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MiR-193a-3p not only modulated GRB7 but also ERBB4.
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Our results indicated that Grb7 over-expression may facilitate invasion and inhibit apoptosis in cervical cancer
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data shows that GRB7 expression in invasive breast cancer correlates with markers of a more aggressive phenotype, including HER2 overexpression, a greater degree of HER2 amplification, ER negativity, and p53 positivity
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The crystal structure of a stapled bicyclic peptide inhibitor G7-B1 in complex with the Grb7-SH2 domain.
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Grb7 protein Ras-associating domain oligomerization has been reported.
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Study provided a direct link between the signal adapter protein Grb7, anti-apoptotic protein Hax1 isoform 1, and Caspase3-mediated apoptosis pathways, and suggests that besides modulating cell migration and signal transduction, Grb7 may also participate in Hax1-related apoptosis pathways mediated by Caspase3.
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Suggest close relationship between Grb7 gene amplification and GRB7 protein overexpression in human ovarian cancer. Immunohistochemistry might have limited diagnostic value in these tumors compared to fluorescence in situ hybridization.
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Grb7 was found to be significantly related to the biological classification of breast cancer
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apo Grb7 SH2 domain crystallized in the trigonal space group P63, whereas the G7-B1-Grb7 SH2 domain complex crystallized in the monoclinic space group P21
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The data reveal that Grb7 plays an important role in breast cancer progression, beyond the context of HER2+ve cell types
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Grb7 protein interacts with Filamin-a, an actin-crosslinking component of the cell cytoskeleton.
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Data suggest that calmodulin controls Grb7-mediated cell migration.
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Data propose the phosphorylation state of Grb7-SH2 domain tyrosine residues could control Grb7 dimerization, and dimerization may be an important regulatory step in Grb7 binding to RTKs such as erbB2.
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GRB7 is a context-dependent oncogene, which modulates the ERBB2 signaling pathway through enhanced phosphorylation of ERBB2 and Akt.
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propose that CaM inhibits the translocation of Grb7 to the nucleus after binding to its CaM-BD and therefore occluding its overlapping NLS
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A series of Grb7 SH2 domain-binding nonphosphorylated peptides in the yeast two-hybrid system, were identified.
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GRB7 protein over-expression is an independent adverse prognostic factor in human breast cancer
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Full-length Grb7 and Hax-1 interact in mammalian cells and Grb7 is tyrosine phosphorylated.
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X-ray diffraction data were collected from crystals to 2.4A resolution for G7-18NATE in complex with its Grb7 SH2 domain.
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proposed helix-swapping of the SH2 domain of Grb7, a regulatory protein implicated in cancer progression and inflammation
