Type |
Details |
Score |
GXD Expression |
Probe: |
MGI:5310482 |
Assay Type: |
RNA in situ |
Annotation Date: |
2012-06-12 |
Strength: |
Absent |
Sex: |
Not Specified |
Emaps: |
EMAPS:3599822 |
|
Stage: |
TS22 |
Assay Id: |
MGI:5423805 |
Age: |
embryonic day 14.5 |
|
|
Specimen Label: |
EH955; Specimen C2512 |
Detected: |
false |
Specimen Num: |
1 |
|
•
•
•
•
•
|
GXD Expression |
Probe: |
MGI:5310482 |
Assay Type: |
RNA in situ |
Annotation Date: |
2012-06-12 |
Strength: |
Absent |
Sex: |
Not Specified |
Emaps: |
EMAPS:3280922 |
|
Stage: |
TS22 |
Assay Id: |
MGI:5423805 |
Age: |
embryonic day 14.5 |
|
|
Specimen Label: |
EH955; Specimen C2512 |
Detected: |
false |
Specimen Num: |
1 |
|
•
•
•
•
•
|
GXD Expression |
Probe: |
MGI:5310482 |
Assay Type: |
RNA in situ |
Annotation Date: |
2012-06-12 |
Strength: |
Absent |
Sex: |
Not Specified |
Emaps: |
EMAPS:1833322 |
|
Stage: |
TS22 |
Assay Id: |
MGI:5423805 |
Age: |
embryonic day 14.5 |
|
|
Specimen Label: |
EH955; Specimen C2512 |
Detected: |
false |
Specimen Num: |
1 |
|
•
•
•
•
•
|
GXD Expression |
Probe: |
MGI:5310482 |
Assay Type: |
RNA in situ |
Annotation Date: |
2012-06-12 |
Strength: |
Absent |
Sex: |
Not Specified |
Emaps: |
EMAPS:3287022 |
|
Stage: |
TS22 |
Assay Id: |
MGI:5423805 |
Age: |
embryonic day 14.5 |
|
|
Specimen Label: |
EH955; Specimen C2512 |
Detected: |
false |
Specimen Num: |
1 |
|
•
•
•
•
•
|
GXD Expression |
Probe: |
MGI:5310482 |
Assay Type: |
RNA in situ |
Annotation Date: |
2012-06-12 |
Strength: |
Absent |
Sex: |
Not Specified |
Emaps: |
EMAPS:1752522 |
|
Stage: |
TS22 |
Assay Id: |
MGI:5423805 |
Age: |
embryonic day 14.5 |
|
|
Specimen Label: |
EH955; Specimen C2512 |
Detected: |
false |
Specimen Num: |
1 |
|
•
•
•
•
•
|
GXD Expression |
Probe: |
MGI:5310482 |
Assay Type: |
RNA in situ |
Annotation Date: |
2012-06-12 |
Strength: |
Absent |
Sex: |
Not Specified |
Emaps: |
EMAPS:1821522 |
|
Stage: |
TS22 |
Assay Id: |
MGI:5423805 |
Age: |
embryonic day 14.5 |
|
|
Specimen Label: |
EH955; Specimen C2512 |
Detected: |
false |
Specimen Num: |
1 |
|
•
•
•
•
•
|
GXD Expression |
Probe: |
MGI:5310482 |
Assay Type: |
RNA in situ |
Annotation Date: |
2012-06-12 |
Strength: |
Absent |
Sex: |
Not Specified |
Emaps: |
EMAPS:3557722 |
|
Stage: |
TS22 |
Assay Id: |
MGI:5423805 |
Age: |
embryonic day 14.5 |
|
|
Specimen Label: |
EH955; Specimen C2512 |
Detected: |
false |
Specimen Num: |
1 |
|
•
•
•
•
•
|
GXD Expression |
Probe: |
MGI:5310482 |
Assay Type: |
RNA in situ |
Annotation Date: |
2012-06-12 |
Strength: |
Absent |
Sex: |
Not Specified |
Emaps: |
EMAPS:1702122 |
|
Stage: |
TS22 |
Assay Id: |
MGI:5423805 |
Age: |
embryonic day 14.5 |
|
|
Specimen Label: |
EH955; Specimen C2512 |
Detected: |
false |
Specimen Num: |
1 |
|
•
•
•
•
•
|
GXD Expression |
Probe: |
MGI:5310482 |
Assay Type: |
RNA in situ |
Annotation Date: |
2012-06-12 |
Strength: |
Absent |
Sex: |
Not Specified |
Emaps: |
EMAPS:1756322 |
|
Stage: |
TS22 |
Assay Id: |
MGI:5423805 |
Age: |
embryonic day 14.5 |
|
|
Specimen Label: |
EH955; Specimen C2512 |
Detected: |
false |
Specimen Num: |
1 |
|
•
•
•
•
•
|
GXD Expression |
Probe: |
MGI:5310482 |
Assay Type: |
RNA in situ |
Annotation Date: |
2012-06-12 |
Strength: |
Absent |
Sex: |
Not Specified |
Emaps: |
EMAPS:1668822 |
|
Stage: |
TS22 |
Assay Id: |
MGI:5423805 |
Age: |
embryonic day 14.5 |
|
|
Specimen Label: |
EH955; Specimen C2512 |
Detected: |
false |
Specimen Num: |
1 |
|
•
•
•
•
•
|
GXD Expression |
Probe: |
MGI:5310482 |
Assay Type: |
RNA in situ |
Annotation Date: |
2012-06-12 |
Strength: |
Absent |
Sex: |
Not Specified |
Emaps: |
EMAPS:1757722 |
|
Stage: |
TS22 |
Assay Id: |
MGI:5423805 |
Age: |
embryonic day 14.5 |
|
|
Specimen Label: |
EH955; Specimen C2512 |
Detected: |
false |
Specimen Num: |
1 |
|
•
•
•
•
•
|
GXD Expression |
Probe: |
MGI:5310482 |
Assay Type: |
RNA in situ |
Annotation Date: |
2012-06-12 |
Strength: |
Absent |
Sex: |
Not Specified |
Emaps: |
EMAPS:1757522 |
|
Stage: |
TS22 |
Assay Id: |
MGI:5423805 |
Age: |
embryonic day 14.5 |
|
|
Specimen Label: |
EH955; Specimen C2512 |
Detected: |
false |
Specimen Num: |
1 |
|
•
•
•
•
•
|
GXD Expression |
Probe: |
MGI:5310482 |
Assay Type: |
RNA in situ |
Annotation Date: |
2012-06-12 |
Strength: |
Absent |
Sex: |
Not Specified |
Emaps: |
EMAPS:1738322 |
|
Stage: |
TS22 |
Assay Id: |
MGI:5423805 |
Age: |
embryonic day 14.5 |
|
|
Specimen Label: |
EH955; Specimen C2512 |
Detected: |
false |
Specimen Num: |
1 |
|
•
•
•
•
•
|
GXD Expression |
Probe: |
MGI:5310482 |
Assay Type: |
RNA in situ |
Annotation Date: |
2012-06-12 |
Strength: |
Absent |
Sex: |
Not Specified |
Emaps: |
EMAPS:1802422 |
|
Stage: |
TS22 |
Assay Id: |
MGI:5423805 |
Age: |
embryonic day 14.5 |
|
|
Specimen Label: |
EH955; Specimen C2512 |
Detected: |
false |
Specimen Num: |
1 |
|
•
•
•
•
•
|
GXD Expression |
Probe: |
MGI:5310482 |
Assay Type: |
RNA in situ |
Annotation Date: |
2012-06-12 |
Strength: |
Absent |
Sex: |
Not Specified |
Emaps: |
EMAPS:1768022 |
|
Stage: |
TS22 |
Assay Id: |
MGI:5423805 |
Age: |
embryonic day 14.5 |
|
Note: |
Expression was not detected in the skull (base and vault). |
Specimen Label: |
EH955; Specimen C2512 |
Detected: |
false |
Specimen Num: |
1 |
|
•
•
•
•
•
|
GXD Expression |
Probe: |
MGI:5310482 |
Assay Type: |
RNA in situ |
Annotation Date: |
2012-06-12 |
Strength: |
Absent |
Sex: |
Not Specified |
Emaps: |
EMAPS:2672022 |
|
Stage: |
TS22 |
Assay Id: |
MGI:5423805 |
Age: |
embryonic day 14.5 |
|
Note: |
Expression was not detected in whisker follicle. |
Specimen Label: |
EH955; Specimen C2512 |
Detected: |
false |
Specimen Num: |
1 |
|
•
•
•
•
•
|
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Publication |
First Author: |
Mouse Genome Informatics Scientific Curators |
Year: |
2009 |
Journal: |
Database Download |
Title: |
Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome 430 2.0 Array Platform |
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Publication |
First Author: |
Aharoni A |
Year: |
2004 |
Journal: |
Proc Natl Acad Sci U S A |
Title: |
Directed evolution of mammalian paraoxonases PON1 and PON3 for bacterial expression and catalytic specialization. |
Volume: |
101 |
Issue: |
2 |
Pages: |
482-7 |
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Transgene |
Type: |
transgene |
Organism: |
mouse, laboratory |
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Publication |
First Author: |
Ikhlef S |
Year: |
2017 |
Journal: |
PLoS One |
Title: |
Human paraoxonase 1 overexpression in mice stimulates HDL cholesterol efflux and reverse cholesterol transport. |
Volume: |
12 |
Issue: |
3 |
Pages: |
e0173385 |
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Publication |
First Author: |
Lu J |
Year: |
2013 |
Journal: |
Biochem Biophys Res Commun |
Title: |
Role of paraoxonase-1 in bone anabolic effects of parathyroid hormone in hyperlipidemic mice. |
Volume: |
431 |
Issue: |
1 |
Pages: |
19-24 |
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•
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Publication |
First Author: |
Bradshaw G |
Year: |
2005 |
Journal: |
Proc Natl Acad Sci U S A |
Title: |
Facilitated replacement of Kupffer cells expressing a paraoxonase-1 transgene is essential for ameliorating atherosclerosis in mice. |
Volume: |
102 |
Issue: |
31 |
Pages: |
11029-34 |
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Publication |
First Author: |
Charles-Schoeman C |
Year: |
2020 |
Journal: |
Sci Rep |
Title: |
Suppression of inflammatory arthritis in human serum paraoxonase 1 transgenic mice. |
Volume: |
10 |
Issue: |
1 |
Pages: |
16848 |
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Allele |
Name: |
transgene insertion 1, Roger A Davis |
Allele Type: |
Transgenic |
Attribute String: |
Inserted expressed sequence |
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Strain |
Attribute String: |
coisogenic, mutant strain, transgenic |
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Publication |
First Author: |
Hegele RA |
Year: |
1995 |
Journal: |
Arterioscler Thromb Vasc Biol |
Title: |
A polymorphism of the paraoxonase gene associated with variation in plasma lipoproteins in a genetic isolate. |
Volume: |
15 |
Issue: |
1 |
Pages: |
89-95 |
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•
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Protein Domain |
Type: |
Family |
Description: |
The serum paraoxonases/arylesterases are enzymes that catalyse the hydrolysisof the toxic metabolites of a variety of organophosphorus insecticides. Theenzymes hydrolyse a broad spectrum of organophosphate substrates, including paraoxon and a number of aromatic carboxylic acid esters (e.g., phenylacetate), and hence confer resistance to organophosphate toxicity []. Mammals have 3 distinct paraoxonase types, termed PON1-3 [, ]. In mice andhumans, the PON genes are found on the same chromosome in close proximity. PON activity has been found in variety of tissues, with highest levels in liver and serum - the source of serum PON is thought to be the liver. Unlike mammals, fish and avian species lack paraoxonase activity. Human and rabbit PONs appear to have two distinct Ca2+ binding sites, onerequired for stability and one required for catalytic activity. The Ca2+dependency of PONs suggests a mechanism of hydrolysis where Ca2+ acts as theelectrophillic catalyst, like that proposed for phospholipase A2. Theparaoxonase enzymes, PON1 and PON3, are high density lipoprotein (HDL)-associated proteins capable of preventing oxidative modification of lowdensity lipoproteins (LPL) []. Although PON2 has oxidative properties, theenzyme does not associate with HDL.Within a given species, PON1, PON2 and PON3 share ~60% amino acid sequence identity, whereas between mammalian species particular PONs (1,2 or 3) share79-90% identity at the amino acid level. Human PON1 and PON3 share numerous conserved phosphorylation and N-glycosylation sites; however, it is not known whether the PON proteins are modified at these sites, or whether modification at these sites is required for activity in vivo []. Rabbit and human serum PON1 also hydrolyse a variety oflactones and cycliccarbonate esters, including naturally occurring lactones and pharmacologicalagents []. Humans have 2 common PON1 allozymes, determined by the presenceof either arginine or glutamine at position 191. The A-type allozyme (glutamine at position 191) causes low paraoxonase activity []; thispolymorphism is associated with variations in cholesterol and lipoproteinlevels. |
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Protein Domain |
Type: |
Domain |
Description: |
This family describes a region that is found in proteins expressed by a variety of eukaryotic and prokaryotic species. These proteins include various enzymes, such as senescence marker protein 30 (SMP-30, ), gluconolactonase () and luciferin-regenerating enzyme (LRE, ). SMP-30 is known to hydrolyse diisopropyl phosphorofluoridate in the liver, and has been noted as having sequence similarity, in the region described in this family, with PON1 () and LRE. |
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Publication |
First Author: |
Billecke S |
Year: |
2000 |
Journal: |
Drug Metab Dispos |
Title: |
Human serum paraoxonase (PON1) isozymes Q and R hydrolyze lactones and cyclic carbonate esters. |
Volume: |
28 |
Issue: |
11 |
Pages: |
1335-42 |
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•
•
•
•
|
Protein Domain |
Type: |
Family |
Description: |
The serum paraoxonases/arylesterases are enzymes that catalyse the hydrolysisof the toxic metabolites of a variety of organophosphorus insecticides. Theenzymes hydrolyse a broad spectrum of organophosphate substrates, including paraoxon and a number of aromatic carboxylic acid esters (e.g., phenylacetate), and hence confer resistance to organophosphate toxicity []. Mammals have 3 distinct paraoxonase types, termed PON1-3 [, ]. In mice andhumans, the PON genes are found on the same chromosome in close proximity. PON activity has been found in variety of tissues, with highest levels in liver and serum - the source of serum PON is thought to be the liver. Unlike mammals, fish and avian species lack paraoxonase activity. Human and rabbit PONs appear to have two distinct Ca2+ binding sites, onerequired for stability and one required for catalytic activity. The Ca2+dependency of PONs suggests a mechanism of hydrolysis where Ca2+ acts as theelectrophillic catalyst, like that proposed for phospholipase A2. Theparaoxonase enzymes, PON1 and PON3, are high density lipoprotein (HDL)-associated proteins capable of preventing oxidative modification of lowdensity lipoproteins (LPL) []. Although PON2 has oxidative properties, theenzyme does not associate with HDL.Within a given species, PON1, PON2 and PON3 share ~60% amino acid sequence identity, whereas between mammalian species particular PONs (1,2 or 3) share79-90% identity at the amino acid level. Human PON1 and PON3 share numerous conserved phosphorylation and N-glycosylation sites; however, it is not known whether the PON proteins are modified at these sites, or whether modification at these sites is required for activity in vivo []. |
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Publication |
First Author: |
Ikhlef S |
Year: |
2016 |
Journal: |
FEBS Lett |
Title: |
Paraoxonase 1-treated oxLDL promotes cholesterol efflux from macrophages by stimulating the PPARγ-LXRα-ABCA1 pathway. |
Volume: |
590 |
Issue: |
11 |
Pages: |
1614-29 |
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•
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Publication |
First Author: |
Rodrigo L |
Year: |
1997 |
Journal: |
Biochem J |
Title: |
Purification and characterization of paraoxon hydrolase from rat liver. |
Volume: |
321 ( Pt 3) |
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Pages: |
595-601 |
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Protein Domain |
Type: |
Family |
Description: |
The serum paraoxonases/arylesterases are enzymes that catalyse the hydrolysisof the toxic metabolites of a variety of organophosphorus insecticides. Theenzymes hydrolyse a broad spectrum of organophosphate substrates, including paraoxon and a number of aromatic carboxylic acid esters (e.g., phenylacetate), and hence confer resistance to organophosphate toxicity []. Mammals have 3 distinct paraoxonase types, termed PON1-3 [, ]. In mice andhumans, the PON genes are found on the same chromosome in close proximity. PON activity has been found in variety of tissues, with highest levels in liver and serum - the source of serum PON is thought to be the liver. Unlike mammals, fish and avian species lack paraoxonase activity. Human and rabbit PONs appear to have two distinct Ca2+ binding sites, onerequired for stability and one required for catalytic activity. The Ca2+dependency of PONs suggests a mechanism of hydrolysis where Ca2+ acts as theelectrophillic catalyst, like that proposed for phospholipase A2. Theparaoxonase enzymes, PON1 and PON3, are high density lipoprotein (HDL)-associated proteins capable of preventing oxidative modification of lowdensity lipoproteins (LPL) []. Although PON2 has oxidative properties, theenzyme does not associate with HDL.Within a given species, PON1, PON2 and PON3 share ~60% amino acid sequence identity, whereas between mammalian species particular PONs (1,2 or 3) share79-90% identity at the amino acid level. Human PON1 and PON3 share numerous conserved phosphorylation and N-glycosylation sites; however, it is not known whether the PON proteins are modified at these sites, or whether modification at these sites is required for activity in vivo []. This family consists of arylesterases (Also known as serum paraoxonase) . These enzymes hydrolyse organophosphorus esters such as paraoxon and are found in the liver and blood. They confer resistance to organophosphate toxicity []. Human arylesterase (PON1) is associated with HDL and may protect against LDL oxidation []. |
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Protein |
Organism: |
Mus musculus/domesticus |
Length: |
355
 |
Fragment?: |
false |
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Protein |
Organism: |
Mus musculus/domesticus |
Length: |
181
 |
Fragment?: |
false |
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Protein |
Organism: |
Mus musculus/domesticus |
Length: |
256
 |
Fragment?: |
true |
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Protein |
Organism: |
Mus musculus/domesticus |
Length: |
200
 |
Fragment?: |
false |
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•
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Protein |
Organism: |
Mus musculus/domesticus |
Length: |
108
 |
Fragment?: |
false |
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•
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Protein |
Organism: |
Mus musculus/domesticus |
Length: |
135
 |
Fragment?: |
true |
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•
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Protein |
Organism: |
Mus musculus/domesticus |
Length: |
354
 |
Fragment?: |
false |
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•
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Protein |
Organism: |
Mus musculus/domesticus |
Length: |
354
 |
Fragment?: |
false |
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Publication |
First Author: |
Wang W |
Year: |
2010 |
Journal: |
J Lipid Res |
Title: |
Genetic deletion of apolipoprotein A-I increases airway hyperresponsiveness, inflammation, and collagen deposition in the lung. |
Volume: |
51 |
Issue: |
9 |
Pages: |
2560-70 |
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Publication |
First Author: |
Zamanian-Daryoush M |
Year: |
2020 |
Journal: |
J Biol Chem |
Title: |
Site-specific 5-hydroxytryptophan incorporation into apolipoprotein A-I impairs cholesterol efflux activity and high-density lipoprotein biogenesis. |
Volume: |
295 |
Issue: |
15 |
Pages: |
4836-4848 |
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Publication |
First Author: |
Robert K |
Year: |
2003 |
Journal: |
J Biol Chem |
Title: |
Altered gene expression in liver from a murine model of hyperhomocysteinemia. |
Volume: |
278 |
Issue: |
34 |
Pages: |
31504-11 |
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•
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•
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Publication |
First Author: |
Shih DM |
Year: |
2006 |
Journal: |
J Lipid Res |
Title: |
A role for FXR and human FGF-19 in the repression of paraoxonase-1 gene expression by bile acids. |
Volume: |
47 |
Issue: |
2 |
Pages: |
384-92 |
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Publication |
First Author: |
She ZG |
Year: |
2009 |
Journal: |
Circ Res |
Title: |
Human paraoxonase gene cluster transgenic overexpression represses atherogenesis and promotes atherosclerotic plaque stability in ApoE-null mice. |
Volume: |
104 |
Issue: |
10 |
Pages: |
1160-8 |
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•
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•
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Publication |
First Author: |
Giordano G |
Year: |
2011 |
Journal: |
Toxicol Appl Pharmacol |
Title: |
Paraoxonase 2 (PON2) in the mouse central nervous system: a neuroprotective role? |
Volume: |
256 |
Issue: |
3 |
Pages: |
369-78 |
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Publication |
First Author: |
Ng CJ |
Year: |
2006 |
Journal: |
J Biol Chem |
Title: |
Paraoxonase-2 deficiency aggravates atherosclerosis in mice despite lower apolipoprotein-B-containing lipoproteins: anti-atherogenic role for paraoxonase-2. |
Volume: |
281 |
Issue: |
40 |
Pages: |
29491-500 |
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Publication |
First Author: |
Teiber JF |
Year: |
2018 |
Journal: |
Biochem Biophys Res Commun |
Title: |
Identification of biologically active δ-lactone eicosanoids as paraoxonase substrates. |
Volume: |
505 |
Issue: |
1 |
Pages: |
87-92 |
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•
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Publication |
First Author: |
Belinskaya T |
Year: |
2012 |
Journal: |
Biochim Biophys Acta |
Title: |
Differences in amino acid residues in the binding pockets dictate substrate specificities of mouse senescence marker protein-30, human paraoxonase1, and squid diisopropylfluorophosphatase. |
Volume: |
1824 |
Issue: |
5 |
Pages: |
701-10 |
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•
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•
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Publication |
First Author: |
Khateeb J |
Year: |
2012 |
Journal: |
Arterioscler Thromb Vasc Biol |
Title: |
Urokinase-type plasminogen activator downregulates paraoxonase 1 expression in hepatocytes by stimulating peroxisome proliferator-activated receptor-γ nuclear export. |
Volume: |
32 |
Issue: |
2 |
Pages: |
449-58 |
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Publication |
First Author: |
DeGroot DE |
Year: |
2014 |
Journal: |
Arch Biochem Biophys |
Title: |
Lack of ligand-selective binding of the aryl hydrocarbon receptor to putative DNA binding sites regulating expression of Bax and paraoxonase 1 genes. |
Volume: |
541 |
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Pages: |
13-20 |
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