메뉴 건너뛰기




Volumn 7, Issue 2, 2005, Pages 179-191

Prognostic, therapeutic, and mechanistic implications of a mouse model of leukemia evoked by Shp2 (PTPN11) mutations

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE; PROTEIN GAB2; PROTEIN KINASE B; PROTEIN TYROSINE PHOSPHATASE SHP 2; STAT5 PROTEIN; UNCLASSIFIED DRUG;

EID: 13844265841     PISSN: 15356108     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ccr.2005.01.010     Document Type: Article
Times cited : (230)

References (77)
  • 1
    • 0142059890 scopus 로고    scopus 로고
    • Molecular mechanism for a role of SHP2 in epidermal growth factor receptor signaling
    • Y.M. Agazie, and M.J. Hayman Molecular mechanism for a role of SHP2 in epidermal growth factor receptor signaling Mol. Cell. Biol. 23 2003 7875 7886
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 7875-7886
    • Agazie, Y.M.1    Hayman, M.J.2
  • 2
    • 0034624828 scopus 로고    scopus 로고
    • A clonogenic common myeloid progenitor that gives rise to all myeloid lineages
    • K. Akashi, D. Traver, T. Miyamoto, and I.L. Weissmann A clonogenic common myeloid progenitor that gives rise to all myeloid lineages Nature 404 2000 193 197
    • (2000) Nature , vol.404 , pp. 193-197
    • Akashi, K.1    Traver, D.2    Miyamoto, T.3    Weissmann, I.L.4
  • 3
    • 0142211311 scopus 로고    scopus 로고
    • Tyrosyl phosphorylation of Shp2 is required for normal ERK activation in response to some, but not all, growth factors
    • T. Araki, H. Nawa, and B.G. Neel Tyrosyl phosphorylation of Shp2 is required for normal ERK activation in response to some, but not all, growth factors J. Biol. Chem. 278 2003 41677 41684
    • (2003) J. Biol. Chem. , vol.278 , pp. 41677-41684
    • Araki, T.1    Nawa, H.2    Neel, B.G.3
  • 5
    • 0030843626 scopus 로고    scopus 로고
    • Juvenile myelomonocytic leukemia
    • M. Arico, A. Biondi, and C.-H. Pui Juvenile myelomonocytic leukemia Blood 90 1997 479 488
    • (1997) Blood , vol.90 , pp. 479-488
    • Arico, M.1    Biondi, A.2    Pui, C.-H.3
  • 6
    • 0142062911 scopus 로고    scopus 로고
    • MLL-rearranged leukemias: Insights from gene expression profiling
    • S.A. Armstrong, T.R. Golub, and S.J. Korsmeyer MLL-rearranged leukemias: Insights from gene expression profiling Semin. Hematol. 40 2003 268 273
    • (2003) Semin. Hematol. , vol.40 , pp. 268-273
    • Armstrong, S.A.1    Golub, T.R.2    Korsmeyer, S.J.3
  • 7
    • 0037279629 scopus 로고    scopus 로고
    • Analysis of Ras-induced overproliferation in Drosophila hemocytes
    • H. Asha, I. Nagy, G. Kovacs, D. Stetson, I. Ando, and C.R. Dearolf Analysis of Ras-induced overproliferation in Drosophila hemocytes Genetics 163 2003 203 215
    • (2003) Genetics , vol.163 , pp. 203-215
    • Asha, H.1    Nagy, I.2    Kovacs, G.3    Stetson, D.4    Ando, I.5    Dearolf, C.R.6
  • 9
    • 0032521428 scopus 로고    scopus 로고
    • Revealing mechanisms for SH2 domain-mediated regulation of the protein tyrosine phosphatase SHP-2
    • D. Barford, and B.G. Neel Revealing mechanisms for SH2 domain-mediated regulation of the protein tyrosine phosphatase SHP-2 Structure 6 1998 249 254
    • (1998) Structure , vol.6 , pp. 249-254
    • Barford, D.1    Neel, B.G.2
  • 10
    • 0028179013 scopus 로고
    • Protein-tyrosine-phosphatase SHPTP2 couples platelet-derived growth factor receptor beta to Ras
    • A. Bennett, T. Tang, S. Sugimoto, C. Walsh, and B. Neel Protein-tyrosine-phosphatase SHPTP2 couples platelet-derived growth factor receptor beta to Ras Proc. Natl. Acad. Sci. USA 91 1994 7335 7339
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 7335-7339
    • Bennett, A.1    Tang, T.2    Sugimoto, S.3    Walsh, C.4    Neel, B.5
  • 12
    • 2342559981 scopus 로고    scopus 로고
    • The TOR pathway: A target for cancer therapy
    • M.A. Bjornsti, and P.J. Houghton The TOR pathway: A target for cancer therapy Nat. Rev. Cancer 4 2004 335 348
    • (2004) Nat. Rev. Cancer , vol.4 , pp. 335-348
    • Bjornsti, M.A.1    Houghton, P.J.2
  • 14
    • 0027160708 scopus 로고
    • Targeted gene expression as a means of altering cell fates and generating dominant phenotypes
    • A.H. Brand, and P. Perrimon Targeted gene expression as a means of altering cell fates and generating dominant phenotypes Development 118 1993 401 415
    • (1993) Development , vol.118 , pp. 401-415
    • Brand, A.H.1    Perrimon, P.2
  • 18
    • 0037443055 scopus 로고    scopus 로고
    • Dynamic regulation of the ras pathway via proteolysis of the NF1 tumor suppressor
    • K. Cichowski, S. Santiago, M. Jardim, B.W. Johnson, and T. Jacks Dynamic regulation of the ras pathway via proteolysis of the NF1 tumor suppressor Genes Dev. 17 2003 449 454
    • (2003) Genes Dev. , vol.17 , pp. 449-454
    • Cichowski, K.1    Santiago, S.2    Jardim, M.3    Johnson, B.W.4    Jacks, T.5
  • 19
    • 0036045381 scopus 로고    scopus 로고
    • Tyrosine kinase fusion genes in chronic myeloproliferative diseases
    • N.C. Cross, and A. Reiter Tyrosine kinase fusion genes in chronic myeloproliferative diseases Leukemia 16 2002 1207 1212
    • (2002) Leukemia , vol.16 , pp. 1207-1212
    • Cross, N.C.1    Reiter, A.2
  • 21
    • 0030297891 scopus 로고    scopus 로고
    • Form and function in protein dephosphorylation
    • J.E. Denu, J.A. Stuckey, M.A. Saper, and J.E. Dixon Form and function in protein dephosphorylation Cell 87 1996 361 364
    • (1996) Cell , vol.87 , pp. 361-364
    • Denu, J.E.1    Stuckey, J.A.2    Saper, M.A.3    Dixon, J.E.4
  • 22
    • 0347725620 scopus 로고    scopus 로고
    • Hyperactivation of protein kinase B and ERK have discrete effects on survival, proliferation and cytokine expression in Nf1-deficient myeloid cells
    • S. Donovan, W. See, J. Bonifas, D. Stokoe, and K.M. Shannon Hyperactivation of protein kinase B and ERK have discrete effects on survival, proliferation and cytokine expression in Nf1-deficient myeloid cells Cancer Cell 2 2002 507 514
    • (2002) Cancer Cell , vol.2 , pp. 507-514
    • Donovan, S.1    See, W.2    Bonifas, J.3    Stokoe, D.4    Shannon, K.M.5
  • 23
    • 0030280090 scopus 로고    scopus 로고
    • Juvenile myelomonocytic leukemia: Molecular undrestanding and prospects for therapy
    • P.D. Emanuel, K.M. Shannon, and R.P. Castleberry Juvenile myelomonocytic leukemia: Molecular undrestanding and prospects for therapy Mol. Med. Today 2 1996 468 475
    • (1996) Mol. Med. Today , vol.2 , pp. 468-475
    • Emanuel, P.D.1    Shannon, K.M.2    Castleberry, R.P.3
  • 24
    • 0031055324 scopus 로고    scopus 로고
    • Development of "substrate-trapping" mutants to identify physiological substrates of protein tyrosine phosphatases
    • A.J. Flint, T. Tiganis, D. Barford, and N.K. Tonks Development of "substrate-trapping" mutants to identify physiological substrates of protein tyrosine phosphatases Proc. Natl. Acad. Sci. USA 94 1997 1680 1685
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 1680-1685
    • Flint, A.J.1    Tiganis, T.2    Barford, D.3    Tonks, N.K.4
  • 25
    • 0026471539 scopus 로고
    • Identification of a human src-homology 2 (SH2) containing tyrosine phosphatase: A putative homolog of Drosophila corkscrew
    • R.M. Freeman Jr., J. Plutzky, and B.G. Neel Identification of a human src-homology 2 (SH2) containing tyrosine phosphatase: A putative homolog of Drosophila corkscrew Proc. Natl. Acad. Sci. USA 89 1992 11239 11243
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 11239-11243
    • Freeman Jr., R.M.1    Plutzky, J.2    Neel, B.G.3
  • 28
    • 0028805449 scopus 로고
    • Metabolic effects of sodium metavanadate in humans with insulin-dependent and noninsulin-dependent diabetes mellitus in vivo and in vitro studies
    • A.B. Goldfine, D.C. Simonson, F. Folli, M.-E. Patti, and C.R. Kahn Metabolic effects of sodium metavanadate in humans with insulin-dependent and noninsulin-dependent diabetes mellitus in vivo and in vitro studies J. Clin. Endocrinol. Metab. 80 1995 3311 3319
    • (1995) J. Clin. Endocrinol. Metab. , vol.80 , pp. 3311-3319
    • Goldfine, A.B.1    Simonson, D.C.2    Folli, F.3    Patti, M.-E.4    Kahn, C.R.5
  • 29
    • 0037333264 scopus 로고    scopus 로고
    • The 'Gab' in signal transduction
    • H. Gu, and B.G. Neel The 'Gab' in signal transduction Trends Cell Biol. 13 2003 122 130
    • (2003) Trends Cell Biol. , vol.13 , pp. 122-130
    • Gu, H.1    Neel, B.G.2
  • 30
    • 0030974476 scopus 로고    scopus 로고
    • Characterization of two SHP-2-associated binding proteins and potential substrates in hematopoietic cells
    • H. Gu, J.D. Griffin, and B.G. Neel Characterization of two SHP-2-associated binding proteins and potential substrates in hematopoietic cells J. Biol. Chem. 272 1997 16421 16430
    • (1997) J. Biol. Chem. , vol.272 , pp. 16421-16430
    • Gu, H.1    Griffin, J.D.2    Neel, B.G.3
  • 32
    • 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
    • H. Hanafusa, S. Torii, T. Yasunaga, K. Matsumoto, and E. Nishida Shp2, an SH2-containing protein-tyrosine phosphatase, positively regulates receptor tyrosine kinase signaling by dephosphorylating and inactivating the inhibitor Sprouty J. Biol. Chem. 279 2004 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
  • 33
    • 0029031668 scopus 로고
    • Activation of a Drosophila Janus Kinase (JAK) causes hematopoietic neoplasia and developmental defects
    • D.A. Harrison, R. Binari, S. Nahreini, M. Gilman, and N. Perrimon Activation of a Drosophila Janus Kinase (JAK) causes hematopoietic neoplasia and developmental defects EMBO J. 14 1995 2857 2865
    • (1995) EMBO J. , vol.14 , pp. 2857-2865
    • Harrison, D.A.1    Binari, R.2    Nahreini, S.3    Gilman, M.4    Perrimon, N.5
  • 34
    • 0028385758 scopus 로고
    • Versatile retroviral vectors for potential use in gene therapy
    • R.G. Hawley, F.H.L. Lieu, A.Z.C. Fong, and T.S. Hawley Versatile retroviral vectors for potential use in gene therapy Gene Ther. 1 1994 136 138
    • (1994) Gene Ther. , vol.1 , pp. 136-138
    • Hawley, R.G.1    Lieu, F.H.L.2    Fong, A.Z.C.3    Hawley, T.S.4
  • 35
  • 38
    • 0030913673 scopus 로고    scopus 로고
    • Matrix adhesion and Ras transformation both activate a phosphoinositide 3-OH kinase and protein kinase B/Akt cellular survival pathway
    • A. Khwaja, P. Rodriguez-Viciana, S. Wennstrom, P.H. Warne, and J. Downward Matrix adhesion and Ras transformation both activate a phosphoinositide 3-OH kinase and protein kinase B/Akt cellular survival pathway EMBO J. 16 1997 2783 2793
    • (1997) EMBO J. , vol.16 , pp. 2783-2793
    • Khwaja, A.1    Rodriguez-Viciana, P.2    Wennstrom, S.3    Warne, P.H.4    Downward, J.5
  • 39
    • 0029085194 scopus 로고
    • Identification of a putative Syp substrate, the PDGFB receptor
    • R.A. Klinghoffer, and A. Kazlauskas Identification of a putative Syp substrate, the PDGFB receptor J. Biol. Chem. 270 1995 22208 22217
    • (1995) J. Biol. Chem. , vol.270 , pp. 22208-22217
    • Klinghoffer, R.A.1    Kazlauskas, A.2
  • 40
    • 0030045594 scopus 로고    scopus 로고
    • Nf1 deficiency causes Ras-mediated granulocyte/macrophage colony stimulating factor hypersensitivity and chronic myeloid leukemia
    • D.A. Largaespada, C.I. Brannan, N.A. Jenkins, and N.G. Copeland Nf1 deficiency causes Ras-mediated granulocyte/macrophage colony stimulating factor hypersensitivity and chronic myeloid leukemia Nat. Genet. 12 1996 137 143
    • (1996) Nat. Genet. , vol.12 , pp. 137-143
    • Largaespada, D.A.1    Brannan, C.I.2    Jenkins, N.A.3    Copeland, N.G.4
  • 42
    • 0026541143 scopus 로고
    • Activation of extracellular signal-regulated kinase, ERK2, by p21ras oncoprotein
    • S.J. Leevers, and C.J. Marshall Activation of extracellular signal-regulated kinase, ERK2, by p21ras oncoprotein EMBO J. 11 1992 569 574
    • (1992) EMBO J. , vol.11 , pp. 569-574
    • Leevers, S.J.1    Marshall, C.J.2
  • 46
    • 0034758469 scopus 로고    scopus 로고
    • Site-specific incorporation of a phosphotyrosine mimetic reveals a role for tyrosine phosphorylation of SHP-2 in cell signaling
    • W. Lu, D. Gong, D. Bar-Sagi, and P.A. Cole Site-specific incorporation of a phosphotyrosine mimetic reveals a role for tyrosine phosphorylation of SHP-2 in cell signaling Mol. Cell 8 2001 759 769
    • (2001) Mol. Cell , vol.8 , pp. 759-769
    • Lu, W.1    Gong, D.2    Bar-Sagi, D.3    Cole, P.A.4
  • 47
    • 0028938172 scopus 로고
    • tum-l Jak kinase causes leukemia-like hematopoietic defects
    • tum-l Jak kinase causes leukemia-like hematopoietic defects EMBO J. 14 1995 1412 1420
    • (1995) EMBO J. , vol.14 , pp. 1412-1420
    • Luo, H.1    Hanratty, W.P.2    Dearolf, C.R.3
  • 48
    • 0034065402 scopus 로고    scopus 로고
    • Clinical pharmacokinetics and therapeutic drug monitoring of sirolimus
    • A. MacDonald, J. Scarola, J.T. Burke, and J.J. Zimmerman Clinical pharmacokinetics and therapeutic drug monitoring of sirolimus Clin. Ther. 22 2000 B101 B121
    • (2000) Clin. Ther. , vol.22
    • MacDonald, A.1    Scarola, J.2    Burke, J.T.3    Zimmerman, J.J.4
  • 49
    • 1042302152 scopus 로고    scopus 로고
    • Blood cells of Drosophilla: Cell lineages and role in host defence
    • M. Meister Blood cells of Drosophilla: Cell lineages and role in host defence Curr. Opin. Immunol. 16 2004 10 15
    • (2004) Curr. Opin. Immunol. , vol.16 , pp. 10-15
    • Meister, M.1
  • 50
    • 0034661522 scopus 로고    scopus 로고
    • The Grb2 binding site is required for the induction of chronic myeloid leukemia-like disease in mice by the Bcr/Abl tyrosine kinase
    • R.P. Million, and R.A. Van Etten The Grb2 binding site is required for the induction of chronic myeloid leukemia-like disease in mice by the Bcr/Abl tyrosine kinase Blood 96 2000 664 670
    • (2000) Blood , vol.96 , pp. 664-670
    • Million, R.P.1    Van Etten, R.A.2
  • 52
    • 0038771965 scopus 로고    scopus 로고
    • The "shp"ing news: SH2 domain-containing tyrosine phosphatases in cell signaling
    • B.G. Neel, H. Gu, and L. Pao The "Shp"ing news: SH2 domain-containing tyrosine phosphatases in cell signaling Trends Biochem. Sci. 28 2003 284 293
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 284-293
    • Neel, B.G.1    Gu, H.2    Pao, L.3
  • 54
    • 0033989423 scopus 로고    scopus 로고
    • Activated mutants of SHP-2 preferentially induce elongation of Xenopus animal caps
    • A.M. O'Reilly, S. Pluskey, S.E. Shoelson, and B.G. Neel Activated mutants of SHP-2 preferentially induce elongation of Xenopus animal caps Mol. Cell. Biol. 20 1999 299 311
    • (1999) Mol. Cell. Biol. , vol.20 , pp. 299-311
    • O'Reilly, A.M.1    Pluskey, S.2    Shoelson, S.E.3    Neel, B.G.4
  • 55
    • 4644276702 scopus 로고    scopus 로고
    • Imatinib targets other than bcr/abl and their clinical relevance in myeloid disorders
    • A. Pardanani, and A. Tefferi Imatinib targets other than bcr/abl and their clinical relevance in myeloid disorders Blood 104 2004 1931 1939
    • (2004) Blood , vol.104 , pp. 1931-1939
    • Pardanani, A.1    Tefferi, A.2
  • 56
    • 0031457622 scopus 로고    scopus 로고
    • Signaling through scaffold, anchoring and adapter proteins
    • T. Pawson, and J.D. Scott Signaling through scaffold, anchoring and adapter proteins Science 278 1997 2075 2080
    • (1997) Science , vol.278 , pp. 2075-2080
    • Pawson, T.1    Scott, J.D.2
  • 57
    • 0026630991 scopus 로고
    • Corkscrew encodes a putative tyrosine phosphatase that functions to transduce the terminal signal from the receptor tyrosine kinase torso
    • L.A. Perkins, I. Larsen, and N. Perrimon corkscrew encodes a putative tyrosine phosphatase that functions to transduce the terminal signal from the receptor tyrosine kinase torso Cell 70 1992 225 236
    • (1992) Cell , vol.70 , pp. 225-236
    • Perkins, L.A.1    Larsen, I.2    Perrimon, N.3
  • 58
    • 1542289021 scopus 로고    scopus 로고
    • Roles of Gab1 and SHP2 in paxillin tyrosine dephosphorylation and Src activation in response to epidermal growth factor
    • Y. Ren, S. Meng, L. Mei, Z.J. Zhao, R. Jove, and J. Wu Roles of Gab1 and SHP2 in paxillin tyrosine dephosphorylation and Src activation in response to epidermal growth factor J. Biol. Chem. 279 2004 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
  • 61
    • 0033614446 scopus 로고    scopus 로고
    • Chronic myeloid leukemia
    • C.L. Sawyers Chronic myeloid leukemia N. Engl. J. Med. 340 1999 1330 1340
    • (1999) N. Engl. J. Med. , vol.340 , pp. 1330-1340
    • Sawyers, C.L.1
  • 62
    • 0032530972 scopus 로고    scopus 로고
    • Transformation of hematopoietic cell lines to growth-factor independence and induction of a fatal myelo- and lymphoproliferative disease in mice by retrovirally transduced TEL/JAK2 fusion genes
    • J. Schwaller, J. Frantsve, J. Aster, I.R. Williams, M.H. Tomasson, T.S. Ross, P. Peeters, L. Van Rompaey, R.A. Van Etten, and R. Ilaria Jr. Transformation of hematopoietic cell lines to growth-factor independence and induction of a fatal myelo- and lymphoproliferative disease in mice by retrovirally transduced TEL/JAK2 fusion genes EMBO J. 17 1998 5321 5333
    • (1998) EMBO J. , vol.17 , pp. 5321-5333
    • Schwaller, J.1    Frantsve, J.2    Aster, J.3    Williams, I.R.4    Tomasson, M.H.5    Ross, T.S.6    Peeters, P.7    Van Rompaey, L.8    Van Etten, R.A.9    Ilaria Jr., R.10
  • 63
    • 0034722894 scopus 로고    scopus 로고
    • Development of anticancer drugs targeting the MAP kinase pathway
    • J. Sebolt-Leopold Development of anticancer drugs targeting the MAP kinase pathway Oncogene 19 2000 6594 6599
    • (2000) Oncogene , vol.19 , pp. 6594-6599
    • Sebolt-Leopold, J.1
  • 64
    • 0030665934 scopus 로고    scopus 로고
    • Myeloid disorders in infants with Noonan syndrome and a resident's "rule" recalled
    • L.E. Side, and K.M. Shannon Myeloid disorders in infants with Noonan syndrome and a resident's "rule" recalled J. Pediatr. 130 1997 857 859
    • (1997) J. Pediatr. , vol.130 , pp. 857-859
    • Side, L.E.1    Shannon, K.M.2
  • 68
    • 3142620903 scopus 로고    scopus 로고
    • Genetic evidence for lineage-related and differentiation stage-related contribution of somatic PTPN11 mutations to leukemogenesis in childhood acute leukemia
    • M. Tartaglia, S. Martinelli, G. Cazzaniga, V. Cordeddu, I. Iavarone, M. Spinelli, C. Palmi, C. Carta, A. Pession, and M. Arico Genetic evidence for lineage-related and differentiation stage-related contribution of somatic PTPN11 mutations to leukemogenesis in childhood acute leukemia Blood 104 2004 307 313
    • (2004) Blood , vol.104 , pp. 307-313
    • Tartaglia, M.1    Martinelli, S.2    Cazzaniga, G.3    Cordeddu, V.4    Iavarone, I.5    Spinelli, M.6    Palmi, C.7    Carta, C.8    Pession, A.9    Arico, M.10
  • 69
    • 0035313868 scopus 로고    scopus 로고
    • Combinatorial control of specificity by protein-tyrosine phosphatases
    • N.K. Tonks, and B.G. Neel Combinatorial control of specificity by protein-tyrosine phosphatases Curr. Opin. Cell Biol. 13 2001 182 195
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 182-195
    • Tonks, N.K.1    Neel, B.G.2
  • 71
    • 0028068607 scopus 로고
    • Interleukin (IL)-3 and granulocyte/macrophage colony-stimulating factor, but not IL-4, induce tyrosine phosphorylation, activation, and association of SHPTP2 with Grb2 and phosphatidylinositol 3′-kinase
    • M.J. Welham, U. Dechert, K.B. Leslie, F. Jirik, and J.W. Schrader Interleukin (IL)-3 and granulocyte/macrophage colony-stimulating factor, but not IL-4, induce tyrosine phosphorylation, activation, and association of SHPTP2 with Grb2 and phosphatidylinositol 3′-kinase J. Biol. Chem. 269 1994 23764 23768
    • (1994) J. Biol. Chem. , vol.269 , pp. 23764-23768
    • Welham, M.J.1    Dechert, U.2    Leslie, K.B.3    Jirik, F.4    Schrader, J.W.5
  • 72
    • 4944249117 scopus 로고    scopus 로고
    • BAY 43-9006 exhibits broad spectrum oral antitumor activity and targets the RAF/MEK/ERK pathway and receptor tyrosine kinases involved in tumor progression and angiogenesis
    • S.M. Wilhelm, C. Carter, L. Tang, D. Wilkie, A. McNabola, H. Rong, C. Chen, X. Zhang, P. Vincent, and M. McHugh BAY 43-9006 exhibits broad spectrum oral antitumor activity and targets the RAF/MEK/ERK pathway and receptor tyrosine kinases involved in tumor progression and angiogenesis Cancer Res. 64 2004 7099 7109
    • (2004) Cancer Res. , vol.64 , pp. 7099-7109
    • Wilhelm, S.M.1    Carter, C.2    Tang, L.3    Wilkie, D.4    McNabola, A.5    Rong, H.6    Chen, C.7    Zhang, X.8    Vincent, P.9    McHugh, M.10
  • 74
    • 0032101134 scopus 로고    scopus 로고
    • Nf1 regulates hematopoietic progenitor cell growth and Ras signaling in response to multiple cytokines
    • Y. Zhang, T.A. Vik, J.W. Ryder, E.F. Srour, T. Jacks, K. Shannon, and D.W. Clapp Nf1 regulates hematopoietic progenitor cell growth and Ras signaling in response to multiple cytokines J. Exp. Med. 187 1998 1893 1902
    • (1998) J. Exp. Med. , vol.187 , pp. 1893-1902
    • Zhang, Y.1    Vik, T.A.2    Ryder, J.W.3    Srour, E.F.4    Jacks, T.5    Shannon, K.6    Clapp, D.W.7
  • 75
    • 0036258332 scopus 로고    scopus 로고
    • Receptor-specific regulation of phosphatidyl 3′-kinase activation by the protein tyrosine phosphatase Shp2
    • S.Q. Zhang, W.G. Tsiaris, T. Araki, G. Wen, L. Minichiello, R. Klein, and B.G. Neel Receptor-specific regulation of phosphatidyl 3′-kinase activation by the protein tyrosine phosphatase Shp2 Mol. Cell. Biol. 22 2002 4062 4072
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 4062-4072
    • Zhang, S.Q.1    Tsiaris, W.G.2    Araki, T.3    Wen, G.4    Minichiello, L.5    Klein, R.6    Neel, B.G.7
  • 77
    • 0027336310 scopus 로고
    • K-pn, a homologue of the metastasis suppressor gene nm23, suppresses the Tum-l hematopoietic oncogene
    • K-pn, a homologue of the metastasis suppressor gene nm23, suppresses the Tum-l hematopoietic oncogene Nat. Genet. 4 1993 195 201
    • (1993) Nat. Genet. , vol.4 , pp. 195-201
    • Zinyk, D.L.1    McGonnigal, B.G.2    Dearolf, C.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.