Collection of Czechoslovak Chemical Communications - digital archive 

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• Kamel Sarah, Thiele Isabel, Neubauer Peter, Wagner Anke: Thermophilic nucleoside phosphorylases: Their properties, characteristics and applications. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 2020, 1868, 140304. <https://doi.org/10.1016/j.bbapap.2019.140304>
• Stachelska-Wierzchowska Alicja, Wierzchowski Jacek, Górka Michał, Bzowska Agnieszka, Stolarski Ryszard, Wielgus-Kutrowska Beata: Tricyclic Nucleobase Analogs and Their Ribosides as Substrates and Inhibitors of Purine-Nucleoside Phosphorylases III. Aminopurine Derivatives. Molecules 2020, 25, 681. <https://doi.org/10.3390/molecules25030681>
• Timofeev Vladimir I., Zhukhlistova Nadezhda E., Abramchik Yuliya A., Fateev Ilya I., Kostromina Maria A., Muravieva Tatiana I., Esipov Roman S., Kuranova Inna P.: Crystal structure of Escherichia coli purine nucleoside phosphorylase in complex with 7-deazahypoxanthine. Acta Crystallogr F Struct Biol Commun 2018, 74, 355. <https://doi.org/10.1107/S2053230X18006337>
• Fateev Ilja V., Kharitonova Maria I., Antonov Konstantin V., Konstantinova Irina D., Stepanenko Vasily N., Esipov Roman S., Seela Frank, Temburnikar Kartik W., Seley‐Radtke Katherine L., Stepchenko Vladimir A., Sokolov Yuri A., Miroshnikov Anatoly I., Mikhailopulo Igor A.: Recognition of Artificial Nucleobases by E. coli Purine Nucleoside Phosphorylase versus its Ser90Ala Mutant in the Synthesis of Base‐Modified Nucleosides. Chemistry A European J 2015, 21, 13401. <https://doi.org/10.1002/chem.201501334>
• Wierzchowski Jacek, Antosiewicz Jan M., Shugar David: 8-Azapurines as isosteric purine fluorescent probes for nucleic acid and enzymatic research. Mol. BioSyst. 2014, 10, 2756. <https://doi.org/10.1039/C4MB00233D>
• Zhou Xinrui, Szeker Kathleen, Janocha Bernd, Böhme Thomas, Albrecht Dirk, Mikhailopulo Igor A., Neubauer Peter: Recombinant purine nucleoside phosphorylases from thermophiles: preparation, properties and activity towards purine and pyrimidine nucleosides. The FEBS Journal 2013, 280, 1475. <https://doi.org/10.1111/febs.12143>
• Ubiali Daniela, Serra Carla D., Serra Immacolata, Morelli Carlo F., Terreni Marco, Albertini Alessandra M., Manitto Paolo, Speranza Giovanna: Production, Characterization and Synthetic Application of a Purine Nucleoside Phosphorylase from Aeromonas hydrophila. Adv Synth Catal 2012, 354, 96. <https://doi.org/10.1002/adsc.201100505>
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• Modrak-Wójcik Anna, Kirilenko Aneta, Shugar David, Kierdaszuk Borys: Role of ionization of the phosphate cosubstrate on phosphorolysis by purine nucleoside phosphorylase (PNP) of bacterial (E. coli) and mammalian (human) origin. Eur Biophys J 2008, 37, 153. <https://doi.org/10.1007/s00249-007-0205-8>
• Włodarczyk Jakub, Stoychev Galitonov Gerasim, Kierdaszuk Borys: Identification of the tautomeric form of formycin A in its complex with Escherichia coli purine nucleoside phosphorylase based on the effect of enzyme–ligand binding on fluorescence and phosphorescence. Eur Biophys J 2004, 33, 377. <https://doi.org/10.1007/s00249-003-0369-9>
• Bentancor L, Trelles J.A, Nóbile M, Lewkowicz E.S, Iribarren A.M: Benzimidazole as deazapurine analogue for microbial transglycosylation. Journal of Molecular Catalysis B: Enzymatic 2004, 29, 3. <https://doi.org/10.1016/j.molcatb.2003.10.007>
• Bennett Eric M., Li Chenglong, Allan Paula W., Parker William B., Ealick Steven E.: Structural Basis for Substrate Specificity of Escherichia coli Purine Nucleoside Phosphorylase. Journal of Biological Chemistry 2003, 278, 47110. <https://doi.org/10.1074/jbc.M304622200>
• Wierzchowski Jacek, Ogiela Maria, Iwańska Beata, Shugar David: Selective fluorescent and fluorogenic substrates for purine-nucleoside phosphorylases from various sources, and direct fluorimetric determination of enzyme levels in human and animal blood. Analytica Chimica Acta 2002, 472, 63. <https://doi.org/10.1016/S0003-2670(02)00938-8>
• Janeba Z., Holý A.: SYNTHESIS OF 8-AMINO AND 8-SUBSTITUTED AMINO DERIVATIVES OF ACYCLIC PURINE NUCLEOSIDE AND NUCLEOTIDE ANALOGS. ALKYLATION OF 8-SUBSTITUTED PURINE BASES. Nucleosides, Nucleotides and Nucleic Acids 2001, 20, 1103. <https://doi.org/10.1081/NCN-100002498>
• Janeba Zlatko, Holý Antonín, Masojídková Milena: Synthesis of 8-Amino- and N-Substituted 8-Aminoadenine Derivatives of Acyclic Nucleoside and Nucleotide Analogs. Collect. Czech. Chem. Commun. 2001, 66, 517. <https://doi.org/10.1135/cccc20010517>
• Bzowska Agnieszka, Kulikowska Ewa, Shugar David: Purine nucleoside phosphorylases: properties, functions, and clinical aspects. Pharmacology & Therapeutics 2000, 88, 349. <https://doi.org/10.1016/S0163-7258(00)00097-8>
• Kleczkowski Leszek A, Kierdaszuk Borys, Modrak-W��jcik Anna, Wierzchowski Jacek, Shugar David, Gamble Mary V., Mata Nathan L., Tsin Andy T., Mertz James R., Blaner William S.: Is leaf ADP-glucose pyrophosphorylase an allosteric enzyme?. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 2000, 1476, 103. <https://doi.org/10.1016/S0167-4838(99)00225-3>
• Janeba Zlatko, Holý Antonín, Masojídková Milena: Synthesis of Acyclic Nucleoside and Nucleotide Analogs Derived from 6-Amino-7H-purin-8(9H)-one. Collect. Czech. Chem. Commun. 2000, 65, 1126. <https://doi.org/10.1135/cccc20001126>
• Boudou Valérie, Imbach Jean-Louis, Gosselin Grilles: Synthesis and Biological Evaluation of 9-(β-L-Arabinofuranosyl)Adenine. Nucleosides and Nucleotides 1999, 18, 2463. <https://doi.org/10.1080/07328319908044620>
• Secrist John A., Parker William B., Allan Paula W., Bennett L. Lee, Waud William R., Truss Jackie W., Fowler Anita T., Montgomery John A., Ealick Steven E., Wells Alan H., Gillespie G. Yancey, Gadi V. K., Sorscher Eric J.: Gene Therapy of Cancer: Activation of Nucleoside Prodrugs withE. coliPurine Nucleoside Phosphorylase. Nucleosides and Nucleotides 1999, 18, 745. <https://doi.org/10.1080/15257779908041562>
• Wielgus-kutrowska B., Tebbe J., Wierzchowski J., Shugar D., Saenger W., Koellner G., Bzowska A.: Binding of Substrates by Purine Nucleoside Phosphorylase (PNP) fromCellulomonas Sp.- Kinetic and Spectrofluorimetric Studies. Nucleosides and Nucleotides 1999, 18, 871. <https://doi.org/10.1080/15257779908041586>
• Bzowska A., Magnowska L., Wielgus-kutrowska B., Kazimierczuk Z.: Synthesis of 2-Chloro-6-aryloxy- and 2-Chloro-6-alkoxyarylpurines and Their Properties in the Purine Nucleoside Phosphorylase (PNP) System. Nucleosides and Nucleotides 1999, 18, 873. <https://doi.org/10.1080/15257779908041587>
• Koellner Gertraud, Luić Marija, Shugar David, Saenger Wolfram, Bzowska Agnieszka: 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 Å resolution. Journal of Molecular Biology 1998, 280, 153. <https://doi.org/10.1006/jmbi.1998.1799>
• Fathi Reza, Nawoschik Kenneth J., Zavoda Melissa, Cook Alan F.: Enzymatic Synthesis of 2′,5′-Dideoxv Purine Nucleosides and Related Compounds. Nucleosides and Nucleotides 1997, 16, 1907. <https://doi.org/10.1080/07328319708002543>
• Parker William B., King Scott A., Allan Paula W., Bennett L. Lee, Secrist John A., Montgomery John A., Gilbert Karen S., Waud William R., Wells Alan H., Gillespie G. Yancey, Sorscher Eric J.: In Vivo Gene Therapy of Cancer with E. coli Purine Nucleoside Phosphorylase. Human Gene Therapy 1997, 8, 1637. <https://doi.org/10.1089/hum.1997.8.14-1637>
• Wielgus‐Kutrowska Beata, Kulikowska Ewa, Wierzchowski Jacek, Bzowska Agnieszka, Shugar David: Nicotinamide Riboside, an Unusual, Non‐Typical, Substrate of Purified Purine‐Nucleoside Phosphorylases. European Journal of Biochemistry 1997, 243, 408. <https://doi.org/10.1111/j.1432-1033.1997.0408a.x>
• Bzowska Agnieszka, Kulikowska Ewa, Poopeiko Nicolai E., Shugar David: Kinetics of Phosphorolysis of 3‐(β‐d‐Ribofuranosyl)Adenine and 3‐(β‐d‐Ribofuranosyl)Hypoxanthine, Non‐Conventional Substrates of Purine‐Nucleoside Phosphorylase. European Journal of Biochemistry 1996, 239, 229. <https://doi.org/10.1111/j.1432-1033.1996.0229u.x>
• Bzowska Agnieszka, Luić Marija, Schröder Werner, Shugar David, Saenger Wolfram, Koellner Gertraud: Calf spleen purine nucleoside phosphorylase: purification, sequence and crystal structure of its complex with an N(7)‐acycloguanosine inhibitor. FEBS Letters 1995, 367, 214. <https://doi.org/10.1016/0014-5793(95)00540-P>
• Bzowska Agnieszka, Kazimierczuk Zygmunt: 2‐Chloro‐2′ ‐deoxyadenosine (Cladribine) and its Analogues are Good Substrates and Potent Selective Inhibitors of Escherichia coli Purine‐Nucleoside Phosphorylase. European Journal of Biochemistry 1995, 233, 886. <https://doi.org/10.1111/j.1432-1033.1995.886_3.x>
• Perlman Michael E., Davis Donald G., Koszalka George W., Tuttle Joel V., London Robert E.: Studies of Inhibitor Binding to Escherichia coli Purine Nucleoside Phosphorylase Using the Transferred Nuclear Overhauser Effect and Rotating-Frame Nuclear Overhauser Enhancement. Biochemistry 1994, 33, 7547. <https://doi.org/10.1021/bi00190a007>
• Draanen Naina A. Van, Koszalka George W.: Synthesis and Biological Evaluation of Pyrimidine and Purine α-L-2′,3′-Dideoxy Nucleosides. Nucleosides and Nucleotides 1994, 13, 1679. <https://doi.org/10.1080/15257779408009473>
• Voegel Johannes J., Altorfer Michael M., Benner Steven A.: The Donor‐Acceptor‐Acceptor Purine Analog: Transformation of 5‐aza‐7‐deaza‐1H‐isoguanine (=4‐aminoimidazo‐[1,2‐a]‐1,3,5‐triazin‐2(1H)‐one) to 2′‐deoxy‐5‐aza‐7‐deaza‐isoguanosine using purine nucleoside phosphorylase. Helvetica Chimica Acta 1993, 76, 2061. <https://doi.org/10.1002/hlca.19930760520>
• Bzowska Agnieszka, Kulikowska Ewa, Shugar David: Formycins A and B and some analogues: selective inhibitors of bacterial (Escherichia coli) purine nucleoside phosphorylase. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 1992, 1120, 239. <https://doi.org/10.1016/0167-4838(92)90243-7>
• Hori Nobuaki, Watanabe Mutsumi, Sunagawa Kenji, Uehara Kyoko, Mikami Yoichi: Production of 5-methyluridine by immobilized thermostable purine nucleoside phosphorylase and pyrimidine nucleoside phosphorylase from Bacillus stearothermophilus JTS 859. Journal of Biotechnology 1991, 17, 121. <https://doi.org/10.1016/0168-1656(91)90003-E>
• Hori Nobuaki, Watanabe Mutsumi, Mikami Yoichi: The Effects of Organic Solvent on the Ribosyl Transfer Reaction by Thermostable Purine Nucleoside Phosphorylase and Pyrimidine Nucleoside Phosphorylase from Bacillus stearothermophilus JTS 859. Biocatalysis 1991, 4, 297. <https://doi.org/10.3109/10242429109000693>
• Shirae H, Kobayashi K, Shiragami H, Irie Y, Yasuda N, Yokozeki K: Production of 2',3'-dideoxyadenosine and 2',3'-dideoxyinosine from 2',3'-dideoxyuridine and the corresponding purine bases by resting cells of Escherichia coli AJ 2595. Appl Environ Microbiol 1989, 55, 419. <https://doi.org/10.1128/aem.55.2.419-424.1989>
• Bzowska A, Kulikowska E, Darzynkiewicz E, Shugar D: Purine nucleoside phosphorylase. Structure-activity relationships for substrate and inhibitor properties of N-1-, N-7-, and C-8-substituted analogues; differentiation of mammalian and bacterial enzymes with N-1-methylinosine and guanosine. Journal of Biological Chemistry 1988, 263, 9212. <https://doi.org/10.1016/S0021-9258(19)76527-2>
• Kirtland G M, Morris T D, Moore P H, O'Brian J J, Edmonds C G, McCloskey J A, Katze J R: Novel salvage of queuine from queuosine and absence of queuine synthesis in Chlorella pyrenoidosa and Chlamydomonas reinhardtii. J Bacteriol 1988, 170, 5633. <https://doi.org/10.1128/jb.170.12.5633-5641.1988>
• Koszalka G W, Vanhooke J, Short S A, Hall W W: Purification and properties of inosine-guanosine phosphorylase from Escherichia coli K-12. J Bacteriol 1988, 170, 3493. <https://doi.org/10.1128/jb.170.8.3493-3498.1988>
• Cook W J, Ealick S E, Krenitsky T A, Stoeckler J D, Helliwell J R, Bugg C E: Crystallization and preliminary x-ray investigation of purine-nucleoside phosphorylase from Escherichia coli. Journal of Biological Chemistry 1985, 260, 12968. <https://doi.org/10.1016/S0021-9258(17)38820-8>
• Gündüz U, Katze J R: Queuine salvage in mammalian cells. Evidence that queuine is generated from queuosine 5'-phosphate. Journal of Biological Chemistry 1984, 259, 1110. <https://doi.org/10.1016/S0021-9258(17)43573-3>
• Birnbaum George I., Lassota Piotr, Shugar David: 8-Chloroguanosine: solid-state and solution conformations and their biological implications. Biochemistry 1984, 23, 5048. <https://doi.org/10.1021/bi00316a034>
• Spector Thomas, Jones Thomas E., Beacham Lowrie M.: Conversion of 2,6-diamino-9-(2-hydroxyethoxymethyl)purine to acyclovir as catalyzed by adenosine deaminase. Biochemical Pharmacology 1983, 32, 2505. <https://doi.org/10.1016/0006-2952(83)90010-2>
• Salamone Salvatore J., Jordan Frank, Jordan Rosy R.: 31P NMR studies on purine nucleoside phosphorylases: Determination of the scissile bond and of the equilibrium constant. Archives of Biochemistry and Biophysics 1982, 217, 139. <https://doi.org/10.1016/0003-9861(82)90487-8>
• Krenitsky Thomas A., Koszalka George W., Tuttle Joel V., Rideout Janet L., Elion Gertrude B.: An enzymic synthesis of purine d-Arabinonucleosides. Carbohydrate Research 1981, 97, 139. <https://doi.org/10.1016/S0008-6215(00)80531-5>
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• Carlson Jeffrey D., Fischer Allan G.: Thyroid purine nucleoside phosphorylase. Biochimica et Biophysica Acta (BBA) - Enzymology 1979, 566, 259. <https://doi.org/10.1016/0005-2744(79)90029-9>