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Volumn 711, Issue 1-2, 2011, Pages 73-86

Choosing the right path: Does DNA-PK help make the decision?

Author keywords

DNA double strand break repair; DNA dependent protein kinase; Non homologous end joining

Indexed keywords

DNA DEPENDENT PROTEIN KINASE; KU ANTIGEN; POLYDEOXYRIBONUCLEOTIDE SYNTHASE;

EID: 79956220705     PISSN: 00275107     EISSN: 09218262     Source Type: Journal    
DOI: 10.1016/j.mrfmmm.2011.02.010     Document Type: Review
Times cited : (116)

References (178)
  • 1
    • 0027285362 scopus 로고
    • Lethality induced by a single site-specific double-strand break in a dispensable yeast plasmid
    • Bennett C.B., Lewis A.L., Baldwin K.K., Resnick M.A. Lethality induced by a single site-specific double-strand break in a dispensable yeast plasmid. Proc. Natl. Acad. Sci. U.S.A. 1993, 90:5613-5617.
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 5613-5617
    • Bennett, C.B.1    Lewis, A.L.2    Baldwin, K.K.3    Resnick, M.A.4
  • 2
    • 76749171752 scopus 로고    scopus 로고
    • Mechanisms of chromosomal rearrangement in the human genome
    • Tsai A.G., Lieber M.R. Mechanisms of chromosomal rearrangement in the human genome. BMC Genom. 2010, 11(Suppl. 1):S1.
    • (2010) BMC Genom. , vol.11 , Issue.SUPPL. 1
    • Tsai, A.G.1    Lieber, M.R.2
  • 4
    • 0019374013 scopus 로고
    • Characterization of a high molecular weight acidic nuclear protein recognized by autoantibodies in sera from patients with polymyositis-scleroderma overlap
    • Mimori T., Akizuki M., Yamagata H., Inada S., Yoshida S., Homma M. Characterization of a high molecular weight acidic nuclear protein recognized by autoantibodies in sera from patients with polymyositis-scleroderma overlap. J. Clin. Invest. 1981, 68:611-620.
    • (1981) J. Clin. Invest. , vol.68 , pp. 611-620
    • Mimori, T.1    Akizuki, M.2    Yamagata, H.3    Inada, S.4    Yoshida, S.5    Homma, M.6
  • 5
    • 0023018810 scopus 로고
    • Characterization of the DNA-binding protein antigen Ku recognized by autoantibodies from patients with rheumatic disorders
    • Mimori T., Hardin J.A., Steitz J.A. Characterization of the DNA-binding protein antigen Ku recognized by autoantibodies from patients with rheumatic disorders. J. Biol. Chem. 1986, 261:2274-2278.
    • (1986) J. Biol. Chem. , vol.261 , pp. 2274-2278
    • Mimori, T.1    Hardin, J.A.2    Steitz, J.A.3
  • 6
    • 0027468265 scopus 로고
    • Binding of Ku protein to DNA. Measurement of affinity for ends and demonstration of binding to nicks
    • Blier P.R., Griffith A.J., Craft J., Hardin J.A. Binding of Ku protein to DNA. Measurement of affinity for ends and demonstration of binding to nicks. J. Biol. Chem. 1993, 268:7594-7601.
    • (1993) J. Biol. Chem. , vol.268 , pp. 7594-7601
    • Blier, P.R.1    Griffith, A.J.2    Craft, J.3    Hardin, J.A.4
  • 7
    • 0027156140 scopus 로고
    • EBP-80, a transcription factor closely resembling the human autoantigen Ku, recognizes single- to double-strand transitions in DNA
    • Falzon M., Fewell J.W., Kuff E.L. EBP-80, a transcription factor closely resembling the human autoantigen Ku, recognizes single- to double-strand transitions in DNA. J. Biol. Chem. 1993, 268:10546-10552.
    • (1993) J. Biol. Chem. , vol.268 , pp. 10546-10552
    • Falzon, M.1    Fewell, J.W.2    Kuff, E.L.3
  • 8
    • 0035833552 scopus 로고    scopus 로고
    • Structure of the Ku heterodimer bound to DNA and its implications for double-strand break repair
    • Walker J.R., Corpina R.A., Goldberg J. Structure of the Ku heterodimer bound to DNA and its implications for double-strand break repair. Nature 2001, 412:607-614.
    • (2001) Nature , vol.412 , pp. 607-614
    • Walker, J.R.1    Corpina, R.A.2    Goldberg, J.3
  • 9
    • 0022827675 scopus 로고
    • Mechanism of interaction between Ku protein and DNA
    • Mimori T., Hardin J.A. Mechanism of interaction between Ku protein and DNA. J. Biol. Chem. 1986, 261:10375-10379.
    • (1986) J. Biol. Chem. , vol.261 , pp. 10375-10379
    • Mimori, T.1    Hardin, J.A.2
  • 10
    • 0026045833 scopus 로고
    • Analysis of the mechanism of interaction of simian Ku protein with DNA
    • Paillard S., Strauss F. Analysis of the mechanism of interaction of simian Ku protein with DNA. Nucleic Acids Res. 1991, 19:5619-5624.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 5619-5624
    • Paillard, S.1    Strauss, F.2
  • 12
    • 70350324640 scopus 로고    scopus 로고
    • Emerging common themes in regulation of PIKKs and PI3Ks
    • Lempiainen H., Halazonetis T.D. Emerging common themes in regulation of PIKKs and PI3Ks. EMBO J. 2009, 28:3067-3073.
    • (2009) EMBO J. , vol.28 , pp. 3067-3073
    • Lempiainen, H.1    Halazonetis, T.D.2
  • 14
    • 0033198709 scopus 로고    scopus 로고
    • Mapping of protein-protein interactions within the DNA-dependent protein kinase complex
    • Gell D., Jackson S.P. Mapping of protein-protein interactions within the DNA-dependent protein kinase complex. Nucleic Acids Res. 1999, 27:3494-3502.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 3494-3502
    • Gell, D.1    Jackson, S.P.2
  • 15
    • 0030746109 scopus 로고    scopus 로고
    • Interaction of DNA-dependent protein kinase with DNA and with Ku: biochemical and atomic-force microscopy studies
    • Yaneva M., Kowalewski T., Lieber M.R. Interaction of DNA-dependent protein kinase with DNA and with Ku: biochemical and atomic-force microscopy studies. EMBO J. 1997, 16:5098-5112.
    • (1997) EMBO J. , vol.16 , pp. 5098-5112
    • Yaneva, M.1    Kowalewski, T.2    Lieber, M.R.3
  • 16
    • 0031708232 scopus 로고    scopus 로고
    • Productive and nonproductive complexes of Ku and DNA-dependent protein kinase at DNA termini
    • West R.B., Yaneva M., Lieber M.R. Productive and nonproductive complexes of Ku and DNA-dependent protein kinase at DNA termini. Mol. Cell. Biol. 1998, 18:5908-5920.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 5908-5920
    • West, R.B.1    Yaneva, M.2    Lieber, M.R.3
  • 17
    • 0033572709 scopus 로고    scopus 로고
    • Geometry of a complex formed by double strand break repair proteins at a single DNA end: recruitment of DNA-PKcs induces inward translocation of Ku protein
    • Yoo S., Dynan W.S. Geometry of a complex formed by double strand break repair proteins at a single DNA end: recruitment of DNA-PKcs induces inward translocation of Ku protein. Nucleic Acids Res. 1999, 27:4679-4686.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 4679-4686
    • Yoo, S.1    Dynan, W.S.2
  • 18
    • 0031930488 scopus 로고    scopus 로고
    • DNA-dependent protein kinase: DNA binding and activation in the absence of Ku
    • Hammarsten O., Chu G. DNA-dependent protein kinase: DNA binding and activation in the absence of Ku. Proc. Natl. Acad. Sci. U.S.A. 1998, 95:525-530.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 525-530
    • Hammarsten, O.1    Chu, G.2
  • 19
    • 0037124373 scopus 로고    scopus 로고
    • Synapsis of DNA ends by DNA-dependent protein kinase
    • DeFazio L.G., Stansel R.M., Griffith J.D., Chu G. Synapsis of DNA ends by DNA-dependent protein kinase. EMBO J. 2002, 21:3192-3200.
    • (2002) EMBO J. , vol.21 , pp. 3192-3200
    • DeFazio, L.G.1    Stansel, R.M.2    Griffith, J.D.3    Chu, G.4
  • 20
    • 33644871780 scopus 로고    scopus 로고
    • Terminal DNA structure and ATP influence binding parameters of the DNA-dependent protein kinase at an early step prior to DNA synapsis
    • Jovanovic M., Dynan W.S. Terminal DNA structure and ATP influence binding parameters of the DNA-dependent protein kinase at an early step prior to DNA synapsis. Nucleic Acids Res. 2006, 34:1112-1120.
    • (2006) Nucleic Acids Res. , vol.34 , pp. 1112-1120
    • Jovanovic, M.1    Dynan, W.S.2
  • 22
    • 78649446475 scopus 로고    scopus 로고
    • A structural model for regulation of NHEJ by DNA-PKcs autophosphorylation
    • Dobbs T.A., Tainer J.A., Lees-Miller S.P. A structural model for regulation of NHEJ by DNA-PKcs autophosphorylation. DNA Repair (Amst.) 2010, 9:1307-1314.
    • (2010) DNA Repair (Amst.) , vol.9 , pp. 1307-1314
    • Dobbs, T.A.1    Tainer, J.A.2    Lees-Miller, S.P.3
  • 23
    • 73849140503 scopus 로고    scopus 로고
    • Crystal structure of DNA-PKcs reveals a large open-ring cradle comprised of HEAT repeats
    • Sibanda B.L., Chirgadze D.Y., Blundell T.L. Crystal structure of DNA-PKcs reveals a large open-ring cradle comprised of HEAT repeats. Nature 2010, 463:118-121.
    • (2010) Nature , vol.463 , pp. 118-121
    • Sibanda, B.L.1    Chirgadze, D.Y.2    Blundell, T.L.3
  • 24
    • 79960616484 scopus 로고    scopus 로고
    • Structural biology of DNA repair: spatial organisation of the multicomponent complexes of nonhomologous end joining
    • Ochi T., Sibanda B.L., Wu Q., Chirgadze D.Y., Bolanos-Garcia V.M., Blundell T.L. Structural biology of DNA repair: spatial organisation of the multicomponent complexes of nonhomologous end joining. J. Nucleic Acids 2010, 2010.
    • (2010) J. Nucleic Acids , vol.2010
    • Ochi, T.1    Sibanda, B.L.2    Wu, Q.3    Chirgadze, D.Y.4    Bolanos-Garcia, V.M.5    Blundell, T.L.6
  • 25
    • 79956189502 scopus 로고    scopus 로고
    • Inhibition of HR by DNA-PK requires kinase activity, is titratable, and is modulated by autophosphorylation, Mol. Cell Biol. 2011, [Epub ahead of print].
    • J.A. Neal, V. Dang, P. Douglas, S.P. Lees-Miller, K. Meek, Inhibition of HR by DNA-PK requires kinase activity, is titratable, and is modulated by autophosphorylation, Mol. Cell Biol. 2011, [Epub ahead of print].
    • Neal, J.A.1    Dang, V.2    Douglas, P.3    Lees-Miller, S.P.4    Meek, K.5
  • 26
    • 0034662228 scopus 로고    scopus 로고
    • Both V(D)J recombination and radioresistance require DNA-PK kinase activity, though minimal levels suffice for V(D)J recombination
    • Kienker L.J., Shin E.K., Meek K. Both V(D)J recombination and radioresistance require DNA-PK kinase activity, though minimal levels suffice for V(D)J recombination. Nucleic Acids Res. 2000, 28:2752-2761.
    • (2000) Nucleic Acids Res. , vol.28 , pp. 2752-2761
    • Kienker, L.J.1    Shin, E.K.2    Meek, K.3
  • 27
    • 0032938747 scopus 로고    scopus 로고
    • Requirement for the kinase activity of human DNA-dependent protein kinase catalytic subunit in DNA strand break rejoining
    • Kurimasa A., Kumano S., Boubnov N.V., Story M.D., Tung C.S., Peterson S.R., Chen D.J. Requirement for the kinase activity of human DNA-dependent protein kinase catalytic subunit in DNA strand break rejoining. Mol. Cell. Biol. 1999, 19:3877-3884.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 3877-3884
    • Kurimasa, A.1    Kumano, S.2    Boubnov, N.V.3    Story, M.D.4    Tung, C.S.5    Peterson, S.R.6    Chen, D.J.7
  • 28
    • 0032972734 scopus 로고    scopus 로고
    • DNA-dependent protein kinase phosphorylation sites in Ku 70/80 heterodimer
    • Chan D.W., Ye R., Veillette C.J., Lees-Miller S.P. DNA-dependent protein kinase phosphorylation sites in Ku 70/80 heterodimer. Biochemistry 1999, 38:1819-1828.
    • (1999) Biochemistry , vol.38 , pp. 1819-1828
    • Chan, D.W.1    Ye, R.2    Veillette, C.J.3    Lees-Miller, S.P.4
  • 29
    • 26644444577 scopus 로고    scopus 로고
    • The DNA-dependent protein kinase catalytic subunit phosphorylation sites in human Artemis
    • Ma Y., Pannicke U., Lu H., Niewolik D., Schwarz K., Lieber M.R. The DNA-dependent protein kinase catalytic subunit phosphorylation sites in human Artemis. J. Biol. Chem. 2005, 280:33839-33846.
    • (2005) J. Biol. Chem. , vol.280 , pp. 33839-33846
    • Ma, Y.1    Pannicke, U.2    Lu, H.3    Niewolik, D.4    Schwarz, K.5    Lieber, M.R.6
  • 31
    • 0031939411 scopus 로고    scopus 로고
    • The XRCC4 gene product is a target for and interacts with the DNA-dependent protein kinase
    • Leber R., Wise T.W., Mizuta R., Meek K. The XRCC4 gene product is a target for and interacts with the DNA-dependent protein kinase. J. Biol. Chem. 1998, 273:1794-1801.
    • (1998) J. Biol. Chem. , vol.273 , pp. 1794-1801
    • Leber, R.1    Wise, T.W.2    Mizuta, R.3    Meek, K.4
  • 32
    • 52049117396 scopus 로고    scopus 로고
    • DNA-PK and ATM phosphorylation sites in XLF/Cernunnos are not required for repair of DNA double strand breaks
    • Yu Y., Mahaney B.L., Yano K., Ye R., Fang S., Douglas P., Chen D.J., Lees-Miller S.P. DNA-PK and ATM phosphorylation sites in XLF/Cernunnos are not required for repair of DNA double strand breaks. DNA Repair (Amst.) 2008, 7:1680-1692.
    • (2008) DNA Repair (Amst.) , vol.7 , pp. 1680-1692
    • Yu, Y.1    Mahaney, B.L.2    Yano, K.3    Ye, R.4    Fang, S.5    Douglas, P.6    Chen, D.J.7    Lees-Miller, S.P.8
  • 33
    • 4444224512 scopus 로고    scopus 로고
    • Phosphorylation and regulation of DNA ligase IV stability by DNA-dependent protein kinase
    • Wang Y.G., Nnakwe C., Lane W.S., Modesti M., Frank K.M. Phosphorylation and regulation of DNA ligase IV stability by DNA-dependent protein kinase. J. Biol. Chem. 2004, 279:37282-37290.
    • (2004) J. Biol. Chem. , vol.279 , pp. 37282-37290
    • Wang, Y.G.1    Nnakwe, C.2    Lane, W.S.3    Modesti, M.4    Frank, K.M.5
  • 34
    • 22044445683 scopus 로고    scopus 로고
    • DNA-PK-dependent phosphorylation of Ku70/80 is not required for non-homologous end joining
    • Douglas P., Gupta S., Morrice N., Meek K., Lees-Miller S.P. DNA-PK-dependent phosphorylation of Ku70/80 is not required for non-homologous end joining. DNA Repair (Amst.) 2005, 4:1006-1018.
    • (2005) DNA Repair (Amst.) , vol.4 , pp. 1006-1018
    • Douglas, P.1    Gupta, S.2    Morrice, N.3    Meek, K.4    Lees-Miller, S.P.5
  • 35
  • 36
    • 0037106180 scopus 로고    scopus 로고
    • Autophosphorylation of the DNA-dependent protein kinase catalytic subunit is required for rejoining of DNA double-strand breaks
    • Chan D.W., Chen B.P., Prithivirajsingh S., Kurimasa A., Story M.D., Qin J., Chen D.J. Autophosphorylation of the DNA-dependent protein kinase catalytic subunit is required for rejoining of DNA double-strand breaks. Genes Dev. 2002, 16:2333-2338.
    • (2002) Genes Dev. , vol.16 , pp. 2333-2338
    • Chan, D.W.1    Chen, B.P.2    Prithivirajsingh, S.3    Kurimasa, A.4    Story, M.D.5    Qin, J.6    Chen, D.J.7
  • 38
    • 0037444375 scopus 로고    scopus 로고
    • Threonines 2638/2647 in DNA-PK are essential for cellular resistance to ionizing radiation
    • Soubeyrand S., Pope L., Pakuts B., Hache R.J. Threonines 2638/2647 in DNA-PK are essential for cellular resistance to ionizing radiation. Cancer Res. 2003, 63:1198-1201.
    • (2003) Cancer Res. , vol.63 , pp. 1198-1201
    • Soubeyrand, S.1    Pope, L.2    Pakuts, B.3    Hache, R.J.4
  • 39
    • 0043133778 scopus 로고    scopus 로고
    • Autophosphorylation of the catalytic subunit of the DNA-dependent protein kinase is required for efficient end processing during DNA double-strand break repair
    • Ding Q., Reddy Y.V., Wang W., Woods T., Douglas P., Ramsden D.A., Lees-Miller S.P., Meek K. Autophosphorylation of the catalytic subunit of the DNA-dependent protein kinase is required for efficient end processing during DNA double-strand break repair. Mol. Cell. Biol. 2003, 23:5836-5848.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 5836-5848
    • Ding, Q.1    Reddy, Y.V.2    Wang, W.3    Woods, T.4    Douglas, P.5    Ramsden, D.A.6    Lees-Miller, S.P.7    Meek, K.8
  • 40
    • 28544448011 scopus 로고    scopus 로고
    • Autophosphorylation of DNA-dependent protein kinase regulates DNA end processing and may also alter double-strand break repair pathway choice
    • Cui X., Yu Y., Gupta S., Cho Y.M., Lees-Miller S.P., Meek K. Autophosphorylation of DNA-dependent protein kinase regulates DNA end processing and may also alter double-strand break repair pathway choice. Mol. Cell. Biol. 2005, 25:10842-10852.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 10842-10852
    • Cui, X.1    Yu, Y.2    Gupta, S.3    Cho, Y.M.4    Lees-Miller, S.P.5    Meek, K.6
  • 42
    • 34248231265 scopus 로고    scopus 로고
    • Trans Autophosphorylation at DNA-dependent protein kinase's two major autophosphorylation site clusters facilitates end processing but not end joining
    • Meek K., Douglas P., Cui X., Ding Q., Lees-Miller S.P. trans Autophosphorylation at DNA-dependent protein kinase's two major autophosphorylation site clusters facilitates end processing but not end joining. Mol. Cell. Biol. 2007, 27:3881-3890.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 3881-3890
    • Meek, K.1    Douglas, P.2    Cui, X.3    Ding, Q.4    Lees-Miller, S.P.5
  • 43
  • 44
    • 33847185190 scopus 로고    scopus 로고
    • The DNA-dependent protein kinase catalytic subunit is phosphorylated in vivo on threonine 3950, a highly conserved amino acid in the protein kinase domain
    • Douglas P., Cui X., Block W.D., Yu Y., Gupta S., Ding Q., Ye R., Morrice N., Lees-Miller S.P., Meek K. The DNA-dependent protein kinase catalytic subunit is phosphorylated in vivo on threonine 3950, a highly conserved amino acid in the protein kinase domain. Mol. Cell. Biol. 2007, 27:1581-1591.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 1581-1591
    • Douglas, P.1    Cui, X.2    Block, W.D.3    Yu, Y.4    Gupta, S.5    Ding, Q.6    Ye, R.7    Morrice, N.8    Lees-Miller, S.P.9    Meek, K.10
  • 45
    • 4043073590 scopus 로고    scopus 로고
    • Autophosphorylation-dependent remodeling of the DNA-dependent protein kinase catalytic subunit regulates ligation of DNA ends
    • Block W.D., Yu Y., Merkle D., Gifford J.L., Ding Q., Meek K., Lees-Miller S.P. Autophosphorylation-dependent remodeling of the DNA-dependent protein kinase catalytic subunit regulates ligation of DNA ends. Nucleic Acids Res. 2004, 32:4351-4357.
    • (2004) Nucleic Acids Res. , vol.32 , pp. 4351-4357
    • Block, W.D.1    Yu, Y.2    Merkle, D.3    Gifford, J.L.4    Ding, Q.5    Meek, K.6    Lees-Miller, S.P.7
  • 46
    • 4544295689 scopus 로고    scopus 로고
    • Non-homologous end joining requires that the DNA-PK complex undergo an autophosphorylation-dependent rearrangement at DNA ends
    • Reddy Y.V., Ding Q., Lees-Miller S.P., Meek K., Ramsden D.A. Non-homologous end joining requires that the DNA-PK complex undergo an autophosphorylation-dependent rearrangement at DNA ends. J. Biol. Chem. 2004, 279:39408-39413.
    • (2004) J. Biol. Chem. , vol.279 , pp. 39408-39413
    • Reddy, Y.V.1    Ding, Q.2    Lees-Miller, S.P.3    Meek, K.4    Ramsden, D.A.5
  • 47
    • 0030009738 scopus 로고    scopus 로고
    • The DNA-dependent protein kinase is inactivated by autophosphorylation of the catalytic subunit
    • Chan D.W., Lees-Miller S.P. The DNA-dependent protein kinase is inactivated by autophosphorylation of the catalytic subunit. J. Biol. Chem. 1996, 271:8936-8941.
    • (1996) J. Biol. Chem. , vol.271 , pp. 8936-8941
    • Chan, D.W.1    Lees-Miller, S.P.2
  • 49
    • 31144478506 scopus 로고    scopus 로고
    • The leucine rich region of DNA-PKcs contributes to its innate DNA affinity
    • Gupta S., Meek K. The leucine rich region of DNA-PKcs contributes to its innate DNA affinity. Nucleic Acids Res. 2005, 33:6972-6981.
    • (2005) Nucleic Acids Res. , vol.33 , pp. 6972-6981
    • Gupta, S.1    Meek, K.2
  • 50
    • 0037155703 scopus 로고    scopus 로고
    • Hairpin opening and overhang processing by an Artemis/DNA-dependent protein kinase complex in nonhomologous end joining and V(D)J recombination
    • Ma Y., Pannicke U., Schwarz K., Lieber M.R. Hairpin opening and overhang processing by an Artemis/DNA-dependent protein kinase complex in nonhomologous end joining and V(D)J recombination. Cell 2002, 108:781-794.
    • (2002) Cell , vol.108 , pp. 781-794
    • Ma, Y.1    Pannicke, U.2    Schwarz, K.3    Lieber, M.R.4
  • 51
    • 77952583540 scopus 로고    scopus 로고
    • Purification and characterization of exonuclease-free Artemis: Implications for DNA-PK-dependent processing of DNA termini in NHEJ-catalyzed DSB repair
    • Pawelczak K.S., Turchi J.J. Purification and characterization of exonuclease-free Artemis: Implications for DNA-PK-dependent processing of DNA termini in NHEJ-catalyzed DSB repair. DNA Repair (Amst.) 2010, 9:670-677.
    • (2010) DNA Repair (Amst.) , vol.9 , pp. 670-677
    • Pawelczak, K.S.1    Turchi, J.J.2
  • 52
    • 79956202951 scopus 로고    scopus 로고
    • Coordination of DNA-PK activation and nuclease processing of DNA termini in NHEJ
    • Pawelczak K.S., Bennett S.M., Turchi J. Coordination of DNA-PK activation and nuclease processing of DNA termini in NHEJ. Antioxid. Redox Signal. 2010.
    • (2010) Antioxid. Redox Signal.
    • Pawelczak, K.S.1    Bennett, S.M.2    Turchi, J.3
  • 55
    • 77958548176 scopus 로고    scopus 로고
    • Functions and Regulation of Artemis: A Goddess in the Maintenance of Genome Integrity
    • Kurosawa A., Adachi N. Functions and Regulation of Artemis: A Goddess in the Maintenance of Genome Integrity. J. Radiat. Res. (Tokyo) 2010.
    • (2010) J. Radiat. Res. (Tokyo)
    • Kurosawa, A.1    Adachi, N.2
  • 56
    • 0037013895 scopus 로고    scopus 로고
    • Involvement of human polynucleotide kinase in double-strand break repair by non-homologous end joining
    • Chappell C., Hanakahi L.A., Karimi-Busheri F., Weinfeld M., West S.C. Involvement of human polynucleotide kinase in double-strand break repair by non-homologous end joining. EMBO J. 2002, 21:2827-2832.
    • (2002) EMBO J. , vol.21 , pp. 2827-2832
    • Chappell, C.1    Hanakahi, L.A.2    Karimi-Busheri, F.3    Weinfeld, M.4    West, S.C.5
  • 59
    • 2342541592 scopus 로고    scopus 로고
    • Stable down-regulation of human polynucleotide kinase enhances spontaneous mutation frequency and sensitizes cells to genotoxic agents
    • Rasouli-Nia A., Karimi-Busheri F., Weinfeld M. Stable down-regulation of human polynucleotide kinase enhances spontaneous mutation frequency and sensitizes cells to genotoxic agents. Proc. Natl. Acad. Sci. U.S.A. 2004, 101:6905-6910.
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 6905-6910
    • Rasouli-Nia, A.1    Karimi-Busheri, F.2    Weinfeld, M.3
  • 60
    • 34547096276 scopus 로고    scopus 로고
    • Human polynucleotide kinase participates in repair of DNA double-strand breaks by nonhomologous end joining but not homologous recombination
    • Karimi-Busheri F., Rasouli-Nia A., Allalunis-Turner J., Weinfeld M. Human polynucleotide kinase participates in repair of DNA double-strand breaks by nonhomologous end joining but not homologous recombination. Cancer Res. 2007, 67:6619-6625.
    • (2007) Cancer Res. , vol.67 , pp. 6619-6625
    • Karimi-Busheri, F.1    Rasouli-Nia, A.2    Allalunis-Turner, J.3    Weinfeld, M.4
  • 61
    • 79956205952 scopus 로고    scopus 로고
    • Polymerases in Nonhomologous end joining: Building a bridge over broken chromosomes
    • Ramsden D. Polymerases in Nonhomologous end joining: Building a bridge over broken chromosomes. Antioxid. Redox Signal. 2010.
    • (2010) Antioxid. Redox Signal.
    • Ramsden, D.1
  • 62
    • 17944397758 scopus 로고    scopus 로고
    • Hydrocephalus, situs inversus, chronic sinusitis, and male infertility in DNA polymerase lambda-deficient mice: possible implication for the pathogenesis of immotile cilia syndrome
    • Kobayashi Y., Watanabe M., Okada Y., Sawa H., Takai H., Nakanishi M., Kawase Y., Suzuki H., Nagashima K., Ikeda K., Motoyama N. Hydrocephalus, situs inversus, chronic sinusitis, and male infertility in DNA polymerase lambda-deficient mice: possible implication for the pathogenesis of immotile cilia syndrome. Mol. Cell. Biol. 2002, 22:2769-2776.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 2769-2776
    • Kobayashi, Y.1    Watanabe, M.2    Okada, Y.3    Sawa, H.4    Takai, H.5    Nakanishi, M.6    Kawase, Y.7    Suzuki, H.8    Nagashima, K.9    Ikeda, K.10    Motoyama, N.11
  • 63
    • 0041931065 scopus 로고    scopus 로고
    • Immunoglobulin kappa light chain gene rearrangement is impaired in mice deficient for DNA polymerase mu
    • Bertocci B., De Smet A., Berek C., Weill J.C., Reynaud C.A. Immunoglobulin kappa light chain gene rearrangement is impaired in mice deficient for DNA polymerase mu. Immunity 2003, 19:203-211.
    • (2003) Immunity , vol.19 , pp. 203-211
    • Bertocci, B.1    De Smet, A.2    Berek, C.3    Weill, J.C.4    Reynaud, C.A.5
  • 64
    • 33745997776 scopus 로고    scopus 로고
    • Nonoverlapping functions of DNA polymerases mu, lambda, and terminal deoxynucleotidyltransferase during immunoglobulin V(D)J recombination in vivo
    • Bertocci B., De Smet A., Weill J.C., Reynaud C.A. Nonoverlapping functions of DNA polymerases mu, lambda, and terminal deoxynucleotidyltransferase during immunoglobulin V(D)J recombination in vivo. Immunity 2006, 25:31-41.
    • (2006) Immunity , vol.25 , pp. 31-41
    • Bertocci, B.1    De Smet, A.2    Weill, J.C.3    Reynaud, C.A.4
  • 66
    • 73349093475 scopus 로고    scopus 로고
    • Translesion DNA synthesis-assisted non-homologous end-joining of complex double-strand breaks prevents loss of DNA sequences in mammalian cells
    • Covo S., de Villartay J.P., Jeggo P.A., Livneh Z. Translesion DNA synthesis-assisted non-homologous end-joining of complex double-strand breaks prevents loss of DNA sequences in mammalian cells. Nucleic Acids Res. 2009, 37:6737-6745.
    • (2009) Nucleic Acids Res. , vol.37 , pp. 6737-6745
    • Covo, S.1    de Villartay, J.P.2    Jeggo, P.A.3    Livneh, Z.4
  • 69
    • 0032585526 scopus 로고    scopus 로고
    • Targeted disruption of the gene encoding DNA ligase IV leads to lethality in embryonic mice
    • Barnes D.E., Stamp G., Rosewell I., Denzel A., Lindahl T. Targeted disruption of the gene encoding DNA ligase IV leads to lethality in embryonic mice. Curr. Biol. 1998, 8:1395-1398.
    • (1998) Curr. Biol. , vol.8 , pp. 1395-1398
    • Barnes, D.E.1    Stamp, G.2    Rosewell, I.3    Denzel, A.4    Lindahl, T.5
  • 70
    • 0035834067 scopus 로고    scopus 로고
    • DNA ligase IV-deficient cells are more resistant to ionizing radiation in the absence of Ku70: Implications for DNA double-strand break repair
    • Adachi N., Ishino T., Ishii Y., Takeda S., Koyama H. DNA ligase IV-deficient cells are more resistant to ionizing radiation in the absence of Ku70: Implications for DNA double-strand break repair. Proc. Natl. Acad. Sci. U.S.A. 2001, 98:12109-12113.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 12109-12113
    • Adachi, N.1    Ishino, T.2    Ishii, Y.3    Takeda, S.4    Koyama, H.5
  • 71
    • 0032185230 scopus 로고    scopus 로고
    • DNA ligase IV is essential for V(D)J recombination and DNA double-strand break repair in human precursor lymphocytes
    • Grawunder U., Zimmer D., Fugmann S., Schwarz K., Lieber M.R. DNA ligase IV is essential for V(D)J recombination and DNA double-strand break repair in human precursor lymphocytes. Mol. Cell 1998, 2:477-484.
    • (1998) Mol. Cell , vol.2 , pp. 477-484
    • Grawunder, U.1    Zimmer, D.2    Fugmann, S.3    Schwarz, K.4    Lieber, M.R.5
  • 74
    • 0037027853 scopus 로고    scopus 로고
    • The embryonic lethality in DNA ligase IV-deficient mice is rescued by deletion of Ku: implications for unifying the heterogeneous phenotypes of NHEJ mutants
    • Karanjawala Z.E., Adachi N., Irvine R.A., Oh E.K., Shibata D., Schwarz K., Hsieh C.L., Lieber M.R. The embryonic lethality in DNA ligase IV-deficient mice is rescued by deletion of Ku: implications for unifying the heterogeneous phenotypes of NHEJ mutants. DNA Repair (Amst.) 2002, 1:1017-1026.
    • (2002) DNA Repair (Amst.) , vol.1 , pp. 1017-1026
    • Karanjawala, Z.E.1    Adachi, N.2    Irvine, R.A.3    Oh, E.K.4    Shibata, D.5    Schwarz, K.6    Hsieh, C.L.7    Lieber, M.R.8
  • 75
    • 0029024927 scopus 로고
    • Molecular cloning and expression of human cDNAs encoding a novel DNA ligase IV and DNA ligase III, an enzyme active in DNA repair and recombination
    • Wei Y.F., Robins P., Carter K., Caldecott K., Pappin D.J., Yu G.L., Wang R.P., Shell B.K., Nash R.A., Schar P., et al. Molecular cloning and expression of human cDNAs encoding a novel DNA ligase IV and DNA ligase III, an enzyme active in DNA repair and recombination. Mol. Cell. Biol. 1995, 15:3206-3216.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 3206-3216
    • Wei, Y.F.1    Robins, P.2    Carter, K.3    Caldecott, K.4    Pappin, D.J.5    Yu, G.L.6    Wang, R.P.7    Shell, B.K.8    Nash, R.A.9    Schar, P.10
  • 76
    • 0032537803 scopus 로고    scopus 로고
    • DNA ligase IV binds to XRCC4 via a motif located between rather than within its BRCT domains
    • Grawunder U., Zimmer D., Leiber M.R. DNA ligase IV binds to XRCC4 via a motif located between rather than within its BRCT domains. Curr. Biol. 1998, 8:873-876.
    • (1998) Curr. Biol. , vol.8 , pp. 873-876
    • Grawunder, U.1    Zimmer, D.2    Leiber, M.R.3
  • 77
    • 0034669204 scopus 로고    scopus 로고
    • Crystal structure of the Xrcc4 DNA repair protein and implications for end joining
    • Junop M.S., Modesti M., Guarne A., Ghirlando R., Gellert M., Yang W. Crystal structure of the Xrcc4 DNA repair protein and implications for end joining. EMBO J. 2000, 19:5962-5970.
    • (2000) EMBO J. , vol.19 , pp. 5962-5970
    • Junop, M.S.1    Modesti, M.2    Guarne, A.3    Ghirlando, R.4    Gellert, M.5    Yang, W.6
  • 79
    • 0242289356 scopus 로고    scopus 로고
    • Tetramerization and DNA ligase IV interaction of the DNA double-strand break repair protein XRCC4 are mutually exclusive
    • Modesti M., Junop M.S., Ghirlando R., van de Rakt M., Gellert M., Yang W., Kanaar R. Tetramerization and DNA ligase IV interaction of the DNA double-strand break repair protein XRCC4 are mutually exclusive. J. Mol. Biol. 2003, 334:215-228.
    • (2003) J. Mol. Biol. , vol.334 , pp. 215-228
    • Modesti, M.1    Junop, M.S.2    Ghirlando, R.3    van de Rakt, M.4    Gellert, M.5    Yang, W.6    Kanaar, R.7
  • 80
    • 0032971199 scopus 로고    scopus 로고
    • Absence of DNA ligase IV protein in XR-1 cells: evidence for stabilization by XRCC4
    • Bryans M., Valenzano M.C., Stamato T.D. Absence of DNA ligase IV protein in XR-1 cells: evidence for stabilization by XRCC4. Mutat. Res. 1999, 433:53-58.
    • (1999) Mutat. Res. , vol.433 , pp. 53-58
    • Bryans, M.1    Valenzano, M.C.2    Stamato, T.D.3
  • 81
    • 0030743386 scopus 로고    scopus 로고
    • Activity of DNA ligase IV stimulated by complex formation with XRCC4 protein in mammalian cells
    • Grawunder U., Wilm M., Wu X., Kulesza P., Wilson T.E., Mann M., Lieber M.R. Activity of DNA ligase IV stimulated by complex formation with XRCC4 protein in mammalian cells. Nature 1997, 388:492-495.
    • (1997) Nature , vol.388 , pp. 492-495
    • Grawunder, U.1    Wilm, M.2    Wu, X.3    Kulesza, P.4    Wilson, T.E.5    Mann, M.6    Lieber, M.R.7
  • 82
    • 0033119394 scopus 로고    scopus 로고
    • DNA binding of Xrcc4 protein is associated with V(D)J recombination but not with stimulation of DNA ligase IV activity
    • Modesti M., Hesse J.E., Gellert M. DNA binding of Xrcc4 protein is associated with V(D)J recombination but not with stimulation of DNA ligase IV activity. EMBO J. 1999, 18:2008-2018.
    • (1999) EMBO J. , vol.18 , pp. 2008-2018
    • Modesti, M.1    Hesse, J.E.2    Gellert, M.3
  • 86
    • 31044432090 scopus 로고    scopus 로고
    • XLF interacts with the XRCC4-DNA ligase IV complex to promote DNA nonhomologous end-joining
    • Ahnesorg P., Smith P., Jackson S.P. XLF interacts with the XRCC4-DNA ligase IV complex to promote DNA nonhomologous end-joining. Cell 2006, 124:301-313.
    • (2006) Cell , vol.124 , pp. 301-313
    • Ahnesorg, P.1    Smith, P.2    Jackson, S.P.3
  • 87
    • 34249938518 scopus 로고    scopus 로고
    • Cernunnos/XLF promotes the ligation of mismatched and noncohesive DNA ends
    • Tsai C.J., Kim S.A., Chu G. Cernunnos/XLF promotes the ligation of mismatched and noncohesive DNA ends. Proc. Natl. Acad. Sci. U.S.A. 2007, 104:7851-7856.
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 7851-7856
    • Tsai, C.J.1    Kim, S.A.2    Chu, G.3
  • 89
    • 34848841930 scopus 로고    scopus 로고
    • Single-stranded DNA ligation and XLF-stimulated incompatible DNA end ligation by the XRCC4-DNA ligase IV complex: influence of terminal DNA sequence
    • Gu J., Lu H., Tsai A.G., Schwarz K., Lieber M.R. Single-stranded DNA ligation and XLF-stimulated incompatible DNA end ligation by the XRCC4-DNA ligase IV complex: influence of terminal DNA sequence. Nucleic Acids Res. 2007, 35:5755-5762.
    • (2007) Nucleic Acids Res. , vol.35 , pp. 5755-5762
    • Gu, J.1    Lu, H.2    Tsai, A.G.3    Schwarz, K.4    Lieber, M.R.5
  • 90
    • 37349113779 scopus 로고    scopus 로고
    • Crystal structure of human XLF: a twist in nonhomologous DNA end-joining
    • Andres S.N., Modesti M., Tsai C.J., Chu G., Junop M.S. Crystal structure of human XLF: a twist in nonhomologous DNA end-joining. Mol. Cell 2007, 28:1093-1101.
    • (2007) Mol. Cell , vol.28 , pp. 1093-1101
    • Andres, S.N.1    Modesti, M.2    Tsai, C.J.3    Chu, G.4    Junop, M.S.5
  • 95
    • 2442707746 scopus 로고    scopus 로고
    • 53BP1 links DNA damage-response pathways to immunoglobulin heavy chain class-switch recombination
    • Manis J.P., Morales J.C., Xia Z., Kutok J.L., Alt F.W., Carpenter P.B. 53BP1 links DNA damage-response pathways to immunoglobulin heavy chain class-switch recombination. Nat. Immunol. 2004, 5:481-487.
    • (2004) Nat. Immunol. , vol.5 , pp. 481-487
    • Manis, J.P.1    Morales, J.C.2    Xia, Z.3    Kutok, J.L.4    Alt, F.W.5    Carpenter, P.B.6
  • 97
    • 33846340098 scopus 로고    scopus 로고
    • Enhanced intra-switch region recombination during immunoglobulin class switch recombination in 53BP1-/- B cells
    • Reina-San-Martin B., Chen J., Nussenzweig A., Nussenzweig M.C. Enhanced intra-switch region recombination during immunoglobulin class switch recombination in 53BP1-/- B cells. Eur. J. Immunol. 2007, 37:235-239.
    • (2007) Eur. J. Immunol. , vol.37 , pp. 235-239
    • Reina-San-Martin, B.1    Chen, J.2    Nussenzweig, A.3    Nussenzweig, M.C.4
  • 99
    • 77955841725 scopus 로고    scopus 로고
    • The MRN complex in double-strand break repair and telomere maintenance
    • Lamarche B.J., Orazio N.I., Weitzman M.D. The MRN complex in double-strand break repair and telomere maintenance. FEBS Lett. 2010, 584:3682-3695.
    • (2010) FEBS Lett. , vol.584 , pp. 3682-3695
    • Lamarche, B.J.1    Orazio, N.I.2    Weitzman, M.D.3
  • 100
    • 77955847245 scopus 로고    scopus 로고
    • Multiple roles of ATM in monitoring and maintaining DNA integrity
    • Derheimer F.A., Kastan M.B. Multiple roles of ATM in monitoring and maintaining DNA integrity. FEBS Lett. 2010, 584:3675-3681.
    • (2010) FEBS Lett. , vol.584 , pp. 3675-3681
    • Derheimer, F.A.1    Kastan, M.B.2
  • 101
    • 0032859119 scopus 로고    scopus 로고
    • Mre11 and Ku70 interact in somatic cells, but are differentially expressed in early meiosis
    • Goedecke W., Eijpe M., Offenberg H.H., van Aalderen M., Heyting C. Mre11 and Ku70 interact in somatic cells, but are differentially expressed in early meiosis. Nat. Genet. 1999, 23:194-198.
    • (1999) Nat. Genet. , vol.23 , pp. 194-198
    • Goedecke, W.1    Eijpe, M.2    Offenberg, H.H.3    van Aalderen, M.4    Heyting, C.5
  • 102
    • 0029791694 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae Ku70 potentiates illegitimate DNA double-strand break repair and serves as a barrier to error-prone DNA repair pathways
    • Boulton S.J., Jackson S.P. Saccharomyces cerevisiae Ku70 potentiates illegitimate DNA double-strand break repair and serves as a barrier to error-prone DNA repair pathways. EMBO J. 1996, 15:5093-5103.
    • (1996) EMBO J. , vol.15 , pp. 5093-5103
    • Boulton, S.J.1    Jackson, S.P.2
  • 108
    • 58149308524 scopus 로고    scopus 로고
    • Altered kinetics of nonhomologous end joining and class switch recombination in ligase IV-deficient B cells
    • Han L., Yu K. Altered kinetics of nonhomologous end joining and class switch recombination in ligase IV-deficient B cells. J. Exp. Med. 2008, 205:2745-2753.
    • (2008) J. Exp. Med. , vol.205 , pp. 2745-2753
    • Han, L.1    Yu, K.2
  • 110
  • 111
    • 46249131123 scopus 로고    scopus 로고
    • Alternative-NHEJ is a mechanistically distinct pathway of mammalian chromosome break repair
    • Bennardo N., Cheng A., Huang N., Stark J.M. Alternative-NHEJ is a mechanistically distinct pathway of mammalian chromosome break repair. PLoS Genet. 2008, 4:e1000110.
    • (2008) PLoS Genet. , vol.4
    • Bennardo, N.1    Cheng, A.2    Huang, N.3    Stark, J.M.4
  • 112
    • 0023659483 scopus 로고
    • Extrachromosomal DNA substrates in pre-B cells undergo inversion or deletion at immunoglobulin V-(D)-J joining signals
    • Hesse J.E., Lieber M.R., Gellert M., Mizuuchi K. Extrachromosomal DNA substrates in pre-B cells undergo inversion or deletion at immunoglobulin V-(D)-J joining signals. Cell 1987, 49:775-783.
    • (1987) Cell , vol.49 , pp. 775-783
    • Hesse, J.E.1    Lieber, M.R.2    Gellert, M.3    Mizuuchi, K.4
  • 113
    • 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. 2010, 79:181-211.
    • (2010) Annu. Rev. Biochem. , vol.79 , pp. 181-211
    • Lieber, M.R.1
  • 114
    • 36749007206 scopus 로고    scopus 로고
    • Linking double-stranded DNA breaks to the recombination activating gene complex directs repair to the nonhomologous end-joining pathway
    • Cui X., Meek K. Linking double-stranded DNA breaks to the recombination activating gene complex directs repair to the nonhomologous end-joining pathway. Proc. Natl. Acad. Sci. U.S.A. 2007, 104:17046-17051.
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 17046-17051
    • Cui, X.1    Meek, K.2
  • 119
    • 0037188898 scopus 로고    scopus 로고
    • Unrepaired DNA breaks in p53-deficient cells lead to oncogenic gene amplification subsequent to translocations
    • Zhu C., Mills K.D., Ferguson D.O., Lee C., Manis J., Fleming J., Gao Y., Morton C.C., Alt F.W. Unrepaired DNA breaks in p53-deficient cells lead to oncogenic gene amplification subsequent to translocations. Cell 2002, 109:811-821.
    • (2002) Cell , vol.109 , pp. 811-821
    • Zhu, C.1    Mills, K.D.2    Ferguson, D.O.3    Lee, C.4    Manis, J.5    Fleming, J.6    Gao, Y.7    Morton, C.C.8    Alt, F.W.9
  • 120
    • 77950462986 scopus 로고    scopus 로고
    • Alternative end-joining is suppressed by the canonical NHEJ component Xrcc4-ligase IV during chromosomal translocation formation
    • Simsek D., Jasin M. Alternative end-joining is suppressed by the canonical NHEJ component Xrcc4-ligase IV during chromosomal translocation formation. Nat. Struct. Mol. Biol. 2010, 17:410-416.
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 410-416
    • Simsek, D.1    Jasin, M.2
  • 121
    • 77950466186 scopus 로고    scopus 로고
    • NHEJ and its backup pathways in chromosomal translocations
    • Lieber M.R. NHEJ and its backup pathways in chromosomal translocations. Nat. Struct. Mol. Biol. 2010, 17:393-395.
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 393-395
    • Lieber, M.R.1
  • 123
    • 54849404458 scopus 로고    scopus 로고
    • MMEJ repair of double-strand breaks (director's cut): deleted sequences and alternative endings
    • McVey M., Lee S.E. MMEJ repair of double-strand breaks (director's cut): deleted sequences and alternative endings. Trends Genet. 2008, 24:529-538.
    • (2008) Trends Genet. , vol.24 , pp. 529-538
    • McVey, M.1    Lee, S.E.2
  • 124
    • 69949173301 scopus 로고    scopus 로고
    • Backup pathways of NHEJ in cells of higher eukaryotes: cell cycle dependence
    • Iliakis G. Backup pathways of NHEJ in cells of higher eukaryotes: cell cycle dependence. Radiother. Oncol. 2009, 92:310-315.
    • (2009) Radiother. Oncol. , vol.92 , pp. 310-315
    • Iliakis, G.1
  • 125
    • 0032085295 scopus 로고    scopus 로고
    • The 3' to 5' exonuclease activity of Mre 11 facilitates repair of DNA double-strand breaks
    • Paull T.T., Gellert M. The 3' to 5' exonuclease activity of Mre 11 facilitates repair of DNA double-strand breaks. Mol. Cell 1998, 1:969-979.
    • (1998) Mol. Cell , vol.1 , pp. 969-979
    • Paull, T.T.1    Gellert, M.2
  • 126
    • 0033563229 scopus 로고    scopus 로고
    • Nbs1 potentiates ATP-driven DNA unwinding and endonuclease cleavage by the Mre11/Rad50 complex
    • Paull T.T., Gellert M. Nbs1 potentiates ATP-driven DNA unwinding and endonuclease cleavage by the Mre11/Rad50 complex. Genes Dev. 1999, 13:1276-1288.
    • (1999) Genes Dev. , vol.13 , pp. 1276-1288
    • Paull, T.T.1    Gellert, M.2
  • 127
    • 71949092988 scopus 로고    scopus 로고
    • Meiotic DNA double-strand break repair requires two nucleases, MRN and Ctp1, to produce a single size class of Rec12 (Spo11)-oligonucleotide complexes
    • Milman N., Higuchi E., Smith G.R. Meiotic DNA double-strand break repair requires two nucleases, MRN and Ctp1, to produce a single size class of Rec12 (Spo11)-oligonucleotide complexes. Mol. Cell Biol. 2009, 29:5998-6005.
    • (2009) Mol. Cell Biol. , vol.29 , pp. 5998-6005
    • Milman, N.1    Higuchi, E.2    Smith, G.R.3
  • 129
    • 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. 2004, 24:9478-9486.
    • (2004) Mol. Cell Biol. , vol.24 , pp. 9478-9486
    • Yu, X.1    Chen, J.2
  • 130
    • 75149189204 scopus 로고    scopus 로고
    • BRCA1 and its toolbox for the maintenance of genome integrity
    • Huen M.S., Sy S.M., Chen J. BRCA1 and its toolbox for the maintenance of genome integrity. Nat. Rev. Mol. Cell Biol. 2010, 11:138-148.
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 138-148
    • Huen, M.S.1    Sy, S.M.2    Chen, J.3
  • 131
    • 68249116573 scopus 로고    scopus 로고
    • DNA end resection: many nucleases make light work
    • Mimitou E.P., Symington L.S. DNA end resection: many nucleases make light work. DNA Repair (Amst.) 2009, 8:983-995.
    • (2009) DNA Repair (Amst.) , vol.8 , pp. 983-995
    • Mimitou, E.P.1    Symington, L.S.2
  • 133
  • 135
    • 0028072098 scopus 로고
    • Purification and characterization of the human Rad51 protein, an analogue of E. coli RecA
    • Benson F.E., Stasiak A., West S.C. Purification and characterization of the human Rad51 protein, an analogue of E. coli RecA. EMBO J. 1994, 13:5764-5771.
    • (1994) EMBO J. , vol.13 , pp. 5764-5771
    • Benson, F.E.1    Stasiak, A.2    West, S.C.3
  • 136
    • 77955910902 scopus 로고    scopus 로고
    • Role of homologous recombination in DNA interstrand crosslink repair
    • Hinz J.M. Role of homologous recombination in DNA interstrand crosslink repair. Environ. Mol. Mutagen. 2010, 51:582-603.
    • (2010) Environ. Mol. Mutagen. , vol.51 , pp. 582-603
    • Hinz, J.M.1
  • 137
    • 77957975815 scopus 로고    scopus 로고
    • Purified human BRCA2 stimulates RAD51-mediated recombination
    • Jensen R.B., Carreira A., Kowalczykowski S.C. Purified human BRCA2 stimulates RAD51-mediated recombination. Nature 2010.
    • (2010) Nature
    • Jensen, R.B.1    Carreira, A.2    Kowalczykowski, S.C.3
  • 141
    • 0030832230 scopus 로고    scopus 로고
    • Isolation of human and mouse genes based on homology to REC2, a recombinational repair gene from the fungus Ustilago maydis
    • Rice M.C., Smith S.T., Bullrich F., Havre P., Kmiec E.B. Isolation of human and mouse genes based on homology to REC2, a recombinational repair gene from the fungus Ustilago maydis. Proc. Natl. Acad. Sci. U.S.A. 1997, 94:7417-7422.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 7417-7422
    • Rice, M.C.1    Smith, S.T.2    Bullrich, F.3    Havre, P.4    Kmiec, E.B.5
  • 143
    • 0032053857 scopus 로고    scopus 로고
    • Identification, characterization, and genetic mapping of Rad51d, a new mouse and human RAD51/RecA-related gene
    • Pittman D.L., Weinberg L.R., Schimenti J.C. Identification, characterization, and genetic mapping of Rad51d, a new mouse and human RAD51/RecA-related gene. Genomics 1998, 49:103-111.
    • (1998) Genomics , vol.49 , pp. 103-111
    • Pittman, D.L.1    Weinberg, L.R.2    Schimenti, J.C.3
  • 144
    • 0032126530 scopus 로고    scopus 로고
    • The XRCC2 DNA repair gene from human and mouse encodes a novel member of the recA/RAD51 family
    • Cartwright R., Tambini C.E., Simpson P.J., Thacker J. The XRCC2 DNA repair gene from human and mouse encodes a novel member of the recA/RAD51 family. Nucleic Acids Res. 1998, 26:3084-3089.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 3084-3089
    • Cartwright, R.1    Tambini, C.E.2    Simpson, P.J.3    Thacker, J.4
  • 146
    • 0035893241 scopus 로고    scopus 로고
    • Mediator function of the human Rad51B-Rad51C complex in Rad51/RPA-catalyzed DNA strand exchange
    • Sigurdsson S., Van Komen S., Bussen W., Schild D., Albala J.S., Sung P. Mediator function of the human Rad51B-Rad51C complex in Rad51/RPA-catalyzed DNA strand exchange. Genes Dev. 2001, 15:3308-3318.
    • (2001) Genes Dev. , vol.15 , pp. 3308-3318
    • Sigurdsson, S.1    Van Komen, S.2    Bussen, W.3    Schild, D.4    Albala, J.S.5    Sung, P.6
  • 147
    • 33749037701 scopus 로고    scopus 로고
    • Mechanism of homologous recombination: mediators and helicases take on regulatory functions
    • Sung P., Klein H. Mechanism of homologous recombination: mediators and helicases take on regulatory functions. Nat. Rev. Mol. Cell Biol. 2006, 7:739-750.
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 739-750
    • Sung, P.1    Klein, H.2
  • 148
    • 0037044802 scopus 로고    scopus 로고
    • Homologous DNA pairing by human recombination factors Rad51 and Rad54
    • Sigurdsson S., Van Komen S., Petukhova G., Sung P. Homologous DNA pairing by human recombination factors Rad51 and Rad54. J. Biol. Chem. 2002, 277:42790-42794.
    • (2002) J. Biol. Chem. , vol.277 , pp. 42790-42794
    • Sigurdsson, S.1    Van Komen, S.2    Petukhova, G.3    Sung, P.4
  • 149
    • 10644264232 scopus 로고    scopus 로고
    • Human Rad54 protein stimulates DNA strand exchange activity of hRad51 protein in the presence of Ca2+
    • Mazina O.M., Mazin A.V. Human Rad54 protein stimulates DNA strand exchange activity of hRad51 protein in the presence of Ca2+. J. Biol. Chem. 2004, 279:52042-52051.
    • (2004) J. Biol. Chem. , vol.279 , pp. 52042-52051
    • Mazina, O.M.1    Mazin, A.V.2
  • 150
    • 33748713412 scopus 로고    scopus 로고
    • Rad54: the Swiss Army knife of homologous recombination?
    • Heyer W.D., Li X., Rolfsmeier M., Zhang X.P. Rad54: the Swiss Army knife of homologous recombination?. Nucleic Acids Res. 2006, 34:4115-4125.
    • (2006) Nucleic Acids Res. , vol.34 , pp. 4115-4125
    • Heyer, W.D.1    Li, X.2    Rolfsmeier, M.3    Zhang, X.P.4
  • 151
    • 50649100744 scopus 로고    scopus 로고
    • Mechanism of eukaryotic homologous recombination
    • San Filippo J., Sung P., Klein H. Mechanism of eukaryotic homologous recombination. Annu. Rev. Biochem. 2008, 77:229-257.
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 229-257
    • San Filippo, J.1    Sung, P.2    Klein, H.3
  • 152
    • 23744447715 scopus 로고    scopus 로고
    • Independent and sequential recruitment of NHEJ and HR factors to DNA damage sites in mammalian cells
    • Kim J.S., Krasieva T.B., Kurumizaka H., Chen D.J., Taylor A.M., Yokomori K. Independent and sequential recruitment of NHEJ and HR factors to DNA damage sites in mammalian cells. J. Cell Biol. 2005, 170:341-347.
    • (2005) J. Cell Biol. , vol.170 , pp. 341-347
    • Kim, J.S.1    Krasieva, T.B.2    Kurumizaka, H.3    Chen, D.J.4    Taylor, A.M.5    Yokomori, K.6
  • 153
    • 0036864626 scopus 로고    scopus 로고
    • Transient stability of DNA ends allows nonhomologous end joining to precede homologous recombination
    • Frank-Vaillant M., Marcand S. Transient stability of DNA ends allows nonhomologous end joining to precede homologous recombination. Mol. Cell 2002, 10:1189-1199.
    • (2002) Mol. Cell , vol.10 , pp. 1189-1199
    • Frank-Vaillant, M.1    Marcand, S.2
  • 155
    • 0032530658 scopus 로고    scopus 로고
    • Homologous recombination and non-homologous end-joining pathways of DNA double-strand break repair have overlapping roles in the maintenance of chromosomal integrity in vertebrate cells
    • Takata M., Sasaki M.S., Sonoda E., Morrison C., Hashimoto M., Utsumi H., Yamaguchi-Iwai Y., Shinohara A., Takeda S. Homologous recombination and non-homologous end-joining pathways of DNA double-strand break repair have overlapping roles in the maintenance of chromosomal integrity in vertebrate cells. EMBO J. 1998, 17:5497-5508.
    • (1998) EMBO J. , vol.17 , pp. 5497-5508
    • Takata, M.1    Sasaki, M.S.2    Sonoda, E.3    Morrison, C.4    Hashimoto, M.5    Utsumi, H.6    Yamaguchi-Iwai, Y.7    Shinohara, A.8    Takeda, S.9
  • 157
    • 0000391880 scopus 로고    scopus 로고
    • Evidence for DNA-PK-dependent and -independent DNA double-strand break repair pathways in mammalian cells as a function of the cell cycle
    • Lee S.E., Mitchell R.A., Cheng A., Hendrickson E.A. Evidence for DNA-PK-dependent and -independent DNA double-strand break repair pathways in mammalian cells as a function of the cell cycle. Mol. Cell. Biol. 1997, 17:1425-1433.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 1425-1433
    • Lee, S.E.1    Mitchell, R.A.2    Cheng, A.3    Hendrickson, E.A.4
  • 158
    • 52049098230 scopus 로고    scopus 로고
    • Comparison of nonhomologous end joining and homologous recombination in human cells
    • Mao Z., Bozzella M., Seluanov A., Gorbunova V. Comparison of nonhomologous end joining and homologous recombination in human cells. DNA Repair (Amst.) 2008, 7:1765-1771.
    • (2008) DNA Repair (Amst.) , vol.7 , pp. 1765-1771
    • Mao, Z.1    Bozzella, M.2    Seluanov, A.3    Gorbunova, V.4
  • 159
    • 0025845230 scopus 로고
    • Comparison of DNA double-strand break rejoining as measured by pulsed field gel electrophoresis, neutral sucrose gradient centrifugation and non-unwinding filter elution in irradiated plateau-phase CHO cells
    • Iliakis G., Blocher D., Metzger L., Pantelias G. Comparison of DNA double-strand break rejoining as measured by pulsed field gel electrophoresis, neutral sucrose gradient centrifugation and non-unwinding filter elution in irradiated plateau-phase CHO cells. Int. J. Radiat. Biol. 1991, 59:927-939.
    • (1991) Int. J. Radiat. Biol. , vol.59 , pp. 927-939
    • Iliakis, G.1    Blocher, D.2    Metzger, L.3    Pantelias, G.4
  • 160
    • 0025739820 scopus 로고
    • Kinetics of DNA double-strand break repair throughout the cell cycle as assayed by pulsed field gel electrophoresis in CHO cells
    • Metzger L., Iliakis G. Kinetics of DNA double-strand break repair throughout the cell cycle as assayed by pulsed field gel electrophoresis in CHO cells. Int. J. Radiat. Biol. 1991, 59:1325-1339.
    • (1991) Int. J. Radiat. Biol. , vol.59 , pp. 1325-1339
    • Metzger, L.1    Iliakis, G.2
  • 161
    • 61549098717 scopus 로고    scopus 로고
    • Replication stress induces genome-wide copy number changes in human cells that resemble polymorphic and pathogenic variants
    • Arlt M.F., Mulle J.G., Schaibley V.M., Ragland R.L., Durkin S.G., Warren S.T., Glover T.W. Replication stress induces genome-wide copy number changes in human cells that resemble polymorphic and pathogenic variants. Am. J. Hum. Genet. 2009, 84:339-350.
    • (2009) Am. J. Hum. Genet. , vol.84 , pp. 339-350
    • Arlt, M.F.1    Mulle, J.G.2    Schaibley, V.M.3    Ragland, R.L.4    Durkin, S.G.5    Warren, S.T.6    Glover, T.W.7
  • 162
    • 0142025259 scopus 로고    scopus 로고
    • Interactive competition between homologous recombination and non-homologous end joining
    • Allen C., Halbrook J., Nickoloff J.A. Interactive competition between homologous recombination and non-homologous end joining. Mol. Cancer Res. 2003, 1:913-920.
    • (2003) Mol. Cancer Res. , vol.1 , pp. 913-920
    • Allen, C.1    Halbrook, J.2    Nickoloff, J.A.3
  • 168
    • 77649225150 scopus 로고    scopus 로고
    • Ku regulates the non-homologous end joining pathway choice of DNA double-strand break repair in human somatic cells
    • Fattah F., Lee E.H., Weisensel N., Wang Y., Lichter N., Hendrickson E.A. Ku regulates the non-homologous end joining pathway choice of DNA double-strand break repair in human somatic cells. PLoS Genet. 2010, 6:e1000855.
    • (2010) PLoS Genet. , vol.6
    • Fattah, F.1    Lee, E.H.2    Weisensel, N.3    Wang, Y.4    Lichter, N.5    Hendrickson, E.A.6
  • 170
    • 0142149190 scopus 로고    scopus 로고
    • Distinct pathways of nonhomologous end joining that are differentially regulated by DNA-dependent protein kinase-mediated phosphorylation
    • Udayakumar D., Bladen C.L., Hudson F.Z., Dynan W.S. Distinct pathways of nonhomologous end joining that are differentially regulated by DNA-dependent protein kinase-mediated phosphorylation. J. Biol. Chem. 2003, 278:41631-41635.
    • (2003) J. Biol. Chem. , vol.278 , pp. 41631-41635
    • Udayakumar, D.1    Bladen, C.L.2    Hudson, F.Z.3    Dynan, W.S.4
  • 174
    • 0028897304 scopus 로고
    • DNA-dependent protein kinase activity is absent in xrs-6 cells: implications for site-specific recombination and DNA double-strand break repair
    • Finnie N.J., Gottlieb T.M., Blunt T., Jeggo P.A., Jackson S.P. DNA-dependent protein kinase activity is absent in xrs-6 cells: implications for site-specific recombination and DNA double-strand break repair. Proc. Natl. Acad. Sci. U.S.A. 1995, 92:320-324.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 320-324
    • Finnie, N.J.1    Gottlieb, T.M.2    Blunt, T.3    Jeggo, P.A.4    Jackson, S.P.5
  • 176
    • 68149110347 scopus 로고    scopus 로고
    • Ku86 represses lethal telomere deletion events in human somatic cells
    • Wang Y., Ghosh G., Hendrickson E.A. Ku86 represses lethal telomere deletion events in human somatic cells. Proc. Natl. Acad. Sci. U.S.A. 2009, 106:12430-12435.
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 12430-12435
    • Wang, Y.1    Ghosh, G.2    Hendrickson, E.A.3
  • 178
    • 78649336706 scopus 로고    scopus 로고
    • The DNA damage response: making it safe to play with knives
    • Ciccia A., Elledge S.J. The DNA damage response: making it safe to play with knives. Mol. Cell 2010, 40:179-204.
    • (2010) Mol. Cell , vol.40 , pp. 179-204
    • Ciccia, A.1    Elledge, S.J.2


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