Interaction of phosphorylated FcεRIγ immunoglobulin receptor tyrosine activation motif-based peptides with dual and single SH2 domains of p72(syk). Assessment of binding parameters and real time binding kinetics

Journal of Biological Chemistry

Volumn 271, Issue 41, 1996, Pages 25308-25315

  Chen, Ting ^a   Repetto, Barbara ^a   Chizzonite, Richard ^a   Pullar, Christine ^a   Burghardt, Charles ^b   Dharm, Elizabeth ^a   Zhao, Zhicheng ^b   Carroll, Robert ^a   Nunes, Perla ^a   Basu, Mitali ^a   Danho, Waleed ^a   Visnick, Mike ^b   Kochan, Jarema ^b   Waugh, David ^a   Gilfillan, Alasdair M ^a,c  

^a HOFFMANN LA ROCHE INC   (United States)

^b Hoffman La Roche Department of Metabolic Diseases   (United States)

^c Preclinical Dermatology Research   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

FC RECEPTOR; ENZYME PRECURSOR; IMMUNOGLOBULIN E RECEPTOR; PEPTIDE FRAGMENT; PHOSPHOPEPTIDE; PHOSPHOTYROSINE; PRIMER DNA; PROTEIN KINASE SYK; PROTEIN TYROSINE KINASE; RECOMBINANT PROTEIN; SIGNAL PEPTIDE;

ARTICLE; BINDING COMPETITION; CARBOXY TERMINAL SEQUENCE; HUMAN; PRIORITY JOURNAL; PROTEIN PHOSPHORYLATION; PROTEIN PROTEIN INTERACTION; RECEPTOR AFFINITY; RECEPTOR OCCUPANCY; AMINO ACID SEQUENCE; BINDING SITE; CELL LINE; CHEMISTRY; ENZYME LINKED IMMUNOSORBENT ASSAY; KINETICS; MAST CELL; METABOLISM; MOLECULAR GENETICS; NUCLEOTIDE SEQUENCE; PHOSPHORYLATION; POLYMERASE CHAIN REACTION; SITE DIRECTED MUTAGENESIS; SRC HOMOLOGY DOMAIN;

AMINO ACID SEQUENCE; BASE SEQUENCE; BINDING SITES; BINDING, COMPETITIVE; CELL LINE; DNA PRIMERS; ENZYME PRECURSORS; ENZYME-LINKED IMMUNOSORBENT ASSAY; HUMANS; INTRACELLULAR SIGNALING PEPTIDES AND PROTEINS; KINETICS; MAST CELLS; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PEPTIDE FRAGMENTS; PHOSPHOPEPTIDES; PHOSPHORYLATION; PHOSPHOTYROSINE; POLYMERASE CHAIN REACTION; PROTEIN-TYROSINE KINASES; RECEPTORS, IGE; RECOMBINANT PROTEINS; SRC HOMOLOGY DOMAINS;

EID: 10144236517     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.271.41.25308     Document Type: Article

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