References
- Marshall BJ, Warren JR. Unidentified curved bacilli in the stomach of patients with gastritis and peptic ulceration. Lancet 1984;1:1311–5.
- Makola D, Peura DA, Crowe SE. Helicobacter pylori infection and related gastrointestinal diseases. J Clin Gastroenterol 2007;41:548–58.
- Robinson K, Atherton JC. The spectrum of Helicobacter-mediated diseases. Annu Rev Pathol Mech Dis 2021;16:123–44.
- Falco MDE, Lucariello A, Iaquinto S, et al. Molecular mechanisms of Helicobacter pylori pathogenesis. J Cell Physiol 2015;230:1702–7.
- Cover TL. Helicobacter pylori diversity and gastric cancer risk. mBio 2016;7:1–9.
- Schistosomes, liver flukes and Helicobacter pylori. IARC Working Group on the Evaluation of Carcinogenic Risks to Humans. Lyon, 7–14 June 1994. IARC Monogr Eval Carcinog Risks Hum 1994;61:1–241.
- Georgopoulos S, Papastergiou V. An update on current and advancing pharmacotherapy options for the treatment of H. pylori infection. Expert Opin Pharmacother 2021;22:729–41.
- De Freitas LC. WHO (2017) Global priority list of antibiotic-resistant bacteria to guide research, discovery, and development of new antibiotics. Cad Pesqui 2013;43:348–65.
- Roszczenko-Jasińska P, Wojtyś MI, Jagusztyn-Krynicka EK. Helicobacter pylori treatment in the post-antibiotics era-searching for new drug targets. Appl Microbiol Biotechnol 2020;104:9891–905.
- Campestre C, De Luca V, Carradori S, et al. Carbonic anhydrases: new perspectives on protein functional role and inhibition in Helicobacter pylori. Front Microbiol 2021;12:1–12.
- Ullman B, Carter D. Hypoxanthine-guanine phosphoribosyltransferase as a therapeutic target in protozoal infections. Infect Agents Dis 1995;4:29–40.
- El Kouni MH. Potential chemotherapeutic targets in the purine metabolism of parasites. Pharmacol Ther 2003;99:283–309.
- de Koning HP, Bridges DJ, Burchmore RJS. Purine and pyrimidine transport in pathogenic protozoa: from biology to therapy. FEMS Microbiol Rev 2005;29:987–1020.
- Hyde JE. Fine targeting of purine salvage in cryptosporidium parasites. Trends Parasitol 2008;24:336–9.
- Berg M, Van der Veken P, Goeminne A, et al. Inhibitors of the purine salvage pathway: a valuable approach for antiprotozoal chemotherapy? Curr Med Chem 2010;17:2456–81.
- Evans GB, Tyler PC, Schramm VL. Immucillins in infectious diseases. ACS Infect Dis 2018;4:107–17.
- Liechti G, Goldberg JB. Helicobacter pylori relies primarily on the purine salvage pathway for purine nucleotide biosynthesis. J Bacteriol 2012;194:839–54.
- Il’icheva IA, Polyakov KM, Mikhailov SN. Strained conformations of nucleosides in active sites of nucleoside phosphorylases. Biomolecules 2020;10:552.
- Koellner G, Luić M, Shugar D, et al. Crystal structure of the ternary complex of E. coli purine nucleoside phosphorylase with formycin B, a structural analogue of the substrate inosine, and phosphate (sulphate) at 2.1 A resolution. J Mol Biol 1998;280:153–66.
- Narczyk M, Bertoša B, Papa L, et al. Helicobacter pylori purine nucleoside phosphorylase shows new distribution patterns of open and closed active site conformations and unusual biochemical features. FEBS J 2018;285:1305–25.
- Štefanić Z, Mikleušević G, Luić M, et al. Structural characterization of purine nucleoside phosphorylase from human pathogen Helicobacter pylori. Int J Biol Macromol 2017;101:518–26.
- Bzowska A, Magnowska L, Kazimierczuk Z. Synthesis of 6-aryloxy- and 6-arylalkoxy-2-chloropurines and their interactions with purine nucleoside phosphorylase from Escherichia coli. Z Naturforsch C 1999;54:1055–67.
- Jones JW, Robins RK. Purine nucleosides. III. Methylation studies of certain naturally occurring purine nucleosides. J Am Chem Soc 1963;85:193–201.
- Schrader WP, Stacy AR, Pollara B. Purification of human erythrocyte adenosine deaminase by affinity column chromatography. J Biol Chem 1976;251:4026–32.
- Bzowska A, Kazimierczuk Z, Seela F. 7-deazapurine 2'-deoxyribofuranosides are noncleavable competitive inhibitors of Escherichia coli purine nucleoside phosphorylase (PNP). Acta Biochim Pol 1998;45:755–68.
- Bzowska A, Kazimierczuk Z. 2-Chloro-2'-deoxyadenosine (cladribine) and its analogues are good substrates and potent selective inhibitors of Escherichia coli purine-nucleoside phosphorylase. Eur J Biochem 1995;233:886–90.
- Kalckar HM, Shafran W. Differential spectrophotometry of purine compounds by means of specific enzymes; Determination of hydroxypurine compounds. J Biol Chem 1947;167:429–43.
- Kulikowska E, Bzowska A, Wierzchowski J, Shugar D. Properties of two unusual, and fluorescent, substrates of purine-nucleoside phosphorylase: 7-methylguanosine and 7-methylinosine. Biochim Biophys Acta (BBA)/Protein Struct Mol 1986;874:355–63.
- Bzowska A, Kulikowska E, Shugar D. Properties of purine nucleoside phosphorylase (PNP) of mammalian and bacterial origin. Z Naturforsch C J Biosci 1990;45:59–70.
- Segel IH, Enzyme kinetics: behavior and analysis of rapid equilibrium and steady-state enzyme systems. Vol. 2. New York, NY: John Wiley Sons; 1993.
- Copeland RA, Enzymes. New York, NY: John Wiley & Sons, Inc.; 2000.
- Irie Y, Tateda K, Matsumoto T, et al. Antibiotic MICs and short time-killing against Helicobacter pylori: therapeutic potential of kanamycin. J Antimicrob Chemother 1997;40:235–40.
- Chowers MY, Keller N, Tal R, et al. Human gastrin: a Helicobacter pylori-specific growth factor. Gastroenterology 1999;117:1113–8.
- Knezevic P, Aleksic Sabo V, Simin N, et al. A colorimetric broth microdilution method for assessment of Helicobacter pylori sensitivity to antimicrobial agents. J Pharm Biomed Anal 2018;152:271–8.
- Krzyżek P, Franiczek R, Krzyżanowska B, et al. In vitro activity of 3-bromopyruvate, an anticancer compound, against antibiotic-susceptible and antibiotic-resistant Helicobacter pylori strains. Cancers (Basel) 2019;11:229.
- EUCAST. Breakpoint tables for interpretation of MICs and zone diameters. Version 11.0, 2021. Available from: http://www.eucast.org.
- Pillai SK, Eliopoulos GM, Moellering RC. Antimicrobial combinations. Antibiotics in laboratory medicine. Philadelphia, PA: Wolters Kluwer Health; 2005:365–409.
- Kabsch W. Xds. Acta Crystallogr D Biol Crystallogr 2010;66:125–32.
- Vagin A, Teplyakov A. MOLREP: an automated program for molecular replacement. J Appl Crystallogr 1997;30:1022–5.
- Liebschner D, Afonine PV, Baker ML, Bunkóczi G, et al. Macromolecular structure determination using X-rays, neutrons and electrons: recent developments in phenix. Acta Crystallogr D Struct Biol 2019;75:861–77.
- Schrödinger LLC. The {PyMOL} molecular graphics system, Version∼1.8. 2015.
- Mikleušević G, Štefanić Z, Narczyk M, et al. Validation of the catalytic mechanism of Escherichia coli purine nucleoside phosphorylase by structural and kinetic studies. Biochimie 2011;93:1610–22.
- Luić M, Štefanić Z. Can crystal symmetry and packing influence the active site conformation of homohexameric purine nucleoside phosphorylases? Croat Chem Acta 2016;89:197–202.