Evidence for Two Distinct Binding Sites for Lipoprotein Lipase on Glycosylphosphatidylinositol-anchored High Density Lipoprotein-binding Protein 1 (GPIHBP1)
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference51 articles.
1. Cellular Lipid Metabolism;Olivecrona,2009
2. Biochemistry and pathophysiology of intravascular and intracellular lipolysis;Young;Genes Dev,2013
3. Glycosylphosphatidylinositol-anchored high-density lipoprotein-binding protein 1 plays a critical role in the lipolytic processing of chylomicrons;Beigneux;Cell Metab,2007
4. GPIHBP1 is responsible for the entry of lipoprotein lipase into capillaries;Davies;Cell Metab,2010
5. The acidic domain of GPIHBP1 is important for the binding of lipoprotein lipase and chylomicrons;Gin;J. Biol. Chem,2008
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1. A negatively charged cluster in the disordered acidic domain of GPIHBP1 provides selectivity in the interaction with lipoprotein lipase;Scientific Reports;2024-08-23
2. A negatively charged cluster in the disordered acidic domain of GPIHBP1 provides selectivity in the interaction with lipoprotein lipase;2024-05-09
3. Macromolecular Interactions of Lipoprotein Lipase (LPL);Subcellular Biochemistry;2024
4. Combined action of albumin and heparin regulates lipoprotein lipase oligomerization, stability, and ligand interactions;PLOS ONE;2023-04-12
5. Disorders of Lipid Metabolism;Braun-Falco´s Dermatology;2022
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