The central helices of ApoA-I can promote ATP-binding cassette transporter A1 (ABCA1)-mediated lipid efflux. Amino acid residues 220-231 of the wild-type ApoA-I are required for lipid efflux in vitro and high density lipoprotein formation in vivo.
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Molecular interactions between apoE and ABCA1: impact on apoE lipidationStructural Insights into High Density Lipoprotein: Old Models and New FactsNew insights into the determination of HDL structure by apolipoproteins: Thematic review series: high density lipoprotein structure, function, and metabolismThe interaction of ApoA-I and ABCA1 triggers signal transduction pathways to mediate efflux of cellular lipidsStructure and stability of apolipoprotein a-I in solution and in discoidal high-density lipoprotein probed by double charge ablation and deletion mutationAcrolein impairs ATP binding cassette transporter A1-dependent cholesterol export from cells through site-specific modification of apolipoprotein A-I.Disruption of the C-terminal helix by single amino acid deletion is directly responsible for impaired cholesterol efflux ability of apolipoprotein A-I Nichinan.apoE3[K146N/R147W] acts as a dominant negative apoE form that prevents remnant clearance and inhibits the biogenesis of HDL.Analysis of covalent modifications of proteins by oxidized phospholipids using a novel method of peptide enrichment.Influence of apolipoprotein (Apo) A-I structure on nascent high density lipoprotein (HDL) particle size distributionA novel folding intermediate state for apolipoprotein A-I: role of the amino and carboxy terminiMolecular etiology of a dominant form of type III hyperlipoproteinemia caused by R142C substitution in apoE4Carboxyl terminus of apolipoprotein A-I (ApoA-I) is necessary for the transport of lipid-free ApoA-I but not prelipidated ApoA-I particles through aortic endothelial cellsEffect of apoA-I Mutations in the Capacity of Reconstituted HDL to Promote ABCG1-Mediated Cholesterol Efflux.Domains of apoE4 required for the biogenesis of apoE-containing HDL.Alteration of negatively charged residues in the 89 to 99 domain of apoA-I affects lipid homeostasis and maturation of HDL.Apolipoprotein A-I exerts bactericidal activity against Yersinia enterocolitica serotype O:3Site-specific oxidation of apolipoprotein A-I impairs cholesterol export by ABCA1, a key cardioprotective function of HDL.Camphene, a Plant Derived Monoterpene, Exerts Its Hypolipidemic Action by Affecting SREBP-1 and MTP ExpressionApoA-IV promotes the biogenesis of apoA-IV-containing HDL particles with the participation of ABCA1 and LCATThree-dimensional models of HDL apoA-I: implications for its assembly and function.The carboxy-terminal region of apoA-I is required for the ABCA1-dependent formation of alpha-HDL but not prebeta-HDL particles in vivo.Conformational adaptation of apolipoprotein A-I to discretely sized phospholipid complexes.FAMP, a novel apoA-I mimetic peptide, suppresses aortic plaque formation through promotion of biological HDL function in ApoE-deficient miceDiscrete roles of apoA-I and apoE in the biogenesis of HDL species: lessons learned from gene transfer studies in different mouse models.Role of the hydrophobic and charged residues in the 218-226 region of apoA-I in the biogenesis of HDLSignificance of the hydrophobic residues 225-230 of apoA-I for the biogenesis of HDL.Residues Leu261, Trp264, and Phe265 account for apolipoprotein E-induced dyslipidemia and affect the formation of apolipoprotein E-containing high-density lipoprotein.Apolipoprotein A-I mimetic peptide helix number and helix linker influence potentially anti-atherogenic properties.High-Density Lipoprotein Biogenesis: Defining the Domains Involved in Human Apolipoprotein A-I LipidationHDL quality and functionality: what can proteins and genes predict?Advances in high-density lipoprotein physiology: surprises, overturns, and promises.High-density lipoprotein (HDL) metabolism and bone mass.The roles of C-terminal helices of human apolipoprotein A-I in formation of high-density lipoprotein particles.Influence of C-terminal α-helix hydrophobicity and aromatic amino acid content on apolipoprotein A-I functionality.Naturally occurring and bioengineered apoA-I mutations that inhibit the conversion of discoidal to spherical HDL: the abnormal HDL phenotypes can be corrected by treatment with LCAT.Pathway of biogenesis of apolipoprotein E-containing HDL in vivo with the participation of ABCA1 and LCAT.ABCA1 mediates unfolding of apolipoprotein AI N terminus on the cell surface before lipidation and release of nascent high-density lipoprotein.Interaction between the N- and C-terminal domains modulates the stability and lipid binding of apolipoprotein A-I.Cultured gallbladder epithelial cells synthesize apolipoproteins A-I and E.
P2860
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P2860
The central helices of ApoA-I can promote ATP-binding cassette transporter A1 (ABCA1)-mediated lipid efflux. Amino acid residues 220-231 of the wild-type ApoA-I are required for lipid efflux in vitro and high density lipoprotein formation in vivo.
description
2002 nî lūn-bûn
@nan
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
2002年论文
@zh
2002年论文
@zh-cn
name
The central helices of ApoA-I ...... lipoprotein formation in vivo.
@en
type
label
The central helices of ApoA-I ...... lipoprotein formation in vivo.
@en
prefLabel
The central helices of ApoA-I ...... lipoprotein formation in vivo.
@en
P2093
P356
P1476
The central helices of ApoA-I ...... lipoprotein formation in vivo
@en
P2093
Angeliki Chroni
Arnold Von Eckardstein
Horng-Yuan Kan
Yoshinari Uehara
P304
P356
10.1074/JBC.M205232200
P407
P577
2002-12-17T00:00:00Z