Human paraoxonases (PON1, PON2, and PON3) are lactonases with overlapping and distinct substrate specificities
about
Interference of bacterial cell-to-cell communication: a new concept of antimicrobial chemotherapy breaks antibiotic resistanceParaoxonase 1 (PON1) as a genetic determinant of susceptibility to organophosphate toxicityLongitudinal changes in PON1 enzymatic activities in Mexican-American mothers and children with different genotypes and haplotypesWhat a Dinner Party! Mechanisms and Functions of Interkingdom Signaling in Host-Pathogen Associations.Mechanisms of Neuroprotection by Quercetin: Counteracting Oxidative Stress and MoreAntioxidant properties of HDLThe human paraoxonase gene cluster as a target in the treatment of atherosclerosisRecent progress in the genetics and epigenetics of paraoxonase: why it is relevant to children's environmental healthInflammation, infection, cancer and all that…the role of paraoxonasesModulation of paraoxonases during infectious diseases and its potential impact on atherosclerosisQuorum quenching revisited--from signal decays to signalling confusionThe enzymes of bacterial census and censorshipParaoxonases as potential antibiofilm agents: their relationship with quorum-sensing signals in Gram-negative bacteriaPON3 is upregulated in cancer tissues and protects against mitochondrial superoxide-mediated cell deathCorrelation between Cholinesterase and Paraoxonase 1 Activities:Case Series of Pesticide Poisoning SubjectsParaoxonase polymorphisms, haplotypes, and enzyme activity in Latino mothers and newbornsHuman paraoxonase-1 (PON1): Gene structure and expression, promiscuous activities and multiple physiological rolesOne enzyme, two functions: PON2 prevents mitochondrial superoxide formation and apoptosis independent from its lactonase activityModulation of paraoxonase 1 and 3 expression after moderate exercise training in the ratFast, Continuous, and High-Throughput (Bio)Chemical Activity Assay for N-Acyl-l-Homoserine Lactone Quorum-Quenching EnzymesParaoxonase 1 and homocysteine metabolism.Paraoxonase 2 decreases renal reactive oxygen species production, lowers blood pressure, and mediates dopamine D2 receptor-induced inhibition of NADPH oxidaseParaoxonases function as unique protectors against cardiovascular diseases and diabetes: Updated experimental and clinical data.In vivo administration of BL-3050: highly stable engineered PON1-HDL complexesNovel Pseudomonas aeruginosa quorum-sensing inhibitors identified in an ultra-high-throughput screen.A metagenomic analysis of soil bacteria extends the diversity of quorum-quenching lactonases.Childhood brain tumors, residential insecticide exposure, and pesticide metabolism genesParaoxonase 2 protein is spatially expressed in the human placenta and selectively reduced in labourHyperthermophilic phosphotriesterases/lactonases for the environment and human health.Evaluation of serum paraoxonase and arylesterase activities in ankylosing spondylitis patientsExploring the role of paraoxonase-2 in bladder cancer: analyses performed on tissue samples, urines and cell cultures.Association analysis of PON2 genetic variants with serum paraoxonase activity and systemic lupus erythematosusQuenching the quorum sensing system: potential antibacterial drug targets.Formation of a vitamin C conjugate of acrolein and its paraoxonase-mediated conversion into 5,6,7,8-tetrahydroxy-4-oxooctanalQuorum quenching agents: resources for antivirulence therapyParaoxonase enzyme protects retinal pigment epithelium from chlorpyrifos insult.Decreased paraoxonase-1 activity is associated with alterations of high-density lipoprotein particles in chronic liver impairmentA systems biology approach to dynamic modeling and inter-subject variability of statin pharmacokinetics in human hepatocytes.High yield expression of an AHL-lactonase from Bacillus sp. B546 in Pichia pastoris and its application to reduce Aeromonas hydrophila mortality in aquaculture.VX hydrolysis by human serum paraoxonase 1: a comparison of experimental and computational results.
P2860
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P2860
Human paraoxonases (PON1, PON2, and PON3) are lactonases with overlapping and distinct substrate specificities
description
2005 nî lūn-bûn
@nan
2005 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
Human paraoxonases (PON1, PON2 ...... stinct substrate specificities
@ast
Human paraoxonases (PON1, PON2 ...... stinct substrate specificities
@en
Human paraoxonases (PON1, PON2 ...... stinct substrate specificities
@en-gb
Human paraoxonases (PON1, PON2 ...... stinct substrate specificities
@nl
type
label
Human paraoxonases (PON1, PON2 ...... stinct substrate specificities
@ast
Human paraoxonases (PON1, PON2 ...... stinct substrate specificities
@en
Human paraoxonases (PON1, PON2 ...... stinct substrate specificities
@en-gb
Human paraoxonases (PON1, PON2 ...... stinct substrate specificities
@nl
prefLabel
Human paraoxonases (PON1, PON2 ...... stinct substrate specificities
@ast
Human paraoxonases (PON1, PON2 ...... stinct substrate specificities
@en
Human paraoxonases (PON1, PON2 ...... stinct substrate specificities
@en-gb
Human paraoxonases (PON1, PON2 ...... stinct substrate specificities
@nl
P2093
P2860
P921
P3181
P1476
Human paraoxonases (PON1, PON2 ...... stinct substrate specificities
@en
P2093
Audrey Speelman
Bert N La Du
Dragomir I Draganov
John F Teiber
Roger Sunahara
Yoichi Osawa
P2860
P304
P3181
P356
10.1194/JLR.M400511-JLR200
P407
P577
2005-06-01T00:00:00Z