate synthase (TS) methylates only dUMP, not dCMP.	2'-deoxyuridylic acid	42-46	thymidylate synthetase	Homo sapiens	0-20
8672425-1	1996	The conserved Asn 229 of thymidylate synthase (TS) forms a cyclic hydrogen bond network with the 3-NH and 4-O of the nucleotide substrate 2"-deoxyuridine 5"-monophosphate (dUMP).	2'-deoxyuridylic acid	172-176	thymidylate synthetase	Homo sapiens	25-45
8790719-0	1996	Molecular mechanism of thymidylate synthase-catalyzed reaction and interaction of the enzyme with 2- and/or 4-substituted analogues of dUMP and 5-fluoro-dUMP.	2'-deoxyuridylic acid	135-139	thymidylate synthetase	Homo sapiens	23-43
8604980-2	1996	The substrate dUMP and the cofactor Mg2+ protect against inactivation and modification, in agreement with the study on E. coli dUTPase (Vertessy et al.	2'-deoxyuridylic acid	14-18	Deoxyuridine triphosphatase	Drosophila melanogaster	127-134
8534956-6	1995	Marrow cells from B12- or folate-deficient patients show a subnormal suppression of 3H-thymidine incorporation after pre-incubation with nonradioactive deoxyuridine, suggesting that such cells suffer from an impairment of the 5,10-methylene-THF-dependent methylation of deoxyuridylate to thymidylate.	2'-deoxyuridylic acid	270-284	NADH:ubiquinone oxidoreductase subunit B3	Homo sapiens	18-21
8711189-1	1996	In the paper a thorough study of the influence of the methemoglobin levels and the occurrence of certain syndromes of clinical symptoms was made in the inhabitants living in the immediate vicinity of the large refuse dumps.	2'-deoxyuridylic acid	217-222	hemoglobin subunit gamma 2	Homo sapiens	54-67
8790719-2	1996	With two dUMP analogues, 5-fluoro-dUMP (FdUMP) and 5-(trifluoromethyl)-dUMP (CF3dUMP), strong thymidylate synthase inhibitors and active forms of drugs, the inhibition mechanism is based on the reaction mechanism.	2'-deoxyuridylic acid	9-13	thymidylate synthetase	Homo sapiens	94-114
8086425-1	1994	The interactions of thymidylate synthase (TS) with deoxyuridylate (dUMP), deoxythymidylate (dTMP) and 5-fluorodeoxyuridylate (FdUMP) were examined by 31P-NMR.	2'-deoxyuridylic acid	51-65	thymidylate synthetase	Homo sapiens	20-40
7647337-1	1995	Thymidylate synthetase (TS) is a key enzyme as a methyl donor in the methylation reaction from dUMP to dTMP.	2'-deoxyuridylic acid	95-99	thymidylate synthetase	Homo sapiens	0-22
7724588-5	1995	An explanation for the binding of dGMP was provided by x-ray diffraction studies that revealed an extensive stacking interaction between the guanine of dGMP and the benzoquinazoline ring of U89 and hydrogen bonds similar to those involved in dUMP binding.	2'-deoxyuridylic acid	242-246	fliF	Drosophila melanogaster	34-38
7724588-5	1995	An explanation for the binding of dGMP was provided by x-ray diffraction studies that revealed an extensive stacking interaction between the guanine of dGMP and the benzoquinazoline ring of U89 and hydrogen bonds similar to those involved in dUMP binding.	2'-deoxyuridylic acid	242-246	fliF	Drosophila melanogaster	152-156
7623777-1	1995	Thymidylate synthase (TS) is a homodimeric enzyme that catalyzes the reductive methylation of dUMP by N5,N10-methylene-5,6,7,8-tetrahydrofolic acid, to form dTMP.	2'-deoxyuridylic acid	94-98	thymidylate synthetase	Homo sapiens	0-20
7779704-3	1995	Similar variations in TS levels and TS activity were detected using the 5-fluorodeoxyuridine monophosphate and deoxyuridine monophosphate biochemical assays.	2'-deoxyuridylic acid	80-106	thymidylate synthetase	Homo sapiens	22-24
7779704-3	1995	Similar variations in TS levels and TS activity were detected using the 5-fluorodeoxyuridine monophosphate and deoxyuridine monophosphate biochemical assays.	2'-deoxyuridylic acid	80-106	thymidylate synthetase	Homo sapiens	36-38
7663176-1	1995	Deoxyuridine 5"-triphosphate nucleotidohydrolase (dUTPase, EC 3.6.1.23) catalyzes the hydrolysis of dUTP to dUMP and pyrophosphate, and plays important roles in nucleotide metabolism and DNA replication.	2'-deoxyuridylic acid	108-112	Deoxyuridine triphosphatase	Drosophila melanogaster	50-57
7574499-1	1995	Thymidylate synthase (TS, EC 2.1.1.45) catalyzes the reductive methylation of dUMP by CH2H4folate to produce dTMP and H2folate.	2'-deoxyuridylic acid	78-82	thymidylate synthetase	Homo sapiens	0-20
7574499-1	1995	Thymidylate synthase (TS, EC 2.1.1.45) catalyzes the reductive methylation of dUMP by CH2H4folate to produce dTMP and H2folate.	2'-deoxyuridylic acid	78-82	thymidylate synthetase	Homo sapiens	22-24
8086425-1	1994	The interactions of thymidylate synthase (TS) with deoxyuridylate (dUMP), deoxythymidylate (dTMP) and 5-fluorodeoxyuridylate (FdUMP) were examined by 31P-NMR.	2'-deoxyuridylic acid	67-71	thymidylate synthetase	Homo sapiens	20-40
8369294-1	1993	In thymidylate synthase (TS, EC 2.1.1.45), the only side chain in direct hydrogen bonding with the pyrimidine ring of the substrate dUMP is asparagine 229 (N229).	2'-deoxyuridylic acid	132-136	thymidylate synthetase	Homo sapiens	3-23
8051080-3	1994	By using the adenovirus 2 major late promoter tagged site-specifically with the photoactivatible cross-linking reagent N3R-dUMP we have localized TBP, two subunits of TFIIA (A35 and A21), TFIIB, and RAP30 along promoter DNA.	2'-deoxyuridylic acid	123-127	TATA-box binding protein	Homo sapiens	146-149
8051080-3	1994	By using the adenovirus 2 major late promoter tagged site-specifically with the photoactivatible cross-linking reagent N3R-dUMP we have localized TBP, two subunits of TFIIA (A35 and A21), TFIIB, and RAP30 along promoter DNA.	2'-deoxyuridylic acid	123-127	general transcription factor IIA subunit 1	Homo sapiens	167-172
8294436-4	1994	Thymidylate synthase bound both mono and polyglutamylated folate substrates and analogs more tightly in the presence of deoxyuridylate.	2'-deoxyuridylic acid	120-134	thymidylate synthetase	Homo sapiens	0-20
8223452-1	1993	dUTP pyrophosphatase (dUTPase; EC 3.6.1.23) catalyses the hydrolysis of dUTP to dUMP and PPi and thereby prevents the incorporation of uracil into DNA during replication.	2'-deoxyuridylic acid	80-84	Deoxyuridine triphosphatase	Drosophila melanogaster	22-29
8399157-2	1993	In order to extent and confirm this paradigm, complexes of thymidylate synthase (TS) and the N-10-(fluoroethyl)quinazolinylfolate analogue CB3731 with either deoxyuridine 5"-monophosphate (dUMP), deoxythymidine 5"-monophosphate (dTMP), or FdUMP were examined from the perspective of the folate analogue using 19F NMR.	2'-deoxyuridylic acid	189-193	thymidylate synthetase	Homo sapiens	59-79
7504257-6	1993	We tested the new algorithm"s ability to reproduce three known ligand-receptor complexes: methotrexate in dihydrofolate reductase, deoxyuridine monophosphate in thymidylate synthase and pancreatic trypsin inhibitor in trypsin.	2'-deoxyuridylic acid	131-157	thymidylate synthetase	Homo sapiens	161-181
8246876-1	1993	Thymidine kinase (TK) and thymidylate synthetase (TS) are known to catalyse the phosphorylation of thymidine for the salvage synthesis of dTMP and the methylation of dUMP for the de novo synthesis of dTMP, respectively.	2'-deoxyuridylic acid	166-170	thymidylate synthetase	Homo sapiens	26-48
8343503-0	1993	Structures of thymidylate synthase with a C-terminal deletion: role of the C-terminus in alignment of 2"-deoxyuridine 5"-monophosphate and 5,10-methylenetetrahydrofolate.	2'-deoxyuridylic acid	102-134	thymidylate synthetase	Homo sapiens	14-34
8400344-1	1993	Thymidylate synthase (TS) is responsible for the conversion of deoxyuridine monophosphate to deoxythymidine monophosphate.	2'-deoxyuridylic acid	63-89	thymidylate synthetase	Homo sapiens	0-20
8400344-1	1993	Thymidylate synthase (TS) is responsible for the conversion of deoxyuridine monophosphate to deoxythymidine monophosphate.	2'-deoxyuridylic acid	63-89	thymidylate synthetase	Homo sapiens	22-24
8450671-6	1993	Substrate specificity was the same for both enzymes with the following relative Vmax values: CMP > UMP > dUMP > dCMP > dAMP > IMP > GMP > dIMP > dGMP.	2'-deoxyuridylic acid	111-115	5'-nucleotidase, cytosolic II	Homo sapiens	150-153
8386036-1	1993	Deoxyuridine 5"-triphosphate nucleotidohydrolase (dUTPase), widespread in nature with a crucial role in the nucleotide metabolism, catalyzes the hydrolysis of dUTP to dUMP and pyrophosphate.	2'-deoxyuridylic acid	167-171	Deoxyuridine triphosphatase	Drosophila melanogaster	50-57
8349008-8	1993	The presence of dUMP, dTMP, or FdUMP interfered with the binding of PLP to thymidylate synthase, and the presence of equimolar amounts of PLP interfered with the binding of dUMP.	2'-deoxyuridylic acid	16-20	thymidylate synthetase	Homo sapiens	75-95
8349008-8	1993	The presence of dUMP, dTMP, or FdUMP interfered with the binding of PLP to thymidylate synthase, and the presence of equimolar amounts of PLP interfered with the binding of dUMP.	2'-deoxyuridylic acid	32-36	thymidylate synthetase	Homo sapiens	75-95
1456447-4	1992	Selective degradation of the dUMP residues in the PCR products with uracil DNA glycosylase (UDG) disrupts base pairing at the termini and generates 3" overhangs.	2'-deoxyuridylic acid	29-33	uracil DNA glycosylase	Homo sapiens	68-90
8249493-0	1993	Specificity of thymidylate synthase inactivation by 4,5-bisubstituted dUMP analogues.	2'-deoxyuridylic acid	70-74	thymidylate synthetase	Homo sapiens	15-35
1456447-4	1992	Selective degradation of the dUMP residues in the PCR products with uracil DNA glycosylase (UDG) disrupts base pairing at the termini and generates 3" overhangs.	2'-deoxyuridylic acid	29-33	uracil DNA glycosylase	Homo sapiens	92-95
1641659-8	1992	High levels of deoxyuridine monophosphate that have been associated with resistance to 5-fluorouracil can be suppressed by hydroxyurea, leading to greater inhibition of thymidylate synthase.	2'-deoxyuridylic acid	15-41	thymidylate synthetase	Homo sapiens	169-189
1430788-1	1992	Thymidylate synthetase catalyses the formation of thymidine monophosphate from deoxyuridine monophosphate.	2'-deoxyuridylic acid	79-105	thymidylate synthetase	Homo sapiens	0-22
1430788-2	1992	Purified thymidylate synthetase can be assayed radiochemically using labelled deoxyuridine monophosphate as substrate, but cells are impervious to deoxyuridine monophosphate and so intracellular thymidylate synthetase activity cannot be assayed in this way.	2'-deoxyuridylic acid	78-104	thymidylate synthetase	Homo sapiens	9-31
1324907-1	1992	In Escherichia coli, most of the dUMP that is used as a substrate for thymidylate synthetase is generated from dCTP through the sequential action of dCTP deaminase and dUTPase.	2'-deoxyuridylic acid	33-37	Deoxyuridine triphosphatase	Drosophila melanogaster	149-175
1557655-4	1992	In nontreated patients we observed a large variation in the activity of TS both at 1 microM and 10 microM dUMP (40- to 80-fold difference).	2'-deoxyuridylic acid	106-110	thymidylate synthetase	Homo sapiens	72-74
1720706-1	1991	Thymidylate synthase (TS; EC 2.1.1.45) is an important cellular enzyme that converts dUMP to dTMP, which is essential for DNA biosynthesis.	2'-deoxyuridylic acid	85-89	thymidylate synthetase	Homo sapiens	0-20
1284431-6	1992	The presence of the substrate dUMP (10 microM) completely protected thymidylate synthase from inhibition.	2'-deoxyuridylic acid	30-34	thymidylate synthetase	Homo sapiens	68-88
1720706-1	1991	Thymidylate synthase (TS; EC 2.1.1.45) is an important cellular enzyme that converts dUMP to dTMP, which is essential for DNA biosynthesis.	2'-deoxyuridylic acid	85-89	thymidylate synthetase	Homo sapiens	22-24
1726854-1	1991	By incorporating dUMP residues into the 5" end of PCR primers, one can generate products which, after treatment with uracil DNA glycosylase (UDG), contain 3" overhangs.	2'-deoxyuridylic acid	17-21	uracil DNA glycosylase	Homo sapiens	117-139
1938887-1	1991	Uracil-DNA-glycosylase has been proposed to function as the first enzyme in strand-directed mismatch repair in eukaryotic organisms, through removal of uracil from dUMP residues periodically inserted into the DNA during DNA replication (Aprelikova, O. N., V. M. Golubovskaya, T. A. Kusmin, and N. V. Tomilin, Mutat.	2'-deoxyuridylic acid	164-168	uracil-DNA glycosylase	Saccharomyces cerevisiae S288C	0-22
1726854-1	1991	By incorporating dUMP residues into the 5" end of PCR primers, one can generate products which, after treatment with uracil DNA glycosylase (UDG), contain 3" overhangs.	2'-deoxyuridylic acid	17-21	uracil DNA glycosylase	Homo sapiens	141-144
2244925-2	1990	We show that 7-hydroxymethotrexate and dideazafolates require the prior binding of dUMP or its fluorinated derivative FdUMP to bind to thymidylate synthase, as does methotrexate.	2'-deoxyuridylic acid	83-87	thymidylate synthetase	Homo sapiens	135-155
2007141-1	1991	Terminal deoxynucleotidyl transferase (terminal transferase) was specifically modified in the DNA binding site by a photoactive DNA substrate (hetero-40-mer duplex containing eight 5-azido-dUMP residues at one 3" end).	2'-deoxyuridylic acid	189-193	DNA nucleotidylexotransferase	Homo sapiens	0-37
2007141-1	1991	Terminal deoxynucleotidyl transferase (terminal transferase) was specifically modified in the DNA binding site by a photoactive DNA substrate (hetero-40-mer duplex containing eight 5-azido-dUMP residues at one 3" end).	2'-deoxyuridylic acid	189-193	DNA nucleotidylexotransferase	Homo sapiens	39-59
1924359-6	1991	The inclusion of dUMP, 5-fluoro-dUMP, or 5,10-methylene-tetrahydrofolate in in vitro translation reactions completely relieved the inhibition of TS mRNA translation by TS protein.	2'-deoxyuridylic acid	17-21	thymidylate synthetase	Homo sapiens	145-147
1924359-6	1991	The inclusion of dUMP, 5-fluoro-dUMP, or 5,10-methylene-tetrahydrofolate in in vitro translation reactions completely relieved the inhibition of TS mRNA translation by TS protein.	2'-deoxyuridylic acid	17-21	thymidylate synthetase	Homo sapiens	168-170
2244925-4	1990	On the other hand, both dUMP and FdUMP exhibited a large cooperative effect on the affinity for thymidylate synthase of the inhibitors, and surprisingly, no significant difference was shown at this level between the natural substrate dUMP and its fluorinated derivative.	2'-deoxyuridylic acid	24-28	thymidylate synthetase	Homo sapiens	96-116
2244925-4	1990	On the other hand, both dUMP and FdUMP exhibited a large cooperative effect on the affinity for thymidylate synthase of the inhibitors, and surprisingly, no significant difference was shown at this level between the natural substrate dUMP and its fluorinated derivative.	2'-deoxyuridylic acid	34-38	thymidylate synthetase	Homo sapiens	96-116
2244925-6	1990	In the presence of FdUMP or dUMP, all the studied compounds except 7-hydroxymethotrexate exhibited a large negative enthalpy variation when binding to thymidylate synthase (from -44 to -91 kJ/mol).	2'-deoxyuridylic acid	20-24	thymidylate synthetase	Homo sapiens	151-171
1694967-3	1990	Since uracil DNA-glycosylase functions to prevent the mutagenic effects of uracil in DNA coming as a product of deamination of cytosine residues or as a result of dUMP incorporation by DNA polymerase, we have studied the perinatal activity of uracil DNA-glycosylase and of 2 enzymes (nucleoside diphosphokinase and dUTPase) involved in dUTP metabolism.	2'-deoxyuridylic acid	163-167	uracil DNA glycosylase	Homo sapiens	6-28
1694967-5	1990	However, misincorporation of dUMP into DNA might be kept to a low frequency by the action of dUTPase present at all developmental stages.	2'-deoxyuridylic acid	29-33	Deoxyuridine triphosphatase	Drosophila melanogaster	93-100
33824328-3	2021	dUTPase catalyses the hydrolytic dephosphorylation of deoxyuridine triphosphate (dUTP) to deoxyuridine monophosphate (dUMP), providing dUMP for thymidylate synthase as part of the thymidylate biosynthesis pathway and maintaining low intracellular dUTP concentrations.	2'-deoxyuridylic acid	90-116	Deoxyuridine triphosphatase	Drosophila melanogaster	0-7
2153555-1	1990	Deoxyuridine triphosphate nucleotidohydrolase (dUTPase), a key enzyme in pyrimidine nucleotide metabolism, specifically hydrolyzes deoxyuridine triphosphate (dUTP) to deoxyuridine monophosphate and inorganic pyrophosphate.	2'-deoxyuridylic acid	167-193	Deoxyuridine triphosphatase	Drosophila melanogaster	47-54
33824328-3	2021	dUTPase catalyses the hydrolytic dephosphorylation of deoxyuridine triphosphate (dUTP) to deoxyuridine monophosphate (dUMP), providing dUMP for thymidylate synthase as part of the thymidylate biosynthesis pathway and maintaining low intracellular dUTP concentrations.	2'-deoxyuridylic acid	118-122	Deoxyuridine triphosphatase	Drosophila melanogaster	0-7
33824328-3	2021	dUTPase catalyses the hydrolytic dephosphorylation of deoxyuridine triphosphate (dUTP) to deoxyuridine monophosphate (dUMP), providing dUMP for thymidylate synthase as part of the thymidylate biosynthesis pathway and maintaining low intracellular dUTP concentrations.	2'-deoxyuridylic acid	135-139	Deoxyuridine triphosphatase	Drosophila melanogaster	0-7
33800923-0	2021	Advanced Spectroscopy and APBS Modeling for Determination of the Role of His190 and Trp103 in Mouse Thymidylate Synthase Interaction with Selected dUMP Analogues.	2'-deoxyuridylic acid	147-151	thymidylate synthase	Mus musculus	100-120
34778377-2	2021	5-Fu/LV prevents cell proliferation by inhibiting thymidylate synthase, which catalyzes the conversion of deoxyuridine monophosphate to deoxythymidine monophosphate.	2'-deoxyuridylic acid	106-132	thymidylate synthase	Mus musculus	50-70
10355777-2	1999	The results show that KSHV/HHV-8 ORF54 encodes a functional dUTPase which specifically hydrolyses dUTP to dUMP.	2'-deoxyuridylic acid	106-110	ORF54	Human gammaherpesvirus 8	33-38
10355777-2	1999	The results show that KSHV/HHV-8 ORF54 encodes a functional dUTPase which specifically hydrolyses dUTP to dUMP.	2'-deoxyuridylic acid	106-110	Deoxyuridine triphosphatase	Drosophila melanogaster	60-67
34247080-7	2021	Water flow regimes within dumps are dominated by matrix and/or preferential flow, depending on dump texture; these flow mechanisms exert a primary control on patterns of aqueous COI release.	2'-deoxyuridylic acid	26-31	mitochondrially encoded cytochrome c oxidase I	Homo sapiens	178-181
34247080-7	2021	Water flow regimes within dumps are dominated by matrix and/or preferential flow, depending on dump texture; these flow mechanisms exert a primary control on patterns of aqueous COI release.	2'-deoxyuridylic acid	95-99	mitochondrially encoded cytochrome c oxidase I	Homo sapiens	178-181
34247080-8	2021	The inability to successfully transfer COI release rates from laboratory or field scale trials to operational scale dumps is primarily due to limitations of testing methods and fundamental characteristics of scale.	2'-deoxyuridylic acid	116-121	mitochondrially encoded cytochrome c oxidase I	Homo sapiens	39-42
35568200-5	2022	This efficient substrate discrimination is in line with the lack of thymidylate synthase and dUTPase in the parasite, which makes dUMP a dead-end product that is potentially harmful if converted to dUTP.	2'-deoxyuridylic acid	130-134	Deoxyuridine triphosphatase	Drosophila melanogaster	93-100
35427566-5	2022	Thymidylate synthase (TYMS), the major target of chemotherapeutic drugs 5-FU or other fluoropyrimidines, which catalyzes the conversion of dUMP to dTMP and provides the sole de novo source of thymidylate for DNA synthesis.	2'-deoxyuridylic acid	139-143	thymidylate synthetase	Homo sapiens	0-20
35427566-5	2022	Thymidylate synthase (TYMS), the major target of chemotherapeutic drugs 5-FU or other fluoropyrimidines, which catalyzes the conversion of dUMP to dTMP and provides the sole de novo source of thymidylate for DNA synthesis.	2'-deoxyuridylic acid	139-143	thymidylate synthetase	Homo sapiens	22-26
3814166-0	1987	Studies on the interaction with thymidylate synthase of analogues of 2"-deoxyuridine-5"-phosphate and 5-fluoro-2"-deoxyuridine-5"-phosphate with modified phosphate groups.	2'-deoxyuridylic acid	69-97	thymidylate synthetase	Homo sapiens	32-52
2693217-6	1989	Kinetic studies with the recombinant enzyme showed that the apparent Km values for deoxyuridylate and 5,10-methylenetetrahydrofolate were 10.5 and 22 microM, respectively, which were similar to the values for TS from mouse cell extracts.	2'-deoxyuridylic acid	83-97	thymidylate synthase	Mus musculus	209-211
2761553-1	1989	An inhibitor of uracil-DNA glycosylase, uracil, induces an increase in the size of pulse-labelled DNA fragments in human cells in vivo suggesting that dUMP incorporation into DNA and uracil-DNA glycosylase contribute to the small size of pulse-labelled DNA.	2'-deoxyuridylic acid	151-155	uracil DNA glycosylase	Homo sapiens	16-38
2525127-6	1989	Consequently, it is postulated that the enhanced activity of 10-propargyl-5,8-dideazafolate in combination with low concentrations of dihydrofolate reductase inhibitors is due to an increase in the ratio of inhibitor to substrate for thymidylate synthase of nearly 10-fold and an extensive enhancement of the dUMP pool.	2'-deoxyuridylic acid	309-313	thymidylate synthetase	Homo sapiens	234-254
2525127-7	1989	These conditions predispose the target enzyme and the cells to more effective metabolic blockade by 10-propargyl-5,8-dideazafolate which is presumably caused by the formation of an inhibited 10-propargyl-5,8-dideazafolate[polyglutamate]-thymidylate synthase-dUMP ternary complex.	2'-deoxyuridylic acid	258-262	thymidylate synthetase	Homo sapiens	237-257
2977717-2	1988	Following inhibition of thymidylate synthase, deoxyuridylate accumulates, as does the cellular content of thymidylate synthase.	2'-deoxyuridylic acid	46-60	thymidylate synthetase	Homo sapiens	24-44
3593415-5	1987	Based on these observations, a sensitive procedure for determining thymidylate synthase activity has been developed in which unbound nucleotides (dUMP, FdUMP) are removed prior to assay of enzyme activity.	2'-deoxyuridylic acid	146-150	thymidylate synthetase	Homo sapiens	67-87
3107544-3	1987	The inhibition of de novo pyrimidine synthesis prevents the production of deoxyuridine-5-phosphate, the substrate for the synthesis of thymidine-5-phosphate via thymidylate synthase, whereas the inhibition of the choline shunt prevents the production of HCHO groups and glycine, both of which are involved in the synthesis of 5,10-methylenetetrahydrofolate, which is a cofactor of thymidylate synthase.	2'-deoxyuridylic acid	74-98	Thymidylate synthase	Drosophila melanogaster	161-181
3107544-3	1987	The inhibition of de novo pyrimidine synthesis prevents the production of deoxyuridine-5-phosphate, the substrate for the synthesis of thymidine-5-phosphate via thymidylate synthase, whereas the inhibition of the choline shunt prevents the production of HCHO groups and glycine, both of which are involved in the synthesis of 5,10-methylenetetrahydrofolate, which is a cofactor of thymidylate synthase.	2'-deoxyuridylic acid	74-98	Thymidylate synthase	Drosophila melanogaster	381-401
3025197-2	1987	Deoxyuridine triphosphatase (dUTPase), an enzyme that catalyzes hydrolysis of dUTP to deoxyuridylate and inorganic pyrophosphate, has been purified approximately 6,000-fold from Drosophila embryos.	2'-deoxyuridylic acid	86-100	Deoxyuridine triphosphatase	Drosophila melanogaster	0-27
3025197-2	1987	Deoxyuridine triphosphatase (dUTPase), an enzyme that catalyzes hydrolysis of dUTP to deoxyuridylate and inorganic pyrophosphate, has been purified approximately 6,000-fold from Drosophila embryos.	2'-deoxyuridylic acid	86-100	Deoxyuridine triphosphatase	Drosophila melanogaster	29-36
3480707-1	1987	The role of the pyrimidine N(3)-H in binding of dUMP derivatives to thymidylate synthase was evaluated with the aid of a new dUMP analogue, 5-fluoro-4-thio-dUMP, synthesized by an improved thiation and enzymatic phosphorylation.	2'-deoxyuridylic acid	48-52	thymidylate synthetase	Homo sapiens	68-88
3480707-1	1987	The role of the pyrimidine N(3)-H in binding of dUMP derivatives to thymidylate synthase was evaluated with the aid of a new dUMP analogue, 5-fluoro-4-thio-dUMP, synthesized by an improved thiation and enzymatic phosphorylation.	2'-deoxyuridylic acid	125-129	thymidylate synthetase	Homo sapiens	68-88
2822457-5	1987	dNase activity occurred with both purine and pyrimidine substrates and was maximal with deoxy analogs (dIMP much greater than dUMP greater than dGMP greater than dTMP = dAMP much greater than dCMP) at a pH optimum of 6.2, but slight cross-reactivity occurred with some nondeoxy substrates (IMP greater than GMP greater than UMP = XMP greater than CMP).	2'-deoxyuridylic acid	126-130	Deoxyribonuclease II	Drosophila melanogaster	0-5
3814166-1	1987	The role of the phosphate moiety of dUMP, and some analogues, in their interaction with mammalian thymidylate synthase, has been investigated.	2'-deoxyuridylic acid	36-40	thymidylate synthetase	Homo sapiens	98-118
3745210-1	1986	The formation of covalent binary complexes of thymidylate synthase and its nucleotide substrate dUMP, product dTMP, and inhibitor, 5-fluorodeoxyuridylate (FdUMP) was investigated using the trichloroacetic acid precipitation method.	2'-deoxyuridylic acid	96-100	thymidylate synthetase	Homo sapiens	46-66
2947954-3	1987	It was found that drugs that have an indirect effect on this enzyme--methotrexate (MTX), hydroxyurea (HU), and 3,4-dihydroxybenzylamine (3,4-DHBA)--acted as noncompetitive inhibitors and the inhibition of thymidylate synthase by these drugs did not result in the accumulation of its substrate, dUMP.	2'-deoxyuridylic acid	294-298	thymidylate synthetase	Homo sapiens	205-225
2947954-4	1987	This suggested that these drugs are also inhibiting steps leading to the formation of dUMP by a mechanism that is coordinated with the inhibition of thymidylate synthase.	2'-deoxyuridylic acid	86-90	thymidylate synthetase	Homo sapiens	149-169
2947954-5	1987	5-Fluorodeoxyuridine (FUDR), a competitive inhibitor of thymidylate synthase, did cause an increase in the dUMP pool size indicating that this drug did not affect the synthesis of this substrate.	2'-deoxyuridylic acid	107-111	thymidylate synthetase	Homo sapiens	56-76
3023902-1	1986	The dCMP deaminase gene (DCD1) of Saccharomyces cerevisiae has been isolated by screening a Sau3A clone bank for complementation of the dUMP auxotrophy exhibited by dcd1 dmp1 haploids.	2'-deoxyuridylic acid	136-140	deoxycytidine monophosphate deaminase	Saccharomyces cerevisiae S288C	25-29
3089276-1	1986	The proposed mechanism of action of thymidylate synthase envisages the formation of a covalent ternary complex of the enzyme with the substrate dUMP and the cofactor 5,10-methylenetetrahydrofolate (CH2H4folate).	2'-deoxyuridylic acid	144-148	thymidylate synthetase	Homo sapiens	36-56
3027327-1	1986	C-4- and C-5-substituted analogues of dUMP were examined as inhibitors of thymidylate synthetase and as topographical probes of its active site by electron spin resonance (ESR).	2'-deoxyuridylic acid	38-42	complement C4A (Rodgers blood group)	Homo sapiens	0-3
3023902-1	1986	The dCMP deaminase gene (DCD1) of Saccharomyces cerevisiae has been isolated by screening a Sau3A clone bank for complementation of the dUMP auxotrophy exhibited by dcd1 dmp1 haploids.	2'-deoxyuridylic acid	136-140	deoxycytidine monophosphate deaminase	Saccharomyces cerevisiae S288C	165-174
3082691-3	1986	The substrate dUMP partially protected thymidylate synthase from inactivation by Agent I, but it did not appreciably protect against inactivation by HTH.	2'-deoxyuridylic acid	14-18	thymidylate synthetase	Homo sapiens	39-59
2415245-12	1986	The activity of thymidylate synthase was measured at a suboptimal concentration of 1 microM and at the optimal concentration of 10 microM deoxyuridine 5"-phosphate.	2'-deoxyuridylic acid	138-163	thymidylate synthetase	Homo sapiens	16-36
6608049-0	1984	Relationship of dUMP and free FdUMP pools to inhibition of thymidylate synthase by 5-fluorouracil.	2'-deoxyuridylic acid	16-20	thymidylate synthase	Mus musculus	59-79
6373725-5	1984	A strain exhibiting an auxotrophic requirement for dUMP was isolated after mutagenesis of a dcd1 tup7 haploid.	2'-deoxyuridylic acid	51-55	deoxycytidine monophosphate deaminase	Saccharomyces cerevisiae S288C	92-96
4081776-0	1985	Investigation of mine and industry dumps in the FRG in relation to a possible release of natural radioactive elements.	2'-deoxyuridylic acid	35-40	FERM, ARH/RhoGEF and pleckstrin domain protein 2	Homo sapiens	48-51
6688493-10	1983	5,8 DideazaisoPteGlu3 bound more tightly to thymidylate synthase than dihydrofolate reductase as indicated by Kis of 0.09 and 0.7 microM when deoxyuridylate and dihydropteroylglutamate, respectively, were the variable substrates.	2'-deoxyuridylic acid	142-156	thymidylate synthetase	Homo sapiens	44-64
6137780-4	1983	The probable explanation for the lack of incorporation of uracil into adult rabbit brain DNA is the presence of a specific, high affinity dUTPase which converts dUTP to dUMP and PP.	2'-deoxyuridylic acid	169-173	Deoxyuridine triphosphatase	Drosophila melanogaster	138-145
6581381-8	1983	These data indicate that human neoplastic cell deoxycytidylate deaminase is a highly regulated allosteric enzyme, which is likely to have a significant influence on cellular dUMP, dCTP and TTP pools.	2'-deoxyuridylic acid	174-178	dCMP deaminase	Homo sapiens	47-72
6449701-1	1980	The biosynthesis of thymine nucleotides in Saccharomyces cerevisiae can be inhibited either by genetic lesions in the structural gene for thymidylate synthetase (TMP1) or by drugs that prevent the methylation of dUMP to dTMP.	2'-deoxyuridylic acid	212-216	thymidylate synthase	Saccharomyces cerevisiae S288C	162-166
6287238-7	1982	In protein extracts from the thymidylate auxotroph (tmp1-6) enzymatic conversion of dUMP to dTMP was barely detectable.	2'-deoxyuridylic acid	84-88	thymidylate synthase	Saccharomyces cerevisiae S288C	52-56
6805512-4	1982	This suggests an inhibitory effect of hydroxyurea on the thymidylate synthase which was proved in experiments in which the conversion of deoxyuridine monophosphate into deoxythymidine monophosphate catalysed by a crude enzyme preparation from P815 cells was inhibited in the presence of hydroxyurea.	2'-deoxyuridylic acid	137-163	thymidylate synthase	Mus musculus	57-77
7279657-7	1981	Our results suggest strongly that uracil-DNA glycosylase has a high degree of selectivity for uracil in dUMP residues located internally in DNA chains and that the recognition of the correct substrate also depends on the residues flanking dUMP being deoxyribonucleotides.	2'-deoxyuridylic acid	104-108	uracil DNA glycosylase	Homo sapiens	34-56
7279657-7	1981	Our results suggest strongly that uracil-DNA glycosylase has a high degree of selectivity for uracil in dUMP residues located internally in DNA chains and that the recognition of the correct substrate also depends on the residues flanking dUMP being deoxyribonucleotides.	2'-deoxyuridylic acid	239-243	uracil DNA glycosylase	Homo sapiens	34-56
7078549-5	1982	In this review, we examine the properties of TSase-dUMP complexes in order to determine if there is an experimental basis for drawing a close analogy between dUMP and FdUMP in their interaction with TSase, and also to evaluate data indicating a potential chemotherapeutic value for TSase-dUMP complexes formed in the presence of folate analogs.	2'-deoxyuridylic acid	51-55	thymidylate synthetase	Homo sapiens	45-50
7078549-5	1982	In this review, we examine the properties of TSase-dUMP complexes in order to determine if there is an experimental basis for drawing a close analogy between dUMP and FdUMP in their interaction with TSase, and also to evaluate data indicating a potential chemotherapeutic value for TSase-dUMP complexes formed in the presence of folate analogs.	2'-deoxyuridylic acid	158-162	thymidylate synthetase	Homo sapiens	45-50
7078549-5	1982	In this review, we examine the properties of TSase-dUMP complexes in order to determine if there is an experimental basis for drawing a close analogy between dUMP and FdUMP in their interaction with TSase, and also to evaluate data indicating a potential chemotherapeutic value for TSase-dUMP complexes formed in the presence of folate analogs.	2'-deoxyuridylic acid	158-162	thymidylate synthetase	Homo sapiens	199-204
7078549-5	1982	In this review, we examine the properties of TSase-dUMP complexes in order to determine if there is an experimental basis for drawing a close analogy between dUMP and FdUMP in their interaction with TSase, and also to evaluate data indicating a potential chemotherapeutic value for TSase-dUMP complexes formed in the presence of folate analogs.	2'-deoxyuridylic acid	158-162	thymidylate synthetase	Homo sapiens	199-204
7078549-5	1982	In this review, we examine the properties of TSase-dUMP complexes in order to determine if there is an experimental basis for drawing a close analogy between dUMP and FdUMP in their interaction with TSase, and also to evaluate data indicating a potential chemotherapeutic value for TSase-dUMP complexes formed in the presence of folate analogs.	2'-deoxyuridylic acid	158-162	thymidylate synthetase	Homo sapiens	45-50
7078549-5	1982	In this review, we examine the properties of TSase-dUMP complexes in order to determine if there is an experimental basis for drawing a close analogy between dUMP and FdUMP in their interaction with TSase, and also to evaluate data indicating a potential chemotherapeutic value for TSase-dUMP complexes formed in the presence of folate analogs.	2'-deoxyuridylic acid	158-162	thymidylate synthetase	Homo sapiens	199-204
7078549-5	1982	In this review, we examine the properties of TSase-dUMP complexes in order to determine if there is an experimental basis for drawing a close analogy between dUMP and FdUMP in their interaction with TSase, and also to evaluate data indicating a potential chemotherapeutic value for TSase-dUMP complexes formed in the presence of folate analogs.	2'-deoxyuridylic acid	158-162	thymidylate synthetase	Homo sapiens	199-204
109088-0	1979	5 (alpha-bromoacetyl)-2"=deoxyuridine 5"-phosphate: a mechanism based affinity label for thymidylate synthetase.	2'-deoxyuridylic acid	25-50	thymidylate synthetase	Homo sapiens	89-111
40612-0	1979	31P NMR studies on the interaction of deoxyuridylate with thymidylate synthase.	2'-deoxyuridylic acid	38-52	thymidylate synthetase	Homo sapiens	58-78
33829766-1	2021	Methylation of 2-deoxyuridine-5"-monophosphate (dUMP) at the C5 position by the obligate dimeric thymidylate synthase (TSase) in the sole de novo biosynthetic pathway to thymidine 5"-monophosphate (dTMP) proceeds by forming a covalent ternary complex with dUMP and cosubstrate 5,10-methylenetetrahydrofolate.	2'-deoxyuridylic acid	15-46	thymidylate synthetase	Homo sapiens	119-124
708736-3	1978	A partially purified DNA polymerase alpha incorporated [3H]dUMP into activated salmon sperm DNA.	2'-deoxyuridylic acid	59-63	DNA polymerase alpha 1, catalytic subunit	Homo sapiens	21-41
699036-2	1978	Small DNA fragments that arise during in vitro DNA synthesis in the presence of dUTP are produced as a result of dUMP incorporation and subsequent post-replication excision repair process initiated by uracil-DNA-glycosylase.	2'-deoxyuridylic acid	113-117	uracil DNA glycosylase	Homo sapiens	201-223
319455-6	1977	These mutant strains have now been found to be defective in deoxyuridinetriphosphate diphosphohydrolase (dUTPase; deoxyuridinetriphosphatase, EC 3.6.1.23), the enzyme that catalyzes the hydrolysis of dUTP to dUMP and PPi.	2'-deoxyuridylic acid	208-212	Deoxyuridine triphosphatase	Drosophila melanogaster	105-112
990190-6	1976	This finding is unexpected in view of the generally accepted indirect role of vitamine B12 in the methylation of deoxyuridine monophosphate to deoxythymidine monophosphate.	2'-deoxyuridylic acid	113-139	NADH:ubiquinone oxidoreductase subunit B3	Homo sapiens	87-90
1277151-15	1976	Deoxyuridine 5"-monophosphate (10(-5) M) effectively protected thymidylate synthetase from heat inactivation in vitro.	2'-deoxyuridylic acid	0-29	thymidylate synthetase	Homo sapiens	63-85
33829766-1	2021	Methylation of 2-deoxyuridine-5"-monophosphate (dUMP) at the C5 position by the obligate dimeric thymidylate synthase (TSase) in the sole de novo biosynthetic pathway to thymidine 5"-monophosphate (dTMP) proceeds by forming a covalent ternary complex with dUMP and cosubstrate 5,10-methylenetetrahydrofolate.	2'-deoxyuridylic acid	15-46	thymidylate synthetase	Homo sapiens	97-117
139127-0	1977	A calorimetric study of the binding of 2"-deoxyuridine-5"-phosphate and 5-fluoro-2"-deoxyuridine-5"-phosphate to thymidylate synthetase.	2'-deoxyuridylic acid	39-67	thymidylate synthetase	Homo sapiens	113-135
786369-5	1976	The carrier adsorbed the enzyme from the crude preparation only in the presence of deoxyuridine 5"-monophosphate (dUMP) in a concentration of 2 X 10(-5) M. The specifically adsorbed thymidylate synthetase was eluted with sacharose-containing buffers in which dUMP was omitted.	2'-deoxyuridylic acid	83-112	thymidylate synthetase	Bos taurus	182-204
786369-5	1976	The carrier adsorbed the enzyme from the crude preparation only in the presence of deoxyuridine 5"-monophosphate (dUMP) in a concentration of 2 X 10(-5) M. The specifically adsorbed thymidylate synthetase was eluted with sacharose-containing buffers in which dUMP was omitted.	2'-deoxyuridylic acid	114-118	thymidylate synthetase	Bos taurus	182-204
786369-5	1976	The carrier adsorbed the enzyme from the crude preparation only in the presence of deoxyuridine 5"-monophosphate (dUMP) in a concentration of 2 X 10(-5) M. The specifically adsorbed thymidylate synthetase was eluted with sacharose-containing buffers in which dUMP was omitted.	2'-deoxyuridylic acid	259-263	thymidylate synthetase	Bos taurus	182-204
33743462-8	2021	The model indicated the flushing of NO3- from the dump should be complete by about 2042 with a peak effluent concentration of NO3- in 2008.	2'-deoxyuridylic acid	50-54	NBL1, DAN family BMP antagonist	Homo sapiens	36-39
33743462-8	2021	The model indicated the flushing of NO3- from the dump should be complete by about 2042 with a peak effluent concentration of NO3- in 2008.	2'-deoxyuridylic acid	50-54	NBL1, DAN family BMP antagonist	Homo sapiens	126-129
33743462-9	2021	The addition of reclamation covers to the model resulted in an immediate decrease in the annual NO3- loading rate but extended the time frame for NO3- release from the dump relative to the no cover case.	2'-deoxyuridylic acid	168-172	NBL1, DAN family BMP antagonist	Homo sapiens	146-149
33997776-3	2020	Past studies have shown that dense subtensors in real-world tensors (e.g., social media, Wikipedia, TCP dumps, etc.)	2'-deoxyuridylic acid	104-109	serine peptidase inhibitor Kazal type 1	Homo sapiens	100-103
33829766-1	2021	Methylation of 2-deoxyuridine-5"-monophosphate (dUMP) at the C5 position by the obligate dimeric thymidylate synthase (TSase) in the sole de novo biosynthetic pathway to thymidine 5"-monophosphate (dTMP) proceeds by forming a covalent ternary complex with dUMP and cosubstrate 5,10-methylenetetrahydrofolate.	2'-deoxyuridylic acid	48-52	thymidylate synthetase	Homo sapiens	97-117
33829766-1	2021	Methylation of 2-deoxyuridine-5"-monophosphate (dUMP) at the C5 position by the obligate dimeric thymidylate synthase (TSase) in the sole de novo biosynthetic pathway to thymidine 5"-monophosphate (dTMP) proceeds by forming a covalent ternary complex with dUMP and cosubstrate 5,10-methylenetetrahydrofolate.	2'-deoxyuridylic acid	48-52	thymidylate synthetase	Homo sapiens	119-124
33829766-1	2021	Methylation of 2-deoxyuridine-5"-monophosphate (dUMP) at the C5 position by the obligate dimeric thymidylate synthase (TSase) in the sole de novo biosynthetic pathway to thymidine 5"-monophosphate (dTMP) proceeds by forming a covalent ternary complex with dUMP and cosubstrate 5,10-methylenetetrahydrofolate.	2'-deoxyuridylic acid	256-260	thymidylate synthetase	Homo sapiens	97-117
33829766-1	2021	Methylation of 2-deoxyuridine-5"-monophosphate (dUMP) at the C5 position by the obligate dimeric thymidylate synthase (TSase) in the sole de novo biosynthetic pathway to thymidine 5"-monophosphate (dTMP) proceeds by forming a covalent ternary complex with dUMP and cosubstrate 5,10-methylenetetrahydrofolate.	2'-deoxyuridylic acid	256-260	thymidylate synthetase	Homo sapiens	119-124
33486616-1	2021	Human thymidylate synthase (hTS) is a 72 kDa homodimeric enzyme responsible for the conversion of deoxyuridine monophosphate (dUMP) to deoxythymidine monophosphate (dTMP), making it the sole source of de novo dTMP in human cells.	2'-deoxyuridylic acid	98-124	thymidylate synthetase	Homo sapiens	6-26
33486616-1	2021	Human thymidylate synthase (hTS) is a 72 kDa homodimeric enzyme responsible for the conversion of deoxyuridine monophosphate (dUMP) to deoxythymidine monophosphate (dTMP), making it the sole source of de novo dTMP in human cells.	2'-deoxyuridylic acid	98-124	APC down-regulated 1	Homo sapiens	28-31
33486616-1	2021	Human thymidylate synthase (hTS) is a 72 kDa homodimeric enzyme responsible for the conversion of deoxyuridine monophosphate (dUMP) to deoxythymidine monophosphate (dTMP), making it the sole source of de novo dTMP in human cells.	2'-deoxyuridylic acid	126-130	thymidylate synthetase	Homo sapiens	6-26
33486616-1	2021	Human thymidylate synthase (hTS) is a 72 kDa homodimeric enzyme responsible for the conversion of deoxyuridine monophosphate (dUMP) to deoxythymidine monophosphate (dTMP), making it the sole source of de novo dTMP in human cells.	2'-deoxyuridylic acid	126-130	APC down-regulated 1	Homo sapiens	28-31
33486616-5	2021	Here, as a preface to detailed NMR characterization, we present backbone amide and ILVM methyl resonance assignments for hTS in apo and dUMP bound forms.	2'-deoxyuridylic acid	136-140	APC down-regulated 1	Homo sapiens	121-124