GPIHBP1 stabilizes lipoprotein lipase and prevents its inhibition by angiopoietin-like 3 and angiopoietin-like 4

This publication has 41 references indexed in Scilit:

• Chylomicronemia With a Mutant GPIHBP1 (Q115P) That Cannot Bind Lipoprotein Lipase
  Arteriosclerosis, Thrombosis, and Vascular Biology, 2009
• Identification of a New Functional Domain in Angiopoietin-like 3 (ANGPTL3) and Angiopoietin-like 4 (ANGPTL4) Involved in Binding and Inhibition of Lipoprotein Lipase (LPL)
  Journal of Biological Chemistry, 2009
• Abnormal Patterns of Lipoprotein Lipase Release into the Plasma in GPIHBP1-deficient Mice
  Published by Elsevier ,2008
• The Acidic Domain of GPIHBP1 Is Important for the Binding of Lipoprotein Lipase and Chylomicrons
  Journal of Biological Chemistry, 2008
• Six new loci associated with blood low-density lipoprotein cholesterol, high-density lipoprotein cholesterol or triglycerides in humans
  Nature Genetics, 2008
• GPIHBP1: an endothelial cell molecule important for the lipolytic processing of chylomicrons
  Current Opinion in Lipidology, 2007
• Lipid-lowering effects of anti-angiopoietin-like 4 antibody recapitulate the lipid phenotype found in angiopoietin-like 4 knockout mice
  Proceedings of the National Academy of Sciences, 2007
• Glycosylphosphatidylinositol-Anchored High-Density Lipoprotein-Binding Protein 1 Plays a Critical Role in the Lipolytic Processing of Chylomicrons
  Cell Metabolism, 2007
• Population-based resequencing of ANGPTL4 uncovers variations that reduce triglycerides and increase HDL
  Nature Genetics, 2007
• Angiopoietin-like protein 4 converts lipoprotein lipase to inactive monomers and modulates lipase activity in adipose tissue
  Proceedings of the National Academy of Sciences, 2006