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Volumn 5, Issue 1, 2012, Pages

Deacetylation of H4-K16Ac and heterochromatin assembly in senescence

Author keywords

[No Author keywords available]

Indexed keywords

HIGH MOBILITY GROUP A1A PROTEIN; HIGH MOBILITY GROUP A2 PROTEIN; HISTONE DEACETYLASE 3; HISTONE H4; LYSINE; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; PROTEIN P16; SIRTUIN 2; TRICHOSTATIN A;

EID: 84865419712     PISSN: None     EISSN: 17568935     Source Type: Journal    
DOI: 10.1186/1756-8935-5-15     Document Type: Article
Times cited : (34)

References (61)
  • 1
    • 34948839944 scopus 로고    scopus 로고
    • Facultative Heterochromatin: Is There a Distinctive Molecular Signature?
    • DOI 10.1016/j.molcel.2007.09.011, PII S1097276507006235
    • Facultative heterochromatin: is there a distinctive molecular signature? Trojer P, Reinberg D, Mol Cell 2007 28 1 1 13 10.1016/j.molcel.2007.09.011 17936700 (Pubitemid 47531977)
    • (2007) Molecular Cell , vol.28 , Issue.1 , pp. 1-13
    • Trojer, P.1    Reinberg, D.2
  • 2
    • 33847076849 scopus 로고    scopus 로고
    • Chromatin Modifications and Their Function
    • DOI 10.1016/j.cell.2007.02.005, PII S0092867407001845
    • Chromatin modifications and their function. Kouzarides T, Cell 2007 128 4 693 705 10.1016/j.cell.2007.02.005 17320507 (Pubitemid 46273577)
    • (2007) Cell , vol.128 , Issue.4 , pp. 693-705
    • Kouzarides, T.1
  • 3
    • 34547875013 scopus 로고    scopus 로고
    • +-dependent deacetylation of H4 lysine 16 by class III HDACs
    • DOI 10.1038/sj.onc.1210617, PII 1210617
    • NAD+dependent deacetylation of H4 lysine 16 by class III HDACs. Vaquero A, Sternglanz R, Reinberg D, Oncogene 2007 26 37 5505 5520 10.1038/sj.onc. 1210617 17694090 (Pubitemid 47255931)
    • (2007) Oncogene , vol.26 , Issue.37 , pp. 5505-5520
    • Vaquero, A.1    Sternglanz, R.2    Reinberg, D.3
  • 4
    • 79953148278 scopus 로고    scopus 로고
    • The effects of histone H4 tail acetylations on cation-induced chromatin folding and self-association
    • 10.1093/nar/gkq900 21047799
    • The effects of histone H4 tail acetylations on cation-induced chromatin folding and self-association. Allahverdi A, Yang R, Korolev N, Fan Y, Davey CA, Liu CF, Nordenskiold L, Nucleic Acids Res 2011 39 5 1680 1691 10.1093/nar/gkq900 21047799
    • (2011) Nucleic Acids Res , vol.39 , Issue.5 , pp. 1680-1691
    • Allahverdi, A.1    Yang, R.2    Korolev, N.3    Fan, Y.4    Davey, C.A.5    Liu, C.F.6    Nordenskiold, L.7
  • 5
    • 32444434989 scopus 로고    scopus 로고
    • Histone H4-K16 acetylation controls chromatin structure and protein interactions
    • DOI 10.1126/science.1124000
    • Histone H4-K16 acetylation controls chromatin structure and protein interactions. Shogren-Knaak M, Ishii H, Sun JM, Pazin MJ, Davie JR, Peterson CL, Science 2006 311 5762 844 847 10.1126/science.1124000 16469925 (Pubitemid 43228847)
    • (2006) Science , vol.311 , Issue.5762 , pp. 844-847
    • Shogren-Knaak, M.1    Ishii, H.2    Sun, J.-M.3    Pazin, M.J.4    Davie, J.R.5    Peterson, C.L.6
  • 6
    • 48449106172 scopus 로고    scopus 로고
    • 30 nm chromatin fibre decompaction requires both H4-K16 acetylation and linker histone eviction
    • 10.1016/j.jmb.2008.04.050 18653199
    • - 30 nm chromatin fibre decompaction requires both H4-K16 acetylation and linker histone eviction. Robinson PJ, An W, Routh A, Martino F, Chapman L, Roeder RG, Rhodes D, J Mol Biol 2008 381 4 816 825 10.1016/j.jmb.2008.04.050 18653199
    • (2008) J Mol Biol , vol.381 , Issue.4 , pp. 816-825
    • Robinson, P.J.1    An, W.2    Routh, A.3    Martino, F.4    Chapman, L.5    Roeder, R.G.6    Rhodes, D.7
  • 7
    • 70149112313 scopus 로고    scopus 로고
    • Histone crosstalk between H3S10ph and H4K16ac generates a histone code that mediates transcription elongation
    • 10.1016/j.cell.2009.07.031 19766566
    • Histone crosstalk between H3S10ph and H4K16ac generates a histone code that mediates transcription elongation. Zippo A, Serafini R, Rocchigiani M, Pennacchini S, Krepelova A, Oliviero S, Cell 2009 138 6 1122 1136 10.1016/j.cell.2009.07.031 19766566
    • (2009) Cell , vol.138 , Issue.6 , pp. 1122-1136
    • Zippo, A.1    Serafini, R.2    Rocchigiani, M.3    Pennacchini, S.4    Krepelova, A.5    Oliviero, S.6
  • 8
    • 70349170114 scopus 로고    scopus 로고
    • Reconstitution of heterochromatin-dependent transcriptional gene silencing
    • 10.1016/j.molcel.2009.07.030 19782027
    • Reconstitution of heterochromatin-dependent transcriptional gene silencing. Johnson A, Li G, Sikorski TW, Buratowski S, Woodcock CL, Moazed D, Mol Cell 2009 35 6 769 781 10.1016/j.molcel.2009.07.030 19782027
    • (2009) Mol Cell , vol.35 , Issue.6 , pp. 769-781
    • Johnson, A.1    Li, G.2    Sikorski, T.W.3    Buratowski, S.4    Woodcock, C.L.5    Moazed, D.6
  • 9
    • 0027183088 scopus 로고
    • The inactive X chromosome in female mammals is distinguished by a lack of histone H4 acetylation, a cytogenetic marker for gene expression
    • DOI 10.1016/0092-8674(93)90419-Q
    • The inactive X chromosome in female mammals is distinguished by a lack of histone H4 acetylation, a cytogenetic marker for gene expression. Jeppesen P, Turner BM, Cell 1993 74 2 281 289 10.1016/0092-8674(93)90419-Q 8343956 (Pubitemid 23221704)
    • (1993) Cell , vol.74 , Issue.2 , pp. 281-289
    • Jeppesen, P.1    Turner, B.M.2
  • 10
    • 77952240405 scopus 로고    scopus 로고
    • The MSL complex: X chromosome and beyond
    • 10.1016/j.gde.2010.01.007 20167472
    • The MSL complex: X chromosome and beyond. Laverty C, Lucci J, Akhtar A, Curr Opin Genet Dev 2010 20 2 171 178 10.1016/j.gde.2010.01.007 20167472
    • (2010) Curr Opin Genet Dev , vol.20 , Issue.2 , pp. 171-178
    • Laverty, C.1    Lucci, J.2    Akhtar, A.3
  • 11
    • 27144546434 scopus 로고    scopus 로고
    • A human protein complex homologous to the Drosophila MSL complex is responsible for the majority of histone H4 acetylation at lysine 16
    • DOI 10.1128/MCB.25.21.9175-9188.2005
    • A human protein complex homologous to the Drosophila MSL complex is responsible for the majority of histone H4 acetylation at lysine 16. Smith ER, Cayrou C, Huang R, Lane WS, Cote J, Lucchesi JC, Mol Cell Biol 2005 25 21 9175 9188 10.1128/MCB.25.21.9175-9188.2005 16227571 (Pubitemid 41507821)
    • (2005) Molecular and Cellular Biology , vol.25 , Issue.21 , pp. 9175-9188
    • Smith, E.R.1    Cayrou, C.2    Huang, R.3    Lane, W.S.4    Cote, J.5    Lucchesi, J.C.6
  • 12
    • 22544480772 scopus 로고    scopus 로고
    • HMOF histone acetyltransferase is required for histone H4 lysine 16 acetylation in mammalian cells
    • DOI 10.1128/MCB.25.15.6798-6810.2005
    • hMOF histone acetyltransferase is required for histone H4 lysine 16 acetylation in mammalian cells. Taipale M, Rea S, Richter K, Vilar A, Lichter P, Imhof A, Akhtar A, Mol Cell Biol 2005 25 15 6798 6810 10.1128/MCB.25.15.6798- 6810.2005 16024812 (Pubitemid 41023250)
    • (2005) Molecular and Cellular Biology , vol.25 , Issue.15 , pp. 6798-6810
    • Taipale, M.1    Rea, S.2    Richter, K.3    Vilar, A.4    Lichter, P.5    Imhof, A.6    Akhtar, A.7
  • 14
    • 78649533191 scopus 로고    scopus 로고
    • MOF and H4 K16 acetylation play important roles in DNA damage repair by modulating recruitment of DNA damage repair protein Mdc1
    • 10.1128/MCB.00350-10 20837706
    • MOF and H4 K16 acetylation play important roles in DNA damage repair by modulating recruitment of DNA damage repair protein Mdc1. Li X, Corsa CA, Pan PW, Wu L, Ferguson D, Yu X, Min J, Dou Y, Mol Cell Biol 2010 30 22 5335 5347 10.1128/MCB.00350-10 20837706
    • (2010) Mol Cell Biol , vol.30 , Issue.22 , pp. 5335-5347
    • Li, X.1    Corsa, C.A.2    Pan, P.W.3    Wu, L.4    Ferguson, D.5    Yu, X.6    Min, J.7    Dou, Y.8
  • 17
    • 4944245398 scopus 로고    scopus 로고
    • Human SirT1 interacts with histone H1 and promotes formation of facultative heterochromatin
    • DOI 10.1016/j.molcel.2004.08.031, PII S1097276504005180
    • Human SirT1 interacts with histone H1 and promotes formation of facultative heterochromatin. Vaquero A, Scher M, Lee D, Erdjument-Bromage H, Tempst P, Reinberg D, Mol Cell 2004 16 1 93 105 10.1016/j.molcel.2004.08.031 15469825 (Pubitemid 39330155)
    • (2004) Molecular Cell , vol.16 , Issue.1 , pp. 93-105
    • Vaquero, A.1    Scher, M.2    Lee, D.3    Erdjument-Bromage, H.4    Tempst, P.5    Reinberg, D.6
  • 18
    • 77956341931 scopus 로고    scopus 로고
    • Human HDAC1 and HDAC2 function in the DNA-damage response to promote DNA nonhomologous end-joining
    • 10.1038/nsmb.1899 20802485
    • Human HDAC1 and HDAC2 function in the DNA-damage response to promote DNA nonhomologous end-joining. Miller KM, Tjeertes JV, Coates J, Legube G, Polo SE, Britton S, Jackson SP, Nat Struct Mol Biol 2010 17 9 1144 1151 10.1038/nsmb.1899 20802485
    • (2010) Nat Struct Mol Biol , vol.17 , Issue.9 , pp. 1144-1151
    • Miller, K.M.1    Tjeertes, J.V.2    Coates, J.3    Legube, G.4    Polo, S.E.5    Britton, S.6    Jackson, S.P.7
  • 19
    • 39149122568 scopus 로고    scopus 로고
    • Interphase nucleo-cytoplasmic shuttling and localization of SIRT2 during mitosis
    • DOI 10.1371/journal.pone.0000784
    • Interphase nucleo-cytoplasmic shuttling and localization of SIRT2 during mitosis. North BJ, Verdin E, PLoS One 2007 2 8 784 10.1371/journal.pone.0000784 17726514 (Pubitemid 351386023)
    • (2007) PLoS ONE , vol.2 , Issue.8
    • North, B.J.1    Verdin, E.2
  • 20
    • 34147182401 scopus 로고    scopus 로고
    • Remodeling of chromatin structure in senescent cells and its potential impact on tumor suppression and aging
    • DOI 10.1016/j.gene.2007.04.020, PII S0378111907001904
    • Remodeling of chromatin structure in senescent cells and its potential impact on tumor suppression and aging. Adams PD, Gene 2007 397 1-2 84 93 17544228 (Pubitemid 46992697)
    • (2007) Gene , vol.397 , Issue.1-2 , pp. 84-93
    • Adams, P.D.1
  • 21
    • 78349257844 scopus 로고    scopus 로고
    • The essence of senescence
    • 10.1101/gad.1971610 21078816
    • The essence of senescence. Kuilman T, Michaloglou C, Mooi WJ, Peeper DS, Genes Dev 2010 24 22 2463 2479 10.1101/gad.1971610 21078816
    • (2010) Genes Dev , vol.24 , Issue.22 , pp. 2463-2479
    • Kuilman, T.1    Michaloglou, C.2    Mooi, W.J.3    Peeper, D.S.4
  • 22
    • 79951912532 scopus 로고    scopus 로고
    • Four faces of cellular senescence
    • 10.1083/jcb.201009094 21321098
    • Four faces of cellular senescence. Rodier F, Campisi J, J Cell Biol 2011 192 4 547 556 10.1083/jcb.201009094 21321098
    • (2011) J Cell Biol , vol.192 , Issue.4 , pp. 547-556
    • Rodier, F.1    Campisi, J.2
  • 23
    • 0037667702 scopus 로고    scopus 로고
    • Rb-mediated heterochromatin formation and silencing of E2F target genes during cellular senescence
    • DOI 10.1016/S0092-8674(03)00401-X
    • Rb-mediated heterochromatin formation and silencing of E2F target genes during cellular senescence. Narita M, Nunez S, Heard E, Lin AW, Hearn SA, Spector DL, Hannon GJ, Lowe SW, Cell 2003 113 6 703 716 10.1016/S0092-8674(03) 00401-X 12809602 (Pubitemid 36724935)
    • (2003) Cell , vol.113 , Issue.6 , pp. 703-716
    • Narita, M.1    Nunez, S.2    Heard, E.3    Narita, M.4    Lin, A.W.5    Hearn, S.A.6    Spector, D.L.7    Hannon, G.J.8    Lowe, S.W.9
  • 24
    • 33746752125 scopus 로고    scopus 로고
    • A Novel Role for High-Mobility Group A Proteins in Cellular Senescence and Heterochromatin Formation
    • DOI 10.1016/j.cell.2006.05.052, PII S0092867406009135
    • A novel role for high-mobility group a proteins in cellular senescence and heterochromatin formation. Narita M, Krizhanovsky V, Nunez S, Chicas A, Hearn SA, Myers MP, Lowe SW, Cell 2006 126 3 503 514 10.1016/j.cell.2006.05.052 16901784 (Pubitemid 44163608)
    • (2006) Cell , vol.126 , Issue.3 , pp. 503-514
    • Narita, M.1    Narita, M.2    Krizhanovsky, V.3    Nunez, S.4    Chicas, A.5    Hearn, S.A.6    Myers, M.P.7    Lowe, S.W.8
  • 25
    • 33845687060 scopus 로고    scopus 로고
    • Loss of linker histone H1 in cellular senescence
    • DOI 10.1083/jcb.200604005
    • Loss of linker histone H1 in cellular senescence. Funayama R, Saito M, Tanobe H, Ishikawa F, J Cell Biol 2006 175 6 869 880 10.1083/jcb.200604005 17158953 (Pubitemid 44969193)
    • (2006) Journal of Cell Biology , vol.175 , Issue.6 , pp. 869-880
    • Funayama, R.1    Saito, M.2    Tanobe, H.3    Ishikawa, F.4
  • 28
    • 77957367167 scopus 로고    scopus 로고
    • Ultra-high performance liquid chromatography-mass spectrometry for the fast profiling of histone post-translational modifications
    • 10.1021/pr100497a 20707390
    • Ultra-high performance liquid chromatography-mass spectrometry for the fast profiling of histone post-translational modifications. Contrepois K, Ezan E, Mann C, Fenaille F, J Proteome Res 2010 9 10 5501 5509 10.1021/pr100497a 20707390
    • (2010) J Proteome Res , vol.9 , Issue.10 , pp. 5501-5509
    • Contrepois, K.1    Ezan, E.2    Mann, C.3    Fenaille, F.4
  • 29
    • 84862642872 scopus 로고    scopus 로고
    • Parallel pathways in RAF-induced senescence and conditions for its reversion
    • 10.1038/onc.2011.481 22020327
    • Parallel pathways in RAF-induced senescence and conditions for its reversion. Jeanblanc M, Ragu S, Gey C, Contrepois K, Courbeyrette R, Thuret JY, Mann C, Oncogene 2012 31 25 3072 3085 10.1038/onc.2011.481 22020327
    • (2012) Oncogene , vol.31 , Issue.25 , pp. 3072-3085
    • Jeanblanc, M.1    Ragu, S.2    Gey, C.3    Contrepois, K.4    Courbeyrette, R.5    Thuret, J.Y.6    Mann, C.7
  • 30
    • 3342929538 scopus 로고    scopus 로고
    • DNA damage checkpoint kinase Chk2 triggers replicative senescence
    • DOI 10.1038/sj.emboj.7600259
    • DNA damage checkpoint kinase Chk2 triggers replicative senescence. Gire V, Roux P, Wynford-Thomas D, Brondello JM, Dulic V, EMBO J 2004 23 13 2554 2563 10.1038/sj.emboj.7600259 15192702 (Pubitemid 38988227)
    • (2004) EMBO Journal , vol.23 , Issue.13 , pp. 2554-2563
    • Gire, V.1    Roux, P.2    Wynford-Thomas, D.3    Brondello, J.-M.4    Dulic, V.5
  • 31
    • 0036714189 scopus 로고    scopus 로고
    • Mitotic-specific methylation of histone H4 Lys 20 follows increased PR-Set7 expression and its localization to mitotic chromosomes
    • DOI 10.1101/gad.1014902
    • Mitotic-specific methylation of histone H4 Lys 20 follows increased PR-Set7 expression and its localization to mitotic chromosomes. Rice JC, Nishioka K, Sarma K, Steward R, Reinberg D, Allis CD, Genes Dev 2002 16 17 2225 2230 10.1101/gad.1014902 12208845 (Pubitemid 35013085)
    • (2002) Genes and Development , vol.16 , Issue.17 , pp. 2225-2230
    • Rice, J.C.1    Nishioka, K.2    Sarma, K.3    Steward, R.4    Reinberg, D.5    David Allis, C.6
  • 32
    • 37549014575 scopus 로고    scopus 로고
    • Certain and progressive methylation of histone H4 at lysine 20 during the cell cycle
    • 10.1128/MCB.01517-07 17967882
    • Certain and progressive methylation of histone H4 at lysine 20 during the cell cycle. Pesavento JJ, Yang H, Kelleher NL, Mizzen CA, Mol Cell Biol 2008 28 1 468 486 10.1128/MCB.01517-07 17967882
    • (2008) Mol Cell Biol , vol.28 , Issue.1 , pp. 468-486
    • Pesavento, J.J.1    Yang, H.2    Kelleher, N.L.3    Mizzen, C.A.4
  • 33
    • 47249157351 scopus 로고    scopus 로고
    • Combinatorial modification of human histone H4 quantitated by two-dimensional liquid chromatography coupled with top down mass spectrometry
    • 10.1074/jbc.M709796200 18381279
    • Combinatorial modification of human histone H4 quantitated by two-dimensional liquid chromatography coupled with top down mass spectrometry. Pesavento JJ, Bullock CR, LeDuc RD, Mizzen CA, Kelleher NL, J Biol Chem 2008 283 22 14927 14937 10.1074/jbc.M709796200 18381279
    • (2008) J Biol Chem , vol.283 , Issue.22 , pp. 14927-14937
    • Pesavento, J.J.1    Bullock, C.R.2    Leduc, R.D.3    Mizzen, C.A.4    Kelleher, N.L.5
  • 34
    • 79952017487 scopus 로고    scopus 로고
    • Quantitative proteomics reveals direct and indirect alterations in the histone code following methyltransferase knockdown
    • 10.1039/c003307c 20577673
    • Quantitative proteomics reveals direct and indirect alterations in the histone code following methyltransferase knockdown. Plazas-Mayorca MD, Bloom JS, Zeissler U, Leroy G, Young NL, DiMaggio PA, Krugylak L, Schneider R, Garcia BA, Mol Biosyst 2010 6 9 1719 1729 10.1039/c003307c 20577673
    • (2010) Mol Biosyst , vol.6 , Issue.9 , pp. 1719-1729
    • Plazas-Mayorca, M.D.1    Bloom, J.S.2    Zeissler, U.3    Leroy, G.4    Young, N.L.5    Dimaggio, P.A.6    Krugylak, L.7    Schneider, R.8    Garcia, B.A.9
  • 36
    • 78649698079 scopus 로고    scopus 로고
    • Global turnover of histone post-translational modifications and variants in human cells
    • 10.1186/1756-8935-3-22 21134274
    • Global turnover of histone post-translational modifications and variants in human cells. Zee BM, Levin RS, Dimaggio PA, Garcia BA, Epigenetics Chromatin 2010 3 1 22 10.1186/1756-8935-3-22 21134274
    • (2010) Epigenetics Chromatin , vol.3 , Issue.1 , pp. 22
    • Zee, B.M.1    Levin, R.S.2    Dimaggio, P.A.3    Garcia, B.A.4
  • 37
    • 30544445468 scopus 로고    scopus 로고
    • Sirt1 inhibitor, Sirtinol, induces senescence-like growth arrest with attenuated Ras-MAPK signaling in human cancer cells
    • DOI 10.1038/sj.onc.1209049, PII 1209049
    • Sirt1 inhibitor, Sirtinol, induces senescence-like growth arrest with attenuated Ras-MAPK signaling in human cancer cells. Ota H, Tokunaga E, Chang K, Hikasa M, Iijima K, Eto M, Kozaki K, Akishita M, Ouchi Y, Kaneki M, Oncogene 2006 25 2 176 185 16170353 (Pubitemid 43083679)
    • (2006) Oncogene , vol.25 , Issue.2 , pp. 176-185
    • Ota, H.1    Tokunaga, E.2    Chang, K.3    Hikasa, M.4    Iijima, K.5    Eto, M.6    Kozaki, K.7    Akishita, M.8    Ouchi, Y.9    Kaneki, M.10
  • 39
    • 22144434077 scopus 로고    scopus 로고
    • The effects of histone deacetylase inhibitors on heterochromatin: Implications for anticancer therapy?
    • DOI 10.1038/sj.embor.7400441
    • The effects of histone deacetylase inhibitors on heterochromatin: implications for anticancer therapy? Taddei A, Roche D, Bickmore WA, Almouzni G, EMBO Rep 2005 6 6 520 524 10.1038/sj.embor.7400441 15940285 (Pubitemid 40973959)
    • (2005) EMBO Reports , vol.6 , Issue.6 , pp. 520-524
    • Taddei, A.1    Roche, D.2    Bickmore, W.A.3    Almouzni, G.4
  • 40
    • 1842861744 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors induce a senescence-like state in human cells by a p16-dependent mechanism that is independent of a mitotic clock
    • DOI 10.1016/j.yexcr.2004.01.017, PII S001448270400031X
    • Histone deacetylase inhibitors induce a senescence-like state in human cells by a p16-dependent mechanism that is independent of a mitotic clock. Munro J, Barr NI, Ireland H, Morrison V, Parkinson EK, Exp Cell Res 2004 295 2 525 538 10.1016/j.yexcr.2004.01.017 15093749 (Pubitemid 38490504)
    • (2004) Experimental Cell Research , vol.295 , Issue.2 , pp. 525-538
    • Munro, J.1    Barr, N.I.2    Ireland, H.3    Morrison, V.4    Parkinson, E.K.5
  • 42
    • 79851493300 scopus 로고    scopus 로고
    • Senescence-associated heterochromatin foci are dispensable for cellular senescence, occur in a cell type- and insult-dependent manner and follow expression of p16(ink4a)
    • 10.4161/cc.10.3.14707 21248468
    • Senescence-associated heterochromatin foci are dispensable for cellular senescence, occur in a cell type- and insult-dependent manner and follow expression of p16(ink4a). Kosar M, Bartkova J, Hubackova S, Hodny Z, Lukas J, Bartek J, Cell Cycle 2011 10 3 457 468 10.4161/cc.10.3.14707 21248468
    • (2011) Cell Cycle , vol.10 , Issue.3 , pp. 457-468
    • Kosar, M.1    Bartkova, J.2    Hubackova, S.3    Hodny, Z.4    Lukas, J.5    Bartek, J.6
  • 43
    • 0041966056 scopus 로고    scopus 로고
    • Reversal of human cellular senescence: Roles of the p53 and p16 pathways
    • DOI 10.1093/emboj/cdg417
    • Reversal of human cellular senescence: roles of the p53 and p16 pathways. Beausejour CM, Krtolica A, Galimi F, Narita M, Lowe SW, Yaswen P, Campisi J, EMBO J 2003 22 16 4212 4222 10.1093/emboj/cdg417 12912919 (Pubitemid 37021749)
    • (2003) EMBO Journal , vol.22 , Issue.16 , pp. 4212-4222
    • Beausejour, C.M.1    Krtolica, A.2    Galimi, F.3    Narita, M.4    Lowe, S.W.5    Yaswen, P.6    Campisi, J.7
  • 45
    • 0036790977 scopus 로고    scopus 로고
    • Diversity, topographic differentiation, and positional memory in human fibroblasts
    • 10.1073/pnas.162488599 12297622
    • Diversity, topographic differentiation, and positional memory in human fibroblasts. Chang HY, Chi JT, Dudoit S, Bondre C, van de Rijn M, Botstein D, Brown PO, Proc Natl Acad Sci U S A 2002 99 20 12877 12882 10.1073/pnas.162488599 12297622
    • (2002) Proc Natl Acad Sci U S A , vol.99 , Issue.20 , pp. 12877-12882
    • Chang, H.Y.1    Chi, J.T.2    Dudoit, S.3    Bondre, C.4    Van De Rijn, M.5    Botstein, D.6    Brown, P.O.7
  • 47
    • 79961083402 scopus 로고    scopus 로고
    • Histone H4 lysine 16 hypoacetylation is associated with defective DNA repair and premature senescence in Zmpste24-deficient mice
    • 10.1073/pnas.1102789108 21746928
    • Histone H4 lysine 16 hypoacetylation is associated with defective DNA repair and premature senescence in Zmpste24-deficient mice. Krishnan V, Chow MZ, Wang Z, Zhang L, Liu B, Liu X, Zhou Z, Proc Natl Acad Sci USA 2011 108 30 12325 12330 10.1073/pnas.1102789108 21746928
    • (2011) Proc Natl Acad Sci USA , vol.108 , Issue.30 , pp. 12325-12330
    • Krishnan, V.1    Chow, M.Z.2    Wang, Z.3    Zhang, L.4    Liu, B.5    Liu, X.6    Zhou, Z.7
  • 48
    • 0023874975 scopus 로고
    • Differential acetylation of core histones in rat cerebral cortex neurons during development and aging
    • 10.1111/j.1432-1033.1988.tb14099.x 3383848
    • Differential acetylation of core histones in rat cerebral cortex neurons during development and aging. Pina B, Martinez P, Suau P, Eur J Biochem 1988 174 2 311 315 10.1111/j.1432-1033.1988.tb14099.x 3383848
    • (1988) Eur J Biochem , vol.174 , Issue.2 , pp. 311-315
    • Pina, B.1    Martinez, P.2    Suau, P.3
  • 50
    • 0037131426 scopus 로고    scopus 로고
    • Postsynthetic trimethylation of histone H4 at lysine 20 in mammalian tissues is associated with aging
    • DOI 10.1074/jbc.M205166200
    • Postsynthetic trimethylation of histone H4 at lysine 20 in mammalian tissues is associated with aging. Sarg B, Koutzamani E, Helliger W, Rundquist I, Lindner HH, J Biol Chem 2002 277 42 39195 39201 10.1074/jbc.M205166200 12154089 (Pubitemid 35190888)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.42 , pp. 39195-39201
    • Sarg, B.1    Koutzamani, E.2    Helliger, W.3    Rundquist, I.4    Lindner, H.H.5
  • 52
    • 33646745137 scopus 로고    scopus 로고
    • Lamin A-dependent nuclear defects in human aging
    • 10.1126/science.1127168 16645051
    • Lamin A-dependent nuclear defects in human aging. Scaffidi P, Misteli T, Science 2006 312 5776 1059 1063 10.1126/science.1127168 16645051
    • (2006) Science , vol.312 , Issue.5776 , pp. 1059-1063
    • Scaffidi, P.1    Misteli, T.2
  • 53
    • 0346463059 scopus 로고    scopus 로고
    • High Intensity ras Signaling Induces Premature Senescence by Activating p38 Pathway in Primary Human Fibroblasts
    • DOI 10.1074/jbc.M308644200
    • High intensity ras signaling induces premature senescence by activating p38 pathway in primary human fibroblasts. Deng Q, Liao R, Wu BL, Sun P, J Biol Chem 2004 279 2 1050 1059 14593117 (Pubitemid 38082626)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.2 , pp. 1050-1059
    • Deng, Q.1    Liao, R.2    Wu, B.-L.3    Sun, P.4
  • 54
    • 58849158388 scopus 로고    scopus 로고
    • How does SIRT1 affect metabolism, senescence and cancer?
    • 10.1038/nrc2562 19132007
    • How does SIRT1 affect metabolism, senescence and cancer? Brooks CL, Gu W, Nat Rev Cancer 2009 9 2 123 128 10.1038/nrc2562 19132007
    • (2009) Nat Rev Cancer , vol.9 , Issue.2 , pp. 123-128
    • Brooks, C.L.1    Gu, W.2
  • 56
    • 77954886825 scopus 로고    scopus 로고
    • The ATAC acetyl transferase complex controls mitotic progression by targeting non-histone substrates
    • 10.1038/emboj.2010.125 20562830
    • The ATAC acetyl transferase complex controls mitotic progression by targeting non-histone substrates. Orpinell M, Fournier M, Riss A, Nagy Z, Krebs AR, Frontini M, Tora L, EMBO J 2010 29 14 2381 2394 10.1038/emboj.2010.125 20562830
    • (2010) EMBO J , vol.29 , Issue.14 , pp. 2381-2394
    • Orpinell, M.1    Fournier, M.2    Riss, A.3    Nagy, Z.4    Krebs, A.R.5    Frontini, M.6    Tora, L.7
  • 58
    • 77950486542 scopus 로고    scopus 로고
    • Dissecting the unique role of the retinoblastoma tumor suppressor during cellular senescence
    • 10.1016/j.ccr.2010.01.023 20385362
    • Dissecting the unique role of the retinoblastoma tumor suppressor during cellular senescence. Chicas A, Wang X, Zhang C, McCurrach M, Zhao Z, Mert O, Dickins RA, Narita M, Zhang M, Lowe SW, Cancer Cell 2010 17 4 376 387 10.1016/j.ccr.2010.01.023 20385362
    • (2010) Cancer Cell , vol.17 , Issue.4 , pp. 376-387
    • Chicas, A.1    Wang, X.2    Zhang, C.3    McCurrach, M.4    Zhao, Z.5    Mert, O.6    Dickins, R.A.7    Narita, M.8    Zhang, M.9    Lowe, S.W.10
  • 60
    • 79961207835 scopus 로고    scopus 로고
    • DNA double-strand breaks in heterochromatin elicit fast repair protein recruitment, histone H2AX phosphorylation and relocation to euchromatin
    • 10.1093/nar/gkr230 21511815
    • DNA double-strand breaks in heterochromatin elicit fast repair protein recruitment, histone H2AX phosphorylation and relocation to euchromatin. Jakob B, Splinter J, Conrad S, Voss KO, Zink D, Durante M, Lobrich M, Taucher-Scholz G, Nucleic Acids Res 2011 39 15 6489 6499 10.1093/nar/gkr230 21511815
    • (2011) Nucleic Acids Res , vol.39 , Issue.15 , pp. 6489-6499
    • Jakob, B.1    Splinter, J.2    Conrad, S.3    Voss, K.O.4    Zink, D.5    Durante, M.6    Lobrich, M.7    Taucher-Scholz, G.8
  • 61
    • 79952314830 scopus 로고    scopus 로고
    • Double-strand breaks in heterochromatin move outside of a dynamic HP1a domain to complete recombinational repair
    • 10.1016/j.cell.2011.02.012 21353298
    • Double-strand breaks in heterochromatin move outside of a dynamic HP1a domain to complete recombinational repair. Chiolo I, Minoda A, Colmenares SU, Polyzos A, Costes SV, Karpen GH, Cell 2011 144 5 732 744 10.1016/j.cell.2011.02. 012 21353298
    • (2011) Cell , vol.144 , Issue.5 , pp. 732-744
    • Chiolo, I.1    Minoda, A.2    Colmenares, S.U.3    Polyzos, A.4    Costes, S.V.5    Karpen, G.H.6


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