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Volumn 2011, Issue , 2011, Pages

P53: The attractive tumor suppressor in the cancer research field

Author keywords

[No Author keywords available]

Indexed keywords

CISPLATIN; CYTOCHROME C; DNA; GROWTH ARREST AND DNA DAMAGE INDUCIBLE PROTEIN 45; HOMEODOMAIN INTERACTING PROTEIN KINASE 2; I KAPPA B KINASE ALPHA; PROTEIN BAX; PROTEIN BCL 2; PROTEIN KINASE C DELTA; PROTEIN MDM2; PROTEIN NOXA; PROTEIN P53; PROTEIN P63; PROTEIN P73; PUMA PROTEIN; SUMO 1 PROTEIN; TRANSCRIPTION FACTOR RUNX1; TRANSCRIPTION FACTOR RUNX2; TRANSCRIPTION FACTOR RUNX3;

EID: 79251534367     PISSN: 11107243     EISSN: 11107251     Source Type: Journal    
DOI: 10.1155/2011/603925     Document Type: Review
Times cited : (102)

References (161)
  • 2
    • 0018769971 scopus 로고
    • Simian virus 40-transformed cells express new species of proteins precipitable by anti-simian virus 40 tumor serum
    • Kress M., May E., Cassingena R., May P., Simian virus 40-transformed cells express new species of proteins precipitable by anti-simian virus 40 tumor serum Journal of Virology 1979 31 2 472 483
    • (1979) Journal of Virology , vol.31 , Issue.2 , pp. 472-483
    • Kress, M.1    May, E.2    Cassingena, R.3    May, P.4
  • 3
    • 0018348655 scopus 로고
    • T antigen is bound to a host protein in SV40 transformed cells
    • Lane D. P., Crawford L. V., T antigen is bound to a host protein in SV40 transformed cells Nature 1979 278 5701 261 263
    • (1979) Nature , vol.278 , Issue.5701 , pp. 261-263
    • Lane, D.P.1    Crawford, L.V.2
  • 4
    • 0018760324 scopus 로고
    • Characterization of a 54K dalton cellular SV40 tumor antigen present in SV40 transformed cells and uninfected embryonal carcinoma cells
    • Linzer D. I. H., Levine A. J., Characterization of a 54K dalton cellular SV40 tumor antigen present in SV40 transformed cells and uninfected embryonal carcinoma cells Cell 1979 17 1 43 52
    • (1979) Cell , vol.17 , Issue.1 , pp. 43-52
    • Linzer, D.I.H.1    Levine, A.J.2
  • 5
    • 0018348936 scopus 로고
    • Identification of new polypeptide species (4855K) immunoprecipitable by antiserum to purified large T antigen and present in SV40-infected and -transformed cells
    • Melero J. A., Stitt D. T., Mangel W. F., Carroll R. B., Identification of new polypeptide species (4855K) immunoprecipitable by antiserum to purified large T antigen and present in SV40-infected and -transformed cells Virology 1979 93 2 466 480
    • (1979) Virology , vol.93 , Issue.2 , pp. 466-480
    • Melero, J.A.1    Stitt, D.T.2    Mangel, W.F.3    Carroll, R.B.4
  • 6
    • 0025876591 scopus 로고
    • The p53 tumour suppressor gene
    • Levine A. J., Momand J., Finlay C. A., The p53 tumour suppressor gene Nature 1991 351 6326 453 456
    • (1991) Nature , vol.351 , Issue.6326 , pp. 453-456
    • Levine, A.J.1    Momand, J.2    Finlay, C.A.3
  • 7
    • 0024382760 scopus 로고
    • The p53 proto-oncogene can act as a suppressor of transformation
    • Finlay C. A., Hinds P. W., Levine A. J., The p53 proto-oncogene can act as a suppressor of transformation Cell 1989 57 7 1083 1093
    • (1989) Cell , vol.57 , Issue.7 , pp. 1083-1093
    • Finlay, C.A.1    Hinds, P.W.2    Levine, A.J.3
  • 9
    • 0025040233 scopus 로고
    • Suppression of human colorectal carcinoma cell growth by wild-type p53
    • Baker S. J., Markowitz S., Fearon E. R., Willson J. K. V., Vogelstein B., Suppression of human colorectal carcinoma cell growth by wild-type p53 Science 1990 249 4971 912 915
    • (1990) Science , vol.249 , Issue.4971 , pp. 912-915
    • Baker, S.J.1    Markowitz, S.2    Fearon, E.R.3    Willson, J.K.V.4    Vogelstein, B.5
  • 11
    • 0025111068 scopus 로고
    • Conditional inhibition of transformation and of cell proliferation by a temperature-sensitive mutant of p53
    • Michalovitz D., Halevy O., Oren M., Conditional inhibition of transformation and of cell proliferation by a temperature-sensitive mutant of p53 Cell 1990 62 4 671 680
    • (1990) Cell , vol.62 , Issue.4 , pp. 671-680
    • Michalovitz, D.1    Halevy, O.2    Oren, M.3
  • 12
    • 0026093164 scopus 로고
    • Cellular localization and cell cycle regulation by a temperature- sensitive p53 protein
    • Martinez J., Georgoff I., Martinez J., Levine A. J., Cellular localization and cell cycle regulation by a temperature-sensitive p53 protein Genes and Development 1991 5 2 151 159
    • (1991) Genes and Development , vol.5 , Issue.2 , pp. 151-159
    • Martinez, J.1    Georgoff, I.2    Martinez, J.3    Levine, A.J.4
  • 16
    • 0024435565 scopus 로고
    • Rearrangements in the p53 gene in Philadelphia chromosome positive chronic myelogenous leukemia
    • Kelman Z., Prokocimer M., Peller S., Kahn Y., Rechavi G., Manor Y., Cohen A., Rotter V., Rearrangements in the p53 gene in Philadelphia chromosome positive chronic myelogenous leukemia Blood 1989 74 7 2318 2324
    • (1989) Blood , vol.74 , Issue.7 , pp. 2318-2324
    • Kelman, Z.1    Prokocimer, M.2    Peller, S.3    Kahn, Y.4    Rechavi, G.5    Manor, Y.6    Cohen, A.7    Rotter, V.8
  • 17
    • 0025711796 scopus 로고
    • Cancer. A deadly inheritance
    • Vogelstein B., Cancer. A deadly inheritance Nature 1990 348 6303 681 682
    • (1990) Nature , vol.348 , Issue.6303 , pp. 681-682
    • Vogelstein, B.1
  • 18
    • 0025265724 scopus 로고
    • Increased expression of mutant forms of p53 oncogene in primary lung cancer
    • Iggo R., Gatter K., Bartek J., Lane D., Harris A. L., Increased expression of mutant forms of p53 oncogene in primary lung cancer Lancet 1990 335 8691 675 679
    • (1990) Lancet , vol.335 , Issue.8691 , pp. 675-679
    • Iggo, R.1    Gatter, K.2    Bartek, J.3    Lane, D.4    Harris, A.L.5
  • 22
    • 0036674617 scopus 로고    scopus 로고
    • Live or let die: The cell's response to p53
    • Vousden K. H., Lu X., Live or let die: the cell's response to p53 Nature Reviews Cancer 2002 2 8 594 604
    • (2002) Nature Reviews Cancer , vol.2 , Issue.8 , pp. 594-604
    • Vousden, K.H.1    Lu, X.2
  • 23
    • 0027983669 scopus 로고
    • Crystal structure of a p53 tumor suppressor-DNA complex: Understanding tumorigenic mutations
    • Cho Y., Gorina S., Jeffrey P. D., Pavletich N. P., Crystal structure of a p53 tumor suppressor-DNA complex: understanding tumorigenic mutations Science 1994 265 5170 346 355
    • (1994) Science , vol.265 , Issue.5170 , pp. 346-355
    • Cho, Y.1    Gorina, S.2    Jeffrey, P.D.3    Pavletich, N.P.4
  • 28
    • 0023931972 scopus 로고
    • Immortalization of rat embryo fibroblasts by the cellular p53 oncogene
    • Rovinski B., Benchimol S., Immortalization of rat embryo fibroblasts by the cellular p53 oncogene Oncogene 1988 2 5 445 452
    • (1988) Oncogene , vol.2 , Issue.5 , pp. 445-452
    • Rovinski, B.1    Benchimol, S.2
  • 30
    • 0024586593 scopus 로고
    • When the products of oncogenes and anti-oncogenes meet
    • Green M. R., When the products of oncogenes and anti-oncogenes meet Cell 1989 56 1 1 3
    • (1989) Cell , vol.56 , Issue.1 , pp. 1-3
    • Green, M.R.1
  • 31
    • 0026669469 scopus 로고
    • P53 Function and dysfunction
    • Vogelstein B., Kinzler K. W., p53 Function and dysfunction Cell 1992 70 4 523 526
    • (1992) Cell , vol.70 , Issue.4 , pp. 523-526
    • Vogelstein, B.1    Kinzler, K.W.2
  • 32
    • 0029888514 scopus 로고    scopus 로고
    • Biological and clinical importance of the p53 tumor suppressor gene
    • Velculescu V. E., El-Deiry W. S., Biological and clinical importance of the p53 tumor suppressor gene Clinical Chemistry 1996 42 6 858 868
    • (1996) Clinical Chemistry , vol.42 , Issue.6 , pp. 858-868
    • Velculescu, V.E.1    El-Deiry, W.S.2
  • 33
    • 0034676455 scopus 로고    scopus 로고
    • Surfing the p53 network
    • Vogelstein B., Lane D., Levine A. J., Surfing the p53 network Nature 2000 408 6810 307 310
    • (2000) Nature , vol.408 , Issue.6810 , pp. 307-310
    • Vogelstein, B.1    Lane, D.2    Levine, A.J.3
  • 34
    • 0033230581 scopus 로고    scopus 로고
    • The cellular response to p53: The decision between life and death
    • Sionov R. V., Haupt Y., The cellular response to p53: the decision between life and death Oncogene 1999 18 45 6145 6157
    • (1999) Oncogene , vol.18 , Issue.45 , pp. 6145-6157
    • Sionov, R.V.1    Haupt, Y.2
  • 36
    • 0345256634 scopus 로고    scopus 로고
    • The role of p53 in chemosensitivity and radiosensitivity
    • El-Deiry W. S., The role of p53 in chemosensitivity and radiosensitivity Oncogene 2003 22 47 7486 7495
    • (2003) Oncogene , vol.22 , Issue.47 , pp. 7486-7495
    • El-Deiry, W.S.1
  • 39
    • 0032161624 scopus 로고    scopus 로고
    • P63, a p53 homolog at 3q2729, encodes multiple products with transactivating, death-inducing, and dominant-negative activities
    • Yang A., Kaghad M., Wang Y., Gillett E., Fleming M. D., Dtsch V., Andrews N. C., Caput D., McKeon F., p63, a p53 homolog at 3q2729, encodes multiple products with transactivating, death-inducing, and dominant-negative activities Molecular Cell 1998 2 3 305 316
    • (1998) Molecular Cell , vol.2 , Issue.3 , pp. 305-316
    • Yang, A.1    Kaghad, M.2    Wang, Y.3    Gillett, E.4    Fleming, M.D.5    Dtsch, V.6    Andrews, N.C.7    Caput, D.8    McKeon, F.9
  • 41
    • 29644436953 scopus 로고    scopus 로고
    • P73, a sophisticated p53 family member in the cancer world
    • Ozaki T., Nakagawara A., p73, a sophisticated p53 family member in the cancer world Cancer Science 2005 96 11 729 737
    • (2005) Cancer Science , vol.96 , Issue.11 , pp. 729-737
    • Ozaki, T.1    Nakagawara, A.2
  • 43
    • 72149097867 scopus 로고    scopus 로고
    • TATA-binding protein (TBP)-like protein is engaged in etoposide-induced apoptosis through transcriptional activation of human TAp63 gene
    • Suenaga Y., Ozaki T., Tanaka Y., Bu Y., Kamijo T., Tokuhisa T., Nakagawara A., Tamura T.-A., TATA-binding protein (TBP)-like protein is engaged in etoposide-induced apoptosis through transcriptional activation of human TAp63 gene Journal of Biological Chemistry 2009 284 51 35433 35440
    • (2009) Journal of Biological Chemistry , vol.284 , Issue.51 , pp. 35433-35440
    • Suenaga, Y.1    Ozaki, T.2    Tanaka, Y.3    Bu, Y.4    Kamijo, T.5    Tokuhisa, T.6    Nakagawara, A.7    Tamura, T.-A.8
  • 44
    • 0037440429 scopus 로고    scopus 로고
    • Regulation of tumor suppressors by nuclear-cytoplasmic shuttling
    • Fabbro M., Henderson B. R., Regulation of tumor suppressors by nuclear-cytoplasmic shuttling Experimental Cell Research 2003 282 2 59 69
    • (2003) Experimental Cell Research , vol.282 , Issue.2 , pp. 59-69
    • Fabbro, M.1    Henderson, B.R.2
  • 47
    • 0037012041 scopus 로고    scopus 로고
    • The proline-rich domain of p53 is required for cooperation with anti-neoplastic agents to promote apoptosis of tumor cells
    • Baptiste N., Friedlander P., Chen X., Prives C., The proline-rich domain of p53 is required for cooperation with anti-neoplastic agents to promote apoptosis of tumor cells Oncogene 2002 21 1 9 21
    • (2002) Oncogene , vol.21 , Issue.1 , pp. 9-21
    • Baptiste, N.1    Friedlander, P.2    Chen, X.3    Prives, C.4
  • 50
    • 0025611503 scopus 로고
    • Genetic mechanisms of tumor suppression by the human p53 gene
    • Chen P.-L., Chen Y., Bookstein R., Lee W.-H., Genetic mechanisms of tumor suppression by the human p53 gene Science 1990 250 4987 1576 1580
    • (1990) Science , vol.250 , Issue.4987 , pp. 1576-1580
    • Chen, P.-L.1    Chen, Y.2    Bookstein, R.3    Lee, W.-H.4
  • 51
    • 0030926817 scopus 로고    scopus 로고
    • Two functional assays employed to detect an unusual mutation in the oligomerisation domain of p53 in a Li-Fraumeni like family
    • Lomax M. E., Barnes D. M., Gilchrist R., Picksley S. M., Varley J. M., Camplejohn R. S., Two functional assays employed to detect an unusual mutation in the oligomerisation domain of p53 in a Li-Fraumeni like family Oncogene 1997 14 15 1869 1874
    • (1997) Oncogene , vol.14 , Issue.15 , pp. 1869-1874
    • Lomax, M.E.1    Barnes, D.M.2    Gilchrist, R.3    Picksley, S.M.4    Varley, J.M.5    Camplejohn, R.S.6
  • 52
    • 0032490875 scopus 로고    scopus 로고
    • Characterization of p53 oligomerization domain mutations isolated from Li-Fraumeni and Li-Fraumeni like family members
    • Lomax M. E., Barnes D. M., Hupp T. R., Picksley S. M., Camplejohn R. S., Characterization of p53 oligomerization domain mutations isolated from Li-Fraumeni and Li-Fraumeni like family members Oncogene 1998 17 5 643 649
    • (1998) Oncogene , vol.17 , Issue.5 , pp. 643-649
    • Lomax, M.E.1    Barnes, D.M.2    Hupp, T.R.3    Picksley, S.M.4    Camplejohn, R.S.5
  • 55
    • 77955175360 scopus 로고    scopus 로고
    • Pharmacological reactivation of mutant p53: From protein structure to the cancer patient
    • Wiman K. G., Pharmacological reactivation of mutant p53: from protein structure to the cancer patient Oncogene 2010 29 30 4245 4252
    • (2010) Oncogene , vol.29 , Issue.30 , pp. 4245-4252
    • Wiman, K.G.1
  • 57
    • 0027496935 scopus 로고
    • The p21 Cdk-interacting protein Cip1 is a potent inhibitor of G1 cyclin-dependent kinases
    • Harper J. W., Adami G. R., Wei N., Keyomarsi K., Elledge S. J., The p21 Cdk-interacting protein Cip1 is a potent inhibitor of G1 cyclin-dependent kinases Cell 1993 75 4 805 816
    • (1993) Cell , vol.75 , Issue.4 , pp. 805-816
    • Harper, J.W.1    Adami, G.R.2    Wei, N.3    Keyomarsi, K.4    Elledge, S.J.5
  • 58
    • 0028342664 scopus 로고
    • Cloning of senescent cell-derived inhibitors of DNA synthesis using an expression screen
    • Noda A., Ning Y., Venable S. F., Pereira-Smith O. M., Smith J. R., Cloning of senescent cell-derived inhibitors of DNA synthesis using an expression screen Experimental Cell Research 1994 211 1 90 98
    • (1994) Experimental Cell Research , vol.211 , Issue.1 , pp. 90-98
    • Noda, A.1    Ning, Y.2    Venable, S.F.3    Pereira-Smith, O.M.4    Smith, J.R.5
  • 59
    • 0034594978 scopus 로고    scopus 로고
    • A ribonucleotide reductase gene involved in a p53-dependent cell-cycle checkpoint for DNA damage
    • Tanaka H., Arakawa H., Yamaguchi T., Shiraishi K., Fukuda S., Matsui K., Takei Y., Nakamura Y., A ribonucleotide reductase gene involved in a p53-dependent cell-cycle checkpoint for DNA damage Nature 2000 404 6773 42 49
    • (2000) Nature , vol.404 , Issue.6773 , pp. 42-49
    • Tanaka, H.1    Arakawa, H.2    Yamaguchi, T.3    Shiraishi, K.4    Fukuda, S.5    Matsui, K.6    Takei, Y.7    Nakamura, Y.8
  • 60
    • 0030965946 scopus 로고    scopus 로고
    • Regulation of p53 stability by MDM2
    • Kubbutat M. H. G., Jones S. N., Vousden K. H., Regulation of p53 stability by MDM2 Nature 1997 387 6630 299 303
    • (1997) Nature , vol.387 , Issue.6630 , pp. 299-303
    • Kubbutat, M.H.G.1    Jones, S.N.2    Vousden, K.H.3
  • 61
    • 0030905284 scopus 로고    scopus 로고
    • MDM2 promotes the rapid degradation of p53
    • Haupt Y., Maya R., Kazaz A., Oren M., MDM2 promotes the rapid degradation of p53 Nature 1997 387 6630 296 299
    • (1997) Nature , vol.387 , Issue.6630 , pp. 296-299
    • Haupt, Y.1    Maya, R.2    Kazaz, A.3    Oren, M.4
  • 62
    • 0031583962 scopus 로고    scopus 로고
    • Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53
    • Honda R., Tanaka H., Yasuda H., Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53 FEBS Letters 1997 420 1 25 27
    • (1997) FEBS Letters , vol.420 , Issue.1 , pp. 25-27
    • Honda, R.1    Tanaka, H.2    Yasuda, H.3
  • 63
    • 0027459198 scopus 로고
    • MDM2 expression is induced by wild type p53 activity
    • Barak Y., Juven T., Haffner R., Oren M., MDM2 expression is induced by wild type p53 activity EMBO Journal 1993 12 2 461 468
    • (1993) EMBO Journal , vol.12 , Issue.2 , pp. 461-468
    • Barak, Y.1    Juven, T.2    Haffner, R.3    Oren, M.4
  • 64
    • 0028238213 scopus 로고
    • Immediate early up-regulation of bax expression by p53 but not TGF 1: A paradigm for distinct apoptotic pathways
    • Selvakumaran M., Lin H.-K., Miyashita T., Wang H. G., Krajewski S., Reed J. C., Hoffman B., Liebermann D., Immediate early up-regulation of bax expression by p53 but not TGF 1: a paradigm for distinct apoptotic pathways Oncogene 1994 9 6 1791 1798
    • (1994) Oncogene , vol.9 , Issue.6 , pp. 1791-1798
    • Selvakumaran, M.1    Lin, H.-K.2    Miyashita, T.3    Wang, H.G.4    Krajewski, S.5    Reed, J.C.6    Hoffman, B.7    Liebermann, D.8
  • 65
    • 33646380068 scopus 로고    scopus 로고
    • At the gates of death
    • Green D. R., At the gates of death Cancer Cell 2006 9 5 328 330
    • (2006) Cancer Cell , vol.9 , Issue.5 , pp. 328-330
    • Green, D.R.1
  • 68
  • 69
    • 0035265686 scopus 로고    scopus 로고
    • PUMA, a novel proapoptotic gene, is induced by p53
    • Nakano K., Vousden K. H., PUMA, a novel proapoptotic gene, is induced by p53 Molecular Cell 2001 7 3 683 694
    • (2001) Molecular Cell , vol.7 , Issue.3 , pp. 683-694
    • Nakano, K.1    Vousden, K.H.2
  • 71
    • 0033767235 scopus 로고    scopus 로고
    • Multiple C-terminal lysine residues target p53 for ubiquitin-proteasome- mediated degradation
    • Rodriguez M. S., Desterro J. M. P., Lain S., Lane D. P., Hay R. T., Multiple C-terminal lysine residues target p53 for ubiquitin-proteasome-mediated degradation Molecular and Cellular Biology 2000 20 22 8458 8467
    • (2000) Molecular and Cellular Biology , vol.20 , Issue.22 , pp. 8458-8467
    • Rodriguez, M.S.1    Desterro, J.M.P.2    Lain, S.3    Lane, D.P.4    Hay, R.T.5
  • 72
    • 0032475878 scopus 로고    scopus 로고
    • Signaling to p53: Breaking the MDM2-p53 circuit
    • Prives C., Signaling to p53: breaking the MDM2-p53 circuit Cell 1998 95 1 5 8
    • (1998) Cell , vol.95 , Issue.1 , pp. 5-8
    • Prives, C.1
  • 77
    • 0037061508 scopus 로고    scopus 로고
    • Deubiquitination of p53 by HAUSP is an important pathway for p53 stabilization
    • Li M., Chen D., Shiloh A., Luo J., Nikolaev A. Y., Qin J., Gu W., Deubiquitination of p53 by HAUSP is an important pathway for p53 stabilization Nature 2002 416 6881 648 653
    • (2002) Nature , vol.416 , Issue.6881 , pp. 648-653
    • Li, M.1    Chen, D.2    Shiloh, A.3    Luo, J.4    Nikolaev, A.Y.5    Qin, J.6    Gu, W.7
  • 78
    • 2942594540 scopus 로고    scopus 로고
    • Protein phosphatase 1, but not protein phosphatase 2A, dephosphorylates DNA-damaging stress-induced phospho-serine 15 of p53
    • Haneda M., Kojima E., Nishikimi A., Hasegawa T., Nakashima I., Isobe K.-I., Protein phosphatase 1, but not protein phosphatase 2A, dephosphorylates DNA-damaging stress-induced phospho-serine 15 of p53 FEBS Letters 2004 567 2-3 171 174
    • (2004) FEBS Letters , vol.567 , Issue.23 , pp. 171-174
    • Haneda, M.1    Kojima, E.2    Nishikimi, A.3    Hasegawa, T.4    Nakashima, I.5    Isobe, K.-I.6
  • 79
    • 33846542682 scopus 로고    scopus 로고
    • A specific PP2A regulatory subunit, B56 , mediates DNA damage-induced dephosphorylation of p53 at Thr55
    • Li H.-H., Cai X., Shouse G. P., Piluso L. G., Liu X., A specific PP2A regulatory subunit, B56, mediates DNA damage-induced dephosphorylation of p53 at Thr55 EMBO Journal 2007 26 2 402 411
    • (2007) EMBO Journal , vol.26 , Issue.2 , pp. 402-411
    • Li, H.-H.1    Cai, X.2    Shouse, G.P.3    Piluso, L.G.4    Liu, X.5
  • 82
    • 0042030879 scopus 로고    scopus 로고
    • Regulatory interactions between the checkpoint kinase Chk1 and the proteins of the DNA-dependent protein kinase complex
    • Goudelock D. M., Jiang K., Pereira E., Russell B., Sanchez Y., Regulatory interactions between the checkpoint kinase Chk1 and the proteins of the DNA-dependent protein kinase complex Journal of Biological Chemistry 2003 278 32 29940 29947
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.32 , pp. 29940-29947
    • Goudelock, D.M.1    Jiang, K.2    Pereira, E.3    Russell, B.4    Sanchez, Y.5
  • 83
    • 0033118933 scopus 로고    scopus 로고
    • DNA damage-inducible phosphorylation of p53 at N-terminal sites including a novel site, Ser20, requires tetramerization
    • Shieh S.-Y., Taya Y., Prives C., DNA damage-inducible phosphorylation of p53 at N-terminal sites including a novel site, Ser20, requires tetramerization EMBO Journal 1999 18 7 1815 1823
    • (1999) EMBO Journal , vol.18 , Issue.7 , pp. 1815-1823
    • Shieh, S.-Y.1    Taya, Y.2    Prives, C.3
  • 84
    • 0042854721 scopus 로고    scopus 로고
    • Allosteric effects mediate CHK2 phosphorylation of the p53 transactivation domain
    • Craig A., Scott M., Burch L., Smith G., Ball K., Hupp T., Allosteric effects mediate CHK2 phosphorylation of the p53 transactivation domain EMBO Reports 2003 4 8 787 792
    • (2003) EMBO Reports , vol.4 , Issue.8 , pp. 787-792
    • Craig, A.1    Scott, M.2    Burch, L.3    Smith, G.4    Ball, K.5    Hupp, T.6
  • 85
    • 0035965319 scopus 로고    scopus 로고
    • Reactive oxygen species-induced phosphorylation of p53 on serine 20 is mediated in part by polo-like kinase-3
    • Xie S., Wang Q., Wu H., Cogswell J., Lu L., Jhanwar-Uniyal M., Dai W., Reactive oxygen species-induced phosphorylation of p53 on serine 20 is mediated in part by polo-like kinase-3 Journal of Biological Chemistry 2001 276 39 36194 36199
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.39 , pp. 36194-36199
    • Xie, S.1    Wang, Q.2    Wu, H.3    Cogswell, J.4    Lu, L.5    Jhanwar-Uniyal, M.6    Dai, W.7
  • 87
    • 33646229039 scopus 로고    scopus 로고
    • Protein kinase C regulates Ser46 phosphorylation of p53 tumor suppressor in the apoptotic response to DNA damage
    • Yoshida K., Liu H., Miki Y., Protein kinase C regulates Ser46 phosphorylation of p53 tumor suppressor in the apoptotic response to DNA damage Journal of Biological Chemistry 2006 281 9 5734 5740
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.9 , pp. 5734-5740
    • Yoshida, K.1    Liu, H.2    Miki, Y.3
  • 88
    • 0025758832 scopus 로고
    • Association of casein kinase II with immunopurified p53
    • Herrmann C. P. E., Kraiss S., Montenarh M., Association of casein kinase II with immunopurified p53 Oncogene 1991 6 5 877 884
    • (1991) Oncogene , vol.6 , Issue.5 , pp. 877-884
    • Herrmann, C.P.E.1    Kraiss, S.2    Montenarh, M.3
  • 89
    • 0030919189 scopus 로고    scopus 로고
    • The in vitro phosphorylation of p53 by calcium-dependent protein kinase Ccharacterization of a protein-kinase-C-binding site on p53
    • Delphin C., Huang K.-P., Scotto C., Chapel A., Vincon M., Chambaz E., Garin J., Baudier J., The in vitro phosphorylation of p53 by calcium-dependent protein kinase Ccharacterization of a protein-kinase-C-binding site on p53 European Journal of Biochemistry 1997 245 3 684 692
    • (1997) European Journal of Biochemistry , vol.245 , Issue.3 , pp. 684-692
    • Delphin, C.1    Huang, K.-P.2    Scotto, C.3    Chapel, A.4    Vincon, M.5    Chambaz, E.6    Garin, J.7    Baudier, J.8
  • 90
    • 0026448672 scopus 로고
    • Regulation of the specific DNA binding function of p53
    • Hupp T. R., Meek D. W., Midgley C. A., Lane D. P., Regulation of the specific DNA binding function of p53 Cell 1992 71 5 875 886
    • (1992) Cell , vol.71 , Issue.5 , pp. 875-886
    • Hupp, T.R.1    Meek, D.W.2    Midgley, C.A.3    Lane, D.P.4
  • 91
    • 0028137084 scopus 로고
    • P53: A glimpse at the puppet behind the shadow play
    • Friend S., p53: a glimpse at the puppet behind the shadow play Science 1994 265 5170 334 335
    • (1994) Science , vol.265 , Issue.5170 , pp. 334-335
    • Friend, S.1
  • 96
    • 26244436281 scopus 로고    scopus 로고
    • Evolutionarily conserved and nonconserved cellular localizations and functions of human SIRT proteins
    • Michishita E., Park J. Y., Burneskis J. M., Barrett J. C., Horikawa I., Evolutionarily conserved and nonconserved cellular localizations and functions of human SIRT proteins Molecular Biology of the Cell 2005 16 10 4623 4635
    • (2005) Molecular Biology of the Cell , vol.16 , Issue.10 , pp. 4623-4635
    • Michishita, E.1    Park, J.Y.2    Burneskis, J.M.3    Barrett, J.C.4    Horikawa, I.5
  • 100
    • 73449091853 scopus 로고    scopus 로고
    • P53 sumoylation: Mechanistic insights from reconstitution studies
    • Wu S.-Y., Chiang C.-M., p53 sumoylation: mechanistic insights from reconstitution studies Epigenetics 2009 4 7 445 451
    • (2009) Epigenetics , vol.4 , Issue.7 , pp. 445-451
    • Wu, S.-Y.1    Chiang, C.-M.2
  • 101
    • 0024280897 scopus 로고
    • O-glycosylation of eukaryotic transcription factors: Implications for mechanisms of transcriptional regulation
    • Jackson S. P., Tjian R., O-glycosylation of eukaryotic transcription factors: implications for mechanisms of transcriptional regulation Cell 1988 55 1 125 133
    • (1988) Cell , vol.55 , Issue.1 , pp. 125-133
    • Jackson, S.P.1    Tjian, R.2
  • 102
    • 0030071548 scopus 로고    scopus 로고
    • Regulation of specific DNA binding by p53: Evidence for a role for O-glycosylation and charged residues at the carboxy-terminus
    • Shaw P., Freeman J., Bovey R., Iggo R., Regulation of specific DNA binding by p53: evidence for a role for O-glycosylation and charged residues at the carboxy-terminus Oncogene 1996 12 4 921 930
    • (1996) Oncogene , vol.12 , Issue.4 , pp. 921-930
    • Shaw, P.1    Freeman, J.2    Bovey, R.3    Iggo, R.4
  • 103
    • 0021228029 scopus 로고
    • Growth regulation of a cellular tumour antigen, p53, in nontransformed cells
    • Reich N. C., Levine A. J., Growth regulation of a cellular tumour antigen, p53, in nontransformed cells Nature 1984 308 5955 199 201
    • (1984) Nature , vol.308 , Issue.5955 , pp. 199-201
    • Reich, N.C.1    Levine, A.J.2
  • 106
    • 0034610751 scopus 로고    scopus 로고
    • A unique, short sequence determines p53 gene basal and UV-inducible expression in normal human cells
    • Noda A., Toma-Aiba Y., Fujiwara Y., A unique, short sequence determines p53 gene basal and UV-inducible expression in normal human cells Oncogene 2000 19 1 21 31
    • (2000) Oncogene , vol.19 , Issue.1 , pp. 21-31
    • Noda, A.1    Toma-Aiba, Y.2    Fujiwara, Y.3
  • 108
    • 10944247187 scopus 로고    scopus 로고
    • The AMP-activated protein kinase pathwaynew players upstream and downstream
    • Hardie D. G., The AMP-activated protein kinase pathwaynew players upstream and downstream Journal of Cell Science 2004 117 23 5479 5487
    • (2004) Journal of Cell Science , vol.117 , Issue.23 , pp. 5479-5487
    • Hardie, D.G.1
  • 109
    • 71649114159 scopus 로고    scopus 로고
    • Transcriptional regulation of tumor suppressor p53 by cAMP-responsive element-binding protein/AMP-activated protein kinase complex in response to glucose deprivation
    • Okoshi R., Ando K., Suenaga Y., Sang M., Kubo N., Kizaki H., Nakagawara A., Ozaki T., Transcriptional regulation of tumor suppressor p53 by cAMP-responsive element-binding protein/AMP-activated protein kinase complex in response to glucose deprivation Genes to Cells 2009 14 12 1429 1440
    • (2009) Genes to Cells , vol.14 , Issue.12 , pp. 1429-1440
    • Okoshi, R.1    Ando, K.2    Suenaga, Y.3    Sang, M.4    Kubo, N.5    Kizaki, H.6    Nakagawara, A.7    Ozaki, T.8
  • 112
    • 0033559256 scopus 로고    scopus 로고
    • A leucine-rich nuclear export signal in the p53 tetramerization domain: Regulation of subcellular localization and p53 activity by NES masking
    • Stommel J. M., Marchenko N. D., Jimenez G. S., Moll U. M., Hope T. J., Wahl G. M., A leucine-rich nuclear export signal in the p53 tetramerization domain: regulation of subcellular localization and p53 activity by NES masking EMBO Journal 1999 18 6 1660 1672
    • (1999) EMBO Journal , vol.18 , Issue.6 , pp. 1660-1672
    • Stommel, J.M.1    Marchenko, N.D.2    Jimenez, G.S.3    Moll, U.M.4    Hope, T.J.5    Wahl, G.M.6
  • 113
    • 34249295787 scopus 로고    scopus 로고
    • Hyperubiquitylation of wild-type p53 contributes to cytoplasmic sequestration in neuroblastoma
    • Becker K., Marchenko N. D., Maurice M., Moll U. M., Hyperubiquitylation of wild-type p53 contributes to cytoplasmic sequestration in neuroblastoma Cell Death and Differentiation 2007 14 7 1350 1360
    • (2007) Cell Death and Differentiation , vol.14 , Issue.7 , pp. 1350-1360
    • Becker, K.1    Marchenko, N.D.2    Maurice, M.3    Moll, U.M.4
  • 114
    • 34047103990 scopus 로고    scopus 로고
    • C-terminal modifications regulate MDM2 dissociation and nuclear export of p53
    • Carter S., Bischof O., Dejean A., Vousden K. H., C-terminal modifications regulate MDM2 dissociation and nuclear export of p53 Nature Cell Biology 2007 9 4 428 435
    • (2007) Nature Cell Biology , vol.9 , Issue.4 , pp. 428-435
    • Carter, S.1    Bischof, O.2    Dejean, A.3    Vousden, K.H.4
  • 115
    • 0037428078 scopus 로고    scopus 로고
    • Parc: A cytoplasmic anchor for p53
    • Nikolaev A. Y., Li M., Puskas N., Qin J., Gu W., Parc: a cytoplasmic anchor for p53 Cell 2003 112 1 29 40
    • (2003) Cell , vol.112 , Issue.1 , pp. 29-40
    • Nikolaev, A.Y.1    Li, M.2    Puskas, N.3    Qin, J.4    Gu, W.5
  • 118
    • 33847276654 scopus 로고    scopus 로고
    • Monoubiquitylation promotes mitochondrial p53 translocation
    • Marchenko N. D., Wolff S., Erster S., Becker K., Moll U. M., Monoubiquitylation promotes mitochondrial p53 translocation EMBO Journal 2007 26 4 923 934
    • (2007) EMBO Journal , vol.26 , Issue.4 , pp. 923-934
    • Marchenko, N.D.1    Wolff, S.2    Erster, S.3    Becker, K.4    Moll, U.M.5
  • 119
    • 0036307307 scopus 로고    scopus 로고
    • P53 stability and activity is regulated by MDM2-mediated induction of alternative p53 translation products
    • Yin Y., Luciani M. G., Fhraeus R., p53 stability and activity is regulated by MDM2-mediated induction of alternative p53 translation products Nature Cell Biology 2002 4 6 462 467
    • (2002) Nature Cell Biology , vol.4 , Issue.6 , pp. 462-467
    • Yin, Y.1    Luciani, M.G.2    Fhraeus, R.3
  • 120
    • 0032557649 scopus 로고    scopus 로고
    • Identification of a novel p53 functional domain that is necessary for mediating apoptosis
    • Zhu J., Zhou W., Jiang J., Chen X., Identification of a novel p53 functional domain that is necessary for mediating apoptosis Journal of Biological Chemistry 1998 273 21 13030 13036
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.21 , pp. 13030-13036
    • Zhu, J.1    Zhou, W.2    Jiang, J.3    Chen, X.4
  • 121
    • 0033535602 scopus 로고    scopus 로고
    • Definition of a p53 transactivation function-deficient mutant and characterization of two independent p53 transactivation subdomains
    • Venot C., Maratrat M., Sierra V., Conseiller E., Debussche L., Definition of a p53 transactivation function-deficient mutant and characterization of two independent p53 transactivation subdomains Oncogene 1999 18 14 2405 2410
    • (1999) Oncogene , vol.18 , Issue.14 , pp. 2405-2410
    • Venot, C.1    Maratrat, M.2    Sierra, V.3    Conseiller, E.4    Debussche, L.5
  • 124
    • 0343280013 scopus 로고    scopus 로고
    • A critical role for histone H2AX in recruitment of repair factors to nuclear foci after DNA damage
    • Paull T. T., Rogakou E. P., Yamazaki V., Kirchgessner C. U., Gellert M., Bonner W. M., A critical role for histone H2AX in recruitment of repair factors to nuclear foci after DNA damage Current Biology 2000 10 15 886 895
    • (2000) Current Biology , vol.10 , Issue.15 , pp. 886-895
    • Paull, T.T.1    Rogakou, E.P.2    Yamazaki, V.3    Kirchgessner, C.U.4    Gellert, M.5    Bonner, W.M.6
  • 125
    • 0037365789 scopus 로고    scopus 로고
    • ATM and related protein kinases: Safeguarding genome integrity
    • Shiloh Y., ATM and related protein kinases: safeguarding genome integrity Nature Reviews Cancer 2003 3 3 155 168
    • (2003) Nature Reviews Cancer , vol.3 , Issue.3 , pp. 155-168
    • Shiloh, Y.1
  • 128
    • 0037468192 scopus 로고    scopus 로고
    • MDC1 is a mediator of the mammalian DNA damage checkpoint
    • Stewart G. S., Wang B., Bigneli C. R., Taylor A. M. R., Elledge S. J., MDC1 is a mediator of the mammalian DNA damage checkpoint Nature 2003 421 6926 961 966
    • (2003) Nature , vol.421 , Issue.6926 , pp. 961-966
    • Stewart, G.S.1    Wang, B.2    Bigneli, C.R.3    Taylor, A.M.R.4    Elledge, S.J.5
  • 130
    • 0037468232 scopus 로고    scopus 로고
    • MDC1 is coupled to activated CHK2 in mammalian DNA damage response pathways
    • Lou Z., Minter-Dykhouse K., Wu X., Chen J., MDC1 is coupled to activated CHK2 in mammalian DNA damage response pathways Nature 2003 421 6926 957 961
    • (2003) Nature , vol.421 , Issue.6926 , pp. 957-961
    • Lou, Z.1    Minter-Dykhouse, K.2    Wu, X.3    Chen, J.4
  • 133
    • 36348962321 scopus 로고    scopus 로고
    • RUNX genes in development and cancer: Regulation of viral gene expression and the discovery of RUNX family genes
    • Ito Y., RUNX genes in development and cancer: regulation of viral gene expression and the discovery of RUNX family genes Advances in Cancer Research 2008 99 33 76
    • (2008) Advances in Cancer Research , vol.99 , pp. 33-76
    • Ito, Y.1
  • 136
    • 0034647718 scopus 로고    scopus 로고
    • An anti-apoptotic role for the p53 family member, p73, during developmental neuron death
    • Pozniak C. D., Radinovic S., Yang A., McKeon F., Kaplan D. R., Miller F. D., An anti-apoptotic role for the p53 family member, p73, during developmental neuron death Science 2000 289 5477 304 306
    • (2000) Science , vol.289 , Issue.5477 , pp. 304-306
    • Pozniak, C.D.1    Radinovic, S.2    Yang, A.3    McKeon, F.4    Kaplan, D.R.5    Miller, F.D.6
  • 138
    • 0032951530 scopus 로고    scopus 로고
    • P73 function is inhibited by tumor-derived p53 mutants in mammalian cells
    • Di Como C. J., Gaiddon C., Prives C., p73 function is inhibited by tumor-derived p53 mutants in mammalian cells Molecular and Cellular Biology 1999 19 2 1438 1449
    • (1999) Molecular and Cellular Biology , vol.19 , Issue.2 , pp. 1438-1449
    • Di Como, C.J.1    Gaiddon, C.2    Prives, C.3
  • 140
    • 0036203514 scopus 로고    scopus 로고
    • Autoinhibitory regulation of p73 by Delta Np73 to modulate cell survival and death through a p73-specific target element within the Delta Np73 promoter
    • Nakagawa T., Autoinhibitory regulation of p73 by Delta Np73 to modulate cell survival and death through a p73-specific target element within the Delta Np73 promoter Molecular and Cellular Biology 2002 22 2575 2585
    • (2002) Molecular and Cellular Biology , vol.22 , pp. 2575-2585
    • Nakagawa, T.1
  • 142
    • 0033379005 scopus 로고    scopus 로고
    • P53 family genes: Structural comparison, expression and mutation
    • Ikawa S., Nakagawara A., Ikawa Y., p53 family genes: structural comparison, expression and mutation Cell Death and Differentiation 1999 6 12 1154 1161
    • (1999) Cell Death and Differentiation , vol.6 , Issue.12 , pp. 1154-1161
    • Ikawa, S.1    Nakagawara, A.2    Ikawa, Y.3
  • 144
    • 0033594491 scopus 로고    scopus 로고
    • P63 is a p53 homologue required for limb and epidermal morphogenesis
    • Mills A. A., Zheng B., Wang X.-J., Vogel H., Roop D. R., Bradley A., p63 is a p53 homologue required for limb and epidermal morphogenesis Nature 1999 398 6729 708 713
    • (1999) Nature , vol.398 , Issue.6729 , pp. 708-713
    • Mills, A.A.1    Zheng, B.2    Wang, X.-J.3    Vogel, H.4    Roop, D.R.5    Bradley, A.6
  • 146
    • 17444390129 scopus 로고    scopus 로고
    • Tumor predisposition in mice mutant for p63 and p73: Evidence for broader tumor suppressor functions for the p53 family
    • Flores E. R., Sengupta S., Miller J. B., Newman J. J., Bronson R., Crowley D., Yang A., McKeon F., Jacks T., Tumor predisposition in mice mutant for p63 and p73: evidence for broader tumor suppressor functions for the p53 family Cancer Cell 2005 7 4 363 373
    • (2005) Cancer Cell , vol.7 , Issue.4 , pp. 363-373
    • Flores, E.R.1    Sengupta, S.2    Miller, J.B.3    Newman, J.J.4    Bronson, R.5    Crowley, D.6    Yang, A.7    McKeon, F.8    Jacks, T.9
  • 147
    • 0033666776 scopus 로고    scopus 로고
    • Role of the p53-homologue p73 in E2F1-induced apoptosis
    • Stiewe T., Putzer B. M., Role of the p53-homologue p73 in E2F1-induced apoptosis Nature Genetics 2000 26 4 464 469
    • (2000) Nature Genetics , vol.26 , Issue.4 , pp. 464-469
    • Stiewe, T.1    Putzer, B.M.2
  • 149
    • 0034609864 scopus 로고    scopus 로고
    • A common E2F-1 and p73 pathway mediates cell death induced by TCR activation
    • Lissy N. A., Davis P. K., Irwin M., Kaelin W. G., Dowdy S. F., A common E2F-1 and p73 pathway mediates cell death induced by TCR activation Nature 2000 407 6804 642 645
    • (2000) Nature , vol.407 , Issue.6804 , pp. 642-645
    • Lissy, N.A.1    Davis, P.K.2    Irwin, M.3    Kaelin, W.G.4    Dowdy, S.F.5
  • 150
    • 77954352759 scopus 로고    scopus 로고
    • Sp1 binds to the external promoter of the p73 gene and induces the expression of TAp73gamma in lung cancer
    • Logotheti S., Sp1 binds to the external promoter of the p73 gene and induces the expression of TAp73gamma in lung cancer FEBS Journal 2010 277 3014 3027
    • (2010) FEBS Journal , vol.277 , pp. 3014-3027
    • Logotheti, S.1
  • 151
    • 0035193044 scopus 로고    scopus 로고
    • The transcriptional repressor ZEB regulates p73 expression at the crossroad between proliferation and differentiation
    • Fontemaggi G., The transcriptional repressor ZEB regulates p73 expression at the crossroad between proliferation and differentiation Molecular and Cellular Biology 2001 21 8461 8470
    • (2001) Molecular and Cellular Biology , vol.21 , pp. 8461-8470
    • Fontemaggi, G.1
  • 152
    • 0033600234 scopus 로고    scopus 로고
    • The tyrosine kinase c-Abl regulates p73 in apoptotic response to cisplatin-induced DNA damage
    • Gong J., Costanzo A., Yang H.-Q., Mellno G., Kaelin W. G. Jr., Levrero M., Wang J. Y. J., The tyrosine kinase c-Abl regulates p73 in apoptotic response to cisplatin-induced DNA damage Nature 1999 399 6738 806 809
    • (1999) Nature , vol.399 , Issue.6738 , pp. 806-809
    • Gong, J.1    Costanzo, A.2    Yang, H.-Q.3    Mellno, G.4    Kaelin Jr., W.G.5    Levrero, M.6    Wang, J.Y.J.7
  • 153
    • 0033600240 scopus 로고    scopus 로고
    • Interaction of c-Abl and p73 and their collaboration to induce apoptosis
    • Agami R., Blandino G., Oren M., Shaul Y., Interaction of c-Abl and p73 and their collaboration to induce apoptosis Nature 1999 399 6738 809 812
    • (1999) Nature , vol.399 , Issue.6738 , pp. 809-812
    • Agami, R.1    Blandino, G.2    Oren, M.3    Shaul, Y.4
  • 155
    • 0037072483 scopus 로고    scopus 로고
    • P73 is regulated by protein kinase C catalytic fragment generated in the apoptotic response to DNA damage
    • Ren J., Datta R., Shioya H., Li Y., Oki E., Biedermann V., Bharti A., Kufe D., p73 is regulated by protein kinase C catalytic fragment generated in the apoptotic response to DNA damage Journal of Biological Chemistry 2002 277 37 33758 33765
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.37 , pp. 33758-33765
    • Ren, J.1    Datta, R.2    Shioya, H.3    Li, Y.4    Oki, E.5    Biedermann, V.6    Bharti, A.7    Kufe, D.8
  • 158
    • 39149136475 scopus 로고    scopus 로고
    • ATM-dependent nuclear accumulation of IKK- plays an important role in the regulation of p73-mediated apoptosis in response to cisplatin
    • Yoshida K., Ozaki T., Furuya K., Nakanishi M., Kikuchi H., Yamamoto H., Ono S., Koda T., Omura K., Nakagawara A., ATM-dependent nuclear accumulation of IKK- plays an important role in the regulation of p73-mediated apoptosis in response to cisplatin Oncogene 2008 27 8 1183 1188
    • (2008) Oncogene , vol.27 , Issue.8 , pp. 1183-1188
    • Yoshida, K.1    Ozaki, T.2    Furuya, K.3    Nakanishi, M.4    Kikuchi, H.5    Yamamoto, H.6    Ono, S.7    Koda, T.8    Omura, K.9    Nakagawara, A.10
  • 159
    • 0042347445 scopus 로고    scopus 로고
    • Cyclin-dependent kinases phosphorylate p73 at Threonine 86 in a cell cycle-dependent manner and negatively regulate p73
    • Gaiddon C., Lokshin M., Gross I., Levasseur D., Taya Y., Loeffler J.-P., Prives C., Cyclin-dependent kinases phosphorylate p73 at Threonine 86 in a cell cycle-dependent manner and negatively regulate p73 Journal of Biological Chemistry 2003 278 30 27421 27431
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.30 , pp. 27421-27431
    • Gaiddon, C.1    Lokshin, M.2    Gross, I.3    Levasseur, D.4    Taya, Y.5    Loeffler, J.-P.6    Prives, C.7


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