메뉴 건너뛰기




Volumn 65, Issue 5, 2017, Pages 801-817.e4

NBS1 Phosphorylation Status Dictates Repair Choice of Dysfunctional Telomeres

Author keywords

[No Author keywords available]

Indexed keywords

CYCLIN DEPENDENT KINASE 2; HISTONE H2AX; NIBRIN; TELOMERIC REPEAT BINDING FACTOR 2; TUMOR SUPPRESSOR P53 BINDING PROTEIN 1; AMINOPEPTIDASE; ATM PROTEIN; ATM PROTEIN, HUMAN; BIRC6 PROTEIN, HUMAN; CDK2 PROTEIN, HUMAN; CELL CYCLE PROTEIN; DCLRE1B PROTEIN, HUMAN; DIPEPTIDYL PEPTIDASE; DNA LIGASE; INHIBITOR OF APOPTOSIS PROTEIN; NBN PROTEIN, HUMAN; NIJMEGEN BREAKAGE SYNDROME 1 PROTEIN, MOUSE; NUCLEAR PROTEIN; POT1 PROTEIN, HUMAN; PROTEIN BINDING; SERINE PROTEINASE; TELOMERE BINDING PROTEIN; TERF2 PROTEIN, HUMAN; TRF2 PROTEIN, MOUSE; TRIPEPTIDYL-PEPTIDASE 1;

EID: 85012899182     PISSN: 10972765     EISSN: 10974164     Source Type: Journal    
DOI: 10.1016/j.molcel.2017.01.016     Document Type: Article
Times cited : (46)

References (74)
  • 2
    • 23144451917 scopus 로고    scopus 로고
    • Cdc2-cyclin E complexes regulate the G1/S phase transition
    • Aleem, E., Kiyokawa, H., Kaldis, P., Cdc2-cyclin E complexes regulate the G1/S phase transition. Nat. Cell Biol. 7 (2005), 831–836.
    • (2005) Nat. Cell Biol. , vol.7 , pp. 831-836
    • Aleem, E.1    Kiyokawa, H.2    Kaldis, P.3
  • 3
    • 0032512720 scopus 로고    scopus 로고
    • Isolation and characterization of PNUTS, a putative protein phosphatase 1 nuclear targeting subunit
    • Allen, P.B., Kwon, Y.G., Nairn, A.C., Greengard, P., Isolation and characterization of PNUTS, a putative protein phosphatase 1 nuclear targeting subunit. J. Biol. Chem. 273 (1998), 4089–4095.
    • (1998) J. Biol. Chem. , vol.273 , pp. 4089-4095
    • Allen, P.B.1    Kwon, Y.G.2    Nairn, A.C.3    Greengard, P.4
  • 4
    • 70350455474 scopus 로고    scopus 로고
    • The mre11 complex and the response to dysfunctional telomeres
    • Attwooll, C.L., Akpinar, M., Petrini, J.H., The mre11 complex and the response to dysfunctional telomeres. Mol. Cell. Biol. 29 (2009), 5540–5551.
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 5540-5551
    • Attwooll, C.L.1    Akpinar, M.2    Petrini, J.H.3
  • 5
    • 11244280890 scopus 로고    scopus 로고
    • Involvement of poly(ADP-ribose) polymerase-1 and XRCC1/DNA ligase III in an alternative route for DNA double-strand breaks rejoining
    • Audebert, M., Salles, B., Calsou, P., Involvement of poly(ADP-ribose) polymerase-1 and XRCC1/DNA ligase III in an alternative route for DNA double-strand breaks rejoining. J. Biol. Chem. 279 (2004), 55117–55126.
    • (2004) J. Biol. Chem. , vol.279 , pp. 55117-55126
    • Audebert, M.1    Salles, B.2    Calsou, P.3
  • 6
    • 0035964864 scopus 로고    scopus 로고
    • Strand-specific postreplicative processing of mammalian telomeres
    • Bailey, S.M., Cornforth, M.N., Kurimasa, A., Chen, D.J., Goodwin, E.H., Strand-specific postreplicative processing of mammalian telomeres. Science 293 (2001), 2462–2465.
    • (2001) Science , vol.293 , pp. 2462-2465
    • Bailey, S.M.1    Cornforth, M.N.2    Kurimasa, A.3    Chen, D.J.4    Goodwin, E.H.5
  • 7
    • 23144465155 scopus 로고    scopus 로고
    • Cdk1: the dominant sibling of Cdk2
    • Bashir, T., Pagano, M., Cdk1: the dominant sibling of Cdk2. Nat. Cell Biol. 7 (2005), 779–781.
    • (2005) Nat. Cell Biol. , vol.7 , pp. 779-781
    • Bashir, T.1    Pagano, M.2
  • 9
    • 0031172801 scopus 로고    scopus 로고
    • Constitutively active protein phosphatase 1alpha causes Rb-dependent G1 arrest in human cancer cells
    • Berndt, N., Dohadwala, M., Liu, C.W., Constitutively active protein phosphatase 1alpha causes Rb-dependent G1 arrest in human cancer cells. Curr. Biol. 7 (1997), 375–386.
    • (1997) Curr. Biol. , vol.7 , pp. 375-386
    • Berndt, N.1    Dohadwala, M.2    Liu, C.W.3
  • 10
    • 84856747932 scopus 로고    scopus 로고
    • Mre11 regulates CtIP-dependent double-strand break repair by interaction with CDK2
    • Buis, J., Stoneham, T., Spehalski, E., Ferguson, D.O., Mre11 regulates CtIP-dependent double-strand break repair by interaction with CDK2. Nat. Struct. Mol. Biol. 19 (2012), 246–252.
    • (2012) Nat. Struct. Mol. Biol. , vol.19 , pp. 246-252
    • Buis, J.1    Stoneham, T.2    Spehalski, E.3    Ferguson, D.O.4
  • 13
    • 22144490491 scopus 로고    scopus 로고
    • DNA processing is not required for ATM-mediated telomere damage response after TRF2 deletion
    • Celli, G.B., de Lange, T., DNA processing is not required for ATM-mediated telomere damage response after TRF2 deletion. Nat. Cell Biol. 7 (2005), 712–718.
    • (2005) Nat. Cell Biol. , vol.7 , pp. 712-718
    • Celli, G.B.1    de Lange, T.2
  • 14
    • 0037033022 scopus 로고    scopus 로고
    • Binding of the concave surface of the Sds22 superhelix to the alpha 4/alpha 5/alpha 6-triangle of protein phosphatase-1
    • Ceulemans, H., Vulsteke, V., De Maeyer, M., Tatchell, K., Stalmans, W., Bollen, M., Binding of the concave surface of the Sds22 superhelix to the alpha 4/alpha 5/alpha 6-triangle of protein phosphatase-1. J Biol Chem. 277 (2002), 47331–47337.
    • (2002) J Biol Chem. , vol.277 , pp. 47331-47337
    • Ceulemans, H.1    Vulsteke, V.2    De Maeyer, M.3    Tatchell, K.4    Stalmans, W.5    Bollen, M.6
  • 15
    • 0029784513 scopus 로고    scopus 로고
    • Cyclin-binding motifs are essential for the function of p21CIP1
    • Chen, J., Saha, P., Kornbluth, S., Dynlacht, B.D., Dutta, A., Cyclin-binding motifs are essential for the function of p21CIP1. Mol. Cell. Biol. 16 (1996), 4673–4682.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 4673-4682
    • Chen, J.1    Saha, P.2    Kornbluth, S.3    Dynlacht, B.D.4    Dutta, A.5
  • 16
    • 43149118369 scopus 로고    scopus 로고
    • Cell cycle-dependent complex formation of BRCA1.CtIP.MRN is important for DNA double-strand break repair
    • Chen, L., Nievera, C.J., Lee, A.Y., Wu, X., Cell cycle-dependent complex formation of BRCA1.CtIP.MRN is important for DNA double-strand break repair. J. Biol. Chem. 283 (2008), 7713–7720.
    • (2008) J. Biol. Chem. , vol.283 , pp. 7713-7720
    • Chen, L.1    Nievera, C.J.2    Lee, A.Y.3    Wu, X.4
  • 17
    • 39749134753 scopus 로고    scopus 로고
    • A shared docking motif in TRF1 and TRF2 used for differential recruitment of telomeric proteins
    • Chen, Y., Yang, Y., van Overbeek, M., Donigian, J.R., Baciu, P., de Lange, T., Lei, M., A shared docking motif in TRF1 and TRF2 used for differential recruitment of telomeric proteins. Science 319 (2008), 1092–1096.
    • (2008) Science , vol.319 , pp. 1092-1096
    • Chen, Y.1    Yang, Y.2    van Overbeek, M.3    Donigian, J.R.4    Baciu, P.5    de Lange, T.6    Lei, M.7
  • 18
    • 79551629028 scopus 로고    scopus 로고
    • A conserved motif within RAP1 has diversified roles in telomere protection and regulation in different organisms
    • Chen, Y., Rai, R., Zhou, Z.R., Kanoh, J., Ribeyre, C., Yang, Y., Zheng, H., Damay, P., Wang, F., Tsujii, H., et al. A conserved motif within RAP1 has diversified roles in telomere protection and regulation in different organisms. Nat Struct Mol Biol. 18 (2011), 213–221.
    • (2011) Nat Struct Mol Biol. , vol.18 , pp. 213-221
    • Chen, Y.1    Rai, R.2    Zhou, Z.R.3    Kanoh, J.4    Ribeyre, C.5    Yang, Y.6    Zheng, H.7    Damay, P.8    Wang, F.9    Tsujii, H.10
  • 19
    • 0031972950 scopus 로고    scopus 로고
    • Phosphorylation of Enabled by the Drosophila Abelson tyrosine kinase regulates the in vivo function and protein-protein interactions of Enabled
    • Comer, A.R., Ahern-Djamali, S.M., Juang, J.L., Jackson, P.D., Hoffmann, F.M., Phosphorylation of Enabled by the Drosophila Abelson tyrosine kinase regulates the in vivo function and protein-protein interactions of Enabled. Mol. Cell. Biol. 18 (1998), 152–160.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 152-160
    • Comer, A.R.1    Ahern-Djamali, S.M.2    Juang, J.L.3    Jackson, P.D.4    Hoffmann, F.M.5
  • 20
    • 84876161358 scopus 로고    scopus 로고
    • Alternative end-joining mechanisms: a historical perspective
    • Decottignies, A., Alternative end-joining mechanisms: a historical perspective. Front. Genet., 4, 2013, 48.
    • (2013) Front. Genet. , vol.4 , pp. 48
    • Decottignies, A.1
  • 21
    • 34548317418 scopus 로고    scopus 로고
    • Protection of telomeres through independent control of ATM and ATR by TRF2 and POT1
    • Denchi, E.L., de Lange, T., Protection of telomeres through independent control of ATM and ATR by TRF2 and POT1. Nature 448 (2007), 1068–1071.
    • (2007) Nature , vol.448 , pp. 1068-1071
    • Denchi, E.L.1    de Lange, T.2
  • 22
    • 68949149732 scopus 로고    scopus 로고
    • Multiple roles for MRE11 at uncapped telomeres
    • Deng, Y., Guo, X., Ferguson, D.O., Chang, S., Multiple roles for MRE11 at uncapped telomeres. Nature 460 (2009), 914–918.
    • (2009) Nature , vol.460 , pp. 914-918
    • Deng, Y.1    Guo, X.2    Ferguson, D.O.3    Chang, S.4
  • 23
    • 70350441980 scopus 로고    scopus 로고
    • Cell cycle-dependent role of MRN at dysfunctional telomeres: ATM signaling-dependent induction of nonhomologous end joining (NHEJ) in G1 and resection-mediated inhibition of NHEJ in G2
    • Dimitrova, N., de Lange, T., Cell cycle-dependent role of MRN at dysfunctional telomeres: ATM signaling-dependent induction of nonhomologous end joining (NHEJ) in G1 and resection-mediated inhibition of NHEJ in G2. Mol. Cell. Biol. 29 (2009), 5552–5563.
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 5552-5563
    • Dimitrova, N.1    de Lange, T.2
  • 26
  • 28
    • 0034847376 scopus 로고    scopus 로고
    • Structure of the TRFH dimerization domain of the human telomeric proteins TRF1 and TRF2
    • Fairall, L., Chapman, L., Moss, H., de Lange, T., Rhodes, D., Structure of the TRFH dimerization domain of the human telomeric proteins TRF1 and TRF2. Mol. Cell 8 (2001), 351–361.
    • (2001) Mol. Cell , vol.8 , pp. 351-361
    • Fairall, L.1    Chapman, L.2    Moss, H.3    de Lange, T.4    Rhodes, D.5
  • 29
    • 84861843272 scopus 로고    scopus 로고
    • CDK targeting of NBS1 promotes DNA-end resection, replication restart and homologous recombination
    • Falck, J., Forment, J.V., Coates, J., Mistrik, M., Lukas, J., Bartek, J., Jackson, S.P., CDK targeting of NBS1 promotes DNA-end resection, replication restart and homologous recombination. EMBO Rep. 13 (2012), 561–568.
    • (2012) EMBO Rep. , vol.13 , pp. 561-568
    • Falck, J.1    Forment, J.V.2    Coates, J.3    Mistrik, M.4    Lukas, J.5    Bartek, J.6    Jackson, S.P.7
  • 31
    • 36248952723 scopus 로고    scopus 로고
    • Dysfunctional telomeres activate an ATM-ATR-dependent DNA damage response to suppress tumorigenesis
    • Guo, X., Deng, Y., Lin, Y., Cosme-Blanco, W., Chan, S., He, H., Yuan, G., Brown, E.J., Chang, S., Dysfunctional telomeres activate an ATM-ATR-dependent DNA damage response to suppress tumorigenesis. EMBO J. 26 (2007), 4709–4719.
    • (2007) EMBO J. , vol.26 , pp. 4709-4719
    • Guo, X.1    Deng, Y.2    Lin, Y.3    Cosme-Blanco, W.4    Chan, S.5    He, H.6    Yuan, G.7    Brown, E.J.8    Chang, S.9
  • 32
    • 66149114020 scopus 로고    scopus 로고
    • Human CtIP mediates cell cycle control of DNA end resection and double strand break repair
    • Huertas, P., Jackson, S.P., Human CtIP mediates cell cycle control of DNA end resection and double strand break repair. J. Biol. Chem. 284 (2009), 9558–9565.
    • (2009) J. Biol. Chem. , vol.284 , pp. 9558-9565
    • Huertas, P.1    Jackson, S.P.2
  • 34
    • 0037515628 scopus 로고    scopus 로고
    • PNUTS, a protein phosphatase 1 (PP1) nuclear targeting subunit. Characterization of its PP1- and RNA-binding domains and regulation by phosphorylation
    • Kim, Y.M., Watanabe, T., Allen, P.B., Kim, Y.M., Lee, S.J., Greengard, P., Nairn, A.C., Kwon, Y.G., PNUTS, a protein phosphatase 1 (PP1) nuclear targeting subunit. Characterization of its PP1- and RNA-binding domains and regulation by phosphorylation. J. Biol. Chem. 278 (2003), 13819–13828.
    • (2003) J. Biol. Chem. , vol.278 , pp. 13819-13828
    • Kim, Y.M.1    Watanabe, T.2    Allen, P.B.3    Kim, Y.M.4    Lee, S.J.5    Greengard, P.6    Nairn, A.C.7    Kwon, Y.G.8
  • 36
    • 43249105463 scopus 로고    scopus 로고
    • Cell cycle control of telomere protection and NHEJ revealed by a ts mutation in the DNA-binding domain of TRF2
    • Konishi, A., de Lange, T., Cell cycle control of telomere protection and NHEJ revealed by a ts mutation in the DNA-binding domain of TRF2. Genes Dev. 22 (2008), 1221–1230.
    • (2008) Genes Dev. , vol.22 , pp. 1221-1230
    • Konishi, A.1    de Lange, T.2
  • 38
    • 12644291188 scopus 로고    scopus 로고
    • Cell cycle-dependent phosphorylation of mammalian protein phosphatase 1 by cdc2 kinase
    • Kwon, Y.G., Lee, S.Y., Choi, Y., Greengard, P., Nairn, A.C., Cell cycle-dependent phosphorylation of mammalian protein phosphatase 1 by cdc2 kinase. Proc. Natl. Acad. Sci. USA 94 (1997), 2168–2173.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 2168-2173
    • Kwon, Y.G.1    Lee, S.Y.2    Choi, Y.3    Greengard, P.4    Nairn, A.C.5
  • 41
    • 17644409069 scopus 로고    scopus 로고
    • ATM activation by DNA double-strand breaks through the Mre11-Rad50-Nbs1 complex
    • Lee, J.H., Paull, T.T., ATM activation by DNA double-strand breaks through the Mre11-Rad50-Nbs1 complex. Science 308 (2005), 551–554.
    • (2005) Science , vol.308 , pp. 551-554
    • Lee, J.H.1    Paull, T.T.2
  • 42
    • 77953229115 scopus 로고    scopus 로고
    • The mechanism of double-strand DNA break repair by the nonhomologous DNA end-joining pathway
    • Lieber, M.R., The mechanism of double-strand DNA break repair by the nonhomologous DNA end-joining pathway. Annu. Rev. Biochem. 79 (2010), 181–211.
    • (2010) Annu. Rev. Biochem. , vol.79 , pp. 181-211
    • Lieber, M.R.1
  • 45
    • 4444293274 scopus 로고    scopus 로고
    • Nijmegen breakage syndrome and DNA double strand break repair by NBS1 complex
    • Matsuura, S., Kobayashi, J., Tauchi, H., Komatsu, K., Nijmegen breakage syndrome and DNA double strand break repair by NBS1 complex. Adv. Biophys. 38 (2004), 65–80.
    • (2004) Adv. Biophys. , vol.38 , pp. 65-80
    • Matsuura, S.1    Kobayashi, J.2    Tauchi, H.3    Komatsu, K.4
  • 50
    • 0031059866 scopus 로고    scopus 로고
    • [20] Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z., Minor, W., [20] Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276 (1997), 307–326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 51
    • 46249125488 scopus 로고    scopus 로고
    • How shelterin protects mammalian telomeres
    • Palm, W., de Lange, T., How shelterin protects mammalian telomeres. Annu. Rev. Genet. 42 (2008), 301–334.
    • (2008) Annu. Rev. Genet. , vol.42 , pp. 301-334
    • Palm, W.1    de Lange, T.2
  • 53
    • 77955419733 scopus 로고    scopus 로고
    • The function of classical and alternative non-homologous end-joining pathways in the fusion of dysfunctional telomeres
    • Rai, R., Zheng, H., He, H., Luo, Y., Multani, A., Carpenter, P.B., Chang, S., The function of classical and alternative non-homologous end-joining pathways in the fusion of dysfunctional telomeres. EMBO J. 29 (2010), 2598–2610.
    • (2010) EMBO J. , vol.29 , pp. 2598-2610
    • Rai, R.1    Zheng, H.2    He, H.3    Luo, Y.4    Multani, A.5    Carpenter, P.B.6    Chang, S.7
  • 54
    • 84960192466 scopus 로고    scopus 로고
    • TRF2-RAP1 is required to protect telomeres from engaging in homologous recombination-mediated deletions and fusions
    • Rai, R., Chen, Y., Lei, M., Chang, S., TRF2-RAP1 is required to protect telomeres from engaging in homologous recombination-mediated deletions and fusions. Nat. Commun., 7, 2016, 10881.
    • (2016) Nat. Commun. , vol.7 , pp. 10881
    • Rai, R.1    Chen, Y.2    Lei, M.3    Chang, S.4
  • 57
    • 84860456242 scopus 로고    scopus 로고
    • Removal of shelterin reveals the telomere end-protection problem
    • Sfeir, A., de Lange, T., Removal of shelterin reveals the telomere end-protection problem. Science 336 (2012), 593–597.
    • (2012) Science , vol.336 , pp. 593-597
    • Sfeir, A.1    de Lange, T.2
  • 58
    • 80755187806 scopus 로고    scopus 로고
    • Double-strand break end resection and repair pathway choice
    • Symington, L.S., Gautier, J., Double-strand break end resection and repair pathway choice. Annu. Rev. Genet. 45 (2011), 247–271.
    • (2011) Annu. Rev. Genet. , vol.45 , pp. 247-271
    • Symington, L.S.1    Gautier, J.2
  • 60
    • 27944496124 scopus 로고    scopus 로고
    • Functional human telomeres are recognized as DNA damage in G2 of the cell cycle
    • Verdun, R.E., Crabbe, L., Haggblom, C., Karlseder, J., Functional human telomeres are recognized as DNA damage in G2 of the cell cycle. Mol. Cell 20 (2005), 551–561.
    • (2005) Mol. Cell , vol.20 , pp. 551-561
    • Verdun, R.E.1    Crabbe, L.2    Haggblom, C.3    Karlseder, J.4
  • 61
    • 84969760939 scopus 로고    scopus 로고
    • Noncanonical views of homology-directed DNA repair
    • Verma, P., Greenberg, R.A., Noncanonical views of homology-directed DNA repair. Genes Dev. 30 (2016), 1138–1154.
    • (2016) Genes Dev. , vol.30 , pp. 1138-1154
    • Verma, P.1    Greenberg, R.A.2
  • 62
    • 84884132386 scopus 로고    scopus 로고
    • SLX4 assembles a telomere maintenance toolkit by bridging multiple endonucleases with telomeres
    • Wan, B., Yin, J., Horvath, K., Sarkar, J., Chen, Y., Wu, J., Wan, K., Lu, J., Gu, P., Yu, E.Y., et al. SLX4 assembles a telomere maintenance toolkit by bridging multiple endonucleases with telomeres. Cell Rep. 4 (2013), 861–869.
    • (2013) Cell Rep. , vol.4 , pp. 861-869
    • Wan, B.1    Yin, J.2    Horvath, K.3    Sarkar, J.4    Chen, Y.5    Wu, J.6    Wan, K.7    Lu, J.8    Gu, P.9    Yu, E.Y.10
  • 63
  • 64
    • 68249127288 scopus 로고    scopus 로고
    • Behind the wheel and under the hood: functions of cyclin-dependent kinases in response to DNA damage
    • Wohlbold, L., Fisher, R.P., Behind the wheel and under the hood: functions of cyclin-dependent kinases in response to DNA damage. DNA Repair (Amst.) 8 (2009), 1018–1024.
    • (2009) DNA Repair (Amst.) , vol.8 , pp. 1018-1024
    • Wohlbold, L.1    Fisher, R.P.2
  • 65
    • 84866170589 scopus 로고    scopus 로고
    • Chemical genetics reveals a specific requirement for Cdk2 activity in the DNA damage response and identifies Nbs1 as a Cdk2 substrate in human cells
    • Wohlbold, L., Merrick, K.A., De, S., Amat, R., Kim, J.H., Larochelle, S., Allen, J.J., Zhang, C., Shokat, K.M., Petrini, J.H., Fisher, R.P., Chemical genetics reveals a specific requirement for Cdk2 activity in the DNA damage response and identifies Nbs1 as a Cdk2 substrate in human cells. PLoS Genet., 8, 2012, e1002935.
    • (2012) PLoS Genet. , vol.8 , pp. e1002935
    • Wohlbold, L.1    Merrick, K.A.2    De, S.3    Amat, R.4    Kim, J.H.5    Larochelle, S.6    Allen, J.J.7    Zhang, C.8    Shokat, K.M.9    Petrini, J.H.10    Fisher, R.P.11
  • 67
    • 33745713451 scopus 로고    scopus 로고
    • Pot1 deficiency initiates DNA damage checkpoint activation and aberrant homologous recombination at telomeres
    • Wu, L., Multani, A.S., He, H., Cosme-Blanco, W., Deng, Y., Deng, J.M., Bachilo, O., Pathak, S., Tahara, H., Bailey, S.M., et al. Pot1 deficiency initiates DNA damage checkpoint activation and aberrant homologous recombination at telomeres. Cell 126 (2006), 49–62.
    • (2006) Cell , vol.126 , pp. 49-62
    • Wu, L.1    Multani, A.S.2    He, H.3    Cosme-Blanco, W.4    Deng, Y.5    Deng, J.M.6    Bachilo, O.7    Pathak, S.8    Tahara, H.9    Bailey, S.M.10
  • 68
    • 77955995270 scopus 로고    scopus 로고
    • Apollo contributes to G overhang maintenance and protects leading-end telomeres
    • Wu, P., van Overbeek, M., Rooney, S., de Lange, T., Apollo contributes to G overhang maintenance and protects leading-end telomeres. Mol. Cell 39 (2010), 606–617.
    • (2010) Mol. Cell , vol.39 , pp. 606-617
    • Wu, P.1    van Overbeek, M.2    Rooney, S.3    de Lange, T.4
  • 69
    • 68249146431 scopus 로고    scopus 로고
    • Role of mammalian Mre11 in classical and alternative nonhomologous end joining
    • Xie, A., Kwok, A., Scully, R., Role of mammalian Mre11 in classical and alternative nonhomologous end joining. Nat. Struct. Mol. Biol. 16 (2009), 814–818.
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 814-818
    • Xie, A.1    Kwok, A.2    Scully, R.3
  • 70
    • 6344264992 scopus 로고    scopus 로고
    • DNA damage-induced cell cycle checkpoint control requires CtIP, a phosphorylation-dependent binding partner of BRCA1 C-terminal domains
    • Yu, X., Chen, J., DNA damage-induced cell cycle checkpoint control requires CtIP, a phosphorylation-dependent binding partner of BRCA1 C-terminal domains. Mol. Cell. Biol. 24 (2004), 9478–9486.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 9478-9486
    • Yu, X.1    Chen, J.2
  • 71
    • 67349246802 scopus 로고    scopus 로고
    • CtIP-BRCA1 modulates the choice of DNA double-strand-break repair pathway throughout the cell cycle
    • Yun, M.H., Hiom, K., CtIP-BRCA1 modulates the choice of DNA double-strand-break repair pathway throughout the cell cycle. Nature 459 (2009), 460–463.
    • (2009) Nature , vol.459 , pp. 460-463
    • Yun, M.H.1    Hiom, K.2
  • 73
    • 0342561644 scopus 로고    scopus 로고
    • Cell-cycle-regulated association of RAD50/MRE11/NBS1 with TRF2 and human telomeres
    • Zhu, X.D., Küster, B., Mann, M., Petrini, J.H., de Lange, T., Cell-cycle-regulated association of RAD50/MRE11/NBS1 with TRF2 and human telomeres. Nat. Genet. 25 (2000), 347–352.
    • (2000) Nat. Genet. , vol.25 , pp. 347-352
    • Zhu, X.D.1    Küster, B.2    Mann, M.3    Petrini, J.H.4    de Lange, T.5
  • 74
    • 0037567268 scopus 로고    scopus 로고
    • Sensing DNA damage through ATRIP recognition of RPA-ssDNA complexes
    • Zou, L., Elledge, S.J., Sensing DNA damage through ATRIP recognition of RPA-ssDNA complexes. Science 300 (2003), 1542–1548.
    • (2003) Science , vol.300 , pp. 1542-1548
    • Zou, L.1    Elledge, S.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.