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Volumn 89, Issue , 2003, Pages 1-34

Mdm2: A regulator of cell growth and death

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN MDM2; PROTEIN P53; MDM2 PROTEIN, HUMAN; MESSENGER RNA; NUCLEAR PROTEIN; ONCOPROTEIN; UBIQUITIN PROTEIN LIGASE;

EID: 0642368221     PISSN: 0065230X     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0065-230X(03)01001-7     Document Type: Article
Times cited : (55)

References (202)
  • 3
    • 0036247821 scopus 로고    scopus 로고
    • p53-Mdm2: The affair that never ends
    • Alarcon-Vargas, D., and Ronai, Z. (2002). p53-Mdm2: The affair that never ends. Carcinogenesis 23, 541-547.
    • (2002) Carcinogenesis , vol.23 , pp. 541-547
    • Alarcon-Vargas, D.1    Ronai, Z.2
  • 4
    • 0034818446 scopus 로고    scopus 로고
    • Post-translational modifications and activation of p53 by genotoxic stresses
    • Appella, E., and Anderson, C. W. (2001). Post-translational modifications and activation of p53 by genotoxic stresses. Eur. J. Biochem. 268, 2764-2772.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 2764-2772
    • Appella, E.1    Anderson, C.W.2
  • 5
    • 0036318662 scopus 로고    scopus 로고
    • Transcriptional regulation of the mdm2 oncogene by p53 requires TRRAP acetyltransferase complexes
    • Ard, P. G., Chatterjee, C., Kunjibettu, S., Adside, L. R., Gralinski, L. E., and McMahon, S. B. (2002). Transcriptional regulation of the mdm2 oncogene by p53 requires TRRAP acetyltransferase complexes. Mol. Cell. Biol. 22, 5650-5661.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 5650-5661
    • Ard, P.G.1    Chatterjee, C.2    Kunjibettu, S.3    Adside, L.R.4    Gralinski, L.E.5    McMahon, S.B.6
  • 7
    • 0034157875 scopus 로고    scopus 로고
    • Mammalian tumor susceptibility gene 101 (TSG101) and the yeast homologue, Vps23p, both function in late endosomal trafficking
    • Babst, M., Odorizzi, G., Estepa, E. J., and Emr, S. D. (2000). Mammalian tumor susceptibility gene 101 (TSG101) and the yeast homologue, Vps23p, both function in late endosomal trafficking. Traffic 1, 248-258.
    • (2000) Traffic , vol.1 , pp. 248-258
    • Babst, M.1    Odorizzi, G.2    Estepa, E.J.3    Emr, S.D.4
  • 8
    • 0033536230 scopus 로고    scopus 로고
    • Mdm2 binds p73α without targeting degradation
    • Balint, E., Bates, S., and Vousden, K. H. (1999). Mdm2 binds p73α without targeting degradation. Oncogene 18, 3923-3929.
    • (1999) Oncogene , vol.18 , pp. 3923-3929
    • Balint, E.1    Bates, S.2    Vousden, K.H.3
  • 9
    • 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., and Prives, C. (2002). The proline-rich domain of p53 is required for cooperation with anti-neoplastic agents to promote apoptosis of tumor cells. Oncogene 21, 9-21.
    • (2002) Oncogene , vol.21 , pp. 9-21
    • Baptiste, N.1    Friedlander, P.2    Chen, X.3    Prives, C.4
  • 10
    • 0036145018 scopus 로고    scopus 로고
    • Multiple roles of the tumor suppressor p53
    • Bargonetti, J., and Manfredi, J. J. (2002). Multiple roles of the tumor suppressor p53. Curr. Opin. Oncol. 14, 86-91.
    • (2002) Curr. Opin. Oncol. , vol.14 , pp. 86-91
    • Bargonetti, J.1    Manfredi, J.J.2
  • 11
    • 0035694469 scopus 로고    scopus 로고
    • Acetylation of p53 activates transcription through recruitment of coactivators/histone acetyltransferases
    • Barlev, N. A., Liu, L., Chehab, N. H., Mansfieild, K., Harris, K. G., Halazonetis, T. D., and Berger, S. L. (2001). Acetylation of p53 activates transcription through recruitment of coactivators/histone acetyltransferases. Mol. Cell 8, 1243-1254.
    • (2001) Mol. Cell , vol.8 , pp. 1243-1254
    • Barlev, N.A.1    Liu, L.2    Chehab, N.H.3    Mansfieild, K.4    Harris, K.G.5    Halazonetis, T.D.6    Berger, S.L.7
  • 12
    • 0036655060 scopus 로고    scopus 로고
    • Alternative and aberrant splicing of MDM2 mRNA in human cancer
    • Bartel, F., Taubert, H., and Harris, L. C. (2002). Alternative and aberrant splicing of MDM2 mRNA in human cancer. Cancer Cell 2, 9-15.
    • (2002) Cancer Cell , vol.2 , pp. 9-15
    • Bartel, F.1    Taubert, H.2    Harris, L.C.3
  • 16
    • 0036340096 scopus 로고    scopus 로고
    • Hypophosphorylation of Mdm2 augments p53 stability
    • Blattner, C., Hay, T., Meek, D. W., and Lane, D. P. (2002). Hypophosphorylation of Mdm2 augments p53 stability. Mol. Cell. Biol. 22, 6170-6182.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 6170-6182
    • Blattner, C.1    Hay, T.2    Meek, D.W.3    Lane, D.P.4
  • 17
    • 0030965298 scopus 로고    scopus 로고
    • Tolerance of high levels of wild-type p53 in transformed epithelial cells dependent on auto-regulation by mdm-2
    • Blaydes, J. P., Gire, V., Rowson, J. M., and Wynford-Thomas, D. (1997). Tolerance of high levels of wild-type p53 in transformed epithelial cells dependent on auto-regulation by mdm-2. Oncogene 14, 1859-1868.
    • (1997) Oncogene , vol.14 , pp. 1859-1868
    • Blaydes, J.P.1    Gire, V.2    Rowson, J.M.3    Wynford-Thomas, D.4
  • 18
    • 0028277934 scopus 로고
    • The p53-associated protein MDM2 contains a newly characterized zinc-binding domain called the RING finger
    • Boddy, M. N., Freemont, P. S., and Borden, K. L. (1994). The p53-associated protein MDM2 contains a newly characterized zinc-binding domain called the RING finger. Trends Biochem. Sci. 19, 198-199.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 198-199
    • Boddy, M.N.1    Freemont, P.S.2    Borden, K.L.3
  • 19
    • 0031282325 scopus 로고    scopus 로고
    • Design of synthetic Mdm2-binding mini protein that activates the p53 response in vivo
    • Bottger, A., Bottger, V., Sparks, A., Liu, W.-L., Howard, S. F., and Lane, D. P. (1997). Design of synthetic Mdm2-binding mini protein that activates the p53 response in vivo. Curr. Biol. 7, 860-869.
    • (1997) Curr. Biol. , vol.7 , pp. 860-869
    • Bottger, A.1    Bottger, V.2    Sparks, A.3    Liu, W.-L.4    Howard, S.F.5    Lane, D.P.6
  • 21
    • 0032080297 scopus 로고    scopus 로고
    • The human oncoprotein MDM2 arrests the cell cycle: Elimination of its cell-cycle-inhibitory function induces tumorigenesis
    • Brown, D. R., Thomas, C. A., and Deb, S. P. (1998). The human oncoprotein MDM2 arrests the cell cycle: Elimination of its cell-cycle-inhibitory function induces tumorigenesis. EMBO J. 17, 2513-2525.
    • (1998) EMBO J. , vol.17 , pp. 2513-2525
    • Brown, D.R.1    Thomas, C.A.2    Deb, S.P.3
  • 25
    • 0035798613 scopus 로고    scopus 로고
    • The Mdm-2 amino terminus is required for Mdm2 binding and SUMO-1 conjugation by the E2 Sumo-1 conjugation enzyme Ubc9
    • Buschmann, T., Lerner, D., Lee, C.-G., and Ronai, Z. (2001a). The Mdm-2 amino terminus is required for Mdm2 binding and SUMO-1 conjugation by the E2 Sumo-1 conjugation enzyme Ubc9. J. Biol. Chem. 276, 40389-40395.
    • (2001) J. Biol. Chem. , vol.276 , pp. 40389-40395
    • Buschmann, T.1    Lerner, D.2    Lee, C.-G.3    Ronai, Z.4
  • 28
    • 0023339504 scopus 로고
    • Molecular analysis and chromosomal mapping of amplified genes isolated from a transformed mouse 3T3 cell line
    • Cahilly-Snyder, L., Yang-Feng, T., Francke, U., and George, D. L. (1987). Molecular analysis and chromosomal mapping of amplified genes isolated from a transformed mouse 3T3 cell line. Somat. Cell Mol. Genet. 13, 235-244.
    • (1987) Somat. Cell Mol. Genet. , vol.13 , pp. 235-244
    • Cahilly-Snyder, L.1    Yang-Feng, T.2    Francke, U.3    George, D.L.4
  • 30
    • 0033059183 scopus 로고    scopus 로고
    • Dose-dependent effects of DNA-damaging agents on p53-mediated cell cycle arrest
    • Chang, D., Chen, F., Zhang, F., McKay, B. C., and Ljungman, M. (1999). Dose-dependent effects of DNA-damaging agents on p53-mediated cell cycle arrest. Cell Growth Differ. 10, 155-162.
    • (1999) Cell Growth Differ. , vol.10 , pp. 155-162
    • Chang, D.1    Chen, F.2    Zhang, F.3    McKay, B.C.4    Ljungman, M.5
  • 32
    • 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. (2000). p53 transcriptional activity is essential for p53-dependent apoptosis following DNA damage. EMBO J. 19, 4967-4975.
    • (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
  • 33
    • 0034716943 scopus 로고    scopus 로고
    • A small synthetic peptide, which inhibits the p53-hdm2 interaction, stimulates the p53 pathway in tumor cell lines
    • Chene, P., Fuchs, J., Bohn, J., Garcia-Echeverria, C., Furet, P., and Fabbro, D. (2000). A small synthetic peptide, which inhibits the p53-hdm2 interaction, stimulates the p53 pathway in tumor cell lines. J. Mol. Biol. 299, 245-253.
    • (2000) J. Mol. Biol. , vol.299 , pp. 245-253
    • Chene, P.1    Fuchs, J.2    Bohn, J.3    Garcia-Echeverria, C.4    Furet, P.5    Fabbro, D.6
  • 34
    • 0027983669 scopus 로고
    • Crystal structure of a p53 tumor suppressor-DNA complex: Understanding tumorigenic mutations
    • Cho, Y., Gorina, S., Jeffrey, P.D., and Pavletich, N. P. (1994). Crystal structure of a p53 tumor suppressor-DNA complex: Understanding tumorigenic mutations. Science 265, 346-355.
    • (1994) Science , vol.265 , pp. 346-355
    • Cho, Y.1    Gorina, S.2    Jeffrey, P.D.3    Pavletich, N.P.4
  • 36
    • 0024431720 scopus 로고    scopus 로고
    • Nuclear and nucleolar targeting sequences of c-erb-A, c-myb, N-myc, p53, HSP70, and HIV tat proteins
    • Dang, C. V., and Lee, W. M. F. (1999). Nuclear and nucleolar targeting sequences of c-erb-A, c-myb, N-myc, p53, HSP70, and HIV tat proteins. J. Biol. Chem. 264, 18019-18023.
    • (1999) J. Biol. Chem. , vol.264 , pp. 18019-18023
    • Dang, C.V.1    Lee, W.M.F.2
  • 39
    • 0028978183 scopus 로고
    • CIP1/WAF1 undergo normal development, but are defective in G1 checkpoint control
    • CIP1/WAF1 undergo normal development, but are defective in G1 checkpoint control. Cell 82, 675-684.
    • (1995) Cell , vol.82 , pp. 675-684
    • Deng, C.1    Zhang, P.2    Harper, J.W.3    Elledge, S.J.4    Leder, P.5
  • 40
    • 0034710940 scopus 로고    scopus 로고
    • Peg3/Pw1 promotes p53-mediated apoptosis by inducing Bax translocation from cytosol to mitochondria
    • Deng, Y., and Wu, X. (2000). Peg3/Pw1 promotes p53-mediated apoptosis by inducing Bax translocation from cytosol to mitochondria. Proc. Natl. Acad. Sci. USA 97, 12050-12055.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 12050-12055
    • Deng, Y.1    Wu, X.2
  • 41
    • 0032951530 scopus 로고    scopus 로고
    • p73 function is inhibited by tumor-derived p53 mutants in mammalian cells
    • Di Como, C. J., Gaiddon, C., and Prives, C. (1999). p73 function is inhibited by tumor-derived p53 mutants in mammalian cells. Mol. Cell. Biol. 19, 1438-1449.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 1438-1449
    • Di Como, C.J.1    Gaiddon, C.2    Prives, C.3
  • 42
    • 0032407889 scopus 로고    scopus 로고
    • The large T antigen of simian virus 40 binds and inactivates p53 but not p73
    • Dobbelstein, M., and Roth, J. (1998). The large T antigen of simian virus 40 binds and inactivates p53 but not p73. J. Gen. Virol. 79, 3079-3083.
    • (1998) J. Gen. Virol. , vol.79 , pp. 3079-3083
    • Dobbelstein, M.1    Roth, J.2
  • 43
    • 0033602462 scopus 로고    scopus 로고
    • Inactivation of the p53-homologue p73 by the mdm2-oncoprotein
    • Dobbelstein, M., Wienzek, S., Konig, C., and Roth, J. (1999). Inactivation of the p53-homologue p73 by the mdm2-oncoprotein. Oncogene 18, 2101-2106.
    • (1999) Oncogene , vol.18 , pp. 2101-2106
    • Dobbelstein, M.1    Wienzek, S.2    Konig, C.3    Roth, J.4
  • 44
    • 0029590161 scopus 로고
    • MDM2 transformation in the absence of p53 and abrogation of the p107 G1 cell-cycle arrest
    • Dubs-Poterszman, M. C., Tocque, B., and Wasylyk, B. (1995). MDM2 transformation in the absence of p53 and abrogation of the p107 G1 cell-cycle arrest. Oncogene 11, 2445-2449.
    • (1995) Oncogene , vol.11 , pp. 2445-2449
    • Dubs-Poterszman, M.C.1    Tocque, B.2    Wasylyk, B.3
  • 45
    • 0028220204 scopus 로고
    • p53-dependent inhibition of cyclin-dependent kinase activities in human fibroblasts during radiation-induced G1 arrest
    • Dulic, V., Kaufmann, W. K., Wilson, S. J., Tisty, T. D., Less, E., Harper, J. W., Elledge, S. J., and Reed, S. I. (1994). p53-dependent inhibition of cyclin-dependent kinase activities in human fibroblasts during radiation-induced G1 arrest. Cell 76, 1013-1023.
    • (1994) Cell , vol.76 , pp. 1013-1023
    • Dulic, V.1    Kaufmann, W.K.2    Wilson, S.J.3    Tisty, T.D.4    Less, E.5    Harper, J.W.6    Elledge, S.J.7    Reed, S.I.8
  • 47
    • 0029760621 scopus 로고    scopus 로고
    • The MDM2 oncoprotein binds specifically to RNA through its RING finger domain
    • Elenbaas, B., Dobbelstein, M., Roth, J., Shenk, T., and Levine, A. J. (1996). The MDM2 oncoprotein binds specifically to RNA through its RING finger domain. Mol. Med. 2, 439-451.
    • (1996) Mol. Med. , vol.2 , pp. 439-451
    • Elenbaas, B.1    Dobbelstein, M.2    Roth, J.3    Shenk, T.4    Levine, A.J.5
  • 48
    • 0034881964 scopus 로고    scopus 로고
    • Transcriptional regulation by p53 through intrinsic DNA/chromatin binding and site-directed cofactor recruitment
    • Espinosa, J. M., and Emerson, B. M. (2001). Transcriptional regulation by p53 through intrinsic DNA/chromatin binding and site-directed cofactor recruitment. Mol. Cell 8, 57-69.
    • (2001) Mol. Cell , vol.8 , pp. 57-69
    • Espinosa, J.M.1    Emerson, B.M.2
  • 49
    • 0035811563 scopus 로고    scopus 로고
    • An alternatively spliced HDM2 product increases p53 activity by inhibiting HDM2
    • Evans, S. C., Viswanathan, M., Grier, J. D., Narayana, M., El-Naggar, A. K., and Lozano, G. (2001). An alternatively spliced HDM2 product increases p53 activity by inhibiting HDM2. Oncogens 20, 4041-4049.
    • (2001) Oncogens , vol.20 , pp. 4041-4049
    • Evans, S.C.1    Viswanathan, M.2    Grier, J.D.3    Narayana, M.4    El-Naggar, A.K.5    Lozano, G.6
  • 51
    • 0025853776 scopus 로고
    • Tumorigenic potential associated with enhanced expression of a gene that is amplified in a mouse tumor cell line
    • Fakharzadeh, S. S., Trusko, S. P., and George, D. L. (1991). Tumorigenic potential associated with enhanced expression of a gene that is amplified in a mouse tumor cell line. EMBO J. 10, 1656-1659.
    • (1991) EMBO J. , vol.10 , pp. 1656-1659
    • Fakharzadeh, S.S.1    Trusko, S.P.2    George, D.L.3
  • 52
    • 0034708458 scopus 로고    scopus 로고
    • Mdm2 is a RING finger-dependent ubiquitin protein ligase for itself and p53
    • Fang, S., Jensen, J. P., Ludwig, R. L., Vousden, K. H., and Weissman, A. M. (2000). Mdm2 Is a RING finger-dependent ubiquitin protein ligase for itself and p53. J. Biol. Chem. 275, 8945-8951.
    • (2000) J. Biol. Chem. , vol.275 , pp. 8945-8951
    • Fang, S.1    Jensen, J.P.2    Ludwig, R.L.3    Vousden, K.H.4    Weissman, A.M.5
  • 56
    • 0032512057 scopus 로고    scopus 로고
    • Mdm2 association with p53 targets its ubiquitination
    • Fuchs, S. Y., Adler, V., Buschmann, T., Wu, X., and Ronai, Z. (1998a). Mdm2 association with p53 targets its ubiquitination. Oncogene 17, 2543-2547.
    • (1998) Oncogene , vol.17 , pp. 2543-2547
    • Fuchs, S.Y.1    Adler, V.2    Buschmann, T.3    Wu, X.4    Ronai, Z.5
  • 57
    • 0032169459 scopus 로고    scopus 로고
    • JNK targets p53 ubiquitination and degradation in nonstressed cells
    • Fuchs, S. Y., Adler, V., Buschmann, T., Yin, Z., Wu, X., Jones, S. J., and Ronai, Z. (1998b). JNK targets p53 ubiquitination and degradation in nonstressed cells. Genes Dev. 12, 2658-2663.
    • (1998) Genes Dev. , vol.12 , pp. 2658-2663
    • Fuchs, S.Y.1    Adler, V.2    Buschmann, T.3    Yin, Z.4    Wu, X.5    Jones, S.J.6    Ronai, Z.7
  • 60
    • 0030575866 scopus 로고    scopus 로고
    • Structure of the p53 tumor suppressor bound to the ankyrin and SH3 domains of 53BP2
    • Gorina, S., and Pavletich, N. P. (1996). Structure of the p53 tumor suppressor bound to the ankyrin and SH3 domains of 53BP2. Science 274, 1001-1005.
    • (1996) Science , vol.274 , pp. 1001-1005
    • Gorina, S.1    Pavletich, N.P.2
  • 62
    • 85047680162 scopus 로고    scopus 로고
    • p53 accumulates but is functionally impaired when DNA synthesis is blocked
    • Gottifredi, V., Shieh, S.-Y., Taya, Y., and Prives, C. (2001). p53 accumulates but is functionally impaired when DNA synthesis is blocked. Proc. Natl. Acad. Sci. USA 98, 1036-1041.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 1036-1041
    • Gottifredi, V.1    Shieh, S.-Y.2    Taya, Y.3    Prives, C.4
  • 64
    • 0033956689 scopus 로고    scopus 로고
    • Identification of a sequence element from p53 that signals for Mdm2-targeted degradation
    • Gu, J., Chen, D., Rosenblum, J., Rubin, R. M., and Yuan, Z.-M. (2000). Identification of a sequence element from p53 that signals for Mdm2-targeted degradation. mol. Cell. Biol. 20, 1243-1253.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 1243-1253
    • Gu, J.1    Chen, D.2    Rosenblum, J.3    Rubin, R.M.4    Yuan, Z.-M.5
  • 66
    • 0030797585 scopus 로고    scopus 로고
    • Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain
    • Gu, W., and Roeder, R. G. (1997). Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain. Cell 9, 595-596.
    • (1997) Cell , vol.9 , pp. 595-596
    • Gu, W.1    Roeder, R.G.2
  • 67
    • 0025161991 scopus 로고
    • Protein-mediated nuclear export of RNA: 5S rRNA containing small RNPs in Xenopus oocytes
    • Guddat, U., Bakken, A. H., and Pieler, T. (1990). Protein-mediated nuclear export of RNA: 5S rRNA containing small RNPs in Xenopus oocytes. Cell 60, 619-628.
    • (1990) Cell , vol.60 , pp. 619-628
    • Guddat, U.1    Bakken, A.H.2    Pieler, T.3
  • 69
    • 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., and Elledge, S. J. (1993). The p21 Cdk-interacting protein Cip1 is a potent inhibitor of G1 cyclin-dependent kinases. Cell 75, 805-816.
    • (1993) Cell , vol.75 , pp. 805-816
    • Harper, J.W.1    Adami, G.R.2    Wei, N.3    Keyomarsi, K.4    Elledge, S.J.5
  • 70
    • 0030905284 scopus 로고    scopus 로고
    • Mdm2 promotes the rapid degradation of p53
    • Haupt, Y., Maya, R., Kazaz, A., and Oren, M. (1997). Mdm2 promotes the rapid degradation of p53. Nature 387, 296-299.
    • (1997) Nature , vol.387 , pp. 296-299
    • Haupt, Y.1    Maya, R.2    Kazaz, A.3    Oren, M.4
  • 71
    • 0034726060 scopus 로고    scopus 로고
    • Multiple sites of in vivo phosphorylation in the MDM2 oncoprotein cluster within two important functional domains
    • Hay, T. J., and Meek, D. W. (2000). Multiple sites of in vivo phosphorylation in the MDM2 oncoprotein cluster within two important functional domains. FEBS Lett. 478, 183-186.
    • (2000) FEBS Lett. , vol.478 , pp. 183-186
    • Hay, T.J.1    Meek, D.W.2
  • 72
    • 0034725918 scopus 로고    scopus 로고
    • Biochemistry: All in the ubiquitin family
    • Hochstrasser, M. (2000). Biochemistry: All in the ubiquitin family. Science 289, 563-564.
    • (2000) Science , vol.289 , pp. 563-564
    • Hochstrasser, M.1
  • 73
    • 0025204548 scopus 로고
    • Bcl-2 is an inner mitochondrial membrane protein that blocks programmed cell death
    • Hockenberry, D., Nunez, G., Milliman, C, Schreiber, R. D., and Korsmeyer, S. J. (1990). Bcl-2 is an inner mitochondrial membrane protein that blocks programmed cell death. Nature 348, 334-336.
    • (1990) Nature , vol.348 , pp. 334-336
    • Hockenberry, D.1    Nunez, G.2    Milliman, C.3    Schreiber, R.D.4    Korsmeyer, S.J.5
  • 74
    • 0033521621 scopus 로고    scopus 로고
    • ARF with Mdm2 inhibits ubiquitin ligase activity of Mdm2 for tumor suppressor p53
    • ARF with Mdm2 inhibits ubiquitin ligase activity of Mdm2 for tumor suppressor p53. EMBO J. 18, 22-27.
    • (1999) EMBO J. , vol.18 , pp. 22-27
    • Honda, R.1    Yasuda, H.2
  • 75
    • 0033082231 scopus 로고    scopus 로고
    • RB regulates the stability and the apoptotic function of p53 via MDM2
    • Hsieh, J.-K., Chan, F. S. G., O'Connor, D. J., Mittnacht, S., Zhong, S., and Lu, X. (1999). RB regulates the stability and the apoptotic function of p53 via MDM2. Mol. Cell 3, 181-193.
    • (1999) Mol. Cell , vol.3 , pp. 181-193
    • Hsieh, J.-K.1    Chan, F.S.G.2    O'Connor, D.J.3    Mittnacht, S.4    Zhong, S.5    Lu, X.6
  • 76
    • 0035977064 scopus 로고    scopus 로고
    • MDM2 can promote the ubiquitination, nuclear export, and degradation of p53 in the absence of direct binding
    • Inoue, T., Geyer, R. K., Howard, D., Yu, Z. K., and Maki, C. G. (2001). MDM2 can promote the ubiquitination, nuclear export, and degradation of p53 in the absence of direct binding. J. Biol. Chem. 276, 45255-45260.
    • (2001) J. Biol. Chem. , vol.276 , pp. 45255-45260
    • Inoue, T.1    Geyer, R.K.2    Howard, D.3    Yu, Z.K.4    Maki, C.G.5
  • 77
    • 0022646788 scopus 로고
    • Localization of gene for human p53 tumour antigen to band 17p13
    • Isobe, M., Emanuel, B. S., Givol, D., Oren, M., and Croce, C. M. (1986). Localization of gene for human p53 tumour antigen to band 17p13. Nature 320, 84-85.
    • (1986) Nature , vol.320 , pp. 84-85
    • Isobe, M.1    Emanuel, B.S.2    Givol, D.3    Oren, M.4    Croce, C.M.5
  • 78
    • 0035868964 scopus 로고    scopus 로고
    • p300/CBP-mediated p53 acetylation is commonly induced by p53-activating agents and inhibited by MDM2
    • Ito, A., Lai, C.-H., Zhao, X., Saito, S., Hamilton, M. H., Appella, E., and Yao, T.-P. (2001). p300/CBP-mediated p53 acetylation is commonly induced by p53-activating agents and inhibited by MDM2. EMBO J. 20, 1131-1340.
    • (2001) EMBO J. , vol.20 , pp. 1131-1340
    • Ito, A.1    Lai, C.-H.2    Zhao, X.3    Saito, S.4    Hamilton, M.H.5    Appella, E.6    Yao, T.-P.7
  • 80
    • 0033963335 scopus 로고    scopus 로고
    • MdmX protects p53 from Mdm2-mediated degradation
    • Jackson, M. W., and Berberich, S. J. (2000). MdmX protects p53 from Mdm2-mediated degradation. Mol. Cell. Biol. 20, 1001-1007.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 1001-1007
    • Jackson, M.W.1    Berberich, S.J.2
  • 82
    • 0035957007 scopus 로고    scopus 로고
    • RB induces Sp1 activity by relieving inhibition mediated by MDM2
    • Johnson-Pais, T., Degnin, C., and Thayer, M. J. (2001). pRB induces Sp1 activity by relieving inhibition mediated by MDM2. Proc. Natl. Acad. Sci. USA 98, 2211-2216.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 2211-2216
    • Johnson-Pais, T.1    Degnin, C.2    Thayer, M.J.3
  • 83
    • 0032417695 scopus 로고    scopus 로고
    • Overexpression of Mdm2 in mice reveals a p53-independent role for Mdm2 in tumorigenesis
    • Jones, S. N., Hancock, A. R., Vogel, H., Donehower, L. A., and Bradley, A. (1998). Overexpression of Mdm2 in mice reveals a p53-independent role for Mdm2 in tumorigenesis. Proc. Natl. Acad. Sci. USA 95, 15608-15612.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 15608-15612
    • Jones, S.N.1    Hancock, A.R.2    Vogel, H.3    Donehower, L.A.4    Bradley, A.5
  • 84
    • 0028834902 scopus 로고
    • Rescue of embryonic lethality in Mdm2-deficient mice by absence of p53
    • Jones, S. N., Roe, A. E., Donehower, L. A., and Bradley, A. (1995). Rescue of embryonic lethality in Mdm2-deficient mice by absence of p53. Nature 378, 206-208.
    • (1995) Nature , vol.378 , pp. 206-208
    • Jones, S.N.1    Roe, A.E.2    Donehower, L.A.3    Bradley, A.4
  • 85
    • 0031564954 scopus 로고    scopus 로고
    • p73 is a human p53-related protein that can induce apoptosis
    • Jost, C. A., Marin, M. C., and Kaelin, W. G., Jr. (1997). p73 is a human p53-related protein that can induce apoptosis. Nature 389, 191-194.
    • (1997) Nature , vol.389 , pp. 191-194
    • Jost, C.A.1    Marin, M.C.2    Kaelin Jr., W.G.3
  • 87
    • 0034921151 scopus 로고    scopus 로고
    • Regulation of p63 function by Mdm2 and MdmX
    • Kadakia, M., Slader, C., and Berberich, S. J. (2001). Regulation of p63 function by Mdm2 and MdmX. DNA Cell Biol. 20, 321-330.
    • (2001) DNA Cell Biol. , vol.20 , pp. 321-330
    • Kadakia, M.1    Slader, C.2    Berberich, S.J.3
  • 91
    • 0033592868 scopus 로고    scopus 로고
    • Rapid ATM-dependent phosphorylation of MDM2 precedes p53 accumulation in response to DNA damage
    • Khosravi, R., Maya, R., Gottlieb, T., Oren, M., Shiloh, Y., and Shkedy, D. (1999). Rapid ATM-dependent phosphorylation of MDM2 precedes p53 accumulation in response to DNA damage. Proc. Natl. Acad. Sci. USA 96, 14973-14977.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 14973-14977
    • Khosravi, R.1    Maya, R.2    Gottlieb, T.3    Oren, M.4    Shiloh, Y.5    Shkedy, D.6
  • 92
    • 0029972806 scopus 로고    scopus 로고
    • p53: Puzzle and paradigm
    • Ko, L. J., and Prives, C. (1996). p53: Puzzle and paradigm. Genes Dev. 10, 1054-1072.
    • (1996) Genes Dev. , vol.10 , pp. 1054-1072
    • Ko, L.J.1    Prives, C.2
  • 93
    • 0033732303 scopus 로고    scopus 로고
    • MDM2 inhibits p300-mediated p53 acetylation and activation by forming a ternary complex with the two proteins
    • Kobet, E., Zeng, X., Zhu, Y., Keller, D., and Lu, H. (2000). MDM2 inhibits p300-mediated p53 acetylation and activation by forming a ternary complex with the two proteins. Proc. Natl. Acad. Sci. USA 97, 12547-12552.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 12547-12552
    • Kobet, E.1    Zeng, X.2    Zhu, Y.3    Keller, D.4    Lu, H.5
  • 94
    • 0031201741 scopus 로고    scopus 로고
    • TSG101 may be the prototype of a class of dominant negative ubiquitin regulators
    • Koonin, E. V., and Abagyan, R. A. (1997). TSG101 may be the prototype of a class of dominant negative ubiquitin regulators. Nature Genet. 16, 330-331.
    • (1997) Nature Genet. , vol.16 , pp. 330-331
    • Koonin, E.V.1    Abagyan, R.A.2
  • 95
    • 0030965946 scopus 로고    scopus 로고
    • Regulation of p53 stability by Mdm2
    • Kubbutat, M. H. G., Jones, S. N., and Vousden, K. H. (1997). Regulation of p53 stability by Mdm2. Nature 387, 299-303.
    • (1997) Nature , vol.387 , pp. 299-303
    • Kubbutat, M.H.G.1    Jones, S.N.2    Vousden, K.H.3
  • 96
    • 0030575937 scopus 로고    scopus 로고
    • Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain
    • Kussie, P. H., Gorina, S., Marechal, V., Elenbaas, B., Moreau, J., Levine, A. J., and Pavletich, N. P. (1996). Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain. Science 274, 948-953.
    • (1996) Science , vol.274 , pp. 948-953
    • Kussie, P.H.1    Gorina, S.2    Marechal, V.3    Elenbaas, B.4    Moreau, J.5    Levine, A.J.6    Pavletich, N.P.7
  • 97
    • 0035799530 scopus 로고    scopus 로고
    • Functional analysis and intracellular localization of p53 modified by SUMO-1
    • Kwek, S. S. S., Derry, J., Tyner, A. L., Shen, Z., and Gudkov, A. V. (2001). Functional analysis and intracellular localization of p53 modified by SUMO-1. Oncogene 20, 2587-2599.
    • (2001) Oncogene , vol.20 , pp. 2587-2599
    • Kwek, S.S.S.1    Derry, J.2    Tyner, A.L.3    Shen, Z.4    Gudkov, A.V.5
  • 99
    • 0028938539 scopus 로고
    • Human oncoprotein MDM2 interacts with the TATA-binding protein in vitro and in vivo
    • Leng, P., Brown, D. R., Deb, S., and Deb, S. P. (1995). Human oncoprotein MDM2 interacts with the TATA-binding protein in vitro and in vivo. Int. J. Oncol. 6, 251-259.
    • (1995) Int. J. Oncol. , vol.6 , pp. 251-259
    • Leng, P.1    Brown, D.R.2    Deb, S.3    Deb, S.P.4
  • 100
    • 1842378642 scopus 로고    scopus 로고
    • II250 and is required for MDM2 regulation of the cyclin a promoter
    • II250 and is required for MDM2 regulation of the cyclin A promoter. J. Biol. Chem. 272, 30651-30661.
    • (1997) J. Biol. Chem. , vol.272 , pp. 30651-30661
    • Leveillard, T.1    Wasylyk, B.2
  • 101
    • 0030941458 scopus 로고    scopus 로고
    • p53, the cellular gatekeeper for growth and division
    • Levine, A. J. (1997). p53, the cellular gatekeeper for growth and division. Cell 88, 323-331.
    • (1997) Cell , vol.88 , pp. 323-331
    • Levine, A.J.1
  • 102
    • 8944239884 scopus 로고    scopus 로고
    • High-risk human papillomavirus E6 protein has two distinct binding sites within p53, of which only one determines degradation
    • Li, X., and Coffino, P. (1996). High-risk human papillomavirus E6 protein has two distinct binding sites within p53, of which only one determines degradation. J. Virol. 70, 4509-4516.
    • (1996) J. Virol. , vol.70 , pp. 4509-4516
    • Li, X.1    Coffino, P.2
  • 103
    • 0035852716 scopus 로고    scopus 로고
    • ATSG101/MDM2 regulatory loop modulates MDM2 degradation and MDM2/p53 feedback control
    • Li, L., Liao, J., Ruland, J., Mak, T. W., and Cohen, S. N. (2001). ATSG101/MDM2 regulatory loop modulates MDM2 degradation and MDM2/p53 feedback control. Proc. Natl. Acad. Sci. USA 98, 1619-1624.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 1619-1624
    • Li, L.1    Liao, J.2    Ruland, J.3    Mak, T.W.4    Cohen, S.N.5
  • 104
    • 0036683093 scopus 로고    scopus 로고
    • Phosphorylation-dependent ubiquitination and degradation of androgen receptor by Akt require Mdm2 ligase
    • Lin, H.-K., Wang, L., Hu, Y.-C., Altuwaijri, S., and Chang, C. (2002). Phosphorylation-dependent ubiquitination and degradation of androgen receptor by Akt require Mdm2 ligase. EMBO J. 21, 4037-4048.
    • (2002) EMBO J. , vol.21 , pp. 4037-4048
    • Lin, H.-K.1    Wang, L.2    Hu, Y.-C.3    Altuwaijri, S.4    Chang, C.5
  • 106
    • 0033998439 scopus 로고    scopus 로고
    • Apoptotic and growth-promoting activity of E2F modulated by MDM2
    • Loughran, O., and La Thangue, N. B. (2000). Apoptotic and growth-promoting activity of E2F modulated by MDM2. Mol. Cell. Biol. 20, 2186-2197.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 2186-2197
    • Loughran, O.1    La Thangue, N.B.2
  • 107
    • 0028979005 scopus 로고
    • II31 protein is a transcriptional coactivator of the p53 protein
    • II31 protein is a transcriptional coactivator of the p53 protein. Proc. Natl. Acad. Sci. USA 92, 5154-5158.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 5154-5158
    • Lu, H.1    Levine, A.J.2
  • 108
    • 0035300512 scopus 로고    scopus 로고
    • Alternative and aberrant messenger RNA splicing of the mdm2 oncogene in invasive breast cancer
    • Lukas, J., Gao, D.-Q., Keshmeshian, M., Wen, W.-H., Tsao-Wei, D., Rosenberg, S., and Press, M. F. (2001). Alternative and aberrant messenger RNA splicing of the mdm2 oncogene in invasive breast cancer. Cancer Res. 61, 3212-3219.
    • (2001) Cancer Res. , vol.61 , pp. 3212-3219
    • Lukas, J.1    Gao, D.-Q.2    Keshmeshian, M.3    Wen, W.-H.4    Tsao-Wei, D.5    Rosenberg, S.6    Press, M.F.7
  • 109
    • 0027999512 scopus 로고
    • The ribosomal L5 protein is associated with mdm-2 and mdm-2-p53 complexes
    • Marechal, V., Elenbaas, B., Piette, J., Nicolas, J. C., and Levine, A. J. (1994). The ribosomal L5 protein is associated with mdm-2 and mdm-2-p53 complexes. Mol. Cell. Biol. 14, 7414-7420.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 7414-7420
    • Marechal, V.1    Elenbaas, B.2    Piette, J.3    Nicolas, J.C.4    Levine, A.J.5
  • 113
    • 0035949588 scopus 로고    scopus 로고
    • A phosphatidylinositol 3-kinase/Akt pathway promotes translocation of Mdm2 from the cytoplasm to the nucleus
    • Mayo, L. D., and Donner, D. B. (2001). A phosphatidylinositol 3-kinase/Akt pathway promotes translocation of Mdm2 from the cytoplasm to the nucleus. Proc. Natl. Acad. Sci. USA 98, 11598-11603.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 11598-11603
    • Mayo, L.D.1    Donner, D.B.2
  • 114
    • 0030665146 scopus 로고    scopus 로고
    • Mdm-2 phosphorylation by DNA-dependent protein kinases prevents interaction with p53
    • Mayo, L. D., Turchi, J. J., and Berberich, S. J. (1997). Mdm-2 phosphorylation by DNA-dependent protein kinases prevents interaction with p53. Cancer Res. 57, 5013-5016.
    • (1997) Cancer Res. , vol.57 , pp. 5013-5016
    • Mayo, L.D.1    Turchi, J.J.2    Berberich, S.J.3
  • 115
    • 0344246051 scopus 로고
    • The gene for human p53 cellular tumor antigen is located on chromosome 17 short arm (17p13)
    • McBride, O. W., Merry, D., and Givol, D. (1986). The gene for human p53 cellular tumor antigen is located on chromosome 17 short arm (17p13). Proc. Natl. Acad. Sci. USA 83, 130-134.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 130-134
    • McBride, O.W.1    Merry, D.2    Givol, D.3
  • 116
    • 0033993450 scopus 로고    scopus 로고
    • The p53 tumor suppressor protein does not regulate expression of its own inhibitor, MDM2, except under conditions of stress
    • Mendrysa, S. A., and Perry, M. E. (2000). The p53 tumor suppressor protein does not regulate expression of its own inhibitor, MDM2, except under conditions of stress. Mol. Cell. Biol. 20, 2023-2030.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 2023-2030
    • Mendrysa, S.A.1    Perry, M.E.2
  • 117
    • 0036467391 scopus 로고    scopus 로고
    • The p53 and Mdm2 families in cancer
    • Michael, D., and Oren, M. (2002). The p53 and Mdm2 families in cancer. Curr. Opin. Genet. Dev. 12, 53-59.
    • (2002) Curr. Opin. Genet. Dev. , vol.12 , pp. 53-59
    • Michael, D.1    Oren, M.2
  • 120
    • 0028883179 scopus 로고
    • Tumor suppressor p53 is a direct transcriptional activator of the human bax gene
    • Miyashita, T., and Reed, J. C. (1995). Tumor suppressor p53 is a direct transcriptional activator of the human bax gene. Cell 80, 293-299.
    • (1995) Cell , vol.80 , pp. 293-299
    • Miyashita, T.1    Reed, J.C.2
  • 123
    • 0031038269 scopus 로고    scopus 로고
    • Mdm-2: "Big brother" of p53
    • Momand, J., and Zambetti, G. P. (1997). Mdm-2: "Big brother" of p53. J. Cell. Biochem. 64, 343-352.
    • (1997) J. Cell. Biochem. , vol.64 , pp. 343-352
    • Momand, J.1    Zambetti, G.P.2
  • 124
    • 0026649648 scopus 로고
    • The mdm-2 oncogene product forms a complex with the p53 protein and inhibits p53-mediated transactivation
    • Momand, J., Zambetti, G. P., Olson, D. C., George, D., and Levine, A. J. (1992). The mdm-2 oncogene product forms a complex with the p53 protein and inhibits p53-mediated transactivation. Cell 69, 1237-1245.
    • (1992) Cell , vol.69 , pp. 1237-1245
    • Momand, J.1    Zambetti, G.P.2    Olson, D.C.3    George, D.4    Levine, A.J.5
  • 126
    • 0028823020 scopus 로고
    • Rescue of early embryonic lethality in mdm2-deficient mice by deletion of p53
    • Montes de Oca Luna, R., Wagner, D. S., and Lozano, G. (1995). Rescue of early embryonic lethality in mdm2-deficient mice by deletion of p53. Nature 378, 203-206.
    • (1995) Nature , vol.378 , pp. 203-206
    • Montes De Oca Luna, R.1    Wagner, D.S.2    Lozano, G.3
  • 128
    • 0034458966 scopus 로고    scopus 로고
    • Multiple lysine mutatins in the C-terminal domain of p53 interfere with Mdm2-dependent protein degradation and ubiquitination
    • Nakamura, S., Roth, J. A., and Mukhopadhyay, T. (2000). Multiple lysine mutatins in the C-terminal domain of p53 interfere with Mdm2-dependent protein degradation and ubiquitination. Mol. Cell Biol. 20, 9391-9398.
    • (2000) Mol. Cell Biol. , vol.20 , pp. 9391-9398
    • Nakamura, S.1    Roth, J.A.2    Mukhopadhyay, T.3
  • 129
    • 0030826733 scopus 로고    scopus 로고
    • Induced N- and C-terminal cleavage of p53: A core fragment of p53, generated by interaction with damaged DNA, promotes cleavage of the N-terminus of full-length p53, whereas ssDNA induces C-terminal cleavage of p53
    • Okorokov, A. L., Ponchel, E, and Milner, J. (1997). Induced N- and C-terminal cleavage of p53: A core fragment of p53, generated by interaction with damaged DNA, promotes cleavage of the N-terminus of full-length p53, whereas ssDNA induces C-terminal cleavage of p53. EMBO J. 19, 6008-6017.
    • (1997) EMBO J. , vol.19 , pp. 6008-6017
    • Okorokov, A.L.1    Ponchel, E.2    Milner, J.3
  • 130
    • 0026740449 scopus 로고
    • Amplification of a gene encoding a p53-associated protein in human sarcomas
    • Oliner, J. D., Kinzler, K. W., Meltzer, P. S., George, D. L., and Vogelstein, B. (1992). Amplification of a gene encoding a p53-associated protein in human sarcomas. Nature 358, 80-83.
    • (1992) Nature , vol.358 , pp. 80-83
    • Oliner, J.D.1    Kinzler, K.W.2    Meltzer, P.S.3    George, D.L.4    Vogelstein, B.5
  • 134
    • 0022344329 scopus 로고
    • The p53 cellular tumor antigen: Gene structure, expression, and protein properties
    • Oren, M. (1985). The p53 cellular tumor antigen: Gene structure, expression, and protein properties. Biochem. Biophys. Acta. 823, 67-78.
    • (1985) Biochem. Biophys. Acta , vol.823 , pp. 67-78
    • Oren, M.1
  • 138
    • 0034863683 scopus 로고    scopus 로고
    • Rescue of embryonic lethality in Mdm4-null mice by loss of Trp53 suggests a nonoverlapping pathway with MDM2 to regulate p53
    • Parant, J., Chavez-Reyes, A., Little, N. A., Yan, W., Reinke, V., Jochemsem, A. G., and Lozano, G. (2001). Rescue of embryonic lethality in Mdm4-null mice by loss of Trp53 suggests a nonoverlapping pathway with MDM2 to regulate p53. Nature Genet. 29, 92-95.
    • (2001) Nature Genet. , vol.29 , pp. 92-95
    • Parant, J.1    Chavez-Reyes, A.2    Little, N.A.3    Yan, W.4    Reinke, V.5    Jochemsem, A.G.6    Lozano, G.7
  • 141
    • 0034732883 scopus 로고    scopus 로고
    • p53 mutational spectra and the role of methylated CpG sequences
    • Pfeifer, G. P. (2000). p53 mutational spectra and the role of methylated CpG sequences. Mutat. Res. 450, 155-166.
    • (2000) Mutat. Res. , vol.450 , pp. 155-166
    • Pfeifer, G.P.1
  • 144
    • 0031180564 scopus 로고    scopus 로고
    • The breast cancer gene product TSG101: A regulator of ubiquitination?
    • Ponting, C. P., Cai, Y. D., and Bork, P. (1997). The breast cancer gene product TSG101: A regulator of ubiquitination? J. Mol. Med. 75, 467-469.
    • (1997) J. Mol. Med. , vol.75 , pp. 467-469
    • Ponting, C.P.1    Cai, Y.D.2    Bork, P.3
  • 145
    • 0033583205 scopus 로고    scopus 로고
    • A novel MDMX transcript expressed in a variety of transformed cell lines encodes a truncated protein with potent p53 repressive activity
    • Rallapalli, R., Strachan, G., Cho, B., Mercer, W. E., and Hall, D. J. (1999). A novel MDMX transcript expressed in a variety of transformed cell lines encodes a truncated protein with potent p53 repressive activity. J. Biol. Chem. 274, 8299-8308.
    • (1999) J. Biol. Chem. , vol.274 , pp. 8299-8308
    • Rallapalli, R.1    Strachan, G.2    Cho, B.3    Mercer, W.E.4    Hall, D.J.5
  • 149
    • 0032518917 scopus 로고    scopus 로고
    • Nucleocytoplasmic shuttling of the hdm2 oncoprotein regulates the levels of the p53 protein via a pathway used by the human immunodeficiency virus rev protein
    • Roth, J., Dobbelstein, M., Freedman, D. A., Shenk, T., and Levine, A. J. (1998). Nucleocytoplasmic shuttling of the hdm2 oncoprotein regulates the levels of the p53 protein via a pathway used by the human immunodeficiency virus rev protein. EMBO J. 17, 554-564.
    • (1998) EMBO J. , vol.17 , pp. 554-564
    • Roth, J.1    Dobbelstein, M.2    Freedman, D.A.3    Shenk, T.4    Levine, A.J.5
  • 151
    • 0027156827 scopus 로고
    • Analysis of a protein-binding domain of p53
    • Ruppert, J. M., and Stillman, B. (1993). Analysis of a protein-binding domain of p53. Mol. Cell Biol. 13, 3811-3820.
    • (1993) Mol. Cell Biol. , vol.13 , pp. 3811-3820
    • Ruppert, J.M.1    Stillman, B.2
  • 152
    • 0036282464 scopus 로고    scopus 로고
    • The expression of murine double minute 2 is a favorable prognostic marker in esophageal squamous cell carcinoma without p53 protein accumulation
    • Saito, K., Tsujitani, S., Oka, S., Ikeguchi, M., Maeta, M., and Kaibara, N. (2002). The expression of murine double minute 2 is a favorable prognostic marker in esophageal squamous cell carcinoma without p53 protein accumulation. Ann. Surg. Oncol. 9, 450-456.
    • (2002) Ann. Surg. Oncol. , vol.9 , pp. 450-456
    • Saito, K.1    Tsujitani, S.2    Oka, S.3    Ikeguchi, M.4    Maeta, M.5    Kaibara, N.6
  • 154
    • 0027358723 scopus 로고
    • The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53
    • Scheffner, M., Huibregtse, J. M., Vierstra, R. D., and Howley, P. M. (1993). The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53. Cell 75, 495-505.
    • (1993) Cell , vol.75 , pp. 495-505
    • Scheffner, M.1    Huibregtse, J.M.2    Vierstra, R.D.3    Howley, P.M.4
  • 155
    • 0030884751 scopus 로고    scopus 로고
    • A novel protein with strong homology to the tumor suppressor p53
    • Schmale, H., and Bamberger, C. (1997). A novel protein with strong homology to the tumor suppressor p53. Oncogene 15, 1363-1367.
    • (1997) Oncogene , vol.15 , pp. 1363-1367
    • Schmale, H.1    Bamberger, C.2
  • 156
    • 0028238213 scopus 로고
    • Immediate early up-regulation of bax expression by p53 but not TGFβ1: A paradigm for distinct apoptotic pathways
    • Selvakumaran, M., Lin, H.-K., Miyashita, T., Wang, H. G., Krajewski, S., Reed, J. C., Hoffman, B., and Liebermann, D. (1994). Immediate early up-regulation of bax expression by p53 but not TGFβ1: A paradigm for distinct apoptotic pathways. Oncogene 9, 1791-1798.
    • (1994) Oncogene , vol.9 , 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
  • 157
    • 0035883863 scopus 로고    scopus 로고
    • Ligand-dependent interaction of the glucocorticoid receptor with p53 enhances their degradation by Hdm2
    • Sengupta, S., and Wasylyk, B. (2001). Ligand-dependent interaction of the glucocorticoid receptor with p53 enhances their degradation by Hdm2. Genes Dev. 15, 2367-2380.
    • (2001) Genes Dev. , vol.15 , pp. 2367-2380
    • Sengupta, S.1    Wasylyk, B.2
  • 159
    • 0033621415 scopus 로고    scopus 로고
    • Stabilization of the MDM2 oncoprotein by interaction with the structurally related MDMX protein
    • Sharp, D. A., Kratowicz, S. A., Sank, M. J., and George, D. L. (1999). Stabilization of the MDM2 oncoprotein by interaction with the structurally related MDMX protein. J. Biol. Chem. 274, 38189-38196.
    • (1999) J. Biol. Chem. , vol.274 , pp. 38189-38196
    • Sharp, D.A.1    Kratowicz, S.A.2    Sank, M.J.3    George, D.L.4
  • 160
    • 0030071548 scopus 로고    scopus 로고
    • Regulation of specific DNA binding by p53: Evidence for a role for O-glycosylation and charged residues at the corboxy-terminus
    • Shaw, P., Freeman, J., Bovey, R., and Iggo, R. (1996). Regulation of specific DNA binding by p53: Evidence for a role for O-glycosylation and charged residues at the corboxy-terminus. Oncogene. 12, 921-930.
    • (1996) Oncogene , vol.12 , pp. 921-930
    • Shaw, P.1    Freeman, J.2    Bovey, R.3    Iggo, R.4
  • 161
    • 0035834428 scopus 로고    scopus 로고
    • Regulation of receptor fate by ubiquitination of activated β2-adrenergic receptor and β-arrestin
    • Shenoy, S. K., McDonald, P. H., Kohout, T. A., and Lefkowitz, R. J. (2001). Regulation of receptor fate by ubiquitination of activated β2-adrenergic receptor and β-arrestin. Science 294, 1307-1313.
    • (2001) Science , vol.294 , pp. 1307-1313
    • Shenoy, S.K.1    McDonald, P.H.2    Kohout, T.A.3    Lefkowitz, R.J.4
  • 162
    • 0030667702 scopus 로고    scopus 로고
    • DNA damage-induced phosphorylation of p53 alleviates inhibition by MDM2
    • Shieh, S.-Y., Ikeda, M., Taya, Y., and Prives, C. (1997). DNA damage-induced phosphorylation of p53 alleviates inhibition by MDM2. Cell 91, 325-334.
    • (1997) Cell , vol.91 , pp. 325-334
    • Shieh, S.-Y.1    Ikeda, M.2    Taya, Y.3    Prives, C.4
  • 164
    • 0029824669 scopus 로고    scopus 로고
    • Alternatively spliced mdm2 transcripts with loss of p53 binding domain sequences: Transforming ability and frequent detection in human cancer
    • Sigalas, I., Calvert, A. H., Anderson, J. J., Neal, D. E., and Lunec, J. (1996). Alternatively spliced mdm2 transcripts with loss of p53 binding domain sequences: Transforming ability and frequent detection in human cancer. Nature Med. 2, 912-917.
    • (1996) Nature Med. , vol.2 , pp. 912-917
    • Sigalas, I.1    Calvert, A.H.2    Anderson, J.J.3    Neal, D.E.4    Lunec, J.5
  • 165
    • 0032085941 scopus 로고    scopus 로고
    • Autoactivation of procaspase-9 by Apaf-1-mediated oligomerization
    • Srinivasula, S. M., Ahmad, M., Fernandes-Alnemri, T., and Alnemri, E. S. (1998). Autoactivation of procaspase-9 by Apaf-1-mediated oligomerization. Mol. Cell 1, 949-957.
    • (1998) Mol. Cell , vol.1 , pp. 949-957
    • Srinivasula, S.M.1    Ahmad, M.2    Fernandes-Alnemri, T.3    Alnemri, E.S.4
  • 167
    • 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., and Wahl, G. M. (1999). A leucine-rich nuclear export signal in the p53 tetramerization domain: Regulation of subcellular localization and p53 activity by NES masking. EMBO J. 18, 1660-1672.
    • (1999) EMBO J. , vol.18 , 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
  • 170
    • 0035824686 scopus 로고    scopus 로고
    • A transcriptionally inactive E2F-1 targets the MDM family of proteins for proteolytic degradation
    • Strachan, G. D., Rallapalli, R., Pucci, B., Lafond, T. P., and Hall, D. J. (2001). A transcriptionally inactive E2F-1 targets the MDM family of proteins for proteolytic degradation. J. Biol. Chem. 276, 45677-45685.
    • (2001) J. Biol. Chem. , vol.276 , pp. 45677-45685
    • Strachan, G.D.1    Rallapalli, R.2    Pucci, B.3    Lafond, T.P.4    Hall, D.J.5
  • 173
    • 0033536063 scopus 로고    scopus 로고
    • ARF stabilizes p53 by blocking nucleo-cytoplasmic shuttling of Mdm2
    • ARF stabilizes p53 by blocking nucleo-cytoplasmic shuttling of Mdm2. Proc. Natl. Acad. Sci. USA 96, 6937-6941.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 6937-6941
    • Tao, W.1    Levine, A.J.2
  • 174
    • 0032980646 scopus 로고    scopus 로고
    • Nucleocytoplasmic shuttling of oncoprotein Hdm2 is required for Hdm2-mediated degradation of p53
    • Tao, W., and Levine, A. J. (1999b). Nucleocytoplasmic shuttling of oncoprotein Hdm2 is required for Hdm2-mediated degradation of p53. Proc. Natl. Acad. Sci. USA 96, 3077-3080.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 3077-3080
    • Tao, W.1    Levine, A.J.2
  • 177
    • 0036561484 scopus 로고    scopus 로고
    • p53 leans on its siblings
    • Urist, M., and Prives, C. (2002). p53 leans on its siblings. Cancer Cell 1, 311-313.
    • (2002) Cancer Cell , vol.1 , pp. 311-313
    • Urist, M.1    Prives, C.2
  • 178
    • 0036674617 scopus 로고    scopus 로고
    • Live or let die: The cell's response to p53
    • Vousden, K. H., and Lu, X. (2002). Live or let die: The cell's response to p53. Nature Rev. Cancer 2, 594-604.
    • (2002) Nature Rev. Cancer , vol.2 , pp. 594-604
    • Vousden, K.H.1    Lu, X.2
  • 179
    • 0030448650 scopus 로고    scopus 로고
    • Identification of a novel p53 functional domain that is necessary for efficient growth suppression
    • Walker, K. K., and Levine, A. J. (1996). Identification of a novel p53 functional domain that is necessary for efficient growth suppression. Proc. Natl. Acad. Sci. USA 93, 15335-15340.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 15335-15340
    • Walker, K.K.1    Levine, A.J.2
  • 181
    • 0035895602 scopus 로고    scopus 로고
    • MDM2 and MDMX can interact differently with ARF and members of the p53 family
    • Wang, X. Q., Arooz, T., Siu, W. Y., Chiu, C. H. S., Lau, A., Yamashita, K., and Poon, R. Y. C. (2001). MDM2 and MDMX can interact differently with ARF and members of the p53 family. FEBS Lett. 490, 202-208.
    • (2001) FEBS Lett. , vol.490 , pp. 202-208
    • Wang, X.Q.1    Arooz, T.2    Siu, W.Y.3    Chiu, C.H.S.4    Lau, A.5    Yamashita, K.6    Poon, R.Y.C.7
  • 182
    • 0035866337 scopus 로고    scopus 로고
    • A possible role of p73 on the modulation of p53 level through MDM2
    • Wang, X. Q., Ongkeko, W. M., Lau, A. W. S., Leung, K. M., and Poon, R. Y. C. (2001). A possible role of p73 on the modulation of p53 level through MDM2. Cancer Res. 61, 1598-1603.
    • (2001) Cancer Res. , vol.61 , pp. 1598-1603
    • Wang, X.Q.1    Ongkeko, W.M.2    Lau, A.W.S.3    Leung, K.M.4    Poon, R.Y.C.5
  • 186
    • 0037073713 scopus 로고    scopus 로고
    • Role of Pin1 in the regulation of p53 stability and p21 transactivation, and cell cycle checkpoints in response to DNA damage
    • Oct 17 epub
    • Wulf, G. M., Liou, Y. C., Ryo, A., Lee, S. W., and Lu, K. P. (2002). Role of Pin1 in the regulation of p53 stability and p21 transactivation, and cell cycle checkpoints in response to DNA damage. J. Biol. Chem. Oct 17 epub.
    • (2002) J. Biol. Chem.
    • Wulf, G.M.1    Liou, Y.C.2    Ryo, A.3    Lee, S.W.4    Lu, K.P.5
  • 187
    • 0032485420 scopus 로고    scopus 로고
    • High prognostic significance of Mdm2/p53 co-overexpression in soft tissue sarcomas of the extremities
    • Wurl, P., Meye, A., Schmidt, H., Lautenschlager, C., Kaltoff, H., Rath, F. W., and Taubert, H. (1998). High prognostic significance of Mdm2/p53 co-overexpression in soft tissue sarcomas of the extremities. Oncogene 16, 1183-1185.
    • (1998) Oncogene , vol.16 , pp. 1183-1185
    • Wurl, P.1    Meye, A.2    Schmidt, H.3    Lautenschlager, C.4    Kaltoff, H.5    Rath, F.W.6    Taubert, H.7
  • 190
    • 0037174133 scopus 로고    scopus 로고
    • P14ARF promotes accumulation of SUMO-1 conjugated (H) Mdm2
    • Xirodimas, D., Chisholm, J., Detserro, J., Lane, D., and Hay, R. (2002). P14ARF promotes accumulation of SUMO-1 conjugated (H) Mdm2. FEBS Lett. 528, 1-3.
    • (2002) FEBS Lett. , vol.528 , pp. 1-3
    • Xirodimas, D.1    Chisholm, J.2    Detserro, J.3    Lane, D.4    Hay, R.5
  • 191
    • 0344995254 scopus 로고    scopus 로고
    • MDM2 and MDMX inhibit the transcriptional activity of ectopically expressed SMAD proteins
    • Yam, C. H., Siu, W. Y., Arooz, T., Chiu, C. H. S., Lau, Á., Wang, X. Q., and Poon, R. Y. C. (1999). MDM2 and MDMX inhibit the transcriptional activity of ectopically expressed SMAD proteins. Cancer Res. 59, 5075-5078.
    • (1999) Cancer Res. , vol.59 , pp. 5075-5078
    • Yam, C.H.1    Siu, W.Y.2    Arooz, T.3    Chiu, C.H.S.4    Lau, Á.5    Wang, X.Q.6    Poon, R.Y.C.7
  • 192
    • 0032161624 scopus 로고    scopus 로고
    • p63, a p53 homolog at 3q27-29 encodes multiple products with transactivating, death-inducing, and dominant-negative activities
    • Yang, A., Kaghad, M., Wang, Y., Gillett, E., Fleming, M. D., Dotsch, V., Andrews, N. C., Caput, D., and McKeon, F. (1998). p63, a p53 homolog at 3q27-29 encodes multiple products with transactivating, death-inducing, and dominant-negative activities. Mol. Cell 2, 305-316.
    • (1998) Mol. Cell , vol.2 , pp. 305-316
    • Yang, A.1    Kaghad, M.2    Wang, Y.3    Gillett, E.4    Fleming, M.D.5    Dotsch, V.6    Andrews, N.C.7    Caput, D.8    McKeon, F.9
  • 193
    • 0028089283 scopus 로고
    • Adenovirus E1B oncoprotein tethers a transcriptional repression domain to p53
    • Yew, P. R., Liu, X., and Berk, A. J. (1994). Adenovirus E1B oncoprotein tethers a transcriptional repression domain to p53. Genes Dev. 8, 190-202.
    • (1994) Genes Dev. , vol.8 , pp. 190-202
    • Yew, P.R.1    Liu, X.2    Berk, A.J.3
  • 196
    • 0035839460 scopus 로고    scopus 로고
    • Cyclin A-CDK phosphorylation regulates MDM2 protein interactions
    • Zhang, T., and Prives, C. (2001). Cyclin A-CDK phosphorylation regulates MDM2 protein interactions. J. Biol. Chem. 176, 29702-29710.
    • (2001) J. Biol. Chem. , vol.176 , pp. 29702-29710
    • Zhang, T.1    Prives, C.2
  • 197
    • 0037044103 scopus 로고    scopus 로고
    • The initial evaluation of non-peptidic small-molecule HDM2 inhibitors based on p53-HDM2 complex structure
    • Zhao, J., Wang, M., Chen, J., Luo, A., Wang, X., Wu, M., Yin, D., and Liu, Z. (2002). The initial evaluation of non-peptidic small-molecule HDM2 inhibitors based on p53-HDM2 complex structure. Cancer Lett. 183, 69-77.
    • (2002) Cancer Lett. , vol.183 , pp. 69-77
    • Zhao, J.1    Wang, M.2    Chen, J.3    Luo, A.4    Wang, X.5    Wu, M.6    Yin, D.7    Liu, Z.8
  • 200
    • 0036312303 scopus 로고    scopus 로고
    • Novel targets of Akt, p21, and MDM2
    • Zhou, B. P., and Hung, M. C. (2002). Novel targets of Akt, p21, and MDM2. Semin. Oncol. 29, 62-70.
    • (2002) Semin. Oncol. , vol.29 , pp. 62-70
    • Zhou, B.P.1    Hung, M.C.2
  • 201
    • 0035736487 scopus 로고    scopus 로고
    • HER-2/neu induces p53 ubiquitination via Akt-mediated MDM2 phosphorylation
    • Zhou, B. P., Liao, Y., Xia, W., Zhou, Y., Spohn, B., and Hung, M.-C. (2001). HER-2/neu induces p53 ubiquitination via Akt-mediated MDM2 phosphorylation. Nature Cell Biol. 3, 973-982.
    • (2001) Nature Cell Biol. , vol.3 , pp. 973-982
    • Zhou, B.P.1    Liao, Y.2    Xia, W.3    Zhou, Y.4    Spohn, B.5    Hung, M.-C.6
  • 202
    • 0032533514 scopus 로고    scopus 로고
    • The potential tumor suppressor p73 differentially regulates cellular p53 target genes
    • Zhu, J., Jiang, J., Zhou, W., and Chen, X. (1998). The potential tumor suppressor p73 differentially regulates cellular p53 target genes. Cancer Res. 58, 5061-5065.
    • (1998) Cancer Res. , vol.58 , pp. 5061-5065
    • Zhu, J.1    Jiang, J.2    Zhou, W.3    Chen, X.4


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