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Journal articles on the topic 'Deoxyuridine triphosphate nucleotidohydrolase'

Author: Grafiati
Published: 4 June 2021
Last updated: 18 February 2022

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1

Bernier-Villamor, Victor, Ana Camacho, Fernando Hidalgo-Zarco, Juana Pérez, Luis M. Ruiz-Pérez, and Dolores González-Pacanowska. "Characterization of deoxyuridine 5′-triphosphate nucleotidohydrolase fromTrypanosoma cruzi1." FEBS Letters 526, no. 1-3 (2002): 147–50. http://dx.doi.org/10.1016/s0014-5793(02)03158-7.

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2

Nguyen, Corinne, Ganasan Kasinathan, Isabel Leal-Cortijo, et al. "Deoxyuridine Triphosphate Nucleotidohydrolase as a Potential Antiparasitic Drug Target." Journal of Medicinal Chemistry 48, no. 19 (2005): 5942–54. http://dx.doi.org/10.1021/jm050111e.

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3

CAMACHO, Ana, Fernando HIDALGO-ZARCO, Victor BERNIER-VILLAMOR, Luis M. RUIZ-PÉREZ, and Dolores GONZÁLEZ-PACANOWSKA. "Properties of Leishmania major dUTP nucleotidohydrolase, a distinct nucleotide-hydrolysing enzyme in kinetoplastids." Biochemical Journal 346, no. 1 (2000): 163–68. http://dx.doi.org/10.1042/bj3460163.

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We have previously reported the presence, in the parasitic protozoan Leishmania major, of an enzyme involved in controlling intracellular dUTP levels. The gene encoding this enzyme has now been overexpressed in Escherichia coli, and the recombinant enzyme was purified to homogeneity. Biochemical and enzymic analyses of the Leishmania enzyme show that it is a novel nucleotidohydrolase highly specific for deoxyuridine 5ʹ-triphosphate. The enzyme has proved to be a dimer by gel filtration and is able to hydrolyse both dUTP and dUDP quite efficiently, acting as a dUTP nucleotidohydrolase (dUTPase)
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4

Castillo-Acosta, Víctor M., Fernando Aguilar-Pereyra, Daniel García-Caballero, Antonio E. Vidal, Luis M. Ruiz-Pérez, and Dolores González-Pacanowska. "Pyrimidine requirements in deoxyuridine triphosphate nucleotidohydrolase deficient Trypanosoma brucei mutants." Molecular and Biochemical Parasitology 187, no. 1 (2013): 9–13. http://dx.doi.org/10.1016/j.molbiopara.2012.11.003.

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5

Hokari, Shigeru, Masahiro Hasegawa, Masahiko Tanaka, Yoshikatsu Sakagishi, and Goro Kikuchi. "Deoxyuridine Triphosphate Nucleotidohydrolase: Distribution of the Enzyme in Various Rat Tissues." Journal of Biochemistry 104, no. 2 (1988): 211–14. http://dx.doi.org/10.1093/oxfordjournals.jbchem.a122444.

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6

Bajaj, Mamta, and Hideaki Moriyama. "Purification, crystallization and preliminary crystallographic analysis of deoxyuridine triphosphate nucleotidohydrolase fromArabidopsis thaliana." Acta Crystallographica Section F Structural Biology and Crystallization Communications 63, no. 5 (2007): 409–11. http://dx.doi.org/10.1107/s1744309107016004.

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7

HOFFMANN, Ingrid, John WIDSTROM, Michael ZEPPEZAUER, and Per Olof NYMAN. "Overproduction and large-scale preparation of deoxyuridine triphosphate nucleotidohydrolase from Escherichia coli." European Journal of Biochemistry 164, no. 1 (1987): 45–51. http://dx.doi.org/10.1111/j.1432-1033.1987.tb10990.x.

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8

CAMACHO, Ana, Rosalía ARREBOLA, Javier PEÑA-DIAZ, Luis M. RUIZ-PÉREZ, and Dolores GONZÁLEZ-PACANOWSKA. "Description of a novel eukaryotic deoxyuridine 5′-triphosphate nucleotidohydrolase in Leishmania major." Biochemical Journal 325, no. 2 (1997): 441–47. http://dx.doi.org/10.1042/bj3250441.

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A Leishmaniamajor full-length cDNA encoding a functional dUTP nucleotidohydrolase (dUTPase; EC 3.6.1.23) was isolated from a cDNA expression library by genetic complementation of dUTPase deficiency in Escherichiacoli. The cDNA contained an open reading frame that encoded a protein of 269 amino acid residues with a calculated molecular mass of 30.3 kDa. Although eukaryotic dUTPases exhibit extensive similarity and there are five amino acid motifs that are common to all currently known dUTPase enzymes, the sequence of the protozoan gene differs significantly from its eukaryotic counterparts. Non
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9

Persson, Rebecca, Maria Harkiolaki, John McGeehan, and Keith S. Wilson. "Crystallization and preliminary crystallographic analysis of deoxyuridine 5′-triphosphate nucleotidohydrolase fromBacillus subtilis." Acta Crystallographica Section D Biological Crystallography 57, no. 6 (2001): 876–78. http://dx.doi.org/10.1107/s0907444901007727.

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10

Ladner, Robert D., Dean E. McNulty, Steven A. Carr, Gerald D. Roberts, and Salvatore J. Caradonna. "Characterization of Distinct Nuclear and Mitochondrial Forms of Human Deoxyuridine Triphosphate Nucleotidohydrolase." Journal of Biological Chemistry 271, no. 13 (1996): 7745–51. http://dx.doi.org/10.1074/jbc.271.13.7745.

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11

Isaksson, Johan, Esmeralda Woestenenk, Christer Sahlberg, and Tatiana Agback. "Backbone nuclear magnetic resonance assignment of human deoxyuridine 5′-triphosphate nucleotidohydrolase (dUTPase)." Biomolecular NMR Assignments 8, no. 1 (2013): 81–84. http://dx.doi.org/10.1007/s12104-013-9457-7.

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12

Pálinkás, Hajnalka, Gergely Rácz, Zoltán Gál, et al. "CRISPR/Cas9-Mediated Knock-Out of dUTPase in Mice Leads to Early Embryonic Lethality." Biomolecules 9, no. 4 (2019): 136. http://dx.doi.org/10.3390/biom9040136.

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Sanitization of nucleotide pools is essential for genome maintenance. 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. Through its action dUTPase efficiently prevents uracil misincorporation into DNA and at the same time provides dUMP, the substrate for de novo thymidylate biosynthesis. Despite its physiological significance, knock-out models of dUTPase have not yet been investigated in mammals, but only in
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13

Williams, M. V., and A. W. Studebaker. "Down–Regulation of Human Deoxyuridine Triphosphate Nucleotidohydrolase (dUTPase) Using Small Interfering RNA (siRNA)." Nucleosides, Nucleotides and Nucleic Acids 23, no. 8-9 (2004): 1467–70. http://dx.doi.org/10.1081/ncn-200027684.

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14

Han, Byung Woo, Jae Young Lee, Jin Kuk Yang, Byung Il Lee, and Se Won Suh. "Crystallization and preliminary X-ray crystallographic analysis of deoxyuridine triphosphate nucleotidohydrolase fromSaccharomyces cerevisiae." Acta Crystallographica Section D Biological Crystallography 57, no. 8 (2001): 1147–49. http://dx.doi.org/10.1107/s0907444901007909.

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15

Williams, M. V., J. Holliday, and R. Glaser. "Induction of a deoxyuridine triphosphate nucleotidohydrolase activity in Epstein-Barr virus-infected cells." Virology 142, no. 2 (1985): 326–33. http://dx.doi.org/10.1016/0042-6822(85)90341-1.

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16

Hemsworth, Glyn R., Olga V. Moroz, Mark J. Fogg, et al. "The Crystal Structure of the Leishmania major Deoxyuridine Triphosphate Nucleotidohydrolase in Complex with Nucleotide Analogues, dUMP, and Deoxyuridine." Journal of Biological Chemistry 286, no. 18 (2011): 16470–81. http://dx.doi.org/10.1074/jbc.m111.224873.

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Members of the Leishmania genus are the causative agents of the life-threatening disease leishmaniasis. New drugs are being sought due to increasing resistance and adverse side effects with current treatments. The knowledge that dUTPase is an essential enzyme and that the all α-helical dimeric kinetoplastid dUTPases have completely different structures compared with the trimeric β-sheet type dUTPase possessed by most organisms, including humans, make the dimeric enzymes attractive drug targets. Here, we present crystal structures of the Leishmania major dUTPase in complex with substrate analog
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17

Kremmer, E., P. Sommer, and F. A. Grässer. "Epstein-barr virus-encoded deoxyuridine triphosphate nucleotidohydrolase (duTPase): A potential target for drug therapy." Transplantation Proceedings 29, no. 1-2 (1997): 812–14. http://dx.doi.org/10.1016/s0041-1345(96)00144-3.

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18

Lerner, A. Martin, Maria E. Ariza, Marshall Williams, et al. "Antibody to Epstein-Barr Virus Deoxyuridine Triphosphate Nucleotidohydrolase and Deoxyribonucleotide Polymerase in a Chronic Fatigue Syndrome Subset." PLoS ONE 7, no. 11 (2012): e47891. http://dx.doi.org/10.1371/journal.pone.0047891.

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19

Hokari, Shigeru, and Yoshikatsu Sakagishi. "Purification and characterization of deoxyuridine triphosphate nucleotidohydrolase from anemic rat spleen: A trimer composition of the enzyme protein." Archives of Biochemistry and Biophysics 253, no. 2 (1987): 350–56. http://dx.doi.org/10.1016/0003-9861(87)90188-3.

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20

Ladner, Robert D., Steven A. Carr, Michael J. Huddleston, Dean E. McNulty, and Salvatore J. Caradonna. "Identification of a Consensus Cyclin-dependent Kinase Phosphorylation Site Unique to the Nuclear Form of Human Deoxyuridine Triphosphate Nucleotidohydrolase." Journal of Biological Chemistry 271, no. 13 (1996): 7752–57. http://dx.doi.org/10.1074/jbc.271.13.7752.

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21

Vertessy, Beata G. "Flexible glycine rich motif ofEscherichia coli deoxyuridine triphosphate nucleotidohydrolase is important for functional but not for structural integrity of the enzyme." Proteins: Structure, Function, and Genetics 28, no. 4 (1997): 568–79. http://dx.doi.org/10.1002/(sici)1097-0134(199708)28:4<568::aid-prot10>3.0.co;2-e.

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22

Williams, Marshall V., and Deborah S. Parris. "Characterization of a herpes simplex virus type 2 deoxyuridine triphosphate nucleotidohydrolase and mapping of a gene conferring type specificity for the enzyme." Virology 156, no. 2 (1987): 282–92. http://dx.doi.org/10.1016/0042-6822(87)90408-9.

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23

Davison, Craig, Roisin Morelli, Catherine Knowlson, et al. "Targeting nucleotide metabolism enhances the efficacy of anthracyclines and anti-metabolites in triple-negative breast cancer." npj Breast Cancer 7, no. 1 (2021). http://dx.doi.org/10.1038/s41523-021-00245-5.

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AbstractTriple-negative breast cancer (TNBC) remains the most lethal breast cancer subtype with poor response rates to the current chemotherapies and a lack of additional effective treatment options. We have identified deoxyuridine 5′-triphosphate nucleotidohydrolase (dUTPase) as a critical gatekeeper that protects tumour DNA from the genotoxic misincorporation of uracil during treatment with standard chemotherapeutic agents commonly used in the FEC regimen. dUTPase catalyses the hydrolytic dephosphorylation of deoxyuridine triphosphate (dUTP) to deoxyuridine monophosphate (dUMP), providing dU
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24

Williams, M. V., and A. W. Studebaker. "Down?Regulation of Human Deoxyuridine Triphosphate Nucleotidohydrolase (dUTPase) Using Small Interfering RNA (siRNA)." ChemInform 36, no. 12 (2005). http://dx.doi.org/10.1002/chin.200512216.

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25

Moro-Bulnes, Ana, Víctor M. Castillo-Acosta, Maria Valente, et al. "Contribution of Cytidine Deaminase to Thymidylate Biosynthesis in Trypanosoma brucei: Intracellular Localization and Properties of the Enzyme." mSphere 4, no. 4 (2019). http://dx.doi.org/10.1128/msphere.00374-19.

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ABSTRACT Cytidine deaminase (CDA) is a pyrimidine salvage enzyme that catalyzes cytidine and deoxycytidine hydrolytic deamination to yield uridine and deoxyuridine. Here we report the biochemical characterization of Trypanosoma brucei CDA as an enzyme within the tetrameric class of the CDA family that efficiently deaminates cytidine, deoxycytidine, and the nucleoside analogue 5-methyl-2′-deoxycytidine. In line with previous studies, we show that RNA interference (RNAi)-mediated CDA depletion impairs T. brucei proliferation when grown in pyrimidine-deficient medium, while supplementation with t
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26

Chia, Catherine P., Noriko Inoguchi, Kyle C. Varon, Bradley M. Bartholomai, and Hideaki Moriyama. "Mitochondrial localization of Dictyostelium discoideum dUTPase mediated by its N-terminus." BMC Research Notes 13, no. 1 (2020). http://dx.doi.org/10.1186/s13104-019-4879-7.

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Abstract Objective The nuclear and mitochondrial genomes of Dictyostelium discoideum, a unicellular eukaryote, have relatively high A+T-contents of 77.5% and 72.65%, respectively. 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. Results The annotated genome of D. discoideum identifies a gene encoding a polypeptide containing the five conserved motifs of homotrimeric dUTPas
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