Differential Utilization of ShcA Tyrosine Residues and Functional Domains in the Transduction of Epidermal Growth Factor-induced Mitogen-activated Protein Kinase Activation in 293T Cells and Nerve Growth Factor-induced Neurite Outgrowth in PC12 Cells

This publication has 35 references indexed in Scilit:

• The Shc adaptor protein is highly phosphorylated at conserved, twin tyrosine residues (Y239/240) that mediate protein–protein interactions
  Current Biology, 1996
• Functional Roles of the Shc Phosphotyrosine Binding and Src Homology 2 Domains in Insulin and Epidermal Growth Factor Signaling
  Published by Elsevier ,1996
• Functional Importance of Amino-terminal Domain of Shc for Interaction with Insulin and Epidermal Growth Factor Receptors in Phosphorylation-independent Manner
  Published by Elsevier ,1996
• Insulin and Epidermal Growth Factor Receptors Regulate Distinct Pools of Grb2-SOS in the Control of Ras Activation
  Published by Elsevier ,1996
• Systematic Mapping of Potential Binding Sites for Shc and Grb2 SH2 Domains on Insulin Receptor Substrate-1 and the Receptors for Insulin, Epidermal Growth Factor, Platelet-derived Growth Factor, and Fibroblast Growth Factor
  Published by Elsevier ,1996
• Binding of Shc to the NPXY Motif Is Mediated by Its N-terminal Domain
  Published by Elsevier ,1995
• A conserved amino-terminal Shc domain binds to phosphotyrosine motifs in activated receptors and phosphopeptides
  Current Biology, 1995
• Membrane targeting of the nucleotide exchange factor Sos is sufficient for activating the Ras signaling pathway
  Cell, 1994
• The Function of GRB2 in Linking the Insulin Receptor to Ras Signaling Pathways
  Science, 1993
• A novel transforming protein (SHC) with an SH2 domain is implicated in mitogenic signal transduction
  Cell, 1992