2.4.2.1 1,N6-ethenoadenine and other fluorescent nucleobase analogs as substrates for purine-nucleoside phosphorylases Spectroscopic and kinetic studies Bacillus cereus 2.4.2.1 1,N6-ethenoadenine and other fluorescent nucleobase analogs as substrates for purine-nucleoside phosphorylases Spectroscopic and kinetic studies Pectobacterium carotovorum 2.4.2.1 1,N6-ethenoadenine and other fluorescent nucleobase analogs as substrates for purine-nucleoside phosphorylases Spectroscopic and kinetic studies Thermus thermophilus 2.4.2.1 1,N6-ethenoadenine and other fluorescent nucleobase analogs as substrates for purine-nucleoside phosphorylases Spectroscopic and kinetic studies Plasmodium lophurae 2.4.2.1 1,N6-ethenoadenine and other fluorescent nucleobase analogs as substrates for purine-nucleoside phosphorylases Spectroscopic and kinetic studies Helicobacter pylori 2.4.2.1 1,N6-ethenoadenine and other fluorescent nucleobase analogs as substrates for purine-nucleoside phosphorylases Spectroscopic and kinetic studies Homo sapiens 2.4.2.1 1,N6-ethenoadenine and other fluorescent nucleobase analogs as substrates for purine-nucleoside phosphorylases Spectroscopic and kinetic studies Escherichia coli 2.4.2.1 1,N6-ethenoadenine and other fluorescent nucleobase analogs as substrates for purine-nucleoside phosphorylases Spectroscopic and kinetic studies Bos taurus 2.4.2.1 1,N6-ethenoadenine and other fluorescent nucleobase analogs as substrates for purine-nucleoside phosphorylases Spectroscopic and kinetic studies Cellulomonas sp. 2.4.2.1 1,N6-ethenoadenine and other fluorescent nucleobase analogs as substrates for purine-nucleoside phosphorylases Spectroscopic and kinetic studies Plasmodium falciparum 2.4.2.1 A synergistic effect of phosphate, pH and Phe159 substitution on the formycin A association to the E. coli purine nucleoside phosphorylase Escherichia coli 2.4.2.1 Catalytic-site design for inverse heavy-enzyme isotope effects in human purine nucleoside phosphorylase Homo sapiens 2.4.2.1 Characterization of the N6-etheno-bridge method to assess extracellular metabolism of adenine nucleotides detection of a possible role for purine nucleoside phosphorylase in adenosine metabolism Homo sapiens 2.4.2.1 Characterization of the N6-etheno-bridge method to assess extracellular metabolism of adenine nucleotides detection of a possible role for purine nucleoside phosphorylase in adenosine metabolism Rattus norvegicus 2.4.2.1 Characterization of the N6-etheno-bridge method to assess extracellular metabolism of adenine nucleotides detection of a possible role for purine nucleoside phosphorylase in adenosine metabolism Rattus norvegicus Wistar-Kyoto 2.4.2.1 Crystal structure of Escherichia coli purine nucleoside phosphorylase complexed with acyclovir Escherichia coli 2.4.2.1 Development, validation and application of a 96-well enzymatic assay based on LC-ESI-MS/MS quantification for the screening of selective inhibitors against Mycobacterium tuberculosis purine nucleoside phosphorylase Mycobacterium tuberculosis 2.4.2.1 Development, validation and application of a 96-well enzymatic assay based on LC-ESI-MS/MS quantification for the screening of selective inhibitors against Mycobacterium tuberculosis purine nucleoside phosphorylase Homo sapiens 2.4.2.1 Efficient synthesis of purine nucleoside analogs by a new trimeric purine nucleoside phosphorylase from Aneurinibacillus migulanus AM007 Aneurinibacillus migulanus 2.4.2.1 Efficient synthesis of purine nucleoside analogs by a new trimeric purine nucleoside phosphorylase from Aneurinibacillus migulanus AM007 Aneurinibacillus migulanus AM007 2.4.2.1 Functional and structural characterization of purine nucleoside phosphorylase from Kluyveromyces lactis and its potential applications in reducing purine content in food Kluyveromyces lactis 2.4.2.1 Functional and structural characterization of purine nucleoside phosphorylase from Kluyveromyces lactis and its potential applications in reducing purine content in food Kluyveromyces lactis CBS 2359 2.4.2.1 Functional and structural characterization of purine nucleoside phosphorylase from Kluyveromyces lactis and its potential applications in reducing purine content in food Kluyveromyces lactis NRRL Y-1140 2.4.2.1 Functional and structural characterization of purine nucleoside phosphorylase from Kluyveromyces lactis and its potential applications in reducing purine content in food Kluyveromyces lactis DSM 70799 2.4.2.1 Functional and structural characterization of purine nucleoside phosphorylase from Kluyveromyces lactis and its potential applications in reducing purine content in food Kluyveromyces lactis WM37 2.4.2.1 Functional and structural characterization of purine nucleoside phosphorylase from Kluyveromyces lactis and its potential applications in reducing purine content in food Kluyveromyces lactis ATCC 8585 2.4.2.1 Functional and structural characterization of purine nucleoside phosphorylase from Kluyveromyces lactis and its potential applications in reducing purine content in food Kluyveromyces lactis NBRC 1267 2.4.2.1 Helicobacterpylori purine nucleoside phosphorylase shows new distribution patterns of open and closed active site conformations and unusual biochemical features Helicobacter pylori 2.4.2.1 Helicobacterpylori purine nucleoside phosphorylase shows new distribution patterns of open and closed active site conformations and unusual biochemical features Helicobacter pylori ATCC 700392 2.4.2.1 Helicobacterpylori purine nucleoside phosphorylase shows new distribution patterns of open and closed active site conformations and unusual biochemical features Helicobacter pylori 26695 2.4.2.1 Hydroxyl-related differences for three dietary flavonoids as inhibitors of human purine nucleoside phosphorylase Homo sapiens 2.4.2.1 Identification of a novel putative inhibitor of the Plasmodium falciparum purine nucleoside phosphorylase exploring the purine salvage pathway to design new antimalarial drugs Plasmodium falciparum 2.4.2.1 Nicotinamide riboside-amino acid conjugates that are stable to purine nucleoside phosphorylase Homo sapiens 2.4.2.1 Origin of enzymatic kinetic isotope effects in human purine nucleoside phosphorylase Homo sapiens 2.4.2.1 Site-selective ribosylation of fluorescent nucleobase analogs using purine-nucleoside phosphorylase as a catalyst effects of point mutations Homo sapiens 2.4.2.1 Site-selective ribosylation of fluorescent nucleobase analogs using purine-nucleoside phosphorylase as a catalyst effects of point mutations Escherichia coli 2.4.2.1 Site-selective ribosylation of fluorescent nucleobase analogs using purine-nucleoside phosphorylase as a catalyst effects of point mutations Bos taurus 2.4.2.1 Structural characterization of purine nucleoside phosphorylase from human pathogen Helicobacter pylori Helicobacter pylori 2.4.2.1 Thermodynamics of the purine nucleoside phosphorylase reaction revealed by computer simulations Homo sapiens 2.4.2.1 Thermophilic nucleoside phosphorylases their properties, characteristics and applications Parageobacillus thermoglucosidasius 2.4.2.1 Thermophilic nucleoside phosphorylases their properties, characteristics and applications Deinococcus geothermalis 2.4.2.1 Thermophilic nucleoside phosphorylases their properties, characteristics and applications Aeropyrum pernix 2.4.2.1 Thermophilic nucleoside phosphorylases their properties, characteristics and applications Geobacillus stearothermophilus 2.4.2.1 Thermophilic nucleoside phosphorylases their properties, characteristics and applications Thermus thermophilus 2.4.2.1 Thermophilic nucleoside phosphorylases their properties, characteristics and applications Pyrococcus furiosus 2.4.2.1 Thermophilic nucleoside phosphorylases their properties, characteristics and applications Pyrococcus furiosus ATCC 43587 2.4.2.1 Thermophilic nucleoside phosphorylases their properties, characteristics and applications Thermus thermophilus DSM 7039 2.4.2.1 Thermophilic nucleoside phosphorylases their properties, characteristics and applications Pyrococcus furiosus Vc1 2.4.2.1 Thermophilic nucleoside phosphorylases their properties, characteristics and applications Deinococcus geothermalis DSM 11300 2.4.2.1 Thermophilic nucleoside phosphorylases their properties, characteristics and applications Deinococcus geothermalis AG-3a 2.4.2.1 Thermophilic nucleoside phosphorylases their properties, characteristics and applications Parageobacillus thermoglucosidasius 11955 2.4.2.1 Thermophilic nucleoside phosphorylases their properties, characteristics and applications Pyrococcus furiosus JCM 8422 2.4.2.1 Thermophilic nucleoside phosphorylases their properties, characteristics and applications Thermus thermophilus ATCC BAA-163 2.4.2.1 Three-dimensional structure of E. coli purine nucleoside phosphorylase at 0.99 A resolution Escherichia coli 2.4.2.1 Tri-cyclic nucleobase analogs and their ribosides as substrates of purine-nucleoside phosphorylases II guanine and isoguanine derivatives Escherichia coli 2.4.2.1 Tricyclic nitrogen base 1,N6-ethenoadenine and its ribosides as substrates for purine-nucleoside phosphorylases spectroscopic and kinetic studies Escherichia coli 2.4.2.1 6-Methylpurine derived sugar modified nucleosides: Synthesis and evaluation of their substrate activity with purine nucleoside phosphorylases Escherichia coli 2.4.2.1 A beta-fluoroamine inhibitor of purine nucleoside phosphorylase Homo sapiens 2.4.2.1 A purine nucleoside phosphorylase in Solanum tuberosum L. (potato) with specificity for cytokinins contributes to the duration of tuber endodormancy Solanum tuberosum 2.4.2.1 Adenosine binding to low-molecular-weight purine nucleoside phosphorylase: the structural basis for recognition based on its complex with the enzyme from Schistosoma mansoni Schistosoma mansoni 2.4.2.1 Adenosine phosphyorylase activity as distinct from inosine-guanosine phosphorylase activity in Sarcoma 180 cells and rat liver Rattus norvegicus 2.4.2.1 Altered enthalpy-entropy compensation in picomolar transition state analogues of human purine nucleoside phosphorylase Homo sapiens 2.4.2.1 Altered thermodynamics from remote mutations altering human toward bovine purine nucleoside phosphorylase Bos taurus 2.4.2.1 Altered thermodynamics from remote mutations altering human toward bovine purine nucleoside phosphorylase Homo sapiens 2.4.2.1 Anopheles gambiae purine nucleoside phosphorylase: catalysis, structure, and inhibition Plasmodium falciparum 2.4.2.1 Anopheles gambiae purine nucleoside phosphorylase: catalysis, structure, and inhibition Anopheles gambiae 2.4.2.1 Anopheles gambiae purine nucleoside phosphorylase: catalysis, structure, and inhibition Homo sapiens 2.4.2.1 Antiproliferative activity of purine nucleoside phosphorylase multisubstrate analogue inhibitors containing difluoromethylene phosphonic acid against leukaemia and lymphoma cells Bos taurus 2.4.2.1 Antiproliferative activity of purine nucleoside phosphorylase multisubstrate analogue inhibitors containing difluoromethylene phosphonic acid against leukaemia and lymphoma cells Homo sapiens 2.4.2.1 Attenuated Plasmodium yoelii lacking purine nucleoside phosphorylase confer protective immunity Plasmodium falciparum 2.4.2.1 Attenuated Plasmodium yoelii lacking purine nucleoside phosphorylase confer protective immunity Plasmodium yoelii 2.4.2.1 Behavior of Plasmodium falciparum purine nucleoside phosphorylase in macromolecular crowded environment Plasmodium falciparum 2.4.2.1 Biochemical and structural characterization of mammalian-like purine nucleoside phosphorylase from the Archaeon Pyrococcus furiosus Pyrococcus furiosus 2.4.2.1 Biosynthesis of nucleoside analogues via thermostable nucleoside phosphorylase Aeropyrum pernix 2.4.2.1 Biosynthesis of nucleoside analogues via thermostable nucleoside phosphorylase Aeropyrum pernix DSM 11879 2.4.2.1 Biosynthesis of the salinosporamide A polyketide synthase substrate chloroethylmalonyl-coenzyme A from S-adenosyl-L-methionine Salinispora tropica 2.4.2.1 Bovine brain purine-nucleoside phosphorylase purification, characterization, and catalytic mechanism Bos taurus 2.4.2.1 Calf spleen purine nucleoside phosphorylase complexed with substrates and substrate analogues Bos taurus 2.4.2.1 Calf spleen purine-nucleoside phosphorylase: crystal structure of the binary complex with a potent multisubstrate analogue inhibitor Bos taurus 2.4.2.1 Cellulomonas sp. purine nucleoside phosphorylase (PNP): comparison with human and E. coli enzymes Cellulomonas sp. 2.4.2.1 Characterization of a recombinant cold-adapted purine nucleoside phosphorylase and its application in ribavirin bioconversion Pseudoalteromonas sp. 2.4.2.1 Characterization of a recombinant cold-adapted purine nucleoside phosphorylase and its application in ribavirin bioconversion Pseudoalteromonas sp. XM2107 2.4.2.1 Characterization of an engineered human purine nucleoside phosphorylase fused to an anti-her2/neu single chain Fv for use in ADEPT Homo sapiens 2.4.2.1 Chinese hamster purine nucleoside phosphorylase Cricetulus griseus 2.4.2.1 Chinese hamster purine-nucleoside phosphorylase: purification, structural, and catalytic properties Cricetulus griseus 2.4.2.1 Cloning and characterization of purine nucleoside phosphorylase in Escherichia coli and subsequent ribavirin biosynthesis using immobilized recombinant cells Escherichia coli 2.4.2.1 Cloning, expression, purification, and some properties of calf purine nucleoside phosphorylase Bos taurus 2.4.2.1 Cloning, overexpression, and purification of functional human purine nucleoside phosphorylase Homo sapiens 2.4.2.1 Cloning, purification and characterisation of a recombinant purine nucleoside phosphorylase from Bacillus halodurans Alk36 Halalkalibacterium halodurans 2.4.2.1 Cloning, purification and characterisation of a recombinant purine nucleoside phosphorylase from Bacillus halodurans Alk36 Halalkalibacterium halodurans Alk36 2.4.2.1 Computer simulations reveal substrate specificity of glycosidic bond cleavage in native and mutant human purine nucleoside phosphorylase Homo sapiens 2.4.2.1 Conformational States of human purine nucleoside phosphorylase at rest, at work, and with transition state analogues Homo sapiens 2.4.2.1 Crystal structure and molecular dynamics studies of human purine nucleoside phosphorylase complexed with 7-deazaguanine Homo sapiens 2.4.2.1 Crystal structure of calf spleen purine nucleoside phosphorylase complexed to a novel purine analogue Bos taurus 2.4.2.1 Crystal structure of calf spleen purine nucleoside phosphorylase in a complex with hypoxanthine at 2.15 A resolution Bos taurus 2.4.2.1 Crystal structure of Escherichia coli PNPase: Central channel residues are involved in processive RNA degradation Escherichia coli 2.4.2.1 Crystal structure of purine nucleoside phosphorylase from Thermus thermophilus Thermus thermophilus 2.4.2.1 Crystal structure of Schistosoma purine nucleoside phosphorylase complexed with a novel monocyclic inhibitor Schistosoma mansoni 2.4.2.1 Crystallization and preliminary X-ray investigation of human erythrocytic purine nucleoside phosphorylase Homo sapiens 2.4.2.1 Crystallization and preliminary x-ray investigation of purine-nucleoside phosphorylase from Escherichia coli Escherichia coli 2.4.2.1 Crystallization and some properties of purine nucleoside phosphorylase from chicken liver Gallus gallus 2.4.2.1 Delivery of replication-competent retrovirus expressing Escherichia coli purine nucleoside phosphorylase increases the metabolism of the prodrug, fludarabine phosphate and suppresses the growth of bladder tumor xenografts Escherichia coli 2.4.2.1 Design and directed evolution of a dideoxy purine nucleoside phosphorylase Homo sapiens 2.4.2.1 Design and evaluation of 5-modified nucleoside analogs as prodrugs for an E. coli purine nucleoside phosphorylase mutant Escherichia coli 2.4.2.1 Design of an adenosine phosphorylase by active-site modification of murine purine nucleoside phosphorylase: enzyme kinetics and molecular dynamics simulation of Asn-243 and Lys-244 substitutions of purine nucleoside phosphorylase Mus musculus 2.4.2.1 Development of a capillary electrophoresis method for analyzing adenosine deaminase and purine nucleoside phosphorylase and its application in inhibitor screening Homo sapiens 2.4.2.1 Development of a new HPLC method using fluorescence detection without derivatization for determining purine nucleoside phosphorylase activity in human plasma Homo sapiens 2.4.2.1 Dynamic expression pattern of distinct genes in the presomitic and somitic mesoderm during Xenopus development Xenopus laevis 2.4.2.1 Effect of the phosphate substrate on drug-inhibitor binding to human purine nucleoside phosphorylase Homo sapiens 2.4.2.1 Effects of some modulators on purine nucleoside phosphorylase activity in myocardial tissue Sus scrofa 2.4.2.1 Escherichia coli purine nucleoside phosphorylase II, the product of the xapA gene Escherichia coli 2.4.2.1 Exploring new inhibitors of Plasmodium falciparum purine nucleoside phosphorylase Plasmodium falciparum 2.4.2.1 Expression of human malaria parasite purine nucleoside phosphorylase in host enzyme-deficient erythrocyte culture. Enzyme characterization and identification of novel inhibitors Homo sapiens 2.4.2.1 Expression of human malaria parasite purine nucleoside phosphorylase in host enzyme-deficient erythrocyte culture. Enzyme characterization and identification of novel inhibitors Plasmodium falciparum 2.4.2.1 Expression, purification, and characterization of recombinant purine nucleoside phosphorylase from Escherichia coli Cellulomonas sp. 2.4.2.1 Expression, purification, and characterization of recombinant purine nucleoside phosphorylase from Escherichia coli Escherichia coli 2.4.2.1 Flow-synthesis of nucleosides catalyzed by an immobilized purine nucleoside phosphorylase from Aeromonas hydrophila: integrated systems of reaction control and product purification Aeromonas hydrophila 2.4.2.1 Formycins A and B and some analogues: selective inhibitors of bacterial (Escherichia coli) purine nucleoside phosphorylase Escherichia coli 2.4.2.1 Four generations of transition-state analogues for human purine nucleoside phosphorylase Homo sapiens 2.4.2.1 Functional analysis of purine nucleoside phosphorylase as a key enzyme in ribavirin metabolism Homo sapiens 2.4.2.1 High-temperature cultivation and 5 mRNA optimization are key factors for the efficient overexpression of thermostable Deinococcus geothermalis purine nucleoside phosphorylase in Escherichia coli Deinococcus geothermalis 2.4.2.1 Homooligomerization is needed for stability: a molecular modelling and solution study of Escherichia coli purine nucleoside phosphorylase Escherichia coli 2.4.2.1 Human erythrocyte purine nucleoside phosphorylase: molecular weight and physical properties. A Theorell-Chance catalytic mechanism Homo sapiens 2.4.2.1 Human red cell purine nucleoside phosphorylase. Purification by biospecific affinity chromatography and physical properties Homo sapiens 2.4.2.1 Identification of 5-fluoro-5-deoxy-D-ribose-1-phosphate as an intermediate in fluorometabolite biosynthesis in Streptomyces cattleya Streptomyces cattleya 2.4.2.1 Identification of a subversive substrate of Trichomonas vaginalis purine nucleoside phosphorylase and the crystal structure of the enzyme-substrate complex Trichomonas vaginalis 2.4.2.1 Immobilized purine nucleoside phosphorylase from Schistosoma mansoni for specific inhibition studies Schistosoma mansoni 2.4.2.1 In vitro reconstituted biotransformation of 4-fluorothreonine from fluoride ion: application of the fluorinase Streptomyces cattleya 2.4.2.1 Inhibition and structure of Toxoplasma gondii purine nucleoside phosphorylase Plasmodium falciparum 2.4.2.1 Inhibition and structure of Toxoplasma gondii purine nucleoside phosphorylase Toxoplasma gondii 2.4.2.1 Inhibition and structure of Trichomonas vaginalis purine nucleoside phosphorylase with picomolar transition state analogues Trichomonas vaginalis 2.4.2.1 Inhibition and structure of Trichomonas vaginalis purine nucleoside phosphorylase with picomolar transition state analogues Homo sapiens 2.4.2.1 Inhibition and structure of Trichomonas vaginalis purine nucleoside phosphorylase with picomolar transition state analogues Bos taurus 2.4.2.1 Inhibition and structure of Trichomonas vaginalis purine nucleoside phosphorylase with picomolar transition state analogues Plasmodium falciparum 2.4.2.1 Inhibition of pyrimidine and purine nucleoside phosphorylases by a 3,5-dichlorobenzoyl-substituted 2-deoxy-D-ribose-1-phosphate derivative Homo sapiens 2.4.2.1 Inhibition of pyrimidine and purine nucleoside phosphorylases by a 3,5-dichlorobenzoyl-substituted 2-deoxy-D-ribose-1-phosphate derivative Mycoplasma hyorhinis 2.4.2.1 Inhibitory properties of nucleotides with difluoromethylenephosphonic acid as a phosphate mimic versus calf spleen purine nucleoside phosphorylase and effect of these analogues on the viability of human blood lymphocytes Bos taurus 2.4.2.1 Insight into catalytically relevant correlated motions in human purine nucleoside phosphorylase Homo sapiens 2.4.2.1 Interactions of calf spleen purine nucleoside phosphorylase with 8-azaguanine, and a bisubstrate analogue inhibitor: implications for the reaction mechanism Bos taurus 2.4.2.1 Interactions of calf spleen purine nucleoside phosphorylase with formycin B and its aglycone - spectroscopic and kinetic studies Bos taurus 2.4.2.1 Interactions of potent multisubstrate analogue inhibitors with purine nucleoside phosphorylase from calf spleen--kinetic and spectrofluorimetric studies Bos taurus 2.4.2.1 Isolation and substrate specificity of an adenine nucleoside phosphorylase from adult Schistosoma mansoni Schistosoma mansoni 2.4.2.1 Isotope-specific and amino acid-specific heavy atom substitutions alter barrier crossing in human purine nucleoside phosphorylase Homo sapiens 2.4.2.1 Kinetic properties of Cellulomonas sp. purine nucleoside phosphorylase with typical and non-typical substrates: implications for the reaction mechanism Cellulomonas sp. 2.4.2.1 Kinetics and crystal structure of human purine nucleoside phosphorylase in complex with 7-methyl-6-thio-guanosine Homo sapiens 2.4.2.1 Kinetics of binding of multisubstrate analogue inhibitor (2-amino-9-[2-(phosphonomethoxy)ethyl]-6-sulfanylpurine) with trimeric purine nucleoside phosphorylase Cellulomonas sp. 2.4.2.1 Kinetics of phosphorolysis of 3-(beta-D-ribofuranosyl)adenine and 3-(beta-D-ribofuranosyl)hypoxanthine, non-conventional substrates of purine-nucleoside phosphorylase Bos taurus 2.4.2.1 Kinetics of phosphorolysis of 3-(beta-D-ribofuranosyl)adenine and 3-(beta-D-ribofuranosyl)hypoxanthine, non-conventional substrates of purine-nucleoside phosphorylase Escherichia coli 2.4.2.1 L-Enantiomers of transition state analogue inhibitors bound to human purine nucleoside phosphorylase Homo sapiens 2.4.2.1 Lentivirus gene therapy for purine nucleoside phosphorylase deficiency Homo sapiens 2.4.2.1 Liver purine nucleoside phosphorylase in Camelus dromedarius: purification and properties Camelus dromedarius 2.4.2.1 Low-molecular-mass purine nucleoside phosphorylase: characterization and application in enzymatic synthesis of nucleoside antiviral drugs Bacillus subtilis 2.4.2.1 Low-molecular-mass purine nucleoside phosphorylase: characterization and application in enzymatic synthesis of nucleoside antiviral drugs Escherichia coli 2.4.2.1 Low-molecular-mass purine nucleoside phosphorylase: characterization and application in enzymatic synthesis of nucleoside antiviral drugs Pseudoalteromonas sp. 2.4.2.1 Low-molecular-mass purine nucleoside phosphorylase: characterization and application in enzymatic synthesis of nucleoside antiviral drugs Bacillus subtilis 168 2.4.2.1 Molecular architecture of E. coli purine nucleoside phosphorylase studied by analytical ultracentrifugation and CD spectroscopy Escherichia coli 2.4.2.1 Molecular cloning, overexpression, purification, crystallization and preliminary X-ray diffraction analysis of a purine nucleoside phosphorylase from Bacillus subtilis strain 168 Bacillus subtilis 2.4.2.1 Molecular cloning, overexpression, purification, crystallization and preliminary X-ray diffraction analysis of a purine nucleoside phosphorylase from Bacillus subtilis strain 168 Bacillus subtilis 168 2.4.2.1 Molecular dynamics studies of a hexameric purine nucleoside phosphorylase Plasmodium falciparum 2.4.2.1 Molecular modeling and dynamics studies of purine nucleoside phosphorylase from Bacteroides fragilis Bacteroides fragilis 2.4.2.1 Molecular modeling, dynamics and docking studies of purine nucleoside phosphorylase from Streptococcus pyogenes Streptococcus pyogenes 2.4.2.1 Molecular properties and a nonidentical trimeric structure of purine nucleoside phosphorylase from chicken liver Gallus gallus 2.4.2.1 Monomeric purine nucleoside phosphorylase from rabbit liver. Purification and characterization Oryctolagus cuniculus 2.4.2.1 Multiple disulfide bridges modulate conformational stability and flexibility in hyperthermophilic archaeal purine nucleoside phosphorylase Saccharolobus solfataricus 2.4.2.1 Multiple disulfide bridges modulate conformational stability and flexibility in hyperthermophilic archaeal purine nucleoside phosphorylase Saccharolobus solfataricus P2 2.4.2.1 N-phosphonocarbonylpyrrolidine derivatives of guanine: a new class of bi-substrate inhibitors of human purine nucleoside phosphorylase Homo sapiens 2.4.2.1 Neighboring group participation in the transition state of human purine nucleoside phosphorylase Homo sapiens 2.4.2.1 New catalytic mechanism for human purine nucleoside phosphorylase Homo sapiens 2.4.2.1 New insights into active site conformation dynamics of E. coli PNP revealed by combined H/D exchange approach and molecular dynamics simulations Escherichia coli 2.4.2.1 New phosphate binding sites in the crystal structure of Escherichia coli purine nucleoside phosphorylase complexed with phosphate and formycin A Escherichia coli 2.4.2.1 Novel multisubstrate inhibitors of mammalian purine nucleoside phosphorylase Bos taurus 2.4.2.1 Open and closed conformation of the E. coli purine nucleoside phosphorylase active center and implications for the catalytic mechanism Escherichia coli 2.4.2.1 Overexpressed proteins may act as mops removing their ligands from the host cells: a case study of calf PNP Bos taurus 2.4.2.1 Overexpression, purification and characterization of functional calf purine nucleoside phosphorylase (PNP) Bos taurus 2.4.2.1 Partial purification and properties of purine nucleoside phosphorylase from rabbit erythrocytes Oryctolagus cuniculus 2.4.2.1 Plasmodium falciparum purine nucleoside phosphorylase is critical for viability of malaria parasites Plasmodium falciparum 2.4.2.1 Plasmodium falciparum purine nucleoside phosphorylase: crystal structures, immucillin inhibitors, and dual catalytic function Plasmodium falciparum 2.4.2.1 Plasmodium falciparum purine nucleoside phosphorylase: crystal structures, immucillin inhibitors, and dual catalytic function Homo sapiens 2.4.2.1 Preliminary crystallographic studies of purine nucleoside phosphorylase from the cariogenic pathogen Streptococcus mutans Streptococcus mutans 2.4.2.1 Probing the mechanism of purine nucleoside phosphorylase by steady-state kinetic studies and ligand binding characterization determined by fluorimetric titrations Cellulomonas sp. 2.4.2.1 Properties of nucleoside phosphorylase from Enterobacter aerogenes Klebsiella aerogenes 2.4.2.1 Properties of purine nucleoside phosphorylase (PNP) of mammalian and bacterial origin Bos taurus 2.4.2.1 Properties of purine nucleoside phosphorylase (PNP) of mammalian and bacterial origin Escherichia coli 2.4.2.1 Properties of purine nucleoside phosphorylase (PNP) of mammalian and bacterial origin Homo sapiens 2.4.2.1 Properties of purine nucleoside phosphorylase from Enterobacter cloacae Enterobacter cloacae 2.4.2.1 Properties of purine nucleoside phosphorylase from Enterobacter cloacae Alcaligenes faecalis 2.4.2.1 Properties of purine nucleoside phosphorylase from Enterobacter cloacae Arthrobacter nucleogenes 2.4.2.1 Properties of purine nucleoside phosphorylase from Enterobacter cloacae Bacterium cadaveris 2.4.2.1 Properties of purine nucleoside phosphorylase from Enterobacter cloacae Corynebacterium vitaeruminis 2.4.2.1 Properties of purine nucleoside phosphorylase from Enterobacter cloacae Cellulomonas cellasea 2.4.2.1 Properties of purine nucleoside phosphorylase from Enterobacter cloacae Micrococcus luteus 2.4.2.1 Properties of purine nucleoside phosphorylase from Enterobacter cloacae Proteus mirabilis 2.4.2.1 Properties of purine nucleoside phosphorylase from Enterobacter cloacae Xanthomonas campestris 2.4.2.1 Properties of purine nucleoside phosphorylase from Enterobacter cloacae Cellulomonas cellasea KY3491 2.4.2.1 Properties of purine nucleoside phosphorylase from Enterobacter cloacae Alcaligenes faecalis KY3106 2.4.2.1 Properties of purine nucleoside phosphorylase from Enterobacter cloacae Xanthomonas campestris KY4208 2.4.2.1 Properties of purine nucleoside phosphorylase from Enterobacter cloacae Bacterium cadaveris KY3402 2.4.2.1 Properties of purine nucleoside phosphorylase from Enterobacter cloacae Proteus mirabilis KY4057 2.4.2.1 Properties of purine nucleoside phosphorylase from Enterobacter cloacae Micrococcus luteus KY 3760 2.4.2.1 Properties of purine nucleoside phosphorylase from Enterobacter cloacae Corynebacterium vitaeruminis KY3459 2.4.2.1 Properties of purine nucleoside phosphorylase from Enterobacter cloacae Arthrobacter nucleogenes KY3168 2.4.2.1 Properties of purine nucleoside phosphorylase from Enterobacter cloacae Enterobacter cloacae KY3074 2.4.2.1 Properties of two unusual, and fluorescent, substrates of purine-nucleoside phosphorylase: 7-methylguanosine and 7-methylinosine Bos taurus 2.4.2.1 Purification and characterization of a purine-nucleoside phosphorylase from bovine thyroid Bos taurus 2.4.2.1 Purification and characterization of human erythrocyte purine nucleoside phosphorylase and its subunits Homo sapiens 2.4.2.1 Purification and characterization of purine nucleoside phosphorylase and pyrimidine nucleoside phosphorylase from Bacillus stearothermophilus TH 6-2 Geobacillus stearothermophilus 2.4.2.1 Purification and characterization of purine nucleoside phosphorylase and pyrimidine nucleoside phosphorylase from Bacillus stearothermophilus TH 6-2 Geobacillus stearothermophilus TH 6-2 2.4.2.1 Purification and characterization of purine nucleoside phosphorylase from developing embryos of Hyalomma dromedarii Hyalomma dromedarii 2.4.2.1 Purification and characterization of purine nucleoside phosphorylase from Proteus vulgaris Proteus vulgaris 2.4.2.1 Purification and characterization of second thermostable purine nucleoside phosphorylase in Bacillus stearothermophilus JTS 859 Geobacillus stearothermophilus 2.4.2.1 Purification and characterization of second thermostable purine nucleoside phosphorylase in Bacillus stearothermophilus JTS 859 Geobacillus stearothermophilus JTS 859 2.4.2.1 Purification and characterization of thermostable purine nucleoside phosphorylase of Bacillus stearothermophilus JTS 859 Geobacillus stearothermophilus 2.4.2.1 Purification and characterization of thermostable purine nucleoside phosphorylase of Bacillus stearothermophilus JTS 859 Geobacillus stearothermophilus JTS 859 2.4.2.1 Purification and partial characterization of purine nucleoside phosphorylase from Serratia marcescens Serratia marcescens 2.4.2.1 Purification and properties of inosine-guanosine phosphorylase from Escherichia coli K-12 Escherichia coli 2.4.2.1 Purification and properties of purine nucleoside phosphorylase from Brevibacterium acetylicum ATCC 954 Exiguobacterium acetylicum 2.4.2.1 Purification and properties of purine nucleoside phosphorylase from Salmonella typhimurium Salmonella enterica subsp. enterica serovar Typhimurium 2.4.2.1 Purifications and properties of orotidine-phosphorolyzing enzyme and purine nucleoside phosphorylase from Erwinia carotovora AJ 2992 Pectobacterium carotovorum 2.4.2.1 Purifications and properties of orotidine-phosphorolyzing enzyme and purine nucleoside phosphorylase from Erwinia carotovora AJ 2992 Pectobacterium carotovorum AJ 2992 2.4.2.1 Purine nucleoside phosphorylase Klebsiella aerogenes 2.4.2.1 Purine nucleoside phosphorylase Aeromonas hydrophila 2.4.2.1 Purine nucleoside phosphorylase Brevibacillus brevis 2.4.2.1 Purine nucleoside phosphorylase Bacillus cereus 2.4.2.1 Purine nucleoside phosphorylase Bacillus subtilis 2.4.2.1 Purine nucleoside phosphorylase Bacillus licheniformis 2.4.2.1 Purine nucleoside phosphorylase Bacterium cadaveris 2.4.2.1 Purine nucleoside phosphorylase Bos taurus 2.4.2.1 Purine nucleoside phosphorylase Canis lupus familiaris 2.4.2.1 Purine nucleoside phosphorylase Gallus gallus 2.4.2.1 Purine nucleoside phosphorylase Columba livia 2.4.2.1 Purine nucleoside phosphorylase Clavibacter michiganensis subsp. sepedonicus 2.4.2.1 Purine nucleoside phosphorylase Oryctolagus cuniculus 2.4.2.1 Purine nucleoside phosphorylase Escherichia coli 2.4.2.1 Purine nucleoside phosphorylase Equus caballus 2.4.2.1 Purine nucleoside phosphorylase Pectobacterium carotovorum 2.4.2.1 Purine nucleoside phosphorylase Felis catus 2.4.2.1 Purine nucleoside phosphorylase Homo sapiens 2.4.2.1 Purine nucleoside phosphorylase Lactobacillus leichmannii 2.4.2.1 Purine nucleoside phosphorylase Leucisus rusticus 2.4.2.1 Purine nucleoside phosphorylase Macaca mulatta 2.4.2.1 Purine nucleoside phosphorylase Micrococcus luteus 2.4.2.1 Purine nucleoside phosphorylase Papio hamadryas 2.4.2.1 Purine nucleoside phosphorylase Proteus vulgaris 2.4.2.1 Purine nucleoside phosphorylase Shewanella putrefaciens 2.4.2.1 Purine nucleoside phosphorylase Rattus norvegicus 2.4.2.1 Purine nucleoside phosphorylase salmon 2.4.2.1 Purine nucleoside phosphorylase Salmonella enterica subsp. enterica serovar Enteritidis 2.4.2.1 Purine nucleoside phosphorylase Sus scrofa 2.4.2.1 Purine nucleoside phosphorylase activity decline is linked to the decay of the trimeric form of the enzyme Bos taurus 2.4.2.1 Purine nucleoside phosphorylase activity in rat cerebrospinal fluid Rattus norvegicus 2.4.2.1 Purine nucleoside phosphorylase and xanthine oxidase activities in erythrocytes and plasma from marine, semiaquatic and terrestrial mammals Sus scrofa 2.4.2.1 Purine nucleoside phosphorylase and xanthine oxidase activities in erythrocytes and plasma from marine, semiaquatic and terrestrial mammals Tursiops truncatus 2.4.2.1 Purine nucleoside phosphorylase and xanthine oxidase activities in erythrocytes and plasma from marine, semiaquatic and terrestrial mammals Lontra longicaudis 2.4.2.1 Purine nucleoside phosphorylase and xanthine oxidase activities in erythrocytes and plasma from marine, semiaquatic and terrestrial mammals Mirounga angustirostris 2.4.2.1 Purine nucleoside phosphorylase deficiency with fatal course in two sisters Homo sapiens 2.4.2.1 Purine nucleoside phosphorylase from bovine lens: purification and properties Bos taurus 2.4.2.1 Purine nucleoside phosphorylase from Cellulomonas sp.: physicochemical properties and binding of substrates determined by ligand-dependent enhancement of enzyme intrinsic fluorescence, and by protective effects of ligands on thermal inactivation of the enzyme Cellulomonas sp. 2.4.2.1 Purine nucleoside phosphorylase from Escherichia coli and Salmonella typhimurium. Purification and some properties Escherichia coli 2.4.2.1 Purine nucleoside phosphorylase from Escherichia coli and Salmonella typhimurium. Purification and some properties Salmonella enterica subsp. enterica serovar Typhimurium 2.4.2.1 Purine nucleoside phosphorylase from human erythrocytes Homo sapiens 2.4.2.1 Purine nucleoside phosphorylase from human erythrocytes. IV. Crystallization and some properties Bos taurus 2.4.2.1 Purine nucleoside phosphorylase from human erythrocytes. IV. Crystallization and some properties Homo sapiens 2.4.2.1 Purine nucleoside phosphorylase from human erythrocytes: physiocochemical properties of the crystalline enzyme Homo sapiens 2.4.2.1 Purine nucleoside phosphorylase from Pseudoalteromonas sp. Bsi590: molecular cloning, gene expression and characterization of the recombinant protein Escherichia coli 2.4.2.1 Purine nucleoside phosphorylase from Pseudoalteromonas sp. Bsi590: molecular cloning, gene expression and characterization of the recombinant protein Pseudoalteromonas sp. 2.4.2.1 Purine nucleoside phosphorylase from Pseudoalteromonas sp. Bsi590: molecular cloning, gene expression and characterization of the recombinant protein Pseudoalteromonas sp. Bsi590 2.4.2.1 Purine nucleoside phosphorylase from rabbit liver Oryctolagus cuniculus 2.4.2.1 Purine nucleoside phosphorylase from Salmonella typhimurium and rat liver Rattus norvegicus 2.4.2.1 Purine nucleoside phosphorylase from Salmonella typhimurium and rat liver Salmonella enterica subsp. enterica serovar Typhimurium 2.4.2.1 Purine nucleoside phosphorylase inhibition as a novel therapeutic approach for B-cell lymphoid malignancies Homo sapiens 2.4.2.1 Purine nucleoside phosphorylase of the malarial parasite, Plasmodium lophurae Plasmodium lophurae 2.4.2.1 Purine nucleoside phosphorylase-catalyzed, phosphate-independent hydrolysis of 2-amino-6-mercapto-7-methylpurine ribonucleoside Bos taurus 2.4.2.1 Purine nucleoside phosphorylase. 1. Structure-function Studies Homo sapiens 2.4.2.1 Purine nucleoside phosphorylase. Catalytic mechanism and transition-state analysis of the arsenolysis reaction Bos taurus 2.4.2.1 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 Bos taurus 2.4.2.1 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 Escherichia coli 2.4.2.1 Purine nucleoside phosphorylase: a potential target for the development of drugs to treat T-cell- and apicomplexan parasite-mediated diseases Plasmodium lophurae 2.4.2.1 Purine nucleoside phosphorylase: a potential target for the development of drugs to treat T-cell- and apicomplexan parasite-mediated diseases Toxoplasma gondii 2.4.2.1 Purine nucleoside phosphorylase: a potential target for the development of drugs to treat T-cell- and apicomplexan parasite-mediated diseases Homo sapiens 2.4.2.1 Purine nucleoside phosphorylase: a potential target for the development of drugs to treat T-cell- and apicomplexan parasite-mediated diseases Bos taurus 2.4.2.1 Purine nucleoside phosphorylase: a potential target for the development of drugs to treat T-cell- and apicomplexan parasite-mediated diseases Plasmodium falciparum 2.4.2.1 Purine nucleoside phosphorylase: a target for drug design Bos taurus 2.4.2.1 Purine nucleoside phosphorylase: a target for drug design Homo sapiens 2.4.2.1 Purine nucleoside phosphorylases from hyperthermophilic Archaea require a CXC motif for stability and folding Pyrococcus furiosus 2.4.2.1 Purine nucleoside phosphorylases purified from rat liver and Novikoff hepatoma cells Rattus norvegicus 2.4.2.1 Purine nucleoside phosphorylases: properties, functions, and clinical aspects Acholeplasma laidlawii 2.4.2.1 Purine nucleoside phosphorylases: properties, functions, and clinical aspects Klebsiella aerogenes 2.4.2.1 Purine nucleoside phosphorylases: properties, functions, and clinical aspects Geobacillus stearothermophilus 2.4.2.1 Purine nucleoside phosphorylases: properties, functions, and clinical aspects Bacillus cereus 2.4.2.1 Purine nucleoside phosphorylases: properties, functions, and clinical aspects Cellulomonas sp. 2.4.2.1 Purine nucleoside phosphorylases: properties, functions, and clinical aspects Pectobacterium carotovorum 2.4.2.1 Purine nucleoside phosphorylases: properties, functions, and clinical aspects Fasciola hepatica 2.4.2.1 Purine nucleoside phosphorylases: properties, functions, and clinical aspects Klebsiella sp. 2.4.2.1 Purine nucleoside phosphorylases: properties, functions, and clinical aspects Micrococcus luteus 2.4.2.1 Purine nucleoside phosphorylases: properties, functions, and clinical aspects Mus musculus 2.4.2.1 Purine nucleoside phosphorylases: properties, functions, and clinical aspects Plasmodium falciparum 2.4.2.1 Purine nucleoside phosphorylases: properties, functions, and clinical aspects Plasmodium lophurae 2.4.2.1 Purine nucleoside phosphorylases: properties, functions, and clinical aspects Proteus vulgaris 2.4.2.1 Purine nucleoside phosphorylases: properties, functions, and clinical aspects Rattus norvegicus 2.4.2.1 Purine nucleoside phosphorylases: properties, functions, and clinical aspects Salmonella enterica subsp. enterica serovar Typhimurium 2.4.2.1 Purine nucleoside phosphorylases: properties, functions, and clinical aspects Serratia marcescens 2.4.2.1 Purine nucleoside phosphorylases: properties, functions, and clinical aspects Saccharolobus solfataricus 2.4.2.1 Purine nucleoside phosphorylases: properties, functions, and clinical aspects Trypanosoma brucei 2.4.2.1 Purine nucleoside phosphorylases: properties, functions, and clinical aspects Trypanosoma cruzi 2.4.2.1 Purine nucleoside phosphorylases: properties, functions, and clinical aspects Homo sapiens 2.4.2.1 Purine nucleoside phosphorylases: properties, functions, and clinical aspects Escherichia coli 2.4.2.1 Purine nucleoside phosphorylases: properties, functions, and clinical aspects Bacillus subtilis 2.4.2.1 Purine nucleoside phosphorylases: properties, functions, and clinical aspects Bos taurus 2.4.2.1 Purine nucleoside phosphorylases: properties, functions, and clinical aspects Saccharomyces cerevisiae 2.4.2.1 Purine salvage in two halophilic archaea: characterization of salvage pathways and isolation of mutants resistant to purine analogs Halobacterium salinarum 2.4.2.1 Purine salvage in two halophilic archaea: characterization of salvage pathways and isolation of mutants resistant to purine analogs Haloferax volcanii 2.4.2.1 Rabbit brain purine nucleoside phosphorylase. Physical and chemical properties. Inhibition studies with aminopterin, folic acid and structurally related compounds Oryctolagus cuniculus 2.4.2.1 Recombinant purine nucleoside phosphorylases from thermophiles: preparation, properties and activity towards purine and pyrimidine nucleosides Aeropyrum pernix 2.4.2.1 Recombinant purine nucleoside phosphorylases from thermophiles: preparation, properties and activity towards purine and pyrimidine nucleosides Aeropyrum pernix DSM 11879 2.4.2.1 Remote mutations alter transition-state structure of human purine nucleoside phosphorylase Homo sapiens 2.4.2.1 Remote mutations and active site dynamics correlate with catalytic properties of purine nucleoside phosphorylase Homo sapiens 2.4.2.1 Second-sphere amino acids contribute to transition-state structure in bovine purine nucleoside phosphorylase Homo sapiens 2.4.2.1 Second-sphere amino acids contribute to transition-state structure in bovine purine nucleoside phosphorylase Bos taurus 2.4.2.1 Sensing purine nucleoside phosphorylase activity by using silver nanoparticles Homo sapiens 2.4.2.1 Simplified analogues of immucillin-G retain potent human purine nucleoside phosphorylase inhibitory activity Homo sapiens 2.4.2.1 Site-selective ribosylation of fluorescent nucleobase analogs using purine-nucleoside phosphorylase as a catalyst: effects of point mutations Bos taurus 2.4.2.1 Spectroscopic and kinetic studies of interactions of calf spleen purine nucleoside phosphorylase with 8-azaguanine, and its 9-(2-phosphonylmethoxyethyl) derivative Bos taurus 2.4.2.1 Structural basis for selective inhibition of purine nucleoside phosphorylase from Schistosoma mansoni: kinetic and structural studies Schistosoma mansoni 2.4.2.1 Structural basis for selective inhibition of purine nucleoside phosphorylase from Schistosoma mansoni: kinetic and structural studies Homo sapiens 2.4.2.1 Structural basis for substrate specificity of Escherichia coli purine nucleoside phosphorylase Escherichia coli 2.4.2.1 Structural bioinformatics study of PNP from Listeria monocytogenes Listeria monocytogenes 2.4.2.1 Structural determinants of the 5-methylthioinosine specificity of Plasmodium purine nucleoside phosphorylase Plasmodium falciparum 2.4.2.1 Structural studies of human purine nucleoside phosphorylase: towards a new specific empirical scoring function Homo sapiens 2.4.2.1 Structure of a mutant human purine nucleoside phosphorylase with the prodrug, 2-fluoro-2-deoxyadenosine and the cytotoxic drug, 2-fluoroadenine Homo sapiens 2.4.2.1 Structure of grouper iridovirus purine nucleoside phosphorylase grouper iridovirus 2.4.2.1 Structure of human PNP complexed with ligands Homo sapiens 2.4.2.1 Structure of purine nucleoside phosphorylase (DeoD) from Bacillus anthracis Bacillus anthracis 2.4.2.1 Structure-activity relationship of a cold-adapted purine nucleoside phosphorylase by site-directed mutagenesis Pseudoalteromonas sp. 2.4.2.1 Structure-activity relationship of a cold-adapted purine nucleoside phosphorylase by site-directed mutagenesis Pseudoalteromonas sp. XM2107 2.4.2.1 Structures for the potential drug target purine nucleoside phosphorylase from Schistosoma mansoni causal agent of Schistosomiasis Schistosoma mansoni 2.4.2.1 Structures of Plasmodium falciparum purine nucleoside phosphorylase complexed with sulfate and its natural substrate inosine Plasmodium falciparum 2.4.2.1 Substrate specificity and kinetic mechanism of purine nucleoside phosphorylase from Mycobacterium tuberculosis Mycobacterium tuberculosis 2.4.2.1 Synthesis and evaluation of the substrate activity of C-6 substituted purine ribosides with E. coli purine nucleoside phosphorylase: palladium mediated cross-coupling of organozinc halides with 6-chloropurine nucleosides Escherichia coli 2.4.2.1 Synthesis of analogs of forodesine HCl, a human purine nucleoside phosphorylase inhibitor-Part I Homo sapiens 2.4.2.1 Synthesis of labeled BCX-4208, a potent inhibitor of purine nucleoside phosphorylase Homo sapiens 2.4.2.1 Targeting gene therapy for hepatocarcinoma cells with the E. coli purine nucleoside phosphorylase suicide gene system directed by a chimeric alpha-fetoprotein promoter Escherichia coli 2.4.2.1 TAT-mediated intracellular delivery of purine nucleoside phosphorylase corrects its deficiency in mice Homo sapiens 2.4.2.1 The chemoenzymatic synthesis of clofarabine and related 2-deoxyfluoroarabinosyl nucleosides: the electronic and stereochemical factors determining substrate recognition by E. coli nucleoside phosphorylases Escherichia coli 2.4.2.1 The crystal structure of Escherichia coli purine nucleoside phosphorylase: a comparison with the human enzyme reveals a conserved topology Escherichia coli 2.4.2.1 The purine nucleoside phosphorylase from Trichomonas vaginalis is a homologue of the bacterial enzyme Trichomonas vaginalis 2.4.2.1 Thermus thermophilus nucleoside phosphorylases active in the synthesis of nucleoside analogues Thermus thermophilus 2.4.2.1 Thermus thermophilus nucleoside phosphorylases active in the synthesis of nucleoside analogues Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039 2.4.2.1 Third-generation immucillins: syntheses and bioactivities of acyclic immucillin inhibitors of human purine nucleoside phosphorylase Homo sapiens 2.4.2.1 Third-generation immucillins: syntheses and bioactivities of acyclic immucillin inhibitors of human purine nucleoside phosphorylase Mus musculus 2.4.2.1 Towards the mechanism of trimeric purine nucleoside phosphorylases: Stopped-flow studies of binding of multisubstrate analogue inhibitor - 2-amino-9-[2-(phosphonomethoxy)ethyl]-6-sulfanylpurine Cellulomonas sp. 2.4.2.1 Toxoplasma gondii purine nucleoside phosphorylase biochemical characterization, inhibitor profiles, and comparison with the Plasmodium falciparum ortholog Toxoplasma gondii 2.4.2.1 Toxoplasma gondii purine nucleoside phosphorylase biochemical characterization, inhibitor profiles, and comparison with the Plasmodium falciparum ortholog Plasmodium falciparum 2.4.2.1 Toxoplasma gondii: localization of purine nucleoside phosphorylase activity in vitro and in vivo by electron microscopy Toxoplasma gondii 2.4.2.1 Toxoplasma gondii: localization of purine nucleoside phosphorylase activity in vitro and in vivo by electron microscopy Toxoplasma gondii ME49 2.4.2.1 Trimeric purine nucleoside phosphorylase from chicken liver having a proteolytic nick on each subunit and its kinetic properties Gallus gallus 2.4.2.1 Trimeric purine nucleoside phosphorylase: exploring postulated one-third-of-the-sites binding in the transition state Bos taurus 2.4.2.1 Two purine nucleoside phosphorylases in Bacillus subtilis. Purification and some properties of the adenosine-specific phosphorylase Bacillus subtilis 2.4.2.1 Two- and three-dimensional quantitative structure-activity relationships for a series of purine nucleoside phosphorylase inhibitors Bos taurus 2.4.2.1 Two-step efficient synthesis of 5-methyluridine via two thermostable nucleoside phosphorylase from Aeropyrum pernix Aeropyrum pernix 2.4.2.1 Unique substrate specificity of purine nucleoside phosphorylases from Thermus thermophilus Thermus thermophilus 2.4.2.1 Unique substrate specificity of purine nucleoside phosphorylases from Thermus thermophilus Thermus thermophilus HB8 / ATCC 27634 / DSM 579 2.4.2.1 Validation of the catalytic mechanism of Escherichia coli purine nucleoside phosphorylase by structural and kinetic studies Escherichia coli 2.4.2.1 Xanthosine and xanthine. Substrate properties with purine nucleoside phosphorylases, and relevance to other enzyme systems Homo sapiens 2.4.2.1 Xanthosine and xanthine. Substrate properties with purine nucleoside phosphorylases, and relevance to other enzyme systems Bos taurus