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Volumn 427, Issue 3, 2015, Pages 626-636

Reshaping Chromatin after DNA Damage: The Choreography of Histone Proteins

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; HISTONE;

EID: 84925659063     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2014.05.025     Document Type: Review
Times cited : (62)

References (97)
  • 1
    • 0017331464 scopus 로고
    • Structure of chromatin
    • R.D. Kornberg Structure of chromatin Annu Rev Biochem 46 1977 931 954
    • (1977) Annu Rev Biochem , vol.46 , pp. 931-954
    • Kornberg, R.D.1
  • 2
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 Å resolution
    • K. Luger, A.W. Mäder, R.K. Richmond, D.F. Sargent, and T.J. Richmond Crystal structure of the nucleosome core particle at 2.8 Å resolution Nature 389 1997 251 260
    • (1997) Nature , vol.389 , pp. 251-260
    • Luger, K.1    Mäder, A.W.2    Richmond, R.K.3    Sargent, D.F.4    Richmond, T.J.5
  • 3
    • 79953163378 scopus 로고    scopus 로고
    • Chromatin higher-order structures and gene regulation
    • G. Li, and D. Reinberg Chromatin higher-order structures and gene regulation Curr Opin Genet Dev 21 2011 175 186
    • (2011) Curr Opin Genet Dev , vol.21 , pp. 175-186
    • Li, G.1    Reinberg, D.2
  • 5
    • 79952534189 scopus 로고    scopus 로고
    • Regulation of chromatin by histone modifications
    • A.J. Bannister, and T. Kouzarides Regulation of chromatin by histone modifications Cell Res 21 2011 381 395
    • (2011) Cell Res , vol.21 , pp. 381-395
    • Bannister, A.J.1    Kouzarides, T.2
  • 6
    • 84899415723 scopus 로고    scopus 로고
    • Every amino acid matters: Essential contributions of histone variants to mammalian development and disease
    • I. Maze, K.-M. Noh, A.A. Soshnev, and C.D. Allis Every amino acid matters: essential contributions of histone variants to mammalian development and disease Nat Rev Genet 15 2014 259 271
    • (2014) Nat Rev Genet , vol.15 , pp. 259-271
    • Maze, I.1    Noh, K.-M.2    Soshnev, A.A.3    Allis, C.D.4
  • 7
    • 35848964068 scopus 로고    scopus 로고
    • Histone chaperones: An escort network regulating histone traffic
    • L. De Koning, A. Corpet, J.E. Haber, and G. Almouzni Histone chaperones: an escort network regulating histone traffic Nat Struct Mol Biol 14 2007 997 1007
    • (2007) Nat Struct Mol Biol , vol.14 , pp. 997-1007
    • De Koning, L.1    Corpet, A.2    Haber, J.E.3    Almouzni, G.4
  • 8
    • 84872051865 scopus 로고    scopus 로고
    • Histone chaperones in nucleosome assembly and human disease
    • R.J. Burgess, and Z. Zhang Histone chaperones in nucleosome assembly and human disease Nat Struct Mol Biol 20 2013 14 22
    • (2013) Nat Struct Mol Biol , vol.20 , pp. 14-22
    • Burgess, R.J.1    Zhang, Z.2
  • 9
    • 80052970429 scopus 로고    scopus 로고
    • Mechanisms for ATP-dependent chromatin remodelling: The means to the end
    • A. Flaus, and T. Owen-Hughes Mechanisms for ATP-dependent chromatin remodelling: the means to the end FEBS J 278 2011 3579 3595
    • (2011) FEBS J , vol.278 , pp. 3579-3595
    • Flaus, A.1    Owen-Hughes, T.2
  • 10
    • 79952539053 scopus 로고    scopus 로고
    • ATP-dependent chromatin remodeling: Genetics, genomics and mechanisms
    • D.C. Hargreaves, and G.R. Crabtree ATP-dependent chromatin remodeling: genetics, genomics and mechanisms Cell Res 21 2011 396 420
    • (2011) Cell Res , vol.21 , pp. 396-420
    • Hargreaves, D.C.1    Crabtree, G.R.2
  • 12
    • 84883797029 scopus 로고    scopus 로고
    • Nucleosome dynamics as modular systems that integrate DNA damage and repair
    • C.L. Peterson, and G. Almouzni Nucleosome dynamics as modular systems that integrate DNA damage and repair Cold Spring Harbor Perspect Biol 5 2013 10.1101/cshperspect.a012658
    • (2013) Cold Spring Harbor Perspect Biol , vol.5
    • Peterson, C.L.1    Almouzni, G.2
  • 13
    • 84875198804 scopus 로고    scopus 로고
    • Chromatin remodeling at DNA double-strand breaks
    • B.D. Price, and A.D. D'Andrea Chromatin remodeling at DNA double-strand breaks Cell 152 2013 1344 1354
    • (2013) Cell , vol.152 , pp. 1344-1354
    • Price, B.D.1    D'Andrea, A.D.2
  • 14
    • 84878918708 scopus 로고    scopus 로고
    • The chromatin response to DNA breaks: Leaving a mark on genome integrity
    • G. Smeenk, and H. van Attikum The chromatin response to DNA breaks: leaving a mark on genome integrity Annu Rev Biochem 82 2013 55 80
    • (2013) Annu Rev Biochem , vol.82 , pp. 55-80
    • Smeenk, G.1    Van Attikum, H.2
  • 15
    • 78649336706 scopus 로고    scopus 로고
    • The DNA damage response: Making it safe to play with knives
    • A. Ciccia, and S.J. Elledge The DNA damage response: making it safe to play with knives Mol Cell 40 2010 179 204
    • (2010) Mol Cell , vol.40 , pp. 179-204
    • Ciccia, A.1    Elledge, S.J.2
  • 16
    • 0026181844 scopus 로고
    • DNA repair and the role of chromatin structure
    • M.J. Smerdon DNA repair and the role of chromatin structure Curr Opin Cell Biol 3 1991 422 428
    • (1991) Curr Opin Cell Biol , vol.3 , pp. 422-428
    • Smerdon, M.J.1
  • 17
    • 84863001577 scopus 로고    scopus 로고
    • Prime, repair, restore: The active role of chromatin in the DNA damage response
    • G. Soria, S.E. Polo, and G. Almouzni Prime, repair, restore: the active role of chromatin in the DNA damage response Mol Cell 46 2012 722 734
    • (2012) Mol Cell , vol.46 , pp. 722-734
    • Soria, G.1    Polo, S.E.2    Almouzni, G.3
  • 18
    • 0019132228 scopus 로고
    • Distribution within chromatin of deoxyribonucleic acid repair synthesis occurring at different times after ultraviolet radiation
    • M.J. Smerdon Distribution within chromatin of deoxyribonucleic acid repair synthesis occurring at different times after ultraviolet radiation Biochemistry 19 1980 2992 3000
    • (1980) Biochemistry , vol.19 , pp. 2992-3000
    • Smerdon, M.J.1
  • 19
    • 0018125018 scopus 로고
    • Nucleosome rearrangement in human chromatin during UV-induced DNA- reapir synthesis
    • M.J. Smerdon, and M.W. Lieberman Nucleosome rearrangement in human chromatin during UV-induced DNA- reapir synthesis Proc Natl Acad Sci USA 75 1978 4238 4241
    • (1978) Proc Natl Acad Sci USA , vol.75 , pp. 4238-4241
    • Smerdon, M.J.1    Lieberman, M.W.2
  • 20
    • 0025248784 scopus 로고
    • Isolation of 8-methoxypsoralen accessible DNA domains from chromatin of intact cells
    • G.A. Mathis, and F.R. Althaus Isolation of 8-methoxypsoralen accessible DNA domains from chromatin of intact cells Cell Biol Toxicol 6 1990 35 45
    • (1990) Cell Biol Toxicol , vol.6 , pp. 35-45
    • Mathis, G.A.1    Althaus, F.R.2
  • 21
    • 84880562168 scopus 로고    scopus 로고
    • Nucleotide excision repair in human cells: Fate of the excised oligonucleotide carrying DNA damage in vivo
    • J. Hu, J.-H. Choi, S. Gaddameedhi, M.G. Kemp, J.T. Reardon, and A. Sancar Nucleotide excision repair in human cells: fate of the excised oligonucleotide carrying DNA damage in vivo J Biol Chem 288 2013 20918 20926
    • (2013) J Biol Chem , vol.288 , pp. 20918-20926
    • Hu, J.1    Choi, J.-H.2    Gaddameedhi, S.3    Kemp, M.G.4    Reardon, J.T.5    Sancar, A.6
  • 22
    • 0037450761 scopus 로고    scopus 로고
    • P53 is a chromatin accessibility factor for nucleotide excision repair of DNA damage
    • C.P. Rubbi, and J. Milner p53 is a chromatin accessibility factor for nucleotide excision repair of DNA damage EMBO J 22 2003 975 986
    • (2003) EMBO J , vol.22 , pp. 975-986
    • Rubbi, C.P.1    Milner, J.2
  • 24
    • 84876328368 scopus 로고    scopus 로고
    • Poly(ADP-ribosyl)ation links the chromatin remodeler SMARCA5/SNF2H to RNF168-dependent DNA damage signaling
    • G. Smeenk, W.W. Wiegant, J.A. Marteijn, M.S. Luijsterburg, N. Sroczynski, and T. Costelloe Poly(ADP-ribosyl)ation links the chromatin remodeler SMARCA5/SNF2H to RNF168-dependent DNA damage signaling J Cell Sci 126 2013 889 903
    • (2013) J Cell Sci , vol.126 , pp. 889-903
    • Smeenk, G.1    Wiegant, W.W.2    Marteijn, J.A.3    Luijsterburg, M.S.4    Sroczynski, N.5    Costelloe, T.6
  • 25
    • 33749657892 scopus 로고    scopus 로고
    • PTMs on H3 variants before chromatin assembly potentiate their final epigenetic state
    • A. Loyola, T. Bonaldi, D. Roche, A. Imhof, and G. Almouzni PTMs on H3 variants before chromatin assembly potentiate their final epigenetic state Mol Cell 24 2006 309 316
    • (2006) Mol Cell , vol.24 , pp. 309-316
    • Loyola, A.1    Bonaldi, T.2    Roche, D.3    Imhof, A.4    Almouzni, G.5
  • 26
    • 0035954427 scopus 로고    scopus 로고
    • Kinetics of core histones in living human cells: Little exchange of H3 and H4 and some rapid exchange of H2B
    • H. Kimura, and P.R. Cook Kinetics of core histones in living human cells: little exchange of H3 and H4 and some rapid exchange of H2B J Cell Biol 153 2001 1341 1353
    • (2001) J Cell Biol , vol.153 , pp. 1341-1353
    • Kimura, H.1    Cook, P.R.2
  • 27
    • 35148894396 scopus 로고    scopus 로고
    • DNA damage-dependent acetylation and ubiquitination of H2AX enhances chromatin dynamics
    • T. Ikura, S. Tashiro, A. Kakino, H. Shima, N. Jacob, and R. Amunugama DNA damage-dependent acetylation and ubiquitination of H2AX enhances chromatin dynamics Mol Cell Biol 27 2007 7028 7040
    • (2007) Mol Cell Biol , vol.27 , pp. 7028-7040
    • Ikura, T.1    Tashiro, S.2    Kakino, A.3    Shima, H.4    Jacob, N.5    Amunugama, R.6
  • 28
    • 84870904979 scopus 로고    scopus 로고
    • Histone H2A.Z controls a critical chromatin remodeling step required for DNA double-strand break repair
    • Y. Xu, M.K. Ayrapetov, C. Xu, O. Gursoy-Yuzugullu, Y. Hu, and B.D. Price Histone H2A.Z controls a critical chromatin remodeling step required for DNA double-strand break repair Mol Cell 48 2012 723 733
    • (2012) Mol Cell , vol.48 , pp. 723-733
    • Xu, Y.1    Ayrapetov, M.K.2    Xu, C.3    Gursoy-Yuzugullu, O.4    Hu, Y.5    Price, B.D.6
  • 29
    • 77957738825 scopus 로고    scopus 로고
    • The p400 ATPase regulates nucleosome stability and chromatin ubiquitination during DNA repair
    • Y. Xu, Y. Sun, X. Jiang, M.K. Ayrapetov, P. Moskwa, and S. Yang The p400 ATPase regulates nucleosome stability and chromatin ubiquitination during DNA repair J Cell Biol 191 2010 31 43
    • (2010) J Cell Biol , vol.191 , pp. 31-43
    • Xu, Y.1    Sun, Y.2    Jiang, X.3    Ayrapetov, M.K.4    Moskwa, P.5    Yang, S.6
  • 30
    • 84868681561 scopus 로고    scopus 로고
    • Nucleolin participates in DNA double-strand break-induced damage response through MDC1-dependent pathway
    • [e49245-5]
    • J. Kobayashi, H. Fujimoto, J. Sato, I. Hayashi, S. Burma, and S. Matsuura Nucleolin participates in DNA double-strand break-induced damage response through MDC1-dependent pathway PLoS One 7 2011 [e49245-5]
    • (2011) PLoS One , vol.7
    • Kobayashi, J.1    Fujimoto, H.2    Sato, J.3    Hayashi, I.4    Burma, S.5    Matsuura, S.6
  • 31
    • 34447551681 scopus 로고    scopus 로고
    • Roles of ATM and NBS1 in chromatin structure modulation and DNA double-strand break repair
    • E. Berkovich, R.J. Monnat, and M.B. Kastan Roles of ATM and NBS1 in chromatin structure modulation and DNA double-strand break repair Nat Cell Biol 9 2007 683 690
    • (2007) Nat Cell Biol , vol.9 , pp. 683-690
    • Berkovich, E.1    Monnat, R.J.2    Kastan, M.B.3
  • 32
    • 84885708301 scopus 로고    scopus 로고
    • Nucleolin mediates nucleosome disruption critical for DNA double-strand break repair
    • M. Goldstein, F.A. Derheimer, J. Tait-Mulder, and M.B. Kastan Nucleolin mediates nucleosome disruption critical for DNA double-strand break repair Proc Natl Acad Sci USA 110 2013 16874 16879
    • (2013) Proc Natl Acad Sci USA , vol.110 , pp. 16874-16879
    • Goldstein, M.1    Derheimer, F.A.2    Tait-Mulder, J.3    Kastan, M.B.4
  • 33
    • 84871942311 scopus 로고    scopus 로고
    • The chromatin remodeler p400 ATPase facilitates Rad51-mediated repair of DNA double-strand breaks
    • C. Courilleau, C. Chailleux, A. Jauneau, F. Grimal, S. Briois, and E. Boutet-Robinet The chromatin remodeler p400 ATPase facilitates Rad51-mediated repair of DNA double-strand breaks J Cell Biol 199 2012 1067 1081
    • (2012) J Cell Biol , vol.199 , pp. 1067-1081
    • Courilleau, C.1    Chailleux, C.2    Jauneau, A.3    Grimal, F.4    Briois, S.5    Boutet-Robinet, E.6
  • 35
    • 0020371381 scopus 로고
    • Effect of histone H1 removal on the distribution of ultraviolet-induced deoxyribonucleic acid repair synthesis within chromatin
    • M.J. Smerdon, J.F. Watkins, and M.W. Lieberman Effect of histone H1 removal on the distribution of ultraviolet-induced deoxyribonucleic acid repair synthesis within chromatin Biochemistry 21 1982 3879 3885
    • (1982) Biochemistry , vol.21 , pp. 3879-3885
    • Smerdon, M.J.1    Watkins, J.F.2    Lieberman, M.W.3
  • 36
    • 33745212870 scopus 로고    scopus 로고
    • Methods for studying chromatin assembly coupled to DNA repair
    • A. Gérard, S.E. Polo, D. Roche, and G. Almouzni Methods for studying chromatin assembly coupled to DNA repair Methods Enzymol 409 2006 358 374
    • (2006) Methods Enzymol , vol.409 , pp. 358-374
    • Gérard, A.1    Polo, S.E.2    Roche, D.3    Almouzni, G.4
  • 37
    • 84866954036 scopus 로고    scopus 로고
    • Chromatin dynamics during nucleotide excision repair: Histones on the move
    • S. Adam, and S.E. Polo Chromatin dynamics during nucleotide excision repair: histones on the move IJMS 13 2012 11895 11911
    • (2012) IJMS , vol.13 , pp. 11895-11911
    • Adam, S.1    Polo, S.E.2
  • 38
    • 33750449326 scopus 로고    scopus 로고
    • New histone incorporation marks sites of UV repair in human cells
    • S.E. Polo, D. Roche, and G. Almouzni New histone incorporation marks sites of UV repair in human cells Cell 127 2006 481 493
    • (2006) Cell , vol.127 , pp. 481-493
    • Polo, S.E.1    Roche, D.2    Almouzni, G.3
  • 39
    • 84882585259 scopus 로고    scopus 로고
    • Enhanced chromatin dynamics by FACT promotes transcriptional restart after UV-induced DNA damage
    • C. Dinant, G. Ampatziadis-Michailidis, H. Lans, M. Tresini, A. Lagarou, and M. Grosbart Enhanced chromatin dynamics by FACT promotes transcriptional restart after UV-induced DNA damage Mol Cell 51 2013 469 479
    • (2013) Mol Cell , vol.51 , pp. 469-479
    • Dinant, C.1    Ampatziadis-Michailidis, G.2    Lans, H.3    Tresini, M.4    Lagarou, A.5    Grosbart, M.6
  • 40
    • 84884889017 scopus 로고    scopus 로고
    • Transcription recovery after DNA damage requires chromatin priming by the H3.3 histone chaperone HIRA
    • S. Adam, S.E. Polo, and G. Almouzni Transcription recovery after DNA damage requires chromatin priming by the H3.3 histone chaperone HIRA Cell 155 2013 94 106
    • (2013) Cell , vol.155 , pp. 94-106
    • Adam, S.1    Polo, S.E.2    Almouzni, G.3
  • 41
    • 84880048047 scopus 로고    scopus 로고
    • Histone acetyltransferase 1 promotes homologous recombination in DNA repair by facilitating histone turnover
    • X. Yang, L. Li, J. Liang, L. Shi, J. Yang, and X. Yi Histone acetyltransferase 1 promotes homologous recombination in DNA repair by facilitating histone turnover J Biol Chem 288 2013 18271 18282
    • (2013) J Biol Chem , vol.288 , pp. 18271-18282
    • Yang, X.1    Li, L.2    Liang, J.3    Shi, L.4    Yang, J.5    Yi, X.6
  • 43
    • 84884897397 scopus 로고    scopus 로고
    • Remodeling and spacing factor 1 (RSF1) deposits centromere proteins at DNA double-strand breaks to promote non-homologous end-joining
    • A. Helfricht, W.W. Wiegant, P.E. Thijssen, A.C. Vertegaal, M.S. Luijsterburg, and H. van Attikum Remodeling and spacing factor 1 (RSF1) deposits centromere proteins at DNA double-strand breaks to promote non-homologous end-joining Cell Cycle 12 2013 3070 3082
    • (2013) Cell Cycle , vol.12 , pp. 3070-3082
    • Helfricht, A.1    Wiegant, W.W.2    Thijssen, P.E.3    Vertegaal, A.C.4    Luijsterburg, M.S.5    Van Attikum, H.6
  • 44
    • 84896868698 scopus 로고    scopus 로고
    • H2A.Z depletion impairs proliferation and viability but not DNA double-strand breaks repair in human immortalized and tumoral cell lines
    • G.-C. Taty-Taty, C. Courilleau, M. Quaranta, A. Carayon, C. Chailleux, and F. Aymard H2A.Z depletion impairs proliferation and viability but not DNA double-strand breaks repair in human immortalized and tumoral cell lines Cell Cycle 13 2014 399 407
    • (2014) Cell Cycle , vol.13 , pp. 399-407
    • Taty-Taty, G.-C.1    Courilleau, C.2    Quaranta, M.3    Carayon, A.4    Chailleux, C.5    Aymard, F.6
  • 47
    • 84868093509 scopus 로고    scopus 로고
    • The histone variant macroH2A1.1 is recruited to DSBs through a mechanism involving PARP1
    • C. Xu, Y. Xu, O. Gursoy-Yuzugullu, and B.D. Price The histone variant macroH2A1.1 is recruited to DSBs through a mechanism involving PARP1 FEBS Lett 586 2012 3920 3925
    • (2012) FEBS Lett , vol.586 , pp. 3920-3925
    • Xu, C.1    Xu, Y.2    Gursoy-Yuzugullu, O.3    Price, B.D.4
  • 48
    • 84859485912 scopus 로고    scopus 로고
    • Monoubiquitinated histone H2A destabilizes photolesion-containing nucleosomes with concomitant release of UV-damaged DNA-binding protein E3 ligase
    • L. Lan, S. Nakajima, M.G. Kapetanaki, C.L. Hsieh, M. Fagerburg, and K. Thickman Monoubiquitinated histone H2A destabilizes photolesion-containing nucleosomes with concomitant release of UV-damaged DNA-binding protein E3 ligase J Biol Chem 287 2012 12036 12049
    • (2012) J Biol Chem , vol.287 , pp. 12036-12049
    • Lan, L.1    Nakajima, S.2    Kapetanaki, M.G.3    Hsieh, C.L.4    Fagerburg, M.5    Thickman, K.6
  • 49
    • 33744781568 scopus 로고    scopus 로고
    • Histone H3 and H4 ubiquitylation by the CUL4-DDB-ROC1 ubiquitin ligase facilitates cellular response to DNA damage
    • H. Wang, L. Zhai, J. Xu, H.-Y. Joo, S. Jackson, and H. Erdjument-Bromage Histone H3 and H4 ubiquitylation by the CUL4-DDB-ROC1 ubiquitin ligase facilitates cellular response to DNA damage Mol Cell 22 2006 383 394
    • (2006) Mol Cell , vol.22 , pp. 383-394
    • Wang, H.1    Zhai, L.2    Xu, J.3    Joo, H.-Y.4    Jackson, S.5    Erdjument-Bromage, H.6
  • 50
    • 84878314537 scopus 로고    scopus 로고
    • Acetylation-mediated proteasomal degradation of core histones during DNA repair and spermatogenesis
    • M.-X. Qian, Y. Pang, C.H. Liu, K. Haratake, B.-Y. Du, and D.-Y. Ji Acetylation-mediated proteasomal degradation of core histones during DNA repair and spermatogenesis Cell 153 2013 1012 1024
    • (2013) Cell , vol.153 , pp. 1012-1024
    • Qian, M.-X.1    Pang, Y.2    Liu, C.H.3    Haratake, K.4    Du, B.-Y.5    Ji, D.-Y.6
  • 51
    • 84856278412 scopus 로고    scopus 로고
    • ATP-dependent chromatin remodeling in the DNA-damage response
    • H. Lans, J.A. Marteijn, and W. Vermeulen ATP-dependent chromatin remodeling in the DNA-damage response Epigenetics Chromatin 5 2012 4
    • (2012) Epigenetics Chromatin , vol.5 , pp. 4
    • Lans, H.1    Marteijn, J.A.2    Vermeulen, W.3
  • 52
    • 78049241459 scopus 로고    scopus 로고
    • INO80 chromatin remodeling complex promotes the removal of UV lesions by the nucleotide excision repair pathway
    • Y. Jiang, X. Wang, S. Bao, R. Guo, D.G. Johnson, and X. Shen INO80 chromatin remodeling complex promotes the removal of UV lesions by the nucleotide excision repair pathway Proc Natl Acad Sci USA 107 2010 17274 17279
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 17274-17279
    • Jiang, Y.1    Wang, X.2    Bao, S.3    Guo, R.4    Johnson, D.G.5    Shen, X.6
  • 53
    • 71049159100 scopus 로고    scopus 로고
    • Modulation of nucleotide excision repair by mammalian SWI/SNF chromatin-remodeling complex
    • Q. Zhao, Q.-E. Wang, A. Ray, G. Wani, C. Han, and K. Milum Modulation of nucleotide excision repair by mammalian SWI/SNF chromatin-remodeling complex J Biol Chem 284 2009 30424 30432
    • (2009) J Biol Chem , vol.284 , pp. 30424-30432
    • Zhao, Q.1    Wang, Q.-E.2    Ray, A.3    Wani, G.4    Han, C.5    Milum, K.6
  • 54
    • 84893460190 scopus 로고    scopus 로고
    • The catalytic subunit of the SWR1 remodeler is a histone chaperone for the H2A.Z-H2B dimer
    • J. Hong, H. Feng, F. Wang, A. Ranjan, J. Chen, and J. Jiang The catalytic subunit of the SWR1 remodeler is a histone chaperone for the H2A.Z-H2B dimer Mol Cell 53 2014 498 505
    • (2014) Mol Cell , vol.53 , pp. 498-505
    • Hong, J.1    Feng, H.2    Wang, F.3    Ranjan, A.4    Chen, J.5    Jiang, J.6
  • 55
    • 84857122396 scopus 로고
    • Chaperoning the histone H3 family
    • A. Hamiche, and M. Shuaib Chaperoning the histone H3 family Biochim Biophys Acta 2013 1819 230 237
    • (1819) Biochim Biophys Acta , vol.2013 , pp. 230-237
    • Hamiche, A.1    Shuaib, M.2
  • 56
    • 0024372060 scopus 로고
    • Purification and characterization of CAF-I, a human cell factor required for chromatin assembly during DNA replication in vitro
    • S. Smith, and B. Stillman Purification and characterization of CAF-I, a human cell factor required for chromatin assembly during DNA replication in vitro Cell 58 1989 15 25
    • (1989) Cell , vol.58 , pp. 15-25
    • Smith, S.1    Stillman, B.2
  • 57
    • 0742304304 scopus 로고    scopus 로고
    • Histone H3.1 and H3.3 complexes mediate nucleosome assembly pathways dependent or independent of DNA synthesis
    • H. Tagami, D. Ray-Gallet, G. Almouzni, and Y. Nakatani Histone H3.1 and H3.3 complexes mediate nucleosome assembly pathways dependent or independent of DNA synthesis Cell 116 2004 51 61
    • (2004) Cell , vol.116 , pp. 51-61
    • Tagami, H.1    Ray-Gallet, D.2    Almouzni, G.3    Nakatani, Y.4
  • 58
    • 0022519177 scopus 로고
    • Chromatin assembly during SV40 DNA replication in vitro
    • B. Stillman Chromatin assembly during SV40 DNA replication in vitro Cell 45 1986 555 565
    • (1986) Cell , vol.45 , pp. 555-565
    • Stillman, B.1
  • 59
    • 84255162049 scopus 로고    scopus 로고
    • Dynamics of histone h3 deposition in vivo reveal a nucleosome gap-filling mechanism for h3.3 to maintain chromatin integrity
    • D. Ray-Gallet, A. Woolfe, I. Vassias, C. Pellentz, N. Lacoste, and A. Puri Dynamics of histone h3 deposition in vivo reveal a nucleosome gap-filling mechanism for h3.3 to maintain chromatin integrity Mol Cell 44 2011 928 941
    • (2011) Mol Cell , vol.44 , pp. 928-941
    • Ray-Gallet, D.1    Woolfe, A.2    Vassias, I.3    Pellentz, C.4    Lacoste, N.5    Puri, A.6
  • 61
    • 0036250827 scopus 로고    scopus 로고
    • Human Asf1 and CAF-1 interact and synergize in a repair-coupled nucleosome assembly pathway
    • J.A. Mello, H.H.W. Silljé, D.M.J. Roche, D.B. Kirschner, E.A. Nigg, and G. Almouzni Human Asf1 and CAF-1 interact and synergize in a repair-coupled nucleosome assembly pathway EMBO Rep 3 2002 329 334
    • (2002) EMBO Rep , vol.3 , pp. 329-334
    • Mello, J.A.1    Silljé, H.H.W.2    Roche, D.M.J.3    Kirschner, D.B.4    Nigg, E.A.5    Almouzni, G.6
  • 62
    • 0032476713 scopus 로고    scopus 로고
    • Recruitment of phosphorylated chromatin assembly factor 1 to chromatin after UV irradiation of human cells
    • E. Martini, D.M. Roche, K. Marheineke, A. Verreault, and G. Almouzni Recruitment of phosphorylated chromatin assembly factor 1 to chromatin after UV irradiation of human cells J Cell Biol 143 1998 563 575
    • (1998) J Cell Biol , vol.143 , pp. 563-575
    • Martini, E.1    Roche, D.M.2    Marheineke, K.3    Verreault, A.4    Almouzni, G.5
  • 63
    • 0141530885 scopus 로고    scopus 로고
    • Local action of the chromatin assembly factor CAF-1 at sites of nucleotide excision repair in vivo
    • C.M. Green, and G. Almouzni Local action of the chromatin assembly factor CAF-1 at sites of nucleotide excision repair in vivo EMBO J 22 2003 5163 5174
    • (2003) EMBO J , vol.22 , pp. 5163-5174
    • Green, C.M.1    Almouzni, G.2
  • 66
    • 84857781943 scopus 로고    scopus 로고
    • A genome-wide homologous recombination screen identifies the RNA-binding protein RBMX as a component of the DNA-damage response
    • B. Adamson, A. Smogorzewska, F.D. Sigoillot, R.W. King, and S.J. Elledge A genome-wide homologous recombination screen identifies the RNA-binding protein RBMX as a component of the DNA-damage response Nat Cell Biol 14 2012 318 328
    • (2012) Nat Cell Biol , vol.14 , pp. 318-328
    • Adamson, B.1    Smogorzewska, A.2    Sigoillot, F.D.3    King, R.W.4    Elledge, S.J.5
  • 67
    • 84874469720 scopus 로고    scopus 로고
    • Chromatin remodeling defects in pediatric and young adult glioblastoma: A tale of a variant histone 3 tail
    • A.M. Fontebasso, X.-Y. Liu, D. Sturm, and N. Jabado Chromatin remodeling defects in pediatric and young adult glioblastoma: a tale of a variant histone 3 tail Brain Pathol 23 2013 210 216
    • (2013) Brain Pathol , vol.23 , pp. 210-216
    • Fontebasso, A.M.1    Liu, X.-Y.2    Sturm, D.3    Jabado, N.4
  • 68
    • 84887512911 scopus 로고    scopus 로고
    • Histone H3.3 mutations: A variant path to cancer
    • B.T.K. Yuen, and P.S. Knoepfler Histone H3.3 mutations: a variant path to cancer Cancer Cell 24 2013 567 574
    • (2013) Cancer Cell , vol.24 , pp. 567-574
    • Yuen, B.T.K.1    Knoepfler, P.S.2
  • 69
    • 84888353557 scopus 로고    scopus 로고
    • Distinct H3F3A and H3F3B driver mutations define chondroblastoma and giant cell tumor of bone
    • S. Behjati, P.S. Tarpey, N. Presneau, S. Scheipl, N. Pillay, and P. Van Loo Distinct H3F3A and H3F3B driver mutations define chondroblastoma and giant cell tumor of bone Nat Genet 45 2013 1479 1482
    • (2013) Nat Genet , vol.45 , pp. 1479-1482
    • Behjati, S.1    Tarpey, P.S.2    Presneau, N.3    Scheipl, S.4    Pillay, N.5    Van Loo, P.6
  • 70
    • 84883304136 scopus 로고    scopus 로고
    • WHSC1 links transcription elongation to HIRA-mediated histone H3.3 deposition
    • N. Sarai, K. Nimura, T. Tamura, T. Kanno, M.C. Patel, and T.D. Heightman WHSC1 links transcription elongation to HIRA-mediated histone H3.3 deposition EMBO J 32 2013 2392 2406
    • (2013) EMBO J , vol.32 , pp. 2392-2406
    • Sarai, N.1    Nimura, K.2    Tamura, T.3    Kanno, T.4    Patel, M.C.5    Heightman, T.D.6
  • 71
    • 84880074392 scopus 로고    scopus 로고
    • Single cell analysis of RNA-mediated histone H3.3 recruitment to a cytomegalovirus promoter-regulated transcription site
    • A. Newhart, I.U. Rafalska-Metcalf, T. Yang, L.M. Joo, S.L. Powers, and A.V. Kossenkov Single cell analysis of RNA-mediated histone H3.3 recruitment to a cytomegalovirus promoter-regulated transcription site J Biol Chem 288 2013 19882 19899
    • (2013) J Biol Chem , vol.288 , pp. 19882-19899
    • Newhart, A.1    Rafalska-Metcalf, I.U.2    Yang, T.3    Joo, L.M.4    Powers, S.L.5    Kossenkov, A.V.6
  • 72
    • 77953955724 scopus 로고    scopus 로고
    • The death-associated protein DAXX is a novel histone chaperone involved in the replication-independent deposition of H3.3
    • P. Drané, K. Ouararhni, A. Depaux, M. Shuaib, and A. Hamiche The death-associated protein DAXX is a novel histone chaperone involved in the replication-independent deposition of H3.3 Genes Dev 24 2010 1253 1265
    • (2010) Genes Dev , vol.24 , pp. 1253-1265
    • Drané, P.1    Ouararhni, K.2    Depaux, A.3    Shuaib, M.4    Hamiche, A.5
  • 73
    • 77649099092 scopus 로고    scopus 로고
    • Distinct factors control histone variant H3.3 localization at specific genomic regions
    • A.D. Goldberg, L.A. Banaszynski, K.-M. Noh, P.W. Lewis, S.J. Elsaesser, and S. Stadler Distinct factors control histone variant H3.3 localization at specific genomic regions Cell 140 2010 678 691
    • (2010) Cell , vol.140 , pp. 678-691
    • Goldberg, A.D.1    Banaszynski, L.A.2    Noh, K.-M.3    Lewis, P.W.4    Elsaesser, S.J.5    Stadler, S.6
  • 74
    • 84894244513 scopus 로고    scopus 로고
    • Mislocalization of the centromeric histone variant CenH3/CENP-A in human cells depends on the chaperone DAXX
    • N. Lacoste, A. Woolfe, H. Tachiwana, A.V. Garea, T. Barth, and S. Cantaloube Mislocalization of the centromeric histone variant CenH3/CENP-A in human cells depends on the chaperone DAXX Mol Cell 53 2014 631 644
    • (2014) Mol Cell , vol.53 , pp. 631-644
    • Lacoste, N.1    Woolfe, A.2    Tachiwana, H.3    Garea, A.V.4    Barth, T.5    Cantaloube, S.6
  • 76
    • 41549112501 scopus 로고    scopus 로고
    • FACT-mediated exchange of histone variant H2AX regulated by phosphorylation of H2AX and ADP-ribosylation of Spt16
    • K. Heo, H. Kim, S.H. Choi, J. Choi, K. Kim, and J. Gu FACT-mediated exchange of histone variant H2AX regulated by phosphorylation of H2AX and ADP-ribosylation of Spt16 Mol Cell 30 2008 86 97
    • (2008) Mol Cell , vol.30 , pp. 86-97
    • Heo, K.1    Kim, H.2    Choi, S.H.3    Choi, J.4    Kim, K.5    Gu, J.6
  • 77
    • 33646841045 scopus 로고    scopus 로고
    • Modulation of nucleosome-binding activity of FACT by poly(ADP-ribosyl)ation
    • J. Huang, W. Chen, Y. Chang, H. Wang, W. Chuang, and S. Lee Modulation of nucleosome-binding activity of FACT by poly(ADP-ribosyl)ation Nucleic Acids Res 34 2006 2398 2407
    • (2006) Nucleic Acids Res , vol.34 , pp. 2398-2407
    • Huang, J.1    Chen, W.2    Chang, Y.3    Wang, H.4    Chuang, W.5    Lee, S.6
  • 78
    • 33847226680 scopus 로고    scopus 로고
    • Structure and function of the histone chaperone CIA/ASF1 complexed with histones H3 and H4
    • R. Natsume, M. Eitoku, Y. Akai, N. Sano, M. Horikoshi, and T. Senda Structure and function of the histone chaperone CIA/ASF1 complexed with histones H3 and H4 Nature 446 2007 338 341
    • (2007) Nature , vol.446 , pp. 338-341
    • Natsume, R.1    Eitoku, M.2    Akai, Y.3    Sano, N.4    Horikoshi, M.5    Senda, T.6
  • 79
    • 37549049820 scopus 로고    scopus 로고
    • Regulation of replication fork progression through histone supply and demand
    • A. Groth, A. Corpet, A.J.L. Cook, D. Roche, J. Bartek, and J. Lukas Regulation of replication fork progression through histone supply and demand Science 318 2007 1928 1931
    • (2007) Science , vol.318 , pp. 1928-1931
    • Groth, A.1    Corpet, A.2    Cook, A.J.L.3    Roche, D.4    Bartek, J.5    Lukas, J.6
  • 80
    • 84863139249 scopus 로고    scopus 로고
    • Human histone acetyltransferase 1 protein preferentially acetylates H4 histone molecules in H3.1-H4 over H3.3-H4
    • H. Zhang, J. Han, Bin Kang, R. Burgess, and Z. Zhang Human histone acetyltransferase 1 protein preferentially acetylates H4 histone molecules in H3.1-H4 over H3.3-H4 J Biol Chem 287 2012 6573 6581
    • (2012) J Biol Chem , vol.287 , pp. 6573-6581
    • Zhang, H.1    Han, J.2    Kang, B.3    Burgess, R.4    Zhang, Z.5
  • 81
    • 79959967141 scopus 로고    scopus 로고
    • Phosphorylation of H4 ser 47 promotes HIRA-mediated nucleosome assembly
    • B. Kang, M. Pu, G. Hu, W. Wen, Z. Dong, and K. Zhao Phosphorylation of H4 Ser 47 promotes HIRA-mediated nucleosome assembly Genes Dev 25 2011 1359 1364
    • (2011) Genes Dev , vol.25 , pp. 1359-1364
    • Kang, B.1    Pu, M.2    Hu, G.3    Wen, W.4    Dong, Z.5    Zhao, K.6
  • 82
    • 84894048601 scopus 로고    scopus 로고
    • Histone chaperone FACT regulates homologous recombination by chromatin remodeling through interaction with RNF20
    • D.V. Oliveira, A. Kato, K. Nakamura, T. Ikura, M. Okada, and J. Kobayashi Histone chaperone FACT regulates homologous recombination by chromatin remodeling through interaction with RNF20 J Cell Sci 127 2014 763 772
    • (2014) J Cell Sci , vol.127 , pp. 763-772
    • Oliveira, D.V.1    Kato, A.2    Nakamura, K.3    Ikura, T.4    Okada, M.5    Kobayashi, J.6
  • 83
    • 77951498720 scopus 로고    scopus 로고
    • A cooperative activation loop among SWI/SNF, gamma-H2AX and H3 acetylation for DNA double-strand break repair
    • H.-S. Lee, J.-H. Park, S.J. Kim, S.-J. Kwon, and J. Kwon A cooperative activation loop among SWI/SNF, gamma-H2AX and H3 acetylation for DNA double-strand break repair EMBO J 29 2010 1434 1445
    • (2010) EMBO J , vol.29 , pp. 1434-1445
    • Lee, H.-S.1    Park, J.-H.2    Kim, S.J.3    Kwon, S.-J.4    Kwon, J.5
  • 84
    • 84896933603 scopus 로고    scopus 로고
    • Histone H3 lysine 14 (H3K14) acetylation facilitates DNA repair in a positioned nucleosome by stabilizing the binding of the chromatin remodeler RSC (Remodels Structure of Chromatin)
    • M.-R. Duan, and M.J. Smerdon Histone H3 lysine 14 (H3K14) acetylation facilitates DNA repair in a positioned nucleosome by stabilizing the binding of the chromatin remodeler RSC (Remodels Structure of Chromatin) J Biol Chem 289 2014 8353 8363
    • (2014) J Biol Chem , vol.289 , pp. 8353-8363
    • Duan, M.-R.1    Smerdon, M.J.2
  • 87
    • 84900463508 scopus 로고    scopus 로고
    • One ring to bring them all - The role of Ku in mammalian non-homologous end joining
    • G.J. Grundy, H.A. Moulding, K.W. Caldecott, and S.L. Rulten One ring to bring them all - the role of Ku in mammalian non-homologous end joining DNA Repair (Amst) 17 2014 30 38
    • (2014) DNA Repair (Amst) , vol.17 , pp. 30-38
    • Grundy, G.J.1    Moulding, H.A.2    Caldecott, K.W.3    Rulten, S.L.4
  • 88
    • 38049064044 scopus 로고    scopus 로고
    • Poly(ADP-ribose)-binding zinc finger motifs in DNA repair/checkpoint proteins
    • I. Ahel, D. Ahel, T. Matsusaka, A.J. Clark, J. Pines, and S.J. Boulton Poly(ADP-ribose)-binding zinc finger motifs in DNA repair/checkpoint proteins Nature 451 2008 81 85
    • (2008) Nature , vol.451 , pp. 81-85
    • Ahel, I.1    Ahel, D.2    Matsusaka, T.3    Clark, A.J.4    Pines, J.5    Boulton, S.J.6
  • 89
    • 77956870690 scopus 로고    scopus 로고
    • Regulation of DNA-damage responses and cell-cycle progression by the chromatin remodelling factor CHD4
    • S.E. Polo, A. Kaidi, L. Baskcomb, Y. Galanty, and S.P. Jackson Regulation of DNA-damage responses and cell-cycle progression by the chromatin remodelling factor CHD4 EMBO J 29 2010 3130 3139
    • (2010) EMBO J , vol.29 , pp. 3130-3139
    • Polo, S.E.1    Kaidi, A.2    Baskcomb, L.3    Galanty, Y.4    Jackson, S.P.5
  • 90
    • 69949123856 scopus 로고    scopus 로고
    • Poly(ADP-ribose)-dependent regulation of DNA repair by the chromatin remodeling enzyme ALC1
    • D. Ahel, Z. Horejsí, N. Wiechens, S.E. Polo, E. Garcia-Wilson, and I. Ahel Poly(ADP-ribose)-dependent regulation of DNA repair by the chromatin remodeling enzyme ALC1 Science 325 2009 1240 1243
    • (2009) Science , vol.325 , pp. 1240-1243
    • Ahel, D.1    Horejsí, Z.2    Wiechens, N.3    Polo, S.E.4    Garcia-Wilson, E.5    Ahel, I.6
  • 91
    • 78649349810 scopus 로고    scopus 로고
    • A chromatin localization screen reveals poly (ADP ribose)-regulated recruitment of the repressive polycomb and NuRD complexes to sites of DNA damage
    • D.M. Chou, B. Adamson, N.E. Dephoure, X. Tan, A.C. Nottke, and K.E. Hurov A chromatin localization screen reveals poly (ADP ribose)-regulated recruitment of the repressive polycomb and NuRD complexes to sites of DNA damage Proc Natl Acad Sci USA 107 2010 18475 18480
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 18475-18480
    • Chou, D.M.1    Adamson, B.2    Dephoure, N.E.3    Tan, X.4    Nottke, A.C.5    Hurov, K.E.6
  • 92
    • 69549083315 scopus 로고    scopus 로고
    • Poly(ADP-ribosyl)ation directs recruitment and activation of an ATP-dependent chromatin remodeler
    • A.J. Gottschalk, G. Timinszky, S.E. Kong, J. Jin, Y. Cai, and S.K. Swanson Poly(ADP-ribosyl)ation directs recruitment and activation of an ATP-dependent chromatin remodeler Proc Natl Acad Sci USA 106 2009 13770 13774
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 13770-13774
    • Gottschalk, A.J.1    Timinszky, G.2    Kong, S.E.3    Jin, J.4    Cai, Y.5    Swanson, S.K.6
  • 93
    • 70449518412 scopus 로고    scopus 로고
    • Histone H3 methylation links DNA damage detection to activation of the tumour suppressor Tip60
    • Y. Sun, X. Jiang, Y. Xu, M.K. Ayrapetov, L.A. Moreau, and J.R. Whetstine Histone H3 methylation links DNA damage detection to activation of the tumour suppressor Tip60 Nat Cell Biol 11 2009 1376 1382
    • (2009) Nat Cell Biol , vol.11 , pp. 1376-1382
    • Sun, Y.1    Jiang, X.2    Xu, Y.3    Ayrapetov, M.K.4    Moreau, L.A.5    Whetstine, J.R.6
  • 94
    • 84869102655 scopus 로고    scopus 로고
    • The emerging role of Polycomb repressors in the response to DNA damage
    • J.H.A. Vissers, M. van Lohuizen, and E. Citterio The emerging role of Polycomb repressors in the response to DNA damage J Cell Sci 125 2012 3939 3948
    • (2012) J Cell Sci , vol.125 , pp. 3939-3948
    • Vissers, J.H.A.1    Van Lohuizen, M.2    Citterio, E.3
  • 95
    • 62849083222 scopus 로고    scopus 로고
    • The emerging role of nuclear architecture in DNA repair and genome maintenance
    • T. Misteli, and E. Soutoglou The emerging role of nuclear architecture in DNA repair and genome maintenance Nat Rev Mol Cell Biol 10 2009 243 254
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 243-254
    • Misteli, T.1    Soutoglou, E.2
  • 96
    • 84886751857 scopus 로고    scopus 로고
    • DNA in motion during double-strand break repair
    • J. Miné-Hattab, and R. Rothstein DNA in motion during double-strand break repair Trends Cell Biol 23 2013 529 536
    • (2013) Trends Cell Biol , vol.23 , pp. 529-536
    • Miné-Hattab, J.1    Rothstein, R.2
  • 97
    • 84875207723 scopus 로고    scopus 로고
    • Chromatin movement in the maintenance of genome stability
    • V. Dion, and S.M. Gasser Chromatin movement in the maintenance of genome stability Cell 152 2013 1355 1364
    • (2013) Cell , vol.152 , pp. 1355-1364
    • Dion, V.1    Gasser, S.M.2


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