The α-helical domain near the amino terminus is essential for dimerization of vascular endothelial growth factor

Journal of Biological Chemistry

Volumn 273, Issue 18, 1998, Pages 11115-11120

  Siemeister, Gerhard ^a   Marmé, Dieter ^a   Martiny Baron, Georg ^a  

^a TUMOR BIOLOGY CENTER   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

VASCULOTROPIN RECEPTOR;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ANGIOGENESIS; ARTICLE; BINDING AFFINITY; BLOOD VESSEL PERMEABILITY; CELL PROLIFERATION; CHO CELL; DIABETIC RETINOPATHY; DIMERIZATION; ENDOTHELIUM CELL; ESCHERICHIA COLI; GENETIC TRANSFECTION; HYDROPHOBICITY; PRIORITY JOURNAL; PROTEIN ANALYSIS; SITE DIRECTED MUTAGENESIS;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMALS; CHO CELLS; CRICETINAE; DIMERIZATION; ENDOTHELIAL GROWTH FACTORS; ESCHERICHIA COLI; LYMPHOKINES; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; VASCULAR ENDOTHELIAL GROWTH FACTOR A; VASCULAR ENDOTHELIAL GROWTH FACTORS;

CRICETINAE; CRICETULUS GRISEUS; ESCHERICHIA COLI;

EID: 0032079869     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.273.18.11115     Document Type: Article

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