Conserved C-terminal residues within the lectin-like domain of LOX-1 are essential for oxidized low-density-lipoprotein binding

Biochemical Journal

Volumn 355, Issue 2, 2001, Pages 289-296

  Chen, M ^a   Narumiya, S ^a   Masaki, T ^a   Sawamura, T ^a  

^a OSAKA UNIVERSITY   (Japan)

Author keywords

Epitope mapping; Lectin like oxidized LDL receptor 1; Monoclonal antibody

Indexed keywords

AMINO ACIDS; ANTIBODIES; CELLS;

BINDING ACTIVITY;

PROTEINS;

ALANINE; LECTIN; LOW DENSITY LIPOPROTEIN RECEPTOR; LYSINE; MONOCLONAL ANTIBODY; OXIDIZED LOW DENSITY LIPOPROTEIN;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMAL CELL; ANIMAL TISSUE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; GENE DELETION; GENE DISRUPTION; GENE EXPRESSION; HUMAN; HUMAN CELL; MOLECULAR CLONING; MOLECULAR RECOGNITION; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; SEQUENCE ANALYSIS;

AMINO ACID SEQUENCE; ANIMALS; BASE SEQUENCE; BLOTTING, WESTERN; DNA, COMPLEMENTARY; EPITOPE MAPPING; HUMANS; LECTINS; LIPOPROTEINS, LDL; MOLECULAR SEQUENCE DATA; MUTAGENESIS; PROTEIN BINDING; RECEPTORS, LDL; RECEPTORS, OXIDIZED LDL; SCAVENGER RECEPTORS, CLASS E; SEQUENCE DELETION; SEQUENCE HOMOLOGY, AMINO ACID; SWINE;

EID: 0035871224     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/0264-6021:3550289     Document Type: Article

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