The acidic domain of GPIHBP1 is important for the binding of lipoprotein lipase and chylomicrons. - Wikidata - wikimedia - TriplyDB

The acidic domain of GPIHBP1 is important for the binding of lipoprotein lipase and chylomicrons.

The acidic domain of GPIHBP1 is important for the binding of lipoprotein lipase and chylomicrons.

http://www.wikidata.org/entity/Q34810602

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Chylomicronemia with a mutant GPIHBP1 (Q115P) that cannot bind lipoprotein lipase GPIHBP1 is responsible for the entry of lipoprotein lipase into capillaries GPIHBP1 stabilizes lipoprotein lipase and prevents its inhibition by angiopoietin-like 3 and angiopoietin-like 4 Evaluation and treatment of hypertriglyceridemia: an Endocrine Society clinical practice guideline The Role of Cdkn1A-Interacting Zinc Finger Protein 1 (CIZ1) in DNA Replication and Pathophysiology Glycosylphosphatidylinositol-anchored high-density lipoprotein-binding protein 1 and the intravascular processing of triglyceride-rich lipoproteins Apolipoprotein A-V dependent modulation of plasma triacylglycerol: a puzzlement Influence of apolipoprotein A-V on the metabolic fate of triacylglycerol GPIHBP1 and lipolysis: an update.Treatment options for hypertriglyceridemia: from risk reduction to pancreatitis.Deletion of the basement membrane heparan sulfate proteoglycan type XVIII collagen causes hypertriglyceridemia in mice and humans GPIHBP1 and the processing of triglyceride-rich lipoproteins GPIHBP1, an endothelial cell transporter for lipoprotein lipase.Intravenous injection of apolipoprotein A-V reconstituted high-density lipoprotein decreases hypertriglyceridemia in apoav-/- mice and requires glycosylphosphatidylinositol-anchored high-density lipoprotein-binding protein 1.Binding preferences for GPIHBP1, a glycosylphosphatidylinositol-anchored protein of capillary endothelial cells Equivalent binding of wild-type lipoprotein lipase (LPL) and S447X-LPL to GPIHBP1, the endothelial cell LPL transporter.Genetic determinants of plasma triglycerides Mutations in lipoprotein lipase that block binding to the endothelial cell transporter GPIHBP1 Assessing the role of the glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein 1 (GPIHBP1) three-finger domain in binding lipoprotein lipase Identification and quantitative mRNA analysis of a novel splice variant of GPIHBP1 in dairy cattle.MZF-1/Elk-1 Complex Binds to Protein Kinase Cα Promoter and Is Involved in Hepatocellular Carcinoma.Evidence for Two Distinct Binding Sites for Lipoprotein Lipase on Glycosylphosphatidylinositol-anchored High Density Lipoprotein-binding Protein 1 (GPIHBP1).Deletion of GPIHBP1 causing severe chylomicronemia Chylomicronemia mutations yield new insights into interactions between lipoprotein lipase and GPIHBP1 New wrinkles in lipoprotein lipase biology.Assessing mechanisms of GPIHBP1 and lipoprotein lipase movement across endothelial cells.The acidic domain of the endothelial membrane protein GPIHBP1 stabilizes lipoprotein lipase activity by preventing unfolding of its catalytic domain.Biochemistry and pathophysiology of intravascular and intracellular lipolysis.Structural and functional analysis of APOA5 mutations identified in patients with severe hypertriglyceridemia.GPIHBP1, a GPI-anchored protein required for the lipolytic processing of triglyceride-rich lipoproteins 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.MZF-1/Elk-1 interaction domain as therapeutic target for protein kinase Cα-based triple-negative breast cancer cells The role of apolipoprotein A5 in obesity and the metabolic syndrome.Monoclonal antibodies that bind to the Ly6 domain of GPIHBP1 abolish the binding of LPL.Mobility of "HSPG-bound" LPL explains how LPL is able to reach GPIHBP1 on capillaries.GPIHBP1 and Plasma Triglyceride Metabolism.Emerging strategies of targeting lipoprotein lipase for metabolic and cardiovascular diseases.Apolipoprotein A-V associates with intrahepatic lipid droplets and influences triglyceride accumulation.Effects of the prosegment and pH on the activity of PCSK9: evidence for additional processing events.

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P2860

The acidic domain of GPIHBP1 is important for the binding of lipoprotein lipase and chylomicrons.

http://www.wikidata.org/entity/Q34810602

description

2008 nî lūn-bûn

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2008 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2008 թվականի օգոստոսին հրատարակված գիտական հոդված

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2008年の論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年论文

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name

The acidic domain of GPIHBP1 i ...... otein lipase and chylomicrons.

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The acidic domain of GPIHBP1 i ...... otein lipase and chylomicrons.

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The acidic domain of GPIHBP1 i ...... otein lipase and chylomicrons.

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The acidic domain of GPIHBP1 i ...... otein lipase and chylomicrons.

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The acidic domain of GPIHBP1 i ...... otein lipase and chylomicrons.

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The acidic domain of GPIHBP1 i ...... otein lipase and chylomicrons.

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The acidic domain of GPIHBP1 i ...... otein lipase and chylomicrons.

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The acidic domain of GPIHBP1 i ...... otein lipase and chylomicrons.

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Journal of Biological Chemistry

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The acidic domain of GPIHBP1 i ...... otein lipase and chylomicrons.

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P2093

Anne P Beigneux

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Brandon S J Davies

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Liya Yin

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Loren G Fong

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Michael M Weinstein

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Peter Gin

http://www.w3.org/2001/XMLSchema#string

Stephen G Young

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P2860

Apolipoprotein A-V interaction with members of the low density lipoprotein receptor gene family

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

Crystal structure of the human urokinase plasminogen activator receptor bound to an antagonist peptide

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

Structure-function studies of human apolipoprotein A-V: a regulator of plasma lipid homeostasis

Animal cell mutants defective in glycosaminoglycan biosynthesis

Expression cloning and characterization of a novel glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein, GPI-HBP1

Identification of specific sites involved in ligand binding by photoaffinity labeling of the receptor for the urokinase-type plasminogen activator. Residues located at equivalent positions in uPAR domains I and III participate in the assembly of a c

Contribution of the carboxy-terminal domain of lipoprotein lipase to interaction with heparin and lipoproteins.

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

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29554-29562

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scholarly article

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10.1074/JBC.M802579200

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P433

43

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P478

283

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P50

André Bensadoun

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2008-08-18T00:00:00Z

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P698

18713736

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P932

2662032

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