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Volumn 11, Issue 1, 2011, Pages 89-98

SHP-1 in cell-cycle regulation

Author keywords

Cancer; CDK2; Cyclin d; p27; Protein tyrosine phosphatase; PTPN6; SH2 domain

Indexed keywords

CYCLIN D1; CYCLIN DEPENDENT KINASE 2; PROTEIN P27; PROTEIN TYROSINE KINASE; PROTEIN TYROSINE PHOSPHATASE; PROTEIN TYROSINE PHOSPHATASE SHP 1;

EID: 79953018682     PISSN: 18715206     EISSN: None     Source Type: Journal    
DOI: 10.2174/187152011794941154     Document Type: Review
Times cited : (63)

References (104)
  • 1
    • 21644456228 scopus 로고    scopus 로고
    • Targeting the cell division cycle in cancer: CDK and cell cycle checkpoint kinase inhibitors
    • Collins, I.; Garrett, M.D. Targeting the cell division cycle in cancer: CDK and cell cycle checkpoint kinase inhibitors. Curr. Opin. Pharmacol., 2005, 5, 366-373.
    • (2005) Curr. Opin. Pharmacol. , vol.5 , pp. 366-373
    • Collins, I.1    Garrett, M.D.2
  • 2
    • 2342625225 scopus 로고    scopus 로고
    • Cyclin C makes an entry into the cell cycle
    • J. Cyclin C makes an entry into the cell cycle. Dev. Cell., 2004, 6, 607-608.
    • (2004) Dev. Cell , vol.6 , pp. 607-608
  • 3
    • 54549101258 scopus 로고    scopus 로고
    • Cyclin-dependent kinases and cell-cycle transitions: Does one fit all
    • Hochegger, H.; Takeda, S.; Hunt, T. Cyclin-dependent kinases and cell-cycle transitions: does one fit all? Nat. Rev. Mol. Cell Biol., 2008, 9, 910-916.
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 910-916
    • Hochegger, H.1    Takeda, S.2    Hunt, T.3
  • 4
    • 60749109846 scopus 로고    scopus 로고
    • Cell cycle, CDKs and cancer: A changing paradigm
    • Malumbres, M.; Barbacid, M. Cell cycle, CDKs and cancer: a changing paradigm. Nat. Rev. Cancer., 2009, 9, 153-166.
    • (2009) Nat. Rev. Cancer. , vol.9 , pp. 153-166
    • Malumbres, M.1    Barbacid, M.2
  • 5
    • 0033564697 scopus 로고    scopus 로고
    • CDK inhibitors: Positive and negative regulators of G1-phase progression
    • Sherr, C.J.; Roberts, J.M. CDK inhibitors: positive and negative regulators of G1-phase progression. Genes Dev., 1999, 13, 1501-1512.
    • (1999) Genes Dev. , vol.13 , pp. 1501-1512
    • Sherr, C.J.1    Roberts, J.M.2
  • 6
    • 0034660892 scopus 로고    scopus 로고
    • The Pezcoller lecture: Cancer cell cycles revisited
    • Sherr, C.J. The Pezcoller lecture: cancer cell cycles revisited. Cancer Res., 2000, 60, 3689-3695.
    • (2000) Cancer Res. , vol.60 , pp. 3689-3695
    • Sherr, C.J.1
  • 7
    • 38849187293 scopus 로고    scopus 로고
    • CDK inhibitors: Cell cycle regulators and beyond
    • Besson, A.; Dowdy, S.F.; Roberts, J.M. CDK inhibitors: cell cycle regulators and beyond. Dev. Cell., 2008, 14, 159-169.
    • (2008) Dev. Cell. , vol.14 , pp. 159-169
    • Besson, A.1    Dowdy, S.F.2    Roberts, J.M.3
  • 8
    • 0033559264 scopus 로고    scopus 로고
    • The p21Cip1 and p27Kip1 CDK 'inhibitors' are essential activators of cyclin D-dependent kinases in murine fibroblasts
    • Cheng, M.; Olivier, P.; Diehl, J.A.; Fero, M.; Roussel, M.F.; Roberts, J.M.; Sherr, C.J. The p21Cip1 and p27Kip1 CDK 'inhibitors' are essential activators of cyclin D-dependent kinases in murine fibroblasts. EMBO J., 1999, 18, 1571-1583.
    • (1999) EMBO J. , vol.18 , pp. 1571-1583
    • Cheng, M.1    Olivier, P.2    Diehl, J.A.3    Fero, M.4    Roussel, M.F.5    Roberts, J.M.6    Sherr, C.J.7
  • 10
    • 0031016121 scopus 로고    scopus 로고
    • RB kinases and RB-binding proteins: New points of view
    • Taya, Y. RB kinases and RB-binding proteins: new points of view. Trends Biochem. Sci., 1997, 22, 14-17.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 14-17
    • Taya, Y.1
  • 11
    • 18344372831 scopus 로고    scopus 로고
    • Cyclins and cdks in development and cancer: A perspective
    • Deshpande, A.; Sicinski, P.; Hinds, P.W. Cyclins and cdks in development and cancer: a perspective. Oncogene, 2005, 24, 2909-2915.
    • (2005) Oncogene , vol.24 , pp. 2909-2915
    • Deshpande, A.1    Sicinski, P.2    Hinds, P.W.3
  • 12
    • 41149150219 scopus 로고    scopus 로고
    • The Cdk inhibitor p27 in human cancer: Prognostic potential and relevance to anticancer therapy
    • Chu, I.M.; Hengst, L.; Slingerland, J.M. The Cdk inhibitor p27 in human cancer: prognostic potential and relevance to anticancer therapy. Nat. Rev. Cancer, 2008, 8, 253-267.
    • (2008) Nat. Rev. Cancer , vol.8 , pp. 253-267
    • Chu, I.M.1    Hengst, L.2    Slingerland, J.M.3
  • 13
    • 33645802169 scopus 로고    scopus 로고
    • Cyclin-dependent kinase pathways as targets for cancer treatment
    • G.I. Cyclin-dependent kinase pathways as targets for cancer treatment. J. Clin. Oncol., 2006, 24, 1770-1783.
    • (2006) J. Clin. Oncol. , vol.24 , pp. 1770-1783
  • 15
    • 0029670477 scopus 로고    scopus 로고
    • Translational control of p27Kip1 accumulation during the cell cycle
    • Hengst, L.; Reed, S.I. Translational control of p27Kip1 accumulation during the cell cycle. Science, 1996, 271, 1861-1864.
    • (1996) Science , vol.271 , pp. 1861-1864
    • Hengst, L.1    Reed, S.I.2
  • 16
    • 0034092911 scopus 로고    scopus 로고
    • Regulation of the cdk inhibitor p27 and its deregulation in cancer
    • Slingerland, J.; Pagano, M. Regulation of the cdk inhibitor p27 and its deregulation in cancer. J. Cell. Physiol., 2000, 183, 10-17.
    • (2000) J. Cell. Physiol. , vol.183 , pp. 10-17
    • Slingerland, J.1    Pagano, M.2
  • 17
    • 0037325853 scopus 로고    scopus 로고
    • Deregulated degradation of the cdk inhibitor p27 and malignant transformation
    • Bloom, J.; Pagano, M. Deregulated degradation of the cdk inhibitor p27 and malignant transformation. Semin. Cancer Biol., 2003, 13, 41-47.
    • (2003) Semin. Cancer Biol. , vol.13 , pp. 41-47
    • Bloom, J.1    Pagano, M.2
  • 18
    • 1042280976 scopus 로고    scopus 로고
    • Deregulation of p27 by oncogenic signaling and its prognostic significance in breast cancer
    • Alkarain, A.; Slingerland, J. Deregulation of p27 by oncogenic signaling and its prognostic significance in breast cancer. Breast Cancer Res., 2004, 6, 13-21.
    • (2004) Breast Cancer Res. , vol.6 , pp. 13-21
    • Alkarain, A.1    Slingerland, J.2
  • 19
    • 0033527656 scopus 로고    scopus 로고
    • Sp1 and NF-Y synergistically mediate the effect of vitamin D3 in the p27Kip1 gene promoter that lacks vitamin D response elements
    • Inoue, T.; Kamiyama, J.; Sakai, T. Sp1 and NF-Y synergistically mediate the effect of vitamin D3 in the p27Kip1 gene promoter that lacks vitamin D response elements. J. Biol. Chem., 1999, 274, 32309-32317.
    • (1999) J. Biol. Chem. , vol.274 , pp. 32309-32317
    • Inoue, T.1    Kamiyama, J.2    Sakai, T.3
  • 21
    • 0034643331 scopus 로고    scopus 로고
    • AFX-like Forkhead transcription factors mediate cell-cycle regulation by Ras and PKB through p27kip1
    • Medema, R.H.; Kops, G.J.; Bos, J.L.; Burgering, B.M. AFX-like Forkhead transcription factors mediate cell-cycle regulation by Ras and PKB through p27kip1. Nature, 2000, 404, 782-787.
    • (2000) Nature , vol.404 , pp. 782-787
    • Medema, R.H.1    Kops, G.J.2    Bos, J.L.3    Burgering, B.M.4
  • 22
    • 0033152165 scopus 로고    scopus 로고
    • Regulation of Akt/PKB activity, cellular growth, and apoptosis in prostate carcinoma cells by MMAC/PTEN
    • Davies, M.A.; Koul, D.; Dhesi, H.; Berman, R.; McDonnell, T.J.; McConkey, D.; Yung, W.K.; Steck, P.A. Regulation of Akt/PKB activity, cellular growth, and apoptosis in prostate carcinoma cells by MMAC/PTEN. Cancer Res., 1999, 59, 2551-2556.
    • (1999) Cancer Res. , vol.59 , pp. 2551-2556
    • Davies, M.A.1    Koul, D.2    Dhesi, H.3    Berman, R.4    McDonnell, T.J.5    McConkey, D.6    Yung, W.K.7    Steck, P.A.8
  • 24
    • 61849153316 scopus 로고    scopus 로고
    • SHP-1 and SHP-2 in T cells: Two phosphatases functioning at many levels
    • Lorenz, U. SHP-1 and SHP-2 in T cells: two phosphatases functioning at many levels. Immunol. Rev., 2009, 228, 342-359.
    • (2009) Immunol. Rev. , vol.228 , pp. 342-359
    • Lorenz, U.1
  • 25
    • 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
  • 26
    • 0026547356 scopus 로고
    • Protein tyrosine phosphatase containing SH2 domains: Characterization, preferential expression in hematopoietic cells, and localization to human chromosome 12p12-p13
    • Yi, T.L.; Cleveland, J.L.; Ihle, J.N. Protein tyrosine phosphatase containing SH2 domains: characterization, preferential expression in hematopoietic cells, and localization to human chromosome 12p12-p13. Mol. Cell. Biol., 1992, 12, 836-846.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 836-846
    • Yi, T.L.1    Cleveland, J.L.2    Ihle, J.N.3
  • 28
    • 0029059985 scopus 로고
    • Human protein tyrosine phosphatase 1C (PTPN6) gene structure: Alternate promoter usage and exon skipping generate multiple transcripts
    • Banville, D.; Stocco, R.; Shen, S.H. Human protein tyrosine phosphatase 1C (PTPN6) gene structure: alternate promoter usage and exon skipping generate multiple transcripts. Genomics, 1995, 27, 165-173.
    • (1995) Genomics , vol.27 , pp. 165-173
    • Banville, D.1    Stocco, R.2    Shen, S.H.3
  • 29
    • 0033215475 scopus 로고    scopus 로고
    • Human 70-kDa SHP-1L differs from 68-kDa SHP-1 in its C-terminal structure and catalytic activity
    • Jin, Y.J.; Yu, C.L.; Burakoff, S.J. Human 70-kDa SHP-1L differs from 68-kDa SHP-1 in its C-terminal structure and catalytic activity. J. Biol. Chem., 1999, 274, 28301-28307.
    • (1999) J. Biol. Chem. , vol.274 , pp. 28301-28307
    • Jin, Y.J.1    Yu, C.L.2    Burakoff, S.J.3
  • 30
    • 23944518951 scopus 로고    scopus 로고
    • A SHPing tale: Perspectives on the regulation of SHP-1 and SHP-2 tyrosine phosphatases by the Cterminal tail
    • Poole, A.W.; Jones, M.L. A SHPing tale: perspectives on the regulation of SHP-1 and SHP-2 tyrosine phosphatases by the Cterminal tail. Cell. Signal., 2005, 17, 1323-1332.
    • (2005) Cell. Signal. , vol.17 , pp. 1323-1332
    • Poole, A.W.1    Jones, M.L.2
  • 31
  • 32
  • 33
    • 0035968310 scopus 로고    scopus 로고
    • A functional nuclear localization sequence in the C-terminal domain of SHP-1
    • Craggs, G.; Kellie, S. A functional nuclear localization sequence in the C-terminal domain of SHP-1. J. Biol. Chem., 2001, 276, 23719-23725.
    • (2001) J. Biol. Chem. , vol.276 , pp. 23719-23725
    • Craggs, G.1    Kellie, S.2
  • 34
    • 34250836302 scopus 로고    scopus 로고
    • Identification of a novel lipid raft-targeting motif in Src homology 2-containing phosphatase 1
    • Sankarshanan, M.; Ma, Z.; Iype, T.; Lorenz, U. Identification of a novel lipid raft-targeting motif in Src homology 2-containing phosphatase 1. J. Immunol., 2007, 179, 483-490.
    • (2007) J. Immunol. , vol.179 , pp. 483-490
    • Sankarshanan, M.1    Ma, Z.2    Iype, T.3    Lorenz, U.4
  • 35
    • 34548461710 scopus 로고    scopus 로고
    • Rapid T cell receptormediated SHP-1 S591 phosphorylation regulates SHP-1 cellular localization and phosphatase activity
    • Liu, Y.; Kruhlak, M.J.; Hao, J.J.; Shaw, S. Rapid T cell receptormediated SHP-1 S591 phosphorylation regulates SHP-1 cellular localization and phosphatase activity. J. Leukoc. Biol., 2007, 82, 742-751.
    • (2007) J. Leukoc. Biol. , vol.82 , pp. 742-751
    • Liu, Y.1    Kruhlak, M.J.2    Hao, J.J.3    Shaw, S.4
  • 36
    • 14044257222 scopus 로고    scopus 로고
    • Localization of Src homology 2 domaincontaining phosphatase 1 (SHP-1) to lipid rafts in T lymphocytes: Functional implications and a role for the SHP-1 carboxyl terminus
    • Fawcett, V.C.; Lorenz, U. Localization of Src homology 2 domaincontaining phosphatase 1 (SHP-1) to lipid rafts in T lymphocytes: functional implications and a role for the SHP-1 carboxyl terminus. J. Immunol., 2005, 174, 2849-2859.
    • (2005) J. Immunol. , vol.174 , pp. 2849-2859
    • Fawcett, V.C.1    Lorenz, U.2
  • 37
    • 0035869308 scopus 로고    scopus 로고
    • Targeting Src homology 2 domain-containing tyrosine phosphatase (SHP-1) into lipid rafts inhibits CD3-induced T cell activation
    • Su, M.W.; Yu, C.L.; Burakoff, S.J.; Jin, Y.J. Targeting Src homology 2 domain-containing tyrosine phosphatase (SHP-1) into lipid rafts inhibits CD3-induced T cell activation. J. Immunol., 2001, 166, 3975-3982.
    • (2001) J. Immunol. , vol.166 , pp. 3975-3982
    • Su, M.W.1    Yu, C.L.2    Burakoff, S.J.3    Jin, Y.J.4
  • 38
    • 0027197067 scopus 로고
    • Mutations at the murine motheaten locus are within the hematopoietic cell protein-tyrosine phosphatase (Hcph) gene
    • Shultz, L.D.; Schweitzer, P.A.; Rajan, T.V.; Yi, T.; Ihle, J.N.; Matthews, R.J.; Thomas, M.L.; Beier, D.R. Mutations at the murine motheaten locus are within the hematopoietic cell protein-tyrosine phosphatase (Hcph) gene. Cell, 1993, 73, 1445-1454.
    • (1993) Cell , vol.73 , pp. 1445-1454
    • Shultz, L.D.1    Schweitzer, P.A.2    Rajan, T.V.3    Yi, T.4    Ihle, J.N.5    Matthews, R.J.6    Thomas, M.L.7    Beier, D.R.8
  • 39
    • 0033794917 scopus 로고    scopus 로고
    • Roles of the SHP-1 tyrosine phosphatase in the negative regulation of cell signalling
    • Zhang, J.; Somani, A.K.; Siminovitch, K.A. Roles of the SHP-1 tyrosine phosphatase in the negative regulation of cell signalling. Semin. Immunol., 2000, 12, 361-378.
    • (2000) Semin. Immunol. , vol.12 , pp. 361-378
    • Zhang, J.1    Somani, A.K.2    Siminovitch, K.A.3
  • 40
    • 0033809993 scopus 로고    scopus 로고
    • Lack of phosphotyrosine phosphatase SHP-1 expression in malignant T-cell lymphoma cells results from methylation of the SHP-1 promoter
    • Zhang, Q.; Raghunath, P.N.; Vonderheid, E.; Odum, N.; Wasik, M.A. Lack of phosphotyrosine phosphatase SHP-1 expression in malignant T-cell lymphoma cells results from methylation of the SHP-1 promoter. Am. J. Pathol., 2000, 157, 1137-1146.
    • (2000) Am. J. Pathol. , vol.157 , pp. 1137-1146
    • Zhang, Q.1    Raghunath, P.N.2    Vonderheid, E.3    Odum, N.4    Wasik, M.A.5
  • 41
    • 0030990384 scopus 로고    scopus 로고
    • Identification of a protein- tyrosine phosphatase (SHP1) different from that associated with acid phosphatase in rat prostate
    • Valencia, A.M.; Oliva, J.L.; Bodega, G.; Chiloeches, A.; Lopez- Ruiz, P.; Prieto, J.C.; Susini, C.; Colás, B. Identification of a protein- tyrosine phosphatase (SHP1) different from that associated with acid phosphatase in rat prostate. FEBS Lett., 1997, 406, 42-48.
    • (1997) FEBS Lett. , vol.406 , pp. 42-48
    • Valencia, A.M.1    Oliva, J.L.2    Bodega, G.3    Chiloeches, A.4    Lopez-Ruiz, P.5    Prieto, J.C.6    Susini, C.7    Colás, B.8
  • 44
    • 0343729328 scopus 로고    scopus 로고
    • Perinuclear localization of the proteintyrosine phosphatase SHP-1 and inhibition of epidermal growth factor-stimulated STAT1/3 activation in A431 cells
    • Tenev, T.; Böhmer, S.A.; Kaufmann, R.; Frese, S.; Bittorf, T.; Beckers, T.; Böhmer, F.D. Perinuclear localization of the proteintyrosine phosphatase SHP-1 and inhibition of epidermal growth factor-stimulated STAT1/3 activation in A431 cells. Eur. J. Cell Biol., 2000, 79, 261-271.
    • (2000) Eur. J. Cell Biol. , vol.79 , pp. 261-271
    • Tenev, T.1    Böhmer, S.A.2    Kaufmann, R.3    Frese, S.4    Bittorf, T.5    Beckers, T.6    Böhmer, F.D.7
  • 45
    • 0344154466 scopus 로고    scopus 로고
    • SHP-1 suppresses cancer cell growth by promoting degradation of JAK kinases
    • Wu, C.; Guan, Q.; Wang, Y.; Zhao, Z.J.; Zhou, G.W. SHP-1 suppresses cancer cell growth by promoting degradation of JAK kinases. J. Cell. Biochem., 2003, 90, 1026-1037.
    • (2003) J. Cell. Biochem. , vol.90 , pp. 1026-1037
    • Wu, C.1    Guan, Q.2    Wang, Y.3    Zhao, Z.J.4    Zhou, G.W.5
  • 46
    • 25444517722 scopus 로고    scopus 로고
    • Protein tyrosine phosphatase κ and SHP-1 are involved in the regulation of cell-cell contacts at adherens junctions in the exocrine pancreas
    • Schnekenburger, J.; Mayerle, J.; Kruger, B.; Buchwalow, I.; Weiss, F.U.; Albrecht, E.; Samoilova, V.E.; Domschke, W.; Lerch, M.M. Protein tyrosine phosphatase κ and SHP-1 are involved in the regulation of cell-cell contacts at adherens junctions in the exocrine pancreas. Gut, 2005, 54, 1445-1455.
    • (2005) Gut , vol.54 , pp. 1445-1455
    • Schnekenburger, J.1    Mayerle, J.2    Kruger, B.3    Buchwalow, I.4    Weiss, F.U.5    Albrecht, E.6    Samoilova, V.E.7    Domschke, W.8    Lerch, M.M.9
  • 47
    • 0038190977 scopus 로고    scopus 로고
    • Negative regulation of beta-catenin signaling by tyrosine phosphatase SHP-1 in intestinal epithelial cells
    • Duchesne, C.; Charland, S.; Asselin, C.; Nahmias, C.; Rivard, N. Negative regulation of beta-catenin signaling by tyrosine phosphatase SHP-1 in intestinal epithelial cells. J. Biol. Chem., 2003, 278, 14274-14283.
    • (2003) J. Biol. Chem. , vol.278 , pp. 14274-14283
    • Duchesne, C.1    Charland, S.2    Asselin, C.3    Nahmias, C.4    Rivard, N.5
  • 49
    • 0032816807 scopus 로고    scopus 로고
    • The tyrosine phosphatase SHP-1 is a negative regulator of osteoclastogenesis and osteoclast resorbing activity: Increased resorption and osteopenia in mev/mev mutant mice
    • Aoki, K.; Didomenico, E.; Sims, N.A.; Mukhopadhyay, K.; Neff, L.; Houghton, A.; Amling, M.; Levy, J.B.; Horne, W.C.; Baron, R. The tyrosine phosphatase SHP-1 is a negative regulator of osteoclastogenesis and osteoclast resorbing activity: increased resorption and osteopenia in mev/mev mutant mice. Bone, 1999, 25, 261-267.
    • (1999) Bone , vol.25 , pp. 261-267
    • Aoki, K.1    Didomenico, E.2    Sims, N.A.3    Mukhopadhyay, K.4    Neff, L.5    Houghton, A.6    Amling, M.7    Levy, J.B.8    Horne, W.C.9    Baron, R.10
  • 50
    • 0042316826 scopus 로고    scopus 로고
    • The protein- tyrosine phosphatase SHP-1 associates with the phosphorylated immunoreceptor tyrosine-based activation motif of Fc gamma RIIa to modulate signaling events in myeloid cells
    • Ganesan, L.P.; Fang, H.; Marsh, C.B.; Tridandapani, S. The protein- tyrosine phosphatase SHP-1 associates with the phosphorylated immunoreceptor tyrosine-based activation motif of Fc gamma RIIa to modulate signaling events in myeloid cells. J. Biol. Chem., 2003, 278, 35710-35717.
    • (2003) J. Biol. Chem. , vol.278 , pp. 35710-35717
    • Ganesan, L.P.1    Fang, H.2    Marsh, C.B.3    Tridandapani, S.4
  • 51
    • 0842328827 scopus 로고    scopus 로고
    • A novel SHP-1/Grb2-dependent mechanism of negative regulation of cytokine- receptor signaling: Contribution of SHP-1 C-terminal tyrosines in cytokine signaling
    • Minoo, P.; Zadeh, M.M.; Rottapel, R.; Lebrun, J.J.; Ali, S. A novel SHP-1/Grb2-dependent mechanism of negative regulation of cytokine- receptor signaling: contribution of SHP-1 C-terminal tyrosines in cytokine signaling. Blood, 2004, 103, 1398-1407.
    • (2004) Blood , vol.103 , pp. 1398-1407
    • Minoo, P.1    Zadeh, M.M.2    Rottapel, R.3    Lebrun, J.J.4    Ali, S.5
  • 52
    • 0033010984 scopus 로고    scopus 로고
    • Separation and characterization of the activated pool of colonystimulating factor 1 receptor forming distinct multimeric complexes with signalling molecules in macrophages
    • Kanagasundaram, V.; Jaworowski, A.; Byrne, R.; Hamilton, J.A. Separation and characterization of the activated pool of colonystimulating factor 1 receptor forming distinct multimeric complexes with signalling molecules in macrophages. Mol. Cell. Biol., 1999, 19, 4079-4092.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 4079-4092
    • Kanagasundaram, V.1    Jaworowski, A.2    Byrne, R.3    Hamilton, J.A.4
  • 53
    • 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
  • 54
    • 0031041185 scopus 로고    scopus 로고
    • Both SH2 domains are involved in interaction of SHP-1 with the epidermal growth factor receptor but cannot confer receptor-directed activity to SHP-1/SHP-2 chimera
    • Tenev, T.; Keilhack, H.; Tomic, S.; Stoyanov, B.; Stein-Gerlach, M.; Lammers, R.; Krivtsov, A.V.; Ullrich, A.; Böhmer, F.D. Both SH2 domains are involved in interaction of SHP-1 with the epidermal growth factor receptor but cannot confer receptor-directed activity to SHP-1/SHP-2 chimera. J. Biol. Chem., 1997, 272, 5966-5973.
    • (1997) J. Biol. Chem. , vol.272 , pp. 5966-5973
    • Tenev, T.1    Keilhack, H.2    Tomic, S.3    Stoyanov, B.4    Stein-Gerlach, M.5    Lammers, R.6    Krivtsov, A.V.7    Ullrich, A.8    Böhmer, F.D.9
  • 55
    • 0032544418 scopus 로고    scopus 로고
    • Phosphotyrosine 1173 mediates binding of the protein-tyrosine phosphatase SHP-1 to the epidermal growth factor receptor and attenuation of receptor signaling
    • Keilhack, H.; Tenev, T.; Nyakatura, E.; Godovac-Zimmermann, J.; Nielsen, L.; Seedorf, K.; Böhmer, F.D. Phosphotyrosine 1173 mediates binding of the protein-tyrosine phosphatase SHP-1 to the epidermal growth factor receptor and attenuation of receptor signaling. J. Biol. Chem., 1998, 273, 24839-24846.
    • (1998) J. Biol. Chem. , vol.273 , pp. 24839-24846
    • Keilhack, H.1    Tenev, T.2    Nyakatura, E.3    Godovac-Zimmermann, J.4    Nielsen, L.5    Seedorf, K.6    Böhmer, F.D.7
  • 57
    • 0032488828 scopus 로고    scopus 로고
    • SHP-1 associates with both platelet-derived growth factor receptor and the p85 subunit of phosphatidylinositol 3-kinase
    • Yu, Z.; Su, L.; Hoglinger, O.; Jaramillo, M.L.; Banville, D.; Shen, S.H. SHP-1 associates with both platelet-derived growth factor receptor and the p85 subunit of phosphatidylinositol 3-kinase. J. Biol. Chem., 1998, 273, 3687-3694.
    • (1998) J. Biol. Chem. , vol.273 , pp. 3687-3694
    • Yu, Z.1    Su, L.2    Hoglinger, O.3    Jaramillo, M.L.4    Banville, D.5    Shen, S.H.6
  • 58
    • 0033600848 scopus 로고    scopus 로고
    • SHP-1 regulates Lck-induced phosphatidylinositol 3-kinase phosphorylation and activity
    • Cuevas, B.; Lu, Y.; Watt, S.; Kumar, R.; Zhang, J.; Siminovitch, K.A.; Mills, G.B. SHP-1 regulates Lck-induced phosphatidylinositol 3-kinase phosphorylation and activity. J. Biol. Chem., 1999, 274, 27583-27589.
    • (1999) J. Biol. Chem. , vol.274 , pp. 27583-27589
    • Cuevas, B.1    Lu, Y.2    Watt, S.3    Kumar, R.4    Zhang, J.5    Siminovitch, K.A.6    Mills, G.B.7
  • 59
    • 0036164502 scopus 로고    scopus 로고
    • Tumor necrosis factor-alpha inhibits growth factor-mediated cell proliferation through SHP-1 activation in endothelial cells
    • Nakagami, H.; Cui, T.X.; Iwai, M.; Shiuchi, T.; Takeda-Matsubara, Y.; Wu, L.; Horiuchi, M. Tumor necrosis factor-alpha inhibits growth factor-mediated cell proliferation through SHP-1 activation in endothelial cells. Arterioscler. Thromb. Vasc. Biol., 2002, 22, 238-242.
    • (2002) Arterioscler. Thromb. Vasc. Biol. , vol.22 , pp. 238-242
    • Nakagami, H.1    Cui, T.X.2    Iwai, M.3    Shiuchi, T.4    Takeda-Matsubara, Y.5    Wu, L.6    Horiuchi, M.7
  • 61
    • 77957822414 scopus 로고    scopus 로고
    • SHP-1 inhibits β-catenin function by inducing its degradation and interfering with its association with TATA-binding protein
    • Simoneau, M.; Coulombe, G.; Vandal, G.; Vezina, A.; Rivard, N. SHP-1 inhibits β-catenin function by inducing its degradation and interfering with its association with TATA-binding protein. Cell. Signal., 2010 23, 269-279.
    • (2010) Cell. Signal. , vol.23 , pp. 269-279
    • Simoneau, M.1    Coulombe, G.2    Vandal, G.3    Vezina, A.4    Rivard, N.5
  • 62
    • 32144453842 scopus 로고    scopus 로고
    • JAK/STAT signal transduction: Regulators and implication in hematological malignancies
    • Valentino, L.; Pierre, J. JAK/STAT signal transduction: regulators and implication in hematological malignancies. Biochem. Pharmacol., 2006, 71, 713-721.
    • (2006) Biochem. Pharmacol. , vol.71 , pp. 713-721
    • Valentino, L.1    Pierre, J.2
  • 64
    • 0035487006 scopus 로고    scopus 로고
    • Neuronal nitric oxide synthase: A substrate for SHP-1 involved in sst2 somatostatin receptor growth inhibitory signaling
    • Lopez, F.; Ferjoux, G.; Cordelier, P.; Saint-Laurent, N.; Esteve, J.P.; Vaysse, N.; Buscail, L.; Susini, C. Neuronal nitric oxide synthase: a substrate for SHP-1 involved in sst2 somatostatin receptor growth inhibitory signaling. FASEB J., 2001, 15, 2300-2302.
    • (2001) FASEB J. , vol.15 , pp. 2300-2302
    • Lopez, F.1    Ferjoux, G.2    Cordelier, P.3    Saint-Laurent, N.4    Esteve, J.P.5    Vaysse, N.6    Buscail, L.7    Susini, C.8
  • 65
    • 32944477371 scopus 로고    scopus 로고
    • Octreotide, a somatostatin analogue, mediates its antiproliferative action in pituitary tumor cells by altering phosphatidylinositol 3-kinase signaling and inducing Zac1 expression
    • Theodoropoulou, M.; Zhang, J.; Laupheimer, S.; Paez-Pereda, M.; Erneux, C.; Florio, T.; Pagotto, U.; Stalla, G.K. Octreotide, a somatostatin analogue, mediates its antiproliferative action in pituitary tumor cells by altering phosphatidylinositol 3-kinase signaling and inducing Zac1 expression. Cancer Res., 2006, 66, 1576-1582.
    • (2006) Cancer Res. , vol.66 , pp. 1576-1582
    • Theodoropoulou, M.1    Zhang, J.2    Laupheimer, S.3    Paez-Pereda, M.4    Erneux, C.5    Florio, T.6    Pagotto, U.7    Stalla, G.K.8
  • 66
    • 0029968569 scopus 로고    scopus 로고
    • Positive effect of overexpressed protein-tyrosine phosphatase PTP1C on mitogen-activated signaling in 293 cells
    • Su, L.; Zhao, Z.; Bouchard, P.; Banville, D.; Fischer, E.H.; Krebs, E.G.; Shen, S.H. Positive effect of overexpressed protein-tyrosine phosphatase PTP1C on mitogen-activated signaling in 293 cells. J. Biol. Chem., 1996, 271, 10385-10390.
    • (1996) J. Biol. Chem. , vol.271 , pp. 10385-10390
    • Su, L.1    Zhao, Z.2    Bouchard, P.3    Banville, D.4    Fischer, E.H.5    Krebs, E.G.6    Shen, S.H.7
  • 67
    • 78650592361 scopus 로고    scopus 로고
    • Deficiency of SHP1 leads to sustained and increased ERK activation in mast cells, thereby inhibiting IL-3-dependent proliferation and cell death
    • Nakata, K.; Suzuki, Y.; Inoue, T.; Ra, C.; Yakura, H.; Mizuno, K. Deficiency of SHP1 leads to sustained and increased ERK activation in mast cells, thereby inhibiting IL-3-dependent proliferation and cell death. Mol. Immunol., 2010, 48, 472-480.
    • (2010) Mol. Immunol. , vol.48 , pp. 472-480
    • Nakata, K.1    Suzuki, Y.2    Inoue, T.3    Ra, C.4    Yakura, H.5    Mizuno, K.6
  • 68
    • 33645646321 scopus 로고    scopus 로고
    • Shp-1 mediates the antiproliferative activity of tissue inhibitor of metalloproteinase-2 in human microvascular endothelial cells
    • Seo, D.W.; Li, H.; Qu, C.K.; Oh, J.; Kim, Y.S.; Diaz, T.; Wei, B.; Han, J.W.; Stetler-Stevenson, W.G. Shp-1 mediates the antiproliferative activity of tissue inhibitor of metalloproteinase-2 in human microvascular endothelial cells. J. Biol. Chem., 2006, 281, 3711-3721.
    • (2006) J. Biol. Chem. , vol.281 , pp. 3711-3721
    • Seo, D.W.1    Li, H.2    Qu, C.K.3    Oh, J.4    Kim, Y.S.5    Diaz, T.6    Wei, B.7    Han, J.W.8    Stetler-Stevenson, W.G.9
  • 70
    • 75149128005 scopus 로고    scopus 로고
    • Knockdown of protein tyrosine phosphatase SHP-1 inhibits G1/S progression in prostate cancer cells through the regulation of components of the cell-cycle machinery
    • Rodriguez-Ubreva, F.J.; Cariaga-Martinez, A.E.; Cortes, M.A.; Romero-De Pablos, M.; Ropero, S.; Lopez-Ruiz, P.; Colas, B. Knockdown of protein tyrosine phosphatase SHP-1 inhibits G1/S progression in prostate cancer cells through the regulation of components of the cell-cycle machinery. Oncogene, 2010, 29, 345-355.
    • (2010) Oncogene , vol.29 , pp. 345-355
    • Rodriguez-Ubreva, F.J.1    Cariaga-Martinez, A.E.2    Cortes, M.A.3    Romero-De pablos, M.4    Ropero, S.5    Lopez-Ruiz, P.6    Colas, B.7
  • 71
    • 0027471557 scopus 로고
    • Cdc25M2 activation of cyclin-dependent kinases by dephosphorylation of threonine-14 and tyrosine-15
    • Sebastian, B.; Kakizuka, A.; Hunter, T. Cdc25M2 activation of cyclin-dependent kinases by dephosphorylation of threonine-14 and tyrosine-15. Proc. Natl. Acad. Sci. U. S. A., 1993, 90, 3521-3524.
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 3521-3524
    • Sebastian, B.1    Kakizuka, A.2    Hunter, T.3
  • 72
    • 0030878257 scopus 로고    scopus 로고
    • Interaction of growth hormone-activated STATs with SH2-containing phosphotyrosine phosphatase SHP-1 and nuclear JAK2 tyrosine kinase
    • Ram, P.A.; Waxman, D.J. Interaction of growth hormone-activated STATs with SH2-containing phosphotyrosine phosphatase SHP-1 and nuclear JAK2 tyrosine kinase. J. Biol. Chem., 1997, 272, 17694-17702.
    • (1997) J. Biol. Chem. , vol.272 , pp. 17694-17702
    • Ram, P.A.1    Waxman, D.J.2
  • 73
    • 40849136040 scopus 로고    scopus 로고
    • Protein tyrosine phosphatase inhibition induces anti-tumor activity: Evidence of Cdk2/p27kip1 and Cdk2/SHP-1 complex formation in human ovarian cancer cells
    • Caron, D.; Savard, P.E.; Doillon, C.J.; Olivier, M.; Shink, E.; Lussier, J.G.; Faure, R.L. Protein tyrosine phosphatase inhibition induces anti-tumor activity: evidence of Cdk2/p27kip1 and Cdk2/SHP-1 complex formation in human ovarian cancer cells. Cancer Lett., 2008, 262, 265-275.
    • (2008) Cancer Lett. , vol.262 , pp. 265-275
    • Caron, D.1    Savard, P.E.2    Doillon, C.J.3    Olivier, M.4    Shink, E.5    Lussier, J.G.6    Faure, R.L.7
  • 74
    • 54449092916 scopus 로고    scopus 로고
    • Activation of Cdk2 stimulates proteasome- dependent truncation of tyrosine phosphatase SHP-1 in human proliferating intestinal epithelial cells
    • Simoneau, M.; Boulanger, J.; Coulombe, G.; Renaud, M.A.; Duchesne, C.; Rivard, N. Activation of Cdk2 stimulates proteasome- dependent truncation of tyrosine phosphatase SHP-1 in human proliferating intestinal epithelial cells. J. Biol. Chem., 2008, 283, 25544-25556.
    • (2008) J. Biol. Chem. , vol.283 , pp. 25544-25556
    • Simoneau, M.1    Boulanger, J.2    Coulombe, G.3    Renaud, M.A.4    Duchesne, C.5    Rivard, N.6
  • 76
    • 0037047268 scopus 로고    scopus 로고
    • Akt-dependent phosphorylation of p27Kip1 promotes binding to 14-3-3 and cytoplasmic localization
    • Fujita, N.; Sato, S.; Katayama, K.; Tsuruo, T. Akt-dependent phosphorylation of p27Kip1 promotes binding to 14-3-3 and cytoplasmic localization. J. Biol. Chem., 2002, 277, 28706-28713.
    • (2002) J. Biol. Chem. , vol.277 , pp. 28706-28713
    • Fujita, N.1    Sato, S.2    Katayama, K.3    Tsuruo, T.4
  • 77
    • 0035834374 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of the catalytic subunit p110 of phosphatidylinositol-3 kinase induced by HMG-CoA reductase inhibitor inhibits its kinase activity in L6 myoblasts
    • Nakagawa, H.; Mutoh, T.; Kumano, T.; Kuriyama, M. Tyrosine phosphorylation of the catalytic subunit p110 of phosphatidylinositol-3 kinase induced by HMG-CoA reductase inhibitor inhibits its kinase activity in L6 myoblasts. FEBS Lett., 2001, 508, 53-56.
    • (2001) FEBS Lett. , vol.508 , pp. 53-56
    • Nakagawa, H.1    Mutoh, T.2    Kumano, T.3    Kuriyama, M.4
  • 78
    • 35348893870 scopus 로고    scopus 로고
    • Targeting the cytoplasmic and nuclear functions of signal transducers and activators of transcription 3 for cancer therapy
    • Germain, D.; Frank, D.A. Targeting the cytoplasmic and nuclear functions of signal transducers and activators of transcription 3 for cancer therapy. Clin. Cancer Res., 2007, 13, 5665-5669.
    • (2007) Clin. Cancer Res. , vol.13 , pp. 5665-5669
    • Germain, D.1    Frank, D.A.2
  • 79
    • 33750632572 scopus 로고    scopus 로고
    • Loss of SHP1 enhances JAK3/STAT3 signaling and decreases proteosome degradation of JAK3 and NPM-ALK in ALK+ anaplastic large-cell lymphoma
    • Han, Y.; Amin, H.M.; Franko, B.; Frantz, C.; Shi, X.; Lai, R. Loss of SHP1 enhances JAK3/STAT3 signaling and decreases proteosome degradation of JAK3 and NPM-ALK in ALK+ anaplastic large-cell lymphoma. Blood, 2006, 108, 2796-2803.
    • (2006) Blood , vol.108 , pp. 2796-2803
    • Han, Y.1    Amin, H.M.2    Franko, B.3    Frantz, C.4    Shi, X.5    Lai, R.6
  • 80
    • 62149113324 scopus 로고    scopus 로고
    • Butein suppresses constitutive and inducible signal transducer and activator of transcription (STAT) 3 activation and STAT3-regulated gene products through the induction of a protein tyrosine phosphatase SHP-1
    • Pandey, M.K.; Sung, B.; Ahn, K.S.; Aggarwal, B.B. Butein suppresses constitutive and inducible signal transducer and activator of transcription (STAT) 3 activation and STAT3-regulated gene products through the induction of a protein tyrosine phosphatase SHP-1. Mol. Pharmacol., 2009, 75, 525-533.
    • (2009) Mol. Pharmacol. , vol.75 , pp. 525-533
    • Pandey, M.K.1    Sung, B.2    Ahn, K.S.3    Aggarwal, B.B.4
  • 81
    • 49249128130 scopus 로고    scopus 로고
    • Guggulsterone, a farnesoid X receptor antagonist, inhibits constitutive and inducible STAT3 activation through induction of a protein tyrosine phosphatase SHP-1
    • Ahn, K.S.; Sethi, G.; Sung, B.; Goel, A.; Ralhan, R.; Aggarwal, B.B. Guggulsterone, a farnesoid X receptor antagonist, inhibits constitutive and inducible STAT3 activation through induction of a protein tyrosine phosphatase SHP-1. Cancer Res., 2008, 68, 4406-4415.
    • (2008) Cancer Res. , vol.68 , pp. 4406-4415
    • Ahn, K.S.1    Sethi, G.2    Sung, B.3    Goel, A.4    Ralhan, R.5    Aggarwal, B.B.6
  • 83
    • 77958468408 scopus 로고    scopus 로고
    • γ-tocotrienol but notγ-tocopherol blocks STAT3 cell signaling pathway through induction of protein-tyrosine phosphatase SHP-1 and sensitizes tumor cells to chemotherapeutic agents
    • Kannappan, R.; Yadav, V.R.; Aggarwal, B.B. γ-tocotrienol but notγ-tocopherol blocks STAT3 cell signaling pathway through induction of protein-tyrosine phosphatase SHP-1 and sensitizes tumor cells to chemotherapeutic agents. J. Biol. Chem., 2010, 285, 33520-33528.
    • (2010) J. Biol. Chem. , vol.285 , pp. 33520-33528
    • Kannappan, R.1    Yadav, V.R.2    Aggarwal, B.B.3
  • 84
    • 34548780771 scopus 로고    scopus 로고
    • Negative autoregulation of Src homology region 2-domain-containing phosphatase-1 in rat basophilic leukemia-2H3 cells
    • Ozawa, T.; Nakata, K.; Mizuno, K.; Yakura, H. Negative autoregulation of Src homology region 2-domain-containing phosphatase-1 in rat basophilic leukemia-2H3 cells. Int. Immunol., 2007, 19, 1049-1061.
    • (2007) Int. Immunol. , vol.19 , pp. 1049-1061
    • Ozawa, T.1    Nakata, K.2    Mizuno, K.3    Yakura, H.4
  • 85
    • 24944513021 scopus 로고    scopus 로고
    • EGFstimulation activates the nuclear localization signal of SHP-1
    • He, D.; Song, X.; Liu, L.; Burk, D.H.; Zhou, G.W. EGFstimulation activates the nuclear localization signal of SHP-1. J. Cell. Biochem., 2005, 94, 944-953.
    • (2005) J. Cell. Biochem. , vol.94 , pp. 944-953
    • He, D.1    Song, X.2    Liu, L.3    Burk, D.H.4    Zhou, G.W.5
  • 86
    • 0034845153 scopus 로고    scopus 로고
    • Role of the tyrosine phosphatase SHP-1 in K562 cell differentiation
    • Bruecher-Encke, B.; Griffin, J.D.; Neel, B.G.; Lorenz, U. Role of the tyrosine phosphatase SHP-1 in K562 cell differentiation. Leukemia, 2001, 15, 1424-1432.
    • (2001) Leukemia , vol.15 , pp. 1424-1432
    • Bruecher-Encke, B.1    Griffin, J.D.2    Neel, B.G.3    Lorenz, U.4
  • 87
    • 0034790737 scopus 로고    scopus 로고
    • Reduction of hematopoietic cell-specific tyrosine phosphatase SHP-1 gene expression in natural killer cell lymphoma and various types of lymphomas/leukemias: Combination analysis with cDNA expression array and tissue microarray
    • Oka, T.; Yoshino, T.; Hayashi, K.; Ohara, N.; Nakanishi, T.; Yamaai, Y.; Hiraki, A.; Sogawa, C.A.; Kondo, E.; Teramoto, N.; Takahashi, K.; Tsuchiyama, J.; Akagi, T. Reduction of hematopoietic cell-specific tyrosine phosphatase SHP-1 gene expression in natural killer cell lymphoma and various types of lymphomas/leukemias: combination analysis with cDNA expression array and tissue microarray. Am. J. Pathol., 2001, 159, 1495-1505.
    • (2001) Am. J. Pathol. , vol.159 , pp. 1495-1505
    • Oka, T.1    Yoshino, T.2    Hayashi, K.3    Ohara, N.4    Nakanishi, T.5    Yamaai, Y.6    Hiraki, A.7    Sogawa, C.A.8    Kondo, E.9    Teramoto, N.10    Takahashi, K.11    Tsuchiyama, J.12    Akagi, T.13
  • 88
    • 4344623279 scopus 로고    scopus 로고
    • Epigenetic dysregulation of the Jak/STAT pathway by frequent aberrant methylation of SHP1 but not SOCS1 in acute leukaemias
    • Chim, C.S.; Wong, A.S.; Kwong, Y.L. Epigenetic dysregulation of the Jak/STAT pathway by frequent aberrant methylation of SHP1 but not SOCS1 in acute leukaemias. Ann. Hematol., 2004, 83, 527-532.
    • (2004) Ann. Hematol. , vol.83 , pp. 527-532
    • Chim, C.S.1    Wong, A.S.2    Kwong, Y.L.3
  • 93
    • 77951239460 scopus 로고    scopus 로고
    • Immunohistochemical detection of tyrosine phosphatase SHP-1 predicts outcome after radical prostatectomy for localized prostate cancer
    • Tassidis, H.; Brokken, L.J.; Jirstrom, K.; Ehrnstrom, R.; Ponten, F.; Ulmert, D.; Bjartell, A.; Harkonen, P.; Wingren, A.G. Immunohistochemical detection of tyrosine phosphatase SHP-1 predicts outcome after radical prostatectomy for localized prostate cancer. Int. J. Cancer., 2010, 126, 2296-2307.
    • (2010) Int. J. Cancer. , vol.126 , pp. 2296-2307
    • Tassidis, H.1    Brokken, L.J.2    Jirstrom, K.3    Ehrnstrom, R.4    Ponten, F.5    Ulmert, D.6    Bjartell, A.7    Harkonen, P.8    Wingren, A.G.9
  • 94
    • 64049083563 scopus 로고    scopus 로고
    • Role of tyrosine phosphatase inhibitors in cancer treatment with emphasis on SH2 domain-containing tyrosine phosphatases (SHPs)
    • Irandoust, M.; van den Berg, T.K.; Kaspers, G.J.; Cloos, J. Role of tyrosine phosphatase inhibitors in cancer treatment with emphasis on SH2 domain-containing tyrosine phosphatases (SHPs). Anticancer Agents Med Chem. 2009, 9, 212-220.
    • (2009) Anticancer Agents Med Chem , vol.9 , pp. 212-220
    • Irandoust, M.1    van den Berg, T.K.2    Kaspers, G.J.3    Cloos, J.4
  • 95
    • 65649086812 scopus 로고    scopus 로고
    • Use of protein tyrosine phosphatase inhibitors as promising targeted therapeutic drugs
    • P. Use of protein tyrosine phosphatase inhibitors as promising targeted therapeutic drugs. Curr. Med. Chem., 2009, 16, 706-733.
    • (2009) Curr. Med. Chem. , vol.16 , pp. 706-733
  • 97
    • 34248631385 scopus 로고    scopus 로고
    • The role of histone deacetylases (HDACs) in human cancer
    • Ropero, S.; Esteller, M. The role of histone deacetylases (HDACs) in human cancer. Mol Oncol. 2007, 1, 19-25.
    • (2007) Mol Oncol , vol.1 , pp. 19-25
    • Ropero, S.1    Esteller, M.2
  • 98
    • 0035897570 scopus 로고    scopus 로고
    • Transcriptional activity of the SHP-1 gene in MCF7 cells is differentially regulated by binding of NF-Y factor to two distinct CCAATelements
    • Xu, Y.; Banville, D.; Zhao, H.F.; Zhao, X.; Shen, S.H. Transcriptional activity of the SHP-1 gene in MCF7 cells is differentially regulated by binding of NF-Y factor to two distinct CCAATelements. Gene, 2001, 269, 141-153.
    • (2001) Gene , vol.269 , pp. 141-153
    • Xu, Y.1    Banville, D.2    Zhao, H.F.3    Zhao, X.4    Shen, S.H.5
  • 99
    • 72949107155 scopus 로고    scopus 로고
    • Ginkgo biloba extract EGb 761 exerts anti-angiogenic effects via activation of tyrosine phosphatases
    • Koltermann, A.; Liebl, J.; Furst, R.; Ammer, H.; Vollmar, A.M.; Zahler, S. Ginkgo biloba extract EGb 761 exerts anti-angiogenic effects via activation of tyrosine phosphatases. J. Cell. Mol. Med., 2009, 13, 2122-2130.
    • (2009) J. Cell. Mol. Med. , vol.13 , pp. 2122-2130
    • Koltermann, A.1    Liebl, J.2    Furst, R.3    Ammer, H.4    Vollmar, A.M.5    Zahler, S.6
  • 100
    • 75149117841 scopus 로고    scopus 로고
    • 5-hydroxy-2-methyl-1,4-naphthoquinone, a vitamin K3 analogue, suppresses STAT3 activation pathway through induction of protein tyrosine phosphatase, SHP-1: Potential role in chemosensitization
    • Sandur, S.K.; Pandey, M.K.; Sung, B.; Aggarwal, B.B. 5-hydroxy-2-methyl-1,4-naphthoquinone, a vitamin K3 analogue, suppresses STAT3 activation pathway through induction of protein tyrosine phosphatase, SHP-1: potential role in chemosensitization. Mol. Cancer Res., 2010, 8, 107-118.
    • (2010) Mol. Cancer Res. , vol.8 , pp. 107-118
    • Sandur, S.K.1    Pandey, M.K.2    Sung, B.3    Aggarwal, B.B.4
  • 101
    • 58649104212 scopus 로고    scopus 로고
    • Boswellic acid blocks signal transducers and activators of transcription 3 signaling, proliferation, and survival of multiple myeloma via the protein tyrosine phosphatase SHP-1
    • Kunnumakkara, A.B.; Nair, A.S.; Sung, B.; Pandey, M.K.; Aggarwal, B.B. Boswellic acid blocks signal transducers and activators of transcription 3 signaling, proliferation, and survival of multiple myeloma via the protein tyrosine phosphatase SHP-1. Mol. Cancer Res., 2009, 7, 118-128.
    • (2009) Mol. Cancer Res. , vol.7 , pp. 118-128
    • Kunnumakkara, A.B.1    Nair, A.S.2    Sung, B.3    Pandey, M.K.4    Aggarwal, B.B.5
  • 102
    • 33748670269 scopus 로고    scopus 로고
    • Phosphopeptide ligands of the SHP-1 N-SH2 domain: Effects on binding and stimulation of phosphatase activity
    • Hampel, K.; Kaufhold, I.; Zacharias, M.; Böhmer, F.D.; Imhof, D. Phosphopeptide ligands of the SHP-1 N-SH2 domain: effects on binding and stimulation of phosphatase activity. ChemMedChem, 2006, 1, 869-877.
    • (2006) ChemMedChem , vol.1 , pp. 869-877
    • Hampel, K.1    Kaufhold, I.2    Zacharias, M.3    Böhmer, F.D.4    Imhof, D.5
  • 103
    • 1842430906 scopus 로고    scopus 로고
    • Shedding light on immunotherapy for cancer
    • S.A. Shedding light on immunotherapy for cancer. N. Engl. J. Med., 2004, 350, 1461-1463.
    • (2004) N. Engl. J. Med. , vol.350 , pp. 1461-1463
  • 104
    • 77953417324 scopus 로고    scopus 로고
    • Novel SHP-1 inhibitors tyrosine phosphatase inhibitor-1 and analogs with preclinical anti-tumor activities as tolerated oral agents
    • Kundu, S.; Fan, K.; Cao, M.; Lindner, D.J.; Zhao, Z.J.; Borden, E.; Yi, T. Novel SHP-1 inhibitors tyrosine phosphatase inhibitor-1 and analogs with preclinical anti-tumor activities as tolerated oral agents. J. Immunol., 2010, 184, 6529-6536.
    • (2010) J. Immunol. , vol.184 , pp. 6529-6536
    • Kundu, S.1    Fan, K.2    Cao, M.3    Lindner, D.J.4    Zhao, Z.J.5    Borden, E.6    Yi, T.7


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