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Volumn 17, Issue 9, 2010, Pages 1144-1151

Human HDAC1 and HDAC2 function in the DNA-damage response to promote DNA nonhomologous end-joining

Author keywords

[No Author keywords available]

Indexed keywords

DOUBLE STRANDED DNA; HISTONE DEACETYLASE 1; HISTONE DEACETYLASE 2; HISTONE H3; HDAC1 PROTEIN, HUMAN; HDAC2 PROTEIN, HUMAN; HISTONE; SMALL INTERFERING RNA;

EID: 77956341931     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb.1899     Document Type: Article
Times cited : (532)

References (60)
  • 1
    • 70350504453 scopus 로고    scopus 로고
    • The DNA-damage response in human biology and disease
    • Jackson, S.P. & Bartek, J. The DNA-damage response in human biology and disease. Nature 461, 1071-1078 (2009).
    • (2009) Nature , vol.461 , pp. 1071-1078
    • Jackson, S.P.1    Bartek, J.2
  • 2
    • 36749022214 scopus 로고    scopus 로고
    • The DNA damage response: Ten years after
    • Harper, J.W. & Elledge, S.J. The DNA damage response: ten years after. Mol. Cell 28, 739-745 (2007).
    • (2007) Mol. Cell , vol.28 , pp. 739-745
    • Harper, J.W.1    Elledge, S.J.2
  • 3
    • 77449086623 scopus 로고    scopus 로고
    • DNA resection in eukaryotes: Deciding how to fx the break
    • Huertas, P. DNA resection in eukaryotes: deciding how to fx the break. Nat. Struct. Mol. Biol. 17, 11-16 (2010).
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 11-16
    • Huertas, P.1
  • 4
    • 0027397867 scopus 로고
    • The DNA-dependent protein kinase: Requirement for DNA ends and association with Ku antigen
    • Gottlieb, T.M. & Jackson, S.P. The DNA-dependent protein kinase: requirement for DNA ends and association with Ku antigen. Cell 72, 131-142 (1993).
    • (1993) Cell , vol.72 , pp. 131-142
    • Gottlieb, T.M.1    Jackson, S.P.2
  • 5
    • 59849089955 scopus 로고    scopus 로고
    • Repair of ionizing radiation-induced DNA double-strand breaks by non-homologous end-joining
    • Mahaney, B.L., Meek, K. & Lees-Miller, S.P. Repair of ionizing radiation-induced DNA double-strand breaks by non-homologous end-joining. Biochem. J. 417, 639-650 (2009).
    • (2009) Biochem. J. , vol.417 , pp. 639-650
    • Mahaney, B.L.1    Meek, K.2    Lees-Miller, S.P.3
  • 6
    • 34250820438 scopus 로고    scopus 로고
    • Chromatin dynamics and the preservation of genetic information
    • Downs, J.A., Nussenzweig, M.C. & Nussenzweig, A. Chromatin dynamics and the preservation of genetic information. Nature 447, 951-958 (2007).
    • (2007) Nature , vol.447 , pp. 951-958
    • Downs, J.A.1    Nussenzweig, M.C.2    Nussenzweig, A.3
  • 7
    • 33847076248 scopus 로고    scopus 로고
    • Chromatin challenges during DNA replication and repair
    • Groth, A., Rocha, W., Verreault, A. & Almouzni, G. Chromatin challenges during DNA replication and repair. Cell 128, 721-733 (2007).
    • (2007) Cell , vol.128 , pp. 721-733
    • Groth, A.1    Rocha, W.2    Verreault, A.3    Almouzni, G.4
  • 8
    • 62849083222 scopus 로고    scopus 로고
    • The emerging role of nuclear architecture in DNA repair and genome maintenance
    • Misteli, T. & Soutoglou, E. The emerging role of nuclear architecture in DNA repair and genome maintenance. Nat. Rev. Mol. Cell Biol. 10, 243-254 (2009).
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 243-254
    • Misteli, T.1    Soutoglou, E.2
  • 9
    • 33847076849 scopus 로고    scopus 로고
    • Chromatin modifcations and their function
    • Kouzarides, T. Chromatin modifcations and their function. Cell 128, 693-705 (2007).
    • (2007) Cell , vol.128 , pp. 693-705
    • Kouzarides, T.1
  • 10
    • 57149136324 scopus 로고    scopus 로고
    • γh2AX and cancer
    • Bonner, W.M. et al. γH2AX and cancer. Nat. Rev. Cancer 8, 957-967 (2008).
    • (2008) Nat. Rev. Cancer , vol.8 , pp. 957-967
    • Bonner, W.M.1
  • 11
    • 33646106590 scopus 로고    scopus 로고
    • γh2AX and MDC1: Anchoring the DNA-damage-response machinery to broken chromosomes
    • Stucki, M. & Jackson, S.P. γH2AX and MDC1: anchoring the DNA-damage-response machinery to broken chromosomes. DNA Repair (Amst.) 5, 534-543 (2006).
    • (2006) DNA Repair (Amst.) , vol.5 , pp. 534-543
    • Stucki, M.1    Jackson, S.P.2
  • 12
    • 59049091728 scopus 로고    scopus 로고
    • RNF168 binds and amplifes ubiquitin conjugates on damaged chromosomes to allow accumulation of repair proteins
    • Doil, C. et al. RNF168 binds and amplifes ubiquitin conjugates on damaged chromosomes to allow accumulation of repair proteins. Cell 136, 435-446 (2009).
    • (2009) Cell , vol.136 , pp. 435-446
    • Doil, C.1
  • 13
    • 36249031962 scopus 로고    scopus 로고
    • RNF8 transduces the DNA-damage signal via histone ubiquitylation and checkpoint protein assembly
    • Huen, M.S. et al. RNF8 transduces the DNA-damage signal via histone ubiquitylation and checkpoint protein assembly. Cell 131, 901-914 (2007).
    • (2007) Cell , vol.131 , pp. 901-914
    • Huen, M.S.1
  • 14
    • 36248966246 scopus 로고    scopus 로고
    • RNF8 ubiquitylates histones at DNA double-strand breaks and promotes assembly of repair proteins
    • Mailand, N. et al. RNF8 ubiquitylates histones at DNA double-strand breaks and promotes assembly of repair proteins. Cell 131, 887-900 (2007).
    • (2007) Cell , vol.131 , pp. 887-900
    • Mailand, N.1
  • 15
    • 36749084931 scopus 로고    scopus 로고
    • Orchestration of the DNA-damage response by the RNF8 ubiquitin ligase
    • Kolas, N.K. et al. Orchestration of the DNA-damage response by the RNF8 ubiquitin ligase. Science 318, 1637-1640 (2007).
    • (2007) Science , vol.318 , pp. 1637-1640
    • Kolas, N.K.1
  • 16
    • 59049103900 scopus 로고    scopus 로고
    • The RIDDLE syndrome protein mediates a ubiquitin-dependent signaling cascade at sites of DNA damage
    • Stewart, G.S. et al. The RIDDLE syndrome protein mediates a ubiquitin-dependent signaling cascade at sites of DNA damage. Cell 136, 420-434 (2009).
    • (2009) Cell , vol.136 , pp. 420-434
    • Stewart, G.S.1
  • 18
    • 67650462882 scopus 로고    scopus 로고
    • A histone code for the DNA damage response in mammalian cells?
    • Corpet, A. & Almouzni, G. A histone code for the DNA damage response in mammalian cells? EMBO J. 28, 1828-1830 (2009).
    • (2009) EMBO J. , vol.28 , pp. 1828-1830
    • Corpet, A.1    Almouzni, G.2
  • 19
    • 30344444484 scopus 로고    scopus 로고
    • Histone acetylation by Trrap-Tip60 modulates loading of repair proteins and repair of DNA double-strand breaks
    • Murr, R. et al. Histone acetylation by Trrap-Tip60 modulates loading of repair proteins and repair of DNA double-strand breaks. Nat. Cell Biol. 8, 91-99 (2006).
    • (2006) Nat. Cell Biol. , vol.8 , pp. 91-99
    • Murr, R.1
  • 20
    • 67650409769 scopus 로고    scopus 로고
    • Screen for DNA-damage-responsive histone modifcations identifes H3K9Ac and H3K56Ac in human cells
    • Tjeertes, J.V., Miller, K.M. & Jackson, S.P. Screen for DNA-damage-responsive histone modifcations identifes H3K9Ac and H3K56Ac in human cells. EMBO J. 28, 1878-1889 (2009).
    • (2009) EMBO J. , vol.28 , pp. 1878-1889
    • Tjeertes, J.V.1    Miller, K.M.2    Jackson, S.P.3
  • 21
    • 69249221533 scopus 로고    scopus 로고
    • Cell cycle-dependent deacetylation of telomeric histone H3 lysine K56 by human SIRT6
    • Michishita, E. et al. Cell cycle-dependent deacetylation of telomeric histone H3 lysine K56 by human SIRT6. Cell Cycle 8, 2664-2666 (2009).
    • (2009) Cell Cycle , vol.8 , pp. 2664-2666
    • Michishita, E.1
  • 22
    • 65549113750 scopus 로고    scopus 로고
    • CBP/p300-mediated acetylation of histone H3 on lysine 56
    • Das, C., Lucia, M.S., Hansen, K.C. & Tyler, J.K. CBP/p300-mediated acetylation of histone H3 on lysine 56. Nature 459, 113-117 (2009).
    • (2009) Nature , vol.459 , pp. 113-117
    • Das, C.1    Lucia, M.S.2    Hansen, K.C.3    Tyler, J.K.4
  • 23
    • 69249229772 scopus 로고    scopus 로고
    • The sirtuin SIRT6 deacetylates H3 K56Ac in vivo to promote genomic stability
    • Yang, B., Zwaans, B.M., Eckersdorff, M. & Lombard, D.B. The sirtuin SIRT6 deacetylates H3 K56Ac in vivo to promote genomic stability. Cell Cycle 8, 2662-2663 (2009).
    • (2009) Cell Cycle , vol.8 , pp. 2662-2663
    • Yang, B.1    Zwaans, B.M.2    Eckersdorff, M.3    Lombard, D.B.4
  • 24
    • 34547897023 scopus 로고    scopus 로고
    • Histone deacetylases and cancer
    • Glozak, M.A. & Seto, E. Histone deacetylases and cancer. Oncogene 26, 5420-5432 (2007).
    • (2007) Oncogene , vol.26 , pp. 5420-5432
    • Glozak, M.A.1    Seto, E.2
  • 25
    • 39749127166 scopus 로고    scopus 로고
    • The Rpd3/Hda1 family of lysine deacetylases: From bacteria and yeast to mice and men
    • Yang, X.J. & Seto, E. The Rpd3/Hda1 family of lysine deacetylases: from bacteria and yeast to mice and men. Nat. Rev. Mol. Cell Biol. 9, 206-218 (2008).
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 206-218
    • Yang, X.J.1    Seto, E.2
  • 26
    • 77949887506 scopus 로고    scopus 로고
    • Mammalian sirtuins: Biological insights and disease relevance
    • Haigis, M.C. & Sinclair, D.A. Mammalian sirtuins: biological insights and disease relevance. Annu. Rev. Pathol. 5, 253-295 (2010).
    • (2010) Annu. Rev. Pathol. , vol.5 , pp. 253-295
    • Haigis, M.C.1    Sinclair, D.A.2
  • 27
    • 55949083044 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: Anticancer compounds
    • Smith, K.T. & Workman, J.L. Histone deacetylase inhibitors: anticancer compounds. Int. J. Biochem. Cell Biol. 41, 21-25 (2009).
    • (2009) Int. J. Biochem. Cell Biol. , vol.41 , pp. 21-25
    • Smith, K.T.1    Workman, J.L.2
  • 28
    • 34748877735 scopus 로고    scopus 로고
    • Inhibition of histone deacetylation: A strategy for tumor radiosensitization
    • Camphausen, K. & Toflon, P.J. Inhibition of histone deacetylation: a strategy for tumor radiosensitization. J. Clin. Oncol. 25, 4051-4056 (2007).
    • (2007) J. Clin. Oncol. , vol.25 , pp. 4051-4056
    • Camphausen, K.1    Toflon, P.J.2
  • 29
    • 77951498531 scopus 로고    scopus 로고
    • High-resolution profling of γ H2AX around DNA double strand breaks in the mammalian genome
    • Iacovoni, J.S. et al. High-resolution profling of γ H2AX around DNA double strand breaks in the mammalian genome. EMBO J. 29, 1446-1457 (2010).
    • (2010) EMBO J. , vol.29 , pp. 1446-1457
    • Iacovoni, J.S.1
  • 30
    • 0344441890 scopus 로고    scopus 로고
    • A DNA damage checkpoint response in telomere-initiated senescence
    • d'Adda di Fagagna, F. et al. A DNA damage checkpoint response in telomere-initiated senescence. Nature 426, 194-198 (2003).
    • (2003) Nature , vol.426 , pp. 194-198
    • D'Adda Di Fagagna, F.1
  • 31
    • 45849099050 scopus 로고    scopus 로고
    • Living on a break: Cellular senescence as a DNA-damage response
    • d'Adda di Fagagna, F. Living on a break: cellular senescence as a DNA-damage response. Nat. Rev. Cancer 8, 512-522 (2008).
    • (2008) Nat. Rev. Cancer , vol.8 , pp. 512-522
    • D'Adda Di Fagagna, F.1
  • 32
    • 33845235459 scopus 로고    scopus 로고
    • Oncogene-induced senescence is part of the tumorigenesis barrier imposed by DNA damage checkpoints
    • Bartkova, J. et al. Oncogene-induced senescence is part of the tumorigenesis barrier imposed by DNA damage checkpoints. Nature 444, 633-637 (2006).
    • (2006) Nature , vol.444 , pp. 633-637
    • Bartkova, J.1
  • 33
    • 33845269825 scopus 로고    scopus 로고
    • Oncogene-induced senescence is a DNA damage response triggered by DNA hyper-replication
    • Di Micco, R. et al. Oncogene-induced senescence is a DNA damage response triggered by DNA hyper-replication. Nature 444, 638-642 (2006).
    • (2006) Nature , vol.444 , pp. 638-642
    • Di Micco, R.1
  • 34
    • 0030944985 scopus 로고    scopus 로고
    • Oncogenic ras provokes premature cell senescence associated with accumulation of p53 and p16INK4a
    • Serrano, M., Lin, A.W., McCurrach, M.E., Beach, D. & Lowe, S.W. Oncogenic ras provokes premature cell senescence associated with accumulation of p53 and p16INK4a. Cell 88, 593-602 (1997).
    • (1997) Cell , vol.88 , pp. 593-602
    • Serrano, M.1    Lin, A.W.2    McCurrach, M.E.3    Beach, D.4    Lowe, S.W.5
  • 35
    • 60549111235 scopus 로고    scopus 로고
    • Histone h3 lysine 56 acetylation is linked to the core transcriptional network in human embryonic stem cells
    • Xie, W. et al. Histone h3 lysine 56 acetylation is linked to the core transcriptional network in human embryonic stem cells. Mol. Cell 33, 417-427 (2009).
    • (2009) Mol. Cell , vol.33 , pp. 417-427
    • Xie, W.1
  • 37
    • 0036829085 scopus 로고    scopus 로고
    • Down-regulation of p300/CBP histone acetyltransferase activates a senescence checkpoint in human melanocytes
    • Bandyopadhyay, D. et al. Down-regulation of p300/CBP histone acetyltransferase activates a senescence checkpoint in human melanocytes. Cancer Res. 62, 6231-6239 (2002).
    • (2002) Cancer Res. , vol.62 , pp. 6231-6239
    • Bandyopadhyay, D.1
  • 38
    • 66749102871 scopus 로고    scopus 로고
    • Histone H3-K56 acetylation is important for genomic stability in mammals
    • Yuan, J., Pu, M., Zhang, Z. & Lou, Z. Histone H3-K56 acetylation is important for genomic stability in mammals. Cell Cycle 8, 1747-1753 (2009).
    • (2009) Cell Cycle , vol.8 , pp. 1747-1753
    • Yuan, J.1    Pu, M.2    Zhang, Z.3    Lou, Z.4
  • 39
    • 33751226576 scopus 로고    scopus 로고
    • Taking it off: Regulation of H3 K56 acetylation by Hst3 and Hst4
    • Miller, K.M., Maas, N.L. & Toczyski, D.P. Taking it off: regulation of H3 K56 acetylation by Hst3 and Hst4. Cell Cycle 5, 2561-2565 (2006).
    • (2006) Cell Cycle , vol.5 , pp. 2561-2565
    • Miller, K.M.1    Maas, N.L.2    Toczyski, D.P.3
  • 40
    • 0035913911 scopus 로고    scopus 로고
    • Negative control of p53 by Sir2alpha promotes cell survival under stress
    • Luo, J. et al. Negative control of p53 by Sir2alpha promotes cell survival under stress. Cell 107, 137-148 (2001).
    • (2001) Cell , vol.107 , pp. 137-148
    • Luo, J.1
  • 41
    • 0141814680 scopus 로고    scopus 로고
    • Developmental defects and p53 hyperacetylation in Sir2 homolog (SIRT1)-defcient mice
    • Cheng, H.L. et al. Developmental defects and p53 hyperacetylation in Sir2 homolog (SIRT1)-defcient mice. Proc. Natl. Acad. Sci. USA 100, 10794-10799 (2003).
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 10794-10799
    • Cheng, H.L.1
  • 42
    • 77952348698 scopus 로고    scopus 로고
    • Histone deacetylase 1 (HDAC1), but not HDAC2, controls embryonic stem cell differentiation
    • Dovey, O.M., Foster, C.T. & Cowley, S.M. Histone deacetylase 1 (HDAC1), but not HDAC2, controls embryonic stem cell differentiation. Proc. Natl. Acad. Sci. USA 107, 8242-8247 (2010).
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 8242-8247
    • Dovey, O.M.1    Foster, C.T.2    Cowley, S.M.3
  • 43
    • 10744233671 scopus 로고    scopus 로고
    • Repair of and checkpoint response to topoisomerase I-mediated DNA damage
    • Pommier, Y. et al. Repair of and checkpoint response to topoisomerase I-mediated DNA damage. Mutat. Res. 532, 173-203 (2003).
    • (2003) Mutat. Res. , vol.532 , pp. 173-203
    • Pommier, Y.1
  • 44
    • 34247477667 scopus 로고    scopus 로고
    • Autophosphorylation of DNA-PKCS regulates its dynamics at DNA double-strand breaks
    • Uematsu, N. et al. Autophosphorylation of DNA-PKCS regulates its dynamics at DNA double-strand breaks. J. Cell Biol. 177, 219-229 (2007).
    • (2007) J. Cell Biol. , vol.177 , pp. 219-229
    • Uematsu, N.1
  • 45
    • 33845484385 scopus 로고    scopus 로고
    • Dynamic assembly of end-joining complexes requires interaction between Ku70/80 and XRCC4
    • Mari, P.O. et al. Dynamic assembly of end-joining complexes requires interaction between Ku70/80 and XRCC4. Proc. Natl. Acad. Sci. USA 103, 18597-18602 (2006).
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 18597-18602
    • Mari, P.O.1
  • 46
    • 0026785616 scopus 로고
    • Immunolocalization of Ku-proteins (p80/p70): Localization of p70 to nucleoli and periphery of both interphase nuclei and metaphase chromosomes
    • Higashiura, M., Shimizu, Y., Tanimoto, M., Morita, T. & Yagura, T. Immunolocalization of Ku-proteins (p80/p70): localization of p70 to nucleoli and periphery of both interphase nuclei and metaphase chromosomes. Exp. Cell Res. 201, 444-451 (1992).
    • (1992) Exp. Cell Res. , vol.201 , pp. 444-451
    • Higashiura, M.1    Shimizu, Y.2    Tanimoto, M.3    Morita, T.4    Yagura, T.5
  • 47
    • 0037179692 scopus 로고    scopus 로고
    • Acetylation of histone H4 by Esa1 is required for DNA double-strand break repair
    • Bird, A.W. et al. Acetylation of histone H4 by Esa1 is required for DNA double-strand break repair. Nature 419, 411-415 (2002).
    • (2002) Nature , vol.419 , pp. 411-415
    • Bird, A.W.1
  • 48
    • 1242342224 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae Sin3p facilitates DNA double-strand break repair
    • Jazayeri, A., McAinsh, A.D. & Jackson, S.P. Saccharomyces cerevisiae Sin3p facilitates DNA double-strand break repair. Proc. Natl. Acad. Sci. USA 101, 1644-1649 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 1644-1649
    • Jazayeri, A.1    McAinsh, A.D.2    Jackson, S.P.3
  • 49
    • 34447508456 scopus 로고    scopus 로고
    • Regulation of histone H3 lysine 56 acetylation in Schizosaccharomyces pombe
    • Xhemalce, B. et al. Regulation of histone H3 lysine 56 acetylation in Schizosaccharomyces pombe. J. Biol. Chem. 282, 15040-15047 (2007).
    • (2007) J. Biol. Chem. , vol.282 , pp. 15040-15047
    • Xhemalce, B.1
  • 50
    • 33847070442 scopus 로고    scopus 로고
    • The role of chromatin during transcription
    • Li, B., Carey, M. & Workman, J.L. The role of chromatin during transcription. Cell 128, 707-719 (2007).
    • (2007) Cell , vol.128 , pp. 707-719
    • Li, B.1    Carey, M.2    Workman, J.L.3
  • 51
    • 69449102464 scopus 로고    scopus 로고
    • Genome-wide mapping of HATs and HDACs reveals distinct functions in active and inactive genes
    • Wang, Z. et al. Genome-wide mapping of HATs and HDACs reveals distinct functions in active and inactive genes. Cell 138, 1019-1031 (2009).
    • (2009) Cell , vol.138 , pp. 1019-1031
    • Wang, Z.1
  • 52
    • 72449175818 scopus 로고    scopus 로고
    • Mammalian SUMO E3-ligases PIAS1 and PIAS4 promote responses to DNA double-strand breaks
    • Galanty, Y. et al. Mammalian SUMO E3-ligases PIAS1 and PIAS4 promote responses to DNA double-strand breaks. Nature 462, 935-939 (2009).
    • (2009) Nature , vol.462 , pp. 935-939
    • Galanty, Y.1
  • 53
    • 34249846884 scopus 로고    scopus 로고
    • Loading of the nonhomologous end joining factor, Ku, on protein-occluded DNA ends
    • Roberts, S.A. & Ramsden, D.A. Loading of the nonhomologous end joining factor, Ku, on protein-occluded DNA ends. J. Biol. Chem. 282, 10605-10613 (2007).
    • (2007) J. Biol. Chem. , vol.282 , pp. 10605-10613
    • Roberts, S.A.1    Ramsden, D.A.2
  • 54
    • 0033615547 scopus 로고    scopus 로고
    • Sensing of ionizing radiation-induced DNA damage by ATM through interaction with histone deacetylase
    • Kim, G.D. et al. Sensing of ionizing radiation-induced DNA damage by ATM through interaction with histone deacetylase. J. Biol. Chem. 274, 31127-31130 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 31127-31130
    • Kim, G.D.1
  • 55
    • 43249103898 scopus 로고    scopus 로고
    • Mutations in String/CDC25 inhibit cell cycle re-entry and neurodegeneration in a Drosophila model of Ataxia telangiectasia
    • Rimkus, S.A. et al. Mutations in String/CDC25 inhibit cell cycle re-entry and neurodegeneration in a Drosophila model of Ataxia telangiectasia. Genes Dev. 22, 1205-1220 (2008).
    • (2008) Genes Dev. , vol.22 , pp. 1205-1220
    • Rimkus, S.A.1
  • 56
    • 47349107760 scopus 로고    scopus 로고
    • ATM signaling facilitates repair of DNA double-strand breaks associated with heterochromatin
    • Goodarzi, A.A. et al. ATM signaling facilitates repair of DNA double-strand breaks associated with heterochromatin. Mol. Cell 31, 167-177 (2008).
    • (2008) Mol. Cell , vol.31 , pp. 167-177
    • Goodarzi, A.A.1
  • 57
    • 17244367849 scopus 로고    scopus 로고
    • DNA damage response as a candidate anti-cancer barrier in early human tumorigenesis
    • Bartkova, J. et al. DNA damage response as a candidate anti-cancer barrier in early human tumorigenesis. Nature 434, 864-870 (2005).
    • (2005) Nature , vol.434 , pp. 864-870
    • Bartkova, J.1
  • 58
    • 17244366865 scopus 로고    scopus 로고
    • Activation of the DNA damage checkpoint and genomic instability in human precancerous lesions
    • Gorgoulis, V.G. et al. Activation of the DNA damage checkpoint and genomic instability in human precancerous lesions. Nature 434, 907-913 (2005).
    • (2005) Nature , vol.434 , pp. 907-913
    • Gorgoulis, V.G.1
  • 59
    • 20144388146 scopus 로고    scopus 로고
    • Loss of acetylation at Lys16 and trimethylation at Lys20 of histone H4 is a common hallmark of human cancer
    • Fraga, M.F. et al. Loss of acetylation at Lys16 and trimethylation at Lys20 of histone H4 is a common hallmark of human cancer. Nat. Genet. 37, 391-400 (2005).
    • (2005) Nat. Genet. , vol.37 , pp. 391-400
    • Fraga, M.F.1
  • 60
    • 34250171437 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: Signalling towards p21cip1/waf1
    • Ocker, M. & Schneider-Stock, R. Histone deacetylase inhibitors: signalling towards p21cip1/waf1. Int. J. Biochem. Cell Biol. 39, 1367-1374 (2007).
    • (2007) Int. J. Biochem. Cell Biol. , vol.39 , pp. 1367-1374
    • Ocker, M.1    Schneider-Stock, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.