메뉴 건너뛰기




Volumn 14, Issue 6, 2014, Pages 567-588

Structure, function, and pathogenesis of SHP2 in developmental disorders and tumorigenesis

Author keywords

Hematologic malignancies; LEOPARD syndrome; Noonan syndromes; PTPN11; SHP2; Tumorigenesis

Indexed keywords

JANUS KINASE; PROTEIN TYROSINE PHOSPHATASE SHP 2; STAT PROTEIN; STAT5 PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN KINASE B; RAF PROTEIN; RAS PROTEIN; ANTINEOPLASTIC AGENT; ENZYME INHIBITOR;

EID: 84907345106     PISSN: 15680096     EISSN: 18735576     Source Type: Journal    
DOI: 10.2174/1568009614666140717105001     Document Type: Article
Times cited : (61)

References (217)
  • 1
    • 79960925570 scopus 로고    scopus 로고
    • Checks and balances: Interplay of RTKs and PTPs in cancer progression
    • Sastry, S.K.; Elferink, L.A. Checks and balances: interplay of RTKs and PTPs in cancer progression. Biochem. Pharmacol., 2011, 82, 435-440.
    • (2011) Biochem. Pharmacol , vol.82 , pp. 435-440
    • Sastry, S.K.1    Elferink, L.A.2
  • 2
    • 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
  • 3
    • 0034572534 scopus 로고    scopus 로고
    • The SHP-2 tyrosine phosphatase: Signaling mechanisms and biological functions
    • Qu, C.K. The SHP-2 tyrosine phosphatase: signaling mechanisms and biological functions. Cell Res., 2000, 10, 279-288.
    • (2000) Cell Res , vol.10 , pp. 279-288
    • Qu, C.K.1
  • 5
    • 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, 6, 45-68.
    • (2005) Annu. Rev. Genomics. Hum. Genet , vol.6 , pp. 45-68
    • Tartaglia, M.1    Gelb, B.D.2
  • 6
    • 84862129375 scopus 로고    scopus 로고
    • Protein Tyrosine Phosphatase SHP-2 (PTPN11) in hematopoiesis and leukemogenesis
    • Liu, X.; Qu, C.K. Protein Tyrosine Phosphatase SHP-2 (PTPN11) in hematopoiesis and leukemogenesis. J. Signal Transduct., 2011, 2011, 195-239.
    • (2011) J. Signal Transduct , vol.2011 , pp. 195-239
    • Liu, X.1    Qu, C.K.2
  • 7
    • 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
  • 8
    • 33846402073 scopus 로고    scopus 로고
    • The role of Shp2 (PTPN11) in cancer
    • Mohi, M.G.; Neel, B.G. The role of Shp2 (PTPN11) in cancer. Curr. Opin. Genet. Dev., 2007, 17, 23-30.
    • (2007) Curr. Opin. Genet. Dev , vol.17 , pp. 23-30
    • Mohi, M.G.1    Neel, B.G.2
  • 9
    • 84866061916 scopus 로고    scopus 로고
    • Dual faces of SH2-containing protein-tyrosine phosphatase Shp2/PTPN11 in tumorigenesis
    • Li, S.; Hsu, D.D.; Wang, H.; Feng, G.S. Dual faces of SH2-containing protein-tyrosine phosphatase Shp2/PTPN11 in tumorigenesis. Front. Med., 2012, 6, 275-279.
    • (2012) Front. Med , vol.6 , pp. 275-279
    • Li, S.1    Hsu, D.D.2    Wang, H.3    Feng, G.S.4
  • 10
    • 18844452664 scopus 로고    scopus 로고
    • Germ-line and somatic PTPN11 mutations in human disease
    • Tartaglia, M.; Gelb, B.D. Germ-line and somatic PTPN11 mutations in human disease. Eur. J. Med. Genet., 2005, 48, 81-96.
    • (2005) Eur. J. Med. Genet , vol.48 , pp. 81-96
    • Tartaglia, M.1    Gelb, B.D.2
  • 12
    • 77958056047 scopus 로고    scopus 로고
    • Protein tyrosine phosphatases as drug targets: Strategies and challenges of inhibitor development
    • Barr, A.J. Protein tyrosine phosphatases as drug targets: strategies and challenges of inhibitor development. Future Med. Chem., 2010, 2, 1563-1576.
    • (2010) Future Med. Chem , vol.2 , pp. 1563-1576
    • Barr, A.J.1
  • 13
  • 14
    • 84872783533 scopus 로고    scopus 로고
    • Small molecule tools for functional interrogation of protein tyrosine phosphatases
    • He, R.; Zeng, L.F.; He, Y.; Zhang, S.; Zhang, Z.Y. Small molecule tools for functional interrogation of protein tyrosine phosphatases. FEBS J., 2013, 280, 731-750.
    • (2013) FEBS J , vol.280 , pp. 731-750
    • He, R.1    Zeng, L.F.2    He, Y.3    Zhang, S.4    Zhang, Z.Y.5
  • 15
    • 0026471539 scopus 로고
    • Identification of a human src homology 2-containing protein-tyrosine-phosphatase: A putative homolog of Drosophila corkscrew
    • Freeman, R.M. Jr.; Plutzky, J.; Neel, B.G. Identification of a human src homology 2-containing protein-tyrosine-phosphatase: a putative homolog of Drosophila corkscrew. Proc. Natl. Acad. Sci. U S A., 1992, 89, 11239-11243.
    • (1992) Proc. Natl. Acad. Sci. U S A , vol.89 , pp. 11239-11243
    • Freeman Jr., R.M.1    Plutzky, J.2    Neel, B.G.3
  • 16
    • 0027531954 scopus 로고
    • A widely expressed human protein-tyrosine phosphatase containing src homology 2 domains
    • Ahmad, S.; Banville, D.; Zhao, Z.; Fischer, E.H.; Shen, S.H. A widely expressed human protein-tyrosine phosphatase containing src homology 2 domains. Proc. Natl. Acad. Sci. U S A., 1993, 90, 2197-2201.
    • (1993) Proc. Natl. Acad. Sci. U S A , vol.90 , pp. 2197-2201
    • Ahmad, S.1    Banville, D.2    Zhao, Z.3    Fischer, E.H.4    Shen, S.H.5
  • 17
    • 0032548830 scopus 로고    scopus 로고
    • Crystal structure of the tyrosine phosphatase SHP-2
    • Hof, P.; Pluskey, S.; Dhe-Paganon, S.; Eck, M.J.; Shoelson, S.E. Crystal structure of the tyrosine phosphatase SHP-2. Cell., 1998, 92, 441-450.
    • (1998) Cell , vol.92 , pp. 441-450
    • Hof, P.1    Pluskey, S.2    Dhe-Paganon, S.3    Eck, M.J.4    Shoelson, S.E.5
  • 18
    • 70349602267 scopus 로고    scopus 로고
    • Protein tyrosine phosphatase SHP-2: A proto-oncogene product that promotes Ras activation
    • Matozaki, T.; Murata, Y.; Saito, Y.; Okazawa, H.; Ohnishi, H. Protein tyrosine phosphatase SHP-2: a proto-oncogene product that promotes Ras activation. Cancer Sci., 2009, 100, 1786-1793.
    • (2009) Cancer Sci , vol.100 , pp. 1786-1793
    • Matozaki, T.1    Murata, Y.2    Saito, Y.3    Okazawa, H.4    Ohnishi, H.5
  • 19
    • 77953510496 scopus 로고    scopus 로고
    • Targeting protein tyrosine phosphatases for anticancer drug discovery
    • Scott, L.M.; Lawrence, H.R.; Sebti, S.M.; Lawrence, N.J.; Wu, J. Targeting protein tyrosine phosphatases for anticancer drug discovery. Curr. Pharm. Des., 2010, 16, 1843-1862.
    • (2010) Curr. Pharm. Des , vol.16 , pp. 1843-1862
    • Scott, L.M.1    Lawrence, H.R.2    Sebti, S.M.3    Lawrence, N.J.4    Wu, J.5
  • 20
    • 42649118836 scopus 로고    scopus 로고
    • Protein tyrosine phosphatases in the JAK/STAT pathway
    • Xu, D.; Qu, C.K. Protein tyrosine phosphatases in the JAK/STAT pathway. Front Biosci., 2008, 13, 4925-4932.
    • (2008) Front Biosci , vol.13 , pp. 4925-4932
    • Xu, D.1    Qu, C.K.2
  • 21
    • 0027399168 scopus 로고
    • Activation of a phosphotyrosine phosphatase by tyrosine phosphorylation
    • Vogel, W.; Lammers, R.; Huang, J.; Ullrich, A. Activation of a phosphotyrosine phosphatase by tyrosine phosphorylation. Science, 1993, 259, 1611-1614.
    • (1993) Science , vol.259 , pp. 1611-1614
    • Vogel, W.1    Lammers, R.2    Huang, J.3    Ullrich, A.4
  • 22
    • 0027531637 scopus 로고
    • SH2-containing phosphotyrosine phosphatase as a target of protein-tyrosine kinases
    • Feng, G.S.; Hui, C.C.; Pawson, T. SH2-containing phosphotyrosine phosphatase as a target of protein-tyrosine kinases. Science, 1993, 259, 1607-1611.
    • (1993) Science , vol.259 , pp. 1607-1611
    • Feng, G.S.1    Hui, C.C.2    Pawson, T.3
  • 23
    • 84891589105 scopus 로고    scopus 로고
    • Antagonism between binding site affinity and conformational dynamics tunes alternative cis-interactions within Shp2
    • Sun, J.; Lu, S.; Ouyang, M.; Lin, L.J.; Zhuo, Y.; Liu, B.; Chien, S.; Neel, B.G.; Wang, Y. Antagonism between binding site affinity and conformational dynamics tunes alternative cis-interactions within Shp2. Nat. Commun., 2013, 4, 2037.
    • (2013) Nat. Commun , vol.4 , pp. 2037
    • Sun, J.1    Lu, S.2    Ouyang, M.3    Lin, L.J.4    Zhuo, Y.5    Liu, B.6    Chien, S.7    Neel, B.G.8    Wang, Y.9
  • 26
    • 33646096207 scopus 로고    scopus 로고
    • PTPN11 (Shp2) mutations in LEOPARD syndrome have dominant negative, not activating, effects
    • Kontaridis, M.I.; Swanson, K.D.; David, F.S.; Barford D.; Neel, B.G. PTPN11 (Shp2) mutations in LEOPARD syndrome have dominant negative, not activating, effects. J. Biol. Chem., 2006, 281, 6785-6792.
    • (2006) J. Biol. Chem , vol.281 , pp. 6785-6792
    • Kontaridis, M.I.1    Swanson, K.D.2    David, F.S.3    Barford, D.4    Neel, B.G.5
  • 28
    • 84877102677 scopus 로고    scopus 로고
    • Protein tyrosine phosphatase SHP2/PTPN11 mistargeting as a consequence of SH2-domain point mutations associated with Noonan Syndrome and leukemia
    • Muller, P.J.; Rigbolt, K.T.; Paterok, D.; Piehler, J.; Vanselow, J.; Lasonder, E.; Andersen, J.S.; Schaper, F.; Sobota, R.M. Protein tyrosine phosphatase SHP2/PTPN11 mistargeting as a consequence of SH2-domain point mutations associated with Noonan Syndrome and leukemia. J. Proteomics, 2013, 84, 132-147.
    • (2013) J. Proteomics , vol.84 , pp. 132-147
    • Muller, P.J.1    Rigbolt, K.T.2    Paterok, D.3    Piehler, J.4    Vanselow, J.5    Lasonder, E.6    Andersen, J.S.7    Schaper, F.8    Sobota, R.M.9
  • 29
    • 34748831102 scopus 로고    scopus 로고
    • The Src homology 2 domain tyrosine phosphatases SHP-1 and SHP-2: Diversified control of cell growth, inflammation, and injury
    • Chong, Z.Z.; Maiese, K. The Src homology 2 domain tyrosine phosphatases SHP-1 and SHP-2: diversified control of cell growth, inflammation, and injury. Histol. Histopathol., 2007, 22, 1251-1267.
    • (2007) Histol. Histopathol , vol.22 , pp. 1251-1267
    • Chong, Z.Z.1    Maiese, K.2
  • 30
    • 3543036342 scopus 로고    scopus 로고
    • Proteintyrosine phosphatase Shp-2 regulates cell spreading, migration, and focal adhesion
    • Yu, D.H.; Qu, C.K.; Henegariu, O.; Lu, X.; Feng, G.S. Proteintyrosine phosphatase Shp-2 regulates cell spreading, migration, and focal adhesion. J. Biol. Chem., 1998, 273, 21125-21131.
    • (1998) J. Biol. Chem , vol.273 , pp. 21125-21131
    • Yu, D.H.1    Qu, C.K.2    Henegariu, O.3    Lu, X.4    Feng, G.S.5
  • 31
    • 38349004658 scopus 로고    scopus 로고
    • The molecular functions of Shp2 in the Ras/Mitogen-activated protein kinase (ERK1/2) pathway
    • Dance, M.; Montagner, A.; Salles, J.P.; Yart, A.; Raynal, P. The molecular functions of Shp2 in the Ras/Mitogen-activated protein kinase (ERK1/2) pathway. Cell Signal., 2008, 20, 453-459.
    • (2008) Cell Signal , vol.20 , pp. 453-459
    • Dance, M.1    Montagner, A.2    Salles, J.P.3    Yart, A.4    Raynal, P.5
  • 32
    • 0142059890 scopus 로고    scopus 로고
    • Molecular mechanism for a role of SHP2 in epidermal growth factor receptor signaling
    • Agazie, Y.M.; Hayman, M.J. Molecular mechanism for a role of SHP2 in epidermal growth factor receptor signaling. Mol. Cell. Biol., 2003, 23, 7875-7886.
    • (2003) Mol. Cell. Biol , vol.23 , pp. 7875-7886
    • Agazie, Y.M.1    Hayman, M.J.2
  • 33
    • 0028179013 scopus 로고
    • Protein-tyrosine-phosphatase SHPTP2 couples platelet-derived growth factor receptor beta to Ras
    • Bennett, A.M.; Tang, T.L.; Sugimoto, S.; Walsh, C.T.; Neel, B.G. Protein-tyrosine-phosphatase SHPTP2 couples platelet-derived growth factor receptor beta to Ras. Proc. Natl. Acad. Sci. U S A., 1994, 91, 7335-7339.
    • (1994) Proc. Natl. Acad. Sci. U S A , vol.91 , pp. 7335-7339
    • Bennett, A.M.1    Tang, T.L.2    Sugimoto, S.3    Walsh, C.T.4    Neel, B.G.5
  • 34
    • 0028124504 scopus 로고
    • Role of SH-PTP2, a protein-tyrosine phosphatase with Src homology 2 domains, in insulin-stimulated Ras activation
    • Noguchi, T.; Matozaki, T.; Horita, K.; Fujioka, Y.; Kasuga, M. Role of SH-PTP2, a protein-tyrosine phosphatase with Src homology 2 domains, in insulin-stimulated Ras activation. Mol. Cell. Biol., 1994, 14, 6674-6682.
    • (1994) Mol. Cell. Biol , vol.14 , pp. 6674-6682
    • Noguchi, T.1    Matozaki, T.2    Horita, K.3    Fujioka, Y.4    Kasuga, M.5
  • 35
    • 14044272770 scopus 로고    scopus 로고
    • A novel role for Gab1 and SHP2 in epidermal growth factorinduced Ras activation
    • Montagner, A.; Yart, A.; Dance, M.; Perret, B.; Salles, J.P.; Raynal, P. A novel role for Gab1 and SHP2 in epidermal growth factorinduced Ras activation. J. Biol. Chem., 2005, 280, 5350-5360.
    • (2005) J. Biol. Chem , vol.280 , pp. 5350-5360
    • Montagner, A.1    Yart, A.2    Dance, M.3    Perret, B.4    Salles, J.P.5    Raynal, P.6
  • 36
    • 66449118043 scopus 로고    scopus 로고
    • Molecular mechanism for SHP2 in promoting HER2-induced signaling and transformation
    • Zhou, X.; Agazie, Y.M. Molecular mechanism for SHP2 in promoting HER2-induced signaling and transformation. J. Biol. Chem., 2009, 284, 12226-12234.
    • (2009) J. Biol. Chem , vol.284 , pp. 12226-12234
    • Zhou, X.1    Agazie, Y.M.2
  • 37
    • 1542289021 scopus 로고    scopus 로고
    • Roles of Gab1 and SHP2 in paxillin tyrosine dephosphorylation and Src activation in response to epidermal growth factor
    • Ren, Y.; Meng, S.; Mei, L.; Zhao, Z.J.; Jove, R.; Wu, J. Roles of Gab1 and SHP2 in paxillin tyrosine dephosphorylation and Src activation in response to epidermal growth factor. J. Biol. Chem., 2004, 279, 8497-8505.
    • (2004) J. Biol. Chem , vol.279 , pp. 8497-8505
    • Ren, Y.1    Meng, S.2    Mei, L.3    Zhao, Z.J.4    Jove, R.5    Wu, J.6
  • 39
    • 0036847930 scopus 로고    scopus 로고
    • Sprouty1 and Sprouty2 provide a control mechanism for the Ras/MAPK signalling pathway
    • Hanafusa, H.; Torii, S.; Yasunaga, T.; Nishida, E. Sprouty1 and Sprouty2 provide a control mechanism for the Ras/MAPK signalling pathway. Nat. Cell Biol., 2002, 4, 850-858.
    • (2002) Nat. Cell Biol , vol.4 , pp. 850-858
    • Hanafusa, H.1    Torii, S.2    Yasunaga, T.3    Nishida, E.4
  • 40
    • 2542433976 scopus 로고    scopus 로고
    • Shp2, an SH2-containing protein-tyrosine phosphatase, positively regulates receptor tyrosine kinase signaling by dephosphorylating and inactivating the inhibitor Sprouty
    • Hanafusa, H.; Torii, S.; Yasunaga, T.; Matsumoto, K.; Nishida, E. Shp2, an SH2-containing protein-tyrosine phosphatase, positively regulates receptor tyrosine kinase signaling by dephosphorylating and inactivating the inhibitor Sprouty. J. Biol. Chem., 2004, 279, 22992-22995.
    • (2004) J. Biol. Chem , vol.279 , pp. 22992-22995
    • Hanafusa, H.1    Torii, S.2    Yasunaga, T.3    Matsumoto, K.4    Nishida, E.5
  • 41
    • 33645739909 scopus 로고    scopus 로고
    • Sprouty proteins are in vivo targets of Corkscrew/ SHP-2 tyrosine phosphatases
    • Jarvis, L.A.; Toering, S.J.; Simon, M.A.; Krasnow, M.A.; Smith-Bolton, R.K. Sprouty proteins are in vivo targets of Corkscrew/ SHP-2 tyrosine phosphatases. Development, 2006, 133, 1133-1142.
    • (2006) Development , vol.133 , pp. 1133-1142
    • Jarvis, L.A.1    Toering, S.J.2    Simon, M.A.3    Krasnow, M.A.4    Smith-Bolton, R.K.5
  • 42
    • 10644259435 scopus 로고    scopus 로고
    • Spred-1 negatively regulates interleukin-3-mediated ERK/mitogen-activated protein (MAP) kinase activation in hematopoietic cells
    • Nonami, A.; Kato, R.; Taniguchi, K.; Yoshiga, D.; Taketomi, T.; Fukuyama, S.; Harada, M.; Sasaki, A.; Yoshimura, A. Spred-1 negatively regulates interleukin-3-mediated ERK/mitogen-activated protein (MAP) kinase activation in hematopoietic cells. J. Biol. Chem., 2004, 279, 52543-52551.
    • (2004) J. Biol. Chem , vol.279 , pp. 52543-52551
    • Nonami, A.1    Kato, R.2    Taniguchi, K.3    Yoshiga, D.4    Taketomi, T.5    Fukuyama, S.6    Harada, M.7    Sasaki, A.8    Yoshimura, A.9
  • 44
    • 33747788689 scopus 로고    scopus 로고
    • Leukemia-associated, constitutively active mutants of SHP2 protein tyrosine phosphatase inhibit NF1 transcriptional activation by the interferon consensus sequence binding protein
    • Huang, W.; Saberwal, G.; Horvath, E.; Zhu, C.; Lindsey, S.; Eklund, E.A. Leukemia-associated, constitutively active mutants of SHP2 protein tyrosine phosphatase inhibit NF1 transcriptional activation by the interferon consensus sequence binding protein. Mol. Cell. Biol., 2006, 26, 6311-6332.
    • (2006) Mol. Cell. Biol , vol.26 , pp. 6311-6332
    • Huang, W.1    Saberwal, G.2    Horvath, E.3    Zhu, C.4    Lindsey, S.5    Eklund, E.A.6
  • 45
    • 0035968279 scopus 로고    scopus 로고
    • Phosphotyrosines 627 and 659 of Gab1 constitute a bisphosphoryl tyrosine-based activation motif (BTAM) conferring binding and activation of SHP2
    • Cunnick, J.M.; Mei, L.; Doupnik, C.A.; Wu, J. Phosphotyrosines 627 and 659 of Gab1 constitute a bisphosphoryl tyrosine-based activation motif (BTAM) conferring binding and activation of SHP2. J. Biol. Chem., 2001, 276, 24380-24387.
    • (2001) J. Biol. Chem , vol.276 , pp. 24380-24387
    • Cunnick, J.M.1    Mei, L.2    Doupnik, C.A.3    Wu, J.4
  • 47
    • 0037078320 scopus 로고    scopus 로고
    • Gab1 and SHP-2 promote Ras/MAPK regulation of epidermal growth and differentiation
    • Cai, T.; Nishida, K.; Hirano, T.; Khavari, P.A. Gab1 and SHP-2 promote Ras/MAPK regulation of epidermal growth and differentiation. J.Cell. Biol., 2002, 159, 103-112.
    • (2002) J.Cell. Biol , vol.159 , pp. 103-112
    • Cai, T.1    Nishida, K.2    Hirano, T.3    Khavari, P.A.4
  • 48
    • 0027158159 scopus 로고
    • The insulin receptor substrate 1 associates with the SH2-containing phosphotyrosine phosphatase Syp
    • Kuhne, M.R.; Pawson, T.; Lienhard, G.E.; Feng, G.S. The insulin receptor substrate 1 associates with the SH2-containing phosphotyrosine phosphatase Syp. J. Biol. Chem., 1993, 268, 11479-11481.
    • (1993) J. Biol. Chem , vol.268 , pp. 11479-11481
    • Kuhne, M.R.1    Pawson, T.2    Lienhard, G.E.3    Feng, G.S.4
  • 49
    • 0031835659 scopus 로고    scopus 로고
    • Binding of Shp2 tyrosine phosphatase to FRS2 is essential for fibroblast growth factor-induced PC12 cell differentiation
    • Hadari, Y.R.; Kouhara, H.; Lax, I.; Schlessinger, J. Binding of Shp2 tyrosine phosphatase to FRS2 is essential for fibroblast growth factor-induced PC12 cell differentiation. Mol. Cell. Biol., 1998, 18, 3966-3973.
    • (1998) Mol. Cell. Biol , vol.18 , pp. 3966-3973
    • Hadari, Y.R.1    Kouhara, H.2    Lax, I.3    Schlessinger, J.4
  • 50
    • 0027179869 scopus 로고
    • The 64-kDa protein that associates with the platelet-derived growth factor receptor beta subunit via Tyr-1009 is the SH2-containing phosphotyrosine phosphatase Syp
    • Kazlauskas, A.; Feng, G.S.; Pawson, T.; Valius, M. The 64-kDa protein that associates with the platelet-derived growth factor receptor beta subunit via Tyr-1009 is the SH2-containing phosphotyrosine phosphatase Syp. Proc. Natl. Acad. Sci. U S A., 1993, 90, 6939-6943.
    • (1993) Proc. Natl. Acad. Sci. U S A , vol.90 , pp. 6939-6943
    • Kazlauskas, A.1    Feng, G.S.2    Pawson, T.3    Valius, M.4
  • 51
    • 0029860950 scopus 로고    scopus 로고
    • A novel membrane glycoprotein, SHPS-1, that binds the SH2-domaincontaining protein tyrosine phosphatase SHP-2 in response to mitogens and cell adhesion
    • Fujioka, Y.; Matozaki, T.; Noguchi, T.; Iwamatsu, A.; Yamao, T.; Takahashi, N.; Tsuda, M.; Takada, T.; Kasuga, M. A novel membrane glycoprotein, SHPS-1, that binds the SH2-domaincontaining protein tyrosine phosphatase SHP-2 in response to mitogens and cell adhesion. Mol. Cell. Biol., 1996, 16, 6887-6899.
    • (1996) Mol. Cell. Biol , vol.16 , pp. 6887-6899
    • Fujioka, Y.1    Matozaki, T.2    Noguchi, T.3    Iwamatsu, A.4    Yamao, T.5    Takahashi, N.6    Tsuda, M.7    Takada, T.8    Kasuga, M.9
  • 52
    • 0034052841 scopus 로고    scopus 로고
    • Dissecting the interaction of SHP-2 with PZR, an immunoglobulin family protein containing immunoreceptor tyrosine-based inhibitory motifs
    • Zhao, R.; Zhao, Z.J. Dissecting the interaction of SHP-2 with PZR, an immunoglobulin family protein containing immunoreceptor tyrosine-based inhibitory motifs. J. Biol. Chem., 2000, 275, 5453-5459.
    • (2000) J. Biol. Chem , vol.275 , pp. 5453-5459
    • Zhao, R.1    Zhao, Z.J.2
  • 53
    • 0030936012 scopus 로고    scopus 로고
    • The proteintyrosine phosphatase SHP-2 binds platelet/endothelial cell adhesion molecule-1 (PECAM-1) and forms a distinct signaling complex during platelet aggregation. Evidence for a mechanistic link between PECAM-1-and integrin-mediated cellular signaling
    • Jackson, D.E.; Ward, C.M.; Wang, R.; Newman, P.J. The proteintyrosine phosphatase SHP-2 binds platelet/endothelial cell adhesion molecule-1 (PECAM-1) and forms a distinct signaling complex during platelet aggregation. Evidence for a mechanistic link between PECAM-1-and integrin-mediated cellular signaling. J. Biol. Chem., 1997, 272, 6986-6993.
    • (1997) J. Biol. Chem , vol.272 , pp. 6986-6993
    • Jackson, D.E.1    Ward, C.M.2    Wang, R.3    Newman, P.J.4
  • 54
    • 0029844431 scopus 로고    scopus 로고
    • Multiple in vivo phosphorylated tyrosine phosphatase SHP-2 engages binding to Grb2 via tyrosine 584
    • Vogel, W.; Ullrich, A. Multiple in vivo phosphorylated tyrosine phosphatase SHP-2 engages binding to Grb2 via tyrosine 584. Cell Growth Differ., 1996, 7, 1589-1597.
    • (1996) Cell Growth Differ , vol.7 , pp. 1589-1597
    • Vogel, W.1    Ullrich, A.2
  • 55
    • 0037088682 scopus 로고    scopus 로고
    • Regulation of the mitogen-activated protein kinase signaling pathway by SHP2
    • Cunnick, J.M.; Meng, S.; Ren, Y.; Desponts, C.; Wang, H.G.; Djeu, J.Y.; Wu, J. Regulation of the mitogen-activated protein kinase signaling pathway by SHP2. J. Biol. Chem., 2002, 277, 9498-9504.
    • (2002) J. Biol. Chem , vol.277 , pp. 9498-9504
    • Cunnick, J.M.1    Meng, S.2    Ren, Y.3    Desponts, C.4    Wang, H.G.5    Djeu, J.Y.6    Wu, J.7
  • 56
    • 26844514477 scopus 로고    scopus 로고
    • Participation of both Gab1 and Gab2 in the activation of the ERK/MAPK pathway by epidermal growth factor
    • Meng, S.; Chen, Z.; Munoz-Antonia, T.; Wu, J. Participation of both Gab1 and Gab2 in the activation of the ERK/MAPK pathway by epidermal growth factor. Biochem. J., 2005, 391, 143-151.
    • (2005) Biochem. J , vol.391 , pp. 143-151
    • Meng, S.1    Chen, Z.2    Munoz-Antonia, T.3    Wu, J.4
  • 57
    • 84874368710 scopus 로고    scopus 로고
    • Grb2 controls phosphorylation of FGFR2 by inhibiting receptor kinase and Shp2 phosphatase activity
    • Ahmed, Z.; Lin, C.C.; Suen, K.M.; Melo, F.A.; Levitt, J.A.; Suhling, K.; Ladbury, J.E. Grb2 controls phosphorylation of FGFR2 by inhibiting receptor kinase and Shp2 phosphatase activity. J. Cell. Biol., 2013, 200, 493-504.
    • (2013) J. Cell. Biol , vol.200 , pp. 493-504
    • Ahmed, Z.1    Lin, C.C.2    Suen, K.M.3    Melo, F.A.4    Levitt, J.A.5    Suhling, K.6    Ladbury, J.E.7
  • 59
    • 84863308607 scopus 로고    scopus 로고
    • LST1/A is a myeloid leukocyte-specific transmembrane adaptor protein recruiting protein tyrosine phosphatases SHP-1 and SHP-2 to the plasma membrane
    • Draber, P.; Stepanek, O.; Hrdinka, M.; Drobek, A.; Chmatal, L.; Mala, L.; Ormsby, T.; Angelisova, P.; Horejsi, V.; Brdicka, T. LST1/A is a myeloid leukocyte-specific transmembrane adaptor protein recruiting protein tyrosine phosphatases SHP-1 and SHP-2 to the plasma membrane. J. Biol. Chem., 2012, 287, 22812-22821.
    • (2012) J. Biol. Chem , vol.287 , pp. 22812-22821
    • Draber, P.1    Stepanek, O.2    Hrdinka, M.3    Drobek, A.4    Chmatal, L.5    Mala, L.6    Ormsby, T.7    Angelisova, P.8    Horejsi, V.9    Brdicka, T.10
  • 60
    • 84891429151 scopus 로고    scopus 로고
    • Receptor tyrosine kinase ubiquitylation involves the dynamic regulation of Cbl-Spry2 by intersectin 1 and the Shp2 tyrosine phosphatase
    • Okur, M.N.; Russo, A.; O'Bryan, J.P. Receptor tyrosine kinase ubiquitylation involves the dynamic regulation of Cbl-Spry2 by intersectin 1 and the Shp2 tyrosine phosphatase. Mol. Cell. Biol., 2014, 34, 271-279.
    • (2014) Mol. Cell. Biol , vol.34 , pp. 271-279
    • Okur, M.N.1    Russo, A.2    O'Bryan, J.P.3
  • 61
    • 84880804841 scopus 로고    scopus 로고
    • The LDL receptor-related protein 1 (LRP1) regulates the PDGF signaling pathway by binding the protein phosphatase SHP-2 and modulating SHP-2-mediated PDGF signaling events
    • Craig, J.; Mikhailenko, I.; Noyes, N.; Migliorini, M.; Strickland, D.K. The LDL receptor-related protein 1 (LRP1) regulates the PDGF signaling pathway by binding the protein phosphatase SHP-2 and modulating SHP-2-mediated PDGF signaling events. PLoS One., 2013, 8, e70432.
    • (2013) PLoS One , vol.8
    • Craig, J.1    Mikhailenko, I.2    Noyes, N.3    Migliorini, M.4    Strickland, D.K.5
  • 62
  • 64
    • 0028837693 scopus 로고
    • Regulation of the Src tyrosine kinase and Syp tyrosine phosphatase by their cellular association
    • Peng, Z.Y.; Cartwright, C.A. Regulation of the Src tyrosine kinase and Syp tyrosine phosphatase by their cellular association. Oncogene, 1995, 11, 1955-1962.
    • (1995) Oncogene , vol.11 , pp. 1955-1962
    • Peng, Z.Y.1    Cartwright, C.A.2
  • 66
    • 84890451693 scopus 로고    scopus 로고
    • Heterogeneous nuclear ribonucleoprotein Q is a novel substrate of SH2 domaincontaining phosphatase-2
    • Watanabe, N.; Kato, T.; Fujita, H.; Kitagawa, S. Heterogeneous nuclear ribonucleoprotein Q is a novel substrate of SH2 domaincontaining phosphatase-2. J. Biochem., 2013, 154, 475-480.
    • (2013) J. Biochem , vol.154 , pp. 475-480
    • Watanabe, N.1    Kato, T.2    Fujita, H.3    Kitagawa, S.4
  • 67
    • 84877593143 scopus 로고    scopus 로고
    • Activating mutations in protein tyrosine phosphatase Ptpn11 (Shp2) enhance reactive oxygen species production that contributes to myeloproliferative disorder
    • Xu, D.; Zheng, H.; Yu, W.M.; Qu, C.K. Activating mutations in protein tyrosine phosphatase Ptpn11 (Shp2) enhance reactive oxygen species production that contributes to myeloproliferative disorder. PLoS One, 2013, 8, e63152.
    • (2013) PLoS One , vol.8
    • Xu, D.1    Zheng, H.2    Yu, W.M.3    Qu, C.K.4
  • 68
    • 0034644539 scopus 로고    scopus 로고
    • Cell signaling by receptor tyrosine kinases
    • Schlessinger, J. Cell signaling by receptor tyrosine kinases. Cell, 2000, 103, 211-225.
    • (2000) Cell , vol.103 , pp. 211-225
    • Schlessinger, J.1
  • 69
    • 32644444482 scopus 로고    scopus 로고
    • Recruitment of the tyrosine phosphatase Src homology 2 domain tyrosine phosphatase-2 to the p85 subunit of phosphatidylinositol-3 (PI-3) kinase is required for insulin-like growth factor-I-dependent PI-3 kinase activation in smooth muscle cells
    • Kwon, M.; Ling, Y.; Maile, L.A.; Badley-Clark, J.; Clemmons, D.R. Recruitment of the tyrosine phosphatase Src homology 2 domain tyrosine phosphatase-2 to the p85 subunit of phosphatidylinositol-3 (PI-3) kinase is required for insulin-like growth factor-I-dependent PI-3 kinase activation in smooth muscle cells. Endocrinology, 2006, 147, 1458-1465.
    • (2006) Endocrinology , vol.147 , pp. 1458-1465
    • Kwon, M.1    Ling, Y.2    Maile, L.A.3    Badley-Clark, J.4    Clemmons, D.R.5
  • 70
    • 34247221517 scopus 로고    scopus 로고
    • The scaffolding adapter Gab1 mediates vascular endothelial growth factor signaling and is required for endothelial cell migration and capillary formation
    • Laramee, M.; Chabot, C.; Cloutier, M.; Stenne, R.; Holgado-Madruga, M.; Wong, A.J; Royal, I. The scaffolding adapter Gab1 mediates vascular endothelial growth factor signaling and is required for endothelial cell migration and capillary formation. J. Biol. Chem., 2007, 282, 7758-7769.
    • (2007) J. Biol. Chem , vol.282 , pp. 7758-7769
    • Laramee, M.1    Chabot, C.2    Cloutier, M.3    Stenne, R.4    Holgado-Madruga, M.5    Wong, A.J.6    Royal, I.7
  • 71
    • 33751084570 scopus 로고    scopus 로고
    • Modulation of alpha-catenin Tyr phosphorylation by SHP2 positively effects cell transformation induced by the constitutively active FGFR3
    • Burks, J.; Agazie, Y.M. Modulation of alpha-catenin Tyr phosphorylation by SHP2 positively effects cell transformation induced by the constitutively active FGFR3. Oncogene, 2006, 25, 7166-7179.
    • (2006) Oncogene , vol.25 , pp. 7166-7179
    • Burks, J.1    Agazie, Y.M.2
  • 72
    • 0242490120 scopus 로고    scopus 로고
    • The phosphotyrosine phosphatase SHP2 is a critical mediator of transformation induced by the oncogenic fibroblast growth factor receptor 3
    • Agazie, Y.M.; Movilla, N.; Ischenko, I.; Hayman, M.J. The phosphotyrosine phosphatase SHP2 is a critical mediator of transformation induced by the oncogenic fibroblast growth factor receptor 3. Oncogene, 2003, 22, 6909-6918.
    • (2003) Oncogene , vol.22 , pp. 6909-6918
    • Agazie, Y.M.1    Movilla, N.2    Ischenko, I.3    Hayman, M.J.4
  • 73
    • 1842525884 scopus 로고    scopus 로고
    • SHP-2 regulates the phosphatidylinositide 3'-kinase/Akt pathway and suppresses caspase 3-mediated apoptosis
    • Ivins Zito, C.; Kontaridis, M.I.; Fornaro, M.; Feng, G.S.; Bennett, A.M. SHP-2 regulates the phosphatidylinositide 3'-kinase/Akt pathway and suppresses caspase 3-mediated apoptosis. J. Cell. Physiol., 2004, 199, 227-236.
    • (2004) J. Cell. Physiol , vol.199 , pp. 227-236
    • Ivins, Z.C.1    Kontaridis, M.I.2    Fornaro, M.3    Feng, G.S.4    Bennett, A.M.5
  • 75
    • 0029831486 scopus 로고    scopus 로고
    • Platelet-derived growth factor-dependent activation of phosphatidylinositol 3-kinase is regulated by receptor binding of SH2-domain-containing proteins which influence Ras activity
    • Klinghoffer, R.A.; Duckworth, B.; Valius, M.; Cantley, L.; Kazlauskas, A. Platelet-derived growth factor-dependent activation of phosphatidylinositol 3-kinase is regulated by receptor binding of SH2-domain-containing proteins which influence Ras activity. Mol. Cell. Biol., 1996, 16, 5905-5914.
    • (1996) Mol. Cell. Biol , vol.16 , pp. 5905-5914
    • Klinghoffer, R.A.1    Duckworth, B.2    Valius, M.3    Cantley, L.4    Kazlauskas, A.5
  • 76
    • 13844256522 scopus 로고    scopus 로고
    • The docking protein Gab1 is the primary mediator of EGF-stimulated activation of the PI-3K/Akt cell survival pathway
    • Mattoon, D.R.; Lamothe, B.; Lax, I.; Schlessinger, J. The docking protein Gab1 is the primary mediator of EGF-stimulated activation of the PI-3K/Akt cell survival pathway. BMC Biol., 2004, 2, 24.
    • (2004) BMC Biol , vol.2 , pp. 24
    • Mattoon, D.R.1    Lamothe, B.2    Lax, I.3    Schlessinger, J.4
  • 77
    • 0036258332 scopus 로고    scopus 로고
    • Receptor-specific regulation of phosphatidylinositol 3'-kinase activation by the protein tyrosine phosphatase Shp2
    • Zhang, S.Q.; Tsiaras, W.G.; Araki, T.; Wen, G.; Minichiello, L.; Klein, R.; Neel, B.G. Receptor-specific regulation of phosphatidylinositol 3'-kinase activation by the protein tyrosine phosphatase Shp2. Mol. Cell. Biol., 2002, 22, 4062-4072.
    • (2002) Mol. Cell. Biol , vol.22 , pp. 4062-4072
    • Zhang, S.Q.1    Tsiaras, W.G.2    Araki, T.3    Wen, G.4    Minichiello, L.5    Klein, R.6    Neel, B.G.7
  • 78
    • 0346101802 scopus 로고    scopus 로고
    • SHP-2 regulates SOCS-1-mediated Janus kinase-2 ubiquitination/degradation downstream of the prolactin receptor
    • Ali, S.; Nouhi, Z.; Chughtai, N. SHP-2 regulates SOCS-1-mediated Janus kinase-2 ubiquitination/degradation downstream of the prolactin receptor. J. Biol. Chem., 2003, 278, 52021-52031.
    • (2003) J. Biol. Chem , vol.278 , pp. 52021-52031
    • Ali, S.1    Nouhi, Z.2    Chughtai, N.3
  • 79
    • 33845939336 scopus 로고    scopus 로고
    • Conditional deletion of Shp2 in the mammary gland leads to impaired lobulo-alveolar outgrowth and attenuated Stat5 activation
    • Ke, Y.; Lesperance, J.; Zhang, E.E.; Bard-Chapeau, E.A.; Oshima, R.G.; Muller, W.J.; Feng, G.S. Conditional deletion of Shp2 in the mammary gland leads to impaired lobulo-alveolar outgrowth and attenuated Stat5 activation. J. Biol. Chem., 2006, 281, 34374-34380.
    • (2006) J. Biol. Chem , vol.281 , pp. 34374-34380
    • Ke, Y.1    Lesperance, J.2    Zhang, E.E.3    Bard-Chapeau, E.A.4    Oshima, R.G.5    Muller, W.J.6    Feng, G.S.7
  • 80
    • 0141567655 scopus 로고    scopus 로고
    • A definitive role of Shp-2 tyrosine phosphatase in mediating embryonic stem cell differentiation and hematopoiesis
    • Chan, R.J.; Johnson, S.A.; Li, Y.; Yoder, M.C.; Feng, G.S. A definitive role of Shp-2 tyrosine phosphatase in mediating embryonic stem cell differentiation and hematopoiesis. Blood, 2003, 102, 2074-2080.
    • (2003) Blood , vol.102 , pp. 2074-2080
    • Chan, R.J.1    Johnson, S.A.2    Li, Y.3    Yoder, M.C.4    Feng, G.S.5
  • 81
    • 0032127977 scopus 로고    scopus 로고
    • Self-renewal of pluripotent embryonic stem cells is mediated via activation of STAT3
    • Niwa, H.; Burdon, T.; Chambers, I.; Smith, A. Self-renewal of pluripotent embryonic stem cells is mediated via activation of STAT3. Genes Dev., 1998, 12, 2048-2060.
    • (1998) Genes Dev , vol.12 , pp. 2048-2060
    • Niwa, H.1    Burdon, T.2    Chambers, I.3    Smith, A.4
  • 82
    • 34748824069 scopus 로고    scopus 로고
    • Deletion of Shp2 in the brain leads to defective proliferation and differentiation in neural stem cells and early postnatal lethality
    • Ke, Y.; Zhang, E.E.; Hagihara, K.; Wu, D.; Pang, Y.; Klein, R.; Curran, T.; Ranscht, B.; Feng, G.S. Deletion of Shp2 in the brain leads to defective proliferation and differentiation in neural stem cells and early postnatal lethality. Mol. Cell. Biol., 2007, 27, 6706-6717.
    • (2007) Mol. Cell. Biol , vol.27 , pp. 6706-6717
    • Ke, Y.1    Zhang, E.E.2    Hagihara, K.3    Wu, D.4    Pang, Y.5    Klein, R.6    Curran, T.7    Ranscht, B.8    Feng, G.S.9
  • 84
    • 0032980574 scopus 로고    scopus 로고
    • Shp-2 tyrosine phosphatase functions as a negative regulator of the interferon-stimulated Jak/STAT pathway
    • You, M.; Yu, D.H.; Feng, G.S. Shp-2 tyrosine phosphatase functions as a negative regulator of the interferon-stimulated Jak/STAT pathway. Mol. Cell. Biol., 1999, 19, 2416-2424.
    • (1999) Mol. Cell. Biol , vol.19 , pp. 2416-2424
    • You, M.1    Yu, D.H.2    Feng, G.S.3
  • 85
    • 0034614626 scopus 로고    scopus 로고
    • Cytosolic tyrosine dephosphorylation of STAT5. Potential role of SHP-2 in STAT5 regulation
    • Yu, C.L.; Jin, Y.J.; Burakoff, S.J. Cytosolic tyrosine dephosphorylation of STAT5. Potential role of SHP-2 in STAT5 regulation. J. Biol. Chem., 2000, 275, 599-604.
    • (2000) J. Biol. Chem , vol.275 , pp. 599-604
    • Yu, C.L.1    Jin, Y.J.2    Burakoff, S.J.3
  • 86
    • 2442711624 scopus 로고    scopus 로고
    • A negative role of SHP-2 tyrosine phosphatase in growth factor-dependent hematopoietic cell survival
    • Chen, J.; Yu, W.M.; Bunting, K.D.; Qu, C.K. A negative role of SHP-2 tyrosine phosphatase in growth factor-dependent hematopoietic cell survival. Oncogene, 2004, 23, 3659-3669.
    • (2004) Oncogene , vol.23 , pp. 3659-3669
    • Chen, J.1    Yu, W.M.2    Bunting, K.D.3    Qu, C.K.4
  • 87
    • 0037163109 scopus 로고    scopus 로고
    • Prolactin induces SHP-2 association with Stat5, nuclear translocation, and binding to the beta-casein gene promoter in mammary cells
    • Chughtai, N.; Schimchowitsch, S.; Lebrun, J.J.; Ali, S. Prolactin induces SHP-2 association with Stat5, nuclear translocation, and binding to the beta-casein gene promoter in mammary cells. J. Biol. Chem., 2002, 277, 31107-31114.
    • (2002) J. Biol. Chem , vol.277 , pp. 31107-31114
    • Chughtai, N.1    Schimchowitsch, S.2    Lebrun, J.J.3    Ali, S.4
  • 88
    • 57749107715 scopus 로고    scopus 로고
    • Nuclear protein tyrosine phosphatase Shp-2 is one important negative regulator of nuclear export of telomerase reverse transcriptase
    • Jakob, S.; Schroeder, P.; Lukosz, M.; Buchner, N.; Spyridopoulos, I.; Altschmied, J.; Haendeler, J. Nuclear protein tyrosine phosphatase Shp-2 is one important negative regulator of nuclear export of telomerase reverse transcriptase. J. Biol. Chem., 2008, 283, 33155-33161.
    • (2008) J. Biol. Chem , vol.283 , pp. 33155-33161
    • Jakob, S.1    Schroeder, P.2    Lukosz, M.3    Buchner, N.4    Spyridopoulos, I.5    Altschmied, J.6    Haendeler, J.7
  • 89
    • 1842611977 scopus 로고    scopus 로고
    • Antioxidants inhibit nuclear export of telomerase reverse transcriptase and delay replicative senescence of endothelial cells
    • Haendeler, J.; Hoffmann, J.; Diehl, J.F.; Vasa, M.; Spyridopoulos, I.; Zeiher, A.M.; Dimmeler, S. Antioxidants inhibit nuclear export of telomerase reverse transcriptase and delay replicative senescence of endothelial cells. Circ. Res., 2004, 94, 768-775.
    • (2004) Circ. Res , vol.94 , pp. 768-775
    • Haendeler, J.1    Hoffmann, J.2    Diehl, J.F.3    Vasa, M.4    Spyridopoulos, I.5    Zeiher, A.M.6    Dimmeler, S.7
  • 90
    • 0038012669 scopus 로고    scopus 로고
    • Role of SHP-2 tyrosine phosphatase in the DNA damage-induced cell death response
    • Yuan, L.; Yu, W.M.; Yuan, Z.; Haudenschild, C.C.; Qu, C.K. Role of SHP-2 tyrosine phosphatase in the DNA damage-induced cell death response. J. Biol. Chem., 2003, 278, 15208-15216.
    • (2003) J. Biol. Chem , vol.278 , pp. 15208-15216
    • Yuan, L.1    Yu, W.M.2    Yuan, Z.3    Haudenschild, C.C.4    Qu, C.K.5
  • 91
    • 30044448590 scopus 로고    scopus 로고
    • SHP-2 phosphatase regulates DNA damage-induced apoptosis and G2/M arrest in catalytically dependent and independent manners, respectively
    • Yuan, L.; Yu, W.M.; Xu, M.; Qu, C.K. SHP-2 phosphatase regulates DNA damage-induced apoptosis and G2/M arrest in catalytically dependent and independent manners, respectively. J. Biol. Chem., 2005, 280, 42701-42706.
    • (2005) J. Biol. Chem , vol.280 , pp. 42701-42706
    • Yuan, L.1    Yu, W.M.2    Xu, M.3    Qu, C.K.4
  • 92
    • 33646555522 scopus 로고    scopus 로고
    • Parafibromin/Hyrax activates Wnt/Wg target gene transcription by direct association with beta-catenin/Armadillo
    • Mosimann, C.; Hausmann, G.; Basler, K. Parafibromin/Hyrax activates Wnt/Wg target gene transcription by direct association with beta-catenin/Armadillo. Cell, 2006, 125, 327-341.
    • (2006) Cell , vol.125 , pp. 327-341
    • Mosimann, C.1    Hausmann, G.2    Basler, K.3
  • 94
    • 19044382634 scopus 로고    scopus 로고
    • The novel role of the C-terminal region of SHP-2. Involvement of Gab1 and SHP-2 phosphatase activity in Elk-1 activation
    • Huang, Q.; Lerner-Marmarosh, N.; Che, W.; Ohta, S.; Osawa, M.; Yoshizumi, M.; Glassman, M.; Yan, C.; Berk, B.C.; Abe, J. The novel role of the C-terminal region of SHP-2. Involvement of Gab1 and SHP-2 phosphatase activity in Elk-1 activation. J. Biol. Chem., 2002, 277, 29330-29341.
    • (2002) J. Biol. Chem , vol.277 , pp. 29330-29341
    • Huang, Q.1    Lerner-Marmarosh, N.2    Che, W.3    Ohta, S.4    Osawa, M.5    Yoshizumi, M.6    Glassman, M.7    Yan, C.8    Berk, B.C.9    Abe, J.10
  • 95
    • 3142723480 scopus 로고    scopus 로고
    • ERK1/2 associates with the c-Met-binding domain of growth factor receptor-bound protein 2 (Grb2)-associated binder-1 (Gab1): Role in ERK1/2 and early growth response factor-1 (Egr-1) nuclear accumulation
    • Osawa, M.; Itoh, S.; Ohta, S.; Huang, Q.; Berk, B.C.; Marmarosh, N.L.; Che, W.; Ding, B.; Yan, C.; Abe, J. ERK1/2 associates with the c-Met-binding domain of growth factor receptor-bound protein 2 (Grb2)-associated binder-1 (Gab1): role in ERK1/2 and early growth response factor-1 (Egr-1) nuclear accumulation. J. Biol. Chem., 2004, 279, 29691-29699.
    • (2004) J. Biol. Chem , vol.279 , pp. 29691-29699
    • Osawa, M.1    Itoh, S.2    Ohta, S.3    Huang, Q.4    Berk, B.C.5    Marmarosh, N.L.6    Che, W.7    Ding, B.8    Yan, C.9    Abe, J.10
  • 96
    • 33144473897 scopus 로고    scopus 로고
    • Gain-of-function/Noonan syndrome SHP-2/Ptpn11 mutants enhance calcium oscillations and impair NFAT signaling
    • Uhlen, P.; Burch, P.M.; Zito, C.I.; Estrada, M.; Ehrlich, B.E.; Bennett, A.M. Gain-of-function/Noonan syndrome SHP-2/Ptpn11 mutants enhance calcium oscillations and impair NFAT signaling. Proc. Natl. Acad. Sci. U S A., 2006, 103, 2160-2165.
    • (2006) Proc. Natl. Acad. Sci. U S A , vol.103 , pp. 2160-2165
    • Uhlen, P.1    Burch, P.M.2    Zito, C.I.3    Estrada, M.4    Ehrlich, B.E.5    Bennett, A.M.6
  • 97
    • 0032570586 scopus 로고    scopus 로고
    • The Shp-2 tyrosine phosphatase has opposite effects in mediating the activation of extracellular signalregulated and c-Jun NH2-terminal mitogen-activated protein kinases
    • Shi, Z.Q.; Lu, W.; Feng, G.S. The Shp-2 tyrosine phosphatase has opposite effects in mediating the activation of extracellular signalregulated and c-Jun NH2-terminal mitogen-activated protein kinases. J. Biol. Chem., 1998, 273, 4904-4908.
    • (1998) J. Biol. Chem , vol.273 , pp. 4904-4908
    • Shi, Z.Q.1    Lu, W.2    Feng, G.S.3
  • 100
    • 0346725939 scopus 로고    scopus 로고
    • Distinct domains in the SHP-2 phosphatase differentially regulate epidermal growth factor receptor/NF-kappaB activation through Gab1 in glioblastoma cells
    • Kapoor, G.S.; Zhan, Y.; Johnson, G.R.; O'Rourke, D.M. Distinct domains in the SHP-2 phosphatase differentially regulate epidermal growth factor receptor/NF-kappaB activation through Gab1 in glioblastoma cells. Mol. Cell. Biol., 2004, 24, 823-836.
    • (2004) Mol. Cell. Biol , vol.24 , pp. 823-836
    • Kapoor, G.S.1    Zhan, Y.2    Johnson, G.R.3    O'Rourke, D.M.4
  • 101
    • 0034681445 scopus 로고    scopus 로고
    • Requirement for protein-tyrosine phosphatase SHP-2 in insulin-induced activation of c-Jun NH(2)-terminal kinase
    • Fukunaga, K.; Noguchi, T.; Takeda, H.; Matozaki, T.; Hayashi, Y.; Itoh, H.; Kasuga, M. Requirement for protein-tyrosine phosphatase SHP-2 in insulin-induced activation of c-Jun NH(2)-terminal kinase. J. Biol. Chem., 2000, 275, 5208-5213.
    • (2000) J. Biol. Chem , vol.275 , pp. 5208-5213
    • Fukunaga, K.1    Noguchi, T.2    Takeda, H.3    Matozaki, T.4    Hayashi, Y.5    Itoh, H.6    Kasuga, M.7
  • 102
    • 41649085870 scopus 로고    scopus 로고
    • Deletion of Ptpn11 (Shp2) in cardiomyocytes causes dilated cardiomyopathy via effects on the extracellular signal-regulated kinase/mitogen-activated protein kinase and RhoA signaling pathways
    • Kontaridis, M.I.; Yang, W.; Bence, K.K.; Cullen, D.; Wang, B.; Bodyak, N.; Ke, Q.; Hinek, A.; Kang, P.M.; Liao, R.; Neel, B.G. Deletion of Ptpn11 (Shp2) in cardiomyocytes causes dilated cardiomyopathy via effects on the extracellular signal-regulated kinase/mitogen-activated protein kinase and RhoA signaling pathways. Circulation, 2008, 117, 1423-1435.
    • (2008) Circulation , vol.117 , pp. 1423-1435
    • Kontaridis, M.I.1    Yang, W.2    Bence, K.K.3    Cullen, D.4    Wang, B.5    Bodyak, N.6    Ke, Q.7    Hinek, A.8    Kang, P.M.9    Liao, R.10    Neel, B.G.11
  • 104
    • 0035865690 scopus 로고    scopus 로고
    • Requirement of Shp-2 tyrosine phosphatase in lymphoid and hematopoietic cell development
    • Qu, C.K.; Nguyen, S.; Chen, J.; Feng, G.S. Requirement of Shp-2 tyrosine phosphatase in lymphoid and hematopoietic cell development. Blood, 2001, 97, 911-914.
    • (2001) Blood , vol.97 , pp. 911-914
    • Qu, C.K.1    Nguyen, S.2    Chen, J.3    Feng, G.S.4
  • 107
    • 37749041167 scopus 로고    scopus 로고
    • Shp2 knockdown and Noonan/LEOPARD mutant Shp2-induced gastrulation defects
    • Jopling, C.; van Geemen, D.; den Hertog, J. Shp2 knockdown and Noonan/LEOPARD mutant Shp2-induced gastrulation defects. PLoS Genet., 2007, 3, e225.
    • (2007) PLoS Genet , vol.3
    • Jopling, C.1    van Geemen, D.2    den Hertog, J.3
  • 110
    • 77955574059 scopus 로고    scopus 로고
    • Noonan syndrome: Clinical aspects and molecular pathogenesis
    • Tartaglia, M.; Zampino, G.; Gelb, B.D. Noonan syndrome: clinical aspects and molecular pathogenesis. Mol. Syndromol., 2010, 1, 2-26.
    • (2010) Mol. Syndromol , vol.1 , pp. 2-26
    • Tartaglia, M.1    Zampino, G.2    Gelb, B.D.3
  • 111
    • 84861875277 scopus 로고    scopus 로고
    • PTPN11-associated mutations in the heart: Has LEOPARD changed Its RASpots?
    • Lauriol, J.; Kontaridis, M.I. PTPN11-associated mutations in the heart: has LEOPARD changed Its RASpots? Trends Cardiovasc. Med., 2011, 21, 97-104.
    • (2011) Trends Cardiovasc. Med , vol.21 , pp. 97-104
    • Lauriol, J.1    Kontaridis, M.I.2
  • 120
    • 84901498936 scopus 로고    scopus 로고
    • Rare copy number variations containing genes involved in RASopathies: Deletion of SHOC2 and duplication of PTPN11
    • Chen, J.L.; Zhu, X.; Zhao, T.L.; Wang, J.; Yang, Y.F.; Tan, Z.P. Rare copy number variations containing genes involved in RASopathies: deletion of SHOC2 and duplication of PTPN11. Mol. Cytogenet., 2014, 7, 28.
    • (2014) Mol. Cytogenet , vol.7 , pp. 28
    • Chen, J.L.1    Zhu, X.2    Zhao, T.L.3    Wang, J.4    Yang, Y.F.5    Tan, Z.P.6
  • 123
    • 24744465207 scopus 로고    scopus 로고
    • Diverse biochemical properties of Shp2 mutants. Implications for disease phenotypes
    • Keilhack, H.; David, F.S.; McGregor, M.; Cantley, L.C.; Neel, B.G. Diverse biochemical properties of Shp2 mutants. Implications for disease phenotypes. J. Biol. Chem., 2005, 280, 30984-30993.
    • (2005) J. Biol. Chem , vol.280 , pp. 30984-30993
    • Keilhack, H.1    David, F.S.2    McGregor, M.3    Cantley, L.C.4    Neel, B.G.5
  • 124
    • 70349304424 scopus 로고    scopus 로고
    • Noonan syndrome is associated with enhanced pERK activity, the repression of which can prevent craniofacial malformations
    • Nakamura, T.; Gulick, J.; Pratt, R.; Robbins, J. Noonan syndrome is associated with enhanced pERK activity, the repression of which can prevent craniofacial malformations. Proc. Natl. Acad. Sci. U S A., 2009, 106, 15436-15441.
    • (2009) Proc. Natl. Acad. Sci. U S A , vol.106 , pp. 15436-15441
    • Nakamura, T.1    Gulick, J.2    Pratt, R.3    Robbins, J.4
  • 126
    • 63849250390 scopus 로고    scopus 로고
    • Noonan syndrome cardiac defects are caused by PTPN11 acting in endocardium to enhance endocardialmesenchymal transformation
    • Araki, T.; Chan, G.; Newbigging, S.; Morikawa, L.; Bronson, R.T.; Neel, B.G. Noonan syndrome cardiac defects are caused by PTPN11 acting in endocardium to enhance endocardialmesenchymal transformation. Proc. Natl. Acad. Sci. U S A., 2009, 106, 4736-4741.
    • (2009) Proc. Natl. Acad. Sci. U S A , vol.106 , pp. 4736-4741
    • Araki, T.1    Chan, G.2    Newbigging, S.3    Morikawa, L.4    Bronson, R.T.5    Neel, B.G.6
  • 127
    • 34547656112 scopus 로고    scopus 로고
    • Mediating ERK 1/2 signaling rescues congenital heart defects in a mouse model of Noonan syndrome
    • Nakamura, T.; Colbert, M.; Krenz, M.; Molkentin, J.D.; Hahn, H.S.; Dorn, G.W. 2nd.; Robbins, J. Mediating ERK 1/2 signaling rescues congenital heart defects in a mouse model of Noonan syndrome. J. Clin. Invest., 2007, 117, 2123-2132.
    • (2007) J. Clin. Invest , vol.117 , pp. 2123-2132
    • Nakamura, T.1    Colbert, M.2    Krenz, M.3    Molkentin, J.D.4    Hahn, H.S.5    Dorn, G.W.6    Robbins, J.7
  • 130
    • 84899624551 scopus 로고    scopus 로고
    • Noonan and LEOPARD syndrome Shp2 variants induce heart displacement defects in zebrafish
    • Bonetti, M.; Paardekooper Overman, J.; Tessadori, F.; Noel, E.; Bakkers, J.; den Hertog, J. Noonan and LEOPARD syndrome Shp2 variants induce heart displacement defects in zebrafish. Development, 2014, 141, 1961-1970.
    • (2014) Development , vol.141 , pp. 1961-1970
    • Bonetti, M.1    Paardekooper, O.J.2    Tessadori, F.3    Noel, E.4    Bakkers, J.5    den Hertog, J.6
  • 131
    • 26844438820 scopus 로고    scopus 로고
    • Noonan syndrome mutation Q79R in Shp2 increases proliferation of valve primordia mesenchymal cells via extracellular signal-regulated kinase 1/2 signaling
    • Krenz, M.; Yutzey, K.E.; Robbins, J. Noonan syndrome mutation Q79R in Shp2 increases proliferation of valve primordia mesenchymal cells via extracellular signal-regulated kinase 1/2 signaling. Circ. Res., 2005, 97, 813-820.
    • (2005) Circ. Res , vol.97 , pp. 813-820
    • Krenz, M.1    Yutzey, K.E.2    Robbins, J.3
  • 132
    • 33646117025 scopus 로고    scopus 로고
    • Reduced phosphatase activity of SHP-2 in LEOPARD syndrome: Consequences for PI3K binding on Gab1
    • Hanna, N.; Montagner, A.; Lee, W.H.; Miteva, M.; Vidal, M.; Vidaud, M.; Parfait, B.; Raynal, P. Reduced phosphatase activity of SHP-2 in LEOPARD syndrome: consequences for PI3K binding on Gab1. FEBS Lett., 2006, 580, 2477-2482.
    • (2006) FEBS Lett , vol.580 , pp. 2477-2482
    • Hanna, N.1    Montagner, A.2    Lee, W.H.3    Miteva, M.4    Vidal, M.5    Vidaud, M.6    Parfait, B.7    Raynal, P.8
  • 138
    • 80053279943 scopus 로고    scopus 로고
    • LEOPARD-type SHP2 mutant Gln510Glu attenuates cardiomyocyte differentiation and promotes cardiac hypertrophy via dysregulation of Akt/GSK-3beta/betacatenin signaling
    • Ishida, H.; Kogaki, S.; Narita, J.; Ichimori, H.; Nawa, N.; Okada, Y.; Takahashi, K.; Ozono, K. LEOPARD-type SHP2 mutant Gln510Glu attenuates cardiomyocyte differentiation and promotes cardiac hypertrophy via dysregulation of Akt/GSK-3beta/betacatenin signaling. Am. J. Physiol. Heart Circ. Physiol., 2011, 301, H1531-H1539.
    • (2011) Am. J. Physiol. Heart Circ. Physiol , vol.301
    • Ishida, H.1    Kogaki, S.2    Narita, J.3    Ichimori, H.4    Nawa, N.5    Okada, Y.6    Takahashi, K.7    Ozono, K.8
  • 139
    • 84255192637 scopus 로고    scopus 로고
    • The PTPN11 loss-of-function mutation Q510E-Shp2 causes hypertrophic cardiomyopathy by dysregulating mTOR signaling
    • Schramm, C.; Fine, D.M.; Edwards, M.A.; Reeb, A.N.; Krenz, M. The PTPN11 loss-of-function mutation Q510E-Shp2 causes hypertrophic cardiomyopathy by dysregulating mTOR signaling. Am. J. Physiol. Heart Circ. Physiol., 2012, 302, H231-H243.
    • (2012) Am. J. Physiol. Heart Circ. Physiol , vol.302
    • Schramm, C.1    Fine, D.M.2    Edwards, M.A.3    Reeb, A.N.4    Krenz, M.5
  • 140
    • 0030797548 scopus 로고    scopus 로고
    • A deletion mutation in the SH2-N domain of Shp-2 severely suppresses hematopoietic cell development
    • Qu, C.K.; Shi, Z.Q.; Shen, R.; Tsai, F.Y.; Orkin, S.H.; Feng, G.S. A deletion mutation in the SH2-N domain of Shp-2 severely suppresses hematopoietic cell development. Mol. Cell. Biol., 1997, 17, 5499-5507.
    • (1997) Mol. Cell. Biol , vol.17 , pp. 5499-5507
    • Qu, C.K.1    Shi, Z.Q.2    Shen, R.3    Tsai, F.Y.4    Orkin, S.H.5    Feng, G.S.6
  • 141
    • 0031708674 scopus 로고    scopus 로고
    • Biased suppression of hematopoiesis and multiple developmental defects in chimeric mice containing Shp-2 mutant cells
    • Qu, C.K.; Yu, W.M.; Azzarelli, B.; Cooper, S.; Broxmeyer, H.E.; Feng, G.S. Biased suppression of hematopoiesis and multiple developmental defects in chimeric mice containing Shp-2 mutant cells. Mol. Cell. Biol., 1998, 18, 6075-6082.
    • (1998) Mol. Cell. Biol , vol.18 , pp. 6075-6082
    • Qu, C.K.1    Yu, W.M.2    Azzarelli, B.3    Cooper, S.4    Broxmeyer, H.E.5    Feng, G.S.6
  • 144
    • 3343005287 scopus 로고    scopus 로고
    • Mutations in PTPN11 are rare in adult myelodysplastic syndromes and acute myeloid leukemia
    • Watkins, F.; Fidler, C.; Boultwood, J.; Wainscoat, J.S. Mutations in PTPN11 are rare in adult myelodysplastic syndromes and acute myeloid leukemia. Am. J. Hematol., 2004, 76, 417.
    • (2004) Am. J. Hematol , vol.76 , pp. 417
    • Watkins, F.1    Fidler, C.2    Boultwood, J.3    Wainscoat, J.S.4
  • 148
    • 73849142941 scopus 로고    scopus 로고
    • Malignant diseases in Noonan syndrome and related disorders
    • Hasle, H. Malignant diseases in Noonan syndrome and related disorders. Horm. Res., 2009, 72 Suppl 2, 8-14.
    • (2009) Horm. Res , vol.72 , Issue.SUPPL. 2 , pp. 8-14
    • Hasle, H.1
  • 149
    • 0030665934 scopus 로고    scopus 로고
    • Myeloid disorders in infants with Noonan syndrome and a resident's rule recalled
    • Side, L.E.; Shannon, K.M. Myeloid disorders in infants with Noonan syndrome and a resident's rule recalled. J. Pediatr., 1997, 130, 857-859.
    • (1997) J. Pediatr , vol.130 , pp. 857-859
    • Side, L.E.1    Shannon, K.M.2
  • 152
    • 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
  • 153
    • 22044452124 scopus 로고    scopus 로고
    • Functional analysis of leukemia-associated PTPN11 mutations in primary hematopoietic cells
    • Schubbert, S.; Lieuw, K.; Rowe, S.L.; Lee, C.M.; Li, X.; Loh, M.L.; Clapp, D.W.; Shannon, K.M. Functional analysis of leukemia-associated PTPN11 mutations in primary hematopoietic cells. Blood, 2005, 106, 311-317.
    • (2005) Blood , vol.106 , pp. 311-317
    • Schubbert, S.1    Lieuw, K.2    Rowe, S.L.3    Lee, C.M.4    Li, X.5    Loh, M.L.6    Clapp, D.W.7    Shannon, K.M.8
  • 155
    • 33947594129 scopus 로고    scopus 로고
    • Hyperactive Ras in developmental disorders and cancer
    • Schubbert, S.; Shannon, K.; Bollag, G. Hyperactive Ras in developmental disorders and cancer. Nat. Rev. Cancer, 2007, 7, 295-308.
    • (2007) Nat. Rev. Cancer , vol.7 , pp. 295-308
    • Schubbert, S.1    Shannon, K.2    Bollag, G.3
  • 156
    • 33646842917 scopus 로고    scopus 로고
    • Effects of a leukemia-associated gain-of-function mutation of SHP-2 phosphatase on interleukin-3 signaling
    • Yu, W.M.; Daino, H.; Chen, J.; Bunting, K.D.; Qu, C.K. Effects of a leukemia-associated gain-of-function mutation of SHP-2 phosphatase on interleukin-3 signaling. J. Biol. Chem., 2006, 281, 5426-5434.
    • (2006) J. Biol. Chem , vol.281 , pp. 5426-5434
    • Yu, W.M.1    Daino, H.2    Chen, J.3    Bunting, K.D.4    Qu, C.K.5
  • 157
    • 63849313577 scopus 로고    scopus 로고
    • Leukemogenic Ptpn11 causes fatal myeloproliferative disorder via cell-autonomous effects on multiple stages of hematopoiesis
    • Chan, G.; Kalaitzidis, D.; Usenko, T.; Kutok, J.L.; Yang, W.; Mohi, M.G.; Neel, B.G. Leukemogenic Ptpn11 causes fatal myeloproliferative disorder via cell-autonomous effects on multiple stages of hematopoiesis. Blood, 2009, 113, 4414-4424.
    • (2009) Blood , vol.113 , pp. 4414-4424
    • Chan, G.1    Kalaitzidis, D.2    Usenko, T.3    Kutok, J.L.4    Yang, W.5    Mohi, M.G.6    Neel, B.G.7
  • 158
    • 78149299101 scopus 로고    scopus 로고
    • A germline gain-of-function mutation in Ptpn11 (Shp-2) phosphatase induces myeloproliferative disease by aberrant activation of hematopoietic stem cells
    • Xu, D.; Wang, S.; Yu, W.M.; Chan, G.; Araki, T.; Bunting, K.D.; Neel, B.G.; Qu, C.K. A germline gain-of-function mutation in Ptpn11 (Shp-2) phosphatase induces myeloproliferative disease by aberrant activation of hematopoietic stem cells. Blood, 2010, 116, 3611-3621.
    • (2010) Blood , vol.116 , pp. 3611-3621
    • Xu, D.1    Wang, S.2    Yu, W.M.3    Chan, G.4    Araki, T.5    Bunting, K.D.6    Neel, B.G.7    Qu, C.K.8
  • 159
    • 0028344097 scopus 로고
    • Mutations of the N-ras gene in juvenile chronic myelogenous leukemia
    • Miyauchi, J.; Asada, M.; Sasaki, M.; Tsunematsu, Y.; Kojima, S.; Mizutani, S. Mutations of the N-ras gene in juvenile chronic myelogenous leukemia. Blood, 1994, 83, 2248-2254.
    • (1994) Blood , vol.83 , pp. 2248-2254
    • Miyauchi, J.1    Asada, M.2    Sasaki, M.3    Tsunematsu, Y.4    Kojima, S.5    Mizutani, S.6
  • 160
    • 0030947237 scopus 로고    scopus 로고
    • Homozygous inactivation of the NF1 gene in bone marrow cells from children with neurofibromatosis type 1 and malignant myeloid disorders
    • Side, L.; Taylor, B.; Cayouette, M.; Conner, E.; Thompson, P.; Luce, M.; Shannon, K. Homozygous inactivation of the NF1 gene in bone marrow cells from children with neurofibromatosis type 1 and malignant myeloid disorders. N. Engl. J. Med., 1997, 336, 1713-1720.
    • (1997) N. Engl. J. Med , vol.336 , pp. 1713-1720
    • Side, L.1    Taylor, B.2    Cayouette, M.3    Conner, E.4    Thompson, P.5    Luce, M.6    Shannon, K.7
  • 161
    • 65549086595 scopus 로고    scopus 로고
    • SHP-2 tyrosine phosphatase in human diseases
    • Zheng, H.; Alter, S.; Qu, C.K. SHP-2 tyrosine phosphatase in human diseases. Int. J. Clin. Exp. Med., 2009, 2, 17-25.
    • (2009) Int. J. Clin. Exp. Med , vol.2 , pp. 17-25
    • Zheng, H.1    Alter, S.2    Qu, C.K.3
  • 165
    • 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
  • 167
    • 84864367909 scopus 로고    scopus 로고
    • Global cancer transitions according to the Human Development Index (2008-2030): A population-based study
    • Bray, F.; Jemal, A.; Grey, N.; Ferlay, J.; Forman, D. Global cancer transitions according to the Human Development Index (2008-2030): a population-based study. Lancet Oncol., 2012, 13, 790-801.
    • (2012) Lancet Oncol , vol.13 , pp. 790-801
    • Bray, F.1    Jemal, A.2    Grey, N.3    Ferlay, J.4    Forman, D.5
  • 169
    • 70449096096 scopus 로고    scopus 로고
    • Helicobacter pylori and gastric adenocarcinoma
    • Herrera, V.; Parsonnet, J. Helicobacter pylori and gastric adenocarcinoma. Clin. Microbiol. Infect., 2009, 15, 971-976.
    • (2009) Clin. Microbiol. Infect , vol.15 , pp. 971-976
    • Herrera, V.1    Parsonnet, J.2
  • 170
    • 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
  • 171
    • 77952534140 scopus 로고    scopus 로고
    • Helicobacter pylori infection, oncogenic pathways and epigenetic mechanisms in gastric carcinogenesis
    • Ding, S.Z.; Goldberg, J.B.; Hatakeyama, M. Helicobacter pylori infection, oncogenic pathways and epigenetic mechanisms in gastric carcinogenesis. Future Oncol., 2010, 6, 851-862.
    • (2010) Future Oncol , vol.6 , pp. 851-862
    • Ding, S.Z.1    Goldberg, J.B.2    Hatakeyama, M.3
  • 172
    • 0037169076 scopus 로고    scopus 로고
    • SHP-2 tyrosine phosphatase as an intracellular target of Helicobacter pylori CagA protein
    • Higashi, H.; Tsutsumi, R.; Muto, S.; Sugiyama, T.; Azuma, T.; Asaka, M.; Hatakeyama, M. SHP-2 tyrosine phosphatase as an intracellular target of Helicobacter pylori CagA protein. Science, 2002, 295, 683-686.
    • (2002) Science , vol.295 , pp. 683-686
    • Higashi, H.1    Tsutsumi, R.2    Muto, S.3    Sugiyama, T.4    Azuma, T.5    Asaka, M.6    Hatakeyama, M.7
  • 173
    • 65049086892 scopus 로고    scopus 로고
    • Helicobacter pylori and gastric carcinogenesis
    • Hatakeyama, M. Helicobacter pylori and gastric carcinogenesis. J. Gastroenterol., 2009, 44, 239-248.
    • (2009) J. Gastroenterol , vol.44 , pp. 239-248
    • Hatakeyama, M.1
  • 174
    • 30344457320 scopus 로고    scopus 로고
    • Helicobacter pylori CagA: A new paradigm for bacterial carcinogenesis
    • Hatakeyama, M.; Higashi, H. Helicobacter pylori CagA: a new paradigm for bacterial carcinogenesis. Cancer Sci., 2005, 96, 835-843.
    • (2005) Cancer Sci , vol.96 , pp. 835-843
    • Hatakeyama, M.1    Higashi, H.2
  • 175
    • 3042545272 scopus 로고    scopus 로고
    • Conditional gene silencing utilizing the lac repressor reveals a role of SHP-2 in cagA-positive Helicobacter pylori pathogenicity
    • Higuchi, M.; Tsutsumi, R.; Higashi, H.; Hatakeyama, M. Conditional gene silencing utilizing the lac repressor reveals a role of SHP-2 in cagA-positive Helicobacter pylori pathogenicity. Cancer Sci., 2004, 95, 442-447.
    • (2004) Cancer Sci , vol.95 , pp. 442-447
    • Higuchi, M.1    Tsutsumi, R.2    Higashi, H.3    Hatakeyama, M.4
  • 177
    • 0036512370 scopus 로고    scopus 로고
    • B-Raf/Rap1 signaling, but not c-Raf-1/Ras, induces the histidine decarboxylase promoter in Helicobacter pylori infection
    • Wessler, S.; Rapp, U.R.; Wiedenmann, B.; Meyer, T.F.; Schoneberg, T.; Hocker, M.; Naumann, M. B-Raf/Rap1 signaling, but not c-Raf-1/Ras, induces the histidine decarboxylase promoter in Helicobacter pylori infection. FASEB J., 2002, 16, 417-419.
    • (2002) FASEB J , vol.16 , pp. 417-419
    • Wessler, S.1    Rapp, U.R.2    Wiedenmann, B.3    Meyer, T.F.4    Schoneberg, T.5    Hocker, M.6    Naumann, M.7
  • 180
    • 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
  • 181
    • 0033604644 scopus 로고    scopus 로고
    • Shp-2 tyrosine phosphatase: Signaling one cell or many
    • Feng, G.S. Shp-2 tyrosine phosphatase: signaling one cell or many. Exp. Cell Res., 1999, 253, 47-54.
    • (1999) Exp. Cell Res , vol.253 , pp. 47-54
    • Feng, G.S.1
  • 182
    • 77954424609 scopus 로고    scopus 로고
    • Overexpression of protein phosphatase non-receptor type 11 (PTPN11) in gastric carcinomas
    • Kim, J.S.; Shin, O.R.; Kim, H.K.; Cho, Y.S.; An, C.H.; Lim, K.W.; Kim, S.S. Overexpression of protein phosphatase non-receptor type 11 (PTPN11) in gastric carcinomas. Dig. Dis. Sci., 2010, 55, 1565-1569.
    • (2010) Dig. Dis. Sci , vol.55 , pp. 1565-1569
    • Kim, J.S.1    Shin, O.R.2    Kim, H.K.3    Cho, Y.S.4    An, C.H.5    Lim, K.W.6    Kim, S.S.7
  • 183
    • 33749267414 scopus 로고    scopus 로고
    • Protein tyrosine-phosphatase expression profiling in gastric cancer tissues
    • Wu, C.W.; Kao, H.L.; Li, A.F.; Chi, C.W.; Lin, W.C. Protein tyrosine-phosphatase expression profiling in gastric cancer tissues. Cancer Lett., 2006, 242, 95-103.
    • (2006) Cancer Lett , vol.242 , pp. 95-103
    • Wu, C.W.1    Kao, H.L.2    Li, A.F.3    Chi, C.W.4    Lin, W.C.5
  • 187
    • 68249139901 scopus 로고    scopus 로고
    • Associations of a PTPN11 G/A polymorphism at intron 3 with Helicobactor pylori seropositivity, gastric atrophy and gastric cancer in Japanese
    • Hishida, A.; Matsuo, K.; Goto, Y.; Naito, M.; Wakai, K.; Tajima, K.; Hamajima, N. Associations of a PTPN11 G/A polymorphism at intron 3 with Helicobactor pylori seropositivity, gastric atrophy and gastric cancer in Japanese. BMC Gastroenterol., 2009, 9, 51.
    • (2009) BMC Gastroenterol , vol.9 , pp. 51
    • Hishida, A.1    Matsuo, K.2    Goto, Y.3    Naito, M.4    Wakai, K.5    Tajima, K.6    Hamajima, N.7
  • 189
    • 84907354428 scopus 로고    scopus 로고
    • PTPN11 Gene polymorphisms, helicobacter pylori infection and susceptibility to gastric cancer in liuzhou area of guangxi province in China
    • Hu, H.B.; Liang, X.L.; He, J.M. PTPN11 Gene polymorphisms, helicobacter pylori infection and susceptibility to gastric cancer in liuzhou area of guangxi province in China. J. Trop. Med., 2009, 9, 1233-1237.
    • (2009) J. Trop. Med , vol.9 , pp. 1233-1237
    • Hu, H.B.1    Liang, X.L.2    He, J.M.3
  • 190
    • 85027935941 scopus 로고    scopus 로고
    • Meta-analysis of the Association Between PTPN11 G/A Polymorphism at Intron 3 with Risk of Gastric Atrophy Among East Asians
    • Pabalan, N.; Singh, N.; Pineda, M.R.; Jarjanazi, H. Meta-analysis of the Association Between PTPN11 G/A Polymorphism at Intron 3 with Risk of Gastric Atrophy Among East Asians. J. Gastrointest. Cancer, 2014.
    • (2014) J. Gastrointest. Cancer
    • Pabalan, N.1    Singh, N.2    Pineda, M.R.3    Jarjanazi, H.4
  • 191
    • 33846084355 scopus 로고    scopus 로고
    • Grb2-associated binder 1 polymorphism was associated with the risk of Helicobactor pylori infection and gastric atrophy
    • Goto, Y.; Ando, T.; Nishio, K.; Kawai, S.; Ishida, Y.; Naito, M.; Goto, H.; Hamajima, N. Grb2-associated binder 1 polymorphism was associated with the risk of Helicobactor pylori infection and gastric atrophy. Int. J. Med. Sci., 2007, 4, 1-6.
    • (2007) Int. J. Med. Sci , vol.4 , pp. 1-6
    • Goto, Y.1    Ando, T.2    Nishio, K.3    Kawai, S.4    Ishida, Y.5    Naito, M.6    Goto, H.7    Hamajima, N.8
  • 194
    • 44049086087 scopus 로고    scopus 로고
    • SHP2 is upregulated in breast cancer cells and in infiltrating ductal carcinoma of the breast, implying its involvement in breast oncogenesis
    • Zhou, X.; Coad, J.; Ducatman, B.; Agazie, Y.M. SHP2 is upregulated in breast cancer cells and in infiltrating ductal carcinoma of the breast, implying its involvement in breast oncogenesis. Histopathology, 2008, 53, 389-402.
    • (2008) Histopathology , vol.53 , pp. 389-402
    • Zhou, X.1    Coad, J.2    Ducatman, B.3    Agazie, Y.M.4
  • 196
    • 0034729686 scopus 로고    scopus 로고
    • Shp-2 mediates v-Src-induced morphological changes and activation of the anti-apoptotic protein kinase Akt
    • Hakak, Y.; Hsu, Y.S.; Martin, G.S. Shp-2 mediates v-Src-induced morphological changes and activation of the anti-apoptotic protein kinase Akt. Oncogene, 2000, 19, 3164-3171.
    • (2000) Oncogene , vol.19 , pp. 3164-3171
    • Hakak, Y.1    Hsu, Y.S.2    Martin, G.S.3
  • 197
    • 67649224094 scopus 로고    scopus 로고
    • The protein tyrosine phosphatase SHP-2 is required for EGFRvIII oncogenic transformation in human glioblastoma cells
    • Zhan, Y.; Counelis, G.J.; O'Rourke, D.M. The protein tyrosine phosphatase SHP-2 is required for EGFRvIII oncogenic transformation in human glioblastoma cells. Exp. Cell Res., 2009, 315, 2343-2357.
    • (2009) Exp. Cell Res , vol.315 , pp. 2343-2357
    • Zhan, Y.1    Counelis, G.J.2    O'Rourke, D.M.3
  • 198
    • 44049108733 scopus 로고    scopus 로고
    • Inhibition of SHP2 leads to mesenchymal to epithelial transition in breast cancer cells
    • Zhou, X.D.; Agazie, Y.M. Inhibition of SHP2 leads to mesenchymal to epithelial transition in breast cancer cells. Cell Death Differ., 2008, 15, 988-996.
    • (2008) Cell Death Differ , vol.15 , pp. 988-996
    • Zhou, X.D.1    Agazie, Y.M.2
  • 202
    • 84863095061 scopus 로고    scopus 로고
    • The tumor suppressor role of Src homology phosphotyrosine phosphatase 2 in hepatocellular carcinoma
    • Jiang, C.; Hu, F.; Tai, Y.; Du, J.; Mao, B.; Yuan, Z.; Wang, Y.; Wei, L. The tumor suppressor role of Src homology phosphotyrosine phosphatase 2 in hepatocellular carcinoma. J. Cancer Res. Clin. Oncol., 2012, 138, 637-646.
    • (2012) J. Cancer Res. Clin. Oncol , vol.138 , pp. 637-646
    • Jiang, C.1    Hu, F.2    Tai, Y.3    Du, J.4    Mao, B.5    Yuan, Z.6    Wang, Y.7    Wei, L.8
  • 203
    • 84885034861 scopus 로고    scopus 로고
    • Expression of SHP2 and related markers in non-small cell lung cancer: A tissue microarray study of 80 cases
    • Tang, C.; Luo, D.; Yang, H.; Wang, Q.; Zhang, R.; Liu, G.; Zhou, X. Expression of SHP2 and related markers in non-small cell lung cancer: a tissue microarray study of 80 cases. Appl. Immunohistochem. Mol. Morphol., 2013, 21, 386-394.
    • (2013) Appl. Immunohistochem. Mol. Morphol , vol.21 , pp. 386-394
    • Tang, C.1    Luo, D.2    Yang, H.3    Wang, Q.4    Zhang, R.5    Liu, G.6    Zhou, X.7
  • 205
    • 79955941397 scopus 로고    scopus 로고
    • SPARCL1, Shp2, MSH2, E-cadherin, p53, ADCY-2 and MAPK are prognosis-related in colorectal cancer
    • Yu, S.J.; Yu, J.K.; Ge, W.T.; Hu, H.G.; Yuan, Y.; Zheng, S. SPARCL1, Shp2, MSH2, E-cadherin, p53, ADCY-2 and MAPK are prognosis-related in colorectal cancer. World J. Gastroenterol., 2011, 17, 2028-2036.
    • (2011) World J. Gastroenterol , vol.17 , pp. 2028-2036
    • Yu, S.J.1    Yu, J.K.2    Ge, W.T.3    Hu, H.G.4    Yuan, Y.5    Zheng, S.6
  • 206
    • 84901506374 scopus 로고    scopus 로고
    • Protein Tyrosine Phosphatases PTP-1B, SHP-2, and PTEN Facilitate Rb/E2FAssociated Apoptotic Signaling
    • Morales, L.D.; Casillas Pavon, E.A.; Shin, J.W.; Garcia, A.; Capetillo, M.; Kim, D.J.; Lieman, J.H. Protein Tyrosine Phosphatases PTP-1B, SHP-2, and PTEN Facilitate Rb/E2FAssociated Apoptotic Signaling. PLoS One, 2014, 9, e97104.
    • (2014) PLoS One , vol.9
    • Morales, L.D.1    Casillas, P.E.A.2    Shin, J.W.3    Garcia, A.4    Capetillo, M.5    Kim, D.J.6    Lieman, J.H.7
  • 207
    • 8544278940 scopus 로고    scopus 로고
    • SHP-2-dependent mitogen-activated protein kinase activation regulates EGFRvIII but not wild-type epidermal growth factor receptor phosphorylation and glioblastoma cell survival
    • Zhan, Y.; O'Rourke, D.M. SHP-2-dependent mitogen-activated protein kinase activation regulates EGFRvIII but not wild-type epidermal growth factor receptor phosphorylation and glioblastoma cell survival. Cancer Res., 2004, 64, 8292-8298.
    • (2004) Cancer Res , vol.64 , pp. 8292-8298
    • Zhan, Y.1    O'Rourke, D.M.2
  • 208
    • 80053938400 scopus 로고    scopus 로고
    • Src homology domain-containing phosphatase 2 suppresses cellular senescence in glioblastoma
    • Sturla, L.M.; Zinn, P.O.; Ng, K.; Nitta, M.; Kozono, D.; Chen, C.C.; Kasper, E.M. Src homology domain-containing phosphatase 2 suppresses cellular senescence in glioblastoma. Br. J. Cancer, 2011, 105, 1235-1243.
    • (2011) Br. J. Cancer , vol.105 , pp. 1235-1243
    • Sturla, L.M.1    Zinn, P.O.2    Ng, K.3    Nitta, M.4    Kozono, D.5    Chen, C.C.6    Kasper, E.M.7
  • 210
    • 84892879708 scopus 로고    scopus 로고
    • Upregulation of Src homology phosphotyrosyl phosphatase 2 (Shp2) expression in oral cancer and knockdown of Shp2 expression inhibit tumor cell viability and invasion in vitro
    • Xie, H.; Huang, S.; Li, W.; Zhao, H.; Zhang, T.; Zhang, D. Upregulation of Src homology phosphotyrosyl phosphatase 2 (Shp2) expression in oral cancer and knockdown of Shp2 expression inhibit tumor cell viability and invasion in vitro. Oral Surg. Oral Med. Oral Pathol. Oral Radiol., 2014, 117, 234-242.
    • (2014) Oral Surg. Oral Med. Oral Pathol. Oral Radiol , vol.117 , pp. 234-242
    • Xie, H.1    Huang, S.2    Li, W.3    Zhao, H.4    Zhang, T.5    Zhang, D.6
  • 212
    • 0035884996 scopus 로고    scopus 로고
    • Sodium stibogluconate is a potent inhibitor of protein tyrosine phosphatases and augments cytokine responses in hemopoietic cell lines
    • Pathak, M.K.; Yi, T. Sodium stibogluconate is a potent inhibitor of protein tyrosine phosphatases and augments cytokine responses in hemopoietic cell lines. J. Immunol., 2001, 167, 3391-3397.
    • (2001) J. Immunol , vol.167 , pp. 3391-3397
    • Pathak, M.K.1    Yi, T.2
  • 216
    • 84884996061 scopus 로고    scopus 로고
    • Identification of cryptotanshinone as an inhibitor of oncogenic protein tyrosine phosphatase SHP2 (PTPN11)
    • Liu, W.; Yu, B.; Xu, G.; Xu, W.R.; Loh, M.L.; Tang, L.D.; Qu, C.K. Identification of cryptotanshinone as an inhibitor of oncogenic protein tyrosine phosphatase SHP2 (PTPN11). J. Med. Chem., 2013, 56, 7212-7221.
    • (2013) J. Med. Chem , vol.56 , pp. 7212-7221
    • Liu, W.1    Yu, B.2    Xu, G.3    Xu, W.R.4    Loh, M.L.5    Tang, L.D.6    Qu, C.K.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.