{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,31]],"date-time":"2026-07-31T14:18:52Z","timestamp":1785507532572,"version":"3.56.0"},"reference-count":91,"publisher":"Oxford University Press (OUP)","issue":"22","license":[{"start":{"date-parts":[[2016,11,10]],"date-time":"2016-11-10T00:00:00Z","timestamp":1478736000000},"content-version":"vor","delay-in-days":1171,"URL":"http:\/\/creativecommons.org\/licenses\/by\/3.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2013,12,1]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:p>Enzymatic synthesis and hydrolysis of nucleoside phosphate compounds play a key role in various biological pathways, like signal transduction, DNA synthesis and metabolism. Although these processes have been studied extensively, numerous key issues regarding the chemical pathway and atomic movements remain open for many enzymatic reactions. Here, using the Mason\u2013Pfizer monkey retrovirus dUTPase, we study the dUTPase-catalyzed hydrolysis of dUTP, an incorrect DNA building block, to elaborate the mechanistic details at high resolution. Combining mass spectrometry analysis of the dUTPase-catalyzed reaction carried out in and quantum mechanics\/molecular mechanics (QM\/MM) simulation, we show that the nucleophilic attack occurs at the \u03b1-phosphate site. Phosphorus-31 NMR spectroscopy (31P-NMR) analysis confirms the site of attack and shows the capability of dUTPase to cleave the dUTP analogue \u03b1,\u03b2-imido-dUTP, containing the imido linkage usually regarded to be non-hydrolyzable. We present numerous X-ray crystal structures of distinct dUTPase and nucleoside phosphate complexes, which report on the progress of the chemical reaction along the reaction coordinate. The presently used combination of diverse structural methods reveals details of the nucleophilic attack and identifies a novel enzyme\u2013product complex structure.<\/jats:p>","DOI":"10.1093\/nar\/gkt756","type":"journal-article","created":{"date-parts":[[2013,8,28]],"date-time":"2013-08-28T02:02:02Z","timestamp":1377655322000},"page":"10542-10555","source":"Crossref","is-referenced-by-count":18,"title":["Catalytic mechanism of \u03b1-phosphate attack in dUTPase is revealed by X-ray crystallographic snapshots of distinct intermediates, 31P-NMR spectroscopy and reaction path modelling"],"prefix":"10.1093","volume":"41","author":[{"given":"Orsolya","family":"Barab\u00e1s","sequence":"first","affiliation":[{"name":"1 Laboratory of Genome Metabolism, Institute of Enzymology, Research Center for Natural Sciences, Hungarian Academy of Sciences, Budapest H-1113, Hungary, 2Laboratory of Molecular Biology, NIDDK, NIH, Bethesda, MD 20892, USA, 3Structural and Computational Biology Unit, European Molecular Biology Laboratory, Heidelberg D-69117, Germany, 4Laboratory of Structural Chemistry and Biology, Institute of Chemistry, E\u00f6tv\u00f6s Lor\u00e1nd University, Budapest H-1117, Hungary, 5Protein Modelling Group MTA-ELTE, Institute of Chemistry, E\u00f6tv\u00f6s Lor\u00e1nd University, Budapest H-1117, Hungary, 6Department of Chemistry, King's College London, London, SE1 1UL, UK, 7Department of Medical Chemistry, University of Szeged, Hungary, 8Department of Computer Science, E\u00f6tv\u00f6s Lor\u00e1nd University, Budapest, Hungary, 9European Molecular Biology Laboratory, Hamburg Outstation, Hamburg D-22603, Germany and 10Department of Applied Biotechnology and Food Sciences, Budapest University of Technology and Economics, Budapest, Hungary"},{"name":"1 Laboratory of Genome Metabolism, Institute of Enzymology, Research Center for Natural Sciences, Hungarian Academy of Sciences, Budapest H-1113, Hungary, 2Laboratory of Molecular Biology, NIDDK, NIH, Bethesda, MD 20892, USA, 3Structural and Computational Biology Unit, European Molecular Biology Laboratory, Heidelberg D-69117, Germany, 4Laboratory of Structural Chemistry and Biology, Institute of Chemistry, E\u00f6tv\u00f6s Lor\u00e1nd University, Budapest H-1117, Hungary, 5Protein Modelling Group MTA-ELTE, Institute of Chemistry, E\u00f6tv\u00f6s Lor\u00e1nd University, Budapest H-1117, Hungary, 6Department of Chemistry, King's College London, London, SE1 1UL, UK, 7Department of Medical Chemistry, University of Szeged, Hungary, 8Department of Computer Science, E\u00f6tv\u00f6s Lor\u00e1nd University, Budapest, Hungary, 9European Molecular Biology Laboratory, Hamburg Outstation, Hamburg D-22603, Germany and 10Department of Applied Biotechnology and Food Sciences, Budapest University of Technology and Economics, Budapest, Hungary"},{"name":"1 Laboratory of Genome Metabolism, Institute of Enzymology, Research Center for Natural Sciences, Hungarian Academy of Sciences, Budapest H-1113, Hungary, 2Laboratory of Molecular Biology, NIDDK, NIH, Bethesda, MD 20892, USA, 3Structural and Computational Biology Unit, European Molecular Biology Laboratory, Heidelberg D-69117, Germany, 4Laboratory of Structural Chemistry and Biology, Institute of Chemistry, E\u00f6tv\u00f6s Lor\u00e1nd University, Budapest H-1117, Hungary, 5Protein Modelling Group MTA-ELTE, Institute of Chemistry, E\u00f6tv\u00f6s Lor\u00e1nd University, Budapest H-1117, Hungary, 6Department of Chemistry, King's College London, London, SE1 1UL, UK, 7Department of Medical Chemistry, University of Szeged, Hungary, 8Department of Computer Science, E\u00f6tv\u00f6s Lor\u00e1nd University, Budapest, Hungary, 9European Molecular Biology Laboratory, Hamburg Outstation, Hamburg D-22603, Germany and 10Department of Applied Biotechnology and Food Sciences, Budapest University of Technology and Economics, Budapest, Hungary"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Veronika","family":"N\u00e9meth","sequence":"additional","affiliation":[{"name":"1 Laboratory of Genome Metabolism, Institute of Enzymology, Research Center for Natural Sciences, Hungarian Academy of Sciences, Budapest H-1113, Hungary, 2Laboratory of Molecular Biology, NIDDK, NIH, Bethesda, MD 20892, USA, 3Structural and Computational Biology Unit, European Molecular Biology Laboratory, Heidelberg D-69117, Germany, 4Laboratory of Structural Chemistry and Biology, Institute of Chemistry, E\u00f6tv\u00f6s Lor\u00e1nd University, Budapest H-1117, Hungary, 5Protein Modelling Group MTA-ELTE, Institute of Chemistry, E\u00f6tv\u00f6s Lor\u00e1nd University, Budapest H-1117, Hungary, 6Department of Chemistry, King's College London, London, SE1 1UL, UK, 7Department of Medical Chemistry, University of Szeged, Hungary, 8Department of Computer Science, E\u00f6tv\u00f6s Lor\u00e1nd University, Budapest, Hungary, 9European Molecular Biology Laboratory, Hamburg Outstation, Hamburg D-22603, Germany and 10Department of Applied Biotechnology and Food Sciences, Budapest University of Technology and Economics, Budapest, Hungary"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Andrea","family":"Bodor","sequence":"additional","affiliation":[{"name":"1 Laboratory of Genome Metabolism, Institute of Enzymology, Research Center for Natural Sciences, Hungarian Academy of Sciences, Budapest H-1113, Hungary, 2Laboratory of Molecular Biology, NIDDK, NIH, Bethesda, MD 20892, USA, 3Structural and Computational Biology Unit, European Molecular Biology Laboratory, Heidelberg D-69117, Germany, 4Laboratory of Structural Chemistry and Biology, Institute of Chemistry, E\u00f6tv\u00f6s Lor\u00e1nd University, Budapest H-1117, Hungary, 5Protein Modelling Group MTA-ELTE, Institute of Chemistry, E\u00f6tv\u00f6s Lor\u00e1nd University, Budapest H-1117, Hungary, 6Department of Chemistry, King's College London, London, SE1 1UL, UK, 7Department of Medical Chemistry, University of Szeged, Hungary, 8Department of Computer Science, E\u00f6tv\u00f6s Lor\u00e1nd University, Budapest, Hungary, 9European Molecular Biology Laboratory, Hamburg Outstation, Hamburg D-22603, Germany and 10Department of Applied Biotechnology and Food Sciences, Budapest University of Technology and Economics, Budapest, Hungary"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Andr\u00e1s","family":"Perczel","sequence":"additional","affiliation":[{"name":"1 Laboratory of Genome Metabolism, Institute of Enzymology, Research Center for Natural Sciences, Hungarian Academy of Sciences, Budapest H-1113, Hungary, 2Laboratory of Molecular Biology, NIDDK, NIH, Bethesda, MD 20892, USA, 3Structural and Computational Biology Unit, European Molecular Biology Laboratory, Heidelberg D-69117, Germany, 4Laboratory of Structural Chemistry and Biology, Institute of Chemistry, E\u00f6tv\u00f6s Lor\u00e1nd University, Budapest H-1117, Hungary, 5Protein Modelling Group MTA-ELTE, Institute of Chemistry, E\u00f6tv\u00f6s Lor\u00e1nd University, Budapest H-1117, Hungary, 6Department of Chemistry, King's College London, London, SE1 1UL, UK, 7Department of Medical Chemistry, University of Szeged, Hungary, 8Department of Computer Science, E\u00f6tv\u00f6s Lor\u00e1nd University, Budapest, Hungary, 9European Molecular Biology Laboratory, Hamburg Outstation, Hamburg D-22603, Germany and 10Department of Applied Biotechnology and Food Sciences, Budapest University of Technology and Economics, Budapest, Hungary"},{"name":"1 Laboratory of Genome Metabolism, Institute of Enzymology, Research Center for Natural Sciences, Hungarian Academy of Sciences, Budapest H-1113, Hungary, 2Laboratory of Molecular Biology, NIDDK, NIH, Bethesda, MD 20892, USA, 3Structural and Computational Biology Unit, European Molecular Biology Laboratory, Heidelberg D-69117, Germany, 4Laboratory of Structural Chemistry and Biology, Institute of Chemistry, E\u00f6tv\u00f6s Lor\u00e1nd University, Budapest H-1117, Hungary, 5Protein Modelling Group MTA-ELTE, Institute of Chemistry, E\u00f6tv\u00f6s Lor\u00e1nd University, Budapest H-1117, Hungary, 6Department of Chemistry, King's College London, London, SE1 1UL, UK, 7Department of Medical Chemistry, University of Szeged, Hungary, 8Department of Computer Science, E\u00f6tv\u00f6s Lor\u00e1nd University, Budapest, Hungary, 9European Molecular Biology Laboratory, Hamburg Outstation, Hamburg D-22603, Germany and 10Department of Applied Biotechnology and Food Sciences, Budapest University of Technology and Economics, Budapest, Hungary"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Edina","family":"Rosta","sequence":"additional","affiliation":[{"name":"1 Laboratory of Genome Metabolism, Institute of Enzymology, Research Center for Natural Sciences, Hungarian Academy of Sciences, Budapest H-1113, Hungary, 2Laboratory of Molecular Biology, NIDDK, NIH, Bethesda, MD 20892, USA, 3Structural and Computational Biology Unit, European Molecular Biology Laboratory, Heidelberg D-69117, Germany, 4Laboratory of Structural Chemistry and Biology, Institute of Chemistry, E\u00f6tv\u00f6s Lor\u00e1nd University, Budapest H-1117, Hungary, 5Protein Modelling Group MTA-ELTE, Institute of Chemistry, E\u00f6tv\u00f6s Lor\u00e1nd University, Budapest H-1117, Hungary, 6Department of Chemistry, King's College London, London, SE1 1UL, UK, 7Department of Medical Chemistry, University of Szeged, Hungary, 8Department of Computer Science, E\u00f6tv\u00f6s Lor\u00e1nd University, Budapest, Hungary, 9European Molecular Biology Laboratory, Hamburg Outstation, Hamburg D-22603, Germany and 10Department of Applied Biotechnology and Food Sciences, Budapest University of Technology and Economics, Budapest, Hungary"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zolt\u00e1n","family":"Kele","sequence":"additional","affiliation":[{"name":"1 Laboratory of Genome Metabolism, Institute of Enzymology, Research Center for Natural Sciences, Hungarian Academy of Sciences, Budapest H-1113, Hungary, 2Laboratory of Molecular Biology, NIDDK, NIH, Bethesda, MD 20892, USA, 3Structural and Computational Biology Unit, European Molecular Biology Laboratory, Heidelberg D-69117, Germany, 4Laboratory of Structural Chemistry and Biology, Institute of Chemistry, E\u00f6tv\u00f6s Lor\u00e1nd University, Budapest H-1117, Hungary, 5Protein Modelling Group MTA-ELTE, Institute of Chemistry, E\u00f6tv\u00f6s Lor\u00e1nd University, Budapest H-1117, Hungary, 6Department of Chemistry, King's College London, London, SE1 1UL, UK, 7Department of Medical Chemistry, University of Szeged, Hungary, 8Department of Computer Science, E\u00f6tv\u00f6s Lor\u00e1nd University, Budapest, Hungary, 9European Molecular Biology Laboratory, Hamburg Outstation, Hamburg D-22603, Germany and 10Department of Applied Biotechnology and Food Sciences, Budapest University of Technology and Economics, Budapest, Hungary"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Imre","family":"Zagyva","sequence":"additional","affiliation":[{"name":"1 Laboratory of Genome Metabolism, Institute of Enzymology, Research Center for Natural Sciences, Hungarian Academy of Sciences, Budapest H-1113, Hungary, 2Laboratory of Molecular Biology, NIDDK, NIH, Bethesda, MD 20892, USA, 3Structural and Computational Biology Unit, European Molecular Biology Laboratory, Heidelberg D-69117, Germany, 4Laboratory of Structural Chemistry and Biology, Institute of Chemistry, E\u00f6tv\u00f6s Lor\u00e1nd University, Budapest H-1117, Hungary, 5Protein Modelling Group MTA-ELTE, Institute of Chemistry, E\u00f6tv\u00f6s Lor\u00e1nd University, Budapest H-1117, Hungary, 6Department of Chemistry, King's College London, London, SE1 1UL, UK, 7Department of Medical Chemistry, University of Szeged, Hungary, 8Department of Computer Science, E\u00f6tv\u00f6s Lor\u00e1nd University, Budapest, Hungary, 9European Molecular Biology Laboratory, Hamburg Outstation, Hamburg D-22603, Germany and 10Department of Applied Biotechnology and Food Sciences, Budapest University of Technology and Economics, Budapest, Hungary"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zolt\u00e1n","family":"Szabadka","sequence":"additional","affiliation":[{"name":"1 Laboratory of Genome Metabolism, Institute of Enzymology, Research Center for Natural Sciences, Hungarian Academy of Sciences, Budapest H-1113, Hungary, 2Laboratory of Molecular Biology, NIDDK, NIH, Bethesda, MD 20892, USA, 3Structural and Computational Biology Unit, European Molecular Biology Laboratory, Heidelberg D-69117, Germany, 4Laboratory of Structural Chemistry and Biology, Institute of Chemistry, E\u00f6tv\u00f6s Lor\u00e1nd University, Budapest H-1117, Hungary, 5Protein Modelling Group MTA-ELTE, Institute of Chemistry, E\u00f6tv\u00f6s Lor\u00e1nd University, Budapest H-1117, Hungary, 6Department of Chemistry, King's College London, London, SE1 1UL, UK, 7Department of Medical Chemistry, University of Szeged, Hungary, 8Department of Computer Science, E\u00f6tv\u00f6s Lor\u00e1nd University, Budapest, Hungary, 9European Molecular Biology Laboratory, Hamburg Outstation, Hamburg D-22603, Germany and 10Department of Applied Biotechnology and Food Sciences, Budapest University of Technology and Economics, Budapest, Hungary"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Vince I.","family":"Grolmusz","sequence":"additional","affiliation":[{"name":"1 Laboratory of Genome Metabolism, Institute of Enzymology, Research Center for Natural Sciences, Hungarian Academy of Sciences, Budapest H-1113, Hungary, 2Laboratory of Molecular Biology, NIDDK, NIH, Bethesda, MD 20892, USA, 3Structural and Computational Biology Unit, European Molecular Biology Laboratory, Heidelberg D-69117, Germany, 4Laboratory of Structural Chemistry and Biology, Institute of Chemistry, E\u00f6tv\u00f6s Lor\u00e1nd University, Budapest H-1117, Hungary, 5Protein Modelling Group MTA-ELTE, Institute of Chemistry, E\u00f6tv\u00f6s Lor\u00e1nd University, Budapest H-1117, Hungary, 6Department of Chemistry, King's College London, London, SE1 1UL, UK, 7Department of Medical Chemistry, University of Szeged, Hungary, 8Department of Computer Science, E\u00f6tv\u00f6s Lor\u00e1nd University, Budapest, Hungary, 9European Molecular Biology Laboratory, Hamburg Outstation, Hamburg D-22603, Germany and 10Department of Applied Biotechnology and Food Sciences, Budapest University of Technology and Economics, Budapest, Hungary"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Matthias","family":"Wilmanns","sequence":"additional","affiliation":[{"name":"1 Laboratory of Genome Metabolism, Institute of Enzymology, Research Center for Natural Sciences, Hungarian Academy of Sciences, Budapest H-1113, Hungary, 2Laboratory of Molecular Biology, NIDDK, NIH, Bethesda, MD 20892, USA, 3Structural and Computational Biology Unit, European Molecular Biology Laboratory, Heidelberg D-69117, Germany, 4Laboratory of Structural Chemistry and Biology, Institute of Chemistry, E\u00f6tv\u00f6s Lor\u00e1nd University, Budapest H-1117, Hungary, 5Protein Modelling Group MTA-ELTE, Institute of Chemistry, E\u00f6tv\u00f6s Lor\u00e1nd University, Budapest H-1117, Hungary, 6Department of Chemistry, King's College London, London, SE1 1UL, UK, 7Department of Medical Chemistry, University of Szeged, Hungary, 8Department of Computer Science, E\u00f6tv\u00f6s Lor\u00e1nd University, Budapest, Hungary, 9European Molecular Biology Laboratory, Hamburg Outstation, Hamburg D-22603, Germany and 10Department of Applied Biotechnology and Food Sciences, Budapest University of Technology and Economics, Budapest, Hungary"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Be\u00e1ta G.","family":"V\u00e9rtessy","sequence":"additional","affiliation":[{"name":"1 Laboratory of Genome Metabolism, Institute of Enzymology, Research Center for Natural Sciences, Hungarian Academy of Sciences, Budapest H-1113, Hungary, 2Laboratory of Molecular Biology, NIDDK, NIH, Bethesda, MD 20892, USA, 3Structural and Computational Biology Unit, European Molecular Biology Laboratory, Heidelberg D-69117, Germany, 4Laboratory of Structural Chemistry and Biology, Institute of Chemistry, E\u00f6tv\u00f6s Lor\u00e1nd University, Budapest H-1117, Hungary, 5Protein Modelling Group MTA-ELTE, Institute of Chemistry, E\u00f6tv\u00f6s Lor\u00e1nd University, Budapest H-1117, Hungary, 6Department of Chemistry, King's College London, London, SE1 1UL, UK, 7Department of Medical Chemistry, University of Szeged, Hungary, 8Department of Computer Science, E\u00f6tv\u00f6s Lor\u00e1nd University, Budapest, Hungary, 9European Molecular Biology Laboratory, Hamburg Outstation, Hamburg D-22603, Germany and 10Department of Applied Biotechnology and Food Sciences, Budapest University of Technology and Economics, Budapest, Hungary"},{"name":"1 Laboratory of Genome Metabolism, Institute of Enzymology, Research Center for Natural Sciences, Hungarian Academy of Sciences, Budapest H-1113, Hungary, 2Laboratory of Molecular Biology, NIDDK, NIH, Bethesda, MD 20892, USA, 3Structural and Computational Biology Unit, European Molecular Biology Laboratory, Heidelberg D-69117, Germany, 4Laboratory of Structural Chemistry and Biology, Institute of Chemistry, E\u00f6tv\u00f6s Lor\u00e1nd University, Budapest H-1117, Hungary, 5Protein Modelling Group MTA-ELTE, Institute of Chemistry, E\u00f6tv\u00f6s Lor\u00e1nd University, Budapest H-1117, Hungary, 6Department of Chemistry, King's College London, London, SE1 1UL, UK, 7Department of Medical Chemistry, University of Szeged, Hungary, 8Department of Computer Science, E\u00f6tv\u00f6s Lor\u00e1nd University, Budapest, Hungary, 9European Molecular Biology Laboratory, Hamburg Outstation, Hamburg D-22603, Germany and 10Department of Applied Biotechnology and Food Sciences, Budapest University of Technology and Economics, Budapest, Hungary"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2013,8,27]]},"reference":[{"key":"2024100114401827100_gkt756-B1","volume-title":"Mechanistic Principles of Enzyme-catalyzed Cleavage of Phosphodiester Bonds","author":"Gerlt","year":"1993"},{"key":"2024100114401827100_gkt756-B2","doi-asserted-by":"crossref","first-page":"938","DOI":"10.1021\/ar000058i","article-title":"The depth of chemical time and the power of enzymes as catalysts","volume":"34","author":"Wolfenden","year":"2001","journal-title":"Acc. Chem. Res."},{"key":"2024100114401827100_gkt756-B3","doi-asserted-by":"crossref","first-page":"485","DOI":"10.1021\/ar9500877","article-title":"Structure and nuclease activity of simple dinuclear metal complexes: quantitative dissection of the role of metal ions","volume":"32","author":"Nicholas","year":"1999","journal-title":"Acc. Chem. Res"},{"key":"2024100114401827100_gkt756-B4","doi-asserted-by":"crossref","first-page":"196","DOI":"10.1038\/nature11181","article-title":"Watching DNA polymerase eta make a phosphodiester bond","volume":"487","author":"Nakamura","year":"2012","journal-title":"Nature"},{"key":"2024100114401827100_gkt756-B5","doi-asserted-by":"crossref","first-page":"97","DOI":"10.1021\/ar800114w","article-title":"Keeping uracil out of DNA: physiological role, structure and catalytic mechanism of dUTPases","volume":"42","author":"Vertessy","year":"2009","journal-title":"Acc. Chem. Res."},{"key":"2024100114401827100_gkt756-B6","doi-asserted-by":"crossref","first-page":"5","DOI":"10.1111\/j.1365-2958.2005.04950.x","article-title":"House cleaning, a part of good housekeeping","volume":"59","author":"Galperin","year":"2006","journal-title":"Mol. Microbiol."},{"key":"2024100114401827100_gkt756-B7","doi-asserted-by":"crossref","first-page":"986","DOI":"10.1016\/j.dnarep.2012.09.007","article-title":"Increased uracil insertion in DNA is cytotoxic and increases the frequency of mutation, double strand break formation and VSG switching in Trypanosoma brucei","volume":"11","author":"Castillo-Acosta","year":"2012","journal-title":"DNA Repair (Amst.)"},{"key":"2024100114401827100_gkt756-B8","doi-asserted-by":"crossref","first-page":"183","DOI":"10.1016\/j.drup.2012.07.002","article-title":"Antifolates in cancer therapy: structure, activity and mechanisms of drug resistance","volume":"15","author":"Gonen","year":"2012","journal-title":"Drug Resist. 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Chem."},{"key":"2024100114401827100_gkt756-B11","doi-asserted-by":"crossref","first-page":"439","DOI":"10.1124\/mol.112.082321","article-title":"Pyrimidine salvage in trypanosoma brucei bloodstream forms and the trypanocidal action of halogenated pyrimidines","volume":"83","author":"Ali","year":"2013","journal-title":"Mol. Pharmacol."},{"key":"2024100114401827100_gkt756-B12","doi-asserted-by":"crossref","first-page":"1407","DOI":"10.1016\/j.dnarep.2006.06.009","article-title":"Quantitative determination of uracil residues in Escherichia coli DNA: Contribution of ung, dug, and dut genes to uracil avoidance","volume":"5","author":"Lari","year":"2006","journal-title":"DNA Repair (Amst)"},{"key":"2024100114401827100_gkt756-B13","doi-asserted-by":"crossref","first-page":"409","DOI":"10.1007\/978-1-59259-725-3_20","volume-title":"Anticancer Development Guide: Antifolate Drugs in Cancer Therapy","author":"Aherne","year":"1999"},{"key":"2024100114401827100_gkt756-B14","doi-asserted-by":"crossref","first-page":"5483","DOI":"10.1021\/jm300416h","article-title":"Discovery of highly potent human deoxyuridine triphosphatase inhibitors based on the conformation restriction strategy","volume":"55","author":"Miyahara","year":"2012","journal-title":"J. Med. Chem."},{"key":"2024100114401827100_gkt756-B15","doi-asserted-by":"crossref","first-page":"2970","DOI":"10.1021\/jm201628y","article-title":"Discovery of a novel class of potent human deoxyuridine triphosphatase inhibitors remarkably enhancing the antitumor activity of thymidylate synthase inhibitors","volume":"55","author":"Miyahara","year":"2012","journal-title":"J. Med. Chem."},{"key":"2024100114401827100_gkt756-B16","doi-asserted-by":"crossref","first-page":"616","DOI":"10.1158\/1535-7163.MCT-11-0781","article-title":"Inhibition of dUTPase induces synthetic lethality with thymidylate synthase-targeted therapies in non-small cell lung cancer","volume":"11","author":"Wilson","year":"2012","journal-title":"Mol. Cancer Ther."},{"key":"2024100114401827100_gkt756-B17","doi-asserted-by":"crossref","first-page":"3029","DOI":"10.1158\/1535-7163.MCT-08-0280","article-title":"Novel opportunities for thymidylate metabolism as a therapeutic target","volume":"7","author":"Wilson","year":"2008","journal-title":"Mol. Cancer Ther."},{"key":"2024100114401827100_gkt756-B18","doi-asserted-by":"crossref","first-page":"369","DOI":"10.1080\/15257770.2011.582849","article-title":"Cellular response to efficient dUTPase RNAi silencing in stable HeLa cell lines perturbs expression levels of genes involved in thymidylate metabolism","volume":"30","author":"Merenyi","year":"2011","journal-title":"Nucleosides Nucleotides Nucleic Acids"},{"key":"2024100114401827100_gkt756-B19","doi-asserted-by":"crossref","first-page":"1816","DOI":"10.1002\/cmdc.201100255","article-title":"Design, synthesis, and evaluation of 5\u2032-diphenyl nucleoside analogues as inhibitors of the Plasmodium falciparum dUTPase","volume":"6","author":"Hampton","year":"2011","journal-title":"Chem. Med. Chem."},{"key":"2024100114401827100_gkt756-B20","doi-asserted-by":"crossref","first-page":"936","DOI":"10.1016\/j.bbapap.2007.04.013","article-title":"Plasmodium falciparum dUTPase: studies on protein stability and binding of deoxyuridine derivatives","volume":"1774","author":"Quesada-Soriano","year":"2007","journal-title":"Biochim. Biophys. Acta"},{"key":"2024100114401827100_gkt756-B21","doi-asserted-by":"crossref","first-page":"329","DOI":"10.1016\/j.str.2004.11.015","article-title":"dUTPase as a platform for antimalarial drug design: structural basis for the selectivity of a class of nucleoside inhibitors","volume":"13","author":"Whittingham","year":"2005","journal-title":"Structure"},{"key":"2024100114401827100_gkt756-B22","doi-asserted-by":"crossref","first-page":"e37461","DOI":"10.1371\/journal.pone.0037461","article-title":"The dUTPase enzyme is essential in Mycobacterium smegmatis","volume":"7","author":"Pecsi","year":"2012","journal-title":"PLoS One"},{"key":"2024100114401827100_gkt756-B23","doi-asserted-by":"crossref","first-page":"e1002738","DOI":"10.1371\/journal.pgen.1002738","article-title":"Uracil-containing DNA in Drosophila: stability, stage-specific accumulation, and developmental involvement","volume":"8","author":"Muha","year":"2012","journal-title":"PLoS Genet."},{"key":"2024100114401827100_gkt756-B24","doi-asserted-by":"crossref","DOI":"10.1021\/bc200221t","article-title":"Enhanced cellular uptake of a new, in silico identified antitubercular candidate by peptide conjugation","author":"Horvati","year":"2012","journal-title":"Bioconjug. Chem."},{"key":"2024100114401827100_gkt756-B25","doi-asserted-by":"crossref","first-page":"8","DOI":"10.1016\/j.bbrc.2008.05.130","article-title":"Active site of mycobacterial dUTPase: structural characteristics and a built-in sensor","volume":"373","author":"Varga","year":"2008","journal-title":"Biochem. Biophys. Res. 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