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Volumn 349, Issue 2, 2006, Pages 497-503

Structure-based design of potent Grb2-SH2 domain antagonists not relying on phosphotyrosine mimics

Author keywords

Cyclic peptides; d Alanine; G1TE analogs; Grb2 SH2 antagonist; Grb2 SH2 domain; Non phosphotyrosine; Tyrosine kinase

Indexed keywords

AMINO ACID; CYCLOPEPTIDE; EPIDERMAL GROWTH FACTOR RECEPTOR 2; GLYCINE; GROWTH FACTOR RECEPTOR BOUND PROTEIN 2 ANTAGONIST; LEUCINE; PHOSPHOTYROSINE; PROTEIN G1TE; PROTEIN SH2; RAS PROTEIN; UNCLASSIFIED DRUG;

EID: 33748434738     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2006.08.059     Document Type: Article
Times cited : (11)

References (40)
  • 1
    • 0028252996 scopus 로고
    • The Grb family of SH2 domain proteins
    • Margolis B. The Grb family of SH2 domain proteins. Prog. Biophys. Mol. Biol. 62 (1994) 223-244
    • (1994) Prog. Biophys. Mol. Biol. , vol.62 , pp. 223-244
    • Margolis, B.1
  • 2
    • 0029584473 scopus 로고
    • Dominant-negative mutants of Grb2 induced reversal of the transformed phenotypes caused by the point mutation-activated rat HER-2/Neu
    • Xie Y., Pendergast A.M., and Hung M.C. Dominant-negative mutants of Grb2 induced reversal of the transformed phenotypes caused by the point mutation-activated rat HER-2/Neu. J. Biol. Chem. 270 (1995) 30717-30724
    • (1995) J. Biol. Chem. , vol.270 , pp. 30717-30724
    • Xie, Y.1    Pendergast, A.M.2    Hung, M.C.3
  • 3
    • 0033545371 scopus 로고    scopus 로고
    • Growth inhibition of breast cancer cells by Grb2 downregulation is correlated with inactivation of mitogen-activated protein kinase in EGFR, but not in ErbB2, cells
    • Tari A.M., Hung M.C., Li K., and Lopez-Berestein G. Growth inhibition of breast cancer cells by Grb2 downregulation is correlated with inactivation of mitogen-activated protein kinase in EGFR, but not in ErbB2, cells. Oncogene 18 (1999) 1325-1332
    • (1999) Oncogene , vol.18 , pp. 1325-1332
    • Tari, A.M.1    Hung, M.C.2    Li, K.3    Lopez-Berestein, G.4
  • 4
    • 0033866182 scopus 로고    scopus 로고
    • Overexpression of Grb2 in inflammatory lesions and preneoplastic foci and tumors induced by N-nitrosodimethylamine in Helicobacter hepaticus-infected and noninfected A/J mice
    • Diwan B.A., Ramakrishna G., Anderson L.M., and Ramljak D. Overexpression of Grb2 in inflammatory lesions and preneoplastic foci and tumors induced by N-nitrosodimethylamine in Helicobacter hepaticus-infected and noninfected A/J mice. Toxicol. Pathol. 28 (2000) 548-554
    • (2000) Toxicol. Pathol. , vol.28 , pp. 548-554
    • Diwan, B.A.1    Ramakrishna, G.2    Anderson, L.M.3    Ramljak, D.4
  • 5
    • 0033809911 scopus 로고    scopus 로고
    • Up-regulation of the protein tyrosine phosphatase SHP-1 in human breast cancer and correlation with GRB2 expression
    • Yip S.S., and Daly R.J. Up-regulation of the protein tyrosine phosphatase SHP-1 in human breast cancer and correlation with GRB2 expression. Int. J. Cancer. 88 (2000) 363-368
    • (2000) Int. J. Cancer. , vol.88 , pp. 363-368
    • Yip, S.S.1    Daly, R.J.2
  • 7
    • 0028000009 scopus 로고
    • Activation of the Ras signalling pathway in human breast cancer cells overexpressing erbB-2
    • Janes P.W., Daly R.J., de Fazio A., and Sutherland R.L. Activation of the Ras signalling pathway in human breast cancer cells overexpressing erbB-2. Oncogene 9 (1994) 3601-3608
    • (1994) Oncogene , vol.9 , pp. 3601-3608
    • Janes, P.W.1    Daly, R.J.2    de Fazio, A.3    Sutherland, R.L.4
  • 8
    • 12844283323 scopus 로고    scopus 로고
    • The SH2 domain: versatile signaling module and pharmaceutical target
    • Machida K., and Mayer B.J. The SH2 domain: versatile signaling module and pharmaceutical target. BBA-Proteins Proteomics. 1747 (2005) 1-25
    • (2005) BBA-Proteins Proteomics. , vol.1747 , pp. 1-25
    • Machida, K.1    Mayer, B.J.2
  • 9
    • 0001558378 scopus 로고    scopus 로고
    • Peptidomimetic SH2 domain antagonists for targeting signal transduction
    • Muller G. Peptidomimetic SH2 domain antagonists for targeting signal transduction. Top. Curr. Chem. 211 (2001) 17-59
    • (2001) Top. Curr. Chem. , vol.211 , pp. 17-59
    • Muller, G.1
  • 10
    • 0033667937 scopus 로고    scopus 로고
    • Structure-based design of compounds inhibiting Grb2-SH2 mediated protein-protein interactions in signal transduction pathways
    • Fretz H., Furet P., Garcia-Echeverria C., Ruhuel J., and Schoepfer J. Structure-based design of compounds inhibiting Grb2-SH2 mediated protein-protein interactions in signal transduction pathways. Curr. Pharm. Des. 6 (2000) 1777-1796
    • (2000) Curr. Pharm. Des. , vol.6 , pp. 1777-1796
    • Fretz, H.1    Furet, P.2    Garcia-Echeverria, C.3    Ruhuel, J.4    Schoepfer, J.5
  • 14
    • 0033584155 scopus 로고    scopus 로고
    • Structure-based design of a non-peptidic antagonist of the SH2 domain of GRB2
    • Caravatti G., Rahuel J., Gay B., and Furet P. Structure-based design of a non-peptidic antagonist of the SH2 domain of GRB2. Bioorg. Med. Chem. Lett. 9 (1999) 1973-1978
    • (1999) Bioorg. Med. Chem. Lett. , vol.9 , pp. 1973-1978
    • Caravatti, G.1    Rahuel, J.2    Gay, B.3    Furet, P.4
  • 19
    • 1242273804 scopus 로고    scopus 로고
    • Structure-activity relationships of small phosphopeptides, inhibitors of Grb2 SH2 domain, and their prodrugs
    • Liu W.-Q., Vidal M., Olszowy C., Million E., Lenoir C., Dhôtel H., and Garbay C. Structure-activity relationships of small phosphopeptides, inhibitors of Grb2 SH2 domain, and their prodrugs. J. Med. Chem. 47 (2004) 1223-1233
    • (2004) J. Med. Chem. , vol.47 , pp. 1223-1233
    • Liu, W.-Q.1    Vidal, M.2    Olszowy, C.3    Million, E.4    Lenoir, C.5    Dhôtel, H.6    Garbay, C.7
  • 21
    • 33644852350 scopus 로고    scopus 로고
    • Discovery of a novel nonphosphorylated pentapeptide motif displaying high affinity for Grb2-SH2 domain by the utilization of 3′-substituted tyrosine derivatives
    • Song Y.-L., Peach M.L., Roller P.P., Qiu S., Wang S.-M., and Long Y.-Q. Discovery of a novel nonphosphorylated pentapeptide motif displaying high affinity for Grb2-SH2 domain by the utilization of 3′-substituted tyrosine derivatives. J. Med. Chem. 49 (2006) 1585-1596
    • (2006) J. Med. Chem. , vol.49 , pp. 1585-1596
    • Song, Y.-L.1    Peach, M.L.2    Roller, P.P.3    Qiu, S.4    Wang, S.-M.5    Long, Y.-Q.6
  • 22
    • 0036417094 scopus 로고    scopus 로고
    • Molecular recognition by SH2 domains
    • Bradshaw J.M., and Waksman G. Molecular recognition by SH2 domains. Adv. Protein Chem. 61 (2003) 161-210
    • (2003) Adv. Protein Chem. , vol.61 , pp. 161-210
    • Bradshaw, J.M.1    Waksman, G.2
  • 23
    • 0035415663 scopus 로고    scopus 로고
    • SH2 domain inhibition: a problem solved?
    • Shakespeare W.C. SH2 domain inhibition: a problem solved?. Curr. Opin. Chem. Biol. 5 (2001) 409-415
    • (2001) Curr. Opin. Chem. Biol. , vol.5 , pp. 409-415
    • Shakespeare, W.C.1
  • 25
    • 0033517027 scopus 로고    scopus 로고
    • Significant compensatory role of position Y-2 conferring high affinity to non-phosphorylated inhibitors of Grb2-SH2 domain
    • Long Y.-Q., Voigt J.H., Lung F.-D.T., King C.R., and Roller P.P. Significant compensatory role of position Y-2 conferring high affinity to non-phosphorylated inhibitors of Grb2-SH2 domain. Bioorg. Med. Chem. Lett. 9 (1999) 2267-2272
    • (1999) Bioorg. Med. Chem. Lett. , vol.9 , pp. 2267-2272
    • Long, Y.-Q.1    Voigt, J.H.2    Lung, F.-D.T.3    King, C.R.4    Roller, P.P.5
  • 26
  • 29
    • 0034967501 scopus 로고    scopus 로고
    • Functional preference of the constituent amino acid residues in a phage-library-based nonphosphorylated inhibitor of the Grb2-SH2 domain
    • Lung F.-D.T., Long Y.-Q., King C.R., Varady J., Wu X.-W., Wang S., and Roller P.P. Functional preference of the constituent amino acid residues in a phage-library-based nonphosphorylated inhibitor of the Grb2-SH2 domain. J. Peptide Res. 57 (2001) 447-454
    • (2001) J. Peptide Res. , vol.57 , pp. 447-454
    • Lung, F.-D.T.1    Long, Y.-Q.2    King, C.R.3    Varady, J.4    Wu, X.-W.5    Wang, S.6    Roller, P.P.7
  • 33
    • 0035940869 scopus 로고    scopus 로고
    • Cysteine sulfoxide derivatives in, Petiveria alliacea
    • Kubec R., and Musah R.A. Cysteine sulfoxide derivatives in, Petiveria alliacea. Phytochemistry 58 (2001) 981-985
    • (2001) Phytochemistry , vol.58 , pp. 981-985
    • Kubec, R.1    Musah, R.A.2
  • 34
    • 0019851373 scopus 로고
    • Synthesis and ring-opening reactions of functionalized sultines. New approach to sparsomycin
    • Liskamp R.M.J., Zeegers H.J.M., and Ottenheijm H.C.J. Synthesis and ring-opening reactions of functionalized sultines. New approach to sparsomycin. J. Org. Chem. 46 (1981) 5408-5413
    • (1981) J. Org. Chem. , vol.46 , pp. 5408-5413
    • Liskamp, R.M.J.1    Zeegers, H.J.M.2    Ottenheijm, H.C.J.3
  • 35
    • 0000779910 scopus 로고
    • Total synthesis and absolute configuration of the natural dipeptide. gamma-glutamylmarasmine
    • Van den Broek L.A.G.M., Breuer M.L., Liskamp R.M.J., and Ottenheijm H.C.J. Total synthesis and absolute configuration of the natural dipeptide. gamma-glutamylmarasmine. J. Org. Chem. 52 (1987) 1511-1517
    • (1987) J. Org. Chem. , vol.52 , pp. 1511-1517
    • Van den Broek, L.A.G.M.1    Breuer, M.L.2    Liskamp, R.M.J.3    Ottenheijm, H.C.J.4
  • 36
    • 0034087890 scopus 로고    scopus 로고
    • Biosensor analysis of the interaction between immobilized human serum albumin and drug compounds for prediction of human serum albumin binding levels
    • Frostell-Karlsson A., Remaeus A., Roos H., Andersson K., Borg P., Hamalainen M., and Karlsson R. Biosensor analysis of the interaction between immobilized human serum albumin and drug compounds for prediction of human serum albumin binding levels. J. Med. Chem. 43 (2000) 1986-1992
    • (2000) J. Med. Chem. , vol.43 , pp. 1986-1992
    • Frostell-Karlsson, A.1    Remaeus, A.2    Roos, H.3    Andersson, K.4    Borg, P.5    Hamalainen, M.6    Karlsson, R.7
  • 37
    • 0032701484 scopus 로고    scopus 로고
    • Improving biosensor analysis
    • Myszka D.G. Improving biosensor analysis. J. Mol. Recognit 12 (1999) 279-284
    • (1999) J. Mol. Recognit , vol.12 , pp. 279-284
    • Myszka, D.G.1
  • 38
    • 84986437005 scopus 로고
    • Macromodel-an integrated software system for modeling organic and bioorganic molecules using molecular mechanics
    • Mohamadi F., Richards N.G.J., Guida W.C., Liskamp R., and Lipton M. Macromodel-an integrated software system for modeling organic and bioorganic molecules using molecular mechanics. J. Comput. Chem. 11 (1990) 440-467
    • (1990) J. Comput. Chem. , vol.11 , pp. 440-467
    • Mohamadi, F.1    Richards, N.G.J.2    Guida, W.C.3    Liskamp, R.4    Lipton, M.5
  • 39
    • 0035913529 scopus 로고    scopus 로고
    • Evaluation and reparametrization of the OPLS-AA force field for proteins via comparison with accurate quantum chemical calculations on peptides
    • Kaminski G.A., Friesner R.A., Tirado-Rives J., and Jorgensen W.L. Evaluation and reparametrization of the OPLS-AA force field for proteins via comparison with accurate quantum chemical calculations on peptides. J. Phys. Chem. B. 105 (2001) 6474-6487
    • (2001) J. Phys. Chem. B. , vol.105 , pp. 6474-6487
    • Kaminski, G.A.1    Friesner, R.A.2    Tirado-Rives, J.3    Jorgensen, W.L.4
  • 40
    • 6044221427 scopus 로고    scopus 로고
    • Exploiting the right side of the Ramachandran plot: substitution of glycines by d-alanine can significantly increase protein stability
    • Anil B., Song B., Tang Y., and Raleigh D.P. Exploiting the right side of the Ramachandran plot: substitution of glycines by d-alanine can significantly increase protein stability. J. Am. Chem. Soc. 126 (2004) 13194-13195
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 13194-13195
    • Anil, B.1    Song, B.2    Tang, Y.3    Raleigh, D.P.4


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