The activation of growth factor receptors induces phosphorylation of tyrosine residues in its
C-terminal part, creating binding sites for SH2 domain-containing proteins. Grb2 is a protein …

Background: Growth factor receptor–bound protein 2 (GRB2) is an adaptor protein with three
Src homology (SH) domains in the order SH3–SH2–SH3. Both SH3 domains of GRB2 are …

Critical intracellular signals in normal and malignant cells are transmitted by the adaptor
protein Grb2 by means of its Src homology 2 (SH2) domain, which binds to phosphotyrosyl …

GRB2 is a small adaptor protein of 217 amino acids comprising one SH2 domain
surrounded by two SH3 domains. GRB2 couples receptor tyrosine kinase activation to Ras …

Growth factor receptor-bound protein 2 (GRB2) is a trivalent adaptor protein and a key
element in signal transduction. It interacts via its flanking nSH3 and cSH3 domains with the …

Previous efforts in the search for molecules capable of blocking the associations between
the activated tyrosine kinase growth factor receptors and the SH2 domain of Grb2 had …

Anarchic cell proliferation, observed in some leukemia and in breast and ovarian cancers,
has been related to dysfunctioning of cytoplasmic or receptor tyrosine kinase activities …

Highly potent inhibitors of the Grb2-SH2 domain have been synthesized. They share the
common sequence: Ac-Pmp-Ac6c-Asn-NH-(3-indolyl-propyl). Different substituents at the 3 …

Grb2, composed entirely of SH2 and SH3 domains, serves as an adaptor protein in
signaling from growth factor-activated tyrosine kinase receptors. It interacts via its SH2 …

Growth factor receptor-bound protein 2 (Grb2) is an extensively studied adaptor protein
involved in cell signaling. Grb2 is a highly flexible protein composed of a single SH2 domain …