title: A complete backbone spectral assignment of lipid-free human apolipoprotein E (apoE).
abstract: Apolipoprotein E is an exchangeable apolipoprotein that plays an important role in lipid/lipoprotein metabolism and cardiovascular diseases. Recent evidence indicates that apoE is also critical in several other important biological processes, including Alzheimer's disease, cognitive function, immunoregulation, cell signaling and infectious diseases. Although the X-ray crystal structure of the apoE N-terminal domain was solved in 1991, there is no structure available for the apoE C-terminal domain and full-length apoE. Here we report a complete NMR backbone spectral assignment of lipid-free human apoE.
authors.affiliation: Department of Biochemistry and Molecular Biology, School of Medicine, Wayne State University, Detroit, MI 48201, USA.
authors.forename: Yonghong
authors.initials: Y
authors.lastname: Zhang
authors.forename: Jianglei
authors.initials: J
authors.lastname: Chen
authors.forename: Jianjun
authors.initials: J
authors.lastname: Wang
mesh_terms: D000595:Amino Acid Sequence; D001057:Apolipoproteins E / Q000737:chemistry*; D002247:Carbon Isotopes / Q000737:chemistry; D006801:Humans; D008055:Lipids / Q000737:chemistry; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009587:Nitrogen Isotopes / Q000737:chemistry; D017434:Protein Structure, Tertiary; D011522:Protons
chemical_list: D001057:Apolipoproteins E; D002247:Carbon Isotopes; D008055:Lipids; D009587:Nitrogen Isotopes; D011522:Protons