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Volumn 36, Issue 2, 2004, Pages 147-150

Dynamics of the p53-Mdm2 feedback loop in individual cells

Author keywords

[No Author keywords available]

Indexed keywords

CYAN FLUORESCENT PROTEIN; HYBRID PROTEIN; PROTEIN MDM2; PROTEIN P53; REGULATOR PROTEIN; TUMOR SUPPRESSOR PROTEIN; YELLOW FLUORESCENT PROTEIN;

EID: 0842332406     PISSN: 10614036     EISSN: None     Source Type: Journal    
DOI: 10.1038/ng1293     Document Type: Article
Times cited : (865)

References (30)
  • 1
  • 2
    • 0037329056 scopus 로고    scopus 로고
    • The p53-Mdm2 module and the ubiquitin system
    • Michael, D. & Oren, M. The p53-Mdm2 module and the ubiquitin system. Semin. Cancer Biol. 13, 49-58 (2003).
    • (2003) Semin. Cancer Biol. , vol.13 , pp. 49-58
    • Michael, D.1    Oren, M.2
  • 3
    • 0030800922 scopus 로고    scopus 로고
    • Mdm2: Keeping p53 under control
    • Piette, J., Neel, H. & Marechal, V. Mdm2: keeping p53 under control. Oncogene 15, 1001-1010 (1997).
    • (1997) Oncogene , vol.15 , pp. 1001-1010
    • Piette, J.1    Neel, H.2    Marechal, V.3
  • 4
    • 0032475878 scopus 로고    scopus 로고
    • Signaling to p53: Breaking the MDM2-p53 circuit
    • Prives, C. Signaling to p53: breaking the MDM2-p53 circuit. Cell 95, 5-8 (1998).
    • (1998) Cell , vol.95 , pp. 5-8
    • Prives, C.1
  • 5
    • 0033959744 scopus 로고    scopus 로고
    • MDM2-master regulator of the p53 tumor suppressor protein
    • Momand, J., Wu, H.H. & Dasgupta, G. MDM2-master regulator of the p53 tumor suppressor protein. Gene 242, 15-29 (2000).
    • (2000) Gene , vol.242 , pp. 15-29
    • Momand, J.1    Wu, H.H.2    Dasgupta, G.3
  • 6
    • 0033552595 scopus 로고    scopus 로고
    • Regulation of p53 in response to DNA damage
    • Larkin, N.D. & Jackson, S.P. Regulation of p53 in response to DNA damage. Oncogene 18, 7644-7655 (1999).
    • (1999) Oncogene , vol.18 , pp. 7644-7655
    • Larkin, N.D.1    Jackson, S.P.2
  • 7
    • 0035370483 scopus 로고    scopus 로고
    • Regulation and function of the p53 tumor suppressor protein
    • Ryan, K.M., Phillips, A.C. & Vousden, K.H. Regulation and function of the p53 tumor suppressor protein. Curr. Opin. Cell Biol. 13, 332-337 (2001).
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 332-337
    • Ryan, K.M.1    Phillips, A.C.2    Vousden, K.H.3
  • 8
    • 0036578795 scopus 로고    scopus 로고
    • Network motifs in the transcriptional regulation network of Escherichia coli
    • Shen-Orr, S., Milo, R., Mangan, S. & Alon, U. Network motifs in the transcriptional regulation network of Escherichia coli. Nat. Genet. 31, 64-68 (2002).
    • (2002) Nat. Genet. , vol.31 , pp. 64-68
    • Shen-Orr, S.1    Milo, R.2    Mangan, S.3    Alon, U.4
  • 9
    • 0034633702 scopus 로고    scopus 로고
    • Generation of Oscillation by the p53-Mdm2 feedback loop: A theoretical and experimental study
    • Lev Bar-Or, R. et al. Generation of Oscillation by the p53-Mdm2 feedback loop: a theoretical and experimental study. Proc. Natl. Acad. Sci. USA 97, 11250-11255 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 11250-11255
    • Lev Bar-Or, R.1
  • 10
    • 0037044575 scopus 로고    scopus 로고
    • The |κB-NF-κB signaling module: Temporal control and selective gene activation
    • Hoffmann, A., Levchenko, A., Scott, M.L. & Baltimore, D. The |κB-NF-κB signaling module: Temporal control and selective gene activation. Science 298, 1241-1245 (2002).
    • (2002) Science , vol.298 , pp. 1241-1245
    • Hoffmann, A.1    Levchenko, A.2    Scott, M.L.3    Baltimore, D.4
  • 11
    • 0027246716 scopus 로고
    • Regulation of p53 protein expression in human breast cancer cell lines
    • Vojtesek, B. & Lane, D.P. Regulation of p53 protein expression in human breast cancer cell lines. J. Cell. Sci. 105, 607-612 (1993).
    • (1993) J. Cell. Sci. , vol.105 , pp. 607-612
    • Vojtesek, B.1    Lane, D.P.2
  • 12
    • 0026543204 scopus 로고
    • p53 gene mutations in non-small-cell lung cancer cell lines and their correlation with the presence of ras mutations and clinical features
    • Mitsudomi, T. et al. p53 gene mutations in non-small-cell lung cancer cell lines and their correlation with the presence of ras mutations and clinical features. Oncogene 7, 171-180 (1992).
    • (1992) Oncogene , vol.7 , pp. 171-180
    • Mitsudomi, T.1
  • 13
    • 0035839460 scopus 로고    scopus 로고
    • Cyclin a-CDK phosphorylation regulates MDM2 protein interactions
    • Zhang, T. & Prives, C. Cyclin a-CDK phosphorylation regulates MDM2 protein interactions. J. Biol. Chem. 276, 29702-29710 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 29702-29710
    • Zhang, T.1    Prives, C.2
  • 14
    • 0033592868 scopus 로고    scopus 로고
    • Rapid ATP-dependent phosphorylation of MDM2 precedes p53 accumulation in response to DNA damage
    • Khosravi, R. et al. Rapid ATP-dependent phosphorylation of MDM2 precedes p53 accumulation in response to DNA damage. Proc. Natl. Acad. Sci. USA 96, 14973-14977 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 14973-14977
    • Khosravi, R.1
  • 15
    • 0035132822 scopus 로고    scopus 로고
    • p53 modulates base excision repair activity in a cell cycle-specific manner after genotoxic stress
    • Offer, H. et al. p53 modulates base excision repair activity in a cell cycle-specific manner after genotoxic stress. Cancer Res. 61, 88-96 (2001).
    • (2001) Cancer Res. , vol.61 , pp. 88-96
    • Offer, H.1
  • 16
    • 0037351881 scopus 로고    scopus 로고
    • Cyclic, proteasome-mediated turnover of unliganded and liganded ERa on responsive promoters is an integral feature of estrogen signaling
    • Reid, G. et al. Cyclic, proteasome-mediated turnover of unliganded and liganded ERa on responsive promoters is an integral feature of estrogen signaling. Mol. Cell 11, 605-707 (2003).
    • (2003) Mol. Cell , vol.11 , pp. 605-707
    • Reid, G.1
  • 17
    • 0037079015 scopus 로고    scopus 로고
    • Computational approaches to cellular rhythms
    • Goldbeter, A. Computational approaches to cellular rhythms. Nature 420, 238-245 (2002)
    • (2002) Nature , vol.420 , pp. 238-245
    • Goldbeter, A.1
  • 18
    • 0032496358 scopus 로고    scopus 로고
    • The biochemical basis of an all-or-none cell fate switch in Xenopus oocytes
    • Ferrell, J.E. Jr. & Machleder, E.M. The biochemical basis of an all-or-none cell fate switch in Xenopus oocytes. Science 280, 895-898 (1998).
    • (1998) Science , vol.280 , pp. 895-898
    • Ferrell Jr., J.E.1    Machleder, E.M.2
  • 19
    • 0347304512 scopus 로고    scopus 로고
    • Possible oscillatory behavior in p53-Mdm2 interaction computer simulation
    • Mihalas, G.I., Simon, Z., Balea, G. & Popa, E. Possible oscillatory behavior in p53-Mdm2 interaction computer simulation. J. Biol. Syst. 8, 21-29 (2000).
    • (2000) J. Biol. Syst. , vol.8 , pp. 21-29
    • Mihalas, G.I.1    Simon, Z.2    Balea, G.3    Popa, E.4
  • 20
    • 0037085271 scopus 로고    scopus 로고
    • PTEN protects p53 from Mdm2 and sensitizes cancer cells to chemotherapy
    • Mayo, L.D., Dixon, J.E., Durden, D.L., Tonks, N.K. & Donner, D.B. PTEN protects p53 from Mdm2 and sensitizes cancer cells to chemotherapy. J. Biol. Chem. 277, 5484-5489 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 5484-5489
    • Mayo, L.D.1    Dixon, J.E.2    Durden, D.L.3    Tonks, N.K.4    Donner, D.B.5
  • 21
    • 0034735896 scopus 로고    scopus 로고
    • Direct transactivation of c-Ha-Ras gene by p53: Evidence for its involvement in p53 transactivation activity and p53-mediated apoptosis
    • Deguin-Chambon, V., Vacher, M., Jullien, M., May, E. & Bourdon, J.C. Direct transactivation of c-Ha-Ras gene by p53: evidence for its involvement in p53 transactivation activity and p53-mediated apoptosis. Oncogene 19, 5831-5841 (2000).
    • (2000) Oncogene , vol.19 , pp. 5831-5841
    • Deguin-Chambon, V.1    Vacher, M.2    Jullien, M.3    May, E.4    Bourdon, J.C.5
  • 22
    • 0345700833 scopus 로고    scopus 로고
    • Building a cell cycle oscillator: Hysteresis and bistability in the activation of Cdc2
    • Pomerening, J.R., Sontag, E.D. & Ferrell, J.E. Jr. Building a cell cycle oscillator: hysteresis and bistability in the activation of Cdc2. Nat. Cell Biol. 5, 346-351 (2003).
    • (2003) Nat. Cell Biol. , vol.5 , pp. 346-351
    • Pomerening, J.R.1    Sontag, E.D.2    Ferrell Jr., J.E.3
  • 23
    • 0037376655 scopus 로고    scopus 로고
    • Sniffers, buzzers, toggles and blinkers: Dynamics of regulatory and signaling pathways in the cell
    • Tyson, J.J., Chen, K.C. & Novak, B. Sniffers, buzzers, toggles and blinkers: dynamics of regulatory and signaling pathways in the cell. Curr. Opin. Cell Biol. 15, 221-231 (2003).
    • (2003) Curr. Opin. Cell Biol. , vol.15 , pp. 221-231
    • Tyson, J.J.1    Chen, K.C.2    Novak, B.3
  • 24
    • 0023551951 scopus 로고
    • Metal dependent binding of a factor in vivo to the metal-responsive elements of the metallothionein 1 gene promoter
    • Andersen, R.D. et al. Metal dependent binding of a factor in vivo to the metal-responsive elements of the metallothionein 1 gene promoter. Mol. Cell Biol. 7, 3574-3581 (1987).
    • (1987) Mol. Cell Biol. , vol.7 , pp. 3574-3581
    • Andersen, R.D.1
  • 25
    • 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. & Vogelstein, B. Amplification of a gene encoding a p53-associated protein in human sarcomas. Nature 358, 80-83 (1992).
    • (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
  • 26
    • 0037628777 scopus 로고    scopus 로고
    • Low-dose rediation: Thresholds, bystander effects, and adaptive responses
    • Bonner, W.M. Low-dose rediation: thresholds, bystander effects, and adaptive responses. Proc. Natl. Acad. Sci. USA 100, 4973-4975 (2003).
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 4973-4975
    • Bonner, W.M.1
  • 27
    • 0033990336 scopus 로고    scopus 로고
    • Heat shock factors and the control of the stress response
    • Santoro, M.G. Heat shock factors and the control of the stress response. Biochem. Pharmacol. 59, 55-63 (2000).
    • (2000) Biochem. Pharmacol. , vol.59 , pp. 55-63
    • Santoro, M.G.1
  • 28
    • 0033635292 scopus 로고    scopus 로고
    • Posttranscriptional regulation of Smoothened is part of a self-correcting mechanism in the Hedgehog signaling system
    • Alcedo, J., Zou, Y. & Noll, M. Posttranscriptional regulation of Smoothened is part of a self-correcting mechanism in the Hedgehog signaling system. Mol. Cell 6, 457-465 (2000).
    • (2000) Mol. Cell , vol.6 , pp. 457-465
    • Alcedo, J.1    Zou, Y.2    Noll, M.3
  • 29
    • 0036124543 scopus 로고    scopus 로고
    • Ime2, a meiosis-specific kinase in yeast, is required for destabilization of its transcriptional activator, Imel
    • Guttman-Raviv, N., Matin, S. & Kassir, Y. Ime2, a meiosis-specific kinase in yeast, is required for destabilization of its transcriptional activator, Imel. Mol. Cell. Biol. 22, 2047-2056 (2002).
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 2047-2056
    • Guttman-Raviv, N.1    Matin, S.2    Kassir, Y.3
  • 30
    • 0025632973 scopus 로고
    • DnaK, DnaJ, and GrpE heat shock proteins negatively regulate heat shock gene expression by controlling the synthesis and stability of sigma 32
    • Straus, D., Walter, W. & Gross, C.A. DnaK, DnaJ, and GrpE heat shock proteins negatively regulate heat shock gene expression by controlling the synthesis and stability of sigma 32. Genes Dev. 4, 2202-2209 (1990).
    • (1990) Genes Dev. , vol.4 , pp. 2202-2209
    • Straus, D.1    Walter, W.2    Gross, C.A.3


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