GPIHBP1: an endothelial cell molecule important for the lipolytic processing of chylomicrons. - Wikidata - wikimedia - TriplyDB

GPIHBP1: an endothelial cell molecule important for the lipolytic processing of chylomicrons.

GPIHBP1: an endothelial cell molecule important for the lipolytic processing of chylomicrons.

http://www.wikidata.org/entity/Q33923844

about

Chylomicronemia with low postheparin lipoprotein lipase levels in the setting of GPIHBP1 defects Normal binding of lipoprotein lipase, chylomicrons, and apo-AV to GPIHBP1 containing a G56R amino acid substitution Chylomicronemia with a mutant GPIHBP1 (Q115P) that cannot bind lipoprotein lipase GPIHBP1 stabilizes lipoprotein lipase and prevents its inhibition by angiopoietin-like 3 and angiopoietin-like 4 Molecular processes that handle -- and mishandle -- dietary lipids Syndecan-1 is the primary heparan sulfate proteoglycan mediating hepatic clearance of triglyceride-rich lipoproteins in mice The ANGPTL3-4-8 model, a molecular mechanism for triglyceride trafficking The angiopoietin-like proteins ANGPTL3 and ANGPTL4 inhibit lipoprotein lipase activity through distinct mechanisms Influence of apolipoprotein A-V on the metabolic fate of triacylglycerol Lipoprotein lipase activity and mass, apolipoprotein C-II mass and polymorphisms of apolipoproteins E and A5 in subjects with prior acute hypertriglyceridaemic pancreatitis GPIHBP1 and lipolysis: an update.Mechanisms of lipase maturation.Mutation of conserved cysteines in the Ly6 domain of GPIHBP1 in familial chylomicronemia.GPIHBP1 and the processing of triglyceride-rich lipoproteins GPIHBP1, an endothelial cell transporter for lipoprotein lipase.Cholesterol intake modulates plasma triglyceride levels in glycosylphosphatidylinositol HDL-binding protein 1-deficient mice.Binding preferences for GPIHBP1, a glycosylphosphatidylinositol-anchored protein of capillary endothelial cells The acidic domain of GPIHBP1 is important for the binding of lipoprotein lipase and chylomicrons.Lipoprotein lipase: from gene to obesity.Assessing the role of the glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein 1 (GPIHBP1) three-finger domain in binding lipoprotein lipase The tissue distribution of lipoprotein lipase determines where chylomicrons bind Identification and quantitative mRNA analysis of a novel splice variant of GPIHBP1 in dairy cattle.New wrinkles in lipoprotein lipase biology.The expression of GPIHBP1, an endothelial cell binding site for lipoprotein lipase and chylomicrons, is induced by peroxisome proliferator-activated receptor-gamma.GPIHBP1, a GPI-anchored protein required for the lipolytic processing of triglyceride-rich lipoproteins Improved cholesterol phenotype analysis by a model relating lipoprotein life cycle processes to particle size.Highly conserved cysteines within the Ly6 domain of GPIHBP1 are crucial for the binding of lipoprotein lipase.The metabolism of triglyceride-rich lipoproteins revisited: new players, new insight.Diagnosis and treatment of severe hypertriglyceridemia.Oral retinoids and plasma lipids.Glycosylation of Asn-76 in mouse GPIHBP1 is critical for its appearance on the cell surface and the binding of chylomicrons and lipoprotein lipase.Chylomicronaemia--current diagnosis and future therapies.Disorders of lipid metabolism in nephrotic syndrome: mechanisms and consequences.Abnormal patterns of lipoprotein lipase release into the plasma in GPIHBP1-deficient mice.Functional validation of GPIHBP1 and identification of a functional mutation in GPIHBP1 for milk fat traits in dairy cattle GPIHBP1 missense mutations often cause multimerization of GPIHBP1 and thereby prevent lipoprotein lipase binding.Lipoprotein lipase deficiency in chronic kidney disease is accompanied by down-regulation of endothelial GPIHBP1 expression.Lipoprotein lipase reaches the capillary lumen in chickens despite an apparent absence of GPIHBP1.

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GPIHBP1: an endothelial cell molecule important for the lipolytic processing of chylomicrons.

http://www.wikidata.org/entity/Q33923844

description

2007 nî lūn-bûn

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2007 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

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2007 թվականի օգոստոսին հրատարակված գիտական հոդված

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GPIHBP1: an endothelial cell m ...... ic processing of chylomicrons.

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GPIHBP1: an endothelial cell m ...... ic processing of chylomicrons.

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GPIHBP1: an endothelial cell m ...... ic processing of chylomicrons.

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Current Opinion in Lipidology

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GPIHBP1: an endothelial cell m ...... ic processing of chylomicrons.

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Anne P Beigneux

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Brandon S J Davies

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Loren G Fong

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Michael M Weinstein

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Peter Gin

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Stephen G Young

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An apolipoprotein influencing triglycerides in humans and mice revealed by comparative sequencing

Cellular signaling by fibroblast growth factor receptors

Apolipoprotein A-V-heparin interactions: implications for plasma lipoprotein metabolism

Glycosylphosphatidylinositol-anchored high-density lipoprotein-binding protein 1 plays a critical role in the lipolytic processing of chylomicrons

Two independent apolipoprotein A5 haplotypes influence human plasma triglyceride levels

Angiopoietin-like protein 4 converts lipoprotein lipase to inactive monomers and modulates lipase activity in adipose tissue

Identification of scavenger receptor SR-BI as a high density lipoprotein receptor

APOA5 and triglyceride metabolism, lesson from human APOA5 deficiency

Apolipoprotein A-V deficiency results in marked hypertriglyceridemia attributable to decreased lipolysis of triglyceride-rich lipoproteins and removal of their remnants

The fatty liver dystrophy (fld) mutation. A new mutant mouse with a developmental abnormality in triglyceride metabolism and associated tissue-specific defects in lipoprotein lipase and hepatic lipase activities

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18

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