메뉴 건너뛰기




Volumn 63, Issue 19, 2003, Pages 6290-6298

The PCPH oncoprotein antagonizes the proapoptotic role of the mammalian target of rapamycin in the response of normal fibroblasts to ionizing radiation

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; CASPASE; CASPASE 3; DNA FRAGMENT; GENE PRODUCT; MAMMALIAN TARGET OF RAPAMYCIN; MESSENGER RNA; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; ONCOPROTEIN; PCPH PROTEIN; PROTEIN KINASE C; PROTEIN P53; TETRACYCLINE; UNCLASSIFIED DRUG;

EID: 0141885091     PISSN: 00085472     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (24)

References (64)
  • 1
    • 0032575752 scopus 로고    scopus 로고
    • Mitochondria and apoptosis
    • Green, D. R., and Reed, J. C. Mitochondria and apoptosis. Science (Wash. DC), 281: 1309-1312, 1998.
    • (1998) Science (Wash. DC) , vol.281 , pp. 1309-1312
    • Green, D.R.1    Reed, J.C.2
  • 2
    • 0034641963 scopus 로고    scopus 로고
    • Defying death after DNA damage
    • Rich, T., Allen, R. L., and Wyllie, A. H. Defying death after DNA damage. Nature (Lond.), 407: 777-783, 2000.
    • (2000) Nature (Lond.) , vol.407 , pp. 777-783
    • Rich, T.1    Allen, R.L.2    Wyllie, A.H.3
  • 3
    • 0035449355 scopus 로고    scopus 로고
    • Cell cycle checkpoint signaling through the ATM and ATR kinases
    • Abraham, R. T. Cell cycle checkpoint signaling through the ATM and ATR kinases. Genes Dev., 15: 2177-2196, 2001.
    • (2001) Genes Dev. , vol.15 , pp. 2177-2196
    • Abraham, R.T.1
  • 4
    • 0034003005 scopus 로고    scopus 로고
    • Stress signals utilize multiple pathways to stabilize p53
    • Ashcroft, M., Taya, Y., and Vousden, K. H. Stress signals utilize multiple pathways to stabilize p53. Mol. Cell. Biol., 20: 3224-3233, 2000.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 3224-3233
    • Ashcroft, M.1    Taya, Y.2    Vousden, K.H.3
  • 7
    • 0031833563 scopus 로고    scopus 로고
    • Mammalian target of rapamycin: Immunosuppressive drugs uncover a novel pathway of cytokine receptor signaling
    • Abraham, R. T. Mammalian target of rapamycin: immunosuppressive drugs uncover a novel pathway of cytokine receptor signaling. Curr. Opin. Immunol., 10: 330-336, 1998.
    • (1998) Curr. Opin. Immunol. , vol.10 , pp. 330-336
    • Abraham, R.T.1
  • 8
    • 0035887446 scopus 로고    scopus 로고
    • Human immunodeficiency virus 1 envelope glycoprotein complex-induced apoptosis involves mammalian target of rapamycin/FKBP12-rapamycin-associated protein-mediated p53 phosphorylation
    • Castedo, M., Ferri, K. F., Blanco, J., Roumier, T., Larochette, N., Barretina, J., Amendola, A., Nardacci, R., Mètivier, D., Este, J. A., Piacentini, M., and Kroemer, G. Human immunodeficiency virus 1 envelope glycoprotein complex-induced apoptosis involves mammalian target of rapamycin/FKBP12-rapamycin-associated protein-mediated p53 phosphorylation. J. Exp. Med., 194: 1097-1110, 2001.
    • (2001) J. Exp. Med. , vol.194 , pp. 1097-1110
    • Castedo, M.1    Ferri, K.F.2    Blanco, J.3    Roumier, T.4    Larochette, N.5    Barretina, J.6    Amendola, A.7    Nardacci, R.8    Mètivier, D.9    Este, J.A.10    Piacentini, M.11    Kroemer, G.12
  • 12
    • 0034659730 scopus 로고    scopus 로고
    • DNA-damaging agents cause inactivation of translational regulators linked to mTOR signalling
    • Tee, A. R., and Proud, C. G. DNA-damaging agents cause inactivation of translational regulators linked to mTOR signalling. Oncogene, 19: 3021-3031, 2000.
    • (2000) Oncogene , vol.19 , pp. 3021-3031
    • Tee, A.R.1    Proud, C.G.2
  • 13
    • 0036160679 scopus 로고    scopus 로고
    • Mammalian target of rapamycin (mTOR): Pro- and anti-apoptotic
    • Castedo, M., Ferri, K. F., and Kroemer, G. Mammalian target of rapamycin (mTOR): pro- and anti-apoptotic. Cell Death Differ., 9: 99-100, 2002.
    • (2002) Cell Death Differ. , vol.9 , pp. 99-100
    • Castedo, M.1    Ferri, K.F.2    Kroemer, G.3
  • 14
    • 0035859956 scopus 로고    scopus 로고
    • p70S6 kinase signals cell survival as well as growth, inactivating the pro-apoptotic molecule BAD
    • Harada, H., Andersen, J. S., Mann, M., Terada, N., and Korsmeyer, S. J. p70S6 kinase signals cell survival as well as growth, inactivating the pro-apoptotic molecule BAD. Proc. Natl. Acad. Sci. USA, 98: 9666-9670, 2001.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 9666-9670
    • Harada, H.1    Andersen, J.S.2    Mann, M.3    Terada, N.4    Korsmeyer, S.J.5
  • 15
    • 0037115523 scopus 로고    scopus 로고
    • Inhibition of the mammalian target of rapamycin sensitizes U87 xenografts to fractionated radiation therapy
    • Eshleman, J. S., Carlson, B. L., Mladek, A. C., Kastner, B. D., Shide, K. L., and Sarkaria, J. N. Inhibition of the mammalian target of rapamycin sensitizes U87 xenografts to fractionated radiation therapy. Cancer Res., 62: 7291-7297, 2002.
    • (2002) Cancer Res. , vol.62 , pp. 7291-7297
    • Eshleman, J.S.1    Carlson, B.L.2    Mladek, A.C.3    Kastner, B.D.4    Shide, K.L.5    Sarkaria, J.N.6
  • 16
    • 0028356525 scopus 로고
    • cph, a novel oncogene which cooperates with H-ras in the transformation of NIH/3T3 fibroblasts
    • Velasco, J. A., Castro, R., Avila, M. A., Laborda, J., DiPaolo, J. A., Cansado, J., and Notario, V. cph, a novel oncogene which cooperates with H-ras in the transformation of NIH/3T3 fibroblasts. Oncogene, 9: 2065-2069, 1994.
    • (1994) Oncogene , vol.9 , pp. 2065-2069
    • Velasco, J.A.1    Castro, R.2    Avila, M.A.3    Laborda, J.4    DiPaolo, J.A.5    Cansado, J.6    Notario, V.7
  • 17
    • 0029997831 scopus 로고    scopus 로고
    • Tissue-specific expression, evolutionary conservation and localization of the cph proto-oncogene on Syrian hamster chromosome X
    • Velasco, J. A., Zimonjic, D. B., Popescu, N. C., Cansado, J., DiPaolo, J. A., Albor, A., and Notario, V. Tissue-specific expression, evolutionary conservation and localization of the cph proto-oncogene on Syrian hamster chromosome X. Oncogene, 12: 2713-2717, 1996.
    • (1996) Oncogene , vol.12 , pp. 2713-2717
    • Velasco, J.A.1    Zimonjic, D.B.2    Popescu, N.C.3    Cansado, J.4    DiPaolo, J.A.5    Albor, A.6    Notario, V.7
  • 18
    • 0036920051 scopus 로고    scopus 로고
    • Gradual deregulation and loss of PCPH expression in the progression of human laryngeal ncoplasia
    • Blánquez, M. J., Regadera, J., Mariño, J., Newman, R. E., and Notario, V. Gradual deregulation and loss of PCPH expression in the progression of human laryngeal ncoplasia. Mol. Carcinog., 35: 186-195, 2002.
    • (2002) Mol. Carcinog. , vol.35 , pp. 186-195
    • Blánquez, M.J.1    Regadera, J.2    Mariño, J.3    Newman, R.E.4    Notario, V.5
  • 19
    • 0035219013 scopus 로고    scopus 로고
    • Expression of the protein product of the PCPH proto-oncogene in human tumor cell lines
    • Rouzaut, A., Recio, J. A., and Notario, V. Expression of the protein product of the PCPH proto-oncogene in human tumor cell lines. Radiat. Res., 155: 181-187, 2001.
    • (2001) Radiat. Res. , vol.155 , pp. 181-187
    • Rouzaut, A.1    Recio, J.A.2    Notario, V.3
  • 20
    • 0036217514 scopus 로고    scopus 로고
    • Deregulated expression of the PCPH proto-oncogene in rat mammary tumors induced with 7,12-dimethylbenz(a)anthracene
    • Solanas, M., Escrich, E., Rouzaut, A., Costa, I., and Notario, V. Deregulated expression of the PCPH proto-oncogene in rat mammary tumors induced with 7,12-dimethylbenz(a)anthracene. Mol. Carcinog., 33: 219-227, 2002.
    • (2002) Mol. Carcinog. , vol.33 , pp. 219-227
    • Solanas, M.1    Escrich, E.2    Rouzaut, A.3    Costa, I.4    Notario, V.5
  • 21
    • 0036570081 scopus 로고    scopus 로고
    • Partial depletion of intracellular ATP mediates the stress-survival function of the PCPH oncoprotein
    • Recio, J. A., Páez, J. G., Sanders, S., Kawakami, T., and Notario, V. Partial depletion of intracellular ATP mediates the stress-survival function of the PCPH oncoprotein. Cancer Res., 62: 2690-2694, 2002.
    • (2002) Cancer Res. , vol.62 , pp. 2690-2694
    • Recio, J.A.1    Páez, J.G.2    Sanders, S.3    Kawakami, T.4    Notario, V.5
  • 22
    • 0033590633 scopus 로고    scopus 로고
    • The product of the cph oncogene is a truncated, nucleotide binding protein that enhances cellular survival to stress
    • Velasco, J. A., Avila, M. A., and Notario, V. The product of the cph oncogene is a truncated, nucleotide binding protein that enhances cellular survival to stress. Oncogene, 18: 689-701, 1999.
    • (1999) Oncogene , vol.18 , pp. 689-701
    • Velasco, J.A.1    Avila, M.A.2    Notario, V.3
  • 23
    • 0035656529 scopus 로고    scopus 로고
    • Identity between the PCPH proto-oncogene and the CD39L4 (ENTPD5) ectonucleoside triphosphate diphosphohydrolase gene
    • Páez, J. G., Recio, J. A., Rouzaut, A., and Notario, V. Identity between the PCPH proto-oncogene and the CD39L4 (ENTPD5) ectonucleoside triphosphate diphosphohydrolase gene. Int. J. Oncol., 19: 1249-1254, 2001.
    • (2001) Int. J. Oncol. , vol.19 , pp. 1249-1254
    • Páez, J.G.1    Recio, J.A.2    Rouzaut, A.3    Notario, V.4
  • 24
    • 0028711861 scopus 로고
    • Poly(ADP-ribose) polymerase in HeLa cells - A high resolution two-dimensional gel analysis
    • Prasad, S., Notario, V., Sharareh, S., and Dritschilo, A. Poly(ADP-ribose) polymerase in HeLa cells-a high resolution two-dimensional gel analysis. Appl. Theor. Electrophoresis, 4: 3-10, 1994.
    • (1994) Appl. Theor. Electrophoresis , vol.4 , pp. 3-10
    • Prasad, S.1    Notario, V.2    Sharareh, S.3    Dritschilo, A.4
  • 25
    • 0002569886 scopus 로고
    • Dye exclusion tests for cell viability
    • P. F. Kruse and M. K. Patterson (eds.). New York: Academic Press
    • Phillips, H. J. Dye exclusion tests for cell viability. In: P. F. Kruse and M. K. Patterson (eds.), Tissue Culture. Methods and Applications, pp. 406-408. New York: Academic Press, 1973.
    • (1973) Tissue Culture. Methods and Applications , pp. 406-408
    • Phillips, H.J.1
  • 26
    • 0034635168 scopus 로고    scopus 로고
    • Substitution of His59 converts CD39 apyrase into an ADPase in a quaternary structure dependent manner
    • Grinthal, A., and Guidotti, G. Substitution of His59 converts CD39 apyrase into an ADPase in a quaternary structure dependent manner. Biochemistry, 39: 9-16, 2000.
    • (2000) Biochemistry , vol.39 , pp. 9-16
    • Grinthal, A.1    Guidotti, G.2
  • 27
    • 0035810654 scopus 로고    scopus 로고
    • The importance of histidine residues in human ecto-nucleoside triphosphate diphosphohydrolase-3 as determined by site-directed mutagenesis
    • Hicks-Berger, C. A., Yang, F., Smith, T. M., and Kirley, T. L. The importance of histidine residues in human ecto-nucleoside triphosphate diphosphohydrolase-3 as determined by site-directed mutagenesis. Biochim. Biophys. Acta, 1547: 72-81, 2001.
    • (2001) Biochim. Biophys. Acta , vol.1547 , pp. 72-81
    • Hicks-Berger, C.A.1    Yang, F.2    Smith, T.M.3    Kirley, T.L.4
  • 29
    • 0040736282 scopus 로고    scopus 로고
    • Mutagenesis of two conserved tryptophan residues of the E-type ATPases: Inactivation and conversion of an ectoapyrase to an ecto-NTPase
    • Smith, T. M., Lewis Carl, S. A., and Kirley, T. L. Mutagenesis of two conserved tryptophan residues of the E-type ATPases: inactivation and conversion of an ectoapyrase to an ecto-NTPase. Biochemistry, 38: 5849-5857, 1999.
    • (1999) Biochemistry , vol.38 , pp. 5849-5857
    • Smith, T.M.1    Lewis Carl, S.A.2    Kirley, T.L.3
  • 30
    • 0033524467 scopus 로고    scopus 로고
    • Site-directed mutagenesis of a human brain ectoapyrase: Evidence that the E-type ATPases are related to the actin/heat shock 70/sugar kinase superfamily
    • Smith, T. M., and Kirley, T. L. Site-directed mutagenesis of a human brain ectoapyrase: evidence that the E-type ATPases are related to the actin/heat shock 70/sugar kinase superfamily. Biochemistry, 38: 321-328, 1999.
    • (1999) Biochemistry , vol.38 , pp. 321-328
    • Smith, T.M.1    Kirley, T.L.2
  • 31
    • 0035799316 scopus 로고    scopus 로고
    • Site-directed mutagenesis of human nucleoside triphosphate diphosphohydrolase 3: The importance of residues in the apyrase conserved regions
    • Yang, F., Hicks-Berger, C. A., Smith, T. M., and Kirley, T. L. Site-directed mutagenesis of human nucleoside triphosphate diphosphohydrolase 3: the importance of residues in the apyrase conserved regions. Biochemistry, 40: 3943-3950, 2001.
    • (2001) Biochemistry , vol.40 , pp. 3943-3950
    • Yang, F.1    Hicks-Berger, C.A.2    Smith, T.M.3    Kirley, T.L.4
  • 32
    • 0034128655 scopus 로고    scopus 로고
    • Biological response to ionizing radiation in mouse embryo fibroblasts with a targeted disruption of the DNA polymerase β gene
    • Miura, M., Watanabe, H., Okochi, K., Sasaki, T., and Shibuya, H. Biological response to ionizing radiation in mouse embryo fibroblasts with a targeted disruption of the DNA polymerase β gene. Radiat. Res., 153: 773-780, 2000.
    • (2000) Radiat. Res. , vol.153 , pp. 773-780
    • Miura, M.1    Watanabe, H.2    Okochi, K.3    Sasaki, T.4    Shibuya, H.5
  • 33
    • 0034234924 scopus 로고    scopus 로고
    • A direct linkage between the phosphoinositide 3-kinase-AKT signaling pathway and the mammalian target of rapamycin in mitogen-stimulated and transformed cells
    • Sekulif, A., Hudson, C. C., Homme, J. L., Yin, P., Otterness, D. M., Karnitz, L. M., and Abraham, R. T. A direct linkage between the phosphoinositide 3-kinase-AKT signaling pathway and the mammalian target of rapamycin in mitogen-stimulated and transformed cells. Cancer Res., 60: 3504-3513, 2000.
    • (2000) Cancer Res. , vol.60 , pp. 3504-3513
    • Sekulif, A.1    Hudson, C.C.2    Homme, J.L.3    Yin, P.4    Otterness, D.M.5    Karnitz, L.M.6    Abraham, R.T.7
  • 34
    • 0034687688 scopus 로고    scopus 로고
    • Cytoplasmic-nuclear shuttling of FKBP12-rapamycin-associated protein is involved in rapamycin-sensitive signaling and translation initiation
    • Kim, J. E., and Chen, J. Cytoplasmic-nuclear shuttling of FKBP12-rapamycin-associated protein is involved in rapamycin-sensitive signaling and translation initiation. Proc. Natl. Acad. Sci. USA, 97: 14340-14345, 2000.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 14340-14345
    • Kim, J.E.1    Chen, J.2
  • 35
    • 0037007014 scopus 로고    scopus 로고
    • FKBP12-rapamycin-associated protein associates with mitochondria and senses osmotic stress via mitochondrial dysfunction
    • Desai, B. N., Myers, B. R., and Schreiber, S. L. FKBP12-rapamycin-associated protein associates with mitochondria and senses osmotic stress via mitochondrial dysfunction. Proc. Natl. Acad. Sci. U S A, 99: 4319-4324, 2002.
    • (2002) Proc. Natl. Acad. Sci. U S A , vol.99 , pp. 4319-4324
    • Desai, B.N.1    Myers, B.R.2    Schreiber, S.L.3
  • 36
    • 0037008730 scopus 로고    scopus 로고
    • Predominant nuclear localization of mammalian target of rapamycin in normal and malignant cells in culture
    • Zhang, X., Shu, L., Hosoi, H., Murti, K. G., and Houghton, P. J. Predominant nuclear localization of mammalian target of rapamycin in normal and malignant cells in culture. J. Biol. Chem., 277: 28127-28134, 2002.
    • (2002) J. Biol. Chem. , vol.277 , pp. 28127-28134
    • Zhang, X.1    Shu, L.2    Hosoi, H.3    Murti, K.G.4    Houghton, P.J.5
  • 38
    • 15844391440 scopus 로고    scopus 로고
    • Mechanism of action of the immunosuppressant rapamycin
    • Dumont, F. J., and Su, Q. Mechanism of action of the immunosuppressant rapamycin. Life Sci., 58: 373-395, 1996.
    • (1996) Life Sci. , vol.58 , pp. 373-395
    • Dumont, F.J.1    Su, Q.2
  • 39
    • 0031298259 scopus 로고    scopus 로고
    • Cleavage of poly(ADP-ribose) polymerase: A sensitive parameter to study cell death
    • Duriez, P. J., and Shah, G. M. Cleavage of poly(ADP-ribose) polymerase: a sensitive parameter to study cell death. Biochem. Cell Biol., 75: 337-349, 1997.
    • (1997) Biochem. Cell Biol. , vol.75 , pp. 337-349
    • Duriez, P.J.1    Shah, G.M.2
  • 40
    • 0034942907 scopus 로고    scopus 로고
    • Crucial role of calpain in hypoxic PC12 cell death: Calpain, but not caspases, mediates degradation of cytoskeletal and proteins and protein kinase C-α 32 and -δ
    • Yamakawa, H., Banno, Y., Nakashima, S., Yoshimura, S., Sawada, M., Nishimura, Y., Nozawa, Y., and Sakai, N. Crucial role of calpain in hypoxic PC12 cell death: calpain, but not caspases, mediates degradation of cytoskeletal proteins and protein kinase C-α 32 and -δ. Neurol. Res., 23: 522-530, 2001.
    • (2001) Neurol. Res. , vol.23 , pp. 522-530
    • Yamakawa, H.1    Banno, Y.2    Nakashima, S.3    Yoshimura, S.4    Sawada, M.5    Nishimura, Y.6    Nozawa, Y.7    Sakai, N.8
  • 41
    • 0034710870 scopus 로고    scopus 로고
    • Phosphorylation of murine p53 at ser-18 regulates the p53 responses to DNA damage
    • Chao, C., Saito, S., Anderson, C. W., Appella, E., and Xu, Y. Phosphorylation of murine p53 at ser-18 regulates the p53 responses to DNA damage. Proc. Natl. Acad. Sci. USA, 97: 11936-11941, 2000.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 11936-11941
    • Chao, C.1    Saito, S.2    Anderson, C.W.3    Appella, E.4    Xu, Y.5
  • 42
    • 0033381054 scopus 로고    scopus 로고
    • Regulation and activation of p53 and its family members
    • Lohrun, M. A. E., and Vousden, K. H. Regulation and activation of p53 and its family members. Cell Death Differ., 6: 1162-1168, 1999.
    • (1999) Cell Death Differ. , vol.6 , pp. 1162-1168
    • Lohrun, M.A.E.1    Vousden, K.H.2
  • 43
    • 0034665461 scopus 로고    scopus 로고
    • p53 transcriptional activity is essential for p53-dependent apoptosis following DNA damage
    • Chao, C., Saito, S., Kang, J., Anderson, C. W., Appella, E., and Xu, Y. p53 transcriptional activity is essential for p53-dependent apoptosis following DNA damage. EMBO J., 19: 4967-4975, 2000.
    • (2000) EMBO J. , vol.19 , pp. 4967-4975
    • Chao, C.1    Saito, S.2    Kang, J.3    Anderson, C.W.4    Appella, E.5    Xu, Y.6
  • 45
    • 0035265686 scopus 로고    scopus 로고
    • PUMA, a novel proapoptotic gene, is induced by p53
    • Nakano, K., and Vousden, K. H. PUMA, a novel proapoptotic gene, is induced by p53. Mol. Cell, 7: 683-694, 2001.
    • (2001) Mol. Cell , vol.7 , pp. 683-694
    • Nakano, K.1    Vousden, K.H.2
  • 48
    • 0035265823 scopus 로고    scopus 로고
    • PUMA induces the rapid apoptosis of colorectal cancer cells
    • Yu, J., Zhang, L., Hwang, P. M., Kinzler, K. W., and Vogelstein, B. PUMA induces the rapid apoptosis of colorectal cancer cells. Mol. Cell., 7: 673-682, 2001.
    • (2001) Mol. Cell. , vol.7 , pp. 673-682
    • Yu, J.1    Zhang, L.2    Hwang, P.M.3    Kinzler, K.W.4    Vogelstein, B.5
  • 49
    • 0028883179 scopus 로고
    • Tumor suppressor p53 is a direct transcriptional activator of the human bax gene
    • Miyashita, T., and Reed, J. C. Tumor suppressor p53 is a direct transcriptional activator of the human bax gene. Cell, 80: 293-299, 1995.
    • (1995) Cell , vol.80 , pp. 293-299
    • Miyashita, T.1    Reed, J.C.2
  • 50
    • 0033635733 scopus 로고    scopus 로고
    • BH3-only proteins-essential initiators of apoptotic cell death
    • Huang, D. C. S., and Strasser, A. BH3-only proteins-essential initiators of apoptotic cell death. Cell, 103: 839-842, 2000.
    • (2000) Cell , vol.103 , pp. 839-842
    • Huang, D.C.S.1    Strasser, A.2
  • 51
    • 0034629291 scopus 로고    scopus 로고
    • p53 induces apoptosis by caspase activation through mitochondrial cytochrome c release
    • Schuler, M., Bossy-Wetzel, E., Goldstein, J. C., Fitzgerald, P., and Green, D. R. p53 induces apoptosis by caspase activation through mitochondrial cytochrome c release. J. Biol. Chem., 275: 7337-7342, 2000.
    • (2000) J. Biol. Chem. , vol.275 , pp. 7337-7342
    • Schuler, M.1    Bossy-Wetzel, E.2    Goldstein, J.C.3    Fitzgerald, P.4    Green, D.R.5
  • 52
    • 0037452759 scopus 로고    scopus 로고
    • PUMA mediates the apoptotic response to p53 in colorectal cancer cells
    • Yu, J., Wang, Z., Kinzler, K. W., Vogelstein, B., and Zhang, L. PUMA mediates the apoptotic response to p53 in colorectal cancer cells. Proc. Natl. Acad. Sci. USA, 100: 1931-1936, 2003.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 1931-1936
    • Yu, J.1    Wang, Z.2    Kinzler, K.W.3    Vogelstein, B.4    Zhang, L.5
  • 54
    • 0026720075 scopus 로고
    • Tight control of gene expression in mammalian cells by tetracycline-responsive promoters
    • Gossen, M., and Bujard, H. Tight control of gene expression in mammalian cells by tetracycline-responsive promoters. Proc. Natl. Acad. Sci. USA, 89: 5547-5551, 1992.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 5547-5551
    • Gossen, M.1    Bujard, H.2
  • 56
    • 0037097863 scopus 로고    scopus 로고
    • Mammalian cell size is controlled by mTOR and its downstream targets S6K1 and 4EBP1/eIF4E
    • Fingar, D. C., Salama, S., Tsou, C., Harlow, E., and Blenis, J. Mammalian cell size is controlled by mTOR and its downstream targets S6K1 and 4EBP1/eIF4E. Genes Dev., 16: 1472-1487, 2002.
    • (2002) Genes Dev. , vol.16 , pp. 1472-1487
    • Fingar, D.C.1    Salama, S.2    Tsou, C.3    Harlow, E.4    Blenis, J.5
  • 58
    • 0343293958 scopus 로고    scopus 로고
    • Both normal and transforming PCPH proteins have guanosine diphosphatase activity, but only the oncoprotein co-operates with Ras in activating extmcellular signal-regulated kinase ERKI
    • Recio, J. A., Páez, J. G., Maskeri, B., Loveland, M., Velasco, J. A., and Notario, V. Both normal and transforming PCPH proteins have guanosine diphosphatase activity, but only the oncoprotein co-operates with Ras in activating extmcellular signal-regulated kinase ERKI. Cancer Res., 60: 1720-1728, 2000.
    • (2000) Cancer Res. , vol.60 , pp. 1720-1728
    • Recio, J.A.1    Páez, J.G.2    Maskeri, B.3    Loveland, M.4    Velasco, J.A.5    Notario, V.6
  • 59
    • 0036776168 scopus 로고    scopus 로고
    • A novel pathway regulating the mammalian target of rapamycin (mTOR) signaling
    • Chen, J., and Fang, Y. A novel pathway regulating the mammalian target of rapamycin (mTOR) signaling. Biochem. Pharmacol., 64: 1071-1077, 2002.
    • (2002) Biochem. Pharmacol. , vol.64 , pp. 1071-1077
    • Chen, J.1    Fang, Y.2
  • 61
    • 0027361047 scopus 로고
    • Activation of phospholipase D: Alternative signal transduction pathway responsive to γ-radiation
    • Avila, M. A., Otero, G., Cansado, J., Dritschilo, A., Velasco, J. A., and Notario, V. Activation of phospholipase D: alternative signal transduction pathway responsive to γ-radiation. Cancer Res., 53: 4474-4476, 1993.
    • (1993) Cancer Res. , vol.53 , pp. 4474-4476
    • Avila, M.A.1    Otero, G.2    Cansado, J.3    Dritschilo, A.4    Velasco, J.A.5    Notario, V.6
  • 62
    • 0035996703 scopus 로고    scopus 로고
    • Isolation and characterization of a 66-kDa protein from rat liver plasma membrane with RhoA-stimulated phospholipase D activity
    • Dunkirk, S. G., Wallert, M. A., Baumgartner, M. L., and Provost, J. J. Isolation and characterization of a 66-kDa protein from rat liver plasma membrane with RhoA-stimulated phospholipase D activity. Protein Expr. Purif., 24: 1-12, 2002.
    • (2002) Protein Expr. Purif. , vol.24 , pp. 1-12
    • Dunkirk, S.G.1    Wallert, M.A.2    Baumgartner, M.L.3    Provost, J.J.4
  • 63
    • 0012177733 scopus 로고    scopus 로고
    • Cyclotherapy: Protection of normal cells and unshielding of cancer cells
    • Blagosklonny, M. V., and Darzynkiewicz, Z. Cyclotherapy: protection of normal cells and unshielding of cancer cells. Cell Cycle, 1: 375-382, 2002.
    • (2002) Cell Cycle , vol.1 , pp. 375-382
    • Blagosklonny, M.V.1    Darzynkiewicz, Z.2
  • 64
    • 0034722888 scopus 로고    scopus 로고
    • The rapamycin-sensitive signal transduction pathway as a target for cancer therapy
    • Hidalgo, M., and Rowinsky, E. K. The rapamycin-sensitive signal transduction pathway as a target for cancer therapy. Oncogene, 19: 6680-6686, 2000.
    • (2000) Oncogene , vol.19 , pp. 6680-6686
    • Hidalgo, M.1    Rowinsky, E.K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.