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Nonphosphorylated peptide ligands for the Grb2 Src homology 2 domain
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Oligino, L.; Lung, F. D. T.; Sastry, L.; Bigelow, J.; Cao, T.; Curran, M.; Burke, T. R., Jr.; Wang, S. M.; Krag, D.; Roller, P. P.; King, C. R. Nonphosphorylated peptide ligands for the Grb2 Src homology 2 domain. J. Biol. Chem. 1997, 272, 29046-29052.
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note
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Absolute configurations of the Pmp residues were not determined unambiguously, rather the L-configuration was assigned to the enantiomer illiciting the more potent inhibition.
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42
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The crystal structures of the SH2 domain of p56(lck) complexed with two phosphonopeptides suggest a gated peptide binding site
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Mikol, V.; Baumann, G.; Keller, T. H.; Manning, U.; Zurini, M. G. M. The crystal structures of the SH2 domain of p56(lck) complexed with two phosphonopeptides suggest a gated peptide binding site. J. Mol. Biol. 1995, 246, 344-355.
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Shahripour, A.; Plummer, M. S.; Lunney, E. A.; Para, K. S.; Stankovic, C. J.; Rubin, J. R.; Humblet, C.; Fergus, J. H.; Marks, J. S.; Herrera, R.; Hubbel, S. E.; Saltiel, A. R.; Sawyer, T. K. Novel phosphotyrosine mimetics in the design of peptide ligands for pp60src SH2 domain. Bioorg. Med. Chem. Lett. 1996, 6, 1209-1214.
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An alternative to phosphotyrosine-containing motifs for binding to an SH2 domain
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Rojas, M.; Yao, S. Y.; Donahue, J. P.; Lin, Y. Z. An alternative to phosphotyrosine-containing motifs for binding to an SH2 domain. Biochem. Biophys. Res. Commun. 1997, 234, 675-680.
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Actinomycin D, C2 and VII, inhibitors of Grb2-Shc interaction produced by streptomyces
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After submission of this manuscript, it was reported that actinomycins are able to potently inhibit Grb2 SH2 domain binding: Nam, J.-Y.; Kim, H.-K.; Son, K.-H.; Kim, S.-U.; Kwon, B.-M.; Han, M. Y.; Chung, Y. J.; Bok, S. H. Actinomycin D, C2 and VII, inhibitors of Grb2-Shc interaction produced by streptomyces. Bioorg. Med. Chem. Lett. 1998, 8, 2001-2002.
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Structural basis for specificity of GRB2-SH2 revealed by a novel ligand binding mode
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Rahuel, J.; Gay, B.; Erdmann, D.; Strauss, A.; GarciaEcheverria, C.; Furet, P.; Caravatti, G.; Fretz, H.; Schoepfer, J.; Grutter, M. G. Structural basis for specificity of GRB2-SH2 revealed by a novel ligand binding mode. Nature Struct. Biol. 1996, 3, 586-589.
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Quantitative analysis of Grb2-Sos1 interaction: The N-terminal SH3 domain of Grb2 mediates affinity
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Sastry, L.; Lin, W. H.; Wong, W. T.; Difiore, P. P.; Scoppa, C. A.; King, C. R. Quantitative analysis of Grb2-Sos1 interaction: The N-terminal SH3 domain of Grb2 mediates affinity. Oncogene 1995, 11, 1107-1112.
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