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Volumn 191, Issue 1-2, 1999, Pages 187-199

Protein kinase CK2-dependent regulation of p53 function: Evidence that the phosphorylation status of the serine 386 (CK2) site of p53 is constitutive and stable

Author keywords

Centrosome; Ck2; Dephosphorylation; p53; Subcellular localisation

Indexed keywords

CASEIN KINASE II; PHOSPHOPROTEIN PHOSPHATASE 1; PROTEIN P53; RECOMBINANT PROTEIN; SERINE;

EID: 0033059744     PISSN: 03008177     EISSN: None     Source Type: Journal    
DOI: 10.1007/978-1-4419-8624-5_23     Document Type: Article
Times cited : (43)

References (70)
  • 1
    • 0029980043 scopus 로고    scopus 로고
    • p53 in growth control and neoplasia
    • Gottlieb TM, Oren M: p53 in growth control and neoplasia. Biochim Biophys Acta1287: 77-102, 1996
    • (1996) Biochim Biophys Acta , vol.1287 , pp. 77-102
    • Gottlieb, T.M.1    Oren, M.2
  • 2
    • 0029972806 scopus 로고    scopus 로고
    • p53: Puzzle and paradigm
    • Ko LJ, Prives C: p53: Puzzle and paradigm. Genes Dev 10: 1054-1072, 1996
    • (1996) Genes Dev , vol.10 , pp. 1054-1072
    • Ko, L.J.1    Prives, C.2
  • 3
    • 0030941458 scopus 로고    scopus 로고
    • p53, the cellular gatekeeper for growth and division
    • Levine AJ: p53, the cellular gatekeeper for growth and division. Cell 88: 323-331, 1997
    • (1997) Cell , vol.88 , pp. 323-331
    • Levine, A.J.1
  • 4
    • 0030564943 scopus 로고    scopus 로고
    • Structural aspects of the p53 protein in relation to gene evolution: A second look
    • Soussi T, May P: Structural aspects of the p53 protein in relation to gene evolution: A second look. J Mol Biol 260: 623-637, 1997
    • (1997) J Mol Biol , vol.260 , pp. 623-637
    • Soussi, T.1    May, P.2
  • 5
    • 0029973389 scopus 로고    scopus 로고
    • Cell-cycle control and its watchman
    • Jacks T, Weinberg RA: Cell-cycle control and its watchman. Nature 381: 643-644, 1996
    • (1996) Nature , vol.381 , pp. 643-644
    • Jacks, T.1    Weinberg, R.A.2
  • 6
    • 0345606992 scopus 로고    scopus 로고
    • p53 - Integrating the complexity
    • Hall PA, Meek D, Lane DP: p53 - Integrating the complexity. J Path 1801-1805, 1996
    • (1996) J Path , pp. 1801-1805
    • Hall, P.A.1    Meek, D.2    Lane, D.P.3
  • 10
    • 0028946766 scopus 로고
    • Accumulation of wild-type p53 protein upon gammairradiation induces a G2 arrest-dependent immunoglobulin kappa light chain gene expression
    • Aloni GR, Schwartz D, Rotter V: Accumulation of wild-type p53 protein upon gammairradiation induces a G2 arrest-dependent immunoglobulin kappa light chain gene expression. EMBO J 14: 1392-1401, 1995
    • (1995) EMBO J , vol.14 , pp. 1392-1401
    • Aloni, G.R.1    Schwartz, D.2    Rotter, V.3
  • 13
    • 0025784539 scopus 로고
    • Wild-type p53 induces apoptosis of myeloid leukaemic cells that is inhibited by interleukin-6
    • Yonish RE, Resnitzky D, Lotem J, Sachs L, Kimchi A, Oren M: Wild-type p53 induces apoptosis of myeloid leukaemic cells that is inhibited by interleukin-6. Nature 352: 345-347, 1991
    • (1991) Nature , vol.352 , pp. 345-347
    • Yonish, R.E.1    Resnitzky, D.2    Lotem, J.3    Sachs, L.4    Kimchi, A.5    Oren, M.6
  • 14
    • 0026523778 scopus 로고
    • Induction of apoptosis by wildtype p53 in a human colon tumor-derived cell line
    • Shaw P, Bovey R, Tardy S, Sahli R, Sordat B, Costa J: Induction of apoptosis by wildtype p53 in a human colon tumor-derived cell line. Proc Natl Acad Sci USA 89: 4495-4499, 1992
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 4495-4499
    • Shaw, P.1    Bovey, R.2    Tardy, S.3    Sahli, R.4    Sordat, B.5    Costa, J.6
  • 15
    • 0027235369 scopus 로고
    • Cancer. A death in the life of p53
    • Lane DP: Cancer. A death in the life of p53 [news; comment]. Nature 362: 786-787, 1993
    • (1993) Nature , vol.362 , pp. 786-787
    • Lane, D.P.1
  • 17
    • 0030025772 scopus 로고    scopus 로고
    • Life (and death) in a malignant tumour
    • Kinzler KW, Vogelstein B: Life (and death) in a malignant tumour. Nature 79: 19-20, 1996
    • (1996) Nature , vol.79 , pp. 19-20
    • Kinzler, K.W.1    Vogelstein, B.2
  • 19
    • 0027498314 scopus 로고
    • The mdm-2 oncogene can overcome wild-type p53 suppression of transformed cell growth
    • Finlay CA: The mdm-2 oncogene can overcome wild-type p53 suppression of transformed cell growth. Mol Cell Biol 13: 301-306, 1993
    • (1993) Mol Cell Biol , vol.13 , pp. 301-306
    • Finlay, C.A.1
  • 20
    • 0029171789 scopus 로고
    • Regulation of transcription functions of the p53 tumor suppressor by the mdm-2 oncogene
    • Chen J, Lin J, Levine AJ: Regulation of transcription functions of the p53 tumor suppressor by the mdm-2 oncogene. Mol Med 1: 42-152, 1995
    • (1995) Mol Med , vol.1 , pp. 42-152
    • Chen, J.1    Lin, J.2    Levine, A.J.3
  • 21
    • 0027522235 scopus 로고
    • Cooperative DNa binding of p53 with TFIID (TBP): A possible mechanism for transcriptional activation
    • published erratum appears in Genes Dev 7: 2652, 1993
    • Chen X, Farmer G, Zhu H, Prywes R, Prives C: Cooperative DNA binding of p53 with TFIID (TBP): A possible mechanism for transcriptional activation [published erratum appears in Genes Dev 7: 2652, 1993]. Genes Dev 7: 1837-1849, 1993
    • (1993) Genes Dev , vol.7 , pp. 1837-1849
    • Chen, X.1    Farmer, G.2    Zhu, H.3    Prywes, R.4    Prives, C.5
  • 22
    • 0344312446 scopus 로고
    • The p53 activation domain binds the TATA boxbinding polypeptide in Holo-TFIID, and a neighboring p53 domain inhibits transcription
    • Liu X, Miller CW, Koeffler PH, Berk AJ: The p53 activation domain binds the TATA boxbinding polypeptide in Holo-TFIID, and a neighboring p53 domain inhibits transcription. Mol Cell Biol 3: 291-330, 1993
    • (1993) Mol Cell Biol , vol.3 , pp. 291-330
    • Liu, X.1    Miller, C.W.2    Koeffler, P.H.3    Berk, A.J.4
  • 23
    • 0028979005 scopus 로고
    • Human TAFII31 protein is a transcriptional coactivator of the p53 protein
    • Lu H, Levine AJ: Human TAFII31 protein is a transcriptional coactivator of the p53 protein. Proc Natl Acad Sci USA 92: 5154-5158, 1995
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 5154-5158
    • Lu, H.1    Levine, A.J.2
  • 24
    • 0027451298 scopus 로고
    • p53 binds to the TATA-binding protein TATA complex
    • Martin DW, Munoz RM, Subler MA, Deb S: p53 binds to the TATA-binding protein TATA complex. J Biol Chem 268: 3062-3067, 1993
    • (1993) J Biol Chem , vol.268 , pp. 3062-3067
    • Martin, D.W.1    Munoz, R.M.2    Subler, M.A.3    Deb, S.4
  • 25
    • 0028922929 scopus 로고
    • p53 transcriptional activation mediated by coactivators TAFII40 and TAFII60
    • Thut CJ, Chen JL, Klemm R, Tjian R: p53 transcriptional activation mediated by coactivators TAFII40 and TAFII60. Science 267: 100-104, 1995
    • (1995) Science , vol.267 , pp. 100-104
    • Thut, C.J.1    Chen, J.L.2    Klemm, R.3    Tjian, R.4
  • 28
    • 0027299244 scopus 로고
    • The trans-activator proteins VP16 and GAL4 bind replication factor A
    • He Z, Brinton BT, Greenblatt J, Hassell JA, Ingles CJ: The trans-activator proteins VP16 and GAL4 bind replication factor A. Cell 73: 1223-1232, 1993
    • (1993) Cell , vol.73 , pp. 1223-1232
    • He, Z.1    Brinton, B.T.2    Greenblatt, J.3    Hassell, J.A.4    Ingles, C.J.5
  • 29
    • 0027195936 scopus 로고
    • The acidic transcriptional activation domains of VP16 and p53 bind the cellular replication protein a and stimulate in vitro BPV-1 DNA replication
    • Li R, Botchan MR: The acidic transcriptional activation domains of VP16 and p53 bind the cellular replication protein A and stimulate in vitro BPV-1 DNA replication. Cell 73: 1207-1221, 1993
    • (1993) Cell , vol.73 , pp. 1207-1221
    • Li, R.1    Botchan, M.R.2
  • 30
    • 33748229853 scopus 로고
    • T-antigen is bound to host protein in SV40-transformed cells
    • Lane DP, Crawford LV: T-antigen is bound to host protein in SV40-transformed cells. Nature 278: 61-263, 1979
    • (1979) Nature , vol.278 , pp. 61-263
    • Lane, D.P.1    Crawford, L.V.2
  • 31
    • 0018760324 scopus 로고
    • Characterization of a 54K daiton cellular SV40 tumor antigen present in SV40-transformed cells and uninfected embryonal carcinoma cells
    • Linzer DI, Levine AJ: Characterization of a 54K daiton cellular SV40 tumor antigen present in SV40-transformed cells and uninfected embryonal carcinoma cells. Cell 17: 43-52, 1979
    • (1979) Cell , vol.17 , pp. 43-52
    • Linzer, D.I.1    Levine, A.J.2
  • 32
    • 0020079972 scopus 로고
    • Adenovirus E1b-58kd tumor antigen and SV40 large tumor antigen are physically associated with the same 54 kd cellular protein in transformed cells
    • Sarnow P, Ho YS, Williams J, Levine AJ: Adenovirus E1b-58kd tumor antigen and SV40 large tumor antigen are physically associated with the same 54 kd cellular protein in transformed cells. Cell 28: 387-394, 1982
    • (1982) Cell , vol.28 , pp. 387-394
    • Sarnow, P.1    Ho, Y.S.2    Williams, J.3    Levine, A.J.4
  • 34
    • 0029055808 scopus 로고
    • Activation of p53 sequence-specific DNA binding by short single strand ends of DNA requires the p53 C-terminus
    • Jayaraman L, Prives C: Activation of p53 sequence-specific DNA binding by short single strand ends of DNA requires the p53 C-terminus. Cell 81: 1021-1029, 1995
    • (1995) Cell , vol.81 , pp. 1021-1029
    • Jayaraman, L.1    Prives, C.2
  • 35
    • 0029013273 scopus 로고
    • p53 and its 14 kDa C-terminal domain recognise primary DNA damage in the form of insertion/ deletion mismatches
    • Lee S, Elenbaas B, Levine A, Griffith J: p53 and its 14 kDa C-terminal domain recognise primary DNA damage in the form of insertion/ deletion mismatches. Cell 81: 1013-1020, 1995
    • (1995) Cell , vol.81 , pp. 1013-1020
    • Lee, S.1    Elenbaas, B.2    Levine, A.3    Griffith, J.4
  • 36
    • 0027284915 scopus 로고
    • p53-catalyzed annealing of complementary single-stranded nucleic acids
    • Oberosler P, Hloch P, Ramsperger U, Stahl H: p53-catalyzed annealing of complementary single-stranded nucleic acids. EMBO J 12: 2389-2396, 1993
    • (1993) EMBO J , vol.12 , pp. 2389-2396
    • Oberosler, P.1    Hloch, P.2    Ramsperger, U.3    Stahl, H.4
  • 38
    • 0030448650 scopus 로고    scopus 로고
    • Identification of a novel p53 functional domain that is necessary for efficient growth suppression
    • Walker KK, Levine AJ: Identification of a novel p53 functional domain that is necessary for efficient growth suppression. Proc Natl Acad Sci USA 93: 15335-15340, 1996
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 15335-15340
    • Walker, K.K.1    Levine, A.J.2
  • 39
    • 0028455516 scopus 로고
    • Post-translational modification of p53
    • Meek DW: Post-translational modification of p53. Seminars in Cancer Biology 5: 203-210, 1994
    • (1994) Seminars in Cancer Biology , vol.5 , pp. 203-210
    • Meek, D.W.1
  • 40
    • 0031971228 scopus 로고    scopus 로고
    • Multisite phosphorylation and the integration of stress signals at p53
    • Meek DW: Multisite phosphorylation and the integration of stress signals at p53. Cellular Signalling 10: 159-166, 1997
    • (1997) Cellular Signalling , vol.10 , pp. 159-166
    • Meek, D.W.1
  • 41
    • 0025143302 scopus 로고
    • The p53 tumour suppressor protein is phosphorylated at serine 389 by casein kinase 2
    • Meek DW, Simon S, Kikkawa U, Eckhart W: The p53 tumour suppressor protein is phosphorylated at serine 389 by casein kinase 2. EMBO J 9: 253-3260, 1990
    • (1990) EMBO J , vol.9 , pp. 253-3260
    • Meek, D.W.1    Simon, S.2    Kikkawa, U.3    Eckhart, W.4
  • 42
    • 0025758832 scopus 로고
    • Association of casein kinase II with immunopurified p53
    • Herrmann CP, Kraiss S, Montenarh M: Association of casein kinase II with immunopurified p53. Oncogene 6: 877-884, 1991
    • (1991) Oncogene , vol.6 , pp. 877-884
    • Herrmann, C.P.1    Kraiss, S.2    Montenarh, M.3
  • 43
    • 0026448672 scopus 로고
    • Regulation of the specific DNA binding function of p53
    • Hupp TR, Meek DW, Midgley CA, Lane DP: Regulation of the specific DNA binding function of p53. Cell 71: 875-886, 1992
    • (1992) Cell , vol.71 , pp. 875-886
    • Hupp, T.R.1    Meek, D.W.2    Midgley, C.A.3    Lane, D.P.4
  • 44
    • 0030816303 scopus 로고    scopus 로고
    • Protein interactions at the carboxyl terminus of p53 result in the induction of its in vitro transactivation potential
    • Mundt M, Hupp T, Merkle C, Hansen S, Lane D, Groner B: Protein interactions at the carboxyl terminus of p53 result in the induction of its in vitro transactivation potential. Oncogene 15: 237-244, 1997
    • (1997) Oncogene , vol.15 , pp. 237-244
    • Mundt, M.1    Hupp, T.2    Merkle, C.3    Hansen, S.4    Lane, D.5    Groner, B.6
  • 45
  • 48
    • 0028131554 scopus 로고
    • Transcriptional activation by p53 correlates with suppression of growth but not transformation
    • Crook T, Marston NJ, Sara EA, Vousden KH: Transcriptional activation by p53 correlates with suppression of growth but not transformation. Cell 79: 817-827, 1994
    • (1994) Cell , vol.79 , pp. 817-827
    • Crook, T.1    Marston, N.J.2    Sara, E.A.3    Vousden, K.H.4
  • 49
    • 0028986133 scopus 로고
    • p53 phosphorylation mutants retain transcription activity
    • Fuchs B, Hecker D, Scheidtmann KH: p53 phosphorylation mutants retain transcription activity. Oncogene 10: 789-793, 1995
    • (1995) Oncogene , vol.10 , pp. 789-793
    • Fuchs, B.1    Hecker, D.2    Scheidtmann, K.H.3
  • 50
    • 0029944721 scopus 로고    scopus 로고
    • Phosphorylation of p53 at the casein kinase II site selectively regulates p53-dependent transcriptional repression but not transactivation
    • Hall SR, Campbell LE, Meek DW: Phosphorylation of p53 at the casein kinase II site selectively regulates p53-dependent transcriptional repression but not transactivation. Nucleic Acids Res 24: 1119-1126, 1996
    • (1996) Nucleic Acids Res , vol.24 , pp. 1119-1126
    • Hall, S.R.1    Campbell, L.E.2    Meek, D.W.3
  • 51
    • 0026484399 scopus 로고
    • Mutation of the casein kinase II phosphorylation site abolishes the anti-proliferative activity of p53
    • Milne DM, Palmer RH, Meek DW: Mutation of the casein kinase II phosphorylation site abolishes the anti-proliferative activity of p53. Nucleic Acids Res 20: 5565-5570, 1992
    • (1992) Nucleic Acids Res , vol.20 , pp. 5565-5570
    • Milne, D.M.1    Palmer, R.H.2    Meek, D.W.3
  • 52
    • 0029951978 scopus 로고    scopus 로고
    • Casein kinase II inhibits the renaturation of complementary DNA strands mediated by p53 protein
    • Filhol O, Baudier J, Chambaz EM, Cochet C: Casein kinase II inhibits the renaturation of complementary DNA strands mediated by p53 protein. Biochem J 316: 331-335, 1996
    • (1996) Biochem J , vol.316 , pp. 331-335
    • Filhol, O.1    Baudier, J.2    Chambaz, E.M.3    Cochet, C.4
  • 53
    • 0028600124 scopus 로고
    • Regulation of casein kinase II by growth factors: A reevaluation
    • Litchfield DW, Dobrowolska G, Krebs EG: Regulation of casein kinase II by growth factors: A reevaluation. Cell Mol Biol Res 40: 373-381, 1994
    • (1994) Cell Mol Biol Res , vol.40 , pp. 373-381
    • Litchfield, D.W.1    Dobrowolska, G.2    Krebs, E.G.3
  • 54
    • 0028600126 scopus 로고
    • A novel system to investigate the phosphorylation of the p53 tumour suppressor protein by the protein kinase CK2
    • McKendrick L, Meek DW: A novel system to investigate the phosphorylation of the p53 tumour suppressor protein by the protein kinase CK2. Cell Mol Biol Res 40: 555-561, 1994
    • (1994) Cell Mol Biol Res , vol.40 , pp. 555-561
    • McKendrick, L.1    Meek, D.W.2
  • 55
    • 0021710934 scopus 로고
    • Hygromycin B phosphotransferase as a selectable marker for DNA transfer experiments with higher eukaryotic cells
    • Blochlinger K, Diggelmann H: Hygromycin B phosphotransferase as a selectable marker for DNA transfer experiments with higher eukaryotic cells. Mol Cell Biol 4: 2929-2931, 1984
    • (1984) Mol Cell Biol , vol.4 , pp. 2929-2931
    • Blochlinger, K.1    Diggelmann, H.2
  • 56
    • 0025212687 scopus 로고
    • Mutation of the serine 312 phosphorylation site does not alter the ability of mouse p53 to inhibit simian virus 40 DNA replication in vivo
    • Meek DW, Eckhart W: Mutation of the serine 312 phosphorylation site does not alter the ability of mouse p53 to inhibit simian virus 40 DNA replication in vivo. J Virol 64: 1734-1744, 1990
    • (1990) J Virol , vol.64 , pp. 1734-1744
    • Meek, D.W.1    Eckhart, W.2
  • 57
    • 0023807923 scopus 로고
    • Phosphorylation of p53 in normal and transformed simian virus 40-transformed NIH 3T3 cells
    • Meek DW, Eckhart W: Phosphorylation of p53 in normal and transformed simian virus 40-transformed NIH 3T3 cells. Mol Cell Biol 8: 461-465, 1988
    • (1988) Mol Cell Biol , vol.8 , pp. 461-465
    • Meek, D.W.1    Eckhart, W.2
  • 58
    • 0028363749 scopus 로고
    • Phosphorylation of the tumour suppressor protein p53 by mitogen activated protein (MAP) kinases
    • Milne DM, Campbell DG, Caudwell FB, Meek DW: Phosphorylation of the tumour suppressor protein p53 by mitogen activated protein (MAP) kinases. J Biol Chem 269: 9253-9260, 1994
    • (1994) J Biol Chem , vol.269 , pp. 9253-9260
    • Milne, D.M.1    Campbell, D.G.2    Caudwell, F.B.3    Meek, D.W.4
  • 59
    • 0029928784 scopus 로고    scopus 로고
    • Interaction sites between catalytic and regulatory subunits in human protein-kinase CK2 oloenzymes as indicated by chemical crosslinking and immunological investigations
    • Krehan A, Lorenz P, Planacoll M, Pyerin W: Interaction sites between catalytic and regulatory subunits in human protein-kinase CK2 oloenzymes as indicated by chemical crosslinking and immunological investigations. Biochemistry 35: 4966-4975, 1996
    • (1996) Biochemistry , vol.35 , pp. 4966-4975
    • Krehan, A.1    Lorenz, P.2    Planacoll, M.3    Pyerin, W.4
  • 60
    • 0019401161 scopus 로고
    • Monoclonal antibodies specific for simian virus 40 tumor antigens
    • Harlow E, Crawford LV, Pim DC, Williamson NM: Monoclonal antibodies specific for simian virus 40 tumor antigens. J Virol 39: 861-869, 1981
    • (1981) J Virol , vol.39 , pp. 861-869
    • Harlow, E.1    Crawford, L.V.2    Pim, D.C.3    Williamson, N.M.4
  • 61
    • 0023357662 scopus 로고
    • Modification of fos proteins: Phosphorylation of c-fos, but not v-fos, is stimulated by 12-tetradecanoyl-phorbol-13-acetate and serum
    • Barber JR, Verma IM: Modification of fos proteins: phosphorylation of c-fos, but not v-fos, is stimulated by 12-tetradecanoyl-phorbol-13-acetate and serum. Mol Cell Biol 7: 2201-2211, 1987
    • (1987) Mol Cell Biol , vol.7 , pp. 2201-2211
    • Barber, J.R.1    Verma, I.M.2
  • 62
    • 0028591832 scopus 로고
    • Development of inhibitors of protein kinases CK1 and CK2 and some related aspects, including donor and acceptor specificities and viral protein kinases
    • Shugar D: Development of inhibitors of protein kinases CK1 and CK2 and some related aspects, including donor and acceptor specificities and viral protein kinases. Cell Mol Biol Res 40: 411-420, 1994
    • (1994) Cell Mol Biol Res , vol.40 , pp. 411-420
    • Shugar, D.1
  • 63
    • 0024397415 scopus 로고
    • The structure and regulation of protein phosphatases
    • Cohen P: The structure and regulation of protein phosphatases. Annu Rev Biochem 58: 453-508, 1989
    • (1989) Annu Rev Biochem , vol.58 , pp. 453-508
    • Cohen, P.1
  • 64
    • 0028089860 scopus 로고
    • Inhibitors of protein-kinases and phosphatases
    • MacKintosh C, MacKintosh RW: Inhibitors of protein-kinases and phosphatases. Trends Biochem Sei 19: 444-448, 1994
    • (1994) Trends Biochem Sei , vol.19 , pp. 444-448
    • MacKintosh, C.1    MacKintosh, R.W.2
  • 65
    • 0026016248 scopus 로고
    • Dephosphorylation of simian virus 40 large-T antigen and p53 protein by protein phosphatase 2A: Inhibition by small-t antigen
    • Scheidtmann KH, Mumby MC, Rundell K, Waiter G: Dephosphorylation of simian virus 40 large-T antigen and p53 protein by protein phosphatase 2A: Inhibition by small-t antigen. Mol Cell Biol 11: 1996-2003, 1991
    • (1991) Mol Cell Biol , vol.11 , pp. 1996-2003
    • Scheidtmann, K.H.1    Mumby, M.C.2    Rundell, K.3    Waiter, G.4
  • 66
    • 0026531390 scopus 로고
    • Casein kinase II is a predominantly nuclear enzyme
    • Krek W, Maridor G, Nigg EA: Casein kinase II is a predominantly nuclear enzyme. J Cell Biol 16(1): 43-55, 1992
    • (1992) J Cell Biol , vol.16 , Issue.1 , pp. 43-55
    • Krek, W.1    Maridor, G.2    Nigg, E.A.3
  • 67
    • 0028519273 scopus 로고
    • Allosteric activation of latent p53 tetramers
    • Hupp TR, Lane DP: Allosteric activation of latent p53 tetramers. Curr Biol 4: 865-875, 1994
    • (1994) Curr Biol , vol.4 , pp. 865-875
    • Hupp, T.R.1    Lane, D.P.2
  • 68
    • 0027174586 scopus 로고
    • Use of the two-hybrid system to identify the domain of p53 involved in oligomerization
    • Iwabuchi K, Li B, Bartei P, Fields S: Use of the two-hybrid system to identify the domain of p53 involved in oligomerization. Oncogene 8: 1693-1696, 1993
    • (1993) Oncogene , vol.8 , pp. 1693-1696
    • Iwabuchi, K.1    Li, B.2    Bartei, P.3    Fields, S.4
  • 69
    • 0029617851 scopus 로고
    • Protein phosphatase 1 interacts with p53BP2, a protein which binds to the tumour supressor p53
    • Helps NR, Barker HM, Elledge SJ, Cohen PTW: Protein phosphatase 1 interacts with p53BP2, a protein which binds to the tumour supressor p53. FEBS Lett 377: 295-300, 1995
    • (1995) FEBS Lett , vol.377 , pp. 295-300
    • Helps, N.R.1    Barker, H.M.2    Elledge, S.J.3    Cohen, P.T.W.4
  • 70
    • 0028966941 scopus 로고
    • p53 is phosphorylated in vitro and in vivo by an ultra-violet radiation-induced protein kinase characteristic of the c-Jun kinase, JNK-1
    • Milne DM, Campbell L, Campbell DG, Meek DW: p53 is phosphorylated in vitro and in vivo by an ultra-violet radiation-induced protein kinase characteristic of the c-Jun kinase, JNK-1. J Biol Chem 270: 5511-5518, 1995
    • (1995) J Biol Chem , vol.270 , pp. 5511-5518
    • Milne, D.M.1    Campbell, L.2    Campbell, D.G.3    Meek, D.W.4


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