메뉴 건너뛰기




Volumn 8, Issue 1, 2010, Pages

A mitotic phosphorylation feedback network connects Cdk1, Plk1, 53BP1, and Chk2 to inactivate the G2/M DNA damage checkpoint

(17)  Van Vugt, Marcel A T M a,h   Gardino, Alexandra K a   Linding, Rune b   Ostheimer, Gerard J a   Reinhardt, H Christian a,i   Ong, Shao En c   Tan, Chris S d   Miao, Hua c   Keezer, Susan M e   Li, Jeijin f   Pawson, Tony c   Lewis, Timothy A c   Carr, Steven A c   Smerdon, Stephen J f   Brummelkamp, Thijn R g   Yaffe, Michael B g   Lichten, Michael a,c  


Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEIN; ATM PROTEIN; CHECKPOINT KINASE 2; CYCLIN DEPENDENT KINASE 1; POLO LIKE KINASE 1; PROTEIN 53BP1; UNCLASSIFIED DRUG; CELL CYCLE PROTEIN; ONCOPROTEIN; POLO-LIKE KINASE 1; PROTEIN SERINE THREONINE KINASE; SIGNAL PEPTIDE; TP53BP1 PROTEIN, HUMAN;

EID: 75749130721     PISSN: 15449173     EISSN: 15457885     Source Type: Journal    
DOI: 10.1371/journal.pbio.1000287     Document Type: Article
Times cited : (188)

References (109)
  • 1
    • 0035902108 scopus 로고    scopus 로고
    • Genome maintenance mechanisms for preventing cancer
    • Hoeijmakers JH (2001) Genome maintenance mechanisms for preventing cancer. Nature 411: 366-374.
    • (2001) Nature , vol.411 , pp. 366-374
    • Hoeijmakers, J.H.1
  • 2
    • 33847737716 scopus 로고    scopus 로고
    • DNA damage checkpoints: From initiation to recovery or adaptation
    • Bartek J, Lukas J (2007) DNA damage checkpoints: from initiation to recovery or adaptation. Curr Opin Cell Biol 19: 238-245.
    • (2007) Curr Opin Cell Biol , vol.19 , pp. 238-245
    • Bartek, J.1    Lukas, J.2
  • 3
    • 36749022214 scopus 로고    scopus 로고
    • The DNA damage response: Ten years after
    • Harper JW, Elledge SJ (2007) The DNA damage response: ten years after. Mol Cell 28: 739-745.
    • (2007) Mol Cell , vol.28 , pp. 739-745
    • Harper, J.W.1    Elledge, S.J.2
  • 4
    • 9244251125 scopus 로고    scopus 로고
    • Cell-cycle checkpoints and cancer
    • Kastan MB, Bartek J (2004) Cell-cycle checkpoints and cancer. Nature 432: 316-323.
    • (2004) Nature , vol.432 , pp. 316-323
    • Kastan, M.B.1    Bartek, J.2
  • 5
    • 0037365789 scopus 로고    scopus 로고
    • ATM and related protein kinases: Safeguarding genome integrity
    • Shiloh Y (2003) ATM and related protein kinases: safeguarding genome integrity. Nat Rev Cancer 3: 155-168.
    • (2003) Nat Rev Cancer , vol.3 , pp. 155-168
    • Shiloh, Y.1
  • 6
    • 0034707047 scopus 로고    scopus 로고
    • The DNA damage response: Putting checkpoints in perspective
    • Zhou BB, Elledge SJ (2000) The DNA damage response: putting checkpoints in perspective. Nature 408: 433-439.
    • (2000) Nature , vol.408 , pp. 433-439
    • Zhou, B.B.1    Elledge, S.J.2
  • 8
    • 17244367849 scopus 로고    scopus 로고
    • DNA damage response as a candidate anti-cancer barrier in early human tumorigenesis
    • Bartkova J, Horejsi Z, Koed K, Kramer A, Tort F, et al. (2005) DNA damage response as a candidate anti-cancer barrier in early human tumorigenesis. Nature 434: 864-870.
    • (2005) Nature , vol.434 , pp. 864-870
    • Bartkova, J.1    Horejsi, Z.2    Koed, K.3    Kramer, A.4    Tort, F.5
  • 9
    • 17244366865 scopus 로고    scopus 로고
    • Activation of the DNA damage checkpoint and genomic instability in human precancerous lesions
    • Gorgoulis VG, Vassiliou LV, Karakaidos P, Zacharatos P, Kotsinas A, et al. (2005) Activation of the DNA damage checkpoint and genomic instability in human precancerous lesions. Nature 434: 907-913.
    • (2005) Nature , vol.434 , pp. 907-913
    • Gorgoulis, V.G.1    Vassiliou, L.V.2    Karakaidos, P.3    Zacharatos, P.4    Kotsinas, A.5
  • 10
    • 33747376928 scopus 로고    scopus 로고
    • DNA repair pathways in clinical practice: Lessons from pediatric cancer susceptibility syndromes
    • Kennedy RD, D'Andrea AD (2006) DNA repair pathways in clinical practice: lessons from pediatric cancer susceptibility syndromes. J Clin Oncol 24: 3799-3808.
    • (2006) J Clin Oncol , vol.24 , pp. 3799-3808
    • Kennedy, R.D.1    D'Andrea, A.D.2
  • 11
    • 0035093737 scopus 로고    scopus 로고
    • DNA double-strand breaks: Signaling, repair and the cancer connection
    • Khanna KK, Jackson SP (2001) DNA double-strand breaks: signaling, repair and the cancer connection. Nat Genet 27: 247-254.
    • (2001) Nat Genet , vol.27 , pp. 247-254
    • Khanna, K.K.1    Jackson, S.P.2
  • 12
    • 0037472924 scopus 로고    scopus 로고
    • DNA damage activates ATM through intermolecular autophosphorylation and dimer dissociation
    • Bakkenist CJ, Kastan MB (2003) DNA damage activates ATM through intermolecular autophosphorylation and dimer dissociation. Nature 421: 499-506.
    • (2003) Nature , vol.421 , pp. 499-506
    • Bakkenist, C.J.1    Kastan, M.B.2
  • 13
    • 33644905252 scopus 로고    scopus 로고
    • Changes in chromatin structure and mobility in living cells at sites of DNA double-strand breaks
    • Kruhlak MJ, Celeste A, Dellaire G, Fernandez-Capetillo O, Muller WG, et al. (2006) Changes in chromatin structure and mobility in living cells at sites of DNA double-strand breaks. J Cell Biol 172: 823-834.
    • (2006) J Cell Biol , vol.172 , pp. 823-834
    • Kruhlak, M.J.1    Celeste, A.2    Dellaire, G.3    Fernandez-Capetillo, O.4    Muller, W.G.5
  • 14
    • 37549028411 scopus 로고    scopus 로고
    • DNA damage-induced acetylation of lysine 3016 of ATM activates ATM kinase activity
    • Sun Y, Xu Y, Roy K, Price BD (2007) DNA damage-induced acetylation of lysine 3016 of ATM activates ATM kinase activity. Mol Cell Biol 27: 8502-8509.
    • (2007) Mol Cell Biol , vol.27 , pp. 8502-8509
    • Sun, Y.1    Xu, Y.2    Roy, K.3    Price, B.D.4
  • 15
    • 22944462083 scopus 로고    scopus 로고
    • Dynamic assembly and sustained retention of 53BP1 at the sites of DNA damage are controlled by Mdc1/NFBD1
    • Bekker-Jensen S, Lukas C, Melander F, Bartek J, Lukas J (2005) Dynamic assembly and sustained retention of 53BP1 at the sites of DNA damage are controlled by Mdc1/NFBD1. J Cell Biol 170: 201-211.
    • (2005) J Cell Biol , vol.170 , pp. 201-211
    • Bekker-Jensen, S.1    Lukas, C.2    Melander, F.3    Bartek, J.4    Lukas, J.5
  • 17
    • 29244434544 scopus 로고    scopus 로고
    • MDC1 directly binds phosphorylated histone H2AX to regulate cellular responses to DNA double-strand breaks
    • Stucki M, Clapperton JA, Mohammad D, Yaffe MB, Smerdon SJ, et al. (2005) MDC1 directly binds phosphorylated histone H2AX to regulate cellular responses to DNA double-strand breaks. Cell 123: 1213-1226.
    • (2005) Cell , vol.123 , pp. 1213-1226
    • Stucki, M.1    Clapperton, J.A.2    Mohammad, D.3    Yaffe, M.B.4    Smerdon, S.J.5
  • 18
    • 57049124828 scopus 로고    scopus 로고
    • 53BP1 facilitates long-range DNA end-joining during V(D)J recombination
    • Difilippantonio S, Gapud E, Wong N, Huang CY, Mahowald G, et al. (2008) 53BP1 facilitates long-range DNA end-joining during V(D)J recombination. Nature 456: 529-533.
    • (2008) Nature , vol.456 , pp. 529-533
    • Difilippantonio, S.1    Gapud, E.2    Wong, N.3    Huang, C.Y.4    Mahowald, G.5
  • 19
    • 57049132043 scopus 로고    scopus 로고
    • 53BP1 promotes nonhomologous end joining of telomeres by increasing chromatin mobility
    • Dimitrova N, Chen YC, Spector DL, de Lange T (2008) 53BP1 promotes nonhomologous end joining of telomeres by increasing chromatin mobility. Nature 456: 524-528.
    • (2008) Nature , vol.456 , pp. 524-528
    • Dimitrova, N.1    Chen, Y.C.2    Spector, D.L.3    de Lange, T.4
  • 21
    • 60549094422 scopus 로고    scopus 로고
    • Cell cycle control by the CDC25 phosphatases. Anticancer Agents
    • Aressy B, Ducommun B (2008) Cell cycle control by the CDC25 phosphatases. Anticancer Agents Med Chem 8: 818-824.
    • (2008) Med Chem , vol.8 , pp. 818-824
    • Aressy, B.1    Ducommun, B.2
  • 22
    • 1842486794 scopus 로고    scopus 로고
    • Cdc25A phosphatase: Combinatorial phosphorylation, ubiquitylation and proteolysis
    • Busino L, Chiesa M, Draetta GF, Donzelli M (2004) Cdc25A phosphatase: combinatorial phosphorylation, ubiquitylation and proteolysis. Oncogene 23: 2050-2056.
    • (2004) Oncogene , vol.23 , pp. 2050-2056
    • Busino, L.1    Chiesa, M.2    Draetta, G.F.3    Donzelli, M.4
  • 24
    • 33645962172 scopus 로고    scopus 로고
    • Posttranscriptional derepression of GADD45alpha by genotoxic stress
    • Lal A, Abdelmohsen K, Pullmann R, Kawai T, Galban S, et al. (2006) Posttranscriptional derepression of GADD45alpha by genotoxic stress. Mol Cell 22: 117-128.
    • (2006) Mol Cell , vol.22 , pp. 117-128
    • Lal, A.1    Abdelmohsen, K.2    Pullmann, R.3    Kawai, T.4    Galban, S.5
  • 25
    • 35548978945 scopus 로고    scopus 로고
    • The impact of a negligent G2/M checkpoint on genomic instability and cancer induction
    • Lobrich M, Jeggo PA (2007) The impact of a negligent G2/M checkpoint on genomic instability and cancer induction. Nat Rev Cancer 7: 861-869.
    • (2007) Nat Rev Cancer , vol.7 , pp. 861-869
    • Lobrich, M.1    Jeggo, P.A.2
  • 26
    • 0034437899 scopus 로고    scopus 로고
    • Arrest, adaptation, and recovery following a chromosome double-strand break in Saccharomyces cerevisiae
    • Lee SE, Pellicioli A, Demeter J, Vaze MP, Gasch AP, et al. (2000) Arrest, adaptation, and recovery following a chromosome double-strand break in Saccharomyces cerevisiae. Cold Spring Harb Symp Quant Biol 65: 303-314.
    • (2000) Cold Spring Harb Symp Quant Biol , vol.65 , pp. 303-314
    • Lee, S.E.1    Pellicioli, A.2    Demeter, J.3    Vaze, M.P.4    Gasch, A.P.5
  • 27
    • 14644438485 scopus 로고    scopus 로고
    • Checkpoint adaptation and recovery: Back with Polo after the break
    • van Vugt MA, Medema RH (2004) Checkpoint adaptation and recovery: back with Polo after the break. Cell Cycle 3: 1383-1386.
    • (2004) Cell Cycle , vol.3 , pp. 1383-1386
    • van Vugt, M.A.1    Medema, R.H.2
  • 28
    • 0344643062 scopus 로고    scopus 로고
    • PP2C phosphatases Ptc2 and Ptc3 are required for DNA checkpoint inactivation after a double-strand break
    • Leroy C, Lee SE, Vaze MB, Ochsenbien F, Guerois R, et al. (2003) PP2C phosphatases Ptc2 and Ptc3 are required for DNA checkpoint inactivation after a double-strand break. Mol Cell 11: 827-835.
    • (2003) Mol Cell , vol.11 , pp. 827-835
    • Leroy, C.1    Lee, S.E.2    Vaze, M.B.3    Ochsenbien, F.4    Guerois, R.5
  • 29
    • 0030885666 scopus 로고    scopus 로고
    • CDC5 and CKII control adaptation to the yeast DNA damage checkpoint
    • Toczyski DP, Galgoczy DJ, Hartwell LH (1997) CDC5 and CKII control adaptation to the yeast DNA damage checkpoint. Cell 90: 1097-1106.
    • (1997) Cell , vol.90 , pp. 1097-1106
    • Toczyski, D.P.1    Galgoczy, D.J.2    Hartwell, L.H.3
  • 30
    • 0036671706 scopus 로고    scopus 로고
    • Recovery from checkpoint-mediated arrest after repair of a double-strand break requires Srs2 helicase
    • Vaze MB, Pellicioli A, Lee SE, Ira G, Liberi G, et al. (2002) Recovery from checkpoint-mediated arrest after repair of a double-strand break requires Srs2 helicase. Mol Cell 10: 373-385.
    • (2002) Mol Cell , vol.10 , pp. 373-385
    • Vaze, M.B.1    Pellicioli, A.2    Lee, S.E.3    Ira, G.4    Liberi, G.5
  • 31
    • 33751301357 scopus 로고    scopus 로고
    • Adaptation to the ionizing radiation-induced G2 checkpoint occurs in human cells and depends on checkpoint kinase 1 and Polo-like kinase 1 kinases
    • Syljuasen RG, Jensen S, Bartek J, Lukas J (2006) Adaptation to the ionizing radiation-induced G2 checkpoint occurs in human cells and depends on checkpoint kinase 1 and Polo-like kinase 1 kinases. Cancer Res 66: 10253-10257.
    • (2006) Cancer Res , vol.66 , pp. 10253-10257
    • Syljuasen, R.G.1    Jensen, S.2    Bartek, J.3    Lukas, J.4
  • 32
    • 4444321565 scopus 로고    scopus 로고
    • Polo-like kinase-1 controls recovery from a G2 DNA damage-induced arrest in mammalian cells
    • van Vugt MA, Bras A, Medema RH (2004) Polo-like kinase-1 controls recovery from a G2 DNA damage-induced arrest in mammalian cells. Mol Cell 15: 799-811.
    • (2004) Mol Cell , vol.15 , pp. 799-811
    • van Vugt, M.A.1    Bras, A.2    Medema, R.H.3
  • 33
    • 2542459341 scopus 로고    scopus 로고
    • Adaptation of a DNA replication checkpoint response depends upon inactivation of Claspin by the Polo-like kinase
    • Yoo HY, Kumagai A, Shevchenko A, Shevchenko A, Dunphy WG (2004) Adaptation of a DNA replication checkpoint response depends upon inactivation of Claspin by the Polo-like kinase. Cell 117: 575-588.
    • (2004) Cell , vol.117 , pp. 575-588
    • Yoo, H.Y.1    Kumagai, A.2    Shevchenko, A.3    Shevchenko, A.4    Dunphy, W.G.5
  • 34
    • 33746429958 scopus 로고    scopus 로고
    • Destruction of Claspin by SCFbetaTrCP restrains Chk1 activation and facilitates recovery from genotoxic stress
    • Mailand N, Bekker-Jensen S, Bartek J, Lukas J (2006) Destruction of Claspin by SCFbetaTrCP restrains Chk1 activation and facilitates recovery from genotoxic stress. Mol Cell 23: 307-318.
    • (2006) Mol Cell , vol.23 , pp. 307-318
    • Mailand, N.1    Bekker-Jensen, S.2    Bartek, J.3    Lukas, J.4
  • 35
    • 33749246225 scopus 로고    scopus 로고
    • Polo-like Kinase-1 controls proteasome-dependent degradation of claspin during checkpoint recovery
    • Mamely I, van Vugt MA, Smits VA, Semple JI, Lemmens B, et al. (2006) Polo-like Kinase-1 controls proteasome-dependent degradation of claspin during checkpoint recovery. Curr Biol 16: 1950-1955.
    • (2006) Curr Biol , vol.16 , pp. 1950-1955
    • Mamely, I.1    van Vugt, M.A.2    Smits, V.A.3    Semple, J.I.4    Lemmens, B.5
  • 36
    • 33746413746 scopus 로고    scopus 로고
    • SCFbetaTrCP-mediated degradation of Claspin regulates recovery from the DNA replication checkpoint response
    • Peschiaroli A, Dorrello NV, Guardavaccaro D, Venere M, Halazonetis T, et al. (2006) SCFbetaTrCP-mediated degradation of Claspin regulates recovery from the DNA replication checkpoint response. Mol Cell 23: 319-329.
    • (2006) Mol Cell , vol.23 , pp. 319-329
    • Peschiaroli, A.1    Dorrello, N.V.2    Guardavaccaro, D.3    Venere, M.4    Halazonetis, T.5
  • 38
    • 1642458099 scopus 로고    scopus 로고
    • Ordered proteolysis in anaphase inactivates Plk1 to contribute to proper mitotic exit in human cells
    • Lindon C, Pines J (2004) Ordered proteolysis in anaphase inactivates Plk1 to contribute to proper mitotic exit in human cells. J Cell Biol 164: 233-241.
    • (2004) J Cell Biol , vol.164 , pp. 233-241
    • Lindon, C.1    Pines, J.2
  • 39
    • 0037195281 scopus 로고    scopus 로고
    • DNA damage during mitosis in human cells delays the metaphase/anaphase transition via the spindle-assembly checkpoint
    • Mikhailov A, Cole RW, Rieder CL (2002) DNA damage during mitosis in human cells delays the metaphase/anaphase transition via the spindle-assembly checkpoint. Curr Biol 12: 1797-1806.
    • (2002) Curr Biol , vol.12 , pp. 1797-1806
    • Mikhailov, A.1    Cole, R.W.2    Rieder, C.L.3
  • 40
    • 36348942399 scopus 로고    scopus 로고
    • Mitosis persists in the absence of Cdk1 activity when proteolysis or protein phosphatase activity is suppressed
    • Skoufias DA, Indorato RL, Lacroix F, Panopoulos A, Margolis RL (2007) Mitosis persists in the absence of Cdk1 activity when proteolysis or protein phosphatase activity is suppressed. J Cell Biol 179: 671-685.
    • (2007) J Cell Biol , vol.179 , pp. 671-685
    • Skoufias, D.A.1    Indorato, R.L.2    Lacroix, F.3    Panopoulos, A.4    Margolis, R.L.5
  • 43
    • 2942598149 scopus 로고    scopus 로고
    • PhosphoSite: A bioinformatics resource dedicated to physiological protein phosphorylation
    • Hornbeck PV, Chabra I, Kornhauser JM, Skrzypek E, Zhang B (2004) PhosphoSite: a bioinformatics resource dedicated to physiological protein phosphorylation. Proteomics 4: 1551-1561.
    • (2004) Proteomics , vol.4 , pp. 1551-1561
    • Hornbeck, P.V.1    Chabra, I.2    Kornhauser, J.M.3    Skrzypek, E.4    Zhang, B.5
  • 44
    • 34247605084 scopus 로고    scopus 로고
    • Proteomic screen defines the Polo-box domain interactome and identifies Rock2 as a Plk1 substrate
    • Lowery DM, Clauser KR, Hjerrild M, Lim D, Alexander J, et al. (2007) Proteomic screen defines the Polo-box domain interactome and identifies Rock2 as a Plk1 substrate. Embo J 26: 2262-2273.
    • (2007) Embo J , vol.26 , pp. 2262-2273
    • Lowery, D.M.1    Clauser, K.R.2    Hjerrild, M.3    Lim, D.4    Alexander, J.5
  • 47
    • 70349526350 scopus 로고    scopus 로고
    • Comparative analysis reveals conserved protein phosphorylation networks implicated in multiple diseases
    • Tan CS, Bodenmiller B, Pasculescu A, Jovanovic M, Hengartner MO, et al. (2009) Comparative analysis reveals conserved protein phosphorylation networks implicated in multiple diseases. Sci Signal 2: ra39.
    • (2009) Sci Signal , vol.2
    • Tan, C.S.1    Bodenmiller, B.2    Pasculescu, A.3    Jovanovic, M.4    Hengartner, M.O.5
  • 48
    • 0042622251 scopus 로고    scopus 로고
    • Scansite 2.0: Proteome-wide prediction of cell signaling interactions using short sequence motifs
    • Obenauer JC, Cantley LC, Yaffe MB (2003) Scansite 2.0: proteome-wide prediction of cell signaling interactions using short sequence motifs. Nucleic Acids Res 31: 3635-3641.
    • (2003) Nucleic Acids Res , vol.31 , pp. 3635-3641
    • Obenauer, J.C.1    Cantley, L.C.2    Yaffe, M.B.3
  • 49
    • 0242515843 scopus 로고    scopus 로고
    • Proteomic screen finds pSer/pThr-binding domain localizing Plk1 to mitotic substrates
    • Elia AE, Cantley LC, Yaffe MB (2003) Proteomic screen finds pSer/pThr-binding domain localizing Plk1 to mitotic substrates. Science 299: 1228-1231.
    • (2003) Science , vol.299 , pp. 1228-1231
    • Elia, A.E.1    Cantley, L.C.2    Yaffe, M.B.3
  • 50
    • 10744221449 scopus 로고    scopus 로고
    • The molecular basis for phosphodependent substrate targeting and regulation of Plks by the Polo-box domain
    • Elia AE, Rellos P, Haire LF, Chao JW, Ivins FJ, et al. (2003) The molecular basis for phosphodependent substrate targeting and regulation of Plks by the Polo-box domain. Cell 115: 83-95.
    • (2003) Cell , vol.115 , pp. 83-95
    • Elia, A.E.1    Rellos, P.2    Haire, L.F.3    Chao, J.W.4    Ivins, F.J.5
  • 51
    • 0037322744 scopus 로고    scopus 로고
    • Active cyclin B1-Cdk1 first appears on centrosomes in prophase
    • Jackman M, Lindon C, Nigg EA, Pines J (2003) Active cyclin B1-Cdk1 first appears on centrosomes in prophase. Nat Cell Biol 5: 143-148.
    • (2003) Nat Cell Biol , vol.5 , pp. 143-148
    • Jackman, M.1    Lindon, C.2    Nigg, E.A.3    Pines, J.4
  • 53
    • 0037468169 scopus 로고    scopus 로고
    • MDC1 is required for the intra-S-phase DNA damage checkpoint
    • Goldberg M, Stucki M, Falck J, D'Amours D, Rahman D, et al. (2003) MDC1 is required for the intra-S-phase DNA damage checkpoint. Nature 421: 952-956.
    • (2003) Nature , vol.421 , pp. 952-956
    • Goldberg, M.1    Stucki, M.2    Falck, J.3    D'Amours, D.4    Rahman, D.5
  • 54
    • 0037468232 scopus 로고    scopus 로고
    • MDC1 is coupled to activated CHK2 in mammalian DNA damage response pathways
    • Lou Z, Minter-Dykhouse K, Wu X, Chen J (2003) MDC1 is coupled to activated CHK2 in mammalian DNA damage response pathways. Nature 421: 957-961.
    • (2003) Nature , vol.421 , pp. 957-961
    • Lou, Z.1    Minter-Dykhouse, K.2    Wu, X.3    Chen, J.4
  • 55
    • 0035972194 scopus 로고    scopus 로고
    • Tumor suppressor p53 binding protein 1 (53BP1) is involved in DNA damage-signaling pathways
    • Rappold I, Iwabuchi K, Date T, Chen J (2001) Tumor suppressor p53 binding protein 1 (53BP1) is involved in DNA damage-signaling pathways. J Cell Biol 153: 613-620.
    • (2001) J Cell Biol , vol.153 , pp. 613-620
    • Rappold, I.1    Iwabuchi, K.2    Date, T.3    Chen, J.4
  • 56
    • 0034739853 scopus 로고    scopus 로고
    • p53 binding protein 1 (53BP1) is an early participant in the cellular response to DNA double-strand breaks
    • Schultz LB, Chehab NH, Malikzay A, Halazonetis TD (2000) p53 binding protein 1 (53BP1) is an early participant in the cellular response to DNA double-strand breaks. J Cell Biol 151: 1381-1390.
    • (2000) J Cell Biol , vol.151 , pp. 1381-1390
    • Schultz, L.B.1    Chehab, N.H.2    Malikzay, A.3    Halazonetis, T.D.4
  • 58
    • 0028047288 scopus 로고
    • Cloning of cDNAs for M-phase phosphoproteins recognized by the MPM2 monoclonal antibody and determination of the phosphorylated epitope
    • Westendorf JM, Rao PN, Gerace L (1994) Cloning of cDNAs for M-phase phosphoproteins recognized by the MPM2 monoclonal antibody and determination of the phosphorylated epitope. Proc Natl Acad Sci U S A 91: 714-718.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 714-718
    • Westendorf, J.M.1    Rao, P.N.2    Gerace, L.3
  • 59
    • 0031438929 scopus 로고    scopus 로고
    • Sequence-specific and phosphorylation-dependent proline isomerization: A potential mitotic regulatory mechanism
    • Yaffe MB, Schutkowski M, Shen M, Zhou XZ, Stukenberg PT, et al. (1997) Sequence-specific and phosphorylation-dependent proline isomerization: a potential mitotic regulatory mechanism. Science 278: 1957-1960.
    • (1997) Science , vol.278 , pp. 1957-1960
    • Yaffe, M.B.1    Schutkowski, M.2    Shen, M.3    Zhou, X.Z.4    Stukenberg, P.T.5
  • 60
    • 10744221485 scopus 로고    scopus 로고
    • In vivo activation of the p53 pathway by small-molecule antagonists of MDM2
    • Vassilev LT, Vu BT, Graves B, Carvajal D, Podlaski F, et al. (2004) In vivo activation of the p53 pathway by small-molecule antagonists of MDM2. Science 303: 844-848.
    • (2004) Science , vol.303 , pp. 844-848
    • Vassilev, L.T.1    Vu, B.T.2    Graves, B.3    Carvajal, D.4    Podlaski, F.5
  • 61
    • 33646343474 scopus 로고    scopus 로고
    • An shRNA barcode screen provides insight into cancer cell vulnerability to MDM2 inhibitors
    • Brummelkamp TR, Fabius AW, Mullenders J, Madiredjo M, Velds A, et al. (2006) An shRNA barcode screen provides insight into cancer cell vulnerability to MDM2 inhibitors. Nat Chem Biol 2: 202-206.
    • (2006) Nat Chem Biol , vol.2 , pp. 202-206
    • Brummelkamp, T.R.1    Fabius, A.W.2    Mullenders, J.3    Madiredjo, M.4    Velds, A.5
  • 62
    • 33846933218 scopus 로고    scopus 로고
    • BI 2536, a potent and selective inhibitor of polo-like kinase 1, inhibits tumor growth in vivo
    • Steegmaier M, Hoffmann M, Baum A, Lenart P, Petronczki M, et al. (2007) BI 2536, a potent and selective inhibitor of polo-like kinase 1, inhibits tumor growth in vivo. Curr Biol 17: 316-322.
    • (2007) Curr Biol , vol.17 , pp. 316-322
    • Steegmaier, M.1    Hoffmann, M.2    Baum, A.3    Lenart, P.4    Petronczki, M.5
  • 63
    • 33846931644 scopus 로고    scopus 로고
    • The small-molecule inhibitor BI 2536 reveals novel insights into mitotic roles of polo-like kinase 1
    • Lenart P, Petronczki M, Steegmaier M, Di Fiore B, Lipp JJ, et al. (2007) The small-molecule inhibitor BI 2536 reveals novel insights into mitotic roles of polo-like kinase 1. Curr Biol 17: 304-315.
    • (2007) Curr Biol , vol.17 , pp. 304-315
    • Lenart, P.1    Petronczki, M.2    Steegmaier, M.3    Di Fiore, B.4    Lipp, J.J.5
  • 64
    • 0038624074 scopus 로고    scopus 로고
    • Polo-like kinase (Plk)1 depletion induces apoptosis in cancer cells
    • Liu X, Erikson RL (2003) Polo-like kinase (Plk)1 depletion induces apoptosis in cancer cells. Proc Natl Acad Sci U S A 100: 5789-5794.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 5789-5794
    • Liu, X.1    Erikson, R.L.2
  • 65
    • 51349144633 scopus 로고    scopus 로고
    • Polo-like kinase-1 is activated by aurora A to promote checkpoint recovery
    • Macurek L, Lindqvist A, Lim D, Lampson MA, Klompmaker R, et al. (2008) Polo-like kinase-1 is activated by aurora A to promote checkpoint recovery. Nature 455: 119-123.
    • (2008) Nature , vol.455 , pp. 119-123
    • Macurek, L.1    Lindqvist, A.2    Lim, D.3    Lampson, M.A.4    Klompmaker, R.5
  • 66
    • 4344718620 scopus 로고    scopus 로고
    • Polo-like kinase-1 is required for bipolar spindle formation but is dispensable for anaphase promoting complex/Cdc20 activation and initiation of cytokinesis
    • van Vugt MA, van de Weerdt BC, Vader G, Janssen H, Calafat J, et al. (2004) Polo-like kinase-1 is required for bipolar spindle formation but is dispensable for anaphase promoting complex/Cdc20 activation and initiation of cytokinesis. J Biol Chem 279: 36841-36854.
    • (2004) J Biol Chem , vol.279 , pp. 36841-36854
    • van Vugt, M.A.1    van de Weerdt, B.C.2    Vader, G.3    Janssen, H.4    Calafat, J.5
  • 67
    • 0036902410 scopus 로고    scopus 로고
    • 53BP1 functions in an ATM-dependent checkpoint pathway that is constitutively activated in human cancer
    • DiTullio RA Jr, Mochan TA, Venere M, Bartkova J, Sehested M, et al. (2002) 53BP1 functions in an ATM-dependent checkpoint pathway that is constitutively activated in human cancer. Nat Cell Biol 4: 998-1002.
    • (2002) Nat Cell Biol , vol.4 , pp. 998-1002
    • DiTullio Jr, R.A.1    Mochan, T.A.2    Venere, M.3    Bartkova, J.4    Sehested, M.5
  • 68
    • 0032475885 scopus 로고    scopus 로고
    • Stimulation of p53-mediated transcriptional activation by the p53-binding proteins, 53BP1 and 53BP2
    • Iwabuchi K, Li B, Massa HF, Trask BJ, Date T, et al. (1998) Stimulation of p53-mediated transcriptional activation by the p53-binding proteins, 53BP1 and 53BP2. J Biol Chem 273: 26061-26068.
    • (1998) J Biol Chem , vol.273 , pp. 26061-26068
    • Iwabuchi, K.1    Li, B.2    Massa, H.F.3    Trask, B.J.4    Date, T.5
  • 69
    • 0038391226 scopus 로고    scopus 로고
    • NFBD1, like 53BP1, is an early and redundant transducer mediating Chk2 phosphorylation in response to DNA damage
    • Peng A, Chen PL (2003) NFBD1, like 53BP1, is an early and redundant transducer mediating Chk2 phosphorylation in response to DNA damage. J Biol Chem 278: 8873-8876.
    • (2003) J Biol Chem , vol.278 , pp. 8873-8876
    • Peng, A.1    Chen, P.L.2
  • 70
    • 0037378527 scopus 로고    scopus 로고
    • p53 Binding protein 53BP1 is required for DNA damage responses and tumor suppression in mice
    • Ward IM, Minn K, van Deursen J, Chen J (2003) p53 Binding protein 53BP1 is required for DNA damage responses and tumor suppression in mice. Mol Cell Biol 23: 2556-2563.
    • (2003) Mol Cell Biol , vol.23 , pp. 2556-2563
    • Ward, I.M.1    Minn, K.2    van Deursen, J.3    Chen, J.4
  • 71
    • 0346059615 scopus 로고    scopus 로고
    • 53BP1 and NFBD1/MDC1-Nbs1 function in parallel interacting pathways activating ataxia-telangiectasia mutated (ATM) in response to DNA damage
    • Mochan TA, Venere M, DiTullio RA Jr, Halazonetis TD (2003) 53BP1 and NFBD1/MDC1-Nbs1 function in parallel interacting pathways activating ataxia-telangiectasia mutated (ATM) in response to DNA damage. Cancer Res 63: 8586-8591.
    • (2003) Cancer Res , vol.63 , pp. 8586-8591
    • Mochan, T.A.1    Venere, M.2    DiTullio Jr, R.A.3    Halazonetis, T.D.4
  • 72
    • 56449084007 scopus 로고    scopus 로고
    • NFBD1/MDC1, 53BP1 and BRCA1 have both redundant and unique roles in the ATM pathway
    • Wilson KA, Stern DF (2008) NFBD1/MDC1, 53BP1 and BRCA1 have both redundant and unique roles in the ATM pathway. Cell Cycle 7: 3584-3594.
    • (2008) Cell Cycle , vol.7 , pp. 3584-3594
    • Wilson, K.A.1    Stern, D.F.2
  • 73
    • 0034326802 scopus 로고    scopus 로고
    • Threonine 68 phosphorylation by ataxia telangiectasia mutated is required for efficient activation of Chk2 in response to ionizing radiation
    • Ahn JY, Schwarz JK, Piwnica-Worms H, Canman CE (2000) Threonine 68 phosphorylation by ataxia telangiectasia mutated is required for efficient activation of Chk2 in response to ionizing radiation. Cancer Res 60: 5934-5936.
    • (2000) Cancer Res , vol.60 , pp. 5934-5936
    • Ahn, J.Y.1    Schwarz, J.K.2    Piwnica-Worms, H.3    Canman, C.E.4
  • 74
    • 0035839526 scopus 로고    scopus 로고
    • The hCds1 (Chk2)-FHA domain is essential for a chain of phosphorylation events on hCds1 that is induced by ionizing radiation
    • Lee CH, Chung JH (2001) The hCds1 (Chk2)-FHA domain is essential for a chain of phosphorylation events on hCds1 that is induced by ionizing radiation. J Biol Chem 276: 30537-30541.
    • (2001) J Biol Chem , vol.276 , pp. 30537-30541
    • Lee, C.H.1    Chung, J.H.2
  • 75
    • 58149084898 scopus 로고    scopus 로고
    • Chk2 oligomerization studied by phosphopeptide ligation: Implications for regulation and phosphodependent interactions
    • Li J, Taylor IA, Lloyd J, Clapperton JA, Howell S, et al. (2008) Chk2 oligomerization studied by phosphopeptide ligation: implications for regulation and phosphodependent interactions. J Biol Chem 283: 36019-36030.
    • (2008) J Biol Chem , vol.283 , pp. 36019-36030
    • Li, J.1    Taylor, I.A.2    Lloyd, J.3    Clapperton, J.A.4    Howell, S.5
  • 76
    • 0036258583 scopus 로고    scopus 로고
    • Chk2 activation and phosphorylation-dependent oligomerization
    • Xu X, Tsvetkov LM, Stern DF (2002) Chk2 activation and phosphorylation-dependent oligomerization. Mol Cell Biol 22: 4419-4432.
    • (2002) Mol Cell Biol , vol.22 , pp. 4419-4432
    • Xu, X.1    Tsvetkov, L.M.2    Stern, D.F.3
  • 77
    • 0038492408 scopus 로고    scopus 로고
    • Identification of a consensus motif for Plk (Polo-like kinase) phosphorylation reveals Myt1 as a Plk1 substrate
    • Nakajima H, Toyoshima-Morimoto F, Taniguchi E, Nishida E (2003) Identification of a consensus motif for Plk (Polo-like kinase) phosphorylation reveals Myt1 as a Plk1 substrate. J Biol Chem 278: 25277-25280.
    • (2003) J Biol Chem , vol.278 , pp. 25277-25280
    • Nakajima, H.1    Toyoshima-Morimoto, F.2    Taniguchi, E.3    Nishida, E.4
  • 78
    • 0036285705 scopus 로고    scopus 로고
    • Structural and functional versatility of the FHA domain in DNA-damage signaling by the tumor suppressor kinase Chk2
    • Li J, Williams BL, Haire LF, Goldberg M, Wilker E, et al. (2002) Structural and functional versatility of the FHA domain in DNA-damage signaling by the tumor suppressor kinase Chk2. Mol Cell 9: 1045-1054.
    • (2002) Mol Cell , vol.9 , pp. 1045-1054
    • Li, J.1    Williams, B.L.2    Haire, L.F.3    Goldberg, M.4    Wilker, E.5
  • 79
    • 70349180626 scopus 로고    scopus 로고
    • Structure and activation mechanism of the CHK2 DNA damage checkpoint kinase
    • Cai Z, Chehab NH, Pavletich NP (2009) Structure and activation mechanism of the CHK2 DNA damage checkpoint kinase. Mol Cell 35: 818-829.
    • (2009) Mol Cell , vol.35 , pp. 818-829
    • Cai, Z.1    Chehab, N.H.2    Pavletich, N.P.3
  • 80
    • 63749131243 scopus 로고    scopus 로고
    • Kinases that control the cell cycle in response to DNA damage: Chk1, Chk2, and MK2
    • Reinhardt HC, Yaffe MB (2009) Kinases that control the cell cycle in response to DNA damage: Chk1, Chk2, and MK2. Curr Opin Cell Biol 21: 245-255.
    • (2009) Curr Opin Cell Biol , vol.21 , pp. 245-255
    • Reinhardt, H.C.1    Yaffe, M.B.2
  • 81
    • 0029829249 scopus 로고    scopus 로고
    • Defect in multiple cell cycle checkpoints in ataxia-telangiectasia postirradiation
    • Beamish H, Williams R, Chen P, Lavin MF (1996) Defect in multiple cell cycle checkpoints in ataxia-telangiectasia postirradiation. J Biol Chem 271: 20486-20493.
    • (1996) J Biol Chem , vol.271 , pp. 20486-20493
    • Beamish, H.1    Williams, R.2    Chen, P.3    Lavin, M.F.4
  • 83
    • 0035848819 scopus 로고    scopus 로고
    • The ATM-Chk2-Cdc25A checkpoint pathway guards against radioresistant DNA synthesis
    • Falck J, Mailand N, Syljuasen RG, Bartek J, Lukas J (2001) The ATM-Chk2-Cdc25A checkpoint pathway guards against radioresistant DNA synthesis. Nature 410: 842-847.
    • (2001) Nature , vol.410 , pp. 842-847
    • Falck, J.1    Mailand, N.2    Syljuasen, R.G.3    Bartek, J.4    Lukas, J.5
  • 84
    • 0032484084 scopus 로고    scopus 로고
    • Linkage of ATM to cell cycle regulation by the Chk2 protein kinase
    • Matsuoka S, Huang M, Elledge SJ (1998) Linkage of ATM to cell cycle regulation by the Chk2 protein kinase. Science 282: 1893-1897.
    • (1998) Science , vol.282 , pp. 1893-1897
    • Matsuoka, S.1    Huang, M.2    Elledge, S.J.3
  • 85
    • 0034306332 scopus 로고    scopus 로고
    • Threonine 68 is required for radiation-induced phosphorylation and activation of Cds1
    • Melchionna R, Chen XB, Blasina A, McGowan CH (2000) Threonine 68 is required for radiation-induced phosphorylation and activation of Cds1. Nat Cell Biol 2: 762-765.
    • (2000) Nat Cell Biol , vol.2 , pp. 762-765
    • Melchionna, R.1    Chen, X.B.2    Blasina, A.3    McGowan, C.H.4
  • 86
    • 0029057336 scopus 로고
    • A single ataxia telangiectasia gene with a product similar to PI-3 kinase
    • Savitsky K, Bar-Shira A, Gilad S, Rotman G, Ziv Y, et al. (1995) A single ataxia telangiectasia gene with a product similar to PI-3 kinase. Science 268: 1749-1753.
    • (1995) Science , vol.268 , pp. 1749-1753
    • Savitsky, K.1    Bar-Shira, A.2    Gilad, S.3    Rotman, G.4    Ziv, Y.5
  • 87
    • 18444379055 scopus 로고    scopus 로고
    • A CHEK2 genetic variant contributing to a substantial fraction of familial breast cancer
    • Vahteristo P, Bartkova J, Eerola H, Syrjakoski K, Ojala S, et al. (2002) A CHEK2 genetic variant contributing to a substantial fraction of familial breast cancer. Am J Hum Genet 71: 432-438.
    • (2002) Am J Hum Genet , vol.71 , pp. 432-438
    • Vahteristo, P.1    Bartkova, J.2    Eerola, H.3    Syrjakoski, K.4    Ojala, S.5
  • 88
    • 46249084662 scopus 로고    scopus 로고
    • Bora and the kinase Aurora A cooperatively activate the kinase Plk1 and control mitotic entry
    • Seki A, Coppinger JA, Jang CY, Yates JR, Fang G (2008) Bora and the kinase Aurora A cooperatively activate the kinase Plk1 and control mitotic entry. Science 320: 1655-1658.
    • (2008) Science , vol.320 , pp. 1655-1658
    • Seki, A.1    Coppinger, J.A.2    Jang, C.Y.3    Yates, J.R.4    Fang, G.5
  • 89
    • 33845666681 scopus 로고    scopus 로고
    • Structural basis for the methylation state-specific recognition of histone H4-K20 by 53BP1 and Crb2 in DNA repair
    • Botuyan MV, Lee J, Ward IM, Kim JE, Thompson JR, et al. (2006) Structural basis for the methylation state-specific recognition of histone H4-K20 by 53BP1 and Crb2 in DNA repair. Cell 127: 1361-1373.
    • (2006) Cell , vol.127 , pp. 1361-1373
    • Botuyan, M.V.1    Lee, J.2    Ward, I.M.3    Kim, J.E.4    Thompson, J.R.5
  • 90
    • 59049091728 scopus 로고    scopus 로고
    • RNF168 binds and amplifies ubiquitin conjugates on damaged chromosomes to allow accumulation of repair proteins
    • Doil C, Mailand N, Bekker-Jensen S, Menard P, Larsen DH, et al. (2009) RNF168 binds and amplifies ubiquitin conjugates on damaged chromosomes to allow accumulation of repair proteins. Cell 136: 435-446.
    • (2009) Cell , vol.136 , pp. 435-446
    • Doil, C.1    Mailand, N.2    Bekker-Jensen, S.3    Menard, P.4    Larsen, D.H.5
  • 91
    • 36249031962 scopus 로고    scopus 로고
    • RNF8 transduces the DNA-damage signal via histone ubiquitylation and checkpoint protein assembly
    • Huen MS, Grant R, Manke I, Minn K, Yu X, et al. (2007) RNF8 transduces the DNA-damage signal via histone ubiquitylation and checkpoint protein assembly. Cell 131: 901-914.
    • (2007) Cell , vol.131 , pp. 901-914
    • Huen, M.S.1    Grant, R.2    Manke, I.3    Minn, K.4    Yu, X.5
  • 92
    • 36248966246 scopus 로고    scopus 로고
    • RNF8 ubiquitylates histones at DNA double-strand breaks and promotes assembly of repair proteins
    • Mailand N, Bekker-Jensen S, Faustrup H, Melander F, Bartek J, et al. (2007) RNF8 ubiquitylates histones at DNA double-strand breaks and promotes assembly of repair proteins. Cell 131: 887-900.
    • (2007) Cell , vol.131 , pp. 887-900
    • Mailand, N.1    Bekker-Jensen, S.2    Faustrup, H.3    Melander, F.4    Bartek, J.5
  • 93
    • 59049103900 scopus 로고    scopus 로고
    • The RIDDLE syndrome protein mediates a ubiquitin-dependent signaling cascade at sites of DNA damage
    • Stewart GS, Panier S, Townsend K, Al-Hakim AK, Kolas NK, et al. (2009) The RIDDLE syndrome protein mediates a ubiquitin-dependent signaling cascade at sites of DNA damage. Cell 136: 420-434.
    • (2009) Cell , vol.136 , pp. 420-434
    • Stewart, G.S.1    Panier, S.2    Townsend, K.3    Al-Hakim, A.K.4    Kolas, N.K.5
  • 94
    • 33846015507 scopus 로고    scopus 로고
    • The tandem BRCT domain of 53BP1 is not required for its repair function
    • Ward I, Kim JE, Minn K, Chini CC, Mer G, et al. (2006) The tandem BRCT domain of 53BP1 is not required for its repair function. J Biol Chem 281: 38472-38477.
    • (2006) J Biol Chem , vol.281 , pp. 38472-38477
    • Ward, I.1    Kim, J.E.2    Minn, K.3    Chini, C.C.4    Mer, G.5
  • 95
    • 33646777783 scopus 로고    scopus 로고
    • Genetic dissection of vertebrate 53BP1: A major role in non-homologous end joining of DNA double strand breaks
    • Nakamura K, Sakai W, Kawamoto T, Bree RT, Lowndes NF, et al. (2006) Genetic dissection of vertebrate 53BP1: a major role in non-homologous end joining of DNA double strand breaks. DNA Repair 5: 741-749.
    • (2006) DNA Repair , vol.5 , pp. 741-749
    • Nakamura, K.1    Sakai, W.2    Kawamoto, T.3    Bree, R.T.4    Lowndes, N.F.5
  • 96
    • 0031438163 scopus 로고    scopus 로고
    • Damage and replication checkpoint control in fission yeast is ensured by interactions of Crb2, a protein with BRCT motif, with Cut5 and Chk1
    • Saka Y, Esashi F, Matsusaka T, Mochida S, Yanagida M (1997) Damage and replication checkpoint control in fission yeast is ensured by interactions of Crb2, a protein with BRCT motif, with Cut5 and Chk1. Genes Dev 11: 3387-3400.
    • (1997) Genes Dev , vol.11 , pp. 3387-3400
    • Saka, Y.1    Esashi, F.2    Matsusaka, T.3    Mochida, S.4    Yanagida, M.5
  • 97
    • 0035105240 scopus 로고    scopus 로고
    • Regulation of Saccharomyces Rad53 checkpoint kinase during adaptation from DNA damage-induced G2/M arrest
    • Pellicioli A, Lee SE, Lucca C, Foiani M, Haber JE (2001) Regulation of Saccharomyces Rad53 checkpoint kinase during adaptation from DNA damage-induced G2/M arrest. Mol Cell 7: 293-300.
    • (2001) Mol Cell , vol.7 , pp. 293-300
    • Pellicioli, A.1    Lee, S.E.2    Lucca, C.3    Foiani, M.4    Haber, J.E.5
  • 98
    • 0032133216 scopus 로고    scopus 로고
    • MEC1-dependent phosphorylation of Rad9p in response to DNA damage
    • Emili A (1998) MEC1-dependent phosphorylation of Rad9p in response to DNA damage. Mol Cell 2: 183-189.
    • (1998) Mol Cell , vol.2 , pp. 183-189
    • Emili, A.1
  • 99
    • 0032504069 scopus 로고    scopus 로고
    • Rad53 FHA domain associated with phosphorylated Rad9 in the DNA damage checkpoint
    • Sun Z, Hsiao J, Fay DS, Stern DF (1998) Rad53 FHA domain associated with phosphorylated Rad9 in the DNA damage checkpoint. Science 281: 272-274.
    • (1998) Science , vol.281 , pp. 272-274
    • Sun, Z.1    Hsiao, J.2    Fay, D.S.3    Stern, D.F.4
  • 100
    • 0032189952 scopus 로고    scopus 로고
    • The budding yeast Rad9 checkpoint protein is subjected to Mec1/Tel1-dependent hyperphosphorylation and interacts with Rad53 after DNA damage
    • Vialard JE, Gilbert CS, Green CM, Lowndes NF (1998) The budding yeast Rad9 checkpoint protein is subjected to Mec1/Tel1-dependent hyperphosphorylation and interacts with Rad53 after DNA damage. Embo J 17: 5679-5688.
    • (1998) Embo J , vol.17 , pp. 5679-5688
    • Vialard, J.E.1    Gilbert, C.S.2    Green, C.M.3    Lowndes, N.F.4
  • 101
    • 27144507868 scopus 로고    scopus 로고
    • Cytokinesis failure generating tetraploids promotes tumorigenesis in p53-null cells
    • Fujiwara T, Bandi M, Nitta M, Ivanova EV, Bronson RT, et al. (2005) Cytokinesis failure generating tetraploids promotes tumorigenesis in p53-null cells. Nature 437: 1043-1047.
    • (2005) Nature , vol.437 , pp. 1043-1047
    • Fujiwara, T.1    Bandi, M.2    Nitta, M.3    Ivanova, E.V.4    Bronson, R.T.5
  • 102
    • 27144518175 scopus 로고    scopus 로고
    • Chromosome nondisjunction yields tetraploid rather than aneuploid cells in human cell lines
    • Shi Q, King RW (2005) Chromosome nondisjunction yields tetraploid rather than aneuploid cells in human cell lines. Nature 437: 1038-1042.
    • (2005) Nature , vol.437 , pp. 1038-1042
    • Shi, Q.1    King, R.W.2
  • 104
    • 33645316142 scopus 로고    scopus 로고
    • Targeting polo-like kinase 1 for cancer therapy
    • Strebhardt K, Ullrich A (2006) Targeting polo-like kinase 1 for cancer therapy. Nat Rev Cancer 6: 321-330.
    • (2006) Nat Rev Cancer , vol.6 , pp. 321-330
    • Strebhardt, K.1    Ullrich, A.2
  • 105
    • 62649112876 scopus 로고    scopus 로고
    • A panel of isogenic human cancer cells suggests a therapeutic approach for cancers with inactivated p53
    • Sur S, Pagliarini R, Bunz F, Rago C, Diaz LA Jr, et al. (2009) A panel of isogenic human cancer cells suggests a therapeutic approach for cancers with inactivated p53. Proc Natl Acad Sci U S A 106: 3964-3969.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 3964-3969
    • Sur, S.1    Pagliarini, R.2    Bunz, F.3    Rago, C.4    Diaz Jr, L.A.5
  • 107
    • 13744252890 scopus 로고    scopus 로고
    • MAFFT version 5: Improvement in accuracy of multiple sequence alignment
    • Katoh K, Kuma K, Toh H, Miyata T (2005) MAFFT version 5: improvement in accuracy of multiple sequence alignment. Nucleic Acids Res 33: 511-518.
    • (2005) Nucleic Acids Res , vol.33 , pp. 511-518
    • Katoh, K.1    Kuma, K.2    Toh, H.3    Miyata, T.4
  • 109
    • 0842320458 scopus 로고    scopus 로고
    • A high-throughput quantitative multiplex kinase assay for monitoring information flow in signaling networks: Application to sepsis-apoptosis
    • Janes KA, Albeck JG, Peng LX, Sorger PK, Lauffenburger DA, et al. (2003) A high-throughput quantitative multiplex kinase assay for monitoring information flow in signaling networks: application to sepsis-apoptosis. Mol Cell Proteomics 2: 463-473.
    • (2003) Mol Cell Proteomics , vol.2 , pp. 463-473
    • Janes, K.A.1    Albeck, J.G.2    Peng, L.X.3    Sorger, P.K.4    Lauffenburger, D.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.