Hyesung Jeon

Summary

Affiliation: Korea Institute of Science and Technology
Country: Korea

Publications

  1. ncbi request reprint An intramolecular spin of the LDL receptor beta propeller
    Hyesung Jeon
    Department of Pathology, Brigham and Women s Hospital and Harvard Medical School, 75 Francis Street, Boston, MA 02115, USA
    Structure 11:133-6. 2003
  2. ncbi request reprint Global defects in the expression and function of the low density lipoprotein receptor (LDLR) associated with two familial hypercholesterolemia mutations resulting in misfolding of the LDLR epidermal growth factor-AB pair
    Emma J Boswell
    Department of Biochemistry, Division of Structural Biology, University of Oxford, South Parks Road, Oxford OX1 3QU, United Kingdom
    J Biol Chem 279:30611-21. 2004
  3. ncbi request reprint Structure and physiologic function of the low-density lipoprotein receptor
    Hyesung Jeon
    Life Sciences Division, Korea Institute of Science and Technology, Seoul 136 791, Korea
    Annu Rev Biochem 74:535-62. 2005
  4. doi request reprint Cellular uptake mechanism and intracellular fate of hydrophobically modified glycol chitosan nanoparticles
    Hae Yun Nam
    Biomedical Research Center, Korea Institute of Science and Technology, 39 1 Hawolgok Dong, Seongbuk gu, Seoul 136 791, South South Korea
    J Control Release 135:259-67. 2009
  5. ncbi request reprint Cooperation between fixed and low pH-inducible interfaces controls lipoprotein release by the LDL receptor
    Natalia Beglova
    Department of Pathology, Brigham and Women s Hospital and Harvard Medical School, 77 Avenue Louis Pasteur, Boston, MA 02115, USA
    Mol Cell 16:281-92. 2004

Collaborators

  • STEPHEN BLACKLOW
  • Hae Yun Nam
  • Emma J Boswell
  • Natalia Beglova
  • Seung Hae Kwon
  • Kwangmeyung Kim
  • Yoonkyung Kim
  • Joon Kim
  • Songwook Her
  • Seo Young Jeong
  • Jae Hyung Park
  • Seung Young Lee
  • Yu Kyoung Oh
  • Hyunjin Chung
  • Seok Min Kwon
  • Ick Chan Kwon
  • Carl Fisher
  • A Kristina Downing

Detail Information

Publications5

  1. ncbi request reprint An intramolecular spin of the LDL receptor beta propeller
    Hyesung Jeon
    Department of Pathology, Brigham and Women s Hospital and Harvard Medical School, 75 Francis Street, Boston, MA 02115, USA
    Structure 11:133-6. 2003
    ..3, now suggests an elegant model to explain how lipoprotein ligands are released from the receptor by exposure to the low-pH environment of the endosome...
  2. ncbi request reprint Global defects in the expression and function of the low density lipoprotein receptor (LDLR) associated with two familial hypercholesterolemia mutations resulting in misfolding of the LDLR epidermal growth factor-AB pair
    Emma J Boswell
    Department of Biochemistry, Division of Structural Biology, University of Oxford, South Parks Road, Oxford OX1 3QU, United Kingdom
    J Biol Chem 279:30611-21. 2004
    ..The results also highlight a range of misfolding defects that may be associated with familial hypercholesterolemia and may enable the prediction of the consequences of homologous disease-causing mutations to other proteins...
  3. ncbi request reprint Structure and physiologic function of the low-density lipoprotein receptor
    Hyesung Jeon
    Life Sciences Division, Korea Institute of Science and Technology, Seoul 136 791, Korea
    Annu Rev Biochem 74:535-62. 2005
    ....
  4. doi request reprint Cellular uptake mechanism and intracellular fate of hydrophobically modified glycol chitosan nanoparticles
    Hae Yun Nam
    Biomedical Research Center, Korea Institute of Science and Technology, 39 1 Hawolgok Dong, Seongbuk gu, Seoul 136 791, South South Korea
    J Control Release 135:259-67. 2009
    ....
  5. ncbi request reprint Cooperation between fixed and low pH-inducible interfaces controls lipoprotein release by the LDL receptor
    Natalia Beglova
    Department of Pathology, Brigham and Women s Hospital and Harvard Medical School, 77 Avenue Louis Pasteur, Boston, MA 02115, USA
    Mol Cell 16:281-92. 2004
    ..This finely tuned balance between interdomain rigidity and flexibility is likely to represent a shared structural feature in proteins of the LDL receptor family...