메뉴 건너뛰기




Volumn 260, Issue 1, 2009, Pages 110-120

A quantitative model of the effect of unreplicated DNA on cell cycle progression in frog egg extracts

Author keywords

Cdc25; Cdk; Checkpoint; Hysteresis; MPF; Wee1

Indexed keywords

CHECKPOINT KINASE 1; DNA; PROTEIN TYROSINE KINASE;

EID: 67949092765     PISSN: 00225193     EISSN: 10958541     Source Type: Journal    
DOI: 10.1016/j.jtbi.2009.05.018     Document Type: Article
Times cited : (6)

References (41)
  • 1
    • 0038418869 scopus 로고    scopus 로고
    • Chk1 and Chk2 kinases in checkpoint control and cancer
    • Bartek J., and Lukas J. Chk1 and Chk2 kinases in checkpoint control and cancer. Cancer Cell 3 (2003) 421-429
    • (2003) Cancer Cell , vol.3 , pp. 421-429
    • Bartek, J.1    Lukas, J.2
  • 2
    • 0141834707 scopus 로고    scopus 로고
    • Phosphorylation of Xenopus Cdc25C at Ser285 interferes with ability to activate a DNA damage replication checkpoint in pre-midblastula embryos
    • Bulavin D.V., Demidenko Z.N., Phillips C., Moody S.A., and Fornace J.A.J. Phosphorylation of Xenopus Cdc25C at Ser285 interferes with ability to activate a DNA damage replication checkpoint in pre-midblastula embryos. Cell Cycle 2 (2003) 263-266
    • (2003) Cell Cycle , vol.2 , pp. 263-266
    • Bulavin, D.V.1    Demidenko, Z.N.2    Phillips, C.3    Moody, S.A.4    Fornace, J.A.J.5
  • 4
    • 0029808466 scopus 로고    scopus 로고
    • Cell cycle checkpoints: preventing an identity crisis
    • Elledge S.J. Cell cycle checkpoints: preventing an identity crisis. Science 274 (1996) 1664-1671
    • (1996) Science , vol.274 , pp. 1664-1671
    • Elledge, S.J.1
  • 5
    • 0025367233 scopus 로고
    • Triggering of cyclin degradation in interphase extracts of amphibian eggs by cdc2 kinase
    • Felix M.A., Labbe J.C., Doree M., Hunt T., and Karsenti E. Triggering of cyclin degradation in interphase extracts of amphibian eggs by cdc2 kinase. Nature 346 (1990) 379-382
    • (1990) Nature , vol.346 , pp. 379-382
    • Felix, M.A.1    Labbe, J.C.2    Doree, M.3    Hunt, T.4    Karsenti, E.5
  • 7
    • 0026006671 scopus 로고
    • A minimal cascade model for the mitotic oscilllator involving cyclin and cdc2 kinase
    • Goldbeter A. A minimal cascade model for the mitotic oscilllator involving cyclin and cdc2 kinase. Proc. Natl. Acad. Sci. USA 88 (1991) 9107-9111
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 9107-9111
    • Goldbeter, A.1
  • 8
    • 0034312277 scopus 로고    scopus 로고
    • Requirement for Atr in phosphorylation of Chk1 and cell cycle regulation in response to DNA replication blocks and UV-damaged DNA in Xenopus egg extracts
    • Guo Z., Kumagai A., Wang S.X., and Dunphy W.G. Requirement for Atr in phosphorylation of Chk1 and cell cycle regulation in response to DNA replication blocks and UV-damaged DNA in Xenopus egg extracts. Genes Dev. 14 (2000) 2745-2756
    • (2000) Genes Dev. , vol.14 , pp. 2745-2756
    • Guo, Z.1    Kumagai, A.2    Wang, S.X.3    Dunphy, W.G.4
  • 9
    • 0034614637 scopus 로고    scopus 로고
    • The hallmarks of cancer
    • Hanahan D., and Weinberg R.A. The hallmarks of cancer. Cell 100 (2000) 57-70
    • (2000) Cell , vol.100 , pp. 57-70
    • Hanahan, D.1    Weinberg, R.A.2
  • 10
    • 67949093153 scopus 로고    scopus 로고
    • He, J., 2007. Design and evaluation of a data-distributed massively parallel implementation of a global optimization algorithm DIRECT. Ph.D., Department of Computer Science, Virginia Polytechnic Insitutute and State University, Blacksburg, VA.
    • He, J., 2007. Design and evaluation of a data-distributed massively parallel implementation of a global optimization algorithm DIRECT. Ph.D., Department of Computer Science, Virginia Polytechnic Insitutute and State University, Blacksburg, VA.
  • 12
    • 0034649590 scopus 로고    scopus 로고
    • Xenopus ATR is a replication-dependent chromatin-binding protein required for the DNA replication checkpoint
    • Hekmat-Nejad M., You Z., Yee M.C., Newport J.W., and Cimprich K.A. Xenopus ATR is a replication-dependent chromatin-binding protein required for the DNA replication checkpoint. Curr. Biol. 10 (2000) 1565-1573
    • (2000) Curr. Biol. , vol.10 , pp. 1565-1573
    • Hekmat-Nejad, M.1    You, Z.2    Yee, M.C.3    Newport, J.W.4    Cimprich, K.A.5
  • 13
    • 0037174161 scopus 로고    scopus 로고
    • Dephosphorylation of the inhibitory phosphorylation site S287 in Xenopus Cdc25C by protein phosphatase-2A is inhibited by 14-3-3 binding
    • Hutchins J.R., Dikovskaya D., and Clarke P.R. Dephosphorylation of the inhibitory phosphorylation site S287 in Xenopus Cdc25C by protein phosphatase-2A is inhibited by 14-3-3 binding. FEBS Lett. 528 (2002) 267-271
    • (2002) FEBS Lett. , vol.528 , pp. 267-271
    • Hutchins, J.R.1    Dikovskaya, D.2    Clarke, P.R.3
  • 14
    • 0027746003 scopus 로고
    • Elimination of cdc2 phosphorylation sites in the cdc25 phosphatase blocks initiation of M-phase
    • Izumi T., and Maller J.L. Elimination of cdc2 phosphorylation sites in the cdc25 phosphatase blocks initiation of M-phase. Mol. Biol. Cell 4 (1993) 1337-1350
    • (1993) Mol. Biol. Cell , vol.4 , pp. 1337-1350
    • Izumi, T.1    Maller, J.L.2
  • 15
    • 0033567028 scopus 로고    scopus 로고
    • A maternal form of the phosphatase Cdc25A regulates early embryonic cell cycles in Xenopus laevis
    • Kim S., Li C., and Maller J. A maternal form of the phosphatase Cdc25A regulates early embryonic cell cycles in Xenopus laevis. Dev. Biol. 212 (1999) 381-391
    • (1999) Dev. Biol. , vol.212 , pp. 381-391
    • Kim, S.1    Li, C.2    Maller, J.3
  • 16
    • 0025980359 scopus 로고
    • The cdc25 protein controls tyrosine dephosphorylation of the cdc2 protein in a cell-free system
    • Kumagai A., and Dunphy W.G. The cdc25 protein controls tyrosine dephosphorylation of the cdc2 protein in a cell-free system. Cell 64 (1991) 903-914
    • (1991) Cell , vol.64 , pp. 903-914
    • Kumagai, A.1    Dunphy, W.G.2
  • 17
    • 0026719599 scopus 로고
    • Regulation of the cdc25 protein during the cell cycle in Xenopus extracts
    • Kumagai A., and Dunphy W.G. Regulation of the cdc25 protein during the cell cycle in Xenopus extracts. Cell 70 (1992) 139-151
    • (1992) Cell , vol.70 , pp. 139-151
    • Kumagai, A.1    Dunphy, W.G.2
  • 18
    • 0029016412 scopus 로고
    • Control of the Cdc2/Cyclin B complex in Xenopus egg extracts arrested at a G2/M checkpoint with DNA synthesis inhibitors
    • Kumagai A., and Dunphy W.G. Control of the Cdc2/Cyclin B complex in Xenopus egg extracts arrested at a G2/M checkpoint with DNA synthesis inhibitors. Mol. Biol. Cell 6 (1995) 199-213
    • (1995) Mol. Biol. Cell , vol.6 , pp. 199-213
    • Kumagai, A.1    Dunphy, W.G.2
  • 19
    • 0031906844 scopus 로고    scopus 로고
    • 14-3-3 Proteins act as negative regulators of the mitotic inducer Cdc25 in Xenopus egg extracts
    • Kumagai A., Yakowec P.S., and Dunphy W.G. 14-3-3 Proteins act as negative regulators of the mitotic inducer Cdc25 in Xenopus egg extracts. Mol. Biol. Cell 9 (1998) 345-354
    • (1998) Mol. Biol. Cell , vol.9 , pp. 345-354
    • Kumagai, A.1    Yakowec, P.S.2    Dunphy, W.G.3
  • 20
    • 0032555924 scopus 로고    scopus 로고
    • The Xenopus Chk1 protein kinase mediates a caffeine-sensitive pathway of checkpoint control in cell-free extracts
    • Kumagai A., Guo Z., Emami K.H., Wang S.X., and Dunphy W.G. The Xenopus Chk1 protein kinase mediates a caffeine-sensitive pathway of checkpoint control in cell-free extracts. J. Cell Biol. 142 (1998) 1559-1569
    • (1998) J. Cell Biol. , vol.142 , pp. 1559-1569
    • Kumagai, A.1    Guo, Z.2    Emami, K.H.3    Wang, S.X.4    Dunphy, W.G.5
  • 21
    • 0035158899 scopus 로고    scopus 로고
    • Positive regulation of Wee1 by Chk1 and 14-3-3 proteins
    • Lee J., Kumagai A., and Dunphy W.G. Positive regulation of Wee1 by Chk1 and 14-3-3 proteins. Mol. Biol. Cell 12 (2001) 551-563
    • (2001) Mol. Biol. Cell , vol.12 , pp. 551-563
    • Lee, J.1    Kumagai, A.2    Dunphy, W.G.3
  • 23
    • 0037106186 scopus 로고    scopus 로고
    • A requirement for replication in inactivation of the ATR-dependent DNA damage checkpoint
    • Lupardus P.J., Byun T., Yee M.C., Hekmat-Nejad M., and Cimprich K.A. A requirement for replication in inactivation of the ATR-dependent DNA damage checkpoint. Genes Dev. 16 (2002) 2327-2332
    • (2002) Genes Dev. , vol.16 , pp. 2327-2332
    • Lupardus, P.J.1    Byun, T.2    Yee, M.C.3    Hekmat-Nejad, M.4    Cimprich, K.A.5
  • 25
    • 0028998865 scopus 로고
    • Cell cycle regulation of a Xenopus Wee1-like kinase
    • Mueller P.R., Coleman T.R., and Dunphy W.G. Cell cycle regulation of a Xenopus Wee1-like kinase. Mol. Biol. Cell 6 (1995) 119-134
    • (1995) Mol. Biol. Cell , vol.6 , pp. 119-134
    • Mueller, P.R.1    Coleman, T.R.2    Dunphy, W.G.3
  • 26
    • 0028783413 scopus 로고
    • Myt1: a membrane-associated inhibitory kinase that phosphorylates Cdc2 on both threonine-14 and tyrosine-15
    • Mueller P.R., Coleman T.R., Kumagai A., and Dunphy W.G. Myt1: a membrane-associated inhibitory kinase that phosphorylates Cdc2 on both threonine-14 and tyrosine-15. Science 270 (1995) 86-90
    • (1995) Science , vol.270 , pp. 86-90
    • Mueller, P.R.1    Coleman, T.R.2    Kumagai, A.3    Dunphy, W.G.4
  • 27
    • 0027716813 scopus 로고
    • Numerical analysis of a comprehensive model of M-phase control in Xenopus oocyte extracts and intact embryos
    • Novak B., and Tyson J.J. Numerical analysis of a comprehensive model of M-phase control in Xenopus oocyte extracts and intact embryos. J. Cell Sci. 106 (1993) 1153-1168
    • (1993) J. Cell Sci. , vol.106 , pp. 1153-1168
    • Novak, B.1    Tyson, J.J.2
  • 28
    • 0036948433 scopus 로고    scopus 로고
    • Toward maintaining the genome: DNA damage and replication checkpoints
    • Nyberg K.A., Michelson R.J., Putnam C.W., and Weinert T.A. Toward maintaining the genome: DNA damage and replication checkpoints. Ann. Rev. Genet. 36 (2002) 617-656
    • (2002) Ann. Rev. Genet. , vol.36 , pp. 617-656
    • Nyberg, K.A.1    Michelson, R.J.2    Putnam, C.W.3    Weinert, T.A.4
  • 29
    • 0025370462 scopus 로고
    • In vitro disassembly of the nuclear lamina and M phase-specific phosphorylation of lamins by cdc2 kinase
    • Peter M., Nakagawa J., Doree M., Labbe J.C., and Nigg E.A. In vitro disassembly of the nuclear lamina and M phase-specific phosphorylation of lamins by cdc2 kinase. Cell 61 (1990) 591-602
    • (1990) Cell , vol.61 , pp. 591-602
    • Peter, M.1    Nakagawa, J.2    Doree, M.3    Labbe, J.C.4    Nigg, E.A.5
  • 30
    • 0345700833 scopus 로고    scopus 로고
    • Buidling a cell cycle oscillator: hysteresis and bistability in activation of Cdc2
    • Pomerening J.R., Sontag E.D., and Ferrell J.E.J. Buidling a cell cycle oscillator: hysteresis and bistability in activation of Cdc2. Nat. Cell Biol. 5 (2003) 346-351
    • (2003) Nat. Cell Biol. , vol.5 , pp. 346-351
    • Pomerening, J.R.1    Sontag, E.D.2    Ferrell, J.E.J.3
  • 31
    • 0037312317 scopus 로고    scopus 로고
    • Molecular anatomy of the DNA damage and DNA replication checkpoints
    • Qin J., and Li L. Molecular anatomy of the DNA damage and DNA replication checkpoints. Radiat. Res. 159 (2003) 139-148
    • (2003) Radiat. Res. , vol.159 , pp. 139-148
    • Qin, J.1    Li, L.2
  • 32
    • 0037032839 scopus 로고    scopus 로고
    • Untangling checkpoints
    • Sagata N. Untangling checkpoints. Science 298 (2002) 1905-1907
    • (2002) Science , vol.298 , pp. 1905-1907
    • Sagata, N.1
  • 35
    • 0037099703 scopus 로고    scopus 로고
    • Chk1 is activated transiently and targets Cdc25A for degradation at the Xenopus midblastula transition
    • Shimuta K., Nakajo N., Uto K., Hayano Y., Okazaki K., and Sagata N. Chk1 is activated transiently and targets Cdc25A for degradation at the Xenopus midblastula transition. EMBO J. 21 (2002) 3694-3703
    • (2002) EMBO J. , vol.21 , pp. 3694-3703
    • Shimuta, K.1    Nakajo, N.2    Uto, K.3    Hayano, Y.4    Okazaki, K.5    Sagata, N.6
  • 38
    • 2542459341 scopus 로고    scopus 로고
    • Adaptation of a DNA replication checkpoint response depends upon inactivation of claspin by the polo-like kinase
    • Yoo H.Y., Kumagai A., Shevchenko A., and Dunphy W.G. Adaptation of a DNA replication checkpoint response depends upon inactivation of claspin by the polo-like kinase. Cell 117 (2004) 575-588
    • (2004) Cell , vol.117 , pp. 575-588
    • Yoo, H.Y.1    Kumagai, A.2    Shevchenko, A.3    Dunphy, W.G.4
  • 39
    • 13444270529 scopus 로고    scopus 로고
    • Parameter estimation from a mathematical model
    • Zwolak J.W., Tyson J.J., and Watson L.T. Parameter estimation from a mathematical model. J. Comput. Biol. 12 (2005) 48-63
    • (2005) J. Comput. Biol. , vol.12 , pp. 48-63
    • Zwolak, J.W.1    Tyson, J.J.2    Watson, L.T.3
  • 40
    • 22144476845 scopus 로고    scopus 로고
    • Globally optimized parameters for a model of mitotic control in frog egg extracts
    • Zwolak J.W., Tyson J.J., and Watson L.T. Globally optimized parameters for a model of mitotic control in frog egg extracts. IEE Proc. Syst. Biol. 152 (2005) 81-92
    • (2005) IEE Proc. Syst. Biol. , vol.152 , pp. 81-92
    • Zwolak, J.W.1    Tyson, J.J.2    Watson, L.T.3
  • 41
    • 34548232138 scopus 로고    scopus 로고
    • ODRPACK95: a weighted orthogonal distance regression code with bound constraints
    • Zwolak J.W., Boggs P.T., and Watson L.T. ODRPACK95: a weighted orthogonal distance regression code with bound constraints. ACM Trans. Math. Software 33 (2007)
    • (2007) ACM Trans. Math. Software , vol.33
    • Zwolak, J.W.1    Boggs, P.T.2    Watson, L.T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.