Conformation of apolipoprotein E both in free and in lipid-bound form may determine the avidity of triglyceride-rich lipoproteins to the LDL receptor: Structural and kinetic study

Biochimica et Biophysica Acta - Molecular and Cell Biology of Lipids

Volumn 1484, Issue 1, 2000, Pages 14-28

  Dergunov, Alexander D ^a   Smirnova, Elizaveta A ^a   Merched, Aksam ^b   Visvikis, Sophie ^b   Siest, Gerard ^b   Yakushkin, Vladimir V ^c   Tsibulsky, Vladimir ^c  

^a NATIONAL MEDICAL RESEARCH CENTER FOR THERAPY AND PREVENTIVE MEDICINE   (Russian Federation)

^b Centre de Medecine Preventive   (France)

^c INSTITUTE OF EXPERIMENTAL CARDIOLOGY   (Russian Federation)

Author keywords

Apolipoprotein B; Apolipoprotein E; Hydrophobic interaction; Low density lipoprotein; Low density lipoprotein receptor; Protein structure and refolding; Self association; Very low density lipoprotein

Indexed keywords

APOLIPOPROTEIN B; APOLIPOPROTEIN E; LOW DENSITY LIPOPROTEIN; LOW DENSITY LIPOPROTEIN RECEPTOR; PHOSPHATIDYLCHOLINE; VERY LOW DENSITY LIPOPROTEIN;

ARTICLE; BINDING AFFINITY; CONTROLLED STUDY; HUMAN; HUMAN TISSUE; HYDROPHOBICITY; MOLECULAR INTERACTION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE;

APOLIPOPROTEINS E; HUMANS; KINETICS; LIPOPROTEINS, LDL; LIPOPROTEINS, VLDL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FOLDING; RECEPTORS, LDL; SOLUTIONS; TEMPERATURE; TRIGLYCERIDES;

EID: 0033950685     PISSN: 13881981     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1388-1981(99)00196-1     Document Type: Article

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