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Volumn 53, Issue 6, 2010, Pages 2482-2493

Salicylic acid based small molecule inhibitor for the oncogenic src homology-2 domain containing protein tyrosine phosphatase-2 (SHP2)

Author keywords

[No Author keywords available]

Indexed keywords

ANTILEUKEMIC AGENT; ANTINEOPLASTIC AGENT; GRANULOCYTE MACROPHAGE COLONY STIMULATING FACTOR; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; PROTEIN TYROSINE PHOSPHATASE SHP 2; PROTEIN TYROSINE PHOSPHATASE SHP 2 INHIBITOR; SALICYLIC ACID; UNCLASSIFIED DRUG;

EID: 77949853380     PISSN: 00222623     EISSN: 15204804     Source Type: Journal    
DOI: 10.1021/jm901645u     Document Type: Article
Times cited : (177)

References (55)
  • 1
    • 0032577051 scopus 로고    scopus 로고
    • The Croonian lecture 1997. the phosphorylation of proteins on tyrosine: Its role in cell growth and disease
    • Hunter, T. The Croonian lecture 1997. The phosphorylation of proteins on tyrosine: its role in cell growth and disease. Philos. Trans. R. Soc. London, Ser. B 1998, 353, 583-605.
    • (1998) Philos. Trans. R. Soc. London, Ser. B , vol.353 , pp. 583-605
    • Hunter, T.1
  • 2
    • 0035313868 scopus 로고    scopus 로고
    • Combinatorial control of the specificity of protein tyrosine phosphatases
    • Tonks, N. K.; Neel, B. G. Combinatorial control of the specificity of protein tyrosine phosphatases. Curr. Opin. Cell Biol. 2001, 13, 182-195.
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 182-195
    • Tonks, N.K.1    Neel, B.G.2
  • 3
    • 0035415662 scopus 로고    scopus 로고
    • Protein tyrosine phosphatases: Prospects for therapeutics
    • Zhang, Z.-Y. Protein tyrosine phosphatases: prospects for therapeutics. Curr. Opin. Chem. Biol. 2001, 5, 416-423.
    • (2001) Curr. Opin. Chem. Biol. , vol.5 , pp. 416-423
    • Zhang, Z.-Y.1
  • 4
    • 33747097252 scopus 로고    scopus 로고
    • Protein kinases and phosphatases as therapeutic targets in cancer
    • Ventura, J. J.; Nebreda, A. R. Protein kinases and phosphatases as therapeutic targets in cancer. Clin. Transi. Oncol. 2006, 5, 153-160.
    • (2006) Clin. Transi. Oncol. , vol.5 , pp. 153-160
    • Ventura, J.J.1    Nebreda, A.R.2
  • 5
    • 22044442973 scopus 로고    scopus 로고
    • Tyrosine kinases as targets for cancer therapy
    • Krause, D. S.; Van Etten, R. A. Tyrosine kinases as targets for cancer therapy. N. Engl. J. Med. 2005, 353, 172-187.
    • (2005) N. Engl. J. Med. , vol.353 , pp. 172-187
    • Krause, D.S.1    Van Etten, R.A.2
  • 6
    • 0038771965 scopus 로고    scopus 로고
    • The "Shp" ing news: SH2 domaincontaining tyrosine phosphatases in cell signaling
    • Neel, B. G.; Gu, H.; Pao, L. The "Shp" ing news: SH2 domaincontaining tyrosine phosphatases in cell signaling. Trends Biochem. Sci. 2003, 28, 284-293.
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 284-293
    • Neel, B.G.1    Gu, H.2    Pao, L.3
  • 7
    • 33846854905 scopus 로고    scopus 로고
    • PTPN11 is the first identified protooncogene that encodes a tyrosine phosphatase
    • Chan, R. J.; Feng, G. S. PTPN11 is the first identified protooncogene that encodes a tyrosine phosphatase. Blood 2007, 109, 862-867.
    • (2007) Blood , vol.109 , pp. 862-867
    • Chan, R.J.1    Feng, G.S.2
  • 8
    • 33846945811 scopus 로고    scopus 로고
    • Protein tyrosine phosphatase function: The substrate perspective
    • Tiganis, T.; Bennett, A. M. Protein tyrosine phosphatase function: the substrate perspective. Biochem. J. 2007, 402, 1-15.
    • (2007) Biochem. J. , vol.402 , pp. 1-15
    • Tiganis, T.1    Bennett, A.M.2
  • 10
    • 18444401014 scopus 로고    scopus 로고
    • Noonan syndrome and related disorders: Genetics and pathogenesis
    • Tartaglia, M.; Gelb, B. D. Noonan syndrome and related disorders: genetics and pathogenesis. Annu. Rev. Genomics Hum. Genet. 2005, 5, 45-68.
    • (2005) Annu. Rev. Genomics Hum. Genet. , vol.5 , pp. 45-68
    • Tartaglia, M.1    Gelb, B.D.2
  • 14
  • 17
    • 43049093663 scopus 로고    scopus 로고
    • The tyrosine phosphatase Shp2 (PTPN11) in cancer
    • Chan, G.; Kalaitzidis, D.; Neel, B. G. The tyrosine phosphatase Shp2 (PTPN11) in cancer. Cancer Metastasis Rev. 2008, 27, 179-192.
    • (2008) Cancer Metastasis Rev. , vol.27 , pp. 179-192
    • Chan, G.1    Kalaitzidis, D.2    Neel, B.G.3
  • 18
    • 44849138413 scopus 로고    scopus 로고
    • Isolation of a distinct class of gain-of-function SHP-2 mutants with oncogenic RAS-like transforming activity from solid tumors
    • Miyamoto, D.; Miyamoto, M.; Takahashi, A.; Yomogita, Y.; Higashi, H.; Kondo, S.; Hatakeyama, M. Isolation of a distinct class of gain-of-function SHP-2 mutants with oncogenic RAS-like transforming activity from solid tumors. Oncogene 2008, 27, 3508-3515.
    • (2008) Oncogene , vol.27 , pp. 3508-3515
    • Miyamoto, D.1    Miyamoto, M.2    Takahashi, A.3    Yomogita, Y.4    Higashi, H.5    Kondo, S.6    Hatakeyama, M.7
  • 19
    • 4544334936 scopus 로고    scopus 로고
    • Oncogenic mechanisms of the Helicobacter pylori CagA protein
    • Hatakeyama, M. Oncogenic mechanisms of the Helicobacter pylori CagA protein. Nat. Rev. Cancer 2004, 4, 688-694.
    • (2004) Nat. Rev. Cancer , vol.4 , pp. 688-694
    • Hatakeyama, M.1
  • 24
    • 57349141440 scopus 로고    scopus 로고
    • Identification of small molecular weight inhibitors of Src homology 2 domain-containing tyrosine phosphatase 2 (SHP-2) via in silico database screening combined with experimental assay
    • Yu, W. M.; Guvench, O.; Mackerell, A. D.; Qu, C. K. Identification of small molecular weight inhibitors of Src homology 2 domain-containing tyrosine phosphatase 2 (SHP-2) via in silico database screening combined with experimental assay. J. Med. Chem. 2008, 51, 7396-7404.
    • (2008) J. Med. Chem. , vol.51 , pp. 7396-7404
    • Yu, W.M.1    Guvench, O.2    Mackerell, A.D.3    Qu, C.K.4
  • 25
    • 62849093631 scopus 로고    scopus 로고
    • A conserved mechanism for control of human and mouse embryonic stem cell pluripotency and differentiation by shp2 tyrosine phosphatase
    • Wu, D.; Pang, Y.; Ke, Y.; Yu, J.; He, Z.; Tautz, L.; Mustelin, T.; Ding, S.; Huang, Z.; Feng, G.-S. A conserved mechanism for control of human and mouse embryonic stem cell pluripotency and differentiation by shp2 tyrosine phosphatase. PLoS One 2009, 4,e4914.
    • (2009) PLoS One , vol.4
    • Wu, D.1    Pang, Y.2    Ke, Y.3    Yu, J.4    He, Z.5    Tautz, L.6    Mustelin, T.7    Ding, S.8    Huang, Z.9    Feng, G.-S.10
  • 26
    • 0036181649 scopus 로고    scopus 로고
    • Protein tyrosine phosphatases: Structure and function, substrate specificity, and inhibitor development
    • Zhang, Z.-Y. Protein tyrosine phosphatases: structure and function, substrate specificity, and inhibitor development. Annu. Rev. Pharmacol. Toxicol. 2002, 42, 209-234.
    • (2002) Annu. Rev. Pharmacol. Toxicol. , vol.42 , pp. 209-234
    • Zhang, Z.-Y.1
  • 27
    • 0031457541 scopus 로고    scopus 로고
    • Identification of a second aryl phosphate-binding site in protein-tyrosine phosphatase IB: A paradigm for inhibitor design
    • Puius, Y. A.; Zhao, Y.; Sullivan, M.; Lawrence, D. S.; Almo, S. C.; Zhang, Z.-Y. Identification of a second aryl phosphate-binding site in protein-tyrosine phosphatase IB: a paradigm for inhibitor design. Proc. Natl. Acad. Sci. U.S.A. 1997, 94, 13420-13425.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 13420-13425
    • Puius, Y.A.1    Zhao, Y.2    Sullivan, M.3    Lawrence, D.S.4    Almo, S.C.5    Zhang, Z.-Y.6
  • 28
    • 34247362854 scopus 로고    scopus 로고
    • PTP1B as a drug target: Recent development in PTP1B inhibitor discovery
    • Zhang, S.; Zhang, Z.-Y. PTP1B as a drug target: recent development in PTP1B inhibitor discovery. Drug Discovery Today 2007, 12, 373-381.
    • (2007) Drug Discovery Today , vol.12 , pp. 373-381
    • Zhang, S.1    Zhang, Z.-Y.2
  • 30
    • 0142180154 scopus 로고    scopus 로고
    • Aurintricarboxylic acid blocks in vitro and in vivo activity of YopH, an essential virulent factor of Yersinia pestis, the agent of plague
    • Liang, F.; Huang, Z.; Lee, S.-Y.; Liang, J.; Ivanov, M. I.; Alonso, A.; Bliska, J. B.; Lawrence, D. S.; Mustelin, T.; Zhang, Z.-Y. Aurintricarboxylic acid blocks in vitro and in vivo activity of YopH, an essential virulent factor of Yersinia pestis, the agent of plague. J. Biol. Chem. 2003, 278, 41734-41741.
    • (2003) J. Biol. Chem. , vol.278 , pp. 41734-41741
    • Liang, F.1    Huang, Z.2    Lee, S.-Y.3    Liang, J.4    Ivanov, M.I.5    Alonso, A.6    Bliska, J.B.7    Lawrence, D.S.8    Mustelin, T.9    Zhang, Z.-Y.10
  • 31
    • 0037366605 scopus 로고    scopus 로고
    • The combinatorial synthesis of bicyclic privileged structures or privileged substructures
    • Horton, D. A.; Bourne, G. T.; Smythe, M. L. The combinatorial synthesis of bicyclic privileged structures or privileged substructures. Chem. Rev. 2003, 103, 893-930.
    • (2003) Chem. Rev. , vol.103 , pp. 893-930
    • Horton, D.A.1    Bourne, G.T.2    Smythe, M.L.3
  • 32
    • 27844463013 scopus 로고    scopus 로고
    • Indole alkaloid marine natural products: An established source of cancer drug leads with considerable promise for the control of parasitic, neurological and other diseases
    • Gul, W.; Hamann, M. T. Indole alkaloid marine natural products: an established source of cancer drug leads with considerable promise for the control of parasitic, neurological and other diseases. Life Sci. 2005, 78 ,442-453.
    • (2005) Life Sci. , vol.78 , pp. 442-453
    • Gul, W.1    Hamann, M.T.2
  • 33
    • 0000096835 scopus 로고    scopus 로고
    • Click chemistry: Diverse chemical function from a few good reactions
    • Kolb, H. C.; Finn, M. G.; Sharpless, K. B. Click chemistry: diverse chemical function from a few good reactions. Angew. Chem., Int. Ed. 2001, 40, 2004-2021.
    • (2001) Angew. Chem., Int. Ed. , vol.40 , pp. 2004-2021
    • Kolb, H.C.1    Finn, M.G.2    Sharpless, K.B.3
  • 34
    • 0037087516 scopus 로고    scopus 로고
    • Click chemistry in situ: Acetylcholinesterase as a reaction vessel for the selective assembly of a femtomolar inhibitor from an array of building blocks
    • Lewis, W. G.; Green, L. G.; Grynszpan, F.; Radić, Z.; Carlier, P. R.; Taylor, P.; Finn, M. G.; Sharpless, K. B. Click chemistry in situ: acetylcholinesterase as a reaction vessel for the selective assembly of a femtomolar inhibitor from an array of building blocks. Angew. Chem., Int. Ed. 2002, 41, 1053-1057.
    • (2002) Angew. Chem., Int. Ed. , vol.41 , pp. 1053-1057
    • Lewis, W.G.1    Green, L.G.2    Grynszpan, F.3    Radić, Z.4    Carlier, P.R.5    Taylor, P.6    Finn, M.G.7    Sharpless, K.B.8
  • 35
    • 0042125393 scopus 로고    scopus 로고
    • A potent and highly selective inhibitor of human alpha-1,3- fucosyltransferase via click chemistry
    • Lee, L. V.; Mitchell, M. L.; Huang, S. J.; Fokin, V. V.; Sharpless, K. B.; Wong, C. H. A potent and highly selective inhibitor of human alpha-1,3-fucosyltransferase via click chemistry. J. Am. Chem. Soc. 2003, 125, 9588-9589.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 9588-9589
    • Lee, L.V.1    Mitchell, M.L.2    Huang, S.J.3    Fokin, V.V.4    Sharpless, K.B.5    Wong, C.H.6
  • 37
    • 33644759169 scopus 로고    scopus 로고
    • Rapid assembly and in situ screening of bidentate inhibitors of protein tyrosine phosphatases
    • Srinivasan, R.; Uttamchandani, M.; Yao, S. Q. Rapid assembly and in situ screening of bidentate inhibitors of protein tyrosine phosphatases. Org. Lett. 2006, 8, 713-716.
    • (2006) Org. Lett. , vol.8 , pp. 713-716
    • Srinivasan, R.1    Uttamchandani, M.2    Yao, S.Q.3
  • 38
    • 33750957233 scopus 로고    scopus 로고
    • A two stage click-based library of protein tyrosine phosphatase inhibitors
    • Xie, J.; Seto, C. T. A two stage click-based library of protein tyrosine phosphatase inhibitors. Bioorg. Med. Chem. 2007, 15, 458-473.
    • (2007) Bioorg. Med. Chem. , vol.15 , pp. 458-473
    • Xie, J.1    Seto, C.T.2
  • 39
    • 38049160121 scopus 로고    scopus 로고
    • Structure, inhibitor, and regulatory mechanism of Lyp, a lymphoid-specific tyrosine phosphatase implicated in autoimmune diseases
    • Yu, X.; Sun, J.-P.; He, Y.; Guo, X.-L.; Liu, S.; Zhou, B.; Hudmon, A.; Zhang, Z.-Y. Structure, inhibitor, and regulatory mechanism of Lyp, a lymphoid-specific tyrosine phosphatase implicated in autoimmune diseases. Proc. Natl. Acad. Sci. U.S.A. 2007, 104, 19767-19772.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 19767-19772
    • Yu, X.1    Sun, J.-P.2    He, Y.3    Guo, X.-L.4    Liu, S.5    Zhou, B.6    Hudmon, A.7    Zhang, Z.-Y.8
  • 40
    • 0032479299 scopus 로고    scopus 로고
    • A common requirement for the catalytic activity and both SH2 domains of SHP-2 in mitogen-activated protein (MAP) kinase activation by the ErbB family of receptors. A specific role for SHP-2 in map, but not c-Jun amino-terminal kinase activation
    • Deb, T. B.; Wong, L.; Salomon, D. S.; Zhou, G.; Dixon, J. E.; Gutkind, J. S.; Thompson, S. A.; Johnson, G. R. A common requirement for the catalytic activity and both SH2 domains of SHP-2 in mitogen-activated protein (MAP) kinase activation by the ErbB family of receptors. A specific role for SHP-2 in map, but not c-Jun amino-terminal kinase activation. J. Biol. Chem. 1998, 273, 16643-16646.
    • (1998) J. Biol. Chem. , vol.273 , pp. 16643-16646
    • Deb, T.B.1    Wong, L.2    Salomon, D.S.3    Zhou, G.4    Dixon, J.E.5    Gutkind, J.S.6    Thompson, S.A.7    Johnson, G.R.8
  • 41
    • 0033587698 scopus 로고    scopus 로고
    • Genetic evidence that Shp-2 tyrosine phosphatase is a signal enhancer of the epidermal growth factor receptor in mammals
    • Qu, C. K.; Yu, W. M.; Azzarelli, B.; Feng, G. S. Genetic evidence that Shp-2 tyrosine phosphatase is a signal enhancer of the epidermal growth factor receptor in mammals. Proc. Natl. Acad. Sci. U.S.A. 1999, 96, 8528-8533.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 8528-8533
    • Qu, C.K.1    Yu, W.M.2    Azzarelli, B.3    Feng, G.S.4
  • 42
    • 0033761488 scopus 로고    scopus 로고
    • The tyrosine phosphatase SHP-2 is required for sustained activation of extracellular signal-regulated kinase and epithelial morphogenesis downstream from the met receptor tyrosine kinase
    • Maroun, C. R.; Naujokas, M. A.; Holgado-Madruga, M.; Wong, A. J.; Park, M. The tyrosine phosphatase SHP-2 is required for sustained activation of extracellular signal-regulated kinase and epithelial morphogenesis downstream from the met receptor tyrosine kinase. Mol. Cell. Biol. 2000, 20, 8513-8525.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 8513-8525
    • Maroun, C.R.1    Naujokas, M.A.2    Holgado-Madruga, M.3    Wong, A.J.4    Park, M.5
  • 43
    • 0027910431 scopus 로고
    • Association of Sos Ras exchange protein with Grb2 is implicated in tyrosine kinase signal transduction and transformation
    • Egan, S. E.; Giddings, B. W.; Brooks, M. W.; Buday, L.; Sizeland, A. M.; Weinberg, R. A. Association of Sos Ras exchange protein with Grb2 is implicated in tyrosine kinase signal transduction and transformation. Nature 1993, 363, 45-51.
    • (1993) Nature , vol.363 , pp. 45-51
    • Egan, S.E.1    Giddings, B.W.2    Brooks, M.W.3    Buday, L.4    Sizeland, A.M.5    Weinberg, R.A.6
  • 44
    • 0026063878 scopus 로고
    • Selective hypersensitivity to granulocyte-macrophage colony-stimulating factor by juvenile chronic myeloid leukemia hematopoietic progenitors
    • Emanuel, P. D.; Bates, L. J.; Castleberry, R. P.; Gualtieri, R. J.; Zuckerman, K. S. Selective hypersensitivity to granulocyte-macrophage colony-stimulating factor by juvenile chronic myeloid leukemia hematopoietic progenitors. Blood 1991, 77, 925-929.
    • (1991) Blood , vol.77 , pp. 925-929
    • Emanuel, P.D.1    Bates, L.J.2    Castleberry, R.P.3    Gualtieri, R.J.4    Zuckerman, K.S.5
  • 45
    • 18244395853 scopus 로고    scopus 로고
    • Human somatic PTPN11 mutations induce hematopoietic-cell hypersensitivity to granulocyte-macrophage colony-stimulating factor
    • Chan, R. J.; Leedy, M. B.; Munugalavadla, V.; Voorhorst, C. S.; Li, Y.; Yu, M.; Kapur, R. Human somatic PTPN11 mutations induce hematopoietic-cell hypersensitivity to granulocyte-macrophage colony-stimulating factor. Blood 2005, 105, 3737-3742.
    • (2005) Blood , vol.105 , pp. 3737-3742
    • Chan, R.J.1    Leedy, M.B.2    Munugalavadla, V.3    Voorhorst, C.S.4    Li, Y.5    Yu, M.6    Kapur, R.7
  • 47
    • 2542559631 scopus 로고    scopus 로고
    • Mechanistic studies on protein tyrosine phosphatases
    • Zhang, Z.-Y. Mechanistic studies on protein tyrosine phosphatases. Prog. Nucleic Acid Res. Mol. Biol. 2003, 73, 171-220.
    • (2003) Prog. Nucleic Acid Res. Mol. Biol. , vol.73 , pp. 171-220
    • Zhang, Z.-Y.1
  • 48
    • 0029066496 scopus 로고
    • Structural basis for phosphotyrosine peptide recognition by protein tyrosine phosphatase IB
    • Jia, Z.; Barford, D.; Flint, A. J.; Tonks, N. K. Structural basis for phosphotyrosine peptide recognition by protein tyrosine phosphatase IB. Science 1995, 268, 1754-1758.
    • (1995) Science , vol.268 , pp. 1754-1758
    • Jia, Z.1    Barford, D.2    Flint, A.J.3    Tonks, N.K.4
  • 50
    • 0034635505 scopus 로고    scopus 로고
    • Structural basis for substrate specificity of protein-tyrosine phosphatase SHP-1
    • Yang, J.; Cheng, Z.; Niu, T.; Liang, X.; Zhao, Z. J.; Zhou, G. W. Structural basis for substrate specificity of protein-tyrosine phosphatase SHP-1. J. Biol. Chem. 2000, 275, 4066-4071.
    • (2000) J. Biol. Chem. , vol.275 , pp. 4066-4071
    • Yang, J.1    Cheng, Z.2    Niu, T.3    Liang, X.4    Zhao, Z.J.5    Zhou, G.W.6
  • 51
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z.; Minow, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 1997, 276, 307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minow, W.2
  • 52
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza, J. AMoRe: an automated package for molecular replacement. Acta Crystallogr. A 1994, 50, 157-163.
    • (1994) Acta Crystallogr. A , vol.50 , pp. 157-163
    • Navaza, J.1
  • 54
    • 0026597444 scopus 로고
    • The free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger, A. T. The free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature 1992, 355, 472-475.
    • (1992) Nature , vol.355 , pp. 472-475
    • Brünger, A.T.1
  • 55
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T. A.; Zou, J. Y.; Cowan, S. W.; Kjeldgaard, G. J. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A. 1991, 47, 110-119.
    • (1991) Acta Crystallogr. A. , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, G.J.4


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