Expression and one-step purification of active lipoprotein lipase contemplated by biophysical considerations.

[1]  A. Remaley,et al.  A VLP-based vaccine targeting ANGPTL3 lowers plasma triglycerides in mice. , 2021, Vaccine.

[2]  D. Ng.  Evolving ANGPTL-based lipid-lowering strategies and beyond. , 2021, Current opinion in lipidology.

[3]  S. Young,et al.  GPIHBP1 and ANGPTL4 Utilize Protein Disorder to Orchestrate Order in Plasma Triglyceride Metabolism and Regulate Compartmentalization of LPL Activity , 2021, Frontiers in Cell and Developmental Biology.

[4]  P. Duell,et al.  Evinacumab for treatment of familial hypercholesterolemia , 2021, Expert review of cardiovascular therapy.

[5]  S. Young,et al.  ANGPTL4 sensitizes lipoprotein lipase to PCSK3 cleavage by catalyzing its unfolding , 2021, Journal of lipid research.

[6]  S. Young,et al.  The intrinsic instability of the hydrolase domain of lipoprotein lipase facilitates its inactivation by ANGPTL4-catalyzed unfolding , 2021, Proceedings of the National Academy of Sciences.

[7]  R. Hegele,et al.  Genetics of Hypertriglyceridemia , 2020, Frontiers in Endocrinology.

[8]  J. Luz,et al.  The structural basis for monoclonal antibody 5D2 binding to the tryptophan-rich loop of lipoprotein lipase , 2020, Journal of Lipid Research.

[9]  F. V. van’t Hooft,et al.  Angiopoietin-like protein 8 differentially regulates ANGPTL3 and ANGPTL4 during postprandial partitioning of fatty acids , 2020, Journal of Lipid Research.

[10]  M. Borgnia,et al.  The structure of helical lipoprotein lipase reveals an unexpected twist in lipase storage , 2020, Proceedings of the National Academy of Sciences.

[11]  S. Young,et al.  Unfolding of monomeric lipoprotein lipase by ANGPTL4: Insight into the regulation of plasma triglyceride metabolism , 2020, Proceedings of the National Academy of Sciences.

[12]  S. Neher,et al.  Endoplasmic reticulum quality control in lipoprotein metabolism , 2019, Molecular and Cellular Endocrinology.

[13]  C. Burd,et al.  Syndecan-1 Mediates Sorting of Soluble Lipoprotein Lipase with Sphingomyelin-Rich Membrane in the Golgi Apparatus. , 2019, Developmental cell.

[14]  J. Trauger,et al.  A lipoprotein lipase–GPI-anchored high-density lipoprotein–binding protein 1 fusion lowers triglycerides in mice: Implications for managing familial chylomicronemia syndrome , 2019, The Journal of Biological Chemistry.

[15]  S. Young,et al.  GPIHBP1 and Lipoprotein Lipase, Partners in Plasma Triglyceride Metabolism. , 2019, Cell metabolism.

[16]  Thomas M. Smith,et al.  Structure of lipoprotein lipase in complex with GPIHBP1 , 2019, Proceedings of the National Academy of Sciences.

[17]  S. Young,et al.  Lipoprotein lipase is active as a monomer , 2019, Proceedings of the National Academy of Sciences.

[18]  S. Young,et al.  Structure of the lipoprotein lipase–GPIHBP1 complex that mediates plasma triglyceride hydrolysis , 2018, Proceedings of the National Academy of Sciences.

[19]  S. Neher,et al.  Coexpression of novel furin-resistant LPL variants with lipase maturation factor 1 enhances LPL secretion and activity[S] , 2018, Journal of Lipid Research.

[20]  D. Salzig,et al.  Single-cell cloning enables the selection of more productive Drosophila melanogaster S2 cells for recombinant protein expression , 2018, Biotechnology reports.

[21]  S. Young,et al.  A disordered acidic domain in GPIHBP1 harboring a sulfated tyrosine regulates lipoprotein lipase , 2018, Proceedings of the National Academy of Sciences.

[22]  S. Shetty,et al.  ANGPTL8 promotes the ability of ANGPTL3 to bind and inhibit lipoprotein lipase , 2017, Molecular metabolism.

[23]  D. Gaudet,et al.  Clinical and biochemical features of different molecular etiologies of familial chylomicronemia. , 2017, Journal of clinical lipidology.

[24]  S. Young,et al.  Autoantibodies against GPIHBP1 as a Cause of Hypertriglyceridemia , 2017, The New England journal of medicine.

[25]  S. Young,et al.  The angiopoietin-like protein ANGPTL4 catalyzes unfolding of the hydrolase domain in lipoprotein lipase and the endothelial membrane protein GPIHBP1 counteracts this unfolding , 2016, eLife.

[26]  S. Young,et al.  The acidic domain of the endothelial membrane protein GPIHBP1 stabilizes lipoprotein lipase activity by preventing unfolding of its catalytic domain , 2016, eLife.

[27]  S. Young,et al.  GPIHBP1 Missense Mutations Often Cause Multimerization of GPIHBP1 and Thereby Prevent Lipoprotein Lipase Binding , 2015, Circulation research.

[28]  L. Scott.  Alipogene Tiparvovec: A Review of Its Use in Adults with Familial Lipoprotein Lipase Deficiency , 2015, Drugs.

[29]  Sang J. Chung,et al.  Intrinsic Tryptophan Fluorescence in the Detection and Analysis of Proteins: A Focus on Förster Resonance Energy Transfer Techniques , 2014, International journal of molecular sciences.

[30]  S. Young,et al.  The GPIHBP1-LPL complex is responsible for the margination of triglyceride-rich lipoproteins in capillaries. , 2014, Cell metabolism.

[31]  S. Young,et al.  Mutations in lipoprotein lipase that block binding to the endothelial cell transporter GPIHBP1 , 2011, Proceedings of the National Academy of Sciences.

[32]  S. Young,et al.  GPIHBP1 is responsible for the entry of lipoprotein lipase into capillaries. , 2010, Cell metabolism.

[33]  P. Pajukanta,et al.  Mutations in LMF1 cause combined lipase deficiency and severe hypertriglyceridemia , 2007, Nature Genetics.

[34]  S. Young,et al.  Glycosylphosphatidylinositol-anchored high-density lipoprotein-binding protein 1 plays a critical role in the lipolytic processing of chylomicrons. , 2007, Cell metabolism.

[35]  M. Ploug,et al.  A new tagging system for production of recombinant proteins in Drosophila S2 cells using the third domain of the urokinase receptor. , 2007, Protein expression and purification.

[36]  N. Seidah,et al.  Proprotein Covertases Are Responsible for Proteolysis and Inactivation of Endothelial Lipase* , 2005, Journal of Biological Chemistry.

[37]  Finn Werner,et al.  Characterization of low-glycosylated forms of soluble human urokinase receptor expressed in Drosophila Schneider 2 cells after deletion of glycosylation-sites. , 2004, Protein expression and purification.

[38]  M. Panteghini,et al.  Measurement of pancreatic lipase activity in serum by a kinetic colorimetric assay using a new chromogenic substrate , 2001, Annals of clinical biochemistry.

[39]  J. Brunzell,et al.  Detailed characterization of the binding site of the lipoprotein lipase-specific monoclonal antibody 5D2. , 1998, Journal of lipid research.

[40]  M. Ploug,et al.  Cell‐induced potentiation of the plasminogen activation system is abolished by a monoclonal antibody that recognizes the NH2‐terminal domain of the urokinase receptor , 1991, FEBS letters.

[41]  T. Olivecrona,et al.  Binding of active and inactive forms of lipoprotein lipase to heparin. Effects of pH. , 1985, The Biochemical journal.

[42]  T. Olivecrona,et al.  Lipoprotein lipase. Mechanism of product inhibition. , 1980, European journal of biochemistry.

[43]  P. Iverius,et al.  Lipoprotein lipase from bovine milk. Isolation procedure, chemical characterization, and molecular weight analysis. , 1976, The Journal of biological chemistry.

[44]  R. S. Gordon,et al.  Idiopathic hyperlipemia: metabolic studies in an affected family. , 1960, The Journal of clinical investigation.

[45]  P. Hahn.  ABOLISHMENT OF ALIMENTARY LIPEMIA FOLLOWING INJECTION OF HEPARIN. , 1943, Science.

[46]  T. Olivecrona,et al.  Phospholipase activity of milk lipoprotein lipase. , 1991, Methods in enzymology.

[47]  A. Yamamoto,et al.  Purification and characterization of lipoprotein lipase from human postheparin plasma and its comparison with purified bovine milk lipoprotein lipase. , 1986, Journal of biochemistry.