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Volumn 11, Issue 6, 2000, Pages 279-292

Oncogenic transformation of cells by a conditionally active form of the protein kinase Akt/PKB

Author keywords

[No Author keywords available]

Indexed keywords

2 (2 AMINO 3 METHOXYPHENYL)CHROMONE; AGAROSE; CYCLIN DEPENDENT KINASE 2; CYCLIN DEPENDENT KINASE INHIBITOR; MITOGEN ACTIVATED PROTEIN KINASE; PROTEIN KINASE B; PROTEIN P27; PROTEIN SERINE THREONINE KINASE;

EID: 0033919237     PISSN: 10449523     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (73)

References (103)
  • 1
    • 0023408333 scopus 로고
    • Multiple mRNA species code for the catalytic subunit of the cAMP-dependent protein kinase from LLC-PK1 cells. Evidence for two forms of the catalytic subunit
    • Adavani, S. R., Schwarz, M., Showers, M. O., Maurer, R. A., and Hemmings, B. A. Multiple mRNA species code for the catalytic subunit of the cAMP-dependent protein kinase from LLC-PK1 cells. Evidence for two forms of the catalytic subunit. Eur. J. Biochem., 167: 221-226, 1987.
    • (1987) Eur. J. Biochem. , vol.167 , pp. 221-226
    • Adavani, S.R.1    Schwarz, M.2    Showers, M.O.3    Maurer, R.A.4    Hemmings, B.A.5
  • 2
    • 0025882091 scopus 로고
    • Molecular cloning and identification of a serine/threonine protein kinase of the second-messenger subfamily
    • Jones, P. F., Jakubowicz, T., Pitossi, F. J., Maurer, F., and Hemmings, B. A. Molecular cloning and identification of a serine/threonine protein kinase of the second-messenger subfamily. Proc. Natl. Acad. Sci. USA, 88: 4171-4175, 1991.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 4171-4175
    • Jones, P.F.1    Jakubowicz, T.2    Pitossi, F.J.3    Maurer, F.4    Hemmings, B.A.5
  • 3
    • 0026006501 scopus 로고
    • Molecular cloning and characterisation of a novel putative protein-serine kinase related to the cAMP-dependent and protein kinase C families
    • Coffer, P. J., and Woodgett, J. R. Molecular cloning and characterisation of a novel putative protein-serine kinase related to the cAMP-dependent and protein kinase C families. Eur. J. Biochem., 207: 475-481, 1991.
    • (1991) Eur. J. Biochem. , vol.207 , pp. 475-481
    • Coffer, P.J.1    Woodgett, J.R.2
  • 4
    • 0026095665 scopus 로고
    • A retroviral oncogene, akt, encoding a serine-threonine kinase containing an SH2-like region
    • Bellacosa, A., Testa, J. R., Staal, S. P., and Tsichlis, P. N. A retroviral oncogene, akt, encoding a serine-threonine kinase containing an SH2-like region. Science (Washington DC), 254: 274-277, 1991.
    • (1991) Science (Washington DC) , vol.254 , pp. 274-277
    • Bellacosa, A.1    Testa, J.R.2    Staal, S.P.3    Tsichlis, P.N.4
  • 5
    • 0001582482 scopus 로고
    • Molecular cloning of the akt oncogene and its human homologues AKT1 and AKT2: Amplification of AKT1 in a primary human gastric adenocarcinoma
    • Staal, S. P. Molecular cloning of the akt oncogene and its human homologues AKT1 and AKT2: amplification of AKT1 in a primary human gastric adenocarcinoma. Proc. Natl. Acad. Sci. USA, 84: 5034-5037, 1987.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 5034-5037
    • Staal, S.P.1
  • 6
    • 0023945139 scopus 로고
    • Thymic lymphoma induction by the AKT8 murine retrovirus
    • Staal, S. P., and Hartley, J. W. Thymic lymphoma induction by the AKT8 murine retrovirus. J. Exp. Med., 167: 1259-1264, 1988.
    • (1988) J. Exp. Med. , vol.167 , pp. 1259-1264
    • Staal, S.P.1    Hartley, J.W.2
  • 7
    • 0017647580 scopus 로고
    • Isolation of transforming murine leukemia viruses from mice with a high incidence of spontaneous lymphoma
    • Staal, S. P., Hartley, J. W., and Rowe, W. P. Isolation of transforming murine leukemia viruses from mice with a high incidence of spontaneous lymphoma. Proc. Natl. Acad. Sci. USA, 74: 3065-3067, 1977.
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 3065-3067
    • Staal, S.P.1    Hartley, J.W.2    Rowe, W.P.3
  • 8
    • 0027242129 scopus 로고
    • The proteins encoded by c-akt and v-akt differ in post-translational modification, subcellular localization and oncogenic potential
    • Ahmed, N. N., Franke, T. F., Bellacosa, A., Datta, K., Gonzalez-Portal, M. E., Taguchi, T., Testa, J. R., and Tsichlis, P. N. The proteins encoded by c-akt and v-akt differ in post-translational modification, subcellular localization and oncogenic potential. Oncogene, 8: 1957-1963, 1993.
    • (1993) Oncogene , vol.8 , pp. 1957-1963
    • Ahmed, N.N.1    Franke, T.F.2    Bellacosa, A.3    Datta, K.4    Gonzalez-Portal, M.E.5    Taguchi, T.6    Testa, J.R.7    Tsichlis, P.N.8
  • 9
    • 0026270993 scopus 로고
    • Molecular cloning of a second form of rac protein kinase
    • Jones, P. F., Jakubowicz, T., and Hemmings, B. A. Molecular cloning of a second form of rac protein kinase. Cell Regul., 2: 1001-1009, 1991.
    • (1991) Cell Regul. , vol.2 , pp. 1001-1009
    • Jones, P.F.1    Jakubowicz, T.2    Hemmings, B.A.3
  • 10
    • 0028799420 scopus 로고
    • Molecular cloning and characterization of a new member of the RAC protein kinase family: Association of the pleckstrin homology domain of three types of RAC protein kinase with protein kinase C subspecies and βγ subunits of G proteins
    • Konishi, H., Kuroda, S., Tanaka, M., Matsuzaki, H., Ono, Y., Kameyama, K., Haga, T., and Kikkawa, U. Molecular cloning and characterization of a new member of the RAC protein kinase family: association of the pleckstrin homology domain of three types of RAC protein kinase with protein kinase C subspecies and βγ subunits of G proteins. Biochem. Biophys. Res. Commun., 216: 526-534, 1995.
    • (1995) Biochem. Biophys. Res. Commun. , vol.216 , pp. 526-534
    • Konishi, H.1    Kuroda, S.2    Tanaka, M.3    Matsuzaki, H.4    Ono, Y.5    Kameyama, K.6    Haga, T.7    Kikkawa, U.8
  • 11
    • 0029079275 scopus 로고
    • The protein kinase encoded by the Akt proto-oncogene is a target of the PDGF-activated phosphatidylinositol 3-kinase
    • Franke, T. F., Yang, S. I., Chan, T. O., Datta, K., Kazlauskas, A., Morrison, D. K., Kaplan, D. R., and Tsichlis, P. N. The protein kinase encoded by the Akt proto-oncogene is a target of the PDGF-activated phosphatidylinositol 3-kinase. Cell, 81: 727-736, 1995.
    • (1995) Cell , vol.81 , pp. 727-736
    • Franke, T.F.1    Yang, S.I.2    Chan, T.O.3    Datta, K.4    Kazlauskas, A.5    Morrison, D.K.6    Kaplan, D.R.7    Tsichlis, P.N.8
  • 12
    • 0029160069 scopus 로고
    • Protein kinase B (c-Akt) in phosphatidylinositol-3-OH kinase signal transduction
    • Burgering, B. M., and Coffer, P. J. Protein kinase B (c-Akt) in phosphatidylinositol-3-OH kinase signal transduction. Nature (Lond.), 376: 599-602, 1995.
    • (1995) Nature (Lond.) , vol.376 , pp. 599-602
    • Burgering, B.M.1    Coffer, P.J.2
  • 13
    • 0031039024 scopus 로고    scopus 로고
    • Direct regulation of the Akt proto-oncogene product by phosphatidylinositol-3,4-bisphosphate
    • Franke, T. F., Kaplan, D. R., Cantley, L C., and Toker, A. Direct regulation of the Akt proto-oncogene product by phosphatidylinositol-3,4-bisphosphate. Science (Washington DC), 275: 665-668, 1997.
    • (1997) Science (Washington DC) , vol.275 , pp. 665-668
    • Franke, T.F.1    Kaplan, D.R.2    Cantley, L.C.3    Toker, A.4
  • 14
    • 0029143388 scopus 로고
    • Insulin stimulates the kinase activity of RAC-PK, a pleckstrin homology domain containing ser/thr kinase
    • Kohn, A. D., Kovacina, K. S., and Roth, R. A. Insulin stimulates the kinase activity of RAC-PK, a pleckstrin homology domain containing ser/thr kinase. EMBO J., 14: 4288-4295, 1995.
    • (1995) EMBO J. , vol.14 , pp. 4288-4295
    • Kohn, A.D.1    Kovacina, K.S.2    Roth, R.A.3
  • 15
    • 0031469453 scopus 로고    scopus 로고
    • Membrane translocation and activation of the Akt kinase in growth factor-stimulated hematopoietic cells
    • Testa, J. R., and Bellacosa, A. Membrane translocation and activation of the Akt kinase in growth factor-stimulated hematopoietic cells. Leuk. Res., 21: 1027-1031, 1997.
    • (1997) Leuk. Res. , vol.21 , pp. 1027-1031
    • Testa, J.R.1    Bellacosa, A.2
  • 17
    • 0029942186 scopus 로고    scopus 로고
    • Activation and phosphorylation of a pleckstrin homology domain containing protein kinase (RAC-PK/PKB) promoted by serum and protein phosphatase inhibitors
    • Andjelkovic, M., Jakubowicz, T., Cron, P., Ming, X. F., Han, J. W., and Hemmings, B. A. Activation and phosphorylation of a pleckstrin homology domain containing protein kinase (RAC-PK/PKB) promoted by serum and protein phosphatase inhibitors. Proc. Natl. Acad. Sci. USA, 93: 5699-5704, 1996.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 5699-5704
    • Andjelkovic, M.1    Jakubowicz, T.2    Cron, P.3    Ming, X.F.4    Han, J.W.5    Hemmings, B.A.6
  • 18
    • 0031127305 scopus 로고    scopus 로고
    • Characterization of a 3-phosphoinositide-dependent protein kinase which phosphorylates and activates protein kinase Bα
    • Alessi, D. R., James, S. R., Downes, C. P., Holmes, A. B., Gaffney, P. R., Reese, C. B., and Cohen, P. Characterization of a 3-phosphoinositide-dependent protein kinase which phosphorylates and activates protein kinase Bα. Curr. Biol., 7: 261-269, 1997.
    • (1997) Curr. Biol. , vol.7 , pp. 261-269
    • Alessi, D.R.1    James, S.R.2    Downes, C.P.3    Holmes, A.B.4    Gaffney, P.R.5    Reese, C.B.6    Cohen, P.7
  • 19
    • 0029810181 scopus 로고    scopus 로고
    • Akt, a pleckstrin homology domain containing kinase, is activated primarily by phosphorylation
    • Kohn, A. D., Takeuchi, F., and Roth, R. A. Akt, a pleckstrin homology domain containing kinase, is activated primarily by phosphorylation. J. Biol. Chem., 271: 21920-21926, 1996.
    • (1996) J. Biol. Chem. , vol.271 , pp. 21920-21926
    • Kohn, A.D.1    Takeuchi, F.2    Roth, R.A.3
  • 20
    • 0032529189 scopus 로고    scopus 로고
    • Caenorhabditis elegans Akt/PKB transduces insulin receptor-like signals from AGE-1 PI3 kinase to the DAF-16 transcription factor
    • Paradis, S., and Ruvkun, G. Caenorhabditis elegans Akt/PKB transduces insulin receptor-like signals from AGE-1 PI3 kinase to the DAF-16 transcription factor. Genes Dev., 12: 2488-2498, 1998.
    • (1998) Genes Dev. , vol.12 , pp. 2488-2498
    • Paradis, S.1    Ruvkun, G.2
  • 21
    • 0029587224 scopus 로고
    • Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase
    • Cross, D. A., Alessi, D. R., Cohen, P., Andjelkovich, M., and Hemmings, B. A. Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B. Nature (Lond.), 378: 785-789, 1995.
    • (1995) B. Nature (Lond.) , vol.378 , pp. 785-789
    • Cross, D.A.1    Alessi, D.R.2    Cohen, P.3    Andjelkovich, M.4    Hemmings, B.A.5
  • 22
    • 0031782480 scopus 로고    scopus 로고
    • Constitutive activation of protein kinase Bα by membrane targeting promotes glucose and system A amino acid transport, protein synthesis, and inactivation of glycogen synthase kinase 3 in L6 muscle cells
    • Hajduch, E., Alessi, D. R., Hemmings, B. A., and Hundal, H. S. Constitutive activation of protein kinase Bα by membrane targeting promotes glucose and system A amino acid transport, protein synthesis, and inactivation of glycogen synthase kinase 3 in L6 muscle cells. Diabetes, 47: 1006-1013, 1998.
    • (1998) Diabetes , vol.47 , pp. 1006-1013
    • Hajduch, E.1    Alessi, D.R.2    Hemmings, B.A.3    Hundal, H.S.4
  • 23
    • 0032557646 scopus 로고    scopus 로고
    • Essential role for protein kinase B (PKB) in insulin-induced glycogen synthase kinase 3 inactivation. Characterization of dominant-negative mutant of PKB
    • van Weeren, P. C., de Bruyn, K. M., de Vries-Smits, A. M., van Lint, J., and Burgering, B. M. Essential role for protein kinase B (PKB) in insulin-induced glycogen synthase kinase 3 inactivation. Characterization of dominant-negative mutant of PKB. J. Biol. Chem., 273: 13150-13156, 1998.
    • (1998) J. Biol. Chem. , vol.273 , pp. 13150-13156
    • Van Weeren, P.C.1    De Bruyn, K.M.2    De Vries-Smits, A.M.3    Van Lint, J.4    Burgering, B.M.5
  • 24
    • 0029908016 scopus 로고    scopus 로고
    • Expression of a constitutively active Akt Ser/Thr kinase in 3T3-L1 adipocytes stimulates glucose uptake and glucose transporter 4 translocation
    • Kohn, A. D., Summers, S. A., Birnbaum, M. J., and Roth, R. A. Expression of a constitutively active Akt Ser/Thr kinase in 3T3-L1 adipocytes stimulates glucose uptake and glucose transporter 4 translocation. J. Biol. Chem., 271: 31372-31378, 1996.
    • (1996) J. Biol. Chem. , vol.271 , pp. 31372-31378
    • Kohn, A.D.1    Summers, S.A.2    Birnbaum, M.J.3    Roth, R.A.4
  • 25
    • 0030806305 scopus 로고    scopus 로고
    • Activation of translation initiation factor eIF2B by insulin requires phosphatktyl inosrtol 3-kinase
    • Welsh, G. I., Stokes, C. M., Wang, X., Sakaue, H., Ogawa, W., Kasuga, M., and Proud, C. G. Activation of translation initiation factor eIF2B by insulin requires phosphatktyl inosrtol 3-kinase. FEBS Lett., 410: 418-422, 1997.
    • (1997) FEBS Lett. , vol.410 , pp. 418-422
    • Welsh, G.I.1    Stokes, C.M.2    Wang, X.3    Sakaue, H.4    Ogawa, W.5    Kasuga, M.6    Proud, C.G.7
  • 26
    • 0032520009 scopus 로고    scopus 로고
    • 4E-BP1, a repressor of mRNA translation, is phosphorylated and inactivated by the Akt(PKB) signaling pathway
    • Gingras, A. C., Kennedy, S. G., O'Leary, M. A., Sonenberg, N., and Hay, N. 4E-BP1, a repressor of mRNA translation, is phosphorylated and inactivated by the Akt(PKB) signaling pathway. Genes Dev., 12: 502-513, 1998.
    • (1998) Genes Dev. , vol.12 , pp. 502-513
    • Gingras, A.C.1    Kennedy, S.G.2    O'Leary, M.A.3    Sonenberg, N.4    Hay, N.5
  • 28
    • 0030884103 scopus 로고    scopus 로고
    • PKB/Akt: Connecting phosphoinositide 3-kinase to cell survival and beyond
    • Marte, B. M., and Downward, J. PKB/Akt: connecting phosphoinositide 3-kinase to cell survival and beyond. Trends Biochem. Sci., 22: 355-358, 1997.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 355-358
    • Marte, B.M.1    Downward, J.2
  • 29
    • 0031913246 scopus 로고    scopus 로고
    • Mechanism of activation and function of protein kinase B
    • Alessi, D. R., and Cohen, P. Mechanism of activation and function of protein kinase B. Curr. Opin. Genet. Dev., 8: 55-62, 1998.
    • (1998) Curr. Opin. Genet. Dev. , vol.8 , pp. 55-62
    • Alessi, D.R.1    Cohen, P.2
  • 30
    • 0032053709 scopus 로고    scopus 로고
    • Mechanisms and consequences of activation of protein kinase B/Akt
    • Downward, J. Mechanisms and consequences of activation of protein kinase B/Akt. Curr. Opin. Cell Biol., 10: 262-267, 1998.
    • (1998) Curr. Opin. Cell Biol. , vol.10 , pp. 262-267
    • Downward, J.1
  • 32
    • 0028963084 scopus 로고
    • Requirement for phosphatidylinositol-3 kinase in the prevention of apoptosis by nerve growth factor
    • Yao, R., and Cooper, G. M. Requirement for phosphatidylinositol-3 kinase in the prevention of apoptosis by nerve growth factor. Science (Washington DC), 267: 2003-2006, 1995.
    • (1995) Science (Washington DC) , vol.267 , pp. 2003-2006
    • Yao, R.1    Cooper, G.M.2
  • 33
    • 0031923788 scopus 로고    scopus 로고
    • Akt, a target of phosphatidylinositol 3-kinase, inhibits apoptosis in a differentiating neuronal cell line
    • Eves, E. M., Xiong, W., Bellacosa, A., Kennedy, S. G., Tsichlis, P. N., Rosner, M. R., and Hay, N. Akt, a target of phosphatidylinositol 3-kinase, inhibits apoptosis in a differentiating neuronal cell line. Mol. Cell. Biol., 18: 2143-2152, 1998.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 2143-2152
    • Eves, E.M.1    Xiong, W.2    Bellacosa, A.3    Kennedy, S.G.4    Tsichlis, P.N.5    Rosner, M.R.6    Hay, N.7
  • 34
    • 0030702123 scopus 로고    scopus 로고
    • Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery
    • Datta, S. R., Dudek, H., Tao, X., Masters, S., Fu, H., Gotoh, Y., and Greenberg, M. E. Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery. Cell, 91: 231-241, 1997.
    • (1997) Cell , vol.91 , pp. 231-241
    • Datta, S.R.1    Dudek, H.2    Tao, X.3    Masters, S.4    Fu, H.5    Gotoh, Y.6    Greenberg, M.E.7
  • 37
    • 0030892234 scopus 로고    scopus 로고
    • Apoptosis by death factor
    • Nagata, S. Apoptosis by death factor. Cell, 88: 355-365, 1997.
    • (1997) Cell , vol.88 , pp. 355-365
    • Nagata, S.1
  • 40
    • 0039058167 scopus 로고    scopus 로고
    • Protection of CD95-mediated apoptosis by activation of phosphatidylinositide 3-kinase and protein kinase B
    • Hausler, P., Papoff, G., Eramo, A., Reif, K., Cantrell, D. A., and Ruberti, G. Protection of CD95-mediated apoptosis by activation of phosphatidylinositide 3-kinase and protein kinase B. Eur. J. Immunol., 28: 57-69, 1998.
    • (1998) Eur. J. Immunol. , vol.28 , pp. 57-69
    • Hausler, P.1    Papoff, G.2    Eramo, A.3    Reif, K.4    Cantrell, D.A.5    Ruberti, G.6
  • 41
    • 0026667730 scopus 로고
    • AKT2, a putative oncogene encoding a member of a subfamily of protein-serine/threonine kinases, is amplified in human ovarian carcinomas
    • Cheng, J. Q., Godwin, A. K., Bellacosa, A., Taguchi, T., Franke, T. F., Hamilton, T. C., Tsichlis, P. N., and Testa, J. R. AKT2, a putative oncogene encoding a member of a subfamily of protein-serine/threonine kinases, is amplified in human ovarian carcinomas. Proc. Natl. Acad. Sci. USA, 89: 9267-9271, 1992.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 9267-9271
    • Cheng, J.Q.1    Godwin, A.K.2    Bellacosa, A.3    Taguchi, T.4    Franke, T.F.5    Hamilton, T.C.6    Tsichlis, P.N.7    Testa, J.R.8
  • 42
    • 0001457668 scopus 로고    scopus 로고
    • Amplification of AKT2 in human pancreatic cells and inhibition of AKT2 expression and tumorigenicity by antisense RNA
    • Cheng, J. Q., Ruggeri, B., Klein, W. M., Sonoda, G., Altomare, D. A., Watson, D. K., and Testa, J. R. Amplification of AKT2 in human pancreatic cells and inhibition of AKT2 expression and tumorigenicity by antisense RNA. Proc. Natl. Acad. Sci. USA, 93: 3636-3641, 1996.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 3636-3641
    • Cheng, J.Q.1    Ruggeri, B.2    Klein, W.M.3    Sonoda, G.4    Altomare, D.A.5    Watson, D.K.6    Testa, J.R.7
  • 43
    • 0032527913 scopus 로고    scopus 로고
    • AKT2, a member of the protein kinase B family, is activated by growth factors, v-Ha-ras, and v-src through phosphatidylinositol 3-kinase in human ovarian epithelial cancer cells
    • Liu, A. X., Testa, J. R., Hamilton, T. C., Jove, R., Nicosia, S. V., and Cheng, J. Q. AKT2, a member of the protein kinase B family, is activated by growth factors, v-Ha-ras, and v-src through phosphatidylinositol 3-kinase in human ovarian epithelial cancer cells. Cancer Res., 58: 2973-2977, 1998.
    • (1998) Cancer Res. , vol.58 , pp. 2973-2977
    • Liu, A.X.1    Testa, J.R.2    Hamilton, T.C.3    Jove, R.4    Nicosia, S.V.5    Cheng, J.Q.6
  • 45
    • 0027385030 scopus 로고
    • Conditional transformation of cells and rapid activation of the mitogen-activated protein kinase cascade by an estradiol-dependent human raf-1 protein kinase
    • Samuels, M. L., Weber, M. J., Bishop, J. M., and McMahon, M. Conditional transformation of cells and rapid activation of the mitogen-activated protein kinase cascade by an estradiol-dependent human raf-1 protein kinase. Mol. Cell. Biol., 13: 6241-6252, 1993.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 6241-6252
    • Samuels, M.L.1    Weber, M.J.2    Bishop, J.M.3    McMahon, M.4
  • 46
    • 0032951523 scopus 로고    scopus 로고
    • Complementation of defective csf-1 receptor signaling and mitogenesis by Raf and v-src
    • Aziz, N., Cherwinski, H., and McMahon, M. Complementation of defective csf-1 receptor signaling and mitogenesis by Raf and v-src. Mol. Cell. Biol., 19: 1101-1115, 1999.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 1101-1115
    • Aziz, N.1    Cherwinski, H.2    McMahon, M.3
  • 47
    • 0029002136 scopus 로고
    • A modified oestrogen receptor ligand-binding domain as an improved switch for the regulation of heterologous proteins
    • Littlewood, T. D., Hancock, D. C., Danielian, P. S., Parker, M. G., and Evan, G. I. A modified oestrogen receptor ligand-binding domain as an improved switch for the regulation of heterologous proteins. Nucleic Acids Res., 23: 1686-1690, 1995.
    • (1995) Nucleic Acids Res. , vol.23 , pp. 1686-1690
    • Littlewood, T.D.1    Hancock, D.C.2    Danielian, P.S.3    Parker, M.G.4    Evan, G.I.5
  • 51
    • 0028909645 scopus 로고
    • Human cyclin E, a nuclear protein essential for the G1-to-S phase transition
    • Ohtsubo, M., Theodoras, A. M., Schumacher, J., Roberts, J. M., and Pagano, M. Human cyclin E, a nuclear protein essential for the G1-to-S phase transition. Mol. Cell. Biol., 15: 2612-2624, 1995.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 2612-2624
    • Ohtsubo, M.1    Theodoras, A.M.2    Schumacher, J.3    Roberts, J.M.4    Pagano, M.5
  • 53
    • 0028179669 scopus 로고
    • p27Kip1, a cyclin-Cdk inhibitor, links transforming growth factor-β and contact inhibition to cell cycle arrest
    • Polyak, K., Kato, J. Y., Solomon, M. J., Sherr, C. J., Massagué, J., Roberts, J. M., and Koff, A. p27Kip1, a cyclin-Cdk inhibitor, links transforming growth factor-β and contact inhibition to cell cycle arrest. Genes Dev., 8: 9-22, 1994.
    • (1994) Genes Dev. , vol.8 , pp. 9-22
    • Polyak, K.1    Kato, J.Y.2    Solomon, M.J.3    Sherr, C.J.4    Massagué, J.5    Roberts, J.M.6    Koff, A.7
  • 56
    • 0030010591 scopus 로고    scopus 로고
    • Mice lacking p27(Kip1) display increased body size, multiple organ hyperplasia, retinal dysplasia, and pituitary tumors
    • Nakayama, K., Ishida, N., Shirane, M., Inomata, A., Inoue, T., Shishido, N., Horii, I., and Loh, D. Y. Mice lacking p27(Kip1) display increased body size, multiple organ hyperplasia, retinal dysplasia, and pituitary tumors. Cell, 85: 707-720, 1996.
    • (1996) Cell , vol.85 , pp. 707-720
    • Nakayama, K.1    Ishida, N.2    Shirane, M.3    Inomata, A.4    Inoue, T.5    Shishido, N.6    Horii, I.7    Loh, D.Y.8
  • 57
    • 0032431028 scopus 로고    scopus 로고
    • PTEN/MMAC1/TEP1 suppresses the tumorigenicity and induces G1 cell cycle arrest in human glioblastoma cells
    • Li, D. M., and Sun, H. PTEN/MMAC1/TEP1 suppresses the tumorigenicity and induces G1 cell cycle arrest in human glioblastoma cells. Proc. Natl. Acad. Sci. USA, 95: 15406-15411, 1998.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 15406-15411
    • Li, D.M.1    Sun, H.2
  • 58
    • 0033974001 scopus 로고    scopus 로고
    • The p21WAF1/CIP1 promoter is methylated in Rat-1 cells: Stable restoration of p53-dependent p21WAF1/CIP1 expression after transfection of a genomic clone containing ihep21WAF1/CIP1 gene
    • Allan, L. A., Duhig, T., Read, M., and Fried, M. The p21WAF1/CIP1 promoter is methylated in Rat-1 cells: stable restoration of p53-dependent p21WAF1/CIP1 expression after transfection of a genomic clone containing ihep21WAF1/CIP1 gene. Mol. Cell. Biol., 20: 1291-1298, 2000.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 1291-1298
    • Allan, L.A.1    Duhig, T.2    Read, M.3    Fried, M.4
  • 59
    • 0032563207 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinase induces scattering and tubulogenesis in epithelial cells through a novel pathway
    • Khwaja, A., Lehmann, K., Marte, B. M., and Downward, J. Phosphoinositide 3-kinase induces scattering and tubulogenesis in epithelial cells through a novel pathway. J. Biol. Chem., 273: 18793-18801, 1998.
    • (1998) J. Biol. Chem. , vol.273 , pp. 18793-18801
    • Khwaja, A.1    Lehmann, K.2    Marte, B.M.3    Downward, J.4
  • 60
    • 0030785701 scopus 로고    scopus 로고
    • Activation of protein kinase B (Akt/RAC-protein kinase) by cellular stress and its association with heat shock protein Hsp27
    • Konishi, H., Matsuzaki, H., Tanaka, M., Takemura, Y., Kuroda, S., Ono, Y., and Kikkawa, U. Activation of protein kinase B (Akt/RAC-protein kinase) by cellular stress and its association with heat shock protein Hsp27. FEBS Lett., 410: 493-498, 1997.
    • (1997) FEBS Lett. , vol.410 , pp. 493-498
    • Konishi, H.1    Matsuzaki, H.2    Tanaka, M.3    Takemura, Y.4    Kuroda, S.5    Ono, Y.6    Kikkawa, U.7
  • 61
    • 0030992837 scopus 로고    scopus 로고
    • Signalling through the lipid products of phosphoinositide-3-OH kinase
    • Toker, A., and Cantley, L. C. Signalling through the lipid products of phosphoinositide-3-OH kinase. Nature (Lond.), 387: 673-676, 1997.
    • (1997) Nature (Lond.) , vol.387 , pp. 673-676
    • Toker, A.1    Cantley, L.C.2
  • 62
    • 0032533225 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3β regulates cyclin D1 proteolysis and subcellular localization
    • Diehl, J. A., Cheng, M., Roussel, M. F., and Sherr, C. J. Glycogen synthase kinase-3β regulates cyclin D1 proteolysis and subcellular localization. Genes Dev., 12: 3499-3511, 1998.
    • (1998) Genes Dev. , vol.12 , pp. 3499-3511
    • Diehl, J.A.1    Cheng, M.2    Roussel, M.F.3    Sherr, C.J.4
  • 63
    • 0032959647 scopus 로고    scopus 로고
    • Activated MEK stimulates expression of AP-1 components independently of phosphotidylinositol 3-kinase (PI3-kinase) but requires a PI3-kinase signal to stimulate DNA synthesis
    • Treinies, I., Paterson, H. F., Hooper, S., Wilson, R., and Marshall, C. J. Activated MEK stimulates expression of AP-1 components independently of phosphotidylinositol 3-kinase (PI3-kinase) but requires a PI3-kinase signal to stimulate DNA synthesis. Mol. Cell. Biol., 19: 321-329, 1999.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 321-329
    • Treinies, I.1    Paterson, H.F.2    Hooper, S.3    Wilson, R.4    Marshall, C.J.5
  • 66
    • 0030860466 scopus 로고    scopus 로고
    • Transforming activity and mitosis-related expression of the AKT2 oncogene: Evidence suggesting a link between cell cycle regulation and oncogenesis
    • Cheng, J. Q., Altomare, D. A., Klein, M. A., Lee, W. C., Kruh, G. D., Lissy, N. A., and Testa, J. R. Transforming activity and mitosis-related expression of the AKT2 oncogene: evidence suggesting a link between cell cycle regulation and oncogenesis. Oncogene, 14: 2793-2801, 1997.
    • (1997) Oncogene , vol.14 , pp. 2793-2801
    • Cheng, J.Q.1    Altomare, D.A.2    Klein, M.A.3    Lee, W.C.4    Kruh, G.D.5    Lissy, N.A.6    Testa, J.R.7
  • 68
    • 0031708412 scopus 로고    scopus 로고
    • Activation of phosphatidylinositol 3-kinase is sufficient for cell cycle entry and promotes cellular changes characteristic of oncogenic transformation
    • Klippel, A., Escombedo, M., Wachowicz, M. S., Apell, G., Brown, T. W., Giedlin, M. A., Kavanaugh, W. M., and Williams, L. T. Activation of phosphatidylinositol 3-kinase is sufficient for cell cycle entry and promotes cellular changes characteristic of oncogenic transformation. Mol. Cell. Biol., 18: 5699-5711, 1998.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 5699-5711
    • Klippel, A.1    Escombedo, M.2    Wachowicz, M.S.3    Apell, G.4    Brown, T.W.5    Giedlin, M.A.6    Kavanaugh, W.M.7    Williams, L.T.8
  • 69
    • 0032558822 scopus 로고    scopus 로고
    • Protein kinase B (PKB/Akt) activity is elevated in glioblastoma cells due to mutations of the tumor suppressor PTEN/MMAC
    • Haas-Kogan, D., Shalev, N., Wong, M., Mills, G., Yount, G., and Stokoe, D. Protein kinase B (PKB/Akt) activity is elevated in glioblastoma cells due to mutations of the tumor suppressor PTEN/MMAC. Curr. Biol., 8: 1195-1198, 1998.
    • (1998) Curr. Biol. , vol.8 , pp. 1195-1198
    • Haas-Kogan, D.1    Shalev, N.2    Wong, M.3    Mills, G.4    Yount, G.5    Stokoe, D.6
  • 73
    • 0032410285 scopus 로고    scopus 로고
    • Cip/Kip cyclin-dependent kinase inhibitors: Brakes of the cell cycle engine during development
    • Nakayama, K. Cip/Kip cyclin-dependent kinase inhibitors: brakes of the cell cycle engine during development. Bioessays, 20: 1020-1029, 1998.
    • (1998) Bioessays , vol.20 , pp. 1020-1029
    • Nakayama, K.1
  • 75
    • 0032561075 scopus 로고    scopus 로고
    • Reduced p27Kip1 expression in hepatocellular carcinomas
    • Hui, A. M., Sun, L., Kanai, Y., Sakamoto, M., and Hirohashi, S. Reduced p27Kip1 expression in hepatocellular carcinomas. Cancer Lett., 132: 67-73, 1998.
    • (1998) Cancer Lett. , vol.132 , pp. 67-73
    • Hui, A.M.1    Sun, L.2    Kanai, Y.3    Sakamoto, M.4    Hirohashi, S.5
  • 77
    • 0032902972 scopus 로고    scopus 로고
    • Cyclin-dependent kinase inhibitor p27Kip1 expression and interaction with other cell cycle-associated proteins in mammary carcinoma
    • Gillett, C. E., Smith, P., Peters, G., Lu, X., and Barnes, D. M. Cyclin-dependent kinase inhibitor p27Kip1 expression and interaction with other cell cycle-associated proteins in mammary carcinoma. J. Pathol., 187: 200-206, 1999.
    • (1999) J. Pathol. , vol.187 , pp. 200-206
    • Gillett, C.E.1    Smith, P.2    Peters, G.3    Lu, X.4    Barnes, D.M.5
  • 78
    • 0031883583 scopus 로고    scopus 로고
    • Reduced levels of the cell-cycle inhibitor p27Kip1 in epithelial dysplasia and carcinoma of the oral cavity
    • Jordan, R. C., Bradley, G., and Slingerland, J. Reduced levels of the cell-cycle inhibitor p27Kip1 in epithelial dysplasia and carcinoma of the oral cavity. Am. J. Pathol., 152: 585-590, 1998.
    • (1998) Am. J. Pathol. , vol.152 , pp. 585-590
    • Jordan, R.C.1    Bradley, G.2    Slingerland, J.3
  • 80
    • 0033558373 scopus 로고    scopus 로고
    • Loss of p27Kip1 expression independently predicts poor prognosis for patients with resectable pancreatic adenocarcinoma
    • Lu, C. D., Morita, S., Ishibashi, T., Hara, H., Isozaki, H., and Tanigawa, N. Loss of p27Kip1 expression independently predicts poor prognosis for patients with resectable pancreatic adenocarcinoma. Cancer (Phila.), 85: 1250-1260, 1999.
    • (1999) Cancer (Phila.) , vol.85 , pp. 1250-1260
    • Lu, C.D.1    Morita, S.2    Ishibashi, T.3    Hara, H.4    Isozaki, H.5    Tanigawa, N.6
  • 82
    • 0033083047 scopus 로고    scopus 로고
    • Reduced expression of the cell cycle inhibitor p27Kip1 in non-small cell lung carcinoma: A prognostic factor independent of Ras
    • Catzavelos, C., Tsao, M. S., DeBoer, G., Bhattacharya, N., Shepherd, F. A., and Slingerland, J. M. Reduced expression of the cell cycle inhibitor p27Kip1 in non-small cell lung carcinoma: a prognostic factor independent of Ras. Cancer Res., 59: 684-688, 1999.
    • (1999) Cancer Res. , vol.59 , pp. 684-688
    • Catzavelos, C.1    Tsao, M.S.2    DeBoer, G.3    Bhattacharya, N.4    Shepherd, F.A.5    Slingerland, J.M.6
  • 83
    • 0032129273 scopus 로고    scopus 로고
    • Overexpression of p27Kip1 inhibits the growth of both normal and transformed human mammary epithelial cells
    • Sgambato, A., Zhang, Y. J., Ciaparrone, M., Soh, J. W., Cittadini, A., Santella, R. M., and Weinstein, I. B. Overexpression of p27Kip1 inhibits the growth of both normal and transformed human mammary epithelial cells. Cancer Res., 58: 3448-3454, 1998.
    • (1998) Cancer Res. , vol.58 , pp. 3448-3454
    • Sgambato, A.1    Zhang, Y.J.2    Ciaparrone, M.3    Soh, J.W.4    Cittadini, A.5    Santella, R.M.6    Weinstein, I.B.7
  • 84
    • 0033563157 scopus 로고    scopus 로고
    • Adenovirus-mediated gene transfer of MMAC1/PTEN to glioblastoma cells inhibits S phase entry by the recruitment of p27Kip1 into cyclin E/CDK2 complexes
    • Cheney, I. W., Neuteboom, S. T., Vaillancourt, M. T., Ramachandra, M., and Bookstein, R. Adenovirus-mediated gene transfer of MMAC1/PTEN to glioblastoma cells inhibits S phase entry by the recruitment of p27Kip1 into cyclin E/CDK2 complexes. Cancer Res., 59: 2318-2323, 1999.
    • (1999) Cancer Res. , vol.59 , pp. 2318-2323
    • Cheney, I.W.1    Neuteboom, S.T.2    Vaillancourt, M.T.3    Ramachandra, M.4    Bookstein, R.5
  • 85
    • 13044305289 scopus 로고    scopus 로고
    • PTEN modulates cell cycle progression and cell survival by regulating phosphatidylinositol 3,4,5-triphosphate and Akt/protein kinase B signaling pathway
    • Sun, H., Lesche, R., Li, D. M., Liliental, J., Zhang, H., Gao, J., Gavrilova, N., Mueller, B., Liu, X., and Wu, H. PTEN modulates cell cycle progression and cell survival by regulating phosphatidylinositol 3,4,5-triphosphate and Akt/protein kinase B signaling pathway. Proc. Natl. Acad. Sci. USA, 96: 6199-6204, 1999.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 6199-6204
    • Sun, H.1    Lesche, R.2    Li, D.M.3    Liliental, J.4    Zhang, H.5    Gao, J.6    Gavrilova, N.7    Mueller, B.8    Liu, X.9    Wu, H.10
  • 86
    • 0033135878 scopus 로고    scopus 로고
    • Ubiquitination of p27 is regulated by Cdk-dependent phosphorylation and trimeric complex formation
    • Montagnoli, A., Fiore, F., Eytan, E., Carrano, A. C., Draetta, G. F., Hershko, A., and Pagano, M. Ubiquitination of p27 is regulated by Cdk-dependent phosphorylation and trimeric complex formation. Genes Dev., 13: 1181-1189, 1999.
    • (1999) Genes Dev. , vol.13 , pp. 1181-1189
    • Montagnoli, A.1    Fiore, F.2    Eytan, E.3    Carrano, A.C.4    Draetta, G.F.5    Hershko, A.6    Pagano, M.7
  • 87
    • 0027978816 scopus 로고
    • The inhibition of glycogen synthase kinase-3 by insulin or insulin-like growth factor 1 in the rat skeletal muscle cell line L6 is blocked by wortmannin, but not by rapamycin: Evidence that wortmannin blocks activation of the mitogen-activated protein kinase pathway in L6 cells between Ras and Raf
    • Cross, D. A., Alessi, D. R., Vandenheede, J. R., McDowell, H. E., Hundal, H. S., and Cohen, P. The inhibition of glycogen synthase kinase-3 by insulin or insulin-like growth factor 1 in the rat skeletal muscle cell line L6 is blocked by wortmannin, but not by rapamycin: evidence that wortmannin blocks activation of the mitogen-activated protein kinase pathway in L6 cells between Ras and Raf. Biochem. J., 303 (Part 1): 21-26, 1994.
    • (1994) Biochem. J. , vol.303 , Issue.PART 1 , pp. 21-26
    • Cross, D.A.1    Alessi, D.R.2    Vandenheede, J.R.3    McDowell, H.E.4    Hundal, H.S.5    Cohen, P.6
  • 88
    • 0030786202 scopus 로고    scopus 로고
    • Conditional inhibition of the mitogen-activated protein kinase cascade by wortmannin. Dependence on signal strength
    • Duckworth, B. C., and Cantley, L. C. Conditional inhibition of the mitogen-activated protein kinase cascade by wortmannin. Dependence on signal strength. J. Biol. Chem., 272: 27665-27670, 1997.
    • (1997) J. Biol. Chem. , vol.272 , pp. 27665-27670
    • Duckworth, B.C.1    Cantley, L.C.2
  • 89
    • 0031398848 scopus 로고    scopus 로고
    • Granulocyte-macrophage colony-stimulating factor and IL-5 activate mitogen-activated protein kinase through Jak2 kinase and phosphatidylinositol 3-kinase in human eosinophils
    • Hiraguri, M., Miike, S., Sano, H., Kurasawa, K., Saito, Y., and Iwamoto, I. Granulocyte-macrophage colony-stimulating factor and IL-5 activate mitogen-activated protein kinase through Jak2 kinase and phosphatidylinositol 3-kinase in human eosinophils. J. Allergy Clin, Immunol., 100: S45-S51, 1997.
    • (1997) J. Allergy Clin, Immunol. , vol.100
    • Hiraguri, M.1    Miike, S.2    Sano, H.3    Kurasawa, K.4    Saito, Y.5    Iwamoto, I.6
  • 90
    • 0029039957 scopus 로고
    • Interleukin-2 triggers a novel phosphatidylinositol 3-kinase-dependent MEK activation pathway
    • Karnitz, L. M., Burns, L A., Sutor, S. L., Blenis, J., and Abraham, R. T. Interleukin-2 triggers a novel phosphatidylinositol 3-kinase-dependent MEK activation pathway. Mol. Cell. Biol., 15: 3049-3057, 1995.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 3049-3057
    • Karnitz, L.M.1    Burns, L.A.2    Sutor, S.L.3    Blenis, J.4    Abraham, R.T.5
  • 91
    • 0029872617 scopus 로고    scopus 로고
    • Requirement for phosphoinositide 3-OH kinase in growth hormone signalling to the mitogen-activated protein kinase and p70s6k pathways
    • Kilgour, E., Gout, I., and Anderson, N. G. Requirement for phosphoinositide 3-OH kinase in growth hormone signalling to the mitogen-activated protein kinase and p70s6k pathways. Biochem. J., 315 (Part 2): 517-522, 1996.
    • (1996) Biochem. J. , vol.315 , Issue.PART 2 , pp. 517-522
    • Kilgour, E.1    Gout, I.2    Anderson, N.G.3
  • 92
    • 15444341547 scopus 로고    scopus 로고
    • Differential activation of mitogen-activated protein kinase by insulin and epidermal growth factor in 3T3-L1 adipocytes: A possible involvement of PI3-kinase in the activation of the MAP kinase by insulin
    • Suga, J., Yoshimasa, Y., Yamada, K., Yamamoto, Y., Inoue, G., Okamoto, M., Hayashi, T., Shigemoto, M., Kosaki, A., Kuzuya, H., and Nakao, K. Differential activation of mitogen-activated protein kinase by insulin and epidermal growth factor in 3T3-L1 adipocytes: a possible involvement of PI3-kinase in the activation of the MAP kinase by insulin. Diabetes, 46: 735-741, 1997.
    • (1997) Diabetes , vol.46 , pp. 735-741
    • Suga, J.1    Yoshimasa, Y.2    Yamada, K.3    Yamamoto, Y.4    Inoue, G.5    Okamoto, M.6    Hayashi, T.7    Shigemoto, M.8    Kosaki, A.9    Kuzuya, H.10    Nakao, K.11
  • 93
    • 0027991899 scopus 로고
    • Wortmannin inhibits the effects of insulin and serum on the activities of glycogen synthase kinase-3 and mitogen-activated protein kinase
    • Welsh, G. I., Foulstone, E. J., Young, S. W., Tavare, J. M., and Proud, C. G. Wortmannin inhibits the effects of insulin and serum on the activities of glycogen synthase kinase-3 and mitogen-activated protein kinase. Biochem. J., 303 (Part 1): 15-20, 1994.
    • (1994) Biochem. J. , vol.303 , Issue.PART 1 , pp. 15-20
    • Welsh, G.I.1    Foulstone, E.J.2    Young, S.W.3    Tavare, J.M.4    Proud, C.G.5
  • 94
    • 0030839766 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase is required for integrin-stimulated AKT and Raf-1/mitogen-activated protein kinase pathway activation
    • King, W. G., Mattaliano, M. D., Chan, T. O., Tsichlis, P. N., and Brugge, J. S. Phosphatidylinositol 3-kinase is required for integrin-stimulated AKT and Raf-1/mitogen-activated protein kinase pathway activation. Mol. Cell. Biol., 17: 4406-4418, 1997.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 4406-4418
    • King, W.G.1    Mattaliano, M.D.2    Chan, T.O.3    Tsichlis, P.N.4    Brugge, J.S.5
  • 95
    • 0033607633 scopus 로고    scopus 로고
    • Phosphorylation and regulation of Raf by Akt (protein kinase B)
    • Zimmermann, S. M. K. Phosphorylation and regulation of Raf by Akt (protein kinase B). Science (Washington DC), 286: 1741-1744, 1999.
    • (1999) Science (Washington DC) , vol.286 , pp. 1741-1744
    • Zimmermann, S.M.K.1
  • 97
    • 0033618410 scopus 로고    scopus 로고
    • Multiple Ras effector pathways contribute to G1 cell cycle progression
    • Gille, H., and Downward, J. Multiple Ras effector pathways contribute to G1 cell cycle progression. J. Biol. Chem., 274: 22033-22040, 1999.
    • (1999) J. Biol. Chem. , vol.274 , pp. 22033-22040
    • Gille, H.1    Downward, J.2
  • 98
    • 0030871667 scopus 로고    scopus 로고
    • High-intensity Raf signal causes cell cycle arrest mediated by p21Cip1
    • Sewing, A., Wiseman, B., Lloyd, A. C., and Land, H. High-intensity Raf signal causes cell cycle arrest mediated by p21Cip1. Mol. Cell. Biol., 17: 5588-5597, 1997.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 5588-5597
    • Sewing, A.1    Wiseman, B.2    Lloyd, A.C.3    Land, H.4
  • 99
    • 0030835430 scopus 로고    scopus 로고
    • Raf-induced proliferation or cell cycle arrest is determined by the level of Raf activity with arrest mediated by p21Cip1
    • Woods, D., Parry, D., Cherwinski, H., Bosch, E., Lees, E., and McMahon, M. Raf-induced proliferation or cell cycle arrest is determined by the level of Raf activity with arrest mediated by p21Cip1. Mol. Cell. Biol., 17: 5598-5611, 1997.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 5598-5611
    • Woods, D.1    Parry, D.2    Cherwinski, H.3    Bosch, E.4    Lees, E.5    McMahon, M.6
  • 100
    • 0027236954 scopus 로고
    • Production of high-titer helper-free retroviruses by transient transfection
    • Pear, W. S., Nolan, G. P., Scott, M. L., and Baltimore, D. Production of high-titer helper-free retroviruses by transient transfection. Proc. Natl. Acad. Sci. USA, 90: 8392-8396, 1993.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 8392-8396
    • Pear, W.S.1    Nolan, G.P.2    Scott, M.L.3    Baltimore, D.4
  • 101
    • 0022185452 scopus 로고
    • Cytochemistry for bromodeoxyuridine/DNA analysis: Stoichiometry and sensitivity
    • Dolbeare, F., Beisker, W., Pallavicini, M. G., Vanderlaan, M., and Gray, J. W. Cytochemistry for bromodeoxyuridine/DNA analysis: stoichiometry and sensitivity. Cytometry, 6: 521-530, 1985.
    • (1985) Cytometry , vol.6 , pp. 521-530
    • Dolbeare, F.1    Beisker, W.2    Pallavicini, M.G.3    Vanderlaan, M.4    Gray, J.W.5
  • 103
    • 0029043888 scopus 로고
    • A novel assay for apoptosis. Flow cytometric detection of phosphatidylserine expression on early apoptotic cells using fluorescein labelled Annexin V
    • Vermes, I., Haanen, C., Steffens-Nakken, H., and Reutelingsperger, C. A novel assay for apoptosis. Flow cytometric detection of phosphatidylserine expression on early apoptotic cells using fluorescein labelled Annexin V. J. Immunol. Methods, 184: 39-51, 1995.
    • (1995) J. Immunol. Methods , vol.184 , pp. 39-51
    • Vermes, I.1    Haanen, C.2    Steffens-Nakken, H.3    Reutelingsperger, C.4


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