Epidermal growth factor receptor tyrosine kinase family members have distinct characteristics that specify their interactions and downstream signaling capabilities. In response to ligand, the receptors dimerize, resulting in activation of their kinase domains. Phosphorylation of specific C-terminal tyrosine residues specifies signal transduction pathways, resulting in mitogenic consequences for the cell. Epidermal growth factor receptors may translocate to the nucleus, initiating transcription.MAb therapeutics may block ligand binding to the ErbB extracellular domain to prevent the conformational changes that promote receptor dimerization. Other MAbs, or a natural compound TNQ, may block dimerization sites in the extracellularanbsp;...
|Title||:||Epidermal Growth Factor Receptor Family Activation and Intracellular Signaling: Implications for Cancer Therapeutics|
|Author||:||Judy M. Richman|
|Publisher||:||ProQuest - 2008|