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Volumn 28, Issue 7, 2000, Pages 826-832

All-trans-retinoic acid induces tyrosine phosphorylation of the CrkL adapter in acute promyelocytic leukemia cells

Author keywords

Leukemia; Retinoic acid; Tyrosine kinases

Indexed keywords

CELL PROTEIN; GLUTATHIONE TRANSFERASE; GUANINE NUCLEOTIDE BINDING PROTEIN; HYBRID PROTEIN; PROTEIN TYROSINE KINASE; RETINOIC ACID;

EID: 0034089137     PISSN: 0301472X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0301-472X(00)00170-3     Document Type: Article
Times cited : (10)

References (51)
  • 1
    • 0028137038 scopus 로고
    • All-trans-retinoic acid in acute promyelocytic leukemia and its potential in other hematologic malignancies
    • Tallman S. All-trans-retinoic acid in acute promyelocytic leukemia and its potential in other hematologic malignancies. Semin Hematol. 31:1994;38.
    • (1994) Semin Hematol , vol.31 , pp. 38
    • Tallman, S.1
  • 2
    • 0029911825 scopus 로고    scopus 로고
    • Treatment of acute promyelocytic leukemia
    • Fenaux P., Degos L. Treatment of acute promyelocytic leukemia. Bailieres Clin Haematol. 9:1996;107.
    • (1996) Bailieres Clin Haematol , vol.9 , pp. 107
    • Fenaux, P.1    Degos, L.2
  • 3
    • 0029767898 scopus 로고    scopus 로고
    • Differentiation therapy in acute myeloid leukemia
    • Tallman S. Differentiation therapy in acute myeloid leukemia. Leukemia. 10:1996;1262.
    • (1996) Leukemia , vol.10 , pp. 1262
    • Tallman, S.1
  • 4
    • 0027957296 scopus 로고
    • Acute promyelocytic leukemia: From genetics to treatment
    • Grignani F., Fagioli M., Alcalay M.et al. Acute promyelocytic leukemia. from genetics to treatment Blood. 83:1994;10.
    • (1994) Blood , vol.83 , pp. 10
    • Grignani, F.1    Fagioli, M.2    Alcalay, M.3
  • 5
    • 0028419153 scopus 로고
    • The retinoid signaling pathway: Molecular and genetic analyses
    • Chambon P. The retinoid signaling pathway. molecular and genetic analyses Semin Cell Biol. 5:1994;115.
    • (1994) Semin Cell Biol , vol.5 , pp. 115
    • Chambon, P.1
  • 6
    • 0029562554 scopus 로고
    • The RXR heterodimers and orphan receptor
    • Mangelsdorf D.J., Evans R.M. The RXR heterodimers and orphan receptor. Cell. 83:1995;841.
    • (1995) Cell , vol.83 , pp. 841
    • Mangelsdorf, D.J.1    Evans, R.M.2
  • 7
    • 0025271098 scopus 로고
    • Retinoic acid induced granulocytic differentiation of HL-60 myeloid leukemia cells is mediated directly through the retinoic acid receptor (RARα)
    • Collins S.J., Robertson K., Mueller L. Retinoic acid induced granulocytic differentiation of HL-60 myeloid leukemia cells is mediated directly through the retinoic acid receptor (RARα). Mol Cell Biol. 10:1990;2154.
    • (1990) Mol Cell Biol , vol.10 , pp. 2154
    • Collins, S.J.1    Robertson, K.2    Mueller, L.3
  • 8
    • 0027078742 scopus 로고
    • A mutated retinoic acid receptor exhibiting dominant-negative activity alters the lineage development of a multipotent hematopoietic cell line
    • Tsai S., Bartelmez S., Heyman R.et al. A mutated retinoic acid receptor exhibiting dominant-negative activity alters the lineage development of a multipotent hematopoietic cell line. Genes Dev. 6:1992;2258.
    • (1992) Genes Dev , vol.6 , pp. 2258
    • Tsai, S.1    Bartelmez, S.2    Heyman, R.3
  • 9
    • 0029671146 scopus 로고    scopus 로고
    • RXR alpha is essential for mediating the all-trans-retinoic acid-induced growth arrest of C2 myogenic cells
    • Froeschle A., Carnac G., Alric S.et al. RXR alpha is essential for mediating the all-trans-retinoic acid-induced growth arrest of C2 myogenic cells. Oncogene. 12:1996;411.
    • (1996) Oncogene , vol.12 , pp. 411
    • Froeschle, A.1    Carnac, G.2    Alric, S.3
  • 10
    • 0000237552 scopus 로고    scopus 로고
    • Role of the PML gene and the retinoic acid pathway
    • Wang Z.G., Delva L., Gaboli M.et al. Role of the PML gene and the retinoic acid pathway. Science. 279:1998;1547.
    • (1998) Science , vol.279 , pp. 1547
    • Wang, Z.G.1    Delva, L.2    Gaboli, M.3
  • 11
    • 15844409506 scopus 로고    scopus 로고
    • Lyn and Fgr protein-tyrosine kinases prevent apoptosis during retinoic acid-induced granulocytic differentiation of HL-60 cells
    • Katagiri K., Yokoyama K.K., Yamamoto T.et al. Lyn and Fgr protein-tyrosine kinases prevent apoptosis during retinoic acid-induced granulocytic differentiation of HL-60 cells. J Biol Chem. 271:1996;11557.
    • (1996) J Biol Chem , vol.271 , pp. 11557
    • Katagiri, K.1    Yokoyama, K.K.2    Yamamoto, T.3
  • 12
    • 0031815756 scopus 로고    scopus 로고
    • Acute promyelocytic leukemia as a model for cross talk between interferon and retinoic acid pathways: From molecular biology to clinical application
    • Gaboli M., Gandini D., Delva L.et al. Acute promyelocytic leukemia as a model for cross talk between interferon and retinoic acid pathways. from molecular biology to clinical application Leuk Lymphoma. 30:1998;11.
    • (1998) Leuk Lymphoma , vol.30 , pp. 11
    • Gaboli, M.1    Gandini, D.2    Delva, L.3
  • 13
    • 0029128365 scopus 로고
    • Association of the interferon-dependent tyrosine kinase Tyk-2 with the hematopoietic cell phosphatase
    • Yetter A., Uddin S., Krolewski J.J.et al. Association of the interferon-dependent tyrosine kinase Tyk-2 with the hematopoietic cell phosphatase. J Biol Chem. 270:1995;18179.
    • (1995) J Biol Chem , vol.270 , pp. 18179
    • Yetter, A.1    Uddin, S.2    Krolewski, J.J.3
  • 14
    • 0030865679 scopus 로고    scopus 로고
    • The IRS-pathway operates distinctively from the Stat-pathway in hematopoietic cells and transduces common and distinct signals during engagement of the insulin or interferon α receptors
    • Uddin S., Fish E.N., Sher D.et al. The IRS-pathway operates distinctively from the Stat-pathway in hematopoietic cells and transduces common and distinct signals during engagement of the insulin or interferon α receptors. Blood. 90:1997;2574.
    • (1997) Blood , vol.90 , pp. 2574
    • Uddin, S.1    Fish, E.N.2    Sher, D.3
  • 15
    • 0033569766 scopus 로고    scopus 로고
    • Activation of the p38 map kinase by Type I interferons
    • Uddin S., Mazchrzak B., Woodson J.et al. Activation of the p38 map kinase by Type I interferons. J Biol Chem. 274:1999;30127.
    • (1999) J Biol Chem , vol.274 , pp. 30127
    • Uddin, S.1    Mazchrzak, B.2    Woodson, J.3
  • 16
    • 0031038399 scopus 로고    scopus 로고
    • Direct binding of CRKL to BCR-ABL is not required for BCR-ABL transformation
    • Heaney C., Kolibaba K., Bhat A.et al. Direct binding of CRKL to BCR-ABL is not required for BCR-ABL transformation. Blood. 89:1997;297.
    • (1997) Blood , vol.89 , pp. 297
    • Heaney, C.1    Kolibaba, K.2    Bhat, A.3
  • 17
    • 0028982917 scopus 로고
    • Interferon α engages the insulin receptor substrate-1 to associate with the phosphatidylinositol 3′-kinase
    • Uddin S., Yenush L., Sun X.-J.et al. Interferon α engages the insulin receptor substrate-1 to associate with the phosphatidylinositol 3′-kinase. J Biol Chem. 270:1995;15938.
    • (1995) J Biol Chem , vol.270 , pp. 15938
    • Uddin, S.1    Yenush, L.2    Sun, X.-J.3
  • 18
    • 0031014969 scopus 로고    scopus 로고
    • +-mediated activation of Rap1 in human platelets
    • +-mediated activation of Rap1 in human platelets. EMBO J. 16:1997;252.
    • (1997) EMBO J , vol.16 , pp. 252
    • Franke, B.1    Akkerman, J.W.2    Bos, J.L.3
  • 19
    • 0032570874 scopus 로고    scopus 로고
    • Costimulation through CD28 suppresses T cell receptor-dependent activation of the Ras-like small GTPase Rap1 in human T lymphocytes
    • Reedquist K.A., Bos J.L. Costimulation through CD28 suppresses T cell receptor-dependent activation of the Ras-like small GTPase Rap1 in human T lymphocytes. J Biol Chem. 273:1998;4494.
    • (1998) J Biol Chem , vol.273 , pp. 4494
    • Reedquist, K.A.1    Bos, J.L.2
  • 20
    • 0032531014 scopus 로고    scopus 로고
    • Activation of the small GTPase rap1 in human neutrophils
    • M'Rabet L., Coffer P., Zwartkruis F.et al. Activation of the small GTPase rap1 in human neutrophils. Blood. 92:1998;2133.
    • (1998) Blood , vol.92 , pp. 2133
    • M'Rabet, L.1    Coffer, P.2    Zwartkruis, F.3
  • 21
    • 0033609850 scopus 로고    scopus 로고
    • Engagement of Gab1 and Gab2 in erythropoietin signalling
    • Wickrema A., Uddin S., Sharma A.et al. Engagement of Gab1 and Gab2 in erythropoietin signalling. J Biol Chem. 274:1999;24469.
    • (1999) J Biol Chem , vol.274 , pp. 24469
    • Wickrema, A.1    Uddin, S.2    Sharma, A.3
  • 22
    • 0028225352 scopus 로고
    • NB4 cells show bilineage potential and aberrant pattern of neutrophil secondary granule protein gene expression
    • Gupta A.K., Kolibaba K., Zibello T.A.et al. NB4 cells show bilineage potential and aberrant pattern of neutrophil secondary granule protein gene expression. Blood. 84:1994;294.
    • (1994) Blood , vol.84 , pp. 294
    • Gupta, A.K.1    Kolibaba, K.2    Zibello, T.A.3
  • 23
    • 0026013478 scopus 로고
    • NB4, a maturation inducible cell line with t(15;17) marker isolated from a human acute promyelocytic leukemia (M3)
    • Lanotte M., Martin-Thoruvenin V., Najman S.et al. NB4, a maturation inducible cell line with t(15;17) marker isolated from a human acute promyelocytic leukemia (M3). Blood. 77:1991;1080.
    • (1991) Blood , vol.77 , pp. 1080
    • Lanotte, M.1    Martin-Thoruvenin, V.2    Najman, S.3
  • 24
    • 17544376424 scopus 로고    scopus 로고
    • Modulation of interferon (IFN)-inducible gene expression by retinoic acid. Up-regulation of Stat1 protein in IFN-unresponsive cells
    • Kolla V., Lindner D.J., Weihua X.et al. Modulation of interferon (IFN)-inducible gene expression by retinoic acid. Up-regulation of Stat1 protein in IFN-unresponsive cells. J Biol Chem. 271:1996;10508.
    • (1996) J Biol Chem , vol.271 , pp. 10508
    • Kolla, V.1    Lindner, D.J.2    Weihua, X.3
  • 25
    • 0030899367 scopus 로고    scopus 로고
    • Modulation of interferon action by retinoids. Induction of murine Stat1 gene expression by retinoic acid
    • Weihua X., Kolla V., Kalvakolanu D.V. Modulation of interferon action by retinoids. Induction of murine Stat1 gene expression by retinoic acid. J Biol Chem. 272:1997;9742.
    • (1997) J Biol Chem , vol.272 , pp. 9742
    • Weihua, X.1    Kolla, V.2    Kalvakolanu, D.V.3
  • 26
    • 0030899018 scopus 로고    scopus 로고
    • Stat1 is induced and activated by all-trans retinoic acid in acute promyelocytic leukemia cells
    • Gianni M., Terao M., Fortino I.et al. Stat1 is induced and activated by all-trans retinoic acid in acute promyelocytic leukemia cells. Blood. 89:1997;1001.
    • (1997) Blood , vol.89 , pp. 1001
    • Gianni, M.1    Terao, M.2    Fortino, I.3
  • 27
    • 0029908573 scopus 로고    scopus 로고
    • Retinoic acid activates interferon regulatory factor gene expression in myeloid cells
    • Matikainen S., Ronni T., Hurme M.et al. Retinoic acid activates interferon regulatory factor gene expression in myeloid cells. Blood. 88:1996;114.
    • (1996) Blood , vol.88 , pp. 114
    • Matikainen, S.1    Ronni, T.2    Hurme, M.3
  • 28
    • 0030972135 scopus 로고    scopus 로고
    • Retinoic acid induces signal transducer and activator of transcription STAT1, STAT2, and p48 expression in myeloid leukemia cells and enhances their responsiveness to interferons
    • Matikainen S., Ronni T., Lehtonen A.et al. Retinoic acid induces signal transducer and activator of transcription STAT1, STAT2, and p48 expression in myeloid leukemia cells and enhances their responsiveness to interferons. Cell Growth Differ. 8:1997;687.
    • (1997) Cell Growth Differ , vol.8 , pp. 687
    • Matikainen, S.1    Ronni, T.2    Lehtonen, A.3
  • 29
    • 0030598824 scopus 로고    scopus 로고
    • Interaction of the c-cbl proto-oncogene product with the Tyk-2 protein tyrosine kinase
    • Uddin S., Gardziola C., Dangat A.et al. Interaction of the c-cbl proto-oncogene product with the Tyk-2 protein tyrosine kinase. Biochem Biophys Res Commun. 225:1996;833.
    • (1996) Biochem Biophys Res Commun , vol.225 , pp. 833
    • Uddin, S.1    Gardziola, C.2    Dangat, A.3
  • 30
    • 0034652014 scopus 로고    scopus 로고
    • Interferon γ activates the C3G-Rap1 signaling pathway
    • Alsayed Y., Uddin S., Ahmad S.et al. Interferon γ activates the C3G-Rap1 signaling pathway. J Immunol. 164:2000;1800.
    • (2000) J Immunol , vol.164 , pp. 1800
    • Alsayed, Y.1    Uddin, S.2    Ahmad, S.3
  • 31
    • 0030778425 scopus 로고    scopus 로고
    • The type I interferon receptor mediates tyrosine phosphorylation of the CrkL adaptor protein
    • Ahmad S., Alsayed Y., Druker B.J.et al. The type I interferon receptor mediates tyrosine phosphorylation of the CrkL adaptor protein. J Biol Chem. 272:1997;29991.
    • (1997) J Biol Chem , vol.272 , pp. 29991
    • Ahmad, S.1    Alsayed, Y.2    Druker, B.J.3
  • 32
    • 0032806841 scopus 로고    scopus 로고
    • CrkL and CrkII participate in the generation of the growth inhibitory effects of interferons on primary hematopoietic progenitors
    • Platanias L.C., Uddin S., Bruno E.et al. CrkL and CrkII participate in the generation of the growth inhibitory effects of interferons on primary hematopoietic progenitors. Exp Hematol. 27:1999;1315.
    • (1999) Exp Hematol , vol.27 , pp. 1315
    • Platanias, L.C.1    Uddin, S.2    Bruno, E.3
  • 33
    • 0033534450 scopus 로고    scopus 로고
    • Activation of a CrkL-Stat5 signaling complex by Type I interferons
    • Fish E.N., Uddin S., Korkmaz M.et al. Activation of a CrkL-Stat5 signaling complex by Type I interferons. J Biol Chem. 274:1999;571.
    • (1999) J Biol Chem , vol.274 , pp. 571
    • Fish, E.N.1    Uddin, S.2    Korkmaz, M.3
  • 34
    • 0032867876 scopus 로고    scopus 로고
    • Retinoic acid and interferon signaling cross talk in normal and RA-resistant APL cells
    • Chelbi-Alix M.K., Pelicano L. Retinoic acid and interferon signaling cross talk in normal and RA-resistant APL cells. Leukemia. 13:1999;1167.
    • (1999) Leukemia , vol.13 , pp. 1167
    • Chelbi-Alix, M.K.1    Pelicano, L.2
  • 35
    • 0031032589 scopus 로고    scopus 로고
    • Retinoic acid and IFN inhibition of cell proliferation is associated with apoptosis in squamous carcinoma cell lines: Role of IRF-1 and Tgase II-dependent pathways
    • Giandomenico V., Lancilotti F., Fiorucci G.et al. Retinoic acid and IFN inhibition of cell proliferation is associated with apoptosis in squamous carcinoma cell lines. role of IRF-1 and Tgase II-dependent pathways Cell Growth Differ. 8:1997;91.
    • (1997) Cell Growth Differ , vol.8 , pp. 91
    • Giandomenico, V.1    Lancilotti, F.2    Fiorucci, G.3
  • 36
    • 0028998961 scopus 로고
    • Growth inhibition of human acute promyelocytic leukemia NB-4 cells by interferons and all-trans-retinoic acid: Trans-modulation of inducible gene expression pathways
    • Kumar R., Korutla L. Growth inhibition of human acute promyelocytic leukemia NB-4 cells by interferons and all-trans-retinoic acid. trans-modulation of inducible gene expression pathways Anticancer Res. 15:1995;353.
    • (1995) Anticancer Res , vol.15 , pp. 353
    • Kumar, R.1    Korutla, L.2
  • 37
    • 0028982945 scopus 로고
    • Interferon alpha-2b and retinoic acid combined treatment affects proliferation and gene expression of human cervical carcinoma cells
    • Lancilotti F., Giandomenico V., Affabris E.et al. Interferon alpha-2b and retinoic acid combined treatment affects proliferation and gene expression of human cervical carcinoma cells. Cancer Res. 55:1995;3158.
    • (1995) Cancer Res , vol.55 , pp. 3158
    • Lancilotti, F.1    Giandomenico, V.2    Affabris, E.3
  • 38
    • 0030690282 scopus 로고    scopus 로고
    • Retinoic acid enhances the expression of interferon-induced proteins: Evidence for multiple mechanisms of action
    • Pelicano L., Li F., Schindler C.et al. Retinoic acid enhances the expression of interferon-induced proteins. evidence for multiple mechanisms of action Oncogene. 15:1998;2349.
    • (1998) Oncogene , vol.15 , pp. 2349
    • Pelicano, L.1    Li, F.2    Schindler, C.3
  • 39
    • 0032727032 scopus 로고    scopus 로고
    • Signaling pathways activated by interferons
    • Platanias L.C., Fish E.N. Signaling pathways activated by interferons. Exp Hematol. 27:1999;1583.
    • (1999) Exp Hematol , vol.27 , pp. 1583
    • Platanias, L.C.1    Fish, E.N.2
  • 40
    • 0028885860 scopus 로고
    • Coupling of the proto-oncogene product c-Cbl to the epidermal growth factor receptor
    • Meisner H., Czech M.P. Coupling of the proto-oncogene product c-Cbl to the epidermal growth factor receptor. J Biol Chem. 270:1995;25332.
    • (1995) J Biol Chem , vol.270 , pp. 25332
    • Meisner, H.1    Czech, M.P.2
  • 41
    • 0029671427 scopus 로고    scopus 로고
    • cbl is a cytosolic adapter protein that associates with phosphoinositide 3-kinase in response to epidermal growth factor in PC12 and other cells
    • cbl is a cytosolic adapter protein that associates with phosphoinositide 3-kinase in response to epidermal growth factor in PC12 and other cells. J Biol Chem. 271:1996;563.
    • (1996) J Biol Chem , vol.271 , pp. 563
    • Soltoff, S.P.1    Cantley, L.2
  • 42
    • 0029043786 scopus 로고
    • Tyrosine phosphorylation and translocation of the c-Cbl protein after activation of tyrosine kinase signaling pathways
    • Tanaka S., Neff L., Baron R.et al. Tyrosine phosphorylation and translocation of the c-Cbl protein after activation of tyrosine kinase signaling pathways. J Biol Chem. 270:1995;14347.
    • (1995) J Biol Chem , vol.270 , pp. 14347
    • Tanaka, S.1    Neff, L.2    Baron, R.3
  • 43
    • 0028901016 scopus 로고
    • Identification of the major tyrosine kinase substrate in signaling complexes formed after engagement of Fcγ receptors
    • Marcilla A., Rivero-Lezcano O.M., Agarwal A.et al. Identification of the major tyrosine kinase substrate in signaling complexes formed after engagement of Fcγ receptors. J Biol Chem. 270:1995;9115.
    • (1995) J Biol Chem , vol.270 , pp. 9115
    • Marcilla, A.1    Rivero-Lezcano, O.M.2    Agarwal, A.3
  • 44
    • 0028027169 scopus 로고
    • The protein product of the c-cblproto-oncogene is the 120 kDa tyrosine phosphorylated protein in Jurkat cells activated via the T cell antigen receptor
    • Donovan J.A., Wange R.L., Langdon W.Y.et al. The protein product of the c-cblproto-oncogene is the 120 kDa tyrosine phosphorylated protein in Jurkat cells activated via the T cell antigen receptor. J Biol Chem. 269:1994;22921.
    • (1994) J Biol Chem , vol.269 , pp. 22921
    • Donovan, J.A.1    Wange, R.L.2    Langdon, W.Y.3
  • 45
    • 0029034440 scopus 로고
    • Interactions of Cbl with Grb-2 and phosphatidylinositol 3′-kinase in activated Jurkat cells
    • Meisner H., Conway B.R., Hartley D.et al. Interactions of Cbl with Grb-2 and phosphatidylinositol 3′-kinase in activated Jurkat cells. J Biol Chem. 15:1995;3571.
    • (1995) J Biol Chem , vol.15 , pp. 3571
    • Meisner, H.1    Conway, B.R.2    Hartley, D.3
  • 46
    • 0028932614 scopus 로고
    • The proto-oncogene product c-Cbl becomes tyrosine phosphorylated by stimulation with GM-CSF or Epo and constitutively binds to the SH3 domain of Grb2/Ash in human hematopoietic cells
    • Odai H., Sasaki K., Iwamatsu A.et al. The proto-oncogene product c-Cbl becomes tyrosine phosphorylated by stimulation with GM-CSF or Epo and constitutively binds to the SH3 domain of Grb2/Ash in human hematopoietic cells. J Biol Chem. 270:1995;10800.
    • (1995) J Biol Chem , vol.270 , pp. 10800
    • Odai, H.1    Sasaki, K.2    Iwamatsu, A.3
  • 47
    • 0028308576 scopus 로고
    • Physical association between Src homology 3 elements and the protein product of the c-cbl proto-oncogene
    • Rivero-Lezcano O.M., Sameshima J.H., Marcilla A.et al. Physical association between Src homology 3 elements and the protein product of the c-cbl proto-oncogene. J Biol Chem. 269:1994;17363.
    • (1994) J Biol Chem , vol.269 , pp. 17363
    • Rivero-Lezcano, O.M.1    Sameshima, J.H.2    Marcilla, A.3
  • 48
    • 0029671073 scopus 로고    scopus 로고
    • cbl is a major substrate of tyrosine phosphorylation upon B cell antigen receptor stimulation and interacts in vivo with Fyn and Syk tyrosine kinases, Grb2 and Shc adaptors, and the p85 subunit of phosphatidylinositol 3-kinase
    • cbl is a major substrate of tyrosine phosphorylation upon B cell antigen receptor stimulation and interacts in vivo with Fyn and Syk tyrosine kinases, Grb2 and Shc adaptors, and the p85 subunit of phosphatidylinositol 3-kinase. J Biol Chem. 271:1996;3187.
    • (1996) J Biol Chem , vol.271 , pp. 3187
    • Panchamoorthy, G.1    Fukazawa, T.2    Miyake, S.3
  • 49
    • 0025368594 scopus 로고
    • Genetic analysis of the Kirsten- ras-revertant 1 gene: Potentiation of its tumor suppressor activity by specific point mutations
    • Kitayama H., Matsuzaki T., Ikawa Y.et al. Genetic analysis of the Kirsten- ras-revertant 1 gene. potentiation of its tumor suppressor activity by specific point mutations Proc Natl Acad Sci U S A. 87:1990;4284.
    • (1990) Proc Natl Acad Sci U S a , vol.87 , pp. 4284
    • Kitayama, H.1    Matsuzaki, T.2    Ikawa, Y.3
  • 50
    • 0027170176 scopus 로고
    • RapV12 antagonizes Ras-dependent activation of ERK1 and ERK2 by LPA and EGF in Rat-1 fibroblasts
    • Cook S., Rubinfeld B., Albert I.et al. RapV12 antagonizes Ras-dependent activation of ERK1 and ERK2 by LPA and EGF in Rat-1 fibroblasts. EMBO J. 12:1993;3475.
    • (1993) EMBO J , vol.12 , pp. 3475
    • Cook, S.1    Rubinfeld, B.2    Albert, I.3
  • 51
    • 0031831487 scopus 로고    scopus 로고
    • Interferon α activates the tyrosine kinase Lyn in hematopoietic cells
    • Uddin S., Grumbach I., Yi T.et al. Interferon α activates the tyrosine kinase Lyn in hematopoietic cells. Br J Haematol. 101:1998;446.
    • (1998) Br J Haematol , vol.101 , pp. 446
    • Uddin, S.1    Grumbach, I.2    Yi, T.3


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