메뉴 건너뛰기




Volumn 20, Issue 3, 2005, Pages 153-163

Tails of histones in DNA double-strand break repair

Author keywords

[No Author keywords available]

Indexed keywords

DOUBLE STRANDED DNA; ENDONUCLEASE; HISTONE; HISTONE H2A; HISTONE H2B; HISTONE H3; HISTONE H4; MITOCHONDRIAL ENZYME; MUTAGENIC AGENT; TYPE II SITE SPECIFIC DEOXYRIBONUCLEASE;

EID: 19544364643     PISSN: 02678357     EISSN: None     Source Type: Journal    
DOI: 10.1093/mutage/gei031     Document Type: Review
Times cited : (18)

References (81)
  • 1
    • 1942439629 scopus 로고    scopus 로고
    • Mechanisms for ATP-dependent chromatin remodelling: Farewell to the tuna-can octamer?
    • Flaus,A. and Owen-Hughes,T. (2004) Mechanisms for ATP-dependent chromatin remodelling: farewell to the tuna-can octamer? Curr. Opin. Genet. Dev., 14, 165-173.
    • (2004) Curr. Opin. Genet. Dev. , vol.14 , pp. 165-173
    • Flaus, A.1    Owen-Hughes, T.2
  • 2
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • Jenuwein,T. and Allis,C.D. (2001) Translating the histone code. Science, 293, 1074-1080.
    • (2001) Science , vol.293 , pp. 1074-1080
    • Jenuwein, T.1    Allis, C.D.2
  • 3
    • 0038700698 scopus 로고    scopus 로고
    • Molecular views of recombination proteins and their control
    • West,S.C. (2003) Molecular views of recombination proteins and their control. Nat. Rev. Mol. Cell Biol., 4, 1-11.
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 1-11
    • West, S.C.1
  • 4
    • 0042839614 scopus 로고    scopus 로고
    • Mechanism and regulation of human non-homologous DNA end-joining
    • Lieber, M.R., Ma,Y., Pannicke.U, and Schwarz,K. (2003) Mechanism and regulation of human non-homologous DNA end-joining, Nat. Rev. Mol. Cell Biol., 4, 712-720.
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 712-720
    • Lieber, M.R.1    Ma, Y.2    Pannicke, U.3    Schwarz, K.4
  • 5
    • 0036261707 scopus 로고    scopus 로고
    • Sensing and repairing DNA double-strand breaks
    • Jackson,S.P. (2002) Sensing and repairing DNA double-strand breaks, Carcinogenesis, 23, 687-696.
    • (2002) Carcinogenesis , vol.23 , pp. 687-696
    • Jackson, S.P.1
  • 6
    • 11144357255 scopus 로고    scopus 로고
    • Cellular machineries for chromosomal DNA repair
    • Peterso,C.L. and Cote,J. (2004) Cellular machineries for chromosomal DNA repair. Genes Dev., 18, 602-616.
    • (2004) Genes Dev. , vol.18 , pp. 602-616
    • Peterso, C.L.1    Cote, J.2
  • 7
    • 2942581154 scopus 로고    scopus 로고
    • The absence of the yeast chromatin assembly factor Asfl increases genomic instability and sister chromatid exchange
    • Prado,F., Cortes-Ledesma,F. and Aguilera,A. (2004) The absence of the yeast chromatin assembly factor Asfl increases genomic instability and sister chromatid exchange, EMBO Rep., 5, 497-502.
    • (2004) EMBO Rep. , vol.5 , pp. 497-502
    • Prado, F.1    Cortes-Ledesma, F.2    Aguilera, A.3
  • 9
    • 0029826906 scopus 로고    scopus 로고
    • Persistent site-specific remodeling of a nucleosome array by transient action of the SWI/SNF complex
    • Owen-HughesT.A., Utley,R.T., Cote,J., Peterson,C.L. and Workman,J.L. (1996) Persistent site-specific remodeling of a nucleosome array by transient action of the SWI/SNF complex, Science, 273, 513-516.
    • (1996) Science , vol.273 , pp. 513-516
    • Owen-Hughes, T.A.1    Utley, R.T.2    Cote, J.3    Peterson, C.L.4    Workman, J.L.5
  • 10
    • 0025133118 scopus 로고
    • Involvement of nucleic acid synthesis in cell killing mechanisms of topoisomerase poisons
    • D'Arpa,P., Beardmore,C. and Liu,L.F. (1990) Involvement of nucleic acid synthesis in cell killing mechanisms of topoisomerase poisons. Cancer Res., 50, 6919-6924.
    • (1990) Cancer Res. , vol.50 , pp. 6919-6924
    • D'Arpa, P.1    Beardmore, C.2    Liu, L.F.3
  • 11
    • 0003433577 scopus 로고    scopus 로고
    • DNA damage and repair
    • Nickoloff,J.A. (ed.). Humana Press, Totowa, NJ
    • Nickoloff,J.A, and Hoekstra,M.F. (1998) DNA damage and repair, In Nickoloff,J.A. (ed.), Contemporary Cancer Research. Humana Press, Totowa, NJ, Vols I and II, pp, 1-32.
    • (1998) Contemporary Cancer Research , vol.1-2 , pp. 1-32
    • Nickoloff, J.A.1    Hoekstra, M.F.2
  • 12
    • 0041903834 scopus 로고    scopus 로고
    • In vivo roles of Rad52, Rad54 and Rad55 proteins in Rad51-mediated recombination
    • Sugawara,N., Wang,X. and Haber,J.E. (2003) In vivo roles of Rad52, Rad54 and Rad55 proteins in Rad51-mediated recombination. Mol. Cell, 12, 209-219.
    • (2003) Mol. Cell , vol.12 , pp. 209-219
    • Sugawara, N.1    Wang, X.2    Haber, J.E.3
  • 13
    • 0026573892 scopus 로고
    • Site-specific recombination determined by I-SceI, a mitochondrial group I intronencoded endonuclease expressed in the yeast nucleus
    • Plessis,A., Perrin,A., Haber,J.E. and Dujon,B. (1992) Site-specific recombination determined by I-SceI, a mitochondrial group I intronencoded endonuclease expressed in the yeast nucleus. Genetics, 130, 451-460.
    • (1992) Genetics , vol.130 , pp. 451-460
    • Plessis, A.1    Perrin, A.2    Haber, J.E.3    Dujon, B.4
  • 14
    • 0033230685 scopus 로고    scopus 로고
    • Construction of a recombinant adenovirus for efficient delivery of the I-SceI yeast endonuclease to human cells and its application in the in vivo cleavage of chromosomes to expose new potential telomeres
    • Anglana,M. and Bacchetti,S. (1999) Construction of a recombinant adenovirus for efficient delivery of the I-SceI yeast endonuclease to human cells and its application in the in vivo cleavage of chromosomes to expose new potential telomeres, Nucleic Acids Res., 27, 4276-4281.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 4276-4281
    • Anglana, M.1    Bacchetti, S.2
  • 15
    • 0035099044 scopus 로고    scopus 로고
    • BRCA2 is required for homology-directed repair of chromosomal breaks
    • Moynahan,M.E., Pierce,A.J, and Jasin,M. (2001) BRCA2 is required for homology-directed repair of chromosomal breaks. Mol. Cell, 7, 263-272.
    • (2001) Mol. Cell , vol.7 , pp. 263-272
    • Moynahan, M.E.1    Pierce, A.J.2    Jasin, M.3
  • 16
    • 4444292641 scopus 로고    scopus 로고
    • SMC1 coordinates DNA double-strand break repair pathways
    • Schar,P., Fasi,M. and Jessberger,R. (2004) SMC1 coordinates DNA double-strand break repair pathways, Nucleic Acids Res., 32, 3921-3929.
    • (2004) Nucleic Acids Res. , vol.32 , pp. 3921-3929
    • Schar, P.1    Fasi, M.2    Jessberger, R.3
  • 18
    • 0032861343 scopus 로고    scopus 로고
    • Megabase chromatin domains involved in DNA double-strand breaks in vivo
    • Rogakou,E.P., Boon,C., Redon,C. and Bonner,W.M. (1999) Megabase chromatin domains involved in DNA double-strand breaks in vivo. J. Cell Biol., 146, 905-915.
    • (1999) J. Cell Biol. , vol.146 , pp. 905-915
    • Rogakou, E.P.1    Boon, C.2    Redon, C.3    Bonner, W.M.4
  • 20
    • 0032536861 scopus 로고    scopus 로고
    • Components of the Ku-dependent non-homologous end-joining pathway are involved in telomeric length maintenance and telomeric silencing
    • Boulton,S.J. and Jackson,S.P. (1998) Components of the Ku-dependent non-homologous end-joining pathway are involved in telomeric length maintenance and telomeric silencing. EMBO J., 17, 1819-1828.
    • (1998) EMBO J. , vol.17 , pp. 1819-1828
    • Boulton, S.J.1    Jackson, S.P.2
  • 21
    • 0034700511 scopus 로고    scopus 로고
    • A role for Saccharomyces cerevisiae histone H2A in DNA repair
    • Downs,J.A., Lowndes,N.F. and Jackson,S.P. (2000) A role for Saccharomyces cerevisiae histone H2A in DNA repair, Nature, 408, 1001-1004.
    • (2000) Nature , vol.408 , pp. 1001-1004
    • Downs, J.A.1    Lowndes, N.F.2    Jackson, S.P.3
  • 22
    • 0036888874 scopus 로고    scopus 로고
    • Histone H3 and the histone acetyltransferase Hatlp contribute to DNA double-strand break repair
    • Qin,S. and Parthun,M.R. (2002) Histone H3 and the histone acetyltransferase Hatlp contribute to DNA double-strand break repair. Mol. Cell. Biol., 22, 8353-8365.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 8353-8365
    • Qin, S.1    Parthun, M.R.2
  • 24
    • 0038531105 scopus 로고    scopus 로고
    • Multiple roles for Saccharomyces cerevisiae histone H2A in telomere position effect, Spt phenotypes and double-strand-break repair
    • Wyatt,H.R., Liaw,H., Green,G.R and Lustig,A.J. (2003) Multiple roles for Saccharomyces cerevisiae histone H2A in telomere position effect, Spt phenotypes and double-strand-break repair. Genetics, 164, 47-64.
    • (2003) Genetics , vol.164 , pp. 47-64
    • Wyatt, H.R.1    Liaw, H.2    Green, G.R.3    Lustig, A.J.4
  • 26
    • 9144269660 scopus 로고    scopus 로고
    • A Snf2 family ATPase complex required for recruitment of the histone H2A variant Htzl
    • Krogan,NJ., Keogh,M.C., Datta,N. et al. (2003) A Snf2 family ATPase complex required for recruitment of the histone H2A variant Htzl. Mol. Cell, 12, 1565-1576.
    • (2003) Mol. Cell , vol.12 , pp. 1565-1576
    • Krogan, N.J.1    Keogh, M.C.2    Datta, N.3
  • 28
    • 0037062492 scopus 로고    scopus 로고
    • Increased ionizing radiation sensitivity and genomic instability in the absence of histone H2AX
    • Bassing,C.H., Chua,K.F., Sekiguchi,J.A. et al. (2002) Increased ionizing radiation sensitivity and genomic instability in the absence of histone H2AX, Proc. Natl Acad. Sci. USA, 99, 8173-8178.
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 8173-8178
    • Bassing, C.H.1    Chua, K.F.2    Sekiguchi, J.A.3
  • 30
    • 2942534912 scopus 로고    scopus 로고
    • Activation of a DNA damage checkpoint response in a TAF1-defective cell line
    • Buchmann,A.M., Skaar,J.R., and DeCaprio,J.A. (2004) Activation of a DNA damage checkpoint response in a TAF1-defective cell line, Mol. Cell. Biol., 24, 5332-5339.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 5332-5339
    • Buchmann, A.M.1    Skaar, J.R.2    DeCaprio, J.A.3
  • 32
    • 0043066728 scopus 로고    scopus 로고
    • Yeast histone 2A serine 129 is essential for the efficient repair of checkpoint-blind DNA damage
    • Redon.C., Pilch,D.R., Rogakou,E.P., Orr,A.H., Lowndes,N.F. and Bonner,W.M. (2003) Yeast histone 2A serine 129 is essential for the efficient repair of checkpoint-blind DNA damage. EMBO Rep., 4, 678-684.
    • (2003) EMBO Rep. , vol.4 , pp. 678-684
    • Redon, C.1    Pilch, D.R.2    Rogakou, E.P.3    Orr, A.H.4    Lowndes, N.F.5    Bonner, W.M.6
  • 33
    • 0032489520 scopus 로고    scopus 로고
    • DNA double-stranded breaks induce histone H2AX phosphorylation on serine 139
    • Rogakou,E.P., Pilch,D.R., Orr,A.H., Ivanova,V.S. and Bonner,W.M. (1998) DNA double-stranded breaks induce histone H2AX phosphorylation on serine 139. J. Biol. Chem., 273, 5858-5868.
    • (1998) J. Biol. Chem. , vol.273 , pp. 5858-5868
    • Rogakou, E.P.1    Pilch, D.R.2    Orr, A.H.3    Ivanova, V.S.4    Bonner, W.M.5
  • 34
    • 3042793923 scopus 로고    scopus 로고
    • Histone H2A phosphorylation controls Crb2 recruitment at DNA breaks, maintains checkpoint arrest, and influences DNA repair in fission yeast
    • Nakamura,T.M., Du,L.L., Redon,C. and Russell,P. (2004) Histone H2A phosphorylation controls Crb2 recruitment at DNA breaks, maintains checkpoint arrest, and influences DNA repair in fission yeast. Mol. Cell. Biol., 24, 6215-6230.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 6215-6230
    • Nakamura, T.M.1    Du, L.L.2    Redon, C.3    Russell, P.4
  • 35
    • 0036712095 scopus 로고    scopus 로고
    • DNA double-strand break-induced phosphorylation of Drosophila histone variant H2Av helps prevent radiation-induced apoptosis
    • Madigan,J.P., Chotkowski,H.L. and Glaser,R.L. (2002) DNA double-strand break-induced phosphorylation of Drosophila histone variant H2Av helps prevent radiation-induced apoptosis. Nucleic Acids Res., 30, 3698-3705.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 3698-3705
    • Madigan, J.P.1    Chotkowski, H.L.2    Glaser, R.L.3
  • 37
    • 12844269263 scopus 로고    scopus 로고
    • Histone H2A and Spt10 cooperate to regulate induction and autoregulation of the CUP1 metallothionein
    • Kuo,H.C. Moore,J.D. and Krebs,J.E. (2004) Histone H2A and Spt10 cooperate to regulate induction and autoregulation of the CUP1 metallothionein. J. Biol. Chem., 280, 104-114.
    • (2004) J. Biol. Chem. , vol.280 , pp. 104-114
    • Kuo, H.C.1    Moore, J.D.2    Krebs, J.E.3
  • 38
    • 0033560796 scopus 로고    scopus 로고
    • The DNA-dependent protein kinase
    • Smith,G.C.M. and Jackson,S.P. (1999) The DNA-dependent protein kinase, Genes Dev., 13, 916-934.
    • (1999) Genes Dev. , vol.13 , pp. 916-934
    • Smith, G.C.M.1    Jackson, S.P.2
  • 39
    • 0035930537 scopus 로고    scopus 로고
    • Histone H2AX is phosphorylated in an ATR-dependent manner in response to replicational stress
    • Ward,I.M. and Chen,J. (2001) Histone H2AX is phosphorylated in an ATR-dependent manner in response to replicational stress. J. Biol. Chem., 276, 47759-47762.
    • (2001) J. Biol. Chem. , vol.276 , pp. 47759-47762
    • Ward, I.M.1    Chen, J.2
  • 40
    • 0035834693 scopus 로고    scopus 로고
    • ATM phosphorylates histone H2AX in response to DNA double-strand breaks
    • Burma,S., Chen,B.P., Murphy,M., Kurimasa.A, and Chen,D.J. (2001) ATM phosphorylates histone H2AX in response to DNA double-strand breaks, J. Biol. Chem., 276, 42462-42467.
    • (2001) J. Biol. Chem. , vol.276 , pp. 42462-42467
    • Burma, S.1    Chen, B.P.2    Murphy, M.3    Kurimasa, A.4    Chen, D.J.5
  • 41
    • 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., Iwabuchi,K., Lobrich,M. and Jeggo,P.A. (2004) ATM and DNA-PK function redundantly to phosphorylate H2AX after exposure to ionizing radiation. Cancer Res., 64, 2390-2396.
    • (2004) Cancer Res. , vol.64 , pp. 2390-2396
    • Stiff, T.1    O'Driscoll, M.2    Rief, N.3    Iwabuchi, K.4    Lobrich, M.5    Jeggo, P.A.6
  • 42
    • 0345073699 scopus 로고    scopus 로고
    • A splicing mutation affecting expression of ataxia-telangiectasia and Rad3-related protein (ATR) results in Seckel syndrome
    • O'Driscoll.M., Ruiz-Perez,V.L., Woods,C.G., Jeggo,P.A. and Goodship,J.A. (2003) A splicing mutation affecting expression of ataxia-telangiectasia and Rad3-related protein (ATR) results in Seckel syndrome. Nat. Genet., 33, 497-501.
    • (2003) Nat. Genet. , vol.33 , pp. 497-501
    • O'Driscoll, M.1    Ruiz-Perez, V.L.2    Woods, C.G.3    Jeggo, P.A.4    Goodship, J.A.5
  • 43
    • 0037012845 scopus 로고    scopus 로고
    • Genomic instability in mice lacking histone H2AX
    • Celeste,A., Petersen,S., Romanienko,P.J. et al. (2002) Genomic instability in mice lacking histone H2AX, Science, 296, 922-927.
    • (2002) Science , vol.296 , pp. 922-927
    • Celeste, A.1    Petersen, S.2    Romanienko, P.J.3
  • 45
    • 0038820065 scopus 로고    scopus 로고
    • Phosphorylation of histone H2AX and activation of Mrell, Rad50, and Nbsl in response to replication-dependent DNA double-strand breaks induced by mammalian DNA topoisomerase I cleavage complexes
    • Furuta,T., Takemura,H., Liao;Z.-Y. et al. (2003) Phosphorylation of histone H2AX and activation of Mrell, Rad50, and Nbsl in response to replication-dependent DNA double-strand breaks induced by mammalian DNA topoisomerase I cleavage complexes. J. Biol, Chem., 278, 20303-20312.
    • (2003) J. Biol. Chem. , vol.278 , pp. 20303-20312
    • Furuta, T.1    Takemura, H.2    Liao, Z.-Y.3
  • 46
    • 0343280013 scopus 로고    scopus 로고
    • A critical role for histone H2AX in recruitment of repair factors to nuclear foci after DNA damage
    • Paull,T.T., Rogakou,E.P., Yamazaki.V., Kirchgessner,CU., Gellert,M. and Bonner,W.M, (2000) A critical role for histone H2AX in recruitment of repair factors to nuclear foci after DNA damage. Curr. Biol, 10, 886-895.
    • (2000) Curr. Biol. , vol.10 , pp. 886-895
    • Paull, T.T.1    Rogakou, E.P.2    Yamazaki, V.3    Kirchgessner, C.U.4    Gellert, M.5    Bonner, W.M.6
  • 47
  • 52
    • 10944233962 scopus 로고    scopus 로고
    • Recruitment of the INO80 complex by H2A phosphorylation links ATP-dependent chromatin remodeling with DNA double-strand break repair
    • Van Attikum,H., Fritsch,O., Hohn,B. and Gasser,S.M. (2004) Recruitment of the INO80 complex by H2A phosphorylation links ATP-dependent chromatin remodeling with DNA double-strand break repair, Cell, 119, 777-788.
    • (2004) Cell , vol.119 , pp. 777-788
    • Van Attikum, H.1    Fritsch, O.2    Hohn, B.3    Gasser, S.M.4
  • 53
  • 54
    • 10944230851 scopus 로고    scopus 로고
    • Around the world of DNA damage INO80 days
    • Cairns,B.R. (2004) Around the world of DNA damage INO80 days. Cell, 119, 733-740.
    • (2004) Cell , vol.119 , pp. 733-740
    • Cairns, B.R.1
  • 55
    • 11144354084 scopus 로고    scopus 로고
    • Nucleosomal histone kinase-1 phosphorylates H2A Thr119 during mitosis in the early Droaophila embryo
    • Aihara,H., Nakagawa, T., Yasui,K. et al. (2004) Nucleosomal histone kinase-1 phosphorylates H2A Thr119 during mitosis in the early Droaophila embryo. Genes Dev., 18, 877-888.
    • (2004) Genes Dev. , vol.18 , pp. 877-888
    • Aihara, H.1    Nakagawa, T.2    Yasui, K.3
  • 56
    • 19544381129 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae histone H2A Ser122 facilitates DNA repair
    • doi: 10.1534/genetics.104.038570
    • Harvey,A.C., Jackson,S.P. and Downs,J.A. (2005) Saccharomyces cerevisiae histone H2A Ser122 facilitates DNA repair. Genetics, doi: 10.1534/genetics.104. 038570.
    • (2005) Genetics
    • Harvey, A.C.1    Jackson, S.P.2    Downs, J.A.3
  • 57
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 Å resolution
    • Luger,K., Mader,A.W., Richmond,R.K., Sargent,D.F. and Richmond,T.J. (1997) Crystal structure of the nucleosome core particle at 2.8 Å resolution. Nature, 389, 251-260.
    • (1997) Nature , vol.389 , pp. 251-260
    • Luger, K.1    Mader, A.W.2    Richmond, R.K.3    Sargent, D.F.4    Richmond, T.J.5
  • 58
    • 0037381213 scopus 로고    scopus 로고
    • Structure and dynamic behavior of nucleosomes
    • Lugar,K. (2003) Structure and dynamic behavior of nucleosomes, Curr. Opin. Genet. Dev., 13, 127-135.
    • (2003) Curr. Opin. Genet. Dev. , vol.13 , pp. 127-135
    • Lugar, K.1
  • 59
    • 0034695456 scopus 로고    scopus 로고
    • Rad6-dependent ubiquitination of histone H2B in yeast
    • Robzyk,K., Recht,J. and Osley,M.A. (2000) Rad6-dependent ubiquitination of histone H2B in yeast. Science, 287, 501-504.
    • (2000) Science , vol.287 , pp. 501-504
    • Robzyk, K.1    Recht, J.2    Osley, M.A.3
  • 60
    • 0037248593 scopus 로고    scopus 로고
    • A conserved RING finger protein required for histone H2B monoubiquitination and cell size control
    • Hwang,W.W., Venkatasubrahmanyam,S., Ianculescu,A.G., Tong,A., Boone,C. and Madhani,H.D. (2003) A conserved RING finger protein required for histone H2B monoubiquitination and cell size control. Mol. Cell, 11, 261-266.
    • (2003) Mol. Cell , vol.11 , pp. 261-266
    • Hwang, W.W.1    Venkatasubrahmanyam, S.2    Ianculescu, A.G.3    Tong, A.4    Boone, C.5    Madhani, H.D.6
  • 61
    • 0037248944 scopus 로고    scopus 로고
    • Brei, an E3 Ubiquitin Iigase required for recruitment and substrate selection of Rad6 at a promoter
    • Wood,A., Krogan,NJ., Dover,J. et al. (2003) Brei, an E3 Ubiquitin Iigase required for recruitment and substrate selection of Rad6 at a promoter. Mol. Cell, 11, 267-274.
    • (2003) Mol. Cell , vol.11 , pp. 267-274
    • Wood, A.1    Krogan, N.J.2    Dover, J.3
  • 62
    • 0037019333 scopus 로고    scopus 로고
    • Ubiquitination of histone H2B regulates H3 methylation and gene silencing in yeast
    • Sun,Z.-W. and Allis,C.D. (2002) Ubiquitination of histone H2B regulates H3 methylation and gene silencing in yeast. Nature, 418, 104-108.
    • (2002) Nature , vol.418 , pp. 104-108
    • Sun, Z.-W.1    Allis, C.D.2
  • 63
    • 1542298300 scopus 로고    scopus 로고
    • H2B ubiquitylation: The end is in sight
    • Oskiy,M.A. (2004) H2B ubiquitylation: the end is in sight. Biochim. Biophys. Acta, 1677, 74-78.
    • (2004) Biochim. Biophys. Acta , vol.1677 , pp. 74-78
    • Oskiy, M.A.1
  • 64
    • 1242271997 scopus 로고    scopus 로고
    • Proteasomal ATPases link ubiquitylation of histone H2B to methylation of histone H3
    • Ezhkova,E. and Tansey,W.P. (2004) Proteasomal ATPases link ubiquitylation of histone H2B to methylation of histone H3. Mol. Cell, 13, 435-442.
    • (2004) Mol. Cell , vol.13 , pp. 435-442
    • Ezhkova, E.1    Tansey, W.P.2
  • 65
    • 3843067547 scopus 로고    scopus 로고
    • Rad6-brel-mediated histone H2B ubiquitylation modulates the formation of double-strand breaks during meiosis
    • Yamashita,K., Shinohara,M. and Shinohara,A. (2004) Rad6-Brel-mediated histone H2B ubiquitylation modulates the formation of double-strand breaks during meiosis. Proc. Natl Acad. Sci. USA, 101, 11380-11385.
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 11380-11385
    • Yamashita, K.1    Shinohara, M.2    Shinohara, A.3
  • 66
    • 0038293152 scopus 로고    scopus 로고
    • Apoptotic phosphorylation of histone H2B is mediated by mammalian sterile twenty kinase
    • Cheung,W.L., Ajiro,K., Samejima,K. et al. (2003) Apoptotic phosphorylation of histone H2B is mediated by mammalian sterile twenty kinase. Cell, 113, 507-517.
    • (2003) Cell , vol.113 , pp. 507-517
    • Cheung, W.L.1    Ajiro, K.2    Samejima, K.3
  • 67
    • 3042685445 scopus 로고    scopus 로고
    • Phoisphorylation of histone H2B at DNA double-strand breaks
    • Femandez-Capetillo,O., Allis,C.D. and Nussenzweig,A. (2004) Phoisphorylation of histone H2B at DNA double-strand breaks. J. Exp. Med., 199, 1671-1677.
    • (2004) J. Exp. Med. , vol.199 , pp. 1671-1677
    • Femandez-Capetillo, O.1    Allis, C.D.2    Nussenzweig, A.3
  • 68
    • 0034647733 scopus 로고    scopus 로고
    • ERKs and p38 kinases mediate ultraviolet B-induced phosphorylation of histone H3 at serine 10
    • Zhong,S.-P., Ma,W.-Y. and Dong,Z. (2000) ERKs and p38 kinases mediate ultraviolet B-induced phosphorylation of histone H3 at serine 10. J. Biol. Chem., 275, 20980-20984.
    • (2000) J. Biol. Chem. , vol.275 , pp. 20980-20984
    • Zhong, S.-P.1    Ma, W.-Y.2    Dong, Z.3
  • 70
    • 0035918301 scopus 로고    scopus 로고
    • MAP kinases mediate UVB-induced phosphorylation of histone H3 at serine 28
    • Zhong,S., Zhang,Y., Jansen,C., Goto,H., Inagaki,M. and Dong,Z. (2001) MAP kinases mediate UVB-induced phosphorylation of histone H3 at serine 28. J. Biol. Chem., 276, 12932-12937.
    • (2001) J. Biol. Chem. , vol.276 , pp. 12932-12937
    • Zhong, S.1    Zhang, Y.2    Jansen, C.3    Goto, H.4    Inagaki, M.5    Dong, Z.6
  • 71
    • 0033609882 scopus 로고    scopus 로고
    • Increased Ser-10 phosphorylation of histone H3 in mitogen-stimulated and oncogene-transformed mouse fibroblasts
    • Chadee,D.N., Hendzel,M.J., Tylipski,C.P., Allis,C.D., Bazett-Jones,D.P., Wright,J.A. and Davie,J.R, (1999) Increased Ser-10 phosphorylation of histone H3 in mitogen-stimulated and oncogene-transformed mouse fibroblasts. J. Biol Chem., 274, 24914-24920.
    • (1999) J. Biol Chem. , vol.274 , pp. 24914-24920
    • Chadee, D.N.1    Hendzel, M.J.2    Tylipski, C.P.3    Allis, C.D.4    Bazett-Jones, D.P.5    Wright, J.A.6    Davie, J.R.7
  • 72
    • 9244252580 scopus 로고    scopus 로고
    • Methylated lysine 79 of histone H3 targets 53BP1 to DNA double-strand breaks
    • Huyen,Y., Zgheib,O., DiTullio,R.A.Jr et al. (2004) Methylated lysine 79 of histone H3 targets 53BP1 to DNA double-strand breaks, Nature, 432, 406-411.
    • (2004) Nature , vol.432 , pp. 406-411
    • Huyen, Y.1    Zgheib, O.2    DiTullio Jr., R.A.3
  • 73
    • 2342565902 scopus 로고    scopus 로고
    • A means to a DNA end: The many roles of Ku
    • Downs,J.A. and Jackson,S.P. (2004) A means to a DNA end: the many roles of Ku, Nat. Rev. Mol. Cell Biol., 5, 367-378.
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 367-378
    • Downs, J.A.1    Jackson, S.P.2
  • 74
    • 0033567954 scopus 로고    scopus 로고
    • NuA4, an essential transcription adaptor/histone H4 acetyltransferase complex containing Esalp and the ATM-related cofactor Tralp
    • Allard,S., Utley, R.T., Savard,J., Clarke,A., Grant,P., Brandl,C.J., Pilus,L., Workman,J.L., and Ĉté.J. (1999) NuA4, an essential transcription adaptor/histone H4 acetyltransferase complex containing Esalp and the ATM-related cofactor Tralp. EMBO J., 18, 5108-5119.
    • (1999) EMBO J. , vol.18 , pp. 5108-5119
    • Allard, S.1    Utley, R.T.2    Savard, J.3    Clarke, A.4    Grant, P.5    Brandl, C.J.6    Pilus, L.7    Workman, J.L.8    Ĉté, J.9
  • 77
    • 8844248619 scopus 로고    scopus 로고
    • Methylation of histone H4 lysine 20 controls recruitment of Crb2 to sites of DNA damage
    • Sanders,S.L., Portoso,M., Mata,J., Bahler,J., Allshire,R.C. and Kouzarides,T. (2004) Methylation of histone H4 lysine 20 controls recruitment of Crb2 to sites of DNA damage. Cell, 119, 603-614.
    • (2004) Cell , vol.119 , pp. 603-614
    • Sanders, S.L.1    Portoso, M.2    Mata, J.3    Bahler, J.4    Allshire, R.C.5    Kouzarides, T.6
  • 78
    • 2342570379 scopus 로고    scopus 로고
    • Hallmarks of senescence in carcinogenesis and cancer therapy
    • Shay,J.W. and Roninson,I.B. (2004) Hallmarks of senescence in carcinogenesis and cancer therapy. Oncogene, 23, 2919-2933.
    • (2004) Oncogene , vol.23 , pp. 2919-2933
    • Shay, J.W.1    Roninson, I.B.2
  • 80
    • 0032965173 scopus 로고    scopus 로고
    • A comparison of the effects of diverse mutagens at the lacZ transgene and Dlb-1 locus in vivo
    • Cosentino,L. and Heddle,J.A. (1999) A comparison of the effects of diverse mutagens at the lacZ transgene and Dlb-1 locus in vivo. Mutagenesis, 14, 113-119.
    • (1999) Mutagenesis , vol.14 , pp. 113-119
    • Cosentino, L.1    Heddle, J.A.2
  • 81
    • 0035162698 scopus 로고    scopus 로고
    • Genomic expression responses to DNA-damaging agents and the regulatory role of the yeast ATR homolog Meclp
    • Gasch,A.P., Huang,M., Metzner,S., Botstein.D., Elledge,S.J. and Brown,P.O. (2001) Genomic expression responses to DNA-damaging agents and the regulatory role of the yeast ATR homolog Meclp. Mol. Biol. Cell, 12, 2987-3003.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 2987-3003
    • Gasch, A.P.1    Huang, M.2    Metzner, S.3    Botstein, D.4    Elledge, S.J.5    Brown, P.O.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.