Do low-affinity ErbB receptor protein interactions represent the base of a cell signaling iceberg?

Expert Review of Proteomics

Volumn 10, Issue 2, 2013, Pages 115-118

  Jones, Richard B ^a  

^a UNIVERSITY OF CHICAGO   (United States)

Author keywords

cell signaling; consensus motifs; ErbB; fluorescence polarization; phosphorylation; phosphotyrosine; protein interactions; protein microarrays; receptor tyrosine kinase; SH2 domains; tyrosine

Indexed keywords

EPIDERMAL GROWTH FACTOR RECEPTOR; FIBROBLAST GROWTH FACTOR RECEPTOR 1; PHOSPHOTYROSINE; PLATELET DERIVED GROWTH FACTOR; PROTEIN SH2; PROTEIN TYROSINE KINASE; REACTIVE OXYGEN METABOLITE; TYROSINE;

AMINO ACID SEQUENCE; AUTOPHOSPHORYLATION; CELL FUNCTION; CONSENSUS SEQUENCE; DISSOCIATION CONSTANT; DISULFIDE BOND; FLUORESCENCE POLARIZATION; HUMAN; IN VITRO STUDY; INTRACELLULAR SIGNALING; LIGAND BINDING; MYRISTYLATION; PEPTIDE LIBRARY; POLARIZATION; PROTEIN INTERACTION; PROTEIN LOCALIZATION; PROTEIN MICROARRAY; PROTEIN PHOSPHORYLATION; REVIEW;

HUMANS; PHOSPHORYLATION; PROTEIN BINDING; RECEPTOR, EPIDERMAL GROWTH FACTOR; SIGNAL TRANSDUCTION;

EID: 84876144805     PISSN: 14789450     EISSN: 17448387     Source Type: Journal    
DOI: 10.1586/epr.12.78     Document Type: Review

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