Autophosphorylation of the two C-terminal tyrosine residues Tyr1316 and Tyr1322 modulates the activity of the insulin receptor kinase in vitro

FEBS Letters

Volumn 479, Issue 1-2, 2000, Pages 67-71

  Tennagels, Norbert ^a   Bergschneider, Eva ^a   Al Hasani, Hadi ^a   Klein, Helmut W ^a  

^a UNIVERSITY OF COLOGNE   (Germany)

Author keywords

Baculovirus expression system; Insulin receptor kinase; Regulatory function; Serine autophosphorylation

Indexed keywords

INSULIN RECEPTOR; PHOSPHOPEPTIDE; PROTEIN TYROSINE KINASE; TYROSINE;

ARTICLE; AUTOPHOSPHORYLATION; BACULOVIRUS; ENZYME ACTIVITY; ENZYME PURIFICATION; ENZYME SUBSTRATE; GENE EXPRESSION; NONHUMAN; PRIORITY JOURNAL; PROTEIN PHOSPHORYLATION; SIGNAL TRANSDUCTION; SITE DIRECTED MUTAGENESIS;

ANIMALS; BASE SEQUENCE; BINDING SITES; CELL LINE; DNA PRIMERS; KINETICS; MUTAGENESIS, SITE-DIRECTED; PHOSPHORYLATION; PROTEIN STRUCTURE, TERTIARY; RECEPTOR, INSULIN; RECOMBINANT FUSION PROTEINS; SPODOPTERA; TYROSINE;

EID: 0034637506     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0014-5793(00)01879-2     Document Type: Article

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