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Volumn 745-746, Issue , 2013, Pages 16-25

Ku80-deleted cells are defective at base excision repair

Author keywords

Base excision repair; Base lesions; Double strand breaks; Nonhomologous end joining; Single strand breaks

Indexed keywords

ALKYLATING AGENT; DNA BINDING PROTEIN; DNA LIGASE IV; HISTONE H2AX; KU ANTIGEN; POLYDEOXYRIBONUCLEOTIDE SYNTHASE; PROTEIN KU80; REACTIVE OXYGEN METABOLITE; UNCLASSIFIED DRUG;

EID: 84878218838     PISSN: 00275107     EISSN: 09218262     Source Type: Journal    
DOI: 10.1016/j.mrfmmm.2013.03.010     Document Type: Article
Times cited : (12)

References (61)
  • 1
    • 33747889722 scopus 로고    scopus 로고
    • Role of non-homologous end joining (NHEJ) in maintaining genomic integrity
    • Burma S., Chen B.P., Chen D.J. Role of non-homologous end joining (NHEJ) in maintaining genomic integrity. DNA Repair (Amst.) 2006, 5:1042-1048.
    • (2006) DNA Repair (Amst.) , vol.5 , pp. 1042-1048
    • Burma, S.1    Chen, B.P.2    Chen, D.J.3
  • 2
    • 0035833552 scopus 로고    scopus 로고
    • Structure of the Ku heterodimer bound to DNA and its implications for double-strand break repair
    • Walker J.R., Corpina R.A., Goldberg J. Structure of the Ku heterodimer bound to DNA and its implications for double-strand break repair. Nature 2001, 412:607-614.
    • (2001) Nature , vol.412 , pp. 607-614
    • Walker, J.R.1    Corpina, R.A.2    Goldberg, J.3
  • 4
    • 31044432090 scopus 로고    scopus 로고
    • XLF interacts with the XRCC4-DNA ligase IV complex to promote DNA nonhomologous end-joining
    • Ahnesorg P., Smith P., Jackson S.P. XLF interacts with the XRCC4-DNA ligase IV complex to promote DNA nonhomologous end-joining. Cell 2006, 124:301-313.
    • (2006) Cell , vol.124 , pp. 301-313
    • Ahnesorg, P.1    Smith, P.2    Jackson, S.P.3
  • 5
    • 3242879122 scopus 로고    scopus 로고
    • The mechanism of vertebrate nonhomologous DNA end joining and its role in V(D)J recombination
    • Lieber M.R., Ma Y., Pannicke U., Schwarz K. The mechanism of vertebrate nonhomologous DNA end joining and its role in V(D)J recombination. DNA Repair (Amst.) 2004, 3:817-826.
    • (2004) DNA Repair (Amst.) , vol.3 , pp. 817-826
    • Lieber, M.R.1    Ma, Y.2    Pannicke, U.3    Schwarz, K.4
  • 6
    • 36849088515 scopus 로고    scopus 로고
    • Deletion of Ku70, Ku80, or both causes early aging without substantially increased cancer
    • Li H., Vogel H., Holcomb V.B., Gu Y., Hasty P. Deletion of Ku70, Ku80, or both causes early aging without substantially increased cancer. Mol. Cell. Biol. 2007, 27:8205-8214.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 8205-8214
    • Li, H.1    Vogel, H.2    Holcomb, V.B.3    Gu, Y.4    Hasty, P.5
  • 7
    • 0030576534 scopus 로고    scopus 로고
    • Ku86-deficient mice exhibit severe combined immunodeficiency and defective processing of V(D)J recombination intermediates
    • Zhu C., Bogue M.A., Lim D.S., Hasty P., Roth D.B. Ku86-deficient mice exhibit severe combined immunodeficiency and defective processing of V(D)J recombination intermediates. Cell 1996, 86:379-389.
    • (1996) Cell , vol.86 , pp. 379-389
    • Zhu, C.1    Bogue, M.A.2    Lim, D.S.3    Hasty, P.4    Roth, D.B.5
  • 10
    • 0031471226 scopus 로고    scopus 로고
    • Hypersensitivity of Ku80-deficient cell lines and mice to DNA damage: the effects of ionizing radiation on growth, survival, and development
    • Nussenzweig A., Sokol K., Burgman P., Li L., Li G.C. Hypersensitivity of Ku80-deficient cell lines and mice to DNA damage: the effects of ionizing radiation on growth, survival, and development. Proc. Natl. Acad. Sci. U. S. A. 1997, 94:13588-13593.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 13588-13593
    • Nussenzweig, A.1    Sokol, K.2    Burgman, P.3    Li, L.4    Li, G.C.5
  • 11
    • 0030858967 scopus 로고    scopus 로고
    • Ku70-deficient embryonic stem cells have increased ionizing radiosensitivity, defective DNA end-binding activity, and inability to support V(D)J recombination
    • Gu Y., Jin S., Gao Y., Weaver D.T., Alt F.W. Ku70-deficient embryonic stem cells have increased ionizing radiosensitivity, defective DNA end-binding activity, and inability to support V(D)J recombination. Proc. Natl. Acad. Sci. U. S. A. 1997, 94:8076-8081.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 8076-8081
    • Gu, Y.1    Jin, S.2    Gao, Y.3    Weaver, D.T.4    Alt, F.W.5
  • 12
    • 67349207122 scopus 로고    scopus 로고
    • Deleting Ku70 is milder than deleting Ku80 in p53-mutant mice and cells
    • Li H., Choi Y.J., Hanes M.A., Marple T., Vogel H., Hasty P. Deleting Ku70 is milder than deleting Ku80 in p53-mutant mice and cells. Oncogene 2009, 28:1875-1878.
    • (2009) Oncogene , vol.28 , pp. 1875-1878
    • Li, H.1    Choi, Y.J.2    Hanes, M.A.3    Marple, T.4    Vogel, H.5    Hasty, P.6
  • 14
    • 0034307416 scopus 로고    scopus 로고
    • An alternate form of Ku80 is required for DNA end-binding activity in mammalian mitochondria
    • Coffey G., Campbell C. An alternate form of Ku80 is required for DNA end-binding activity in mammalian mitochondria. Nucleic Acids Res. 2000, 28:3793-3800.
    • (2000) Nucleic Acids Res. , vol.28 , pp. 3793-3800
    • Coffey, G.1    Campbell, C.2
  • 15
    • 34247599335 scopus 로고    scopus 로고
    • A unified view of base excision repair: lesion-dependent protein complexes regulated by post-translational modification
    • Almeida K.H., Sobol R.W. A unified view of base excision repair: lesion-dependent protein complexes regulated by post-translational modification. DNA Repair (Amst.) 2007, 6:695-711.
    • (2007) DNA Repair (Amst.) , vol.6 , pp. 695-711
    • Almeida, K.H.1    Sobol, R.W.2
  • 16
    • 0344585962 scopus 로고    scopus 로고
    • DNA N-glycosylase deficient mice: a tale of redundancy
    • Parsons J.L., Elder R.H. DNA N-glycosylase deficient mice: a tale of redundancy. Mutat. Res. 2003, 531:165-175.
    • (2003) Mutat. Res. , vol.531 , pp. 165-175
    • Parsons, J.L.1    Elder, R.H.2
  • 19
    • 4344582945 scopus 로고    scopus 로고
    • A genotoxic screen: rapid analysis of cellular dose-response to a wide range of agents that either damage DNA or alter genome maintenance pathways
    • Marple T., Li H., Hasty P. A genotoxic screen: rapid analysis of cellular dose-response to a wide range of agents that either damage DNA or alter genome maintenance pathways. Mutat. Res. 2004, 554:253-266.
    • (2004) Mutat. Res. , vol.554 , pp. 253-266
    • Marple, T.1    Li, H.2    Hasty, P.3
  • 20
    • 24944506364 scopus 로고    scopus 로고
    • Non-homologous end joining but not homologous recombination, enables survival for cells exposed to a histone deacetylase inhibitor
    • Yaneva M., Li H., Marple T., Hasty P. Non-homologous end joining but not homologous recombination, enables survival for cells exposed to a histone deacetylase inhibitor. Nucleic Acids Res. 2005, 33:5320-5330.
    • (2005) Nucleic Acids Res. , vol.33 , pp. 5320-5330
    • Yaneva, M.1    Li, H.2    Marple, T.3    Hasty, P.4
  • 21
    • 0028966181 scopus 로고
    • DNA polymerase beta conducts the gap-filling step in uracil-initiated base excision repair in a bovine testis nuclear extract
    • Singhal R.K., Prasad R., Wilson S.H. DNA polymerase beta conducts the gap-filling step in uracil-initiated base excision repair in a bovine testis nuclear extract. J. Biol. Chem. 1995, 270:949-957.
    • (1995) J. Biol. Chem. , vol.270 , pp. 949-957
    • Singhal, R.K.1    Prasad, R.2    Wilson, S.H.3
  • 23
    • 0032894008 scopus 로고    scopus 로고
    • Direct involvement of p53 in the base excision repair pathway of the DNA repair machinery
    • Offer H., Wolkowicz R., Matas D., Blumenstein S., Livneh Z., Rotter V. Direct involvement of p53 in the base excision repair pathway of the DNA repair machinery. FEBS Lett. 1999, 450:197-204.
    • (1999) FEBS Lett. , vol.450 , pp. 197-204
    • Offer, H.1    Wolkowicz, R.2    Matas, D.3    Blumenstein, S.4    Livneh, Z.5    Rotter, V.6
  • 24
    • 3242887420 scopus 로고    scopus 로고
    • The role of the non-homologous end-joining pathway in lymphocyte development
    • Rooney S., Chaudhuri J., Alt F.W. The role of the non-homologous end-joining pathway in lymphocyte development. Immunol. Rev. 2004, 200:115-131.
    • (2004) Immunol. Rev. , vol.200 , pp. 115-131
    • Rooney, S.1    Chaudhuri, J.2    Alt, F.W.3
  • 26
    • 0035104857 scopus 로고    scopus 로고
    • Genotoxicity of streptonigrin: a review
    • Bolzan A.D., Bianchi M.S. Genotoxicity of streptonigrin: a review. Mutat. Res. 2001, 488:25-37.
    • (2001) Mutat. Res. , vol.488 , pp. 25-37
    • Bolzan, A.D.1    Bianchi, M.S.2
  • 27
    • 0021288059 scopus 로고
    • Paraquat: model for oxidant-initiated toxicity
    • Bus J.S., Gibson J.E. Paraquat: model for oxidant-initiated toxicity. Environ. Health Perspect. 1984, 55:37-46.
    • (1984) Environ. Health Perspect. , vol.55 , pp. 37-46
    • Bus, J.S.1    Gibson, J.E.2
  • 28
    • 0345061277 scopus 로고    scopus 로고
    • Association of XRCC1 and tyrosyl DNA phosphodiesterase (Tdp1) for the repair of topoisomerase I-mediated DNA lesions
    • Plo I., Liao Z.Y., Barcelo J.M., Kohlhagen G., Caldecott K.W., Weinfeld M., Pommier Y. Association of XRCC1 and tyrosyl DNA phosphodiesterase (Tdp1) for the repair of topoisomerase I-mediated DNA lesions. DNA Repair (Amst.) 2003, 2:1087-1100.
    • (2003) DNA Repair (Amst.) , vol.2 , pp. 1087-1100
    • Plo, I.1    Liao, Z.Y.2    Barcelo, J.M.3    Kohlhagen, G.4    Caldecott, K.W.5    Weinfeld, M.6    Pommier, Y.7
  • 30
    • 0032033603 scopus 로고    scopus 로고
    • Diversity of DNA topoisomerases I and inhibitors
    • Pommier Y. Diversity of DNA topoisomerases I and inhibitors. Biochimie 1998, 80:255-270.
    • (1998) Biochimie , vol.80 , pp. 255-270
    • Pommier, Y.1
  • 31
    • 10944251591 scopus 로고    scopus 로고
    • Repair and genetic consequences of endogenous DNA base damage in mammalian cells
    • Barnes D.E., Lindahl T. Repair and genetic consequences of endogenous DNA base damage in mammalian cells. Annu. Rev. Genet. 2004, 38:445-476.
    • (2004) Annu. Rev. Genet. , vol.38 , pp. 445-476
    • Barnes, D.E.1    Lindahl, T.2
  • 32
    • 22244448679 scopus 로고    scopus 로고
    • The role of base excision repair in the sensitivity and resistance to temozolomide-mediated cell death
    • Trivedi R.N., Almeida K.H., Fornsaglio J.L., Schamus S., Sobol R.W. The role of base excision repair in the sensitivity and resistance to temozolomide-mediated cell death. Cancer Res. 2005, 65:6394-6400.
    • (2005) Cancer Res. , vol.65 , pp. 6394-6400
    • Trivedi, R.N.1    Almeida, K.H.2    Fornsaglio, J.L.3    Schamus, S.4    Sobol, R.W.5
  • 33
    • 0142009654 scopus 로고    scopus 로고
    • A requirement for PARP-1 for the assembly or stability of XRCC1 nuclear foci at sites of oxidative DNA damage
    • El-Khamisy S.F., Masutani M., Suzuki H., Caldecott K.W. A requirement for PARP-1 for the assembly or stability of XRCC1 nuclear foci at sites of oxidative DNA damage. Nucleic Acids Res. 2003, 31:5526-5533.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 5526-5533
    • El-Khamisy, S.F.1    Masutani, M.2    Suzuki, H.3    Caldecott, K.W.4
  • 34
    • 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
  • 35
    • 33644866836 scopus 로고    scopus 로고
    • Quantitative correlation between cellular proliferation and nuclear poly (ADP-ribose) polymerase (PARP-1)
    • Kun E., Kirsten E., Bauer P.I., Ordahl C.P. Quantitative correlation between cellular proliferation and nuclear poly (ADP-ribose) polymerase (PARP-1). Int. J. Mol. Med. 2006, 17:293-300.
    • (2006) Int. J. Mol. Med. , vol.17 , pp. 293-300
    • Kun, E.1    Kirsten, E.2    Bauer, P.I.3    Ordahl, C.P.4
  • 37
    • 0030854373 scopus 로고    scopus 로고
    • Random mutagenesis of the poly(ADP-ribose) polymerase catalytic domain reveals amino acids involved in polymer branching
    • Rolli V., O'Farrell M., Menissier-de Murcia J., de Murcia G. Random mutagenesis of the poly(ADP-ribose) polymerase catalytic domain reveals amino acids involved in polymer branching. Biochemistry 1997, 36:12147-12154.
    • (1997) Biochemistry , vol.36 , pp. 12147-12154
    • Rolli, V.1    O'Farrell, M.2    Menissier-de Murcia, J.3    de Murcia, G.4
  • 38
    • 84455161816 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase 1 (PARP-1) binds to 8-oxoguanine-DNA glycosylase (OGG1)
    • Noren Hooten N., Kompaniez K., Barnes J., Lohani A., Evans M.K. Poly(ADP-ribose) polymerase 1 (PARP-1) binds to 8-oxoguanine-DNA glycosylase (OGG1). J. Biol. Chem. 2011, 286:44679-44690.
    • (2011) J. Biol. Chem. , vol.286 , pp. 44679-44690
    • Noren Hooten, N.1    Kompaniez, K.2    Barnes, J.3    Lohani, A.4    Evans, M.K.5
  • 39
    • 80355135233 scopus 로고    scopus 로고
    • PARP inhibitors in breast cancer: BRCA and beyond
    • Rios J., Puhalla S. PARP inhibitors in breast cancer: BRCA and beyond. Oncology (Williston Park) 2011, 25:1014-1025.
    • (2011) Oncology (Williston Park) , vol.25 , pp. 1014-1025
    • Rios, J.1    Puhalla, S.2
  • 41
    • 18144413027 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase activity prevents signaling pathways for cell cycle arrest after DNA methylating agent exposure
    • Horton J.K., Stefanick D.F., Naron J.M., Kedar P.S., Wilson S.H. Poly(ADP-ribose) polymerase activity prevents signaling pathways for cell cycle arrest after DNA methylating agent exposure. J. Biol. Chem. 2005, 280:15773-15785.
    • (2005) J. Biol. Chem. , vol.280 , pp. 15773-15785
    • Horton, J.K.1    Stefanick, D.F.2    Naron, J.M.3    Kedar, P.S.4    Wilson, S.H.5
  • 42
    • 0034663530 scopus 로고    scopus 로고
    • DNA polymerase beta is required for efficient DNA strand break repair induced by methyl methanesulfonate but not by hydrogen peroxide
    • Fortini P., Pascucci B., Belisario F., Dogliotti E. DNA polymerase beta is required for efficient DNA strand break repair induced by methyl methanesulfonate but not by hydrogen peroxide. Nucleic Acids Res. 2000, 28:3040-3046.
    • (2000) Nucleic Acids Res. , vol.28 , pp. 3040-3046
    • Fortini, P.1    Pascucci, B.2    Belisario, F.3    Dogliotti, E.4
  • 43
    • 0037193540 scopus 로고    scopus 로고
    • Involvement of DNA polymerase beta in protection against the cytotoxicity of oxidative DNA damage
    • Horton J.K., Baker A., Berg B.J., Sobol R.W., Wilson S.H. Involvement of DNA polymerase beta in protection against the cytotoxicity of oxidative DNA damage. DNA Repair (Amst.) 2002, 1:317-333.
    • (2002) DNA Repair (Amst.) , vol.1 , pp. 317-333
    • Horton, J.K.1    Baker, A.2    Berg, B.J.3    Sobol, R.W.4    Wilson, S.H.5
  • 44
    • 0026571874 scopus 로고
    • Role of a major autoepitope in forming the DNA binding site of the p70 (Ku) antigen
    • Chou C.H., Wang J., Knuth M.W., Reeves W.H. Role of a major autoepitope in forming the DNA binding site of the p70 (Ku) antigen. J. Exp. Med. 1992, 175:1677-1684.
    • (1992) J. Exp. Med. , vol.175 , pp. 1677-1684
    • Chou, C.H.1    Wang, J.2    Knuth, M.W.3    Reeves, W.H.4
  • 45
    • 0031974492 scopus 로고    scopus 로고
    • Identification of two domains of the p70 Ku protein mediating dimerization with p80 and DNA binding
    • Wang J., Dong X., Myung K., Hendrickson E.A., Reeves W.H. Identification of two domains of the p70 Ku protein mediating dimerization with p80 and DNA binding. J. Biol. Chem. 1998, 273:842-848.
    • (1998) J. Biol. Chem. , vol.273 , pp. 842-848
    • Wang, J.1    Dong, X.2    Myung, K.3    Hendrickson, E.A.4    Reeves, W.H.5
  • 46
    • 0028060111 scopus 로고
    • Similar DNA binding properties of free P70 (KU) subunit and P70/P80 heterodimer
    • Wang J., Satoh M., Chou C.H., Reeves W.H. Similar DNA binding properties of free P70 (KU) subunit and P70/P80 heterodimer. FEBS Lett. 1994, 351:219-224.
    • (1994) FEBS Lett. , vol.351 , pp. 219-224
    • Wang, J.1    Satoh, M.2    Chou, C.H.3    Reeves, W.H.4
  • 47
    • 0028090278 scopus 로고
    • Assembly and DNA binding of recombinant Ku (p70/p80) autoantigen defined by a novel monoclonal antibody specific for p70/p80 heterodimers
    • Wang J., Satoh M., Pierani A., Schmitt J., Chou C.H., Stunnenberg H.G., Roeder R.G., Reeves W.H. Assembly and DNA binding of recombinant Ku (p70/p80) autoantigen defined by a novel monoclonal antibody specific for p70/p80 heterodimers. J. Cell Sci. 1994, 107(Pt 11):3223-3233.
    • (1994) J. Cell Sci. , vol.107 , Issue.PART 11 , pp. 3223-3233
    • Wang, J.1    Satoh, M.2    Pierani, A.3    Schmitt, J.4    Chou, C.H.5    Stunnenberg, H.G.6    Roeder, R.G.7    Reeves, W.H.8
  • 50
    • 0035896594 scopus 로고    scopus 로고
    • Human ku70 interacts with heterochromatin protein 1alpha
    • Song K., Jung Y., Jung D., Lee I. Human ku70 interacts with heterochromatin protein 1alpha. J. Biol. Chem. 2001, 276:8321-8327.
    • (2001) J. Biol. Chem. , vol.276 , pp. 8321-8327
    • Song, K.1    Jung, Y.2    Jung, D.3    Lee, I.4
  • 51
    • 0032859119 scopus 로고    scopus 로고
    • Mre11 Ku70 interact in somatic cells, but are differentially expressed in early meiosis
    • Goedecke W., Eijpe M., Offenberg H.H., van Aalderen M., Heyting C. Mre11 Ku70 interact in somatic cells, but are differentially expressed in early meiosis. Nat. Genet. 1999, 23:194-198.
    • (1999) Nat. Genet. , vol.23 , pp. 194-198
    • Goedecke, W.1    Eijpe, M.2    Offenberg, H.H.3    van Aalderen, M.4    Heyting, C.5
  • 52
    • 0034093748 scopus 로고    scopus 로고
    • Ionizing radiation exposure results in up-regulation of Ku70 via a p53/ataxia-telangiectasia-mutated protein-dependent mechanism
    • Brown K.D., Lataxes T.A., Shangary S., Mannino J.L., Giardina J.F., Chen J., Baskaran R. Ionizing radiation exposure results in up-regulation of Ku70 via a p53/ataxia-telangiectasia-mutated protein-dependent mechanism. J. Biol. Chem. 2000, 275:6651-6656.
    • (2000) J. Biol. Chem. , vol.275 , pp. 6651-6656
    • Brown, K.D.1    Lataxes, T.A.2    Shangary, S.3    Mannino, J.L.4    Giardina, J.F.5    Chen, J.6    Baskaran, R.7
  • 54
    • 34247564493 scopus 로고    scopus 로고
    • Interaction of a cyclin E fragment with Ku70 regulates Bax-mediated apoptosis
    • Mazumder S., Plesca D., Kinter M., Almasan A. Interaction of a cyclin E fragment with Ku70 regulates Bax-mediated apoptosis. Mol. Cell. Biol. 2007, 27:3511-3520.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 3511-3520
    • Mazumder, S.1    Plesca, D.2    Kinter, M.3    Almasan, A.4
  • 57
    • 33645524585 scopus 로고    scopus 로고
    • Granzyme A, which causes single-stranded DNA damage, targets the double-strand break repair protein Ku70
    • Zhu P., Zhang D., Chowdhury D., Martinvalet D., Keefe D., Shi L., Lieberman J. Granzyme A, which causes single-stranded DNA damage, targets the double-strand break repair protein Ku70. EMBO Rep. 2006, 7:431-437.
    • (2006) EMBO Rep. , vol.7 , pp. 431-437
    • Zhu, P.1    Zhang, D.2    Chowdhury, D.3    Martinvalet, D.4    Keefe, D.5    Shi, L.6    Lieberman, J.7
  • 58
    • 0034609947 scopus 로고    scopus 로고
    • Ku70 can translocate to the nucleus independent of Ku80 translocation and DNA-PK autophosphorylation
    • Koike M., Shiomi T., Koike A. Ku70 can translocate to the nucleus independent of Ku80 translocation and DNA-PK autophosphorylation. Biochem. Biophys. Res. Commun. 2000, 276:1105-1111.
    • (2000) Biochem. Biophys. Res. Commun. , vol.276 , pp. 1105-1111
    • Koike, M.1    Shiomi, T.2    Koike, A.3
  • 59
    • 48949117384 scopus 로고    scopus 로고
    • NF-kappaB p65 regulates nuclear translocation of Ku70 via degradation of heat shock cognate protein 70 in pancreatic acinar AR42J cells
    • Lim J.W., Kim K.H., Kim H. NF-kappaB p65 regulates nuclear translocation of Ku70 via degradation of heat shock cognate protein 70 in pancreatic acinar AR42J cells. Int. J. Biochem. Cell Biol. 2008, 40:2065-2077.
    • (2008) Int. J. Biochem. Cell Biol. , vol.40 , pp. 2065-2077
    • Lim, J.W.1    Kim, K.H.2    Kim, H.3
  • 60
    • 0032568213 scopus 로고    scopus 로고
    • Human normal peripheral blood B-lymphocytes are deficient in DNA-dependent protein kinase activity due to the expression of a variant form of the Ku86 protein
    • Muller C., Dusseau C., Calsou P., Salles B. Human normal peripheral blood B-lymphocytes are deficient in DNA-dependent protein kinase activity due to the expression of a variant form of the Ku86 protein. Oncogene 1998, 16:1553-1560.
    • (1998) Oncogene , vol.16 , pp. 1553-1560
    • Muller, C.1    Dusseau, C.2    Calsou, P.3    Salles, B.4
  • 61
    • 0032145477 scopus 로고    scopus 로고
    • Cells deleted for Brca2 COOH terminus exhibit hypersensitivity to gamma-radiation and premature senescence
    • Morimatsu M., Donoho G., Hasty P. Cells deleted for Brca2 COOH terminus exhibit hypersensitivity to gamma-radiation and premature senescence. Cancer Res. 1998, 58:3441-3447.
    • (1998) Cancer Res. , vol.58 , pp. 3441-3447
    • Morimatsu, M.1    Donoho, G.2    Hasty, P.3


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