Lindahl T. 1993. Instability and decay of the primary structure of DNA. Nature. 362, 709–715.
Article CAS PubMed Google Scholar
Friedberg E.C., Walker G.C., Siede W., Wood R.D., Schultz R.A., Ellenberger T. 2006. DNA Repair and Mutagenesis.Washington, D.C.: ASM Press.
Berger S.H., Pittman D.L., Wyatt M.D. 2008. Uracil in DNA: consequences for carcinogenesis and chemotherapy. Biochem. Pharmacol. 76, 697–706.
Article CAS PubMed PubMed Central Google Scholar
Kavli B., Slupphaug G., Krokan H.E. 2021. Genomic uracil in biology, immunity and cancer. In DNA Damage, DNA Repair and Disease. Dizdaroglu, M., Lloyd, R.S., Eds. London: Royal Soc. Chem., pp. 220–248.
Persson R., Cedergren-Zeppezauer E.S., Wilson K.S. 2001. Homotrimeric dUTPases: structural solutions for specific recognition and hydrolysis of dUTP. Curr. Protein Pept. Sci. 2, 287–300.
Article CAS PubMed Google Scholar
Vértessy B.G., Tóth J. 2009. Keeping uracil out of DNA: physiological role, structure and catalytic mechanism of dUTPases. Acc. Chem. Res. 42, 97–106.
Article PubMed PubMed Central Google Scholar
Kouzminova E.A., Kuzminov A. 2004. Chromosomal fragmentation in dUTPase-deficient mutants of Escherichia coli and its recombinational repair. Mol. Microbiol. 51, 1279–1295.
Article CAS PubMed Google Scholar
Kouzminova E.A., Kuzminov A. 2006. Fragmentation of replicating chromosomes triggered by uracil in DNA. J. Mol. Biol. 355, 20–33.
Article CAS PubMed Google Scholar
Ting H., Kouzminova E.A., Kuzminov A. 2008. Synthetic lethality with the dut defect in Escherichia coli reveals layers of DNA damage of increasing complexity due to uracil incorporation. J. Bacteriol. 190, 5841–5854.
Article CAS PubMed PubMed Central Google Scholar
Pálinkás H.L., Rácz G.A., Gál Z., Hoffmann O.I., Tihanyi G., Róna G., Gócza E., Hiripi L., Vértessy B.G. 2019. CRISPR/Cas9-mediated knock-out of dUTPase in mice leads to early embryonic lethality. Biomolecules. 9, 136.
Article PubMed PubMed Central Google Scholar
Cedergren-Zeppezauer E.S., Larsson G., Nyman P.O., Dauter Z., Wilson K.S. 1992. Crystal structure of a dUTPase. Nature. 355, 740–743.
Article CAS PubMed Google Scholar
Larsson G., Svensson L.A., Nyman P.O. 1996. Crystal structure of the Escherichia coli dUTPase in complex with a substrate analogue (dUDP). Nat. Struct. Biol. 3, 532–538.
Article CAS PubMed Google Scholar
Mol C.D., Harris J.M., McIntosh E.M., Tainer J.A. 1996. Human dUTP pyrophosphatase: uracil recognition by a β hairpin and active sites formed by three separate subunits. Structure. 4, 1077–1092.
Article CAS PubMed Google Scholar
González A., Larsson G., Persson R., Cedergren-Zeppezauer E. 2001. Atomic resolution structure of Escherichia coli dUTPase determined ab initio. Acta Crystallogr. D Biol. Crystallogr. 57, 767–774.
Barabás O., Pongrácz V., Kovári J., Wilmanns M., Vértessy B.G. 2004. Structural insights into the catalytic mechanism of phosphate ester hydrolysis by dUTPase. J. Biol. Chem. 279, 42907–42915.
Varga B., Barabás O., Kovári J., Tóth J., Hunyadi-Gulyás É., Klement É., Medzihradszky K.F., Tölgyesi F., Fidy J., Vértessy B.G. 2007. Active site closure facilitates juxtaposition of reactant atoms for initiation of catalysis by human dUTPase. FEBS Lett. 581, 4783–4788.
Article CAS PubMed Google Scholar
Kovári J., Barabás O., Varga B., Békési A., Tölgyesi F., Fidy J., Nagy J., Vértessy B.G. 2008. Methylene substitution at the α–β bridging position within the phosphate chain of dUDP profoundly perturbs ligand accommodation into the dUTPase active site. Proteins. 71, 308–319.
Benedek A., Temesváry-Kis F., Khatanbaatar T., Leveles I., Surányi É.V., Szabó J.E., Wunderlich L., Vértessy B.G. 2019. The role of a key amino acid position in species-specific proteinaceous dUTPase inhibition. Biomolecules. 9, 221.
Article CAS PubMed PubMed Central Google Scholar
Larsson G., Nyman P.O., Kvassman J.-O. 1996. Kinetic characterization of dUTPase from Escherichia coli. J. Biol. Chem. 271, 24010–24016.
Article CAS PubMed Google Scholar
Mustafi D., Bekesi A., Vertessy B.G., Makinen M.W. 2003. Catalytic and structural role of the metal ion in dUTP pyrophosphatase. Proc. Natl Acad. Sci. U. S. A. 100, 5670–5675.
Article CAS PubMed PubMed Central Google Scholar
Fiser A., Vértessy B.G. 2000. Altered subunit communication in subfamilies of trimeric dUTPases. Biochem. Biophys. Res. Commun. 279, 534–542.
Article CAS PubMed Google Scholar
Arkin M.R., Wells J.A. 2004. Small-molecule inhibitors of protein–protein interactions: Progressing towards the dream. Nat. Rev. Drug Discov. 3, 301–317.
Article CAS PubMed Google Scholar
Petta I., Lievens S., Libert C., Tavernier J., De Bosscher K. 2016. Modulation of protein–protein interactions for the development of novel therapeutics. Mol. Ther. 24, 707–718.
Article CAS PubMed PubMed Central Google Scholar
Senisterra G., Chau I., Vedadi M. 2012. Thermal denaturation assays in chemical biology. Assay Drug Dev. Technol. 10, 128–136.
Article CAS PubMed Google Scholar
Magnusson A.O., Szekrenyi A., Joosten H.-J., Finnigan J., Charnock S., Fessner W.-D. 2019. nanoDSF as screening tool for enzyme libraries and biotechnology development. FEBS J. 286, 184–204.
Article CAS PubMed Google Scholar
Kotov V., Mlynek G., Vesper O., Pletzer M., Wald J., Teixeira-Duarte C.M., Celia H., Garcia-Alai M., Nussberger S., Buchanan S.K., Morais-Cabral J.H., Loew C., Djinovic-Carugo K., Marlovits T.C. 2021. In-depth interrogation of protein thermal unfolding data with MoltenProt. Protein Sci. 30, 201–217.
Article CAS PubMed Google Scholar
Eftink M.R. 1994. The use of fluorescence methods to monitor unfolding transitions in proteins. Biophys. J. 66, 482–501.
Article CAS PubMed PubMed Central Google Scholar
Krissinel E., Henrick K. 2007. Inference of macromolecular assemblies from crystalline state. J. Mol. Biol. 372, 774–797.
Article CAS PubMed Google Scholar
Fraczkiewicz R., Braun W. 1998. Exact and efficient analytical calculation of the accessible surface areas and their gradients for macromolecules. J. Comput. Chem. 19, 319–333.
Vivian J.T., Callis P.R. 2001. Mechanisms of tryptophan fluorescence shifts in proteins. Biophys. J. 80, 2093–2109.
Article CAS PubMed PubMed Central Google Scholar
Yoshikawa H., Hirano A., Arakawa T., Shiraki K. 2012. Effects of alcohol on the solubility and structure of native and disulfide-modified bovine serum albumin. Int. J. Biol. Macromol. 50, 1286–1291.
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