PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 8611496-1 1996 Thymidylate synthase (TS) methylates only dUMP, not dCMP. 2'-deoxyuridylic acid 42-46 thymidylate synthetase Homo sapiens 0-20 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 126-130 thymidylate synthetase Homo sapiens 6-26 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 45-63 thymidylate synthetase Homo sapiens 0-5 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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