Wong, W T, Schumacher, C, Salcini, A E, Romano, A, Castagnino, P, Pelicci, P G, ...
In this report we structurally and functionally define a binding domain that is involved in protein association and that we have designated EH (for Eps15 homology domain). This domain was identified...
Constitutive phosphorylation of eps8 in tumor cell lines: relevance to malignant transformation.
Matoskova, B, Wong, W T, Salcini, A E, Pelicci, P G, Di Fiore, P P
eps8, a recently identified tyrosine kinase substrate, has been shown to augment epidermal growth factor (EGF) responsiveness, implicating it in EGF receptor (EGFR)-mediated mitogenic signaling. We...
Lotti, L V, Lanfrancone, L, Migliaccio, E, Zompetta, C, Pelicci, G, Salcini, A E, ...
The intracellular localization of Shc proteins was analyzed by immunofluorescence and immunoelectron microscopy in normal cells and cells expressing the epidermal growth factor receptor or the...
Chen, Y, Grall, D, Salcini, A E, Pelicci, P G, Pouysségur, J, Van Obberghen-Schilling, E
The serine protease thrombin activates G protein signaling systems that lead to Ras activation and, in certain cells, proliferation. Whereas the steps leading to Ras activation by G protein-coupled...
Migliaccio, E, Mele, S, Salcini, A E, Pelicci, G, Lai, K M, Superti-Furga, G, ...
Shc proteins are targets of activated tyrosine kinases and are implicated in the transmission of activation signals to Ras. The p46shc and p52shc isoforms share a C-terminal SH2 domain, a proline-...
Recognition specificity of individual EH domains of mammals and yeast.
Paoluzi, S, Castagnoli, L, Lauro, I, Salcini, A E, Coda, L, Fre', S, ...
The Eps homology (EH) domain is a recently described protein binding module that is found, in multiple or single copies, in several proteins in species as diverse as human and yeast. In this work, we...
Wong, W T, Schumacher, C, Salcini, A E, Romano, A, Castagnino, P, Pelicci, P G, ...
In this report we structurally and functionally define a binding domain that is involved in protein association and that we have designated EH (for Eps15 homology domain). This domain was identified...
Constitutive phosphorylation of eps8 in tumor cell lines: relevance to malignant transformation.
Matoskova, B, Wong, W T, Salcini, A E, Pelicci, P G, Di Fiore, P P
eps8, a recently identified tyrosine kinase substrate, has been shown to augment epidermal growth factor (EGF) responsiveness, implicating it in EGF receptor (EGFR)-mediated mitogenic signaling. We...
Lotti, L V, Lanfrancone, L, Migliaccio, E, Zompetta, C, Pelicci, G, Salcini, A E, ...
The intracellular localization of Shc proteins was analyzed by immunofluorescence and immunoelectron microscopy in normal cells and cells expressing the epidermal growth factor receptor or the...
Chen, Y, Grall, D, Salcini, A E, Pelicci, P G, Pouysségur, J, Van Obberghen-Schilling, E
The serine protease thrombin activates G protein signaling systems that lead to Ras activation and, in certain cells, proliferation. Whereas the steps leading to Ras activation by G protein-coupled...
Migliaccio, E, Mele, S, Salcini, A E, Pelicci, G, Lai, K M, Superti-Furga, G, ...
Shc proteins are targets of activated tyrosine kinases and are implicated in the transmission of activation signals to Ras. The p46shc and p52shc isoforms share a C-terminal SH2 domain, a proline-...
Recognition specificity of individual EH domains of mammals and yeast.
Paoluzi, S, Castagnoli, L, Lauro, I, Salcini, A E, Coda, L, Fre', S, ...
The Eps homology (EH) domain is a recently described protein binding module that is found, in multiple or single copies, in several proteins in species as diverse as human and yeast. In this work, we...