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Volumn 3, Issue 8-9, 2004, Pages 909-918

Role of DNA-PK in the cellular response to DNA double-strand breaks

Author keywords

Apoptosis; DNA double strand breaks; DNA dependent protein kinase; Innate immunity; Non homologous end joining; Phosphorylation; Telomere maintenance

Indexed keywords

BACTERIAL DNA; DNA DEPENDENT PROTEIN KINASE; DOUBLE STRANDED DNA;

EID: 3242886503     PISSN: 15687864     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.dnarep.2004.03.021     Document Type: Review
Times cited : (199)

References (98)
  • 1
    • 0035093737 scopus 로고    scopus 로고
    • DNA double-strand breaks: Signaling, repair and the cancer connection
    • Khanna K.K., Jackson S.P. DNA double-strand breaks: signaling, repair and the cancer connection. Nat. Genet. 27:2001;247-254
    • (2001) Nat. Genet. , vol.27 , pp. 247-254
    • Khanna, K.K.1    Jackson, S.P.2
  • 2
    • 0033560796 scopus 로고    scopus 로고
    • The DNA-dependent protein kinase
    • Smith G.C., Jackson S.P. The DNA-dependent protein kinase. Genes Dev. 13:1999;916-934
    • (1999) Genes Dev. , vol.13 , pp. 916-934
    • Smith, G.C.1    Jackson, S.P.2
  • 3
    • 0037365789 scopus 로고    scopus 로고
    • ATM and related protein kinases: Safeguarding genome integrity
    • Shiloh Y. ATM and related protein kinases: safeguarding genome integrity. Nat. Rev. Cancer. 3:2003;155-168
    • (2003) Nat. Rev. Cancer , vol.3 , pp. 155-168
    • Shiloh, Y.1
  • 4
    • 0035856495 scopus 로고    scopus 로고
    • DNA repair: How Ku makes ends meet?
    • Doherty A.J., Jackson S.P. DNA repair: how Ku makes ends meet? Curr. Biol. 11:2001;R920-924
    • (2001) Curr. Biol. , vol.11 , pp. 920-924
    • Doherty, A.J.1    Jackson, S.P.2
  • 5
    • 0033006852 scopus 로고    scopus 로고
    • A DNA repair protein with multiple cellular functions?
    • Featherstone C., Jackson Ku S.P. A DNA repair protein with multiple cellular functions? Mutat. Res. 434:1999;3-15
    • (1999) Mutat. Res. , vol.434 , pp. 3-15
    • Featherstone, C.1    Jackson Ku, S.P.2
  • 6
    • 0032509097 scopus 로고    scopus 로고
    • Cryo-EM imaging of the catalytic subunit of the DNA-dependent protein kinase
    • Chiu C.Y., Cary R.B., Chen D.J., Peterson S.R., Stewart P.L. Cryo-EM imaging of the catalytic subunit of the DNA-dependent protein kinase. J. Mol. Biol. 284:1998;1075-1081
    • (1998) J. Mol. Biol. , vol.284 , pp. 1075-1081
    • Chiu, C.Y.1    Cary, R.B.2    Chen, D.J.3    Peterson, S.R.4    Stewart, P.L.5
  • 7
    • 0033104498 scopus 로고    scopus 로고
    • Structure of DNA-dependent protein kinase: Implications for its regulation by DNA
    • Leuther K.K., Hammarsten O., Kornberg R.D., Chu G. Structure of DNA-dependent protein kinase: implications for its regulation by DNA. Embo. J. 18:1999;1114-1123
    • (1999) Embo. J. , vol.18 , pp. 1114-1123
    • Leuther, K.K.1    Hammarsten, O.2    Kornberg, R.D.3    Chu, G.4
  • 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. 412:2001;607-614
    • (2001) Nature , vol.412 , pp. 607-614
    • Walker, J.R.1    Corpina, R.A.2    Goldberg, J.3
  • 9
    • 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. 27:1999;3494-3502
    • (1999) Nucleic Acids Res. , vol.27 , pp. 3494-3502
    • Gell, D.1    Jackson, S.P.2
  • 11
    • 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. 95:1998;525-530
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 525-530
    • Hammarsten, O.1    Chu, G.2
  • 12
    • 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. 27:1999;4679-4686
    • (1999) Nucleic Acids Res. , vol.27 , pp. 4679-4686
    • Yoo, S.1    Dynan, W.S.2
  • 14
    • 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. 21:2002;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
  • 15
    • 0037187199 scopus 로고    scopus 로고
    • Defining interactions between DNA-PK and ligase IV/XRCC4
    • Hsu H.L., Yannone S.M., Chen D.J. Defining interactions between DNA-PK and ligase IV/XRCC4. DNA Repair (Amst.). 1:2002;225-235
    • (2002) DNA Repair (Amst.) , vol.1 , pp. 225-235
    • Hsu, H.L.1    Yannone, S.M.2    Chen, D.J.3
  • 16
    • 0037423743 scopus 로고    scopus 로고
    • Coordinated assembly of Ku and p460 subunits of the DNA-dependent protein kinase on DNA ends is necessary for XRCC4-ligase IV recruitment
    • Calsou P., Delteil C., Frit P., Drouet J., Salles B. Coordinated assembly of Ku and p460 subunits of the DNA-dependent protein kinase on DNA ends is necessary for XRCC4-ligase IV recruitment. J. Mol. Biol. 326:2003;93-103
    • (2003) J. Mol. Biol. , vol.326 , pp. 93-103
    • Calsou, P.1    Delteil, C.2    Frit, P.3    Drouet, J.4    Salles, B.5
  • 17
    • 0034714199 scopus 로고    scopus 로고
    • Interactions of the DNA ligase IV-XRCC4 complex with DNA ends and the DNA-dependent protein kinase
    • Chen L., Trujillo K., Sung P., Tomkinson A.E. Interactions of the DNA ligase IV-XRCC4 complex with DNA ends and the DNA-dependent protein kinase. J. Biol. Chem. 275:2000;26196-26205
    • (2000) J. Biol. Chem. , vol.275 , pp. 26196-26205
    • Chen, L.1    Trujillo, K.2    Sung, P.3    Tomkinson, A.E.4
  • 18
    • 0037224429 scopus 로고    scopus 로고
    • Requirement for XRCC4 and DNA ligase IV in alignment-based gap filling for nonhomologous DNA end joining in vitro
    • Lee J.W., Yannone S.M., Chen D.J., Povirk L.F. Requirement for XRCC4 and DNA ligase IV in alignment-based gap filling for nonhomologous DNA end joining in vitro. Cancer Res. 63:2003;22-24
    • (2003) Cancer Res. , vol.63 , pp. 22-24
    • Lee, J.W.1    Yannone, S.M.2    Chen, D.J.3    Povirk, L.F.4
  • 19
    • 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. 273:1998;1794-1801
    • (1998) J. Biol. Chem. , vol.273 , pp. 1794-1801
    • Leber, R.1    Wise, T.W.2    Mizuta, R.3    Meek, K.4
  • 27
    • 0035851181 scopus 로고    scopus 로고
    • Werner syndrome protein is regulated and phosphorylated by DNA-dependent protein kinase
    • Yannone S.M., Roy S., Chan D.W., Murphy M.B., Huang S., Campisi J., Chen D.J. Werner syndrome protein is regulated and phosphorylated by DNA-dependent protein kinase. J. Biol. Chem. 276:2001;38242-38248
    • (2001) J. Biol. Chem. , vol.276 , pp. 38242-38248
    • Yannone, S.M.1    Roy, S.2    Chan, D.W.3    Murphy, M.B.4    Huang, S.5    Campisi, J.6    Chen, D.J.7
  • 29
    • 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. 108:2002;781-794
    • (2002) Cell , vol.108 , pp. 781-794
    • Ma, Y.1    Pannicke, U.2    Schwarz, K.3    Lieber, M.R.4
  • 30
    • 3242879122 scopus 로고    scopus 로고
    • The mechanism of vertebrate nonhomologous DNA end joining and its role in V(D)J recombination
    • M. Lieber, The mechanism of vertebrate nonhomologous DNA end joining and its role in V(D)J recombination, DNA Repair 3 (2004) 817-826.
    • (2004) DNA Repair , vol.3 , pp. 817-826
    • Lieber, M.1
  • 31
    • 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. 19:1999;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
  • 33
    • 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. 271:1996;8936-8941
    • (1996) J. Biol. Chem. , vol.271 , pp. 8936-8941
    • Chan, D.W.1    Lees-Miller, S.P.2
  • 34
    • 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. 16:2002;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
  • 36
    • 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. 63:2003;1198-1201
    • (2003) Cancer Res. , vol.63 , pp. 1198-1201
    • Soubeyrand, S.1    Pope, L.2    Pakuts, B.3    Hache, R.J.4
  • 37
    • 0033621392 scopus 로고    scopus 로고
    • Substrate specificities and identification of putative substrates of ATM kinase family members
    • Kim S.T., Lim D.S., Canman C.E., Kastan M.B. Substrate specificities and identification of putative substrates of ATM kinase family members. J. Biol. Chem. 274:1999;37538-37543
    • (1999) J. Biol. Chem. , vol.274 , pp. 37538-37543
    • Kim, S.T.1    Lim, D.S.2    Canman, C.E.3    Kastan, M.B.4
  • 38
    • 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. 23:2003;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
  • 39
    • 0032574750 scopus 로고    scopus 로고
    • Homology-directed repair is a major double-strand break repair pathway in mammalian cells
    • Liang F., Han M., Romanienko P.J., Jasin M. Homology-directed repair is a major double-strand break repair pathway in mammalian cells. Proc. Natl. Acad. Sci. U.S.A. 95:1998;5172-5177
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 5172-5177
    • Liang, F.1    Han, M.2    Romanienko, P.J.3    Jasin, M.4
  • 40
    • 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. 17:1997;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
  • 41
    • 0037133699 scopus 로고    scopus 로고
    • DNA-dependent protein kinase suppresses double-strand break-induced and spontaneous homologous recombination
    • Allen C., Kurimasa A., Brenneman M.A., Chen D.J., Nickoloff J.A. DNA-dependent protein kinase suppresses double-strand break-induced and spontaneous homologous recombination. Proc. Natl. Acad. Sci. U.S.A. 99:2002;3758-3763
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 3758-3763
    • Allen, C.1    Kurimasa, A.2    Brenneman, M.A.3    Chen, D.J.4    Nickoloff, J.A.5
  • 44
    • 0033104517 scopus 로고    scopus 로고
    • Replication-mediated DNA damage by camptothecin induces phosphorylation of RPA by DNA-dependent protein kinase and dissociates RPA:DNA-PK complexes
    • Shao R.G., Cao C.X., Zhang H., Kohn K.W., Wold M.S., Pommier Y. Replication-mediated DNA damage by camptothecin induces phosphorylation of RPA by DNA-dependent protein kinase and dissociates RPA:DNA-PK complexes. Embo. J. 18:1999;1397-1406
    • (1999) Embo. J. , vol.18 , pp. 1397-1406
    • Shao, R.G.1    Cao, C.X.2    Zhang, H.3    Kohn, K.W.4    Wold, M.S.5    Pommier, Y.6
  • 45
    • 0035577796 scopus 로고    scopus 로고
    • Replication protein A2 phosphorylation after DNA damage by the coordinated action of ataxia telangiectasia-mutated and DNA-dependent protein kinase
    • Wang H., Guan J., Perrault A.R., Wang Y., Iliakis G. Replication protein A2 phosphorylation after DNA damage by the coordinated action of ataxia telangiectasia-mutated and DNA-dependent protein kinase. Cancer Res. 61:2001;8554-8563
    • (2001) Cancer Res. , vol.61 , pp. 8554-8563
    • Wang, H.1    Guan, J.2    Perrault, A.R.3    Wang, Y.4    Iliakis, G.5
  • 46
    • 0035374588 scopus 로고    scopus 로고
    • Protein phosphatases regulate DNA-dependent protein kinase activity
    • Douglas P., Moorhead G.B., Ye R., Lees-Miller S.P. Protein phosphatases regulate DNA-dependent protein kinase activity. J. Biol. Chem. 276:2001;18992-18998
    • (2001) J. Biol. Chem. , vol.276 , pp. 18992-18998
    • Douglas, P.1    Moorhead, G.B.2    Ye, R.3    Lees-Miller, S.P.4
  • 49
    • 0142240342 scopus 로고    scopus 로고
    • BRCT repeats as phosphopeptide-binding modules involved in protein targeting
    • Manke I.A., Lowery D.M., Nguyen A., Yaffe M.B. BRCT repeats as phosphopeptide-binding modules involved in protein targeting. Science. 302:2003;636-639
    • (2003) Science , vol.302 , pp. 636-639
    • Manke, I.A.1    Lowery, D.M.2    Nguyen, A.3    Yaffe, M.B.4
  • 50
    • 0346101743 scopus 로고    scopus 로고
    • Phosphopeptide binding specificities of BRCA1 COOH-terminal (BRCT) domains
    • Rodriguez M., Yu X., Chen J., Songyang Z. Phosphopeptide binding specificities of BRCA1 COOH-terminal (BRCT) domains. J. Biol. Chem. 278:2003;52914-52918
    • (2003) J. Biol. Chem. , vol.278 , pp. 52914-52918
    • Rodriguez, M.1    Yu, X.2    Chen, J.3    Songyang, Z.4
  • 51
    • 0142147272 scopus 로고    scopus 로고
    • The BRCT domain is a phospho-protein binding domain
    • Yu X., Chini C.C., He M., Mer G., Chen J. The BRCT domain is a phospho-protein binding domain. Science. 302:2003;639-642
    • (2003) Science , vol.302 , pp. 639-642
    • Yu, X.1    Chini, C.C.2    He, M.3    Mer, G.4    Chen, J.5
  • 52
    • 0034597794 scopus 로고    scopus 로고
    • Telomere states and cell fates
    • Blackburn E.H. Telomere states and cell fates. Nature. 408:2000;53-56
    • (2000) Nature , vol.408 , pp. 53-56
    • Blackburn, E.H.1
  • 53
    • 0032076127 scopus 로고    scopus 로고
    • Yeast Ku as a regulator of chromosomal DNA end structure
    • Gravel S., Larrivee M., Labrecque P., Wellinger R.J. Yeast Ku as a regulator of chromosomal DNA end structure. Science. 280:1998;741-744
    • (1998) Science , vol.280 , pp. 741-744
    • Gravel, S.1    Larrivee, M.2    Labrecque, P.3    Wellinger, R.J.4
  • 54
    • 0032536861 scopus 로고    scopus 로고
    • Components of the Ku-dependent non-homologous end-joining pathway are involved in telomeric length maintenance and telomeric silencing
    • Boulton S.J., Jackson S.P. Components of the Ku-dependent non-homologous end-joining pathway are involved in telomeric length maintenance and telomeric silencing. Embo. J. 17:1998;1819-1828
    • (1998) Embo. J. , vol.17 , pp. 1819-1828
    • Boulton, S.J.1    Jackson, S.P.2
  • 55
    • 0033597820 scopus 로고    scopus 로고
    • Ku binds telomeric DNA in vitro
    • Bianchi A., de Lange T. Ku binds telomeric DNA in vitro. J. Biol. Chem. 274:1999;21223-21227
    • (1999) J. Biol. Chem. , vol.274 , pp. 21223-21227
    • Bianchi, A.1    De Lange, T.2
  • 57
    • 0035822641 scopus 로고    scopus 로고
    • Effects of DNA non-homologous end-joining factors on telomere length and chromosomal stability in mammalian cells
    • d'Adda di Fagagna F., Hande M.P., Tong W.M., Roth D., Lansdorp P.M., Wang Z.Q., Jackson S.P. Effects of DNA non-homologous end-joining factors on telomere length and chromosomal stability in mammalian cells. Curr. Biol. 11:2001;1192-1196
    • (2001) Curr. Biol. , vol.11 , pp. 1192-1196
    • D'Adda Di Fagagna, F.1    Hande, M.P.2    Tong, W.M.3    Roth, D.4    Lansdorp, P.M.5    Wang, Z.Q.6    Jackson, S.P.7
  • 60
    • 0034280093 scopus 로고    scopus 로고
    • Mammalian Ku86 protein prevents telomeric fusions independently of the length of TTAGGG repeats and the G-strand overhang
    • Samper E., Goytisolo F.A., Slijepcevic P., van Buul P.P., Blasco M.A. Mammalian Ku86 protein prevents telomeric fusions independently of the length of TTAGGG repeats and the G-strand overhang. EMBO Rep. 1:2000;244-252
    • (2000) EMBO Rep. , vol.1 , pp. 244-252
    • Samper, E.1    Goytisolo, F.A.2    Slijepcevic, P.3    Van Buul, P.P.4    Blasco, M.A.5
  • 63
    • 0035023139 scopus 로고    scopus 로고
    • The absence of the dna-dependent protein kinase catalytic subunit in mice results in anaphase bridges and in increased telomeric fusions with normal telomere length and G-strand overhang
    • Goytisolo F.A., Samper E., Edmonson S., Taccioli G.E., Blasco M.A. The absence of the dna-dependent protein kinase catalytic subunit in mice results in anaphase bridges and in increased telomeric fusions with normal telomere length and G-strand overhang. Mol. Cell Biol. 21:2001;3642-3651
    • (2001) Mol. Cell Biol. , vol.21 , pp. 3642-3651
    • Goytisolo, F.A.1    Samper, E.2    Edmonson, S.3    Taccioli, G.E.4    Blasco, M.A.5
  • 64
  • 66
    • 0029972806 scopus 로고    scopus 로고
    • P53: Puzzle and paradigm
    • Ko L.J., Prives C. p53: puzzle and paradigm. Genes. Dev. 10:1996;1054-1072
    • (1996) Genes. Dev. , vol.10 , pp. 1054-1072
    • Ko, L.J.1    Prives, C.2
  • 69
    • 0026523766 scopus 로고
    • Phosphorylation sites in the amino-terminal region of mouse p53
    • Wang Y., Eckhart W. Phosphorylation sites in the amino-terminal region of mouse p53. Proc. Natl. Acad. Sci. U.S.A. 89:1992;4231-4235
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 4231-4235
    • Wang, Y.1    Eckhart, W.2
  • 70
    • 0026687883 scopus 로고
    • Human DNA-activated protein kinase phosphorylates serines 15 and 37 in the amino-terminal transactivation domain of human p53
    • Lees-Miller S.P., Sakaguchi K., Ullrich S.J., Appella E., Anderson C.W. Human DNA-activated protein kinase phosphorylates serines 15 and 37 in the amino-terminal transactivation domain of human p53. Mol. Cell Biol. 12:1992;5041-5049
    • (1992) Mol. Cell Biol. , vol.12 , pp. 5041-5049
    • Lees-Miller, S.P.1    Sakaguchi, K.2    Ullrich, S.J.3    Appella, E.4    Anderson, C.W.5
  • 71
    • 0029858143 scopus 로고    scopus 로고
    • V(D)J recombination activates a p53-dependent DNA damage checkpoint in scid lymphocyte precursors
    • Guidos C.J., Williams C.J., Grandal I., Knowles G., Huang M.T., Danska J.S. V(D)J recombination activates a p53-dependent DNA damage checkpoint in scid lymphocyte precursors. Genes Dev. 10:1996;2038-2054
    • (1996) Genes Dev. , vol.10 , pp. 2038-2054
    • Guidos, C.J.1    Williams, C.J.2    Grandal, I.3    Knowles, G.4    Huang, M.T.5    Danska, J.S.6
  • 72
    • 0030446964 scopus 로고    scopus 로고
    • P53 induction, cell cycle checkpoints, and apoptosis in DNAPK-deficient scid mice
    • Gurley K.E., Kemp C.J. p53 induction, cell cycle checkpoints, and apoptosis in DNAPK-deficient scid mice. Carcinogenesis. 17:1996;2537-2542
    • (1996) Carcinogenesis , vol.17 , pp. 2537-2542
    • Gurley, K.E.1    Kemp, C.J.2
  • 73
    • 0029941651 scopus 로고    scopus 로고
    • P53-Dependent cell cycle arrests are preserved in DNA-activated protein kinase-deficient mouse fibroblasts
    • Huang L.C., Clarkin K.C., Wahl G.M. p53-Dependent cell cycle arrests are preserved in DNA-activated protein kinase-deficient mouse fibroblasts. Cancer Res. 56:1996;2940-2944
    • (1996) Cancer Res. , vol.56 , pp. 2940-2944
    • Huang, L.C.1    Clarkin, K.C.2    Wahl, G.M.3
  • 74
    • 0031025079 scopus 로고    scopus 로고
    • DNA-dependent protein kinase is not required for accumulation of p53 or cell cycle arrest after DNA damage
    • Rathmell W.K., Kaufmann W.K., Hurt J.C., Byrd L.L., Chu G. DNA-dependent protein kinase is not required for accumulation of p53 or cell cycle arrest after DNA damage. Cancer Res. 57:1997;68-74
    • (1997) Cancer Res. , vol.57 , pp. 68-74
    • Rathmell, W.K.1    Kaufmann, W.K.2    Hurt, J.C.3    Byrd, L.L.4    Chu, G.5
  • 75
    • 0032514485 scopus 로고    scopus 로고
    • DNA-dependent protein kinase acts upstream of p53 in response to DNA damage
    • Woo R.A., McLure K.G., Lees-Miller S.P., Rancourt D.E., Lee P.W. DNA-dependent protein kinase acts upstream of p53 in response to DNA damage. Nature. 394:1998;700-704
    • (1998) Nature , vol.394 , pp. 700-704
    • Woo, R.A.1    McLure, K.G.2    Lees-Miller, S.P.3    Rancourt, D.E.4    Lee, P.W.5
  • 76
    • 0033532174 scopus 로고    scopus 로고
    • The ability of p53 to activate downstream genes p21(WAF1/cip1) and MDM2, and cell cycle arrest following DNA damage is delayed and attenuated in scid cells deficient in the DNA-dependent protein kinase
    • Kachnic L.A., Wu B., Wunsch H., Mekeel K.L., DeFrank J.S., Tang W., Powell S.N. The ability of p53 to activate downstream genes p21(WAF1/cip1) and MDM2, and cell cycle arrest following DNA damage is delayed and attenuated in scid cells deficient in the DNA-dependent protein kinase. J. Biol. Chem. 274:1999;13111-13117
    • (1999) J. Biol. Chem. , vol.274 , pp. 13111-13117
    • Kachnic, L.A.1    Wu, B.2    Wunsch, H.3    Mekeel, K.L.4    Defrank, J.S.5    Tang, W.6    Powell, S.N.7
  • 80
    • 0036270993 scopus 로고    scopus 로고
    • DNA repair/pro-apoptotic dual-role proteins in five major DNA repair pathways: Fail-safe protection against carcinogenesis
    • Bernstein C., Bernstein H., Payne C.M., Garewal H. DNA repair/pro-apoptotic dual-role proteins in five major DNA repair pathways: fail-safe protection against carcinogenesis. Mutat. Res. 511:2002;145-178
    • (2002) Mutat. Res. , vol.511 , pp. 145-178
    • Bernstein, C.1    Bernstein, H.2    Payne, C.M.3    Garewal, H.4
  • 83
    • 0037124322 scopus 로고    scopus 로고
    • DNA damage-induced apoptosis requires the DNA-dependent protein kinase, and is mediated by the latent population of p53
    • Woo R.A., Jack M.T., Xu Y., Burma S., Chen D.J., Lee P.W. DNA damage-induced apoptosis requires the DNA-dependent protein kinase, and is mediated by the latent population of p53. Embo. J. 21:2002;3000-3008
    • (2002) Embo. J. , vol.21 , pp. 3000-3008
    • Woo, R.A.1    Jack, M.T.2    Xu, Y.3    Burma, S.4    Chen, D.J.5    Lee, P.W.6
  • 84
    • 0028131554 scopus 로고
    • Transcriptional activation by p53 correlates with suppression of growth but not transformation
    • Crook T., Marston N.J., Sara E.A., Vousden K.H. Transcriptional activation by p53 correlates with suppression of growth but not transformation. Cell. 79:1994;817-827
    • (1994) Cell , vol.79 , pp. 817-827
    • Crook, T.1    Marston, N.J.2    Sara, E.A.3    Vousden, K.H.4
  • 86
    • 0034025078 scopus 로고    scopus 로고
    • The p53 response to DNA damage in vivo is independent of DNA-dependent protein kinase
    • Jhappan C., Yusufzai T.M., Anderson S., Anver M.R., Merlino G. The p53 response to DNA damage in vivo is independent of DNA-dependent protein kinase. Mol. Cell Biol. 20:2000;4075-4083
    • (2000) Mol. Cell Biol. , vol.20 , pp. 4075-4083
    • Jhappan, C.1    Yusufzai, T.M.2    Anderson, S.3    Anver, M.R.4    Merlino, G.5
  • 88
    • 0031093496 scopus 로고    scopus 로고
    • The DNA-dependent protein kinase catalytic subunit (p460) is cleaved during Fas-mediated apoptosis in Jurkat cells
    • McConnell K.R., Dynan W.S., Hardin J.A. The DNA-dependent protein kinase catalytic subunit (p460) is cleaved during Fas-mediated apoptosis in Jurkat cells. J. Immunol. 158:1997;2083-2089
    • (1997) J. Immunol. , vol.158 , pp. 2083-2089
    • McConnell, K.R.1    Dynan, W.S.2    Hardin, J.A.3
  • 89
    • 0030666222 scopus 로고    scopus 로고
    • Innate immunity: The virtues of a non-clonal system of recognition
    • Medzhitov R., Janeway C.A. Jr. Innate immunity: the virtues of a non-clonal system of recognition. Cell. 91:1997;295-298
    • (1997) Cell , vol.91 , pp. 295-298
    • Medzhitov, R.1    Janeway Jr., C.A.2
  • 90
    • 0031050034 scopus 로고    scopus 로고
    • Innate immunity: Impact on the adaptive immune response
    • Medzhitov R., Janeway C.A. Jr. Innate immunity: impact on the adaptive immune response. Curr. Opin. Immunol. 9:1997;4-9
    • (1997) Curr. Opin. Immunol. , vol.9 , pp. 4-9
    • Medzhitov, R.1    Janeway Jr., C.A.2
  • 91
    • 0029984358 scopus 로고    scopus 로고
    • CpG motifs present in bacteria DNA rapidly induce lymphocytes to secrete interleukin 6, interleukin 12, and interferon gamma
    • Klinman D.M., Yi A.K., Beaucage S.L., Conover J., Krieg A.M. CpG motifs present in bacteria DNA rapidly induce lymphocytes to secrete interleukin 6, interleukin 12, and interferon gamma. Proc. Natl. Acad. Sci. U.S.A. 93:1996;2879-2883
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 2879-2883
    • Klinman, D.M.1    Yi, A.K.2    Beaucage, S.L.3    Conover, J.4    Krieg, A.M.5
  • 92
    • 0032995849 scopus 로고    scopus 로고
    • Bacterial CpG DNA activates immune cells to signal infectious danger
    • Wagner H. Bacterial CpG DNA activates immune cells to signal infectious danger. Adv. Immunol. 73:1999;329-368
    • (1999) Adv. Immunol. , vol.73 , pp. 329-368
    • Wagner, H.1
  • 94
    • 0037099629 scopus 로고    scopus 로고
    • Potential role of phosphatidylinositol 3 kinase, rather than DNA-dependent protein kinase, in CpG DNA-induced immune activation
    • Ishii K.J., Takeshita F., Gursel I., Gursel M., Conover J., Nussenzweig A., Klinman D.M. Potential role of phosphatidylinositol 3 kinase, rather than DNA-dependent protein kinase, in CpG DNA-induced immune activation. J. Exp. Med. 196:2002;269-274
    • (2002) J. Exp. Med. , vol.196 , pp. 269-274
    • Ishii, K.J.1    Takeshita, F.2    Gursel, I.3    Gursel, M.4    Conover, J.5    Nussenzweig, A.6    Klinman, D.M.7
  • 96
    • 0032015647 scopus 로고    scopus 로고
    • Virus infection induces the assembly of coordinately activated transcription factors on the IFN-beta enhancer in vivo
    • Wathelet M.G., Lin C.H., Parekh B.S., Ronco L.V., Howley P.M., Maniatis T. Virus infection induces the assembly of coordinately activated transcription factors on the IFN-beta enhancer in vivo. Mol. Cell. 1:1998;507-518
    • (1998) Mol. Cell , vol.1 , pp. 507-518
    • Wathelet, M.G.1    Lin, C.H.2    Parekh, B.S.3    Ronco, L.V.4    Howley, P.M.5    Maniatis, T.6
  • 97
    • 0032861343 scopus 로고    scopus 로고
    • Megabase chromatin domains involved in DNA double-strand breaks in vivo
    • Rogakou E.P., Boon C., Redon C., Bonner W.M. Megabase chromatin domains involved in DNA double-strand breaks in vivo. J. Cell Biol. 146:1999;905-916
    • (1999) J. Cell Biol. , vol.146 , pp. 905-916
    • Rogakou, E.P.1    Boon, C.2    Redon, C.3    Bonner, W.M.4
  • 98
    • 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. Tumor suppressor p53 binding protein 1 (53BP1) is involved in DNA damage-signaling pathways. J. Cell Biol. 153:2001;613-620
    • (2001) J. Cell Biol. , vol.153 , pp. 613-620
    • Rappold, I.1    Iwabuchi, K.2    Date, T.3    Chen, J.4


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