2.4.2.1 Purine nucleoside phosphorylases: properties, functions, and clinical aspects Acholeplasma laidlawii 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 Purine nucleoside phosphorylase Aeromonas hydrophila 2.4.2.1 Thermophilic nucleoside phosphorylases their properties, characteristics and applications Aeropyrum pernix 2.4.2.1 Biosynthesis of nucleoside analogues via thermostable nucleoside phosphorylase Aeropyrum pernix 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 Two-step efficient synthesis of 5-methyluridine via two thermostable nucleoside phosphorylase from Aeropyrum pernix Aeropyrum pernix 2.4.2.1 Biosynthesis of nucleoside analogues via thermostable nucleoside phosphorylase Aeropyrum pernix DSM 11879 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 Properties of purine nucleoside phosphorylase from Enterobacter cloacae Alcaligenes faecalis 2.4.2.1 Properties of purine nucleoside phosphorylase from Enterobacter cloacae Alcaligenes faecalis KY3106 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 Anopheles gambiae purine nucleoside phosphorylase: catalysis, structure, and inhibition Anopheles gambiae 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 Arthrobacter nucleogenes KY3168 2.4.2.1 Structure of purine nucleoside phosphorylase (DeoD) from Bacillus anthracis Bacillus anthracis 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 Purine nucleoside phosphorylase Bacillus cereus 2.4.2.1 Purine nucleoside phosphorylases: properties, functions, and clinical aspects Bacillus cereus 2.4.2.1 Purine nucleoside phosphorylase Bacillus licheniformis 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 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 Purine nucleoside phosphorylase Bacillus subtilis 2.4.2.1 Purine nucleoside phosphorylases: properties, functions, and clinical aspects Bacillus subtilis 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 Low-molecular-mass purine nucleoside phosphorylase: characterization and application in enzymatic synthesis of nucleoside antiviral drugs Bacillus subtilis 168 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 Properties of purine nucleoside phosphorylase from Enterobacter cloacae Bacterium cadaveris 2.4.2.1 Purine nucleoside phosphorylase Bacterium cadaveris 2.4.2.1 Properties of purine nucleoside phosphorylase from Enterobacter cloacae Bacterium cadaveris KY3402 2.4.2.1 Molecular modeling and dynamics studies of purine nucleoside phosphorylase from Bacteroides fragilis Bacteroides fragilis 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 Site-selective ribosylation of fluorescent nucleobase analogs using purine-nucleoside phosphorylase as a catalyst effects of point mutations Bos taurus 2.4.2.1 Altered thermodynamics from remote mutations altering human toward bovine purine nucleoside phosphorylase Bos taurus 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 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 Cloning, expression, purification, and some properties of calf purine nucleoside phosphorylase Bos taurus 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 Inhibition and structure of Trichomonas vaginalis purine nucleoside phosphorylase with picomolar transition state analogues Bos taurus 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 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 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 Novel multisubstrate inhibitors of mammalian purine nucleoside phosphorylase Bos taurus 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 Properties of purine nucleoside phosphorylase (PNP) of mammalian and bacterial origin Bos taurus 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 Purine nucleoside phosphorylase Bos taurus 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 from bovine lens: purification and properties Bos taurus 2.4.2.1 Purine nucleoside phosphorylase from human erythrocytes. IV. Crystallization and some properties Bos taurus 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. 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: 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 target for drug design Bos taurus 2.4.2.1 Purine nucleoside phosphorylases: properties, functions, and clinical aspects Bos taurus 2.4.2.1 Second-sphere amino acids contribute to transition-state structure in bovine purine nucleoside phosphorylase Bos taurus 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 Trimeric purine nucleoside phosphorylase: exploring postulated one-third-of-the-sites binding in the transition state Bos taurus 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 Xanthosine and xanthine. Substrate properties with purine nucleoside phosphorylases, and relevance to other enzyme systems Bos taurus 2.4.2.1 Purine nucleoside phosphorylase Brevibacillus brevis 2.4.2.1 Liver purine nucleoside phosphorylase in Camelus dromedarius: purification and properties Camelus dromedarius 2.4.2.1 Purine nucleoside phosphorylase Canis lupus familiaris 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 Cellulomonas cellasea KY3491 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 Cellulomonas sp. purine nucleoside phosphorylase (PNP): comparison with human and E. coli enzymes Cellulomonas sp. 2.4.2.1 Expression, purification, and characterization of recombinant purine nucleoside phosphorylase from Escherichia coli Cellulomonas sp. 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 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 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 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 phosphorylases: properties, functions, and clinical aspects Cellulomonas sp. 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 Purine nucleoside phosphorylase Clavibacter michiganensis subsp. sepedonicus 2.4.2.1 Purine nucleoside phosphorylase Columba livia 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 Corynebacterium vitaeruminis KY3459 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 Thermophilic nucleoside phosphorylases their properties, characteristics and applications Deinococcus geothermalis 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 Thermophilic nucleoside phosphorylases their properties, characteristics and applications Deinococcus geothermalis AG-3a 2.4.2.1 Thermophilic nucleoside phosphorylases their properties, characteristics and applications Deinococcus geothermalis DSM 11300 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 Enterobacter cloacae KY3074 2.4.2.1 Purine nucleoside phosphorylase Equus caballus 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 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 Crystal structure of Escherichia coli purine nucleoside phosphorylase complexed with acyclovir Escherichia coli 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 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 Cloning and characterization of purine nucleoside phosphorylase in Escherichia coli and subsequent ribavirin biosynthesis using immobilized recombinant cells Escherichia coli 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 Crystallization and preliminary x-ray investigation of purine-nucleoside phosphorylase from Escherichia coli Escherichia coli 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 evaluation of 5-modified nucleoside analogs as prodrugs for an E. coli purine nucleoside phosphorylase mutant Escherichia coli 2.4.2.1 Escherichia coli purine nucleoside phosphorylase II, the product of the xapA gene Escherichia coli 2.4.2.1 Expression, purification, and characterization of recombinant purine nucleoside phosphorylase from Escherichia coli Escherichia coli 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 Homooligomerization is needed for stability: a molecular modelling and solution study of Escherichia coli purine nucleoside phosphorylase Escherichia coli 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 Low-molecular-mass purine nucleoside phosphorylase: characterization and application in enzymatic synthesis of nucleoside antiviral drugs Escherichia coli 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 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 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 Properties of purine nucleoside phosphorylase (PNP) of mammalian and bacterial origin Escherichia coli 2.4.2.1 Purification and properties of inosine-guanosine phosphorylase from Escherichia coli K-12 Escherichia coli 2.4.2.1 Purine nucleoside phosphorylase Escherichia coli 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 Pseudoalteromonas sp. Bsi590: molecular cloning, gene expression and characterization of the recombinant protein Escherichia coli 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 phosphorylases: properties, functions, and clinical aspects Escherichia coli 2.4.2.1 Structural basis for substrate specificity of Escherichia coli purine nucleoside phosphorylase Escherichia coli 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 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 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 Validation of the catalytic mechanism of Escherichia coli purine nucleoside phosphorylase by structural and kinetic studies Escherichia coli 2.4.2.1 Purification and properties of purine nucleoside phosphorylase from Brevibacterium acetylicum ATCC 954 Exiguobacterium acetylicum 2.4.2.1 Purine nucleoside phosphorylases: properties, functions, and clinical aspects Fasciola hepatica 2.4.2.1 Purine nucleoside phosphorylase Felis catus 2.4.2.1 Crystallization and some properties of purine nucleoside phosphorylase from chicken liver Gallus gallus 2.4.2.1 Molecular properties and a nonidentical trimeric structure of purine nucleoside phosphorylase from chicken liver Gallus gallus 2.4.2.1 Purine nucleoside phosphorylase Gallus gallus 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 Thermophilic nucleoside phosphorylases their properties, characteristics and applications 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 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 thermostable purine nucleoside phosphorylase of Bacillus stearothermophilus JTS 859 Geobacillus stearothermophilus 2.4.2.1 Purine nucleoside phosphorylases: properties, functions, and clinical aspects 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 JTS 859 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 Structure of grouper iridovirus purine nucleoside phosphorylase grouper iridovirus 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 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 1,N6-ethenoadenine and other fluorescent nucleobase analogs as substrates for purine-nucleoside phosphorylases Spectroscopic and kinetic studies 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 2.4.2.1 Structural characterization of purine nucleoside phosphorylase from human pathogen Helicobacter pylori 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 26695 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 1,N6-ethenoadenine and other fluorescent nucleobase analogs as substrates for purine-nucleoside phosphorylases Spectroscopic and kinetic studies Homo sapiens 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 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 Hydroxyl-related differences for three dietary flavonoids as inhibitors of human purine nucleoside phosphorylase Homo sapiens 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 Thermodynamics of the purine nucleoside phosphorylase reaction revealed by computer simulations Homo sapiens 2.4.2.1 A beta-fluoroamine inhibitor of purine nucleoside phosphorylase Homo sapiens 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 Homo sapiens 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 Homo sapiens 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 Cloning, overexpression, and purification of functional human purine nucleoside phosphorylase Homo sapiens 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 Crystallization and preliminary X-ray investigation of human erythrocytic purine nucleoside phosphorylase Homo sapiens 2.4.2.1 Design and directed evolution of a dideoxy purine nucleoside phosphorylase Homo sapiens 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 Effect of the phosphate substrate on drug-inhibitor binding to human purine nucleoside phosphorylase 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 Homo sapiens 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 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 Inhibition and structure of Trichomonas vaginalis purine nucleoside phosphorylase with picomolar transition state analogues 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 Homo sapiens 2.4.2.1 Insight into catalytically relevant correlated motions in human purine nucleoside phosphorylase Homo sapiens 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 Kinetics and crystal structure of human purine nucleoside phosphorylase in complex with 7-methyl-6-thio-guanosine Homo sapiens 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 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 Plasmodium falciparum purine nucleoside phosphorylase: crystal structures, immucillin inhibitors, and dual catalytic function Homo sapiens 2.4.2.1 Properties of purine nucleoside phosphorylase (PNP) of mammalian and bacterial origin Homo sapiens 2.4.2.1 Purification and characterization of human erythrocyte purine nucleoside phosphorylase and its subunits Homo sapiens 2.4.2.1 Purine nucleoside phosphorylase Homo sapiens 2.4.2.1 Purine nucleoside phosphorylase deficiency with fatal course in two sisters Homo sapiens 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 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 inhibition as a novel therapeutic approach for B-cell lymphoid malignancies Homo sapiens 2.4.2.1 Purine nucleoside phosphorylase. 1. Structure-function Studies 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 Homo sapiens 2.4.2.1 Purine nucleoside phosphorylase: a target for drug design Homo sapiens 2.4.2.1 Purine nucleoside phosphorylases: properties, functions, and clinical aspects Homo sapiens 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 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 Structural basis for selective inhibition of purine nucleoside phosphorylase from Schistosoma mansoni: kinetic and structural studies Homo sapiens 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 human PNP complexed with ligands Homo sapiens 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 TAT-mediated intracellular delivery of purine nucleoside phosphorylase corrects its deficiency in mice Homo sapiens 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 Xanthosine and xanthine. Substrate properties with purine nucleoside phosphorylases, and relevance to other enzyme systems Homo sapiens 2.4.2.1 Purification and characterization of purine nucleoside phosphorylase from developing embryos of Hyalomma dromedarii Hyalomma dromedarii 2.4.2.1 Properties of nucleoside phosphorylase from Enterobacter aerogenes Klebsiella aerogenes 2.4.2.1 Purine nucleoside phosphorylase Klebsiella aerogenes 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 Klebsiella sp. 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 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 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 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 NBRC 1267 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 WM37 2.4.2.1 Purine nucleoside phosphorylase Lactobacillus leichmannii 2.4.2.1 Purine nucleoside phosphorylase Leucisus rusticus 2.4.2.1 Structural bioinformatics study of PNP from Listeria monocytogenes Listeria monocytogenes 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 Macaca mulatta 2.4.2.1 Properties of purine nucleoside phosphorylase from Enterobacter cloacae Micrococcus luteus 2.4.2.1 Purine nucleoside phosphorylase Micrococcus luteus 2.4.2.1 Purine nucleoside phosphorylases: properties, functions, and clinical aspects Micrococcus luteus 2.4.2.1 Properties of purine nucleoside phosphorylase from Enterobacter cloacae Micrococcus luteus KY 3760 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 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 Purine nucleoside phosphorylases: properties, functions, and clinical aspects Mus musculus 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 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 Substrate specificity and kinetic mechanism of purine nucleoside phosphorylase from Mycobacterium tuberculosis Mycobacterium tuberculosis 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 Monomeric purine nucleoside phosphorylase from rabbit liver. Purification and characterization Oryctolagus cuniculus 2.4.2.1 Partial purification and properties of purine nucleoside phosphorylase from rabbit erythrocytes Oryctolagus cuniculus 2.4.2.1 Purine nucleoside phosphorylase Oryctolagus cuniculus 2.4.2.1 Purine nucleoside phosphorylase from rabbit liver Oryctolagus cuniculus 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 Purine nucleoside phosphorylase Papio hamadryas 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 Parageobacillus thermoglucosidasius 11955 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 Purifications and properties of orotidine-phosphorolyzing enzyme and purine nucleoside phosphorylase from Erwinia carotovora AJ 2992 Pectobacterium carotovorum 2.4.2.1 Purine nucleoside phosphorylase Pectobacterium carotovorum 2.4.2.1 Purine nucleoside phosphorylases: properties, functions, and clinical aspects 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 1,N6-ethenoadenine and other fluorescent nucleobase analogs as substrates for purine-nucleoside phosphorylases Spectroscopic and kinetic studies Plasmodium falciparum 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 Anopheles gambiae purine nucleoside phosphorylase: catalysis, structure, and inhibition Plasmodium falciparum 2.4.2.1 Attenuated Plasmodium yoelii lacking purine nucleoside phosphorylase confer protective immunity Plasmodium falciparum 2.4.2.1 Behavior of Plasmodium falciparum purine nucleoside phosphorylase in macromolecular crowded environment Plasmodium falciparum 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 Plasmodium falciparum 2.4.2.1 Inhibition and structure of Toxoplasma gondii purine nucleoside phosphorylase Plasmodium falciparum 2.4.2.1 Inhibition and structure of Trichomonas vaginalis purine nucleoside phosphorylase with picomolar transition state analogues Plasmodium falciparum 2.4.2.1 Molecular dynamics studies of a hexameric purine nucleoside phosphorylase Plasmodium falciparum 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 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 phosphorylases: properties, functions, and clinical aspects Plasmodium falciparum 2.4.2.1 Structural determinants of the 5-methylthioinosine specificity of Plasmodium purine nucleoside phosphorylase Plasmodium falciparum 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 Toxoplasma gondii purine nucleoside phosphorylase biochemical characterization, inhibitor profiles, and comparison with the Plasmodium falciparum ortholog Plasmodium falciparum 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 Purine nucleoside phosphorylase of the malarial parasite, Plasmodium lophurae 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 Plasmodium lophurae 2.4.2.1 Purine nucleoside phosphorylases: properties, functions, and clinical aspects Plasmodium lophurae 2.4.2.1 Attenuated Plasmodium yoelii lacking purine nucleoside phosphorylase confer protective immunity Plasmodium yoelii 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 Proteus mirabilis KY4057 2.4.2.1 Purification and characterization of purine nucleoside phosphorylase from Proteus vulgaris Proteus vulgaris 2.4.2.1 Purine nucleoside phosphorylase Proteus vulgaris 2.4.2.1 Purine nucleoside phosphorylases: properties, functions, and clinical aspects Proteus vulgaris 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 Low-molecular-mass purine nucleoside phosphorylase: characterization and application in enzymatic synthesis of nucleoside antiviral drugs 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. 2.4.2.1 Structure-activity relationship of a cold-adapted purine nucleoside phosphorylase by site-directed mutagenesis 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 Characterization of a recombinant cold-adapted purine nucleoside phosphorylase and its application in ribavirin bioconversion Pseudoalteromonas sp. XM2107 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 Thermophilic nucleoside phosphorylases their properties, characteristics and applications Pyrococcus furiosus 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 Purine nucleoside phosphorylases from hyperthermophilic Archaea require a CXC motif for stability and folding 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 Pyrococcus furiosus JCM 8422 2.4.2.1 Thermophilic nucleoside phosphorylases their properties, characteristics and applications Pyrococcus furiosus Vc1 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 Adenosine phosphyorylase activity as distinct from inosine-guanosine phosphorylase activity in Sarcoma 180 cells and rat liver Rattus norvegicus 2.4.2.1 Purine nucleoside phosphorylase Rattus norvegicus 2.4.2.1 Purine nucleoside phosphorylase activity in rat cerebrospinal fluid Rattus norvegicus 2.4.2.1 Purine nucleoside phosphorylase from Salmonella typhimurium and rat liver Rattus norvegicus 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 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 Multiple disulfide bridges modulate conformational stability and flexibility in hyperthermophilic archaeal purine nucleoside phosphorylase Saccharolobus solfataricus 2.4.2.1 Purine nucleoside phosphorylases: properties, functions, and clinical aspects 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 Purine nucleoside phosphorylases: properties, functions, and clinical aspects Saccharomyces cerevisiae 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 Purine nucleoside phosphorylase salmon 2.4.2.1 Purine nucleoside phosphorylase Salmonella enterica subsp. enterica serovar Enteritidis 2.4.2.1 Purification and properties of purine nucleoside phosphorylase from Salmonella typhimurium Salmonella enterica subsp. enterica serovar Typhimurium 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 Salmonella typhimurium and rat liver Salmonella enterica subsp. enterica serovar Typhimurium 2.4.2.1 Purine nucleoside phosphorylases: properties, functions, and clinical aspects Salmonella enterica subsp. enterica serovar Typhimurium 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 Crystal structure of Schistosoma purine nucleoside phosphorylase complexed with a novel monocyclic inhibitor Schistosoma mansoni 2.4.2.1 Immobilized purine nucleoside phosphorylase from Schistosoma mansoni for specific inhibition studies Schistosoma mansoni 2.4.2.1 Isolation and substrate specificity of an adenine nucleoside phosphorylase from adult Schistosoma mansoni Schistosoma mansoni 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 Structures for the potential drug target purine nucleoside phosphorylase from Schistosoma mansoni causal agent of Schistosomiasis Schistosoma mansoni 2.4.2.1 Purification and partial characterization of purine nucleoside phosphorylase from Serratia marcescens Serratia marcescens 2.4.2.1 Purine nucleoside phosphorylases: properties, functions, and clinical aspects Serratia marcescens 2.4.2.1 Purine nucleoside phosphorylase Shewanella putrefaciens 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 Preliminary crystallographic studies of purine nucleoside phosphorylase from the cariogenic pathogen Streptococcus mutans Streptococcus mutans 2.4.2.1 Molecular modeling, dynamics and docking studies of purine nucleoside phosphorylase from Streptococcus pyogenes Streptococcus pyogenes 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 In vitro reconstituted biotransformation of 4-fluorothreonine from fluoride ion: application of the fluorinase Streptomyces cattleya 2.4.2.1 Effects of some modulators on purine nucleoside phosphorylase activity in myocardial tissue Sus scrofa 2.4.2.1 Purine nucleoside phosphorylase Sus scrofa 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 1,N6-ethenoadenine and other fluorescent nucleobase analogs as substrates for purine-nucleoside phosphorylases Spectroscopic and kinetic studies Thermus thermophilus 2.4.2.1 Thermophilic nucleoside phosphorylases their properties, characteristics and applications Thermus thermophilus 2.4.2.1 Crystal structure of purine nucleoside phosphorylase from Thermus thermophilus Thermus thermophilus 2.4.2.1 Thermus thermophilus nucleoside phosphorylases active in the synthesis of nucleoside analogues Thermus thermophilus 2.4.2.1 Unique substrate specificity of purine nucleoside phosphorylases from Thermus thermophilus Thermus thermophilus 2.4.2.1 Thermophilic nucleoside phosphorylases their properties, characteristics and applications Thermus thermophilus ATCC BAA-163 2.4.2.1 Thermophilic nucleoside phosphorylases their properties, characteristics and applications Thermus thermophilus DSM 7039 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 Unique substrate specificity of purine nucleoside phosphorylases from Thermus thermophilus Thermus thermophilus HB8 / ATCC 27634 / DSM 579 2.4.2.1 Inhibition and structure of Toxoplasma gondii purine nucleoside phosphorylase 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 Toxoplasma gondii 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: 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 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 Inhibition and structure of Trichomonas vaginalis purine nucleoside phosphorylase with picomolar transition state analogues Trichomonas vaginalis 2.4.2.1 The purine nucleoside phosphorylase from Trichomonas vaginalis is a homologue of the bacterial enzyme Trichomonas vaginalis 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 phosphorylase and xanthine oxidase activities in erythrocytes and plasma from marine, semiaquatic and terrestrial mammals Tursiops truncatus 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 Xanthomonas campestris KY4208 2.4.2.1 Dynamic expression pattern of distinct genes in the presomitic and somitic mesoderm during Xenopus development Xenopus laevis