The GPIHBP1-LPL complex is responsible for the margination of triglyceride-rich lipoproteins in capillaries.
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Triglyceride-Rich Lipoproteins and Remnants: Targets for Therapy?The ANGPTL3-4-8 model, a molecular mechanism for triglyceride traffickingJCL Roundtable: Hypertriglyceridemia due to defects in lipoprotein lipase functionPalmoplantar Keratoderma in Slurp2-Deficient MiceHigh-resolution imaging of dietary lipids in cells and tissues by NanoSIMS analysis.The tissue distribution of lipoprotein lipase determines where chylomicrons bindEvidence for Two Distinct Binding Sites for Lipoprotein Lipase on Glycosylphosphatidylinositol-anchored High Density Lipoprotein-binding Protein 1 (GPIHBP1).Meta-analysis derived atopic dermatitis (MADAD) transcriptome defines a robust AD signature highlighting the involvement of atherosclerosis and lipid metabolism pathwaysApoc2 loss-of-function zebrafish mutant as a genetic model of hyperlipidemia.The acidic domain of the endothelial membrane protein GPIHBP1 stabilizes lipoprotein lipase activity by preventing unfolding of its catalytic domain.Fatty Acids and Breast Cancer: Make Them on Site or Have Them Delivered.Mobility of "HSPG-bound" LPL explains how LPL is able to reach GPIHBP1 on capillaries.An LPL-specific monoclonal antibody, 88B8, that abolishes the binding of LPL to GPIHBP1.GPIHBP1 and Plasma Triglyceride Metabolism.Angiopoietin-like 4 Modifies the Interactions between Lipoprotein Lipase and Its Endothelial Cell Transporter GPIHBP1.NanoSIMS imaging: an approach for visualizing and quantifying lipids in cells and tissues.A new monoclonal antibody, 4-1a, that binds to the amino terminus of human lipoprotein lipase.The angiopoietin-like protein ANGPTL4 catalyzes unfolding of the hydrolase domain in lipoprotein lipase and the endothelial membrane protein GPIHBP1 counteracts this unfolding.ANGPTL8 promotes the ability of ANGPTL3 to bind and inhibit lipoprotein lipase.Lipoprotein lipase reaches the capillary lumen in chickens despite an apparent absence of GPIHBP1.GPIHBP1: two get tangled.Mutating a conserved cysteine in GPIHBP1 reduces amounts of GPIHBP1 in capillaries and abolishes LPL binding.Apolipoprotein C-III inhibits triglyceride hydrolysis by GPIHBP1-bound LPL.GPIHBP1 autoantibodies in a patient with unexplained chylomicronemia.Hypertriglyceridemia and atherosclerosis.We FRET so You Don't Have To: New Models of the Lipoprotein Lipase Dimer.Lipoprotein Lipase Expression in Chronic Lymphocytic Leukemia: New Insights into Leukemic Progression.Striated muscle gene therapy for the treatment of lipoprotein lipase deficiency.Impaired thermogenesis and sharp increases in plasma triglyceride levels in GPIHBP1-deficient mice during cold exposure.Apolipoprotein C-II: New findings related to genetics, biochemistry, and role in triglyceride metabolism.
P2860
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P2860
The GPIHBP1-LPL complex is responsible for the margination of triglyceride-rich lipoproteins in capillaries.
description
2014 nî lūn-bûn
@nan
2014年の論文
@ja
2014年論文
@yue
2014年論文
@zh-hant
2014年論文
@zh-hk
2014年論文
@zh-mo
2014年論文
@zh-tw
2014年论文
@wuu
2014年论文
@zh
2014年论文
@zh-cn
name
The GPIHBP1-LPL complex is res ...... h lipoproteins in capillaries.
@en
The GPIHBP1-LPL complex is res ...... h lipoproteins in capillaries.
@nl
type
label
The GPIHBP1-LPL complex is res ...... h lipoproteins in capillaries.
@en
The GPIHBP1-LPL complex is res ...... h lipoproteins in capillaries.
@nl
prefLabel
The GPIHBP1-LPL complex is res ...... h lipoproteins in capillaries.
@en
The GPIHBP1-LPL complex is res ...... h lipoproteins in capillaries.
@nl
P2093
P2860
P50
P1433
P1476
The GPIHBP1-LPL complex is res ...... h lipoproteins in capillaries.
@en
P2093
Angelica Tatar
Anne P Beigneux
Chika Nobumori
Chris N Goulbourne
Chris R M Grovenor
Ira J Goldberg
Jeffrey D Esko
Loren G Fong
Oludotun Adeyo
P2860
P304
P356
10.1016/J.CMET.2014.01.017
P577
2014-04-10T00:00:00Z