3.1.8.1 Active site hydrophobicity and the convergent evolution of paraoxonase activity in structurally divergent enzymes the case of serum paraoxonase 1 Oryctolagus cuniculus 3.1.8.1 Alteration of paraoxonase, arylesterase and lactonase activities in people around fluoride endemic area of Tamil Nadu, India Homo sapiens 3.1.8.1 An efficient thermostable organophosphate hydrolase and its application in pesticide decontamination Saccharolobus solfataricus 3.1.8.1 Catalytic efficiencies of directly evolved phosphotriesterase variants with structurally different organophosphorus compounds in vitro Brevundimonas diminuta 3.1.8.1 Cloning of an organophosphorus hydrolase (opdD) gene of Lactobacillus sakei WCP904 isolated from chlorpyrifos-impregnated kimchi and hydrolysis activities of its gene product for organophosphorus pesticides Latilactobacillus sakei 3.1.8.1 Cloning of an organophosphorus hydrolase (opdD) gene of Lactobacillus sakei WCP904 isolated from chlorpyrifos-impregnated kimchi and hydrolysis activities of its gene product for organophosphorus pesticides Latilactobacillus sakei WCP904 3.1.8.1 Conformational disorganization within the active site of a recently evolved organophosphate hydrolase limits its catalytic efficiency Lucilia cuprina 3.1.8.1 Engineering and introduction of de novo disulphide bridges in organophosphorus hydrolase enzyme for thermostability improvement Brevundimonas diminuta 3.1.8.1 Engineering Pseudomonas putida KT2440 for simultaneous degradation of organophosphates and pyrethroids and its application in bioremediation of soil Stenotrophomonas sp. YC-1 3.1.8.1 Expression and purification of biologically active recombinant human paraoxonase 1 from a Drosophila S2 stable cell line Homo sapiens 3.1.8.1 Expression and purification of biologically active recombinant human paraoxonase 1 from inclusion bodies of Escherichia coli Homo sapiens 3.1.8.1 Expression of recombinant organophosphorus hydrolase in the original producer of the enzyme, Sphingobium fuliginis ATCC 27551 Sphingobium fuliginis 3.1.8.1 Extensive hydrolysis of phosphonates as unexpected behaviour of the known His6-organophosphorus hydrolase Homo sapiens 3.1.8.1 Harnessing hyperthermostable lactonase from Sulfolobus solfataricus for biotechnological applications Saccharolobus solfataricus 3.1.8.1 High yield production and purification of two recombinant thermostable phosphotriesterase-like lactonases from Sulfolobus acidocaldarius and Sulfolobus solfataricus useful as bioremediation tools and bioscavengers Sulfolobus acidocaldarius 3.1.8.1 High yield production and purification of two recombinant thermostable phosphotriesterase-like lactonases from Sulfolobus acidocaldarius and Sulfolobus solfataricus useful as bioremediation tools and bioscavengers Saccharolobus solfataricus 3.1.8.1 High-level extracellular secretion of organophosphorous hydrolase of Flavobacterium sp. in Escherichia coli BL21(DE3)pLysS Flavobacterium sp. MTCC 2495 3.1.8.1 Invitro evaluation of the catalytic activity of paraoxonases and phosphotriesterases predicts the enzyme circulatory levels required for invivo protection against organophosphate intoxications Pseudomonas sp. 3.1.8.1 Invitro evaluation of the catalytic activity of paraoxonases and phosphotriesterases predicts the enzyme circulatory levels required for invivo protection against organophosphate intoxications Brevundimonas diminuta 3.1.8.1 Invitro evaluation of the catalytic activity of paraoxonases and phosphotriesterases predicts the enzyme circulatory levels required for invivo protection against organophosphate intoxications Homo sapiens 3.1.8.1 Invitro evaluation of the catalytic activity of paraoxonases and phosphotriesterases predicts the enzyme circulatory levels required for invivo protection against organophosphate intoxications Agrobacterium tumefaciens 3.1.8.1 Multiple reaction products from the hydrolysis of chiral and prochiral organophosphate substrates by the phosphotriesterase from Sphingobium sp. TCM1 Sphingobium sp. TCM1 3.1.8.1 New and highly active microbial phosphotriesterase sources Streptomyces phaeochromogenes 3.1.8.1 New and highly active microbial phosphotriesterase sources Pseudarthrobacter oxydans 3.1.8.1 New and highly active microbial phosphotriesterase sources Nocardia asteroides 3.1.8.1 New and highly active microbial phosphotriesterase sources Streptomyces griseus 3.1.8.1 New and highly active microbial phosphotriesterase sources Rhodococcus corynebacterioides 3.1.8.1 New and highly active microbial phosphotriesterase sources Brevundimonas diminuta 3.1.8.1 New and highly active microbial phosphotriesterase sources Streptomyces phaeochromogenes CCRC 10811 3.1.8.1 New and highly active microbial phosphotriesterase sources Pseudarthrobacter oxydans ATCC 14358 3.1.8.1 New and highly active microbial phosphotriesterase sources Pseudarthrobacter oxydans ATCC 14359 3.1.8.1 New and highly active microbial phosphotriesterase sources Nocardia asteroides ATCC 19296 3.1.8.1 New and highly active microbial phosphotriesterase sources Rhodococcus corynebacterioides ATCC 14898 3.1.8.1 New and highly active microbial phosphotriesterase sources Streptomyces griseus ATCC 39116 3.1.8.1 New chemiluminescent substrates of paraoxonase 1 with improved specificity synthesis and properties Homo sapiens 3.1.8.1 Organophosphate hydrolase interacts with Ton components and is targeted to the membrane only in the presence of the ExbB/ExbD complex Sphingobium fuliginis 3.1.8.1 Organophosphate hydrolase is a lipoprotein and interacts with Pi-specific transport system to facilitate growth of Brevundimonas diminuta using OP insecticide as source of Phosphate Brevundimonas diminuta 3.1.8.1 Paraoxonase 1 Q192R genotype and activity affect homocysteine thiolactone levels in humans Homo sapiens 3.1.8.1 Paraoxonase and arylesterase activities in patients with papillary thyroid cancer Homo sapiens 3.1.8.1 Paraoxonase and arylesterase levels in autoimmune thyroid diseases Homo sapiens 3.1.8.1 Paraoxonase and arylesterase levels in Behcets disease and their relations with the disease activity Homo sapiens 3.1.8.1 Paraoxonase-1 arylesterase activity is an independent predictor of myeloperoxidase levels in overweight patients with or without cardiovascular complications Homo sapiens 3.1.8.1 Rational design of paraoxonase 1 (PON1) for the efficient hydrolysis of organophosphates Oryctolagus cuniculus 3.1.8.1 Rational engineering of a native hyperthermostable lactonase into a broad spectrum phosphotriesterase Saccharolobus solfataricus 3.1.8.1 Serum paraoxonase and arylesterase values as antioxidants in healthy premature infants at fasting and posprandial times Homo sapiens 3.1.8.1 The activities of serum paraoxonase and arylesterase and lipid profile in acute myeloid leukemia preliminary results Homo sapiens 3.1.8.1 The common variant Q192R at the paraoxonase 1 (PON1) gene and its activity are responsible for a portion of the altered antioxidant status in type 2 diabetes Homo sapiens 3.1.8.1 The crystal structure of the phosphotriesterase from M. tuberculosis, another member of phosphotriesterase-like lactonase family Mycobacterium tuberculosis 3.1.8.1 The crystal structure of the phosphotriesterase from M. tuberculosis, another member of phosphotriesterase-like lactonase family Mycobacterium tuberculosis H37Rv 3.1.8.1 The crystal structure of the phosphotriesterase from M. tuberculosis, another member of phosphotriesterase-like lactonase family Mycobacterium tuberculosis ATCC 25618 3.1.8.1 The effect of divalent metal chelators and cadmium on serum phosphotriesterase, lactonase and arylesterase activities of paraoxonase 1 Homo sapiens 3.1.8.1 Theoretical studies on catalysis mechanisms of serum paraoxonase 1 and phosphotriesterase diisopropyl fluorophosphatase suggest the alteration of substrate preference from paraoxonase to DFP Oryctolagus cuniculus 3.1.8.1 Toward understanding the catalytic mechanism of human paraoxonase 1 site-specific mutagenesis at position 192 Homo sapiens 3.1.8.1 Towards understanding the catalytic mechanism of human paraoxonase 1 experimental and in silico mutagenesis studies Homo sapiens 3.1.8.1 Transcriptional regulation of human paraoxonase 1 by nuclear receptors Homo sapiens 3.1.8.1 Transition State Analysis of the Reaction Catalyzed by the Phosphotriesterase from Sphingobium sp. TCM1 Sphingobium sp. TCM1 3.1.8.1 Urinary organophosphate insecticide metabolite concentrations during pregnancy and childrens interpersonal, communication, repetitive, and stereotypic behaviors at 8 years of age the home study Homo sapiens 3.1.8.1 Variants of phosphotriesterase for the enhanced detoxification of the chemical warfare agent VR Brevundimonas diminuta 3.1.8.1 A fluorogenic substrate for detection of organophosphatase activity Homo sapiens 3.1.8.1 A new automated method for phenotyping arylesterase (EC 3.1.1.2) based upon inhibition of enzymatic hydrolysis of 4-nitrophenyl acetate by phenyl acetate Homo sapiens 3.1.8.1 A new phosphotriesterase from Sulfolobus acidocaldarius and its comparison with the homologue from Sulfolobus solfataricus Sulfolobus acidocaldarius 3.1.8.1 A new phosphotriesterase from Sulfolobus acidocaldarius and its comparison with the homologue from Sulfolobus solfataricus Sulfolobus acidocaldarius DSM 639 3.1.8.1 A novel thermostable arylesterase from the archaeon Sulfolobus solfataricus P1: purification, characterization, and expression Saccharolobus solfataricus 3.1.8.1 A novel thermostable arylesterase from the archaeon Sulfolobus solfataricus P1: purification, characterization, and expression Saccharolobus solfataricus P1 3.1.8.1 A thermostable phosphotriesterase from the archaeon Sulfolobus solfataricus: cloning, overexpression and properties Saccharolobus solfataricus 3.1.8.1 A thermostable phosphotriesterase from the archaeon Sulfolobus solfataricus: cloning, overexpression and properties Saccharolobus solfataricus MT-4 / DSM 5833 3.1.8.1 Activity and lifetime of organophosphorous hydrolase (OPH) immobilized using layer-by-layer nano self-assembly on silicon microchannels Homo sapiens 3.1.8.1 Activity of paraoxonase 1 (PON1) and its relationship to markers of lipoprotein oxidation in healthy Slovaks Homo sapiens 3.1.8.1 Age-related paraoxonase activity changes in Turkish population Homo sapiens 3.1.8.1 Altering the substrate specificity of organophosphorus hydrolase for enhanced hydrolysis of chlorpyrifos Escherichia coli K-12 3.1.8.1 Altering the substrate specificity of organophosphorus hydrolase for enhanced hydrolysis of chlorpyrifos Escherichia coli K-12 XL1-Blue 3.1.8.1 Aminopeptidase P mediated detoxification of organophosphonate analogues of sarin: mechanistic and stereochemical study at the phosphorus atom of the substrate Escherichia coli 3.1.8.1 Amphenicol and macrolide derived antibiotics inhibit paraoxonase enzyme activity in human serum and human hepatoma cells (HepG2) in vitro Homo sapiens 3.1.8.1 Analogues with fluorescent leaving groups for screening and selection of enzymes that efficiently hydrolyze organophosphorus nerve agents Brevundimonas diminuta 3.1.8.1 Analogues with fluorescent leaving groups for screening and selection of enzymes that efficiently hydrolyze organophosphorus nerve agents Homo sapiens 3.1.8.1 Analysis of active-site amino-acid residues of human serum paraoxonase using competitive substrates Homo sapiens 3.1.8.1 Anomalous scattering analysis of Agrobacterium radiobacter phosphotriesterase: the prominent role of iron in the heterobinuclear active site Agrobacterium tumefaciens 3.1.8.1 Anti-inflammatory therapy with tumour necrosis factor alpha inhibitors improves high-density lipoprotein cholesterol antioxidative capacity in rheumatoid arthritis patients Homo sapiens 3.1.8.1 Arylesterase and paraoxonase activity of paraoxonase (PON1) affected by ischemia in the plasma of patients with arterial occlusion of the lower limbs Homo sapiens 3.1.8.1 Aspirin is a substrate for paraoxonase-like activity: implications in atherosclerosis Homo sapiens 3.1.8.1 Bacterial cell surface display of organophosphorus hydrolase for selective screening of improved hydrolysis of organophosphate nerve agents Escherichia coli 3.1.8.1 Baculovirus-mediated expression and purification of human serum paraoxonase 1A Homo sapiens 3.1.8.1 Balancing the stability and the catalytic specificities of OP hydrolases with enhanced V-agent activities Brevundimonas diminuta 3.1.8.1 Bimetallic binding motifs in organophosphorus hydrolase are important for catalysis and structural organization Escherichia coli 3.1.8.1 Binding of a designed substrate analogue to diisopropyl fluorophosphatase: implications for the phosphotriesterase mechanism Loligo vulgaris 3.1.8.1 Biodegradation of organophosphate pesticide using recombinant Cyanobacteria with surface- and intracellular-expressed organophosphorus hydrolase Flavobacterium sp. 3.1.8.1 Boosted large-scale production and purification of a thermostable archaeal phosphotriesterase-like lactonase for organophosphate decontamination Saccharolobus solfataricus 3.1.8.1 Boosted large-scale production and purification of a thermostable archaeal phosphotriesterase-like lactonase for organophosphate decontamination Saccharolobus solfataricus DSM 1617 3.1.8.1 Bovine paraoxonase 1 activities in serum and distribution in lipoproteins Bos taurus 3.1.8.1 Calcium binding by human and rabbit serum paraoxonases. Structural stability and enzymic activity Oryctolagus cuniculus 3.1.8.1 Calcium binding by human and rabbit serum paraoxonases. Structural stability and enzymic activity Homo sapiens 3.1.8.1 Catalytic biomaterials: Engineering organophosphate hydrolase to form self-assembling enzymatic hydrogels Flavobacterium sp. 3.1.8.1 Catalytic biomaterials: Engineering organophosphate hydrolase to form self-assembling enzymatic hydrogels Flavobacterium sp. ATCC 27 551 3.1.8.1 Catalytic properties and distribution profiles of paraoxonase and cholinesterase phenotypes in human sera Homo sapiens 3.1.8.1 Catalytic versatility and backups in enzyme active sites: the case of serum paraoxonase 1 synthetic construct 3.1.8.1 Characterisation of the organophosphate hydrolase catalytic activity of SsoPox Saccharolobus solfataricus 3.1.8.1 Characterisation of the organophosphate hydrolase catalytic activity of SsoPox Saccharolobus solfataricus P2 3.1.8.1 Characteristics of the genetically determined allozymic forms of human serum paraoxonase/arylesterase Homo sapiens 3.1.8.1 Characterization of a novel organophosphorus hydrolase from Nocardiodes simplex NRRL B-24074 Pimelobacter simplex 3.1.8.1 Characterization of a phosphotriesterase-like lactonase from Sulfolobus solfataricus and its immobilization for disruption of quorum sensing Saccharolobus solfataricus 3.1.8.1 Characterization of a phosphotriesterase-like lactonase from Sulfolobus solfataricus and its immobilization for disruption of quorum sensing Saccharolobus solfataricus P2 3.1.8.1 Characterization of a phosphotriesterase-like lactonase from the hyperthermoacidophilic crenarchaeon Vulcanisaeta moutnovskia Vulcanisaeta moutnovskia 3.1.8.1 Characterization of cDNA clones encoding rabbit and human serum paraoxonase: the mature protein retains its signal sequence Oryctolagus cuniculus 3.1.8.1 Characterization of cDNA clones encoding rabbit and human serum paraoxonase: the mature protein retains its signal sequence Homo sapiens 3.1.8.1 Characterization of human paraoxonase 1 variants suggest that His residues at 115 and 134 positions are not always needed for the lactonase/arylesterase activities of the enzyme Homo sapiens 3.1.8.1 Characterization of organophosphorus hydrolases and the genetic manipulation of the phosphotriesterase from Pseudomonas diminuta Flavobacterium sp. 3.1.8.1 Characterization of paraoxonase activity in pericardial fluid: usefulness as a marker of coronary disease Homo sapiens 3.1.8.1 Cigarette smoke extract inhibits plasma paraoxonase activity by modification of the enzyme s free thiols Homo sapiens 3.1.8.1 Clinical study on the effect of simvastatin on paraoxonase activity Homo sapiens 3.1.8.1 Comparison of purified human and rabbit serum paraoxonases Oryctolagus cuniculus 3.1.8.1 Comparison of purified human and rabbit serum paraoxonases Homo sapiens 3.1.8.1 Comparison of the ability of paraoxonases 1 and 3 to attenuate the in vitro oxidation of low-density lipoprotein and reduce macrophage oxidative stress Homo sapiens 3.1.8.1 Computational characterization of how the VX nerve agent binds human serum paraoxonase 1 Homo sapiens 3.1.8.1 Consumption of wonderful variety pomegranate juice and extract by diabetic patients increases paraoxonase 1 association with high-density lipoprotein and stimulates its catalytic activities Homo sapiens 3.1.8.1 Crystal structure of VmoLac, a tentative quorum quenching lactonase from the extremophilic crenarchaeon Vulcanisaeta moutnovskia Vulcanisaeta moutnovskia 3.1.8.1 Crystal structure of VmoLac, a tentative quorum quenching lactonase from the extremophilic crenarchaeon Vulcanisaeta moutnovskia Vulcanisaeta moutnovskia 768-28 3.1.8.1 Crystallization and preliminary X-ray diffraction analysis of the hyperthermophilic Sulfolobus islandicus lactonase Sulfolobus islandicus 3.1.8.1 Crystallization and preliminary X-ray diffraction analysis of the hyperthermophilic Sulfolobus islandicus lactonase Sulfolobus islandicus M.16.4 3.1.8.1 Crystallization and preliminary X-ray diffraction analysis of the hyperthermophilic Sulfolobus solfataricus phosphotriesterase Saccharolobus solfataricus 3.1.8.1 Crystallization and preliminary X-ray diffraction analysis of the hyperthermophilic Sulfolobus solfataricus phosphotriesterase Saccharolobus solfataricus MT-4 / DSM 5833 3.1.8.1 Crystallization and preliminary X-ray diffraction analysis of the organophosphorus hydrolase OPHC2 from Pseudomonas pseudoalcaligenes Pseudomonas oleovorans 3.1.8.1 Decreased paraoxonase and arylesterase activities in the pathogenesis of future atherosclerotic heart disease in women with gestational diabetes mellitus Homo sapiens 3.1.8.1 Decreased serum paraoxonase-1 activity during intestinal nematode (Nippostrongylus brasiliensis) infection in rats Rattus norvegicus 3.1.8.1 Decreased stability of the M54 isoform of paraoxonase as a contributory factor to variations in human serum paraoxonase concentrations Homo sapiens 3.1.8.1 Di-oleoyl phosphatidylcholine (PC-18:1) stimulates paraoxonase 1 (PON1) enzymatic and biological activities: in vitro and in vivo studies Mus musculus 3.1.8.1 Differences in the kinetic properties, effect of calcium and sensitivity to inhibitors of paraoxon hydrolase activity in rat plasma and microsomal fraction from rat liver Rattus norvegicus 3.1.8.1 Differential effect of lysophospholipids on activities of human plasma paraoxonase1, either soluble or lipid-bound Homo sapiens 3.1.8.1 Differential effects of some antibiotics on paraoxonase enzyme activity on human hepatoma cells (HepG2) in vitro Homo sapiens 3.1.8.1 Differential hydrolysis of homocysteine thiolactone by purified human serum (192)Q and (192)R PON1 isoenzymes Homo sapiens 3.1.8.1 Direct detection of stereospecific soman hydrolysis by wild-type human serum paraoxonase Homo sapiens 3.1.8.1 Directed evolution of mammalian paraoxonases PON1 and PON3 for bacterial expression and catalytic specialization Homo sapiens 3.1.8.1 Directed evolution of mammalian paraoxonases PON1 and PON3 for bacterial expression and catalytic specialization Mus musculus 3.1.8.1 Directed evolution of mammalian paraoxonases PON1 and PON3 for bacterial expression and catalytic specialization Oryctolagus cuniculus 3.1.8.1 Directed evolution of phosphotriesterase from Pseudomonas diminuta for heterologous expression in Escherichia coli results in stabilization of the metal-free state Brevundimonas diminuta 3.1.8.1 Distinction between A-esterases and arylesterases. Implications for esterase classification Bos taurus 3.1.8.1 Distinction between A-esterases and arylesterases. Implications for esterase classification Felis catus 3.1.8.1 Distinction between A-esterases and arylesterases. Implications for esterase classification Homo sapiens 3.1.8.1 Distinction between A-esterases and arylesterases. Implications for esterase classification Hydrochoerus hydrochaeris 3.1.8.1 Distinction between A-esterases and arylesterases. Implications for esterase classification Meles taxus 3.1.8.1 Distinction between A-esterases and arylesterases. Implications for esterase classification Mus musculus 3.1.8.1 Distinction between A-esterases and arylesterases. Implications for esterase classification no activity in aves 3.1.8.1 Distinction between A-esterases and arylesterases. Implications for esterase classification Rattus norvegicus 3.1.8.1 Distinction between A-esterases and arylesterases. Implications for esterase classification Sus scrofa 3.1.8.1 Distribution and some biochemical properties of rat paraoxonase activity Homo sapiens 3.1.8.1 Distribution and some biochemical properties of rat paraoxonase activity Rattus norvegicus 3.1.8.1 Distribution of paraoxonase-1 gene polymorphisms and enzyme activity in a Peruvian population Homo sapiens 3.1.8.1 Distribution spectrum of paraoxonase activity in HDL fractions Homo sapiens 3.1.8.1 Drosophila are protected from Pseudomonas aeruginosa lethality by transgenic expression of paraoxonase-1 Homo sapiens 3.1.8.1 Dynamic variation in allele-specific gene expression of Paraoxonase-1 in murine and human tissues Mus musculus 3.1.8.1 Effect of organophosphorus hydrolysing enzymes on obidoxime-induced reactivation of organophosphate-inhibited human acetylcholinesterase Brevundimonas diminuta 3.1.8.1 Effect of some analgesics on paraoxonase-1 purified from human serum Homo sapiens 3.1.8.1 Effects of caloric restriction and gender on rat serum paraoxonase 1 activity Rattus norvegicus 3.1.8.1 Effects of some metals on paraoxonase activity from shark Scyliorhinus canicula Scyliorhinus canicula 3.1.8.1 Efficient hydrolysis of the chemical warfare nerve agent tabun by recombinant and purified human and rabbit serum paraoxonase 1 Oryctolagus cuniculus 3.1.8.1 Efficient hydrolysis of the chemical warfare nerve agent tabun by recombinant and purified human and rabbit serum paraoxonase 1 Homo sapiens 3.1.8.1 Engineered recombinant human paraoxonase 1 (rHuPON1) purified from Escherichia coli protects against organophosphate poisoning Homo sapiens 3.1.8.1 Enhanced activity and stability of organophosphorus hydrolase via interaction with an amphiphilic polymer Brevundimonas diminuta 3.1.8.1 Enzymatically active paraoxonase-1 is located at the external membrane of producing cells and released by a high affinity, saturable, desorption mechanism Homo sapiens 3.1.8.1 Evaluation of organophosphorus chemicals-degrading enzymes: a comparison of Escherichia coli and human cytosolic aminopeptidase P Escherichia coli 3.1.8.1 Evaluation of organophosphorus chemicals-degrading enzymes: a comparison of Escherichia coli and human cytosolic aminopeptidase P Homo sapiens 3.1.8.1 Evaluation of paraoxonase and arylesterase activities in Egyptian patients with ankylosing spondylitis Homo sapiens 3.1.8.1 Evidence that several conserved histidine residues are required for hydrolytic activity of human paraoxonase/arylesterase Homo sapiens 3.1.8.1 Expression of organophosphorus hydrolase OPHC2 in Pichia pastoris: purification and characterization Pseudomonas oleovorans 3.1.8.1 Expression of organophosphorus hydrolase OPHC2 in Pichia pastoris: purification and characterization Pseudomonas oleovorans C2-1 3.1.8.1 Expression, purification, and characterization of a novel methyl parathion hydrolase Plesiomonas sp. 3.1.8.1 Expression, purification, and characterization of a novel methyl parathion hydrolase Plesiomonas sp. M6 3.1.8.1 Formation and disposition of diethylphosphoryl-obidoxime, a potent anticholinesterase that is hydrolyzed by human paraoxonase (PON1) Homo sapiens 3.1.8.1 Functional analysis of organophosphorus hydrolase variants with high degradation activity towards organophosphate pesticides Escherichia coli 3.1.8.1 Functional analysis of organophosphorus hydrolase variants with high degradation activity towards organophosphate pesticides Escherichia coli K-12 3.1.8.1 Functional analysis of organophosphorus hydrolase variants with high degradation activity towards organophosphate pesticides Escherichia coli K-12 XL1-Blue 3.1.8.1 Generation of a mutagenized organophosphorus hydrolase for the biodegradation of the organophosphate pesticides malathion and demeton-S Flavobacterium sp. 3.1.8.1 Generation of a mutagenized organophosphorus hydrolase for the biodegradation of the organophosphate pesticides malathion and demeton-S Flavobacterium sp. ATCC 27551 3.1.8.1 Ghrelin, paraoxonase and arylesterase levels in depressive patients before and after citalopram treatment Homo sapiens 3.1.8.1 High affinity, stability, and lactonase activity of serum paraoxonase PON1 anchored on HDL with ApoA-I Homo sapiens 3.1.8.1 High levels of homocysteine and low serum paraoxonase 1 arylesterase activity in children with autism Homo sapiens 3.1.8.1 High-density lipoprotein cholesterol and paraoxonase 1 (PON1) genetics and serum PON1 activity in prepubertal children in Spain Homo sapiens 3.1.8.1 Human liver paraoxonase (PON1): subcellular distribution and characterization Homo sapiens 3.1.8.1 Human paraoxonases (PON1, PON2, and PON3) are lactonases with overlapping and distinct substrate specificities Homo sapiens 3.1.8.1 Human serum paraoxonase (PON1) isozymes Q and R hydrolyze lactones and cyclic carbonate esters Homo sapiens 3.1.8.1 Hyperthermophilic phosphotriesterases/lactonases for the environment and human health Sulfolobus acidocaldarius 3.1.8.1 Hyperthermophilic phosphotriesterases/lactonases for the environment and human health Saccharolobus solfataricus 3.1.8.1 Identification of paraoxonase 3 in rat liver microsomes: purification and biochemical properties Rattus norvegicus 3.1.8.1 Identification of two rat liver proteins with paraoxonase activity: biochemical evidence for the identity of paraoxonase and arylesterase Rattus norvegicus 3.1.8.1 Immunohistochemical analysis of paraoxonases-1, 2, and 3 expression in normal mouse tissues Mus musculus 3.1.8.1 Improved degradation of organophosphorus nerve agents and p-nitrophenol by Pseudomonas putida JS444 with surface-expressed organophosphorus hydrolase Pseudomonas putida 3.1.8.1 Improved degradation of organophosphorus nerve agents and p-nitrophenol by Pseudomonas putida JS444 with surface-expressed organophosphorus hydrolase Pseudomonas putida JS444 3.1.8.1 Improving the promiscuous nerve agent hydrolase activity of a thermostable archaeal lactonase Saccharolobus solfataricus 3.1.8.1 Improving the promiscuous nerve agent hydrolase activity of a thermostable archaeal lactonase Saccharolobus solfataricus P2 3.1.8.1 In crystallo capture of a Michaelis complex and product-binding modes of a bacterial phosphotriesterase Agrobacterium tumefaciens 3.1.8.1 In silico analyses of substrate interactions with human serum paraoxonase 1 Homo sapiens 3.1.8.1 In vitro efficacy of paraoxonase 1 from multiple sources against various organophosphates Oryctolagus cuniculus 3.1.8.1 In vitro efficacy of paraoxonase 1 from multiple sources against various organophosphates Homo sapiens 3.1.8.1 In vitro efficacy of some cattle drugs on bovine serum paraoxonase 1 (PON1) activity Bos taurus 3.1.8.1 In vitro inhibition effect of some dihydroxy coumarin compounds on purified human serum paraoxonase 1 (PON1) Homo sapiens 3.1.8.1 Inactivation of organophosphorus nerve agents by the phosphotriesterase from Pseudomonas diminuta Brevundimonas diminuta 3.1.8.1 Induction of paraoxonase 1 and apolipoprotein A-I gene expression by aspirin Homo sapiens 3.1.8.1 Induction of paraoxonase 1 and apolipoprotein A-I gene expression by aspirin Mus musculus 3.1.8.1 Inhibitory potency against human acetylcholinesterase and enzymatic hydrolysis of fluorogenic nerve agent mimics by human paraoxonase 1 and squid diisopropyl fluorophosphatase Homo sapiens 3.1.8.1 Insertion of an unnatural amino acid into the protein structure: preparation and properties of 3-fluorotyrosine-containing organophosphate hydrolase Brevundimonas diminuta 3.1.8.1 Integrative analytical approach by capillary electrophoresis and kinetics under high pressure optimized for deciphering intrinsic and extrinsic cofactors that modulate activity and stability of human paraoxonase (PON1) Homo sapiens 3.1.8.1 Integrative analytical approach by capillary electrophoresis and kinetics under high pressure optimized for deciphering intrinsic and extrinsic cofactors that modulate activity and stability of human paraoxonase (PON1) synthetic construct 3.1.8.1 Interplay between amino acid residues at positions 192 and 115 in modulating hydrolytic activities of human paraoxonase 1 Homo sapiens 3.1.8.1 Intravenous anesthetics inhibit human paraoxonase-1 (PON1) activity in vitro and in vivo Homo sapiens 3.1.8.1 Investigation of the possible protective role of gallic acid on paraoxanase and arylesterase activities in livers of rats with acute alcohol intoxication Rattus norvegicus 3.1.8.1 L-arginine ameliorates arylesterase/paraoxonase activity of paraoxonase-1 in hypercholesterolemic rats Rattus norvegicus 3.1.8.1 Levels of paraoxonase and arylesterase activities and malondialdehyde in workers exposed to ionizing radiation Homo sapiens 3.1.8.1 Maternal chronic hepatitis B virus is implicated with low neonatal paraoxonase/arylesterase activities Homo sapiens 3.1.8.1 Measurement of paraoxonase (PON1) status as a potential biomarker of susceptibility to organophosphate toxicity Homo sapiens 3.1.8.1 Mechanism for the hydrolysis of organophosphates by the bacterial phosphotriesterase Brevundimonas diminuta 3.1.8.1 Mechanism-based inactivation of phosphotriesterase by reaction of a critical histidine with a ketene intermediate Brevundimonas diminuta 3.1.8.1 Mechanistic insights into the hydrolysis of organophosphorus compounds by paraoxonase-1: exploring the limits of substrate tolerance in a promiscuous enzyme synthetic construct 3.1.8.1 Metabolic engineering of Pseudomonas putida for the utilization of parathion as a carbon and energy source. Pseudomonas putida 3.1.8.1 Metabolic engineering of Pseudomonas putida for the utilization of parathion as a carbon and energy source. Pseudomonas putida KT 2442 3.1.8.1 Mn2+ modulates the kinetic properties of an archaeal member of the PLL family Sulfolobus acidocaldarius 3.1.8.1 Modulation of paraoxonase (PON1) activity Homo sapiens 3.1.8.1 Molecular weight and substrate characteristics of human serum arylesterase following purification by immuno-affinity chromatography Homo sapiens 3.1.8.1 Multiple forms of sheep serum A-esterase activity associated with the high-density lipoprotein Ovis aries 3.1.8.1 Multiple substrates for paraoxonase-1 during oxidation of phosphatidylcholine by peroxynitrite Homo sapiens 3.1.8.1 Nitrite-mediated inactivation of human plasma paraoxonase-1: possible beneficial effect of aromatic amino acids Homo sapiens 3.1.8.1 Novel nucleophiles enhance the human serum paraoxonase 1 (PON1)-mediated detoxication of organophosphates Homo sapiens 3.1.8.1 Novel purification strategy for human PON1 and inhibition of the activity by cephalosporin and aminoglikozide derived antibiotics Homo sapiens 3.1.8.1 Oligomeric states of the detergent-solubilized human serum paraoxonase (PON1) Homo sapiens 3.1.8.1 Organophosphate hydrolase - an enzyme catalyzing degradation of phosphorus-containing toxins and pesticides Brevundimonas diminuta 3.1.8.1 Organophosphate hydrolase - an enzyme catalyzing degradation of phosphorus-containing toxins and pesticides Flavobacterium sp. 3.1.8.1 Organophosphate hydrolase - an enzyme catalyzing degradation of phosphorus-containing toxins and pesticides Rattus norvegicus 3.1.8.1 Organophosphate hydrolases as catalytic bioscavengers of organophosphorus nerve agents Brevundimonas diminuta 3.1.8.1 Organophosphate hydrolases as catalytic bioscavengers of organophosphorus nerve agents Homo sapiens 3.1.8.1 Oxidative inactivation of lactonase activity of purified human paraoxonase 1 (PON1) Homo sapiens 3.1.8.1 Paraoxonase (PON1) polymorphism and activity as the determinants of sensitivity to organophosphates in human subjects Homo sapiens 3.1.8.1 Paraoxonase 1 (PON1) organophosphate hydrolysis is not reduced in ALS Homo sapiens 3.1.8.1 Paraoxonase 1 (PON1) status and substrate hydrolysis Homo sapiens 3.1.8.1 Paraoxonase 1 activities and polymorphisms in autism spectrum disorders Homo sapiens 3.1.8.1 Paraoxonase 1 phenotype distribution and activity differs in subjects with newly diagnosed Type 2 diabetes (the CODAM Study) Homo sapiens 3.1.8.1 Paraoxonase activity against nerve gases measured by capillary electrophoresis and characterization of human serum paraoxonase (PON1) polymorphism in the coding region (Q192R) Homo sapiens 3.1.8.1 Paraoxonase and arylesterase activities in untreated dipper and non-dipper hypertensive patients Homo sapiens 3.1.8.1 Paraoxonase and arylesterase activity and total oxidative/anti-oxidative status in patients with idiopathic Parkinson's disease Homo sapiens 3.1.8.1 Paraoxonase and arylesterase levels in rheumatoid arthritis Homo sapiens 3.1.8.1 Paraoxonase inhibits high-density lipoprotein oxidation and preserves its functions. A possible peroxidative role for paraoxonase Homo sapiens 3.1.8.1 Paraoxonase-1 reduces monocyte chemotaxis and adhesion to endothelial cells due to oxidation of palmitoyl, linoleoyl glycerophosphorylcholine Homo sapiens 3.1.8.1 Paraoxonase-2 is a ubiquitously expressed protein with antioxidant properties and is capable of preventing cell-mediated oxidative modification of low density lipoprotein Homo sapiens 3.1.8.1 Paraoxonase/arylesterase in serum of patients with type II diabetes mellitus Homo sapiens 3.1.8.1 Paraoxonase/arylesterase ratio, PON1 192Q/R polymorphism and PON1 status are associated with increased risk of ischemic stroke Homo sapiens 3.1.8.1 Partial characterization of an enzyme that hydrolyzes sarin, soman, tabun, and diisopropyl phosphorofluoridate (DFP) Rattus norvegicus 3.1.8.1 Partial purification of paraoxonase from rat liver Rattus norvegicus 3.1.8.1 Photonic crystal sensor for organophosphate nerve agents utilizing the organophosphorus hydrolase enzyme Homo sapiens 3.1.8.1 Polymorphisms of paraoxonase (PON1) and their significance in clinical toxicology of organophosphates Homo sapiens 3.1.8.1 PON1 status is influenced by oxidative stress and inflammation in coronary heart disease patients Homo sapiens 3.1.8.1 Preferable stimulation of PON1 arylesterase activity by phosphatidylcholines with unsaturated acyl chains or oxidized acyl chains at sn-2 position Homo sapiens 3.1.8.1 Properties of hexahistidine-tagged organophosphate hydrolase Brevundimonas diminuta 3.1.8.1 Properties of hexahistidine-tagged organophosphate hydrolase Brevundimonas diminuta VKM B-1297 3.1.8.1 Protective efficacy of catalytic bioscavenger, paraoxonase 1 against sarin and soman exposure in guinea pigs Oryctolagus cuniculus 3.1.8.1 Protective efficacy of catalytic bioscavenger, paraoxonase 1 against sarin and soman exposure in guinea pigs Homo sapiens 3.1.8.1 Purification and characterization of a novel organophosphorus pesticide hydrolase from Penicillium lilacinum BP303 Purpureocillium lilacinum 3.1.8.1 Purification and characterization of a novel organophosphorus pesticide hydrolase from Penicillium lilacinum BP303 Purpureocillium lilacinum BP303 3.1.8.1 Purification and characterization of a phosphoric triester hydrolase from the tufted apple bud moth, Platynota idaeusalis (Walker) Platynota idaeusalis 3.1.8.1 Purification and characterization of functional human paraoxonase-1 expressed in Trichoplusia ni larvae Homo sapiens 3.1.8.1 Purification and characterization of paraoxon hydrolase from rat liver Rattus norvegicus 3.1.8.1 Purification and characterization of paraoxonase 1 (PON1) from Swiss Black, Holstein, and Montofon bovines Bos taurus 3.1.8.1 Purification human PON1Q192 and PON1R192 isoenzymes by hydrophobic interaction chromatography and investigation of the inhibition by metals Homo sapiens 3.1.8.1 Purification of His6-organophosphate hydrolase using monolithic supermacroporous polyacrylamide cryogels developed for immobilized metal affinity chromatography Brevundimonas diminuta 3.1.8.1 Purification of Holstein bull semen paraoxonase 1 (PON1) by hydrophobic interaction chromatography and investigation of its inhibition kinetics by heavy metals Bos taurus 3.1.8.1 Purification of human serum paraoxonase/arylesterase. Evidence for one esterase catalyzing both activities Homo sapiens 3.1.8.1 Purification of rabbit and human serum paraoxonase Oryctolagus cuniculus 3.1.8.1 Purification of rabbit and human serum paraoxonase Homo sapiens 3.1.8.1 Purification of two rat hepatic proteins with A-esterase activity toward chlorpyrifos-oxon and paraoxon Rattus norvegicus 3.1.8.1 Rat liver paraoxonase: subcellular distribution and characterization Rattus norvegicus 3.1.8.1 Rational design of organophosphorus hydrolase with high catalytic efficiency for detoxifying a V-type nerve agent Flavobacterium sp. 3.1.8.1 Reconsideration of the catalytic center and mechanism of mammalian paraoxonase/arylesterase Homo sapiens 3.1.8.1 Reduced paraoxonase 1/arylesterase activity and its post-therapeutic increase in obstructive sleep apnea syndrome: A preliminary study Homo sapiens 3.1.8.1 Rhodococcus lactonase with organophosphate hydrolase (OPH) activity and His6-tagged OPH with lactonase activity: evolutionary proximity of the enzymes and new possibilities in their application Rhodococcus ruber 3.1.8.1 Rhodococcus lactonase with organophosphate hydrolase (OPH) activity and His6-tagged OPH with lactonase activity: evolutionary proximity of the enzymes and new possibilities in their application Rhodococcus erythropolis 3.1.8.1 Rhodococcus lactonase with organophosphate hydrolase (OPH) activity and His6-tagged OPH with lactonase activity: evolutionary proximity of the enzymes and new possibilities in their application Rhodococcus ruber AC-1513D 3.1.8.1 Rhodococcus lactonase with organophosphate hydrolase (OPH) activity and His6-tagged OPH with lactonase activity: evolutionary proximity of the enzymes and new possibilities in their application Rhodococcus erythropolis AC-1514D 3.1.8.1 SacPox from the thermoacidophilic crenarchaeon Sulfolobus acidocaldarius is a proficient lactonase Sulfolobus acidocaldarius 3.1.8.1 SacPox from the thermoacidophilic crenarchaeon Sulfolobus acidocaldarius is a proficient lactonase Sulfolobus acidocaldarius DSM 639 3.1.8.1 Serum arylesterase and paraoxonase activity in patients with chronic hepatitis Homo sapiens 3.1.8.1 Serum lipid profile, oxidative status, and paraoxonase 1 activity in hyperemesis gravidarum Homo sapiens 3.1.8.1 Serum paraoxonase (PON1) isozymes: the quantitative analysis of isozymes affecting individual sensitivity to environmental chemicals Homo sapiens 3.1.8.1 Serum paraoxonase and arylesterase activities and oxidative stress levels in patients with SSRI intoxication Homo sapiens 3.1.8.1 Serum paraoxonase and arylesterase activities in esophageal cancer: A controlled study Homo sapiens 3.1.8.1 Serum paraoxonase and arylesterase activities in metabolic syndrome in Zahedan, southeast Iran Homo sapiens 3.1.8.1 Serum paraoxonase and arylesterase activities in patients with epithelial ovarian cancer Homo sapiens 3.1.8.1 Serum paraoxonase and arylesterase activities in patients with lacunar infarction: a case control study Homo sapiens 3.1.8.1 Serum paraoxonase and arylesterase activities in various forms of hepatitis B virus infection Homo sapiens 3.1.8.1 Serum paraoxonase and arylesterase activity and oxidative status in patients with multiple sclerosis Homo sapiens 3.1.8.1 Serum paraoxonase-1 activity in Helicobacter pylori infected subjects Homo sapiens 3.1.8.1 Serum paraoxonase/arylesterase activities in phenylketonuric patients on diet Homo sapiens 3.1.8.1 Solubilization and purification of A-esterase from mouse hepatic microsomes Mus musculus 3.1.8.1 Stability of highly purified human paraoxonase (PON1): Association with human phosphate binding protein (HPBP) is essential for preserving its active conformation(s) Homo sapiens 3.1.8.1 Stabilization of the active form(s) of human paraoxonase by human phosphate-binding protein Homo sapiens 3.1.8.1 Stereo-specific synthesis of analogs of nerve agents and their utilization for selection and characterization of paraoxonase (PON1) catalytic scavengers synthetic construct 3.1.8.1 Stereoselective detoxification of chiral sarin and soman analogues by phosphotriesterase Brevundimonas diminuta 3.1.8.1 Stereoselective hydrolysis of organophosphate nerve agents by the bacterial phosphotriesterase Homo sapiens 3.1.8.1 Structural and enzymatic characterization of the lactonase SisLac from Sulfolobus islandicus Sulfolobus islandicus 3.1.8.1 Structural and enzymatic characterization of the lactonase SisLac from Sulfolobus islandicus Sulfolobus islandicus M.16.4 3.1.8.1 Structural and mutational studies of organophosphorus hydrolase reveal a cryptic and functional allosteric-binding site Brevundimonas diminuta 3.1.8.1 Structural basis for natural lactonase and promiscuous phosphotriesterase activities Saccharolobus solfataricus 3.1.8.1 Structural basis for thermostability revealed through the identification and characterization of a highly thermostable phosphotriesterase-like lactonase from Geobacillus stearothermophilus Geobacillus stearothermophilus 3.1.8.1 Structural basis for thermostability revealed through the identification and characterization of a highly thermostable phosphotriesterase-like lactonase from Geobacillus stearothermophilus Geobacillus stearothermophilus 10 3.1.8.1 Structural determinants of the high thermal stability of SsoPox from the hyperthermophilic archaeon Sulfolobus solfataricus Saccharolobus solfataricus 3.1.8.1 Structural determinants of the high thermal stability of SsoPox from the hyperthermophilic archaeon Sulfolobus solfataricus Saccharolobus solfataricus P2 3.1.8.1 Structure and evolution of the serum paraoxonase family of detoxifying and anti-atherosclerotic enzymes Homo sapiens 3.1.8.1 Structure-reactivity studies of serum paraoxonase PON1 suggest that its native activity is lactonase Homo sapiens 3.1.8.1 Structure/function analyses of human serum paraoxonase (HuPON1) mutants designed from a DFPase-like homology model Homo sapiens 3.1.8.1 Studies on human serum paraoxonase/arylesterase Homo sapiens 3.1.8.1 Substrate specificity of human serum paraoxonase Homo sapiens 3.1.8.1 Synthesis of cholesterol-conjugated magnetic nanoparticles for purification of human paraoxonase 1 Homo sapiens 3.1.8.1 Tandem purification of two HDL-associated partner proteins in human plasma, paraoxonase (PON1) and phosphate binding protein (HPBP) using hydroxyapatite chromatography Homo sapiens 3.1.8.1 The activity of paraoxonase and arylesterase in patients with osteomyelitis Homo sapiens 3.1.8.1 The binding of substrate analogs to phosphotriesterase Brevundimonas diminuta 3.1.8.1 The development of human sera tests for HDL-bound serum PON1 and its lipolactonase activity Homo sapiens 3.1.8.1 The effect of diet on paraoxonase 1/arylesterase activities in patients with disorders of galactose metabolism Homo sapiens 3.1.8.1 The effects of substrate orientation on the mechanism of a phosphotriesterase Agrobacterium tumefaciens 3.1.8.1 The histidine 115-histidine 134 dyad mediates the lactonase activity of mammalian serum paraoxonases Homo sapiens 3.1.8.1 The importance of high-density lipoproteins for paraoxonase-1 secretion, stability, and activity Homo sapiens 3.1.8.1 The importance of high-density lipoproteins for paraoxonase-1 secretion, stability, and activity Mus musculus 3.1.8.1 The role of paraoxonase (PON1) in the detoxication of organophosphates and its human polymorphism Homo sapiens 3.1.8.1 The toxicity of mixtures of specific organophosphate compounds is modulated by paraoxonase 1 status Mus musculus 3.1.8.1 Update on biochemical properties of recombinant Pseudomonas diminuta phosphotriesterase Brevundimonas diminuta 3.1.8.1 Use of OpdA, an organophosphorus (OP) hydrolase, prevents lethality in an African green monkey model of acute OP poisoning Agrobacterium tumefaciens