individual publications

• academic article

  • Assessing the role of the glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein 1 (GPIHBP1) three-finger domain in binding lipoprotein lipase.  Journal of Biological Chemistry.  286:19735-19743. 2011
  • Binding preferences for GPIHBP1, a glycosylphosphatidylinositol-anchored protein of capillary endothelial cells.  Arteriosclerosis Thrombosis and Vascular Biology.  31:176-182. 2011
  • GPIHBP1, an endothelial cell transporter for lipoprotein lipase.  Journal of Lipid Research.  52:1869-1884. 2011
  • Mutations in lipoprotein lipase that block binding to the endothelial cell transporter GPIHBP1.  Proceedings of the National Academy of Sciences of the United States of America.  108:7980-7984. 2011
  • Cholesterol Intake modulates plasma triglyceride levels in GPIHBP1-deficient mice.  Arteriosclerosis Thrombosis and Vascular Biology.  30:2106-2013. 2010
  • Chylomicronemia with low postheparin lipoprotein lipase levels in the setting of GPIHBP1 defects.  Circulation: Cardiovascular Genetics.  3:169-178. 2010
  • GPIHBP1 is responsible for the entry of lipoprotein lipase in capillaries.  Cell Metabolism.  12:42-52. 2010
  • Unexpected expression pattern for glycosylphosphatidylinositol-anchored HDL-binding protein1 (GPIHBP1) in mouse tissues revealed by positron emission tomography scanning.  Journal of Biological Chemistry.  285:39239-39248. 2010
  • GPIHBP1 and lipolysis: an update.  Current Opinion in Lipidology.  20:211-216. 2009
  • GPIHBP1, a GPI-anchored protein required for lipolytic processing of triglyceride-rich lipoproteins.  Journal of Lipid Research.  . 2009
  • Highly conserved cysteines within the Ly6 domain of GPIHBP1 are crucial for the binding of lipoprotein lipase.  Journal of Biological Chemistry.  284:30240-30247. 2009
  • Abnormal patterns of lipoprotein lipase release into plasma in GPIHBP1-deficient mice.  Journal of Biological Chemistry.  283:34511-34518. 2008
  • Glycosylation of Ans-76 in mouse GPIHBP1 is critical for its appearance on the cell surface and the binding of chylomicrons and lipoprotein lipase.  Journal of Lipid Research.  49:1312-1321. 2008
  • The acidic domain of GPIHBP1 is important for the binding of lipoprotein lipase and chylomicrons.  Journal of Biological Chemistry.  283:29554-29562. 2008
  • GPIHBP1: an endothelial cell molecule important for the lipolytic processing of chylomicrons.  Current Opinion in Lipidology.  18:389-96. 2007
  • Glycosylphosphatidylinositol-Anchored High-density Lipoprotein –Binding Protein 1 plays a critical role in the lipolytic processing of chylomicrons.  Cell Metabolism.  5:279-291. 2007
  • Normal binding of lipoprotein lipase, chylomicrons, and apo-AV to GPIHBP1 containing a G56R amino acid substitution.  Biochimica et Biophysica Acta.  1771:1464-1468. 2007

• chapter

  • New developments in the lipolytic processing of triglyceride-rich lipoproteins.  Adipose Tissue in Health and Disease. 2010
  • Lipoprotein Size and Susceptibility to Atherosclerosis—Insights from Genetically Modified Mouse Models.  In Murine Atherosclerosis. 2007
  • New Developments in the Lipolytic Processing of Triglyceride-rich Lipoproteins.  In Adipose Tissue in Health and Disease. 2007

• document part

  • Two mutations in GPIHBP1 cause severe chylomicronemia and provide evidence for a critical role of GPIHBP1 in human triglyceride metabolism 2009
  • Two mutations in GPIHBP1 cause severe chylomicronemia and provide evidence for a critical role of GPIHBP1 in human triglyceride metabolism 2009