메뉴 건너뛰기




Volumn 5, Issue 12, 2010, Pages

The effect of DNA-dependent protein kinase on adeno-associated virus replication

Author keywords

[No Author keywords available]

Indexed keywords

DNA DEPENDENT PROTEIN KINASE; KU ANTIGEN; WORTMANNIN; ANDROSTANE DERIVATIVE; CELL NUCLEUS ANTIGEN; DNA BINDING PROTEIN; ENZYME INHIBITOR; SMALL INTERFERING RNA;

EID: 78650859568     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0015073     Document Type: Article
Times cited : (17)

References (87)
  • 1
    • 0027468265 scopus 로고
    • Binding of Ku protein to DNA. Measurement of affinity for ends and demonstration of binding to nicks
    • Blier PR, Griffith AJ, Craft J, Hardin JA (1993) Binding of Ku protein to DNA. Measurement of affinity for ends and demonstration of binding to nicks. J Biol Chem 268: 7594-7601.
    • (1993) J Biol Chem , vol.268 , pp. 7594-7601
    • Blier, P.R.1    Griffith, A.J.2    Craft, J.3    Hardin, J.A.4
  • 2
    • 0026570651 scopus 로고
    • Ku polypeptides synthesized in vitro assemble into complexes which recognize ends of double-stranded DNA
    • Griffith AJ, Blier PR, Mimori T, Hardin JA (1992) Ku polypeptides synthesized in vitro assemble into complexes which recognize ends of double-stranded DNA. J Biol Chem 267: 331-338.
    • (1992) J Biol Chem , vol.267 , pp. 331-338
    • Griffith, A.J.1    Blier, P.R.2    Mimori, T.3    Hardin, J.A.4
  • 3
    • 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 (2001) Structure of the Ku heterodimer bound to DNA and its implications for double-strand break repair. Nature 412: 607-614.
    • (2001) Nature , vol.412 , pp. 607-614
    • Walker, J.R.1    Corpina, R.A.2    Goldberg, J.3
  • 4
    • 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 AE (2000) Interactions of the DNA ligase IV-XRCC4 complex with DNA ends and the DNA-dependent protein kinase. J Biol Chem 275: 26196-26205.
    • (2000) J Biol Chem , vol.275 , pp. 26196-26205
    • Chen, L.1    Trujillo, K.2    Sung, P.3    Tomkinson, A.E.4
  • 5
    • 14844292557 scopus 로고    scopus 로고
    • DNA-dependent protein kinase and XRCC4-DNA ligase IV mobilization in the cell in response to DNA double strand breaks
    • Drouet J, Delteil C, Lefrancois J, Concannon P, Salles B, et al. (2005) DNA-dependent protein kinase and XRCC4-DNA ligase IV mobilization in the cell in response to DNA double strand breaks. J Biol Chem 280: 7060-7069.
    • (2005) J Biol Chem , vol.280 , pp. 7060-7069
    • Drouet, J.1    Delteil, C.2    Lefrancois, J.3    Concannon, P.4    Salles, B.5
  • 6
    • 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 MR (2002) Hairpin opening and overhang processing by an Artemis/DNA-dependent protein kinase complex in nonhomologous end joining and V(D)J recombination. Cell 108: 781-794.
    • (2002) Cell , vol.108 , pp. 781-794
    • Ma, Y.1    Pannicke, U.2    Schwarz, K.3    Lieber, M.R.4
  • 7
    • 0035917489 scopus 로고    scopus 로고
    • Artemis, a novel DNA double-strand break repair/V(D)J recombination protein, is mutated in human severe combined immune deficiency
    • Moshous D, Callebaut I, de Chasseval R, Corneo B, Cavazzana-Calvo M, et al. (2001) Artemis, a novel DNA double-strand break repair/V(D)J recombination protein, is mutated in human severe combined immune deficiency. Cell 105: 177-186.
    • (2001) Cell , vol.105 , pp. 177-186
    • Moshous, D.1    Callebaut, I.2    de Chasseval, R.3    Corneo, B.4    Cavazzana-Calvo, M.5
  • 8
    • 0037106180 scopus 로고    scopus 로고
    • Autophosphorylation of the DNA-dependent protein kinase catalytic subunit is required for rejoining of DNA double-strand breaks
    • Chan DW, Chen BP, Prithivirajsingh S, Kurimasa A, Story MD, et al. (2002) Autophosphorylation of the DNA-dependent protein kinase catalytic subunit is required for rejoining of DNA double-strand breaks. Genes Dev 16: 2333-2338.
    • (2002) Genes Dev , vol.16 , pp. 2333-2338
    • Chan, D.W.1    Chen, B.P.2    Prithivirajsingh, S.3    Kurimasa, A.4    Story, M.D.5
  • 9
    • 17644384427 scopus 로고    scopus 로고
    • Cell cycle dependence of DNA-dependent protein kinase phosphorylation in response to DNA double strand breaks
    • Chen BP, Chan DW, Kobayashi J, Burma S, Asaithamby A, et al. (2005) Cell cycle dependence of DNA-dependent protein kinase phosphorylation in response to DNA double strand breaks. J Biol Chem 280: 14709-14715.
    • (2005) J Biol Chem , vol.280 , pp. 14709-14715
    • Chen, B.P.1    Chan, D.W.2    Kobayashi, J.3    Burma, S.4    Asaithamby, A.5
  • 10
    • 20444475018 scopus 로고    scopus 로고
    • DNA-dependent protein kinase is a molecular target for the development of noncytotoxic radiation-sensitizing drugs
    • Shinohara ET, Geng L, Tan J, Chen H, Shir Y, et al. (2005) DNA-dependent protein kinase is a molecular target for the development of noncytotoxic radiation-sensitizing drugs. Cancer Res 65: 4987-4992.
    • (2005) Cancer Res , vol.65 , pp. 4987-4992
    • Shinohara, E.T.1    Geng, L.2    Tan, J.3    Chen, H.4    Shir, Y.5
  • 11
    • 20144373772 scopus 로고    scopus 로고
    • Inhibition of the DNA-dependent protein kinase catalytic subunit radiosensitizes malignant glioma cells by inducing autophagy
    • Daido S, Yamamoto A, Fujiwara K, Sawaya R, Kondo S, et al. (2005) Inhibition of the DNA-dependent protein kinase catalytic subunit radiosensitizes malignant glioma cells by inducing autophagy. Cancer Res 65: 4368-4375.
    • (2005) Cancer Res , vol.65 , pp. 4368-4375
    • Daido, S.1    Yamamoto, A.2    Fujiwara, K.3    Sawaya, R.4    Kondo, S.5
  • 12
    • 0029803485 scopus 로고    scopus 로고
    • Wortmannin is a potent inhibitor of DNA double strand break but not single strand break repair in Chinese hamster ovary cells
    • Boulton S, Kyle S, Yalcintepe L, Durkacz BW (1996) Wortmannin is a potent inhibitor of DNA double strand break but not single strand break repair in Chinese hamster ovary cells. Carcinogenesis 17: 2285-2290.
    • (1996) Carcinogenesis , vol.17 , pp. 2285-2290
    • Boulton, S.1    Kyle, S.2    Yalcintepe, L.3    Durkacz, B.W.4
  • 13
    • 0030066023 scopus 로고    scopus 로고
    • The phosphatidylinositol 3-kinase inhibitor wortmannin sensitizes murine fibroblasts and human tumor cells to radiation and blocks induction of p53 following DNA damage
    • Price BD, Youmell MB (1996) The phosphatidylinositol 3-kinase inhibitor wortmannin sensitizes murine fibroblasts and human tumor cells to radiation and blocks induction of p53 following DNA damage. Cancer Res 56: 246- 250.
    • (1996) Cancer Res , vol.56 , pp. 246-250
    • Price, B.D.1    Youmell, M.B.2
  • 14
    • 0033152759 scopus 로고    scopus 로고
    • Competitive and noncompetitive inhibition of the DNA-dependent protein kinase
    • Izzard RA, Jackson SP, Smith GC (1999) Competitive and noncompetitive inhibition of the DNA-dependent protein kinase. Cancer Res 59: 2581-2586.
    • (1999) Cancer Res , vol.59 , pp. 2581-2586
    • Izzard, R.A.1    Jackson, S.P.2    Smith, G.C.3
  • 15
    • 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 RA, Jack MT, Xu Y, Burma S, Chen DJ, et al. (2002) DNA damage-induced apoptosis requires the DNA-dependent protein kinase, and is mediated by the latent population of p53. Embo J 21: 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
  • 16
    • 12344324602 scopus 로고    scopus 로고
    • DNA-dependent protein kinase enhances DNA damage-induced apoptosis in association with Friend gp70
    • Yamaguchi S, Hasegawa M, Aizawa S, Tanaka K, Yoshida K, et al. (2005) DNA-dependent protein kinase enhances DNA damage-induced apoptosis in association with Friend gp70. Leuk Res 29: 307-316.
    • (2005) Leuk Res , vol.29 , pp. 307-316
    • Yamaguchi, S.1    Hasegawa, M.2    Aizawa, S.3    Tanaka, K.4    Yoshida, K.5
  • 17
    • 0031795922 scopus 로고    scopus 로고
    • Inactivation of DNA-dependent protein kinase by protein kinase Cdelta: Implications for apoptosis
    • Bharti A, Kraeft SK, Gounder M, Pandey P, Jin S, et al. (1998) Inactivation of DNA-dependent protein kinase by protein kinase Cdelta: implications for apoptosis. Mol Cell Biol 18: 6719-6728.
    • (1998) Mol Cell Biol , vol.18 , pp. 6719-6728
    • Bharti, A.1    Kraeft, S.K.2    Gounder, M.3    Pandey, P.4    Jin, S.5
  • 18
    • 0034669104 scopus 로고    scopus 로고
    • Ku acts in a unique way at the mammalian telomere to prevent end joining
    • Hsu HL, Gilley D, Galande SA, Hande MP, Allen B, et al. (2000) Ku acts in a unique way at the mammalian telomere to prevent end joining. Genes Dev 14: 2807-2812.
    • (2000) Genes Dev , vol.14 , pp. 2807-2812
    • Hsu, H.L.1    Gilley, D.2    Galande, S.A.3    Hande, M.P.4    Allen, B.5
  • 19
    • 0000595683 scopus 로고    scopus 로고
    • Fields B, ed. Fields Virology. Philadelphia, PA: Raven Press
    • Berns KI (1996) Parvoviridae: The Viruses and their replication. In: Fields B, ed. Fields Virology. Philadelphia, PA: Raven Press. pp 2173-2197.
    • (1996) Parvoviridae: The Viruses and Their Replication , pp. 2173-2197
    • Berns, K.I.1
  • 20
    • 0025362618 scopus 로고
    • The AAV origin binding protein Rep68 is an ATP-dependent site-specific endonuclease with DNA helicase activity
    • Im DS, Muzyczka N (1990) The AAV origin binding protein Rep68 is an ATP-dependent site-specific endonuclease with DNA helicase activity. Cell 61: 447-457.
    • (1990) Cell , vol.61 , pp. 447-457
    • Im, D.S.1    Muzyczka, N.2
  • 21
    • 0032853990 scopus 로고    scopus 로고
    • Rep-mediated nicking of the adeno-associated virus origin requires two biochemical activities, DNA helicase activity and transesterification
    • Brister JR, Muzyczka N (1999) Rep-mediated nicking of the adeno-associated virus origin requires two biochemical activities, DNA helicase activity and transesterification. J Virol 73: 9325-9336.
    • (1999) J Virol , vol.73 , pp. 9325-9336
    • Brister, J.R.1    Muzyczka, N.2
  • 22
    • 0033899961 scopus 로고    scopus 로고
    • Mechanism of Rep-mediated adeno-associated virus origin nicking
    • Brister JR, Muzyczka N (2000) Mechanism of Rep-mediated adeno-associated virus origin nicking. J Virol 74: 7762-7771.
    • (2000) J Virol , vol.74 , pp. 7762-7771
    • Brister, J.R.1    Muzyczka, N.2
  • 23
    • 0028307303 scopus 로고
    • Adeno-associated virus (AAV) Rep proteins mediate complex formation between AAV DNA and its integration site in human DNA
    • Weitzman MD, Kyostio SR, Kotin RM, Owens RA (1994) Adeno-associated virus (AAV) Rep proteins mediate complex formation between AAV DNA and its integration site in human DNA. Proc Natl Acad Sci U S A 91: 5808-5812.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 5808-5812
    • Weitzman, M.D.1    Kyostio, S.R.2    Kotin, R.M.3    Owens, R.A.4
  • 24
    • 0021257303 scopus 로고
    • Genetics of adeno-associated virus: Isolation and preliminary characterization of adeno-associated virus type 2 mutants
    • Hermonat PL, Labow MA, Wright R, Berns KI, Muzyczka N (1984) Genetics of adeno-associated virus: isolation and preliminary characterization of adeno-associated virus type 2 mutants. J Virol 51: 329-339.
    • (1984) J Virol , vol.51 , pp. 329-339
    • Hermonat, P.L.1    Labow, M.A.2    Wright, R.3    Berns, K.I.4    Muzyczka, N.5
  • 26
    • 0028050094 scopus 로고
    • Adeno-associated virus DNA replication in vitro: Activation by a maltose binding protein/Rep 68 fusion protein
    • Ward P, Urcelay E, Kotin R, Safer B, Berns KI (1994) Adeno-associated virus DNA replication in vitro: activation by a maltose binding protein/Rep 68 fusion protein. J Virol 68: 6029-6037.
    • (1994) J Virol , vol.68 , pp. 6029-6037
    • Ward, P.1    Urcelay, E.2    Kotin, R.3    Safer, B.4    Berns, K.I.5
  • 27
    • 0029888985 scopus 로고    scopus 로고
    • In vitro replication of adeno-associated virus DNA: Enhancement by extracts from adenovirus-infected HeLa cells
    • Ward P, Berns KI (1996) In vitro replication of adeno-associated virus DNA: enhancement by extracts from adenovirus-infected HeLa cells. J Virol 70: 4495-4501.
    • (1996) J Virol , vol.70 , pp. 4495-4501
    • Ward, P.1    Berns, K.I.2
  • 28
    • 0024428509 scopus 로고
    • Expression from the adeno-associated virus p5 and p19 promoters is negatively regulated in trans by the rep protein
    • Beaton A, Palumbo P, Berns KI (1989) Expression from the adeno-associated virus p5 and p19 promoters is negatively regulated in trans by the rep protein. J Virol 63: 4450-4454.
    • (1989) J Virol , vol.63 , pp. 4450-4454
    • Beaton, A.1    Palumbo, P.2    Berns, K.I.3
  • 29
    • 0022451185 scopus 로고
    • Positive and negative autoregulation of the adeno-associated virus type 2 genome
    • Labow MA, Hermonat PL, Berns KI (1986) Positive and negative autoregulation of the adeno-associated virus type 2 genome. J Virol 60: 251-258.
    • (1986) J Virol , vol.60 , pp. 251-258
    • Labow, M.A.1    Hermonat, P.L.2    Berns, K.I.3
  • 30
    • 0031014018 scopus 로고    scopus 로고
    • The adeno-associated virus (AAV) Rep protein acts as both a repressor and an activator to regulate AAV transcription during a productive infection
    • Pereira DJ, McCarty DM, Muzyczka N (1997) The adeno-associated virus (AAV) Rep protein acts as both a repressor and an activator to regulate AAV transcription during a productive infection. J Virol 71: 1079-1088.
    • (1997) J Virol , vol.71 , pp. 1079-1088
    • Pereira, D.J.1    McCarty, D.M.2    Muzyczka, N.3
  • 31
    • 0030958815 scopus 로고    scopus 로고
    • The adeno-associated virus type 2 p40 promoter requires a proximal Sp1 interaction and a p19 CArG-like element to facilitate Rep transactivation
    • Pereira DJ, Muzyczka N (1997) The adeno-associated virus type 2 p40 promoter requires a proximal Sp1 interaction and a p19 CArG-like element to facilitate Rep transactivation. J Virol 71: 4300-4309.
    • (1997) J Virol , vol.71 , pp. 4300-4309
    • Pereira, D.J.1    Muzyczka, N.2
  • 32
    • 0031048047 scopus 로고    scopus 로고
    • The cellular transcription factor SP1 and an unknown cellular protein are required to mediate Rep protein activation of the adeno-associated virus p19 promoter
    • Pereira DJ, Muzyczka N (1997) The cellular transcription factor SP1 and an unknown cellular protein are required to mediate Rep protein activation of the adeno-associated virus p19 promoter. J Virol 71: 1747-1756.
    • (1997) J Virol , vol.71 , pp. 1747-1756
    • Pereira, D.J.1    Muzyczka, N.2
  • 33
    • 0025946426 scopus 로고
    • Sequences required for coordinate induction of adeno-associated virus p19 and p40 promoters by Rep protein
    • McCarty DM, Christensen M, Muzyczka N (1991) Sequences required for coordinate induction of adeno-associated virus p19 and p40 promoters by Rep protein. J Virol 65: 2936-2945.
    • (1991) J Virol , vol.65 , pp. 2936-2945
    • McCarty, D.M.1    Christensen, M.2    Muzyczka, N.3
  • 34
    • 0030862039 scopus 로고    scopus 로고
    • Control of adeno-associated virus type 2 cap gene expression: Relative influence of helper virus, terminal repeats, and Rep proteins
    • Weger S, Wistuba A, Grimm D, Kleinschmidt JA (1997) Control of adeno-associated virus type 2 cap gene expression: relative influence of helper virus, terminal repeats, and Rep proteins. J Virol 71: 8437-8447.
    • (1997) J Virol , vol.71 , pp. 8437-8447
    • Weger, S.1    Wistuba, A.2    Grimm, D.3    Kleinschmidt, J.A.4
  • 35
    • 0032826095 scopus 로고    scopus 로고
    • Adeno-associated virus type 2 protein interactions: Formation of pre-encapsidation complexes
    • Dubielzig R, King JA, Weger S, Kern A, Kleinschmidt JA (1999) Adeno-associated virus type 2 protein interactions: formation of pre-encapsidation complexes. J Virol 73: 8989-8998.
    • (1999) J Virol , vol.73 , pp. 8989-8998
    • Dubielzig, R.1    King, J.A.2    Weger, S.3    Kern, A.4    Kleinschmidt, J.A.5
  • 36
    • 0035875669 scopus 로고    scopus 로고
    • DNA helicase-mediated packaging of adeno-associated virus type 2 genomes into preformed capsids
    • King JA, Dubielzig R, Grimm D, Kleinschmidt JA (2001) DNA helicase-mediated packaging of adeno-associated virus type 2 genomes into preformed capsids. EMBO J 20: 3282-3291.
    • (2001) EMBO J , vol.20 , pp. 3282-3291
    • King, J.A.1    Dubielzig, R.2    Grimm, D.3    Kleinschmidt, J.A.4
  • 38
    • 0026070440 scopus 로고
    • Targeted integration of adeno-associated virus (AAV) into human chromosome 19
    • Samulski RJ, Zhu X, Xiao X, Brook JD, Housman DE, et al. (1991) Targeted integration of adeno-associated virus (AAV) into human chromosome 19. Embo J 10: 3941-3950.
    • (1991) Embo J , vol.10 , pp. 3941-3950
    • Samulski, R.J.1    Zhu, X.2    Xiao, X.3    Brook, J.D.4    Housman, D.E.5
  • 39
    • 0030896361 scopus 로고    scopus 로고
    • Adeno-associated virus Rep78 protein and terminal repeats enhance integration of DNA sequences into the cellular genome
    • Balague C, Kalla M, Zhang WW (1997) Adeno-associated virus Rep78 protein and terminal repeats enhance integration of DNA sequences into the cellular genome. J Virol 71: 3299-3306.
    • (1997) J Virol , vol.71 , pp. 3299-3306
    • Balague, C.1    Kalla, M.2    Zhang, W.W.3
  • 40
    • 0037125986 scopus 로고    scopus 로고
    • A p5 integration efficiency element mediates Rep-dependent integration into AAVS1 at chromosome 19
    • Philpott NJ, Gomos J, Berns KI, Falck-Pedersen E (2002) A p5 integration efficiency element mediates Rep-dependent integration into AAVS1 at chromosome 19. Proc Natl Acad Sci U S A 99: 12381-12385.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 12381-12385
    • Philpott, N.J.1    Gomos, J.2    Berns, K.I.3    Falck-Pedersen, E.4
  • 41
    • 34249801792 scopus 로고    scopus 로고
    • Purification of host cell enzymes involved in adeno-associated virus DNA replication
    • Nash K, Chen W, McDonald WF, Zhou X, Muzyczka N (2007) Purification of host cell enzymes involved in adeno-associated virus DNA replication. J Virol 81: 5777-5787.
    • (2007) J Virol , vol.81 , pp. 5777-5787
    • Nash, K.1    Chen, W.2    McDonald, W.F.3    Zhou, X.4    Muzyczka, N.5
  • 42
    • 38349096769 scopus 로고    scopus 로고
    • Complete in vitro reconstitution of adeno-associated virus DNA replication requires the minichromosome maintenance complex proteins
    • Nash K, Chen W, Muzyczka N (2008) Complete in vitro reconstitution of adeno-associated virus DNA replication requires the minichromosome maintenance complex proteins. J Virol 82: 1458-1464.
    • (2008) J Virol , vol.82 , pp. 1458-1464
    • Nash, K.1    Chen, W.2    Muzyczka, N.3
  • 43
    • 0031901455 scopus 로고    scopus 로고
    • Cellular proteins required for adeno-associated virus DNA replication in the absence of adenovirus coinfection
    • Ni TH, McDonald WF, Zolotukhin I, Melendy T, Waga S, et al. (1998) Cellular proteins required for adeno-associated virus DNA replication in the absence of adenovirus coinfection. J Virol 72: 2777-2787.
    • (1998) J Virol , vol.72 , pp. 2777-2787
    • Ni, T.H.1    McDonald, W.F.2    Zolotukhin, I.3    Melendy, T.4    Waga, S.5
  • 44
    • 10744231280 scopus 로고    scopus 로고
    • The Rep protein of adeno-associated virus type 2 interacts with single-stranded DNA-binding proteins that enhance viral replication
    • Stracker TH, Cassell GD, Ward P, Loo YM, van Breukelen B, et al. (2004) The Rep protein of adeno-associated virus type 2 interacts with single-stranded DNA-binding proteins that enhance viral replication. J Virol 78: 441-453.
    • (2004) J Virol , vol.78 , pp. 441-453
    • Stracker, T.H.1    Cassell, G.D.2    Ward, P.3    Loo, Y.M.4    van Breukelen, B.5
  • 45
    • 58149376502 scopus 로고    scopus 로고
    • Identification of cellular proteins that interact with the adeno-associated virus rep protein
    • Nash K, Chen W, Salganik M, Muzyczka N (2009) Identification of cellular proteins that interact with the adeno-associated virus rep protein. J Virol 83: 454-469.
    • (2009) J Virol , vol.83 , pp. 454-469
    • Nash, K.1    Chen, W.2    Salganik, M.3    Muzyczka, N.4
  • 46
    • 0025820474 scopus 로고
    • A subset of herpes simplex virus replication genes provides helper functions for productive adeno-associated virus replication
    • Weindler FW, Heilbronn R (1991) A subset of herpes simplex virus replication genes provides helper functions for productive adeno-associated virus replication. J Virol 65: 2476-2483.
    • (1991) J Virol , vol.65 , pp. 2476-2483
    • Weindler, F.W.1    Heilbronn, R.2
  • 47
    • 33646733648 scopus 로고    scopus 로고
    • Role of the herpes simplex virus helicase-primase complex during adeno-associated virus DNA replication
    • Slanina H, Weger S, Stow ND, Kuhrs A, Heilbronn R (2006) Role of the herpes simplex virus helicase-primase complex during adeno-associated virus DNA replication. J Virol 80: 5241-5250.
    • (2006) J Virol , vol.80 , pp. 5241-5250
    • Slanina, H.1    Weger, S.2    Stow, N.D.3    Kuhrs, A.4    Heilbronn, R.5
  • 48
    • 63449112088 scopus 로고    scopus 로고
    • Definition of herpes simplex virus type 1 helper activities for adeno-associated virus early replication events
    • Alazard-Dany N, Nicolas A, Ploquin A, Strasser R, Greco A, et al. (2009) Definition of herpes simplex virus type 1 helper activities for adeno-associated virus early replication events. PLoS Pathog 5: e1000340.
    • (2009) PLoS Pathog , vol.5
    • Alazard-Dany, N.1    Nicolas, A.2    Ploquin, A.3    Strasser, R.4    Greco, A.5
  • 49
    • 13644257036 scopus 로고    scopus 로고
    • Identification of a replication-defective herpes simplex virus for recombinant adeno-associated virus type 2 (rAAV2) particle assembly using stable producer cell lines
    • Toublanc E, Benraiss A, Bonnin D, Blouin V, Brument N, et al. (2004) Identification of a replication-defective herpes simplex virus for recombinant adeno-associated virus type 2 (rAAV2) particle assembly using stable producer cell lines. J Gene Med 6: 555-564.
    • (2004) J Gene Med , vol.6 , pp. 555-564
    • Toublanc, E.1    Benraiss, A.2    Bonnin, D.3    Blouin, V.4    Brument, N.5
  • 50
    • 13144305062 scopus 로고    scopus 로고
    • Sustained secretion of human alpha-1-antitrypsin from murine muscle transduced with adeno-associated virus vectors
    • Song S, Morgan M, Ellis T, Poirier A, Chesnut K, et al. (1998) Sustained secretion of human alpha-1-antitrypsin from murine muscle transduced with adeno-associated virus vectors. Proc Natl Acad Sci U S A 95: 14384-14388.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 14384-14388
    • Song, S.1    Morgan, M.2    Ellis, T.3    Poirier, A.4    Chesnut, K.5
  • 51
    • 1242319264 scopus 로고    scopus 로고
    • DNA-dependent PK inhibits adeno-associated virus DNA integration
    • Song S, Lu Y, Choi YK, Han Y, Tang Q, et al. (2004) DNA-dependent PK inhibits adeno-associated virus DNA integration. Proc Natl Acad Sci U S A 101: 2112-2116.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 2112-2116
    • Song, S.1    Lu, Y.2    Choi, Y.K.3    Han, Y.4    Tang, Q.5
  • 52
    • 0030827207 scopus 로고    scopus 로고
    • Recombinant adeno-associated virus type 2 replication and packaging is entirely supported by a herpes simplex virus type 1 amplicon expressing Rep and Cap
    • Conway JE, Zolotukhin S, Muzyczka N, Hayward GS, Byrne BJ (1997) Recombinant adeno-associated virus type 2 replication and packaging is entirely supported by a herpes simplex virus type 1 amplicon expressing Rep and Cap. J Virol 71: 8780-8789.
    • (1997) J Virol , vol.71 , pp. 8780-8789
    • Conway, J.E.1    Zolotukhin, S.2    Muzyczka, N.3    Hayward, G.S.4    Byrne, B.J.5
  • 53
    • 0024697626 scopus 로고
    • The inhibition of prostaglandin E1-induced corneal neovascularization by steroid eye drops
    • Chang CT, Chen YL, Lee SH, Lue CM, Lin MT (1989) The inhibition of prostaglandin E1-induced corneal neovascularization by steroid eye drops. Taiwan Yi Xue Hui Za Zhi 88: 707-711.
    • (1989) Taiwan Yi Xue Hui Za Zhi , vol.88 , pp. 707-711
    • Chang, C.T.1    Chen, Y.L.2    Lee, S.H.3    Lue, C.M.4    Lin, M.T.5
  • 55
    • 0020086215 scopus 로고
    • Effect of deletions in adenovirus early region 1 genes upon replication of adeno-associated virus
    • Laughlin CA, Jones N, Carter BJ (1982) Effect of deletions in adenovirus early region 1 genes upon replication of adeno-associated virus. J Virol 41: 868-876.
    • (1982) J Virol , vol.41 , pp. 868-876
    • Laughlin, C.A.1    Jones, N.2    Carter, B.J.3
  • 56
    • 34547946751 scopus 로고    scopus 로고
    • Chk1 instability is coupled to mitotic cell death of p53-deficient cells in response to virus-induced DNA damage signaling
    • Jurvansuu J, Fragkos M, Ingemarsdotter C, Beard P (2007) Chk1 instability is coupled to mitotic cell death of p53-deficient cells in response to virus-induced DNA damage signaling. J Mol Biol 372: 397-406.
    • (2007) J Mol Biol , vol.372 , pp. 397-406
    • Jurvansuu, J.1    Fragkos, M.2    Ingemarsdotter, C.3    Beard, P.4
  • 57
    • 10644254331 scopus 로고    scopus 로고
    • Viral transport of DNA damage that mimics a stalled replication fork
    • Jurvansuu J, Raj K, Stasiak A, Beard P (2005) Viral transport of DNA damage that mimics a stalled replication fork. J Virol 79: 569-580.
    • (2005) J Virol , vol.79 , pp. 569-580
    • Jurvansuu, J.1    Raj, K.2    Stasiak, A.3    Beard, P.4
  • 58
    • 66149143110 scopus 로고    scopus 로고
    • Adeno-associated virus replication induces a DNA damage response coordinated by DNA-dependent protein kinase
    • Schwartz RA, Carson CT, Schuberth C, Weitzman MD (2009) Adeno-associated virus replication induces a DNA damage response coordinated by DNA-dependent protein kinase. J Virol 83: 6269-6278.
    • (2009) J Virol , vol.83 , pp. 6269-6278
    • Schwartz, R.A.1    Carson, C.T.2    Schuberth, C.3    Weitzman, M.D.4
  • 59
    • 0032889431 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 immediate-early protein vmw110 induces the proteasome-dependent degradation of the catalytic subunit of DNA-dependent protein kinase
    • Parkinson J, Lees-Miller SP, Everett RD (1999) Herpes simplex virus type 1 immediate-early protein vmw110 induces the proteasome-dependent degradation of the catalytic subunit of DNA-dependent protein kinase. J Virol 73: 650-657.
    • (1999) J Virol , vol.73 , pp. 650-657
    • Parkinson, J.1    Lees-Miller, S.P.2    Everett, R.D.3
  • 60
    • 0023018824 scopus 로고
    • Latent infection of KB cells with adeno-associated virus type 2
    • Laughlin CA, Cardellichio CB, Coon HC (1986) Latent infection of KB cells with adeno-associated virus type 2. J Virol 60: 515-524.
    • (1986) J Virol , vol.60 , pp. 515-524
    • Laughlin, C.A.1    Cardellichio, C.B.2    Coon, H.C.3
  • 61
    • 0023889191 scopus 로고
    • Adeno-associated virus general transduction vectors: Analysis of proviral structures
    • McLaughlin SK, Collis P, Hermonat PL, Muzyczka N (1988) Adeno-associated virus general transduction vectors: analysis of proviral structures. J Virol 62: 1963-1973.
    • (1988) J Virol , vol.62 , pp. 1963-1973
    • McLaughlin, S.K.1    Collis, P.2    Hermonat, P.L.3    Muzyczka, N.4
  • 62
    • 0034004021 scopus 로고    scopus 로고
    • Mutational analysis of adeno-associated virus type 2 Rep68 protein endonuclease activity on partially single-stranded substrates
    • Davis MD, Wu J, Owens RA (2000) Mutational analysis of adeno-associated virus type 2 Rep68 protein endonuclease activity on partially single-stranded substrates. J Virol 74: 2936-2942.
    • (2000) J Virol , vol.74 , pp. 2936-2942
    • Davis, M.D.1    Wu, J.2    Owens, R.A.3
  • 63
    • 0033052212 scopus 로고    scopus 로고
    • Analysis of the effects of charge cluster mutations in adeno-associated virus Rep68 protein in vitro
    • Davis MD, Wonderling RS, Walker SL, Owens RA (1999) Analysis of the effects of charge cluster mutations in adeno-associated virus Rep68 protein in vitro. J Virol 73: 2084-2093.
    • (1999) J Virol , vol.73 , pp. 2084-2093
    • Davis, M.D.1    Wonderling, R.S.2    Walker, S.L.3    Owens, R.A.4
  • 64
    • 0032826397 scopus 로고    scopus 로고
    • Factors affecting the terminal resolution site endonuclease, helicase, and ATPase activities of adeno-associated virus type 2 Rep proteins
    • Wu J, Davis MD, Owens RA (1999) Factors affecting the terminal resolution site endonuclease, helicase, and ATPase activities of adeno-associated virus type 2 Rep proteins. J Virol 73: 8235-8244.
    • (1999) J Virol , vol.73 , pp. 8235-8244
    • Wu, J.1    Davis, M.D.2    Owens, R.A.3
  • 65
    • 0030896669 scopus 로고    scopus 로고
    • Mutational analysis of the adeno-associated virus Rep68 protein: Identification of critical residues necessary for site-specific endonuclease activity
    • Walker SL, Wonderling RS, Owens RA (1997) Mutational analysis of the adeno-associated virus Rep68 protein: identification of critical residues necessary for site-specific endonuclease activity. J Virol 71: 2722-2730.
    • (1997) J Virol , vol.71 , pp. 2722-2730
    • Walker, S.L.1    Wonderling, R.S.2    Owens, R.A.3
  • 66
    • 0030846525 scopus 로고    scopus 로고
    • Mutational analysis of the adeno-associated virus type 2 Rep68 protein helicase motifs
    • Walker SL, Wonderling RS, Owens RA (1997) Mutational analysis of the adeno-associated virus type 2 Rep68 protein helicase motifs. J Virol 71: 6996-7004.
    • (1997) J Virol , vol.71 , pp. 6996-7004
    • Walker, S.L.1    Wonderling, R.S.2    Owens, R.A.3
  • 67
    • 0028290387 scopus 로고
    • Identification of linear DNA sequences that specifically bind the adeno-associated virus Rep protein
    • McCarty DM, Pereira DJ, Zolotukhin I, Zhou X, Ryan JH, et al. (1994) Identification of linear DNA sequences that specifically bind the adeno-associated virus Rep protein. J Virol 68: 4988-4997.
    • (1994) J Virol , vol.68 , pp. 4988-4997
    • McCarty, D.M.1    Pereira, D.J.2    Zolotukhin, I.3    Zhou, X.4    Ryan, J.H.5
  • 68
    • 0030026754 scopus 로고    scopus 로고
    • Sequence requirements for binding of Rep68 to the adeno-associated virus terminal repeats
    • Ryan JH, Zolotukhin S, Muzyczka N (1996) Sequence requirements for binding of Rep68 to the adeno-associated virus terminal repeats. J Virol 70: 1542-1553.
    • (1996) J Virol , vol.70 , pp. 1542-1553
    • Ryan, J.H.1    Zolotukhin, S.2    Muzyczka, N.3
  • 69
    • 0023947989 scopus 로고
    • DNA amplification of adeno-associated virus as a response to cellular genotoxic stress
    • Yalkinoglu AO, Heilbronn R, Burkle A, Schlehofer JR, zur Hausen H (1988) DNA amplification of adeno-associated virus as a response to cellular genotoxic stress. Cancer Res 48: 3123-3129.
    • (1988) Cancer Res , vol.48 , pp. 3123-3129
    • Yalkinoglu, A.O.1    Heilbronn, R.2    Burkle, A.3    Schlehofer, J.R.4    Hausen, H.Z.5
  • 70
    • 0031965318 scopus 로고    scopus 로고
    • Role of the adenovirus DNA-binding protein in in vitro adeno-associated virus DNA replication
    • Ward P, Dean FB, O'Donnell ME, Berns KI (1998) Role of the adenovirus DNA-binding protein in in vitro adeno-associated virus DNA replication. J Virol 72: 420-427.
    • (1998) J Virol , vol.72 , pp. 420-427
    • Ward, P.1    Dean, F.B.2    O'Donnell, M.E.3    Berns, K.I.4
  • 71
    • 0034790801 scopus 로고    scopus 로고
    • Rep-dependent initiation of adeno-associated virus type 2 DNA replication by a herpes simplex virus type 1 replication complex in a reconstituted system
    • Ward P, Falkenberg M, Elias P, Weitzman M, Linden RM (2001) Rep-dependent initiation of adeno-associated virus type 2 DNA replication by a herpes simplex virus type 1 replication complex in a reconstituted system. J Virol 75: 10250-10258.
    • (2001) J Virol , vol.75 , pp. 10250-10258
    • Ward, P.1    Falkenberg, M.2    Elias, P.3    Weitzman, M.4    Linden, R.M.5
  • 72
    • 0035194442 scopus 로고    scopus 로고
    • Involvement of cellular double-stranded DNA break binding proteins in processing of the recombinant adeno-associated virus genome
    • Zentilin L, Marcello A, Giacca M (2001) Involvement of cellular double-stranded DNA break binding proteins in processing of the recombinant adeno-associated virus genome. J Virol 75: 12279-12287.
    • (2001) J Virol , vol.75 , pp. 12279-12287
    • Zentilin, L.1    Marcello, A.2    Giacca, M.3
  • 73
    • 33646160992 scopus 로고    scopus 로고
    • The biology of Ku and its potential oncogenic role in cancer
    • Gullo C, Au M, Feng G, Teoh G (2006) The biology of Ku and its potential oncogenic role in cancer. Biochim Biophys Acta 1765: 223-234.
    • (2006) Biochim Biophys Acta , vol.1765 , pp. 223-234
    • Gullo, C.1    Au, M.2    Feng, G.3    Teoh, G.4
  • 75
    • 0043133778 scopus 로고    scopus 로고
    • Autopho-sphorylation 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 YV, Wang W, Woods T, Douglas P, et al. (2003) Autopho-sphorylation 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: 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
  • 76
    • 4043073590 scopus 로고    scopus 로고
    • Autopho-sphorylation-dependent remodeling of the DNA-dependent protein kinase catalytic subunit regulates ligation of DNA ends
    • Block WD, Yu Y, Merkle D, Gifford JL, Ding Q, et al. (2004) Autopho-sphorylation-dependent remodeling of the DNA-dependent protein kinase catalytic subunit regulates ligation of DNA ends. Nucleic Acids Res 32: 4351-4357.
    • (2004) Nucleic Acids Res , vol.32 , pp. 4351-4357
    • Block, W.D.1    Yu, Y.2    Merkle, D.3    Gifford, J.L.4    Ding, Q.5
  • 77
    • 0028116725 scopus 로고
    • Human DNA helicase II: A novel DNA unwinding enzyme identified as the Ku autoantigen
    • Tuteja N, Tuteja R, Ochem A, Taneja P, Huang NW, et al. (1994) Human DNA helicase II: a novel DNA unwinding enzyme identified as the Ku autoantigen. EMBO J 13: 4991-5001.
    • (1994) EMBO J , vol.13 , pp. 4991-5001
    • Tuteja, N.1    Tuteja, R.2    Ochem, A.3    Taneja, P.4    Huang, N.W.5
  • 78
    • 0037383480 scopus 로고    scopus 로고
    • Consequences of DNA-dependent protein kinase catalytic subunit deficiency on recombinant adeno-associated virus genome circularization and heterodimerization in muscle tissue
    • Duan D, Yue Y, Engelhardt JF (2003) Consequences of DNA-dependent protein kinase catalytic subunit deficiency on recombinant adeno-associated virus genome circularization and heterodimerization in muscle tissue. J Virol 77: 4751-4759.
    • (2003) J Virol , vol.77 , pp. 4751-4759
    • Duan, D.1    Yue, Y.2    Engelhardt, J.F.3
  • 79
    • 0035957384 scopus 로고    scopus 로고
    • Effect of DNA-dependent protein kinase on the molecular fate of the rAAV2 genome in skeletal muscle
    • Song S, Laipis PJ, Berns KI, Flotte TR (2001) Effect of DNA-dependent protein kinase on the molecular fate of the rAAV2 genome in skeletal muscle. Proc Natl Acad Sci U S A 98: 4084-4088.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 4084-4088
    • Song, S.1    Laipis, P.J.2    Berns, K.I.3    Flotte, T.R.4
  • 80
    • 33750357800 scopus 로고    scopus 로고
    • Host cell DNA repair pathways in adeno-associated viral genome processing
    • Choi VW, McCarty DM, Samulski RJ (2006) Host cell DNA repair pathways in adeno-associated viral genome processing. J Virol 80: 10346-10356.
    • (2006) J Virol , vol.80 , pp. 10346-10356
    • Choi, V.W.1    McCarty, D.M.2    Samulski, R.J.3
  • 81
    • 35148863458 scopus 로고    scopus 로고
    • The role of DNA-PKcs and artemis in opening viral DNA hairpin termini in various tissues in mice
    • Inagaki K, Ma C, Storm TA, Kay MA, Nakai H (2007) The role of DNA-PKcs and artemis in opening viral DNA hairpin termini in various tissues in mice. J Virol 81: 11304-11321.
    • (2007) J Virol , vol.81 , pp. 11304-11321
    • Inagaki, K.1    Ma, C.2    Storm, T.A.3    Kay, M.A.4    Nakai, H.5
  • 82
    • 0037130170 scopus 로고    scopus 로고
    • Adenovirus oncoproteins inactivate the Mre11-Rad50-NBS1 DNA repair complex
    • Stracker TH, Carson CT, Weitzman MD (2002) Adenovirus oncoproteins inactivate the Mre11-Rad50-NBS1 DNA repair complex. Nature 418: 348-352.
    • (2002) Nature , vol.418 , pp. 348-352
    • Stracker, T.H.1    Carson, C.T.2    Weitzman, M.D.3
  • 83
    • 36348963101 scopus 로고    scopus 로고
    • The Mre11/Rad50/Nbs1 complex limits adeno-associated virus transduction and replication
    • Schwartz RA, Palacios JA, Cassell GD, Adam S, Giacca M, et al. (2007) The Mre11/Rad50/Nbs1 complex limits adeno-associated virus transduction and replication. J Virol 81: 12936-12945.
    • (2007) J Virol , vol.81 , pp. 12936-12945
    • Schwartz, R.A.1    Palacios, J.A.2    Cassell, G.D.3    Adam, S.4    Giacca, M.5
  • 84
    • 0347157844 scopus 로고    scopus 로고
    • Mcm4,6,7 uses a ''pump in ring'' mechanism to unwind DNA by steric exclusion and actively translocate along a duplex
    • Kaplan DL, Davey MJ, O'Donnell M (2003) Mcm4,6,7 uses a ''pump in ring'' mechanism to unwind DNA by steric exclusion and actively translocate along a duplex. J Biol Chem 278: 49171-49182.
    • (2003) J Biol Chem , vol.278 , pp. 49171-49182
    • Kaplan, D.L.1    Davey, M.J.2    O'Donnell, M.3
  • 85
    • 0032954382 scopus 로고    scopus 로고
    • Biochemical characterization of adeno-associated virus rep68 DNA helicase and ATPase activities
    • Zhou X, Zolotukhin I, Im DS, Muzyczka N (1999) Biochemical characterization of adeno-associated virus rep68 DNA helicase and ATPase activities. J Virol 73: 1580-1590.
    • (1999) J Virol , vol.73 , pp. 1580-1590
    • Zhou, X.1    Zolotukhin, I.2    Im, D.S.3    Muzyczka, N.4
  • 86
    • 0029995531 scopus 로고    scopus 로고
    • A ''humanized'' green fluorescent protein cDNA adapted for high-level expression in mammalian cells
    • Zolotukhin S, Potter M, Hauswirth WW, Guy J, Muzyczka N (1996) A ''humanized'' green fluorescent protein cDNA adapted for high-level expression in mammalian cells. J Virol 70: 4646-4654.
    • (1996) J Virol , vol.70 , pp. 4646-4654
    • Zolotukhin, S.1    Potter, M.2    Hauswirth, W.W.3    Guy, J.4    Muzyczka, N.5
  • 87
    • 0037112508 scopus 로고    scopus 로고
    • Silencing expression of the catalytic subunit of DNA-dependent protein kinase by small interfering RNA sensitizes human cells for radiation-induced chromosome damage, cell killing, and mutation
    • Peng Y, Zhang Q, Nagasawa H, Okayasu R, Liber HL, et al. (2002) Silencing expression of the catalytic subunit of DNA-dependent protein kinase by small interfering RNA sensitizes human cells for radiation-induced chromosome damage, cell killing, and mutation. Cancer Res 62: 6400-6404.
    • (2002) Cancer Res , vol.62 , pp. 6400-6404
    • Peng, Y.1    Zhang, Q.2    Nagasawa, H.3    Okayasu, R.4    Liber, H.L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.