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Volumn 86, Issue 3, 2013, Pages 440-449

Detection and repair of ionizing radiation-induced dna double strand breaks: New developments in nonhomologous end joining

Author keywords

[No Author keywords available]

Indexed keywords

CHEMOTHERAPY; DNA; IONIZING RADIATION; JOINING; RADIATION SHIELDING; REPAIR;

EID: 84880615973     PISSN: 03603016     EISSN: 1879355X     Source Type: Journal    
DOI: 10.1016/j.ijrobp.2013.01.011     Document Type: Article
Times cited : (119)

References (152)
  • 1
    • 77953229115 scopus 로고    scopus 로고
    • The mechanism of double-strand DNA break repair by the nonhomologous DNA end-joining pathway
    • Lieber MR. 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
  • 2
    • 59849089955 scopus 로고    scopus 로고
    • Repair of ionizing radiationinduced DNA double-strand breaks by non-homologous end-joining
    • Mahaney BL, Meek K, Lees-Miller SP. Repair of ionizing radiationinduced DNA double-strand breaks by non-homologous end-joining. Biochem J 2009;417:639-650.
    • (2009) Biochem J , vol.417 , pp. 639-650
    • Mahaney, B.L.1    Meek, K.2    Lees-Miller, S.P.3
  • 3
    • 0037124373 scopus 로고    scopus 로고
    • Synapsis of DNA ends by DNA-dependent protein kinase
    • DeFazio LG, Stansel RM, Griffith JD, et al. 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
  • 4
    • 0027397867 scopus 로고
    • The DNA-dependent protein kinase: Requirement for DNA ends and association with ku antigen
    • Gottlieb TM, Jackson SP. The DNA-dependent protein kinase: Requirement for DNA ends and association with ku antigen. Cell 1993;72:131-142.
    • (1993) Cell , vol.72 , pp. 131-142
    • Gottlieb, T.M.1    Jackson, S.P.2
  • 5
    • 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 NV, et al. 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
  • 6
    • 33744924482 scopus 로고    scopus 로고
    • Preclinical evaluation of a potent novel DNA-dependent protein kinase inhibitor nu7441
    • Zhao Y, Thomas HD, Batey MA, et al. Preclinical evaluation of a potent novel DNA-dependent protein kinase inhibitor nu7441. Cancer Res 2006;66:5354-5362.
    • (2006) Cancer Res , vol.66 , pp. 5354-5362
    • Zhao, Y.1    Thomas, H.D.2    Batey, M.A.3
  • 7
    • 79955663428 scopus 로고    scopus 로고
    • Tidying up loose ends: The role of polynucleotide kinase/phosphatase in DNA strand break repair
    • Weinfeld M, Mani RS, Abdou I, et al. Tidying up loose ends: The role of polynucleotide kinase/phosphatase in DNA strand break repair. Trends Biochem Sci 2011;36:262-271.
    • (2011) Trends Biochem Sci , vol.36 , pp. 262-271
    • Weinfeld, M.1    Mani, R.S.2    Abdou, I.3
  • 8
    • 80052052892 scopus 로고    scopus 로고
    • Tyrosyl-DNA phosphodiesterase 1 (tdp1) inhibitors
    • Huang SN, Pommier Y, Marchand C. Tyrosyl-DNA phosphodiesterase 1 (tdp1) inhibitors. Expert Opin Ther Pat 2011;21:1285-1292.
    • (2011) Expert Opin Ther Pat , vol.21 , pp. 1285-1292
    • Huang, S.N.1    Pommier, Y.2    Marchand, C.3
  • 9
    • 77749270650 scopus 로고    scopus 로고
    • Yeast tdp1 regulates the fidelity of nonhomologous end joining
    • Bahmed K, Nitiss KC, Nitiss JL. Yeast tdp1 regulates the fidelity of nonhomologous end joining. Proc Natl Acad Sci U S A 2010;107: 4057-4062.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 4057-4062
    • Bahmed, K.1    Nitiss, K.C.2    Nitiss, J.L.3
  • 10
    • 57749110749 scopus 로고    scopus 로고
    • Molecular mechanism of DNA deadenylation by the neurological disease protein aprataxin
    • Rass U, Ahel I, West SC. Molecular mechanism of DNA deadenylation by the neurological disease protein aprataxin. J Biol Chem 2008;283:33994-34001.
    • (2008) J Biol Chem , vol.283 , pp. 33994-34001
    • Rass, U.1    Ahel, I.2    West, S.C.3
  • 11
    • 79951562112 scopus 로고    scopus 로고
    • End-processing during nonhomologous end-joining: A role for exonuclease 1
    • Bahmed K, Seth A, Nitiss KC, et al. End-processing during nonhomologous end-joining: A role for exonuclease 1. Nucleic Acids Res 2011;39:970-978.
    • (2011) Nucleic Acids Res , vol.39 , pp. 970-978
    • Bahmed, K.1    Seth, A.2    Nitiss, K.C.3
  • 12
    • 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 2009;16: 814-818.
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 814-818
    • Xie, A.1    Kwok, A.2    Scully, R.3
  • 13
    • 61749092799 scopus 로고    scopus 로고
    • The ku80 carboxy terminus stimulates joining and artemis-mediated processing of DNA ends
    • Weterings E, Verkaik NS, Keijzers G, et al. The ku80 carboxy terminus stimulates joining and artemis-mediated processing of DNA ends. Mol Cell Biol 2009;29:1134-1142.
    • (2009) Mol Cell Biol , vol.29 , pp. 1134-1142
    • Weterings, E.1    Verkaik, N.S.2    Keijzers, G.3
  • 14
    • 47249106520 scopus 로고    scopus 로고
    • Werner protein cooperates with the xrcc4-DNA ligase iv complex in end-processing
    • Kusumoto R, Dawut L, Marchetti C, et al. Werner protein cooperates with the xrcc4-DNA ligase iv complex in end-processing. Biochemistry 2008;47:7548-7556.
    • (2008) Biochemistry , vol.47 , pp. 7548-7556
    • Kusumoto, R.1    Dawut, L.2    Marchetti, C.3
  • 15
    • 84868679968 scopus 로고    scopus 로고
    • DNA polymerases in nonhomologous end joining: Are there any benefits to standing out from the crowd'
    • Ramsden DA, Asagoshi K. DNA polymerases in nonhomologous end joining: Are there any benefits to standing out from the crowd' Environ Mol Mutagen 2012;53:741-751.
    • (2012) Environ Mol Mutagen , vol.53 , pp. 741-751
    • Ramsden, D.A.1    Asagoshi, K.2
  • 16
    • 84870587195 scopus 로고    scopus 로고
    • The dynamics of ku70/80 and DNA-pkcs at dsbs induced by ionizing radiation is dependent on the complexity of damage
    • Reynolds P, Anderson JA, Harper JV, et al. The dynamics of ku70/80 and DNA-pkcs at dsbs induced by ionizing radiation is dependent on the complexity of damage. Nucleic Acids Res 2012;40: 10821-10831.
    • (2012) Nucleic Acids Res , vol.40 , pp. 10821-10831
    • Reynolds, P.1    Anderson, J.A.2    Harper, J.V.3
  • 17
    • 9744220428 scopus 로고    scopus 로고
    • A pathway of double-strand break rejoining dependent upon atm, artemis, and proteins locating to gamma-h2ax foci
    • Riballo E, Ku'hne M, Rief N, et al. A pathway of double-strand break rejoining dependent upon atm, artemis, and proteins locating to gamma-h2ax foci. Mol Cell 2004;16:715-724.
    • (2004) Mol Cell , vol.16 , pp. 715-724
    • Riballo, E.1    Kuhne, M.2    Rief, N.3
  • 18
    • 84866935347 scopus 로고    scopus 로고
    • The heterochromatic barrier to DNA double strand break repair: How to get the entry visa
    • Goodarzi AA, Jeggo PA. The heterochromatic barrier to DNA double strand break repair: How to get the entry visa. Int J Mol Sci 2012;13: 11844-11860.
    • (2012) Int J Mol Sci , vol.13 , pp. 11844-11860
    • Goodarzi, A.A.1    Jeggo, P.A.2
  • 19
    • 39449112668 scopus 로고    scopus 로고
    • Mechanistic flexibility as a conserved theme across 3 billion years of nonhomologous DNA end-joining
    • Gu J, Lieber MR. Mechanistic flexibility as a conserved theme across 3 billion years of nonhomologous DNA end-joining. Genes Dev 2008;22:411-415.
    • (2008) Genes Dev , vol.22 , pp. 411-415
    • Gu, J.1    Lieber, M.R.2
  • 20
    • 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 WS. 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
  • 21
    • 34247477667 scopus 로고    scopus 로고
    • Autophosphorylation of DNA-pkcs regulates its dynamics at DNA double-strand breaks
    • Uematsu N, Weterings E, Yano K, et al. Autophosphorylation of DNA-pkcs regulates its dynamics at DNA double-strand breaks. J Cell Biol 2007;177:219-229.
    • (2007) J Cell Biol , vol.177 , pp. 219-229
    • Uematsu, N.1    Weterings, E.2    Yano, K.3
  • 22
    • 74049134920 scopus 로고    scopus 로고
    • Ku and DNA-dependent protein kinase dynamic conformations and assembly regulate DNA binding and the initial non-homologous end joining complex
    • Hammel M, Yu Y, Mahaney BL, et al. Ku and DNA-dependent protein kinase dynamic conformations and assembly regulate DNA binding and the initial non-homologous end joining complex. J Biol Chem 2010;285:1414-1423.
    • (2010) J Biol Chem , vol.285 , pp. 1414-1423
    • Hammel, M.1    Yu, Y.2    Mahaney, B.L.3
  • 23
    • 0033198709 scopus 로고    scopus 로고
    • Mapping of protein-protein interactions within the DNA-dependent protein kinase complex
    • Gell D, Jackson SP. 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
  • 24
    • 15844394846 scopus 로고    scopus 로고
    • Conserved modes of recruitment of atm, atr and DNA-PKcs to sites of DNA damage
    • Falck J, Coates J, Jackson SP. Conserved modes of recruitment of atm, atr and DNA-PKcs to sites of DNA damage. Nature 2005;434: 605-611.
    • (2005) Nature , vol.434 , pp. 605-611
    • Falck, J.1    Coates, J.2    Jackson, S.P.3
  • 25
    • 0037102588 scopus 로고    scopus 로고
    • Ku heterodimer binds to both ends of the werner protein and functional interaction occurs at the werner n-terminus
    • Karmakar P, Snowden CM, Ramsden DA, et al. Ku heterodimer binds to both ends of the werner protein and functional interaction occurs at the werner n-terminus. Nucleic Acids Res 2002;30: 3583-3591.
    • (2002) Nucleic Acids Res , vol.30 , pp. 3583-3591
    • Karmakar, P.1    Snowden, C.M.2    Ramsden, D.A.3
  • 26
    • 33845484385 scopus 로고    scopus 로고
    • Dynamic assembly of end-joining complexes requires interaction between ku70/80 and xrcc4
    • Mari PO, Florea BI, Persengiev SP, et al. Dynamic assembly of end-joining complexes requires interaction between ku70/80 and xrcc4. Proc Natl Acad Sci U S A 2006;103:18597-18602.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 18597-18602
    • Mari, P.O.1    Florea, B.I.2    Persengiev, S.P.3
  • 27
    • 34247602569 scopus 로고    scopus 로고
    • Interaction of the ku heterodimer with the DNA ligase iv/xrcc4 complex and its regulation by DNA-PK
    • Costantini S, Woodbine L, Andreoli L, et al. Interaction of the ku heterodimer with the DNA ligase iv/xrcc4 complex and its regulation by DNA-PK. DNA Repair (Amst) 2007;6:712-722.
    • (2007) DNA Repair (Amst) , vol.6 , pp. 712-722
    • Costantini, S.1    Woodbine, L.2    Andreoli, L.3
  • 28
    • 37849018404 scopus 로고    scopus 로고
    • Ku recruits XLF to DNA double-strand breaks
    • Yano K, Morotomi-Yano K, Wang S-Y, et al. Ku recruits XLF to DNA double-strand breaks. EMBO Rep 2008;9:91-96.
    • (2008) EMBO Rep , vol.9 , pp. 91-96
    • Yano, K.1    Morotomi-Yano, K.2    Wang, S.-Y.3
  • 29
    • 79952573454 scopus 로고    scopus 로고
    • Functional significance of the interaction with ku in DNA double-strand break recognition of XLF
    • Yano KI, Morotomi-Yano K, Lee K-J, et al. Functional significance of the interaction with ku in DNA double-strand break recognition of XLF. FEBS Lett 2011;585:841-846.
    • (2011) FEBS Lett , vol.585 , pp. 841-846
    • Yano, K.I.1    Morotomi-Yano, K.2    Lee, K.-J.3
  • 30
    • 84872853376 scopus 로고    scopus 로고
    • APLF promotes the assembly and activity of non-homologous end joining protein complexes
    • Grundy GJ, Rulten SL, Zeng Z, et al. APLF promotes the assembly and activity of non-homologous end joining protein complexes. EMBO J 2013;32:112-125.
    • (2013) EMBO J , vol.32 , pp. 112-125
    • Grundy, G.J.1    Rulten, S.L.2    Zeng, Z.3
  • 31
    • 77951621112 scopus 로고    scopus 로고
    • Ku is a 5'-drp/ap lyase that excises nucleotide damage near broken ends
    • Roberts SA, Strande N, Burkhalter MD, et al. Ku is a 5'-drp/ap lyase that excises nucleotide damage near broken ends. Nature 2010;464: 1214-1217.
    • (2010) Nature , vol.464 , pp. 1214-1217
    • Roberts, S.A.1    Strande, N.2    Burkhalter, M.D.3
  • 32
    • 84860010935 scopus 로고    scopus 로고
    • Specificity of the drp/ap lyase of ku promotes nonhomologous end joining (nhej) fidelity at damaged ends
    • Strande N, Roberts SA, Oh S, et al. Specificity of the drp/ap lyase of ku promotes nonhomologous end joining (nhej) fidelity at damaged ends. J Biol Chem 2012;287:13686-13693.
    • (2012) J Biol Chem , vol.287 , pp. 13686-13693
    • Strande, N.1    Roberts, S.A.2    Oh, S.3
  • 33
    • 40049096125 scopus 로고    scopus 로고
    • Cryo-EM structure of the DNAdependent protein kinase catalytic subunit at subnanometer resolution reveals alpha helices and insight into DNA binding
    • Williams DR, Lee KJ, Shi J, et al. Cryo-EM structure of the DNAdependent protein kinase catalytic subunit at subnanometer resolution reveals alpha helices and insight into DNA binding. Structure 2008;16:468-477.
    • (2008) Structure , vol.16 , pp. 468-477
    • Williams, D.R.1    Lee, K.J.2    Shi, J.3
  • 34
    • 0032509097 scopus 로고    scopus 로고
    • Cryo-em imaging of the catalytic subunit of the DNA-dependent protein kinase
    • Chiu CY, Cary RB, Chen DJ, et al. Cryo-em imaging of the catalytic subunit of the DNA-dependent protein kinase. J Mol Biol 1998;284: 1075-1081.
    • (1998) J Mol Biol , vol.284 , pp. 1075-1081
    • Chiu, C.Y.1    Cary, R.B.2    Chen, D.J.3
  • 35
    • 0242576857 scopus 로고    scopus 로고
    • Visualization of DNA-induced conformational changes in the DNA repair kinase DNA-pkcs
    • Boskovic J, Rivera-Calzada A, Maman JD, et al. Visualization of DNA-induced conformational changes in the DNA repair kinase DNA-pkcs. EMBO J 2003;22:5875-5882.
    • (2003) EMBO J , vol.22 , pp. 5875-5882
    • Boskovic, J.1    Rivera-Calzada, A.2    Maman, J.D.3
  • 36
    • 73849140503 scopus 로고    scopus 로고
    • Crystal structure of DNApkcs reveals a large open-ring cradle comprised of heat repeats
    • Sibanda BL, Chirgadze DY, Blundell TL. Crystal structure of DNApkcs 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
  • 37
    • 78649446475 scopus 로고    scopus 로고
    • A structural model for regulation of NHEJ by DNA-pkcs autophosphorylation
    • Dobbs TA, Tainer JA, Lees-Miller SP. 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
  • 38
    • 70350324640 scopus 로고    scopus 로고
    • Emerging common themes in regulation of PIKKs and PI3Ks
    • Lempiainen H, Halazonetis TD. 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
  • 39
    • 33847193121 scopus 로고    scopus 로고
    • XRCC4:DNA ligase IV can ligate incompatible DNA ends and can ligate across gaps
    • Gu J, Lu H, Tippin B, et al. XRCC4:DNA ligase IV can ligate incompatible DNA ends and can ligate across gaps. EMBO J 2007; 26:1010-1023.
    • (2007) EMBO J , vol.26 , pp. 1010-1023
    • Gu, J.1    Lu, H.2    Tippin, B.3
  • 40
    • 34249685474 scopus 로고    scopus 로고
    • Length-dependent binding of human XLF to DNA and stimulation of XRCC4.DNA ligase IV activity
    • Lu H, Pannicke U, Schwarz K, et al. Length-dependent binding of human XLF to DNA and stimulation of XRCC4.DNA ligase IV activity. J Biol Chem 2007;282:11155-11162.
    • (2007) J Biol Chem , vol.282 , pp. 11155-11162
    • Lu, H.1    Pannicke, U.2    Schwarz, K.3
  • 41
    • 34249938518 scopus 로고    scopus 로고
    • Cernunnos/XLF promotes the ligation of mismatched and noncohesive DNA ends
    • Tsai CJ, Kim SA, 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
  • 42
    • 59649122967 scopus 로고    scopus 로고
    • XLF-cernunnos promotes DNA ligase IV-XRCC4 re-adenylation following ligation
    • Riballo E, Woodbine L, Stiff T, et al. XLF-cernunnos promotes DNA ligase IV-XRCC4 re-adenylation following ligation. Nucleic Acids Res 2009;37:482-492.
    • (2009) Nucleic Acids Res , vol.37 , pp. 482-492
    • Riballo, E.1    Woodbine, L.2    Stiff, T.3
  • 43
    • 84863531762 scopus 로고    scopus 로고
    • Structural insights into the role of domain flexibility in human DNA ligase IV
    • Ochi T, Wu Q, Chirgadze DY, et al. Structural insights into the role of domain flexibility in human DNA ligase IV. Structure 2012;20: 1212-1222.
    • (2012) Structure , vol.20 , pp. 1212-1222
    • Ochi, T.1    Wu, Q.2    Chirgadze, D.Y.3
  • 44
    • 80052738767 scopus 로고    scopus 로고
    • XRCC4 interactions with XRCC4-like factor (XLF) create an extended grooved scaffold for DNA ligation and double-strand break repair
    • Hammel M, Rey M, Yu Y, et al. XRCC4 interactions with XRCC4-like factor (XLF) create an extended grooved scaffold for DNA ligation and double-strand break repair. J Biol Chem 2011;286:32638-32650.
    • (2011) J Biol Chem , vol.286 , pp. 32638-32650
    • Hammel, M.1    Rey, M.2    Yu, Y.3
  • 45
    • 79961219743 scopus 로고    scopus 로고
    • Structural characterization of filaments formed by human XRCC4-cernunnos/XLF complex involved in nonhomologous DNA end-joining
    • Ropars V, Drevet P, Legrand P, et al. Structural characterization of filaments formed by human XRCC4-cernunnos/XLF complex involved in nonhomologous DNA end-joining. Proc Natl Acad Sci U S A 2011;108:12663-12668.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 12663-12668
    • Ropars, V.1    Drevet, P.2    Legrand, P.3
  • 46
    • 80053358977 scopus 로고    scopus 로고
    • Non-homologous endjoining partners in a helical dance: Structural studies of XLFXRCC4 interactions
    • 1382 p following 1392
    • Wu Q, Ochi T, Matak-Vinkovic D, et al. Non-homologous endjoining partners in a helical dance: Structural studies of XLFXRCC4 interactions. Biochem Soc Trans 2011;39:1387-1392. suppl 1382 p following 1392.
    • (2011) Biochem Soc Trans , vol.39 , Issue.SUPPL. , pp. 1387-1392
    • Wu, Q.1    Ochi, T.2    Matak-Vinkovic, D.3
  • 48
    • 84874878472 scopus 로고    scopus 로고
    • XRCC4 and XLF form long helical protein filaments suitable for DNA end protection and alignment to facilitate DNA double strand break repair
    • Published on the web 5 February 2013, 10.1139/ bcb-2012-0058
    • Mahaney BL, Hammel M, Meek K, et al. XRCC4 and XLF form long helical protein filaments suitable for DNA end protection and alignment to facilitate DNA double strand break repair. Biochemistry and Cell Biology, Published on the web 5 February 2013, 10.1139/ bcb-2012-0058
    • Biochemistry and Cell Biology
    • Mahaney, B.L.1    Hammel, M.2    Meek, K.3
  • 49
    • 84863798398 scopus 로고    scopus 로고
    • Artemis C-terminal region facilitates V(D)J recombination through its interactions with DNA ligase IV and DNA-PKCS
    • Malu S, De Ioannes P, Kozlov M, et al. Artemis C-terminal region facilitates V(D)J recombination through its interactions with DNA ligase IV and DNA-PKCS. J Exp Med 2012;209:955-963.
    • (2012) J Exp Med , vol.209 , pp. 955-963
    • Malu, S.1    De Ioannes, P.2    Kozlov, M.3
  • 50
    • 84871686867 scopus 로고    scopus 로고
    • Structural basis of DNA ligase IV-Artemis interaction in nonhomologous end-joining
    • De Ioannes P, Malu S, Cortes P, et al. Structural basis of DNA ligase IV-Artemis interaction in nonhomologous end-joining. Cell Rep 2012;2:1505-1512.
    • (2012) Cell Rep , vol.2 , pp. 1505-1512
    • De Ioannes, P.1    Malu, S.2    Cortes, P.3
  • 51
    • 0035191378 scopus 로고    scopus 로고
    • Crystal structure of an XRCC4-DNA ligase IV complex
    • Sibanda BL, Critchlow SE, Begun J, et al. Crystal structure of an XRCC4-DNA ligase IV complex. Nat Struct Biol 2001;8:1015-1019.
    • (2001) Nat Struct Biol , vol.8 , pp. 1015-1019
    • Sibanda, B.L.1    Critchlow, S.E.2    Begun, J.3
  • 52
    • 66349086714 scopus 로고    scopus 로고
    • Structural and functional interaction between the human DNA repair proteins DNA ligase IV and XRCC4
    • Wu PY, Frit P, Meesala S, et al. Structural and functional interaction between the human DNA repair proteins DNA ligase IV and XRCC4. Mol Cell Biol 2009;29:3163-3172.
    • (2009) Mol Cell Biol , vol.29 , pp. 3163-3172
    • Wu, P.Y.1    Frit, P.2    Meesala, S.3
  • 53
    • 78149459696 scopus 로고    scopus 로고
    • XLF regulates filament architecture of the XRCC4 ligase IV complex
    • Hammel M, Yu Y, Fang S, et al. XLF regulates filament architecture of the XRCC4 ligase IV complex. Structure 2010;18:1431-1442.
    • (2010) Structure , vol.18 , pp. 1431-1442
    • Hammel, M.1    Yu, Y.2    Fang, S.3
  • 54
    • 70450224460 scopus 로고    scopus 로고
    • Electron microscopy of XRCC4 and the DNA ligase IV-XRCC4 DNA repair complex
    • Recuero-Checa MA, DoréS, Arias Palomo E, et al. Electron microscopy of XRCC4 and the DNA ligase IV-XRCC4 DNA repair complex. DNA Repair (Amst) 2009;8:1380-1389.
    • (2009) DNA Repair (Amst) , vol.8 , pp. 1380-1389
    • Recuero-Checa, M.A.1    És, D.2    Arias Palomo, E.3
  • 55
    • 0035833552 scopus 로고    scopus 로고
    • Structure of the ku heterodimer bound to DNA and its implications for double-strand break repair
    • Walker JR, Corpina RA, 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
  • 56
    • 49749093073 scopus 로고    scopus 로고
    • Ku80 removal from DNA through double strand break-induced ubiquitylation
    • Postow L, Ghenoiu C, Woo EM, et al. Ku80 removal from DNA through double strand break-induced ubiquitylation. J Cell Biol 2008;182:467-479.
    • (2008) J Cell Biol , vol.182 , pp. 467-479
    • Postow, L.1    Ghenoiu, C.2    Woo, E.M.3
  • 57
    • 80052765854 scopus 로고    scopus 로고
    • Destroying the ring: Freeing DNA from ku with ubiquitin
    • Postow L. Destroying the ring: Freeing DNA from ku with ubiquitin. FEBS Lett 2011;585:2876-2882.
    • (2011) FEBS Lett , vol.585 , pp. 2876-2882
    • Postow, L.1
  • 58
    • 84862777619 scopus 로고    scopus 로고
    • The E3 ligase RNF8 regulates KU80 removal and NHEJ repair
    • Feng L, Chen J. The E3 ligase RNF8 regulates KU80 removal and NHEJ repair. Nat Struct Mol Biol 2012;19:201-206.
    • (2012) Nat Struct Mol Biol , vol.19 , pp. 201-206
    • Feng, L.1    Chen, J.2
  • 59
    • 80052566950 scopus 로고    scopus 로고
    • PARP regulates nonhomologous end joining through retention of Ku at double-strand breaks
    • Couto CA, Wang HY, Green JC, et al. PARP regulates nonhomologous end joining through retention of Ku at double-strand breaks. J Cell Biol 2011;194:367-375.
    • (2011) J Cell Biol , vol.194 , pp. 367-375
    • Couto, C.A.1    Wang, H.Y.2    Green, J.C.3
  • 60
    • 80053447704 scopus 로고    scopus 로고
    • Release of Ku and MRN from DNA ends by Mre11 nuclease activity and Ctp1 is required for homologous recombination repair of double-strand breaks
    • Langerak P, Mejia-Ramirez E, Limbo O, et al. Release of Ku and MRN from DNA ends by Mre11 nuclease activity and Ctp1 is required for homologous recombination repair of double-strand breaks. PLoS Genet 2011;7:e1002271.
    • (2011) PLoS Genet , vol.7
    • Langerak, P.1    Mejia-Ramirez, E.2    Limbo, O.3
  • 61
    • 2242484657 scopus 로고    scopus 로고
    • Identification of in vitro and in vivo phosphorylation sites in the catalytic subunit of the DNAdependent protein kinase
    • Douglas P, Sapkota GP, Morrice N, et al. Identification of in vitro and in vivo phosphorylation sites in the catalytic subunit of the DNAdependent protein kinase. Biochem J 2002;368:243-251.
    • (2002) Biochem J , vol.368 , pp. 243-251
    • Douglas, P.1    Sapkota, G.P.2    Morrice, N.3
  • 62
    • 79956220705 scopus 로고    scopus 로고
    • Choosing the right path: Does DNA-PK help make the decision'
    • Neal JA, Meek K. Choosing the right path: Does DNA-PK help make the decision' Mutat Res 2011;711:73-86.
    • (2011) Mutat Res , vol.711 , pp. 73-86
    • Neal, J.A.1    Meek, K.2
  • 63
    • 0030009738 scopus 로고    scopus 로고
    • The DNA-dependent protein kinase is inactivated by autophosphorylation of the catalytic subunit
    • Chan DW, Lees-Miller SP. 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
  • 64
    • 57949116437 scopus 로고    scopus 로고
    • DNA-PK: The means to justify the ends'
    • Meek K, Dang V, Lees-Miller SP. DNA-PK: The means to justify the ends' Adv Immunol 2008;99:33-58.
    • (2008) Adv Immunol , vol.99 , pp. 33-58
    • Meek, K.1    Dang, V.2    Lees-Miller, S.P.3
  • 65
    • 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 YVR, Wang W, et al. 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    Yvr, R.2    Wang, W.3
  • 66
    • 79955519714 scopus 로고    scopus 로고
    • Congenital bone marrow failure in DNA-PKcs mutant mice associated with deficiencies in DNA repair
    • Zhang S, Yajima H, Huynh H, et al. Congenital bone marrow failure in DNA-PKcs mutant mice associated with deficiencies in DNA repair. J Cell Biol 2011;193:295-305.
    • (2011) J Cell Biol , vol.193 , pp. 295-305
    • Zhang, S.1    Yajima, H.2    Huynh, H.3
  • 67
    • 79953134635 scopus 로고    scopus 로고
    • Inhibition of homologous recombination by DNA-dependent protein kinase requires kinase activity, is titratable, and is modulated by autophosphorylation
    • Neal JA, Dang V, Douglas P, et al. Inhibition of homologous recombination by DNA-dependent protein kinase requires kinase activity, is titratable, and is modulated by autophosphorylation. Mol Cell Biol 2011;31:1719-1733.
    • (2011) Mol Cell Biol , vol.31 , pp. 1719-1733
    • Neal, J.A.1    Dang, V.2    Douglas, P.3
  • 68
    • 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 WD, et al. 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
  • 69
    • 0035374588 scopus 로고    scopus 로고
    • Protein phosphatases regulate DNA-dependent protein kinase activity
    • Douglas P, Moorhead GB, Ye R, et al. Protein phosphatases regulate DNA-dependent protein kinase activity. J Biol Chem 2001;276: 18992-18998.
    • (2001) J Biol Chem , vol.276 , pp. 18992-18998
    • Douglas, P.1    Moorhead, G.B.2    Ye, R.3
  • 70
    • 0842320995 scopus 로고    scopus 로고
    • DNA-PKcs function regulated specifically by protein phosphatase 5
    • Wechsler T, Chen BPC, Harper R, et al. DNA-PKcs function regulated specifically by protein phosphatase 5. Proc Natl Acad Sci U S A 2004;101:1247-1252.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 1247-1252
    • Wechsler, T.1    Bpc, C.2    Harper, R.3
  • 71
    • 77749334700 scopus 로고    scopus 로고
    • Protein phosphatase 6 interacts with the DNA-dependent protein kinase catalytic subunit and dephosphorylates gamma-h2ax
    • Douglas P, Zhong J, Ye R, et al. Protein phosphatase 6 interacts with the DNA-dependent protein kinase catalytic subunit and dephosphorylates gamma-h2ax. Mol Cell Biol 2010;30:1368-1381.
    • (2010) Mol Cell Biol , vol.30 , pp. 1368-1381
    • Douglas, P.1    Zhong, J.2    Ye, R.3
  • 72
    • 84887212592 scopus 로고    scopus 로고
    • Activation of DNA-PK by ionizing radiation is mediated by protein phosphatase 6
    • Mi J, Dziegielewski J, Bolesta E, et al. Activation of DNA-PK by ionizing radiation is mediated by protein phosphatase 6. PLoS One 2009;4:e4395.
    • (2009) PLoS One , vol.4
    • Mi, J.1    Dziegielewski, J.2    Bolesta, E.3
  • 73
    • 56849086731 scopus 로고    scopus 로고
    • Displacement affinity chromatography of protein phosphatase one (PP1) complexes
    • Moorhead GBG, Trinkle-Mulcahy L, Nimick M, et al. Displacement affinity chromatography of protein phosphatase one (PP1) complexes. BMC Biochem 2008;9:28.
    • (2008) BMC Biochem , vol.9 , pp. 28
    • Gbg, M.1    Trinkle-Mulcahy, L.2    Nimick, M.3
  • 74
    • 77953547290 scopus 로고    scopus 로고
    • Choreographing the DNA damage response: PP6 joins the dance
    • Douglas P, Moorhead G, Xu X, et al. Choreographing the DNA damage response: PP6 joins the dance. Cell Cycle 2010;9: 1221-1222.
    • (2010) Cell Cycle , vol.9 , pp. 1221-1222
    • Douglas, P.1    Moorhead, G.2    Xu, X.3
  • 75
    • 70149108072 scopus 로고    scopus 로고
    • A nonhomologous end-joining pathway is required for protein phosphatase 2A promotion of DNA double-strand break repair
    • Wang Q, Gao F, Wang T, et al. A nonhomologous end-joining pathway is required for protein phosphatase 2A promotion of DNA double-strand break repair. Neoplasia 2009;11:1012-1021.
    • (2009) Neoplasia , vol.11 , pp. 1012-1021
    • Wang, Q.1    Gao, F.2    Wang, T.3
  • 76
    • 84861185981 scopus 로고    scopus 로고
    • Phosphoproteomic analysis reveals that PP4 dephosphorylates KAP-1 impacting the DNA damage response
    • Lee DH, Goodarzi AA, Adelman GO, et al. Phosphoproteomic analysis reveals that PP4 dephosphorylates KAP-1 impacting the DNA damage response. EMBO J 2012;31:2403-2415.
    • (2012) EMBO J , vol.31 , pp. 2403-2415
    • Lee, D.H.1    Goodarzi, A.A.2    Adelman, G.O.3
  • 77
    • 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, et al. 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
  • 78
    • 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 BL, Yano K, et al. 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
  • 79
    • 0242268028 scopus 로고    scopus 로고
    • DNA-PK phosphorylation sites in XRCC4 are not required for survival after radiation or for V(D)J recombination
    • Yu Y, Wang W, Ding Q, et al. DNA-PK phosphorylation sites in XRCC4 are not required for survival after radiation or for V(D)J recombination. DNA Repair (Amst) 2003;2:1239-1252.
    • (2003) DNA Repair (Amst) , vol.2 , pp. 1239-1252
    • Yu, Y.1    Wang, W.2    Ding, Q.3
  • 80
    • 77956210664 scopus 로고    scopus 로고
    • Delineation of the XRCC4- interacting region in the globular head domain of Cernunnos/XLF
    • Malivert L, Ropars V, Nunez M, et al. Delineation of the XRCC4- interacting region in the globular head domain of Cernunnos/XLF. J Biol Chem 2010;285:26475-26483.
    • (2010) J Biol Chem , vol.285 , pp. 26475-26483
    • Malivert, L.1    Ropars, V.2    Nunez, M.3
  • 81
    • 0032544413 scopus 로고    scopus 로고
    • Requirement for an interaction of XRCC4 with DNA ligase IV for wild-type V(D)J recombination and DNA double-strand break repair in vivo
    • Grawunder U, Zimmer D, Kulesza P, et al. Requirement for an interaction of XRCC4 with DNA ligase IV for wild-type V(D)J recombination and DNA double-strand break repair in vivo. J Biol Chem 1998;273:24708-24714.
    • (1998) J Biol Chem , vol.273 , pp. 24708-24714
    • Grawunder, U.1    Zimmer, D.2    Kulesza, P.3
  • 82
    • 84863230094 scopus 로고    scopus 로고
    • XRCC4's interaction with XLF is required for coding (but not signal) end joining
    • Roy S, Andres SN, Vergnes A, et al. XRCC4's interaction with XLF is required for coding (but not signal) end joining. Nucleic Acids Res 2012;40:1684-1694.
    • (2012) Nucleic Acids Res , vol.40 , pp. 1684-1694
    • Roy, S.1    Andres, S.N.2    Vergnes, A.3
  • 83
    • 82255181570 scopus 로고    scopus 로고
    • Phosphorylation of polynucleotide kinase/ phosphatase by DNA-dependent protein kinase and ataxiatelangiectasia mutated regulates its association with sites of DNA damage
    • Zolner AE, Abdou I, Ye R, et al. Phosphorylation of polynucleotide kinase/ phosphatase by DNA-dependent protein kinase and ataxiatelangiectasia mutated regulates its association with sites of DNA damage. Nucleic Acids Res 2011;39:9224-9237.
    • (2011) Nucleic Acids Res , vol.39 , pp. 9224-9237
    • Zolner, A.E.1    Abdou, I.2    Ye, R.3
  • 84
    • 79960013303 scopus 로고    scopus 로고
    • ATM-mediated phosphorylation of polynucleotide kinase/phosphatase is required for effective DNA double-strand break repair
    • Segal-Raz H, Mass G, Baranes-Bachar K, et al. ATM-mediated phosphorylation of polynucleotide kinase/phosphatase is required for effective DNA double-strand break repair. EMBO Rep 2011;12: 713-719.
    • (2011) EMBO Rep , vol.12 , pp. 713-719
    • Segal-Raz, H.1    Mass, G.2    Baranes-Bachar, K.3
  • 85
    • 20144370280 scopus 로고    scopus 로고
    • Ataxia-telangiectasia-mutated dependent phosphorylation of Artemis in response to DNA damage
    • Chen L, Morio T, Minegishi Y, et al. Ataxia-telangiectasia-mutated dependent phosphorylation of Artemis in response to DNA damage. Cancer Sci 2005;96:134-141.
    • (2005) Cancer Sci , vol.96 , pp. 134-141
    • Chen, L.1    Morio, T.2    Minegishi, Y.3
  • 86
    • 9244239168 scopus 로고    scopus 로고
    • Phosphorylation of Artemis following irradiation-induced DNA damage
    • Poinsignon C, de Chasseval R, Soubeyrand S, et al. Phosphorylation of Artemis following irradiation-induced DNA damage. Eur J Immunol 2004;34:3146-3155.
    • (2004) Eur J Immunol , vol.34 , pp. 3146-3155
    • Poinsignon, C.1    De Chasseval, R.2    Soubeyrand, S.3
  • 87
    • 34247507469 scopus 로고    scopus 로고
    • Ataxia telangiectasia mutated (ATM) is essential for DNA-PKcs phosphorylations at the thr-2609 cluster upon DNA double strand break
    • Chen BP, Uematsu N, Kobayashi J, et al. Ataxia telangiectasia mutated (ATM) is essential for DNA-PKcs phosphorylations at the thr-2609 cluster upon DNA double strand break. J Biol Chem 2007; 282:6582-6587.
    • (2007) J Biol Chem , vol.282 , pp. 6582-6587
    • Chen, B.P.1    Uematsu, N.2    Kobayashi, J.3
  • 88
    • 70350763838 scopus 로고    scopus 로고
    • ATM and Artemis promote homologous recombination of radiation-induced DNA double-strand breaks in G2
    • Beucher A, Birraux J, Tchouandong L, et al. ATM and Artemis promote homologous recombination of radiation-induced DNA double-strand breaks in G2. Embo J 2009;28:3413-3427.
    • (2009) Embo J , vol.28 , pp. 3413-3427
    • Beucher, A.1    Birraux, J.2    Tchouandong, L.3
  • 89
    • 78649938817 scopus 로고    scopus 로고
    • ATM-dependent and -independent dynamics of the nuclear phosphoproteome after DNA damage
    • Bensimon A, Schmidt A, Ziv Y, et al. ATM-dependent and -independent dynamics of the nuclear phosphoproteome after DNA damage. Sci Signal 2010;3:rs3.
    • (2010) Sci Signal , vol.3
    • Bensimon, A.1    Schmidt, A.2    Ziv, Y.3
  • 90
    • 77953148666 scopus 로고    scopus 로고
    • Site-specific phosphorylation dynamics of the nuclear proteome during the DNA damage response
    • Bennetzen MV, Larsen DH, Bunkenborg J, et al. Site-specific phosphorylation dynamics of the nuclear proteome during the DNA damage response. Mol Cell Proteomics 2010;9:1314-1323.
    • (2010) Mol Cell Proteomics , vol.9 , pp. 1314-1323
    • Bennetzen, M.V.1    Larsen, D.H.2    Bunkenborg, J.3
  • 91
    • 38049184488 scopus 로고    scopus 로고
    • Profiling of UV-induced ATM/ATR signaling pathways
    • Stokes MP, Rush J, Macneil J, et al. Profiling of UV-induced ATM/ATR signaling pathways. Proc Natl Acad Sci U S A 2007; 104:19855-19860.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 19855-19860
    • Stokes, M.P.1    Rush, J.2    Macneil, J.3
  • 92
    • 34249947699 scopus 로고    scopus 로고
    • ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage
    • Matsuoka S, Ballif BA, Smogorzewska A, et al. ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Science 2007;316:1160-1166.
    • (2007) Science , vol.316 , pp. 1160-1166
    • Matsuoka, S.1    Ballif, B.A.2    Smogorzewska, A.3
  • 93
    • 65549111779 scopus 로고    scopus 로고
    • Essential role for DNA-PKcs in DNA double-strand break repair and apoptosis in atm-deficient lymphocytes
    • Callén E, Jankovic M, Wong N, et al. Essential role for DNA-PKcs in DNA double-strand break repair and apoptosis in atm-deficient lymphocytes. Molecular Cell 2009;34:285-297.
    • (2009) Molecular Cell , vol.34 , pp. 285-297
    • Callén, E.1    Jankovic, M.2    Wong, N.3
  • 94
    • 1942538492 scopus 로고    scopus 로고
    • ATM and DNA-PK function redundantly to phosphorylate H2AX after exposure to ionizing radiation
    • Stiff T, O'Driscoll M, rief N, et al. ATM and DNA-PK function redundantly to phosphorylate H2AX after exposure to ionizing radiation. Cancer Res 2004;64:2390-2396.
    • (2004) Cancer Res , vol.64 , pp. 2390-2396
    • Stiff, T.1    Odriscoll, M.2    Rief, N.3
  • 95
    • 80053620911 scopus 로고    scopus 로고
    • Essential role for DNAPK- mediated phosphorylation of NR4A nuclear orphan receptors in DNA double-strand break repair
    • Malewicz M, Kadkhodaei B, Kee N, et al. Essential role for DNAPK- mediated phosphorylation of NR4A nuclear orphan receptors in DNA double-strand break repair. Genes Dev 2011;25:2031-2040.
    • (2011) Genes Dev , vol.25 , pp. 2031-2040
    • Malewicz, M.1    Kadkhodaei, B.2    Kee, N.3
  • 96
    • 84863371816 scopus 로고    scopus 로고
    • Heat shock protein 90alpha (Hsp90alpha) is phosphorylated in response to DNA damage and accumulates in repair foci
    • Quanz M, Herbette A, Sayarath M, et al. Heat shock protein 90alpha (Hsp90alpha) is phosphorylated in response to DNA damage and accumulates in repair foci. J Biol Chem 2012;287:8803-8815.
    • (2012) J Biol Chem , vol.287 , pp. 8803-8815
    • Quanz, M.1    Herbette, A.2    Sayarath, M.3
  • 97
    • 84864692966 scopus 로고    scopus 로고
    • Heat shock protein 90a (HSP90a), a substrate and chaperone of DNA-PK necessary for the apoptotic response
    • Solier S, Kohn KW, Scroggins B, et al. Heat shock protein 90a (HSP90a), a substrate and chaperone of DNA-PK necessary for the apoptotic response. Proc Natl Acad Sci U S A 2012;109:12866-12872.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 12866-12872
    • Solier, S.1    Kohn, K.W.2    Scroggins, B.3
  • 98
    • 70449840425 scopus 로고    scopus 로고
    • Cell nonhomologous end joining capacity controls SAF-A phosphorylation by DNA-PK in response to DNA double-strand breaks inducers
    • Britton S, Froment C, Frit P, et al. Cell nonhomologous end joining capacity controls SAF-A phosphorylation by DNA-PK in response to DNA double-strand breaks inducers. Cell Cycle 2009;8:3717-3722.
    • (2009) Cell Cycle , vol.8 , pp. 3717-3722
    • Britton, S.1    Froment, C.2    Frit, P.3
  • 99
    • 61849155778 scopus 로고    scopus 로고
    • HnRNP-U is a specific DNA-dependent protein kinase substrate phosphorylated in response to DNA double-strand breaks
    • Berglund FM, Clarke PR. hnRNP-U is a specific DNA-dependent protein kinase substrate phosphorylated in response to DNA double-strand breaks. Biochem Biophys Res Commun 2009;381: 59-64.
    • (2009) Biochem Biophys Res Commun , vol.381 , pp. 59-64
    • Berglund, F.M.1    Clarke, P.R.2
  • 100
    • 34247245102 scopus 로고    scopus 로고
    • A novel human AP endonuclease with conserved zinc-finger-like motifs involved in DNA strand break responses
    • Kanno S, Kuzuoaka H, Sasao S, et al. A novel human AP endonuclease with conserved zinc-finger-like motifs involved in DNA strand break responses. EMBO J 2007;26:2094-2103.
    • (2007) EMBO J , vol.26 , pp. 2094-2103
    • Kanno, S.1    Kuzuoaka, H.2    Sasao, S.3
  • 101
    • 37549023517 scopus 로고    scopus 로고
    • APLF (C2orf13) facilitates nonhomologous end-joining and undergoes ATM-dependent hyperphosphorylation following ionizing radiation
    • Macrae CJ, McCulloch RD, Ylanko J, et al. APLF (C2orf13) facilitates nonhomologous end-joining and undergoes ATM-dependent hyperphosphorylation following ionizing radiation. DNA Repair (Amst) 2008;7:292-302.
    • (2008) DNA Repair (Amst) , vol.7 , pp. 292-302
    • Macrae, C.J.1    McCulloch, R.D.2    Ylanko, J.3
  • 102
    • 78650756134 scopus 로고    scopus 로고
    • PARP-3 and APLF function together to accelerate nonhomologous end-joining
    • Rulten SL, Fisher A, Robert I, et al. PARP-3 and APLF function together to accelerate nonhomologous end-joining. Mol Cell 2011; 41:33-45.
    • (2011) Mol Cell , vol.41 , pp. 33-45
    • Rulten, S.L.1    Fisher, A.2    Robert, I.3
  • 103
    • 47049104588 scopus 로고    scopus 로고
    • APLF (C2orf13) is a novel component of poly(ADP-Ribose) signaling in mammalian cells
    • Rulten SL, Cortes-Ledesma F, Guo L, et al. APLF (C2orf13) is a novel component of poly(ADP-Ribose) signaling in mammalian cells. Mol Cell Biol 2008;28:4620-4628.
    • (2008) Mol Cell Biol , vol.28 , pp. 4620-4628
    • Rulten, S.L.1    Cortes-Ledesma, F.2    Guo, L.3
  • 104
    • 78650745979 scopus 로고    scopus 로고
    • DNA repair factor APLF is a histone chaperone
    • Mehrotra PV, Ahel D, Ryan DP, et al. DNA repair factor APLF is a histone chaperone. Mol Cell 2011;41:46-55.
    • (2011) Mol Cell , vol.41 , pp. 46-55
    • Mehrotra, P.V.1    Ahel, D.2    Ryan, D.P.3
  • 105
    • 79956223052 scopus 로고    scopus 로고
    • Biochemical characterization of metnase's endonuclease activity and its role in NHEJ repair
    • Beck BD, Lee S, Williamson E, et al. Biochemical characterization of metnase's endonuclease activity and its role in NHEJ repair. Biochemistry 2011;50:4360-4370.
    • (2011) Biochemistry , vol.50 , pp. 4360-4370
    • Beck, B.D.1    Lee, S.2    Williamson, E.3
  • 106
    • 79952256559 scopus 로고    scopus 로고
    • Methylation of histone H3 lysine 36 enhances DNA repair by nonhomologous end-joining
    • Fnu S, Williamson EA, De Haro LP, et al. Methylation of histone H3 lysine 36 enhances DNA repair by nonhomologous end-joining. Proc Natl Acad Sci U S A 2011;108:540-545.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 540-545
    • Fnu, S.1    Williamson, E.A.2    De Haro, L.P.3
  • 107
    • 77956341931 scopus 로고    scopus 로고
    • Human HDAC1 and HDAC 2 function in the DNA-damage response to promote DNA nonhomologous end-joining
    • Miller KM, Tjeertes JV, Coates J, et al. Human HDAC1 and HDAC 2 function in the DNA-damage response to promote DNA nonhomologous end-joining. Nat Struct Mol Biol 2010;17:1144-1151.
    • (2010) Nat Struct Mol Biol , vol.17 , pp. 1144-1151
    • Miller, K.M.1    Tjeertes, J.V.2    Coates, J.3
  • 108
    • 36249031962 scopus 로고    scopus 로고
    • RNF8 transduces the DNAdamage signal via histone ubiquitylation and checkpoint protein assembly
    • Huen MS, Grant R, Manke I, et al. RNF8 transduces the DNAdamage signal via histone ubiquitylation and checkpoint protein assembly. Cell 2007;131:901-914.
    • (2007) Cell , vol.131 , pp. 901-914
    • Huen, M.S.1    Grant, R.2    Manke, I.3
  • 109
    • 36248966246 scopus 로고    scopus 로고
    • RNF8 ubiquitylates histones at DNA double-strand breaks and promotes assembly of repair proteins
    • Mailand N, Bekker-Jensen S, Faustrup H, et al. RNF8 ubiquitylates histones at DNA double-strand breaks and promotes assembly of repair proteins. Cell 2007;131:887-900.
    • (2007) Cell , vol.131 , pp. 887-900
    • Mailand, N.1    Bekker-Jensen, S.2    Faustrup, H.3
  • 110
    • 36749084931 scopus 로고    scopus 로고
    • Orchestration of the DNAdamage response by the RNF8 ubiquitin ligase
    • Kolas NK, Chapman JR, Nakada S, et al. Orchestration of the DNAdamage response by the RNF8 ubiquitin ligase. Science 2007;318: 1637-1640.
    • (2007) Science , vol.318 , pp. 1637-1640
    • Kolas, N.K.1    Chapman, J.R.2    Nakada, S.3
  • 111
    • 37349096996 scopus 로고    scopus 로고
    • Distinct roles of chromatinassociated proteins MDC1 and 53BP1 in mammalian double-strand break repair
    • Xie A, Hartlerode A, Stucki M, et al. Distinct roles of chromatinassociated proteins MDC1 and 53BP1 in mammalian double-strand break repair. Mol Cell 2007;28:1045-1057.
    • (2007) Mol Cell , vol.28 , pp. 1045-1057
    • Xie, A.1    Hartlerode, A.2    Stucki, M.3
  • 112
    • 79551665780 scopus 로고    scopus 로고
    • MMSET regulates histone H4K20 methylation and 53BP1 accumulation at DNA damage sites
    • Pei H, Zhang L, Luo K, et al. MMSET regulates histone H4K20 methylation and 53BP1 accumulation at DNA damage sites. Nature 2011;470:124-128.
    • (2011) Nature , vol.470 , pp. 124-128
    • Pei, H.1    Zhang, L.2    Luo, K.3
  • 113
    • 57049132043 scopus 로고    scopus 로고
    • 53BP1 promotes nonhomologous end joining of telomeres by increasing chromatin mobility
    • Dimitrova N, Chen YC, Spector DL, et al. 53BP1 promotes nonhomologous end joining of telomeres by increasing chromatin mobility. Nature 2008;456:524-528.
    • (2008) Nature , vol.456 , pp. 524-528
    • Dimitrova, N.1    Chen, Y.C.2    Spector, D.L.3
  • 114
    • 57049124828 scopus 로고    scopus 로고
    • 53BP1 facilitates longrange DNA end-joining during V(D)J recombination
    • Difilippantonio S, Gapud E, Wong N, et al. 53BP1 facilitates longrange DNA end-joining during V(D)J recombination. Nature 2008; 456:529-533.
    • (2008) Nature , vol.456 , pp. 529-533
    • Difilippantonio, S.1    Gapud, E.2    Wong, N.3
  • 115
    • 84865364870 scopus 로고    scopus 로고
    • Playing the end game: DNA double-strand break repair pathway choice
    • Chapman JR, Taylor MR, Boulton SJ. Playing the end game: DNA double-strand break repair pathway choice. Mol Cell 2012; 47:497-510.
    • (2012) Mol Cell , vol.47 , pp. 497-510
    • Chapman, J.R.1    Taylor, M.R.2    Boulton, S.J.3
  • 116
    • 84859004905 scopus 로고    scopus 로고
    • Exo1 plays a major role in DNA end resection in humans and influences double-strand break repair and damage signaling decisions
    • Tomimatsu N, Mukherjee B, Deland K, et al. Exo1 plays a major role in DNA end resection in humans and influences double-strand break repair and damage signaling decisions. DNA Repair (Amst) 2012;11: 441-448.
    • (2012) DNA Repair (Amst) , vol.11 , pp. 441-448
    • Tomimatsu, N.1    Mukherjee, B.2    Deland, K.3
  • 117
    • 42949165854 scopus 로고    scopus 로고
    • PKBalpha/akt1 acts downstream of DNA-PK in the DNA double-strand break response and promotes survival
    • Bozulic L, Surucu B, Hynx D, et al. PKBalpha/akt1 acts downstream of DNA-PK in the DNA double-strand break response and promotes survival. Mol Cell 2008;30:203-213.
    • (2008) Mol Cell , vol.30 , pp. 203-213
    • Bozulic, L.1    Surucu, B.2    Hynx, D.3
  • 118
    • 84864018780 scopus 로고    scopus 로고
    • Akt promotes post-irradiation survival of human tumor cells through initiation, progression, and termination of DNA-PKcs-dependent DNA double-strand break repair
    • Toulany M, Lee KJ, Fattah KR, et al. Akt promotes post-irradiation survival of human tumor cells through initiation, progression, and termination of DNA-PKcs-dependent DNA double-strand break repair. Mol Cancer Res 2012;10:945-957.
    • (2012) Mol Cancer Res , vol.10 , pp. 945-957
    • Toulany, M.1    Lee, K.J.2    Fattah, K.R.3
  • 119
    • 34347223656 scopus 로고    scopus 로고
    • Somatic mutations in the tyrosine kinase domain of epidermal growth factor receptor (EGFR) abrogate EGFR-mediated radioprotection in non-small cell lung carcinoma
    • Das AK, Chen BP, Story MD, et al. Somatic mutations in the tyrosine kinase domain of epidermal growth factor receptor (EGFR) abrogate EGFR-mediated radioprotection in non-small cell lung carcinoma. Cancer Res 2007;67:5267-5274.
    • (2007) Cancer Res , vol.67 , pp. 5267-5274
    • Das, A.K.1    Chen, B.P.2    Story, M.D.3
  • 120
    • 24744449739 scopus 로고    scopus 로고
    • Radiation-induced epidermal growth factor receptor nuclear import is linked to activation of DNA-dependent protein kinase
    • Dittmann K, Mayer C, Fehrenbacher B, et al. Radiation-induced epidermal growth factor receptor nuclear import is linked to activation of DNA-dependent protein kinase. J Biol Chem 2005;280: 31182-31189.
    • (2005) J Biol Chem , vol.280 , pp. 31182-31189
    • Dittmann, K.1    Mayer, C.2    Fehrenbacher, B.3
  • 121
    • 84867647937 scopus 로고    scopus 로고
    • Threonine 2609 phosphorylation of the DNA-dependent protein kinase is a critical prerequisite for epidermal growth factor receptor-mediated radiation resistance
    • Javvadi P, Makino H, Das AK, et al. Threonine 2609 phosphorylation of the DNA-dependent protein kinase is a critical prerequisite for epidermal growth factor receptor-mediated radiation resistance. Mol Cancer Res 2012;10:1359-1368.
    • (2012) Mol Cancer Res , vol.10 , pp. 1359-1368
    • Javvadi, P.1    Makino, H.2    Das, A.K.3
  • 122
    • 79959814259 scopus 로고    scopus 로고
    • DNA ligase III promotes alternative nonhomologous end-joining during chromosomal translocation formation
    • Simsek D, Brunet E, Wong SY-W, et al. DNA ligase III promotes alternative nonhomologous end-joining during chromosomal translocation formation. PLoS Genet 2011;7:e1002080.
    • (2011) PLoS Genet , vol.7
    • Simsek, D.1    Brunet, E.2    Sy-W, W.3
  • 123
    • 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
  • 124
    • 80755187806 scopus 로고    scopus 로고
    • Double-strand break end resection and repair pathway choice
    • Symington LS, Gautier J. Double-strand break end resection and repair pathway choice. Annu Rev Genet 2011;45:247-271.
    • (2011) Annu Rev Genet , vol.45 , pp. 247-271
    • Symington, L.S.1    Gautier, J.2
  • 125
    • 67349246802 scopus 로고    scopus 로고
    • CTIP-BRCA1 modulates the choice of DNA double-strand-break repair pathway throughout the cell cycle
    • Yun MH, Hiom K. CTIP-BRCA1 modulates the choice of DNA double-strand-break repair pathway throughout the cell cycle. Nature 2009;459:460-463.
    • (2009) Nature , vol.459 , pp. 460-463
    • Yun, M.H.1    Hiom, K.2
  • 126
    • 79952762235 scopus 로고    scopus 로고
    • Factors determining DNA double-strand break repair pathway choice in G2 phase
    • Shibata A, Conrad S, Birraux J, et al. Factors determining DNA double-strand break repair pathway choice in G2 phase. EMBO J 2011;30:1079-1092.
    • (2011) EMBO J , vol.30 , pp. 1079-1092
    • Shibata, A.1    Conrad, S.2    Birraux, J.3
  • 127
    • 39749166975 scopus 로고    scopus 로고
    • DNA repair pathways as targets for cancer therapy
    • Helleday T, Petermann E, Lundin C, et al. DNA repair pathways as targets for cancer therapy. Nat Rev Cancer 2008;8:193-204.
    • (2008) Nat Rev Cancer , vol.8 , pp. 193-204
    • Helleday, T.1    Petermann, E.2    Lundin, C.3
  • 128
    • 78650350366 scopus 로고    scopus 로고
    • DNA-dependent protein kinase (DNA-PK) inhibitors. Synthesis and biological activity of quinolin-4- one and pyridopyrimidin-4-one surrogates for the chromen-4-one chemotype
    • Cano C, Barbeau OR, Bailey C, et al. DNA-dependent protein kinase (DNA-PK) inhibitors. Synthesis and biological activity of quinolin-4- one and pyridopyrimidin-4-one surrogates for the chromen-4-one chemotype. J Med Chem 2010;53:8498-8507.
    • (2010) J Med Chem , vol.53 , pp. 8498-8507
    • Cano, C.1    Barbeau, O.R.2    Bailey, C.3
  • 129
    • 78751644441 scopus 로고    scopus 로고
    • DNA-dependent protein kinase (DNA-PK) inhibitors: Structure-activity relationships for Oalkoxyphenylchromen- 4-one probes of the ATP-binding domain
    • Clapham KM, Bardos J, Finlay MR, et al. DNA-dependent protein kinase (DNA-PK) inhibitors: Structure-activity relationships for Oalkoxyphenylchromen- 4-one probes of the ATP-binding domain. Bioorg Med Chem Lett 2011;21:966-970.
    • (2011) Bioorg Med Chem Lett , vol.21 , pp. 966-970
    • Clapham, K.M.1    Bardos, J.2    Finlay, M.R.3
  • 130
    • 77950336368 scopus 로고    scopus 로고
    • Atropisomeric 8- arylchromen-4-ones exhibit enantioselective inhibition of the DNA-dependent protein kinase (DNA-PK)
    • Cano C, Golding BT, Haggerty K, et al. Atropisomeric 8- arylchromen-4-ones exhibit enantioselective inhibition of the DNA-dependent protein kinase (DNA-PK). Org Biomol Chem 2010; 8:1922-1928.
    • (2010) Org Biomol Chem , vol.8 , pp. 1922-1928
    • Cano, C.1    Golding, B.T.2    Haggerty, K.3
  • 131
    • 84864633030 scopus 로고    scopus 로고
    • Potent enantioselective inhibition of DNA-dependent protein kinase (DNA-PK) by atropisomeric chromenone derivatives
    • Clapham KM, Rennison T, Jones G, et al. Potent enantioselective inhibition of DNA-dependent protein kinase (DNA-PK) by atropisomeric chromenone derivatives. Org Biomol Chem 2012;10: 6747-6757.
    • (2012) Org Biomol Chem , vol.10 , pp. 6747-6757
    • Clapham, K.M.1    Rennison, T.2    Jones, G.3
  • 132
    • 77449112182 scopus 로고    scopus 로고
    • Mechanism of action of an imidopiperidine inhibitor of human polynucleotide kinase/ phosphatase
    • Freschauf GK, Mani RS, Mereniuk TR, et al. Mechanism of action of an imidopiperidine inhibitor of human polynucleotide kinase/ phosphatase. J Biol Chem 2010;285:2351-2360.
    • (2010) J Biol Chem , vol.285 , pp. 2351-2360
    • Freschauf, G.K.1    Mani, R.S.2    Mereniuk, T.R.3
  • 133
    • 70350244540 scopus 로고    scopus 로고
    • Identification of a small molecule inhibitor of the human DNA repair enzyme polynucleotide kinase/phosphatase
    • Freschauf GK, Karimi-Busheri F, Ulaczyk-Lesanko A, et al. Identification of a small molecule inhibitor of the human DNA repair enzyme polynucleotide kinase/phosphatase. Cancer Res 2009;69: 7739-7746.
    • (2009) Cancer Res , vol.69 , pp. 7739-7746
    • Freschauf, G.K.1    Karimi-Busheri, F.2    Ulaczyk-Lesanko, A.3
  • 134
    • 67650471685 scopus 로고    scopus 로고
    • Inhibition of poly(ADP-ribose) polymerase in tumors from BRCA mutation carriers
    • Fong PC, Boss DS, Yap TA, et al. Inhibition of poly(ADP-ribose) polymerase in tumors from BRCA mutation carriers. N Engl J Med 2009;361:123-134.
    • (2009) N Engl J Med , vol.361 , pp. 123-134
    • Fong, P.C.1    Boss, D.S.2    Yap, T.A.3
  • 135
    • 79952747328 scopus 로고    scopus 로고
    • Nonhomologous end joining drives poly(ADP-ribose) polymerase (PARP) inhibitor lethality in homologous recombination-deficient cells
    • Patel AG, Sarkaria JN, Kaufmann SH. Nonhomologous end joining drives poly(ADP-ribose) polymerase (PARP) inhibitor lethality in homologous recombination-deficient cells. Proc Natl Acad Sci U S A 2011;108:3406-3411.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 3406-3411
    • Patel, A.G.1    Sarkaria, J.N.2    Kaufmann, S.H.3
  • 136
    • 84861907790 scopus 로고    scopus 로고
    • Enhanced cytotoxicity of PARP inhibition in mantle cell lymphoma harbouring mutations in both ATM and p53
    • Williamson CT, Kubota E, Hamill JD, et al. Enhanced cytotoxicity of PARP inhibition in mantle cell lymphoma harbouring mutations in both ATM and p53. EMBO Mol Med 2012;4:515-527.
    • (2012) EMBO Mol Med , vol.4 , pp. 515-527
    • Williamson, C.T.1    Kubota, E.2    Hamill, J.D.3
  • 137
    • 77953879925 scopus 로고    scopus 로고
    • Ku70 corrupts DNA repair in the absence of the fanconi anemia pathway
    • Pace P, Mosedale G, Hodskinson MR, et al. Ku70 corrupts DNA repair in the absence of the fanconi anemia pathway. Science 2010; 329:219-223.
    • (2010) Science , vol.329 , pp. 219-223
    • Pace, P.1    Mosedale, G.2    Hodskinson, M.R.3
  • 138
    • 77954310242 scopus 로고    scopus 로고
    • Preventing nonhomologous end joining suppresses DNA repair defects of Fanconi anemia
    • Adamo A, Collis SJ, Adelman CA, et al. Preventing nonhomologous end joining suppresses DNA repair defects of Fanconi anemia. Molecular Cell 2010;39:25-35.
    • (2010) Molecular Cell , vol.39 , pp. 25-35
    • Adamo, A.1    Collis, S.J.2    Adelman, C.A.3
  • 139
    • 84882314152 scopus 로고    scopus 로고
    • DNA double strand break repair by non-homologous end joining and its clinical relevance
    • Kelley MR, editor., San Diego, CA: Academic Press
    • Weinfeld M, Lees-Miller SP. DNA double strand break repair by non-homologous end joining and its clinical relevance. In: Kelley MR, editor. DNA Repair in Cancer Therapy: Molecular Targets and Clinical Applications. San Diego, CA: Academic Press; 2012. p. 161-190.
    • (2012) DNA Repair in Cancer Therapy: Molecular Targets and Clinical Applications , pp. 161-190
    • Weinfeld, M.1    Lees-Miller, S.P.2
  • 140
    • 38049088157 scopus 로고    scopus 로고
    • DNA-activated protein kinase functions in a newly observed s phase checkpoint that links histone mrna abundance with DNA replication
    • Muller B, Blackburn J, Feijoo C, et al. DNA-activated protein kinase functions in a newly observed s phase checkpoint that links histone mrna abundance with DNA replication. J Cell Biol 2007; 179:1385-1398.
    • (2007) J Cell Biol , vol.179 , pp. 1385-1398
    • Muller, B.1    Blackburn, J.2    Feijoo, C.3
  • 141
    • 62149105212 scopus 로고    scopus 로고
    • A role of DNA-pk for the metabolic gene regulation in response to insulin
    • Wong RH, Chang I, Hudak CS, et al. A role of DNA-pk for the metabolic gene regulation in response to insulin. Cell 2009;136: 1056-1072.
    • (2009) Cell , vol.136 , pp. 1056-1072
    • Wong, R.H.1    Chang, I.2    Hudak, C.S.3
  • 142
    • 79953299693 scopus 로고    scopus 로고
    • Involvement of DNA-dependent protein kinase in normal cell cycle progression through mitosis
    • Lee KJ, Lin YF, Chou HY, et al. Involvement of DNA-dependent protein kinase in normal cell cycle progression through mitosis. J Biol Chem 2011;286:12796-12802.
    • (2011) J Biol Chem , vol.286 , pp. 12796-12802
    • Lee, K.J.1    Lin, Y.F.2    Chou, H.Y.3
  • 143
    • 77951705618 scopus 로고    scopus 로고
    • Inactivation of DNA-dependent protein kinase leads to spindle disruption and mitotic catastrophe with attenuated checkpoint protein 2 phosphorylation in response to DNA damage
    • Shang ZF, Huang B, Xu QZ, et al. Inactivation of DNA-dependent protein kinase leads to spindle disruption and mitotic catastrophe with attenuated checkpoint protein 2 phosphorylation in response to DNA damage. Cancer Res 2010;70:3657-3666.
    • (2010) Cancer Res , vol.70 , pp. 3657-3666
    • Shang, Z.F.1    Huang, B.2    Xu, Q.Z.3
  • 144
    • 84873037745 scopus 로고    scopus 로고
    • Steroidogenic factor-1 (nr5a1) maintains centrosome homeostasis in steroidogenic cells by restricting centrosomal DNA-PK activation
    • Wang CY, Kao YH, Lai PY, et al. Steroidogenic factor-1 (nr5a1) maintains centrosome homeostasis in steroidogenic cells by restricting centrosomal DNA-PK activation. Mol Cell Biol 2013;33:476-484.
    • (2013) Mol Cell Biol , vol.33 , pp. 476-484
    • Wang, C.Y.1    Kao, Y.H.2    Lai, P.Y.3
  • 145
    • 33745255099 scopus 로고    scopus 로고
    • A topoisomerase iibeta-mediated dsdna break required for regulated transcription
    • Ju BG, Lunyak VV, Perissi V, et al. A topoisomerase iibeta-mediated dsdna break required for regulated transcription. Science 2006;312: 1798-1802.
    • (2006) Science , vol.312 , pp. 1798-1802
    • Ju, B.G.1    Lunyak, V.V.2    Perissi, V.3
  • 146
    • 79958109315 scopus 로고    scopus 로고
    • A DNA-dependent stress response involving DNA-pk occurs in hypoxic cells and contributes to cellular adaptation to hypoxia
    • Bouquet F, Ousset M, Biard D, et al. A DNA-dependent stress response involving DNA-pk occurs in hypoxic cells and contributes to cellular adaptation to hypoxia. J Cell Sci 2011;124:1943-1951.
    • (2011) J Cell Sci , vol.124 , pp. 1943-1951
    • Bouquet, F.1    Ousset, M.2    Biard, D.3
  • 147
    • 84869115801 scopus 로고    scopus 로고
    • Identification and characterization of a small inhibitory peptide that can target DNA-pkcs autophosphorylation and increase tumor radiosensitivity
    • Sun X, Yang C, Liu H, et al. Identification and characterization of a small inhibitory peptide that can target DNA-pkcs autophosphorylation and increase tumor radiosensitivity. Int J Radiat Oncol Biol Phys 2012;84:1212-1219.
    • Int J Radiat Oncol Biol Phys , vol.2012 , Issue.84 , pp. 1212-1219
    • Sun, X.1    Yang, C.2    Liu, H.3
  • 148
    • 84864875154 scopus 로고    scopus 로고
    • Chemosensitization of cancer cells by ku-0060648, a dual inhibitor of DNA-pk and pi-3k
    • Munck JM, Batey MA, Zhao Y, et al. Chemosensitization of cancer cells by ku-0060648, a dual inhibitor of DNA-pk and pi-3k. Mol Cancer Ther 2012;11:1789-1798.
    • (2012) Mol Cancer Ther , vol.11 , pp. 1789-1798
    • Munck, J.M.1    Batey, M.A.2    Zhao, Y.3
  • 149
    • 84861626653 scopus 로고    scopus 로고
    • Intranuclear delivery of a novel antibody-derived radiosensitizer targeting the DNA-dependent protein kinase catalytic subunit
    • Xiong H, Lee RJ, Haura EB, et al. Intranuclear delivery of a novel antibody-derived radiosensitizer targeting the DNA-dependent protein kinase catalytic subunit. Int J Radiat Oncol Biol Phys 2012; 83:1023-1030.
    • (2012) Int J Radiat Oncol Biol Phys , vol.83 , pp. 1023-1030
    • Xiong, H.1    Lee, R.J.2    Haura, E.B.3
  • 150
    • 58149294243 scopus 로고    scopus 로고
    • Effect of zstk474, a novel phosphatidylinositol 3-kinase inhibitor, on DNA-dependent protein kinase
    • Kong D, Yaguchi S, Yamori T. Effect of zstk474, a novel phosphatidylinositol 3-kinase inhibitor, on DNA-dependent protein kinase. Biol Pharm Bull 2009;32:297-300.
    • (2009) Biol Pharm Bull , vol.32 , pp. 297-300
    • Kong, D.1    Yaguchi, S.2    Yamori, T.3
  • 151
    • 77957597727 scopus 로고    scopus 로고
    • Discovery of phosphatidylinositol 3-kinase inhibitory compounds from the screening committee of anticancer drugs (scads) library
    • Kong D, Yamazaki K, Yamori T. Discovery of phosphatidylinositol 3-kinase inhibitory compounds from the screening committee of anticancer drugs (scads) library. Biol Pharm Bull 2010;33:1600-1604.
    • (2010) Biol Pharm Bull , vol.33 , pp. 1600-1604
    • Kong, D.1    Yamazaki, K.2    Yamori, T.3
  • 152
    • 77956356660 scopus 로고    scopus 로고
    • Zstk474, a novel phosphatidylinositol 3-kinase inhibitor identified using the jfcr39 drug discovery system
    • Kong DX, Yamori T. Zstk474, a novel phosphatidylinositol 3-kinase inhibitor identified using the jfcr39 drug discovery system. Acta Pharmacol Sin 2010;31:1189-1197.
    • (2010) Acta Pharmacol Sin , vol.31 , pp. 1189-1197
    • Kong, D.X.1    Yamori, T.2


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