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Titolo:
Structural models of human apolipoprotein A-I: a critical analysis and review
Autore:
Brouillette, CG; Anantharamaiah, GM; Engler, JA; Borhani, DW;
Indirizzi:
Univ Alabama, Ctr Biophys Sci & Engn, Birmingham, AL 35294 USA Univ Alabama Birmingham AL USA 35294 Sci & Engn, Birmingham, AL 35294 USA Univ Alabama, Atherosclerosis Res Unit, Birmingham, AL 35294 USA Univ Alabama Birmingham AL USA 35294 s Res Unit, Birmingham, AL 35294 USA Univ Alabama, Dept Biochem & Mol Genet, Birmingham, AL 35294 USA Univ Alabama Birmingham AL USA 35294 Mol Genet, Birmingham, AL 35294 USA BASF Biores Corp, Worcester, MA 01605 USA BASF Biores Corp Worcester MA USA 01605 res Corp, Worcester, MA 01605 USA
Titolo Testata:
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR AND CELL BIOLOGY OF LIPIDS
fascicolo: 1-2, volume: 1531, anno: 2001,
pagine: 4 - 46
SICI:
1388-1981(20010330)1531:1-2<4:SMOHAA>2.0.ZU;2-Y
Fonte:
ISI
Lingua:
ENG
Soggetto:
HIGH-DENSITY-LIPOPROTEIN; LECITHIN-CHOLESTEROL-ACYLTRANSFERASE; CORONARY HEART-DISEASE; MOLTEN GLOBULE STATE; SYNTHETIC PEPTIDE ANALOGS; AMPHIPATHIC ALPHA-HELIX; RECEPTOR-BINDING DOMAIN; TRIGLYCERIDE TRANSFER PROTEIN; MIGRATORIA APOLIPOPHORIN-III; SITE-DIRECTED MUTAGENESIS;
Keywords:
apolipoprotein A-I mutant; high density lipoprotein; exchangeable apolipoprotein; apolipoprotein E; apolipophorin III; molten globule; HDL model; lipid binding; protein folding;
Tipo documento:
Review
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
260
Recensione:
Indirizzi per estratti:
Indirizzo: Brouillette, CG Univ Alabama, Ctr Biophys Sci & Engn, 1918 Univ Blvd, Birmingham, AL 35294USA Univ Alabama 1918 Univ Blvd Birmingham AL USA 35294 294USA
Citazione:
C.G. Brouillette et al., "Structural models of human apolipoprotein A-I: a critical analysis and review", BBA-MOL C B, 1531(1-2), 2001, pp. 4-46

Abstract

Human apolipoprotein (apo) A-I has been the subject of intense investigation because of its well-documented antiatherogenic properties. About 70% of the protein found in high density lipoprotein complexes is apo A-I, a molecule that contains a series of highly homologous amphiphatic alpha -helices. A number of significant experimental observations have allowed increasing sophisticated structural models for both the lipid-bound and the lipid-freeforms of the apo A-I molecule to be tested critically. It seems clear, forexample, that interactions between amphipathic domains in apo A-I may be crucial to understanding the dynamic nature of the molecule and the pathwaysby which the lipid-free molecule binds to lipid, both in a discoidal and aspherical particle. The state of the art of these structural studies is discussed and placed in context with current models and concepts of the physiological role of apo A-I and high-density lipoprotein in atherosclerosis and lipid metabolism. (C) 2001 Elsevier Science B.V. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 27/01/20 alle ore 08:00:30