메뉴 건너뛰기




Volumn 19, Issue 11, 2003, Pages 1137-1145

Histone variants: The third way of nucleosome differentiation;Différenciation du nucléosome: Le rôle des variants de l'histone H2A

Author keywords

[No Author keywords available]

Indexed keywords

DNA; HISTONE; HISTONE H2A; HISTONE H2B; HISTONE H3; HISTONE H4;

EID: 0242666070     PISSN: 07670974     EISSN: None     Source Type: Journal    
DOI: 10.1051/medsci/200319111137     Document Type: Review
Times cited : (5)

References (56)
  • 1
    • 0035814925 scopus 로고    scopus 로고
    • Chromatin remodeling enzymes: Who's on first?
    • Fry CJ, Peterson CL. Chromatin remodeling enzymes: who's on first? Curr Biol 2001; 11: R185-97.
    • (2001) Curr Biol , vol.11
    • Fry, C.J.1    Peterson, C.L.2
  • 2
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications
    • Strahl BD, Allis CD. The language of covalent histone modifications. Nature 2000; 403: 41-5.
    • (2000) Nature , vol.403 , pp. 41-45
    • Strahl, B.D.1    Allis, C.D.2
  • 3
    • 0017365534 scopus 로고
    • Non-allelic variants of histones 2a, 2b and 3 in mammals
    • Franklin SG, Zweidler A. Non-allelic variants of histones 2a, 2b and 3 in mammals. Nature 1977; 266: 273-5.
    • (1977) Nature , vol.266 , pp. 273-275
    • Franklin, S.G.1    Zweidler, A.2
  • 4
    • 0019319471 scopus 로고
    • Histone 2A, a heteromorphous family of eight protein species
    • West MH, Bonner WM. Histone 2A, a heteromorphous family of eight protein species. Biochemistry 1980; 19: 3238-45.
    • (1980) Biochemistry , vol.19 , pp. 3238-3245
    • West, M.H.1    Bonner, W.M.2
  • 5
    • 0035931749 scopus 로고    scopus 로고
    • A novel chromatin protein, distantly related to histone H2A, is largely excluded from the inactive X chromosome
    • Chadwick BP, Willard HF. A novel chromatin protein, distantly related to histone H2A, is largely excluded from the inactive X chromosome. J Cell Biol 2001; 152: 375-84.
    • (2001) J Cell Biol , vol.152 , pp. 375-384
    • Chadwick, B.P.1    Willard, H.F.2
  • 6
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 Å resolution
    • Luger K, Mader AW, Richmond RK, Sagent DF, Richmond TJ. Crystal structure of the nucleosome core particle at 2.8 Å resolution. Nature 1997; 389: 251-60.
    • (1997) Nature , vol.389 , pp. 251-260
    • Luger, K.1    Mader, A.W.2    Richmond, R.K.3    Sagent, D.F.4    Richmond, T.J.5
  • 7
    • 0024395794 scopus 로고
    • H2A.X. A histone isoprotein with a conserved C-terminal sequence, is encoded by a novel mRNA with both DNA replication type and polyA 3′ processing signals
    • Mannironi C, Bonner WM, Hatch CL. H2A.X. a histone isoprotein with a conserved C-terminal sequence, is encoded by a novel mRNA with both DNA replication type and polyA 3′ processing signals. Nucleic Acids Res 1989; 17: 9113-26.
    • (1989) Nucleic Acids Res , vol.17 , pp. 9113-9126
    • Mannironi, C.1    Bonner, W.M.2    Hatch, C.L.3
  • 8
    • 0019876876 scopus 로고
    • Quantitative determination of histone modification. H2A acetylation and phosphorylation
    • Pantazis P, Bonner WM. Quantitative determination of histone modification. H2A acetylation and phosphorylation. J Biol Chem 1981; 256: 4669-75.
    • (1981) J Biol Chem , vol.256 , pp. 4669-4675
    • Pantazis, P.1    Bonner, W.M.2
  • 9
    • 0024334484 scopus 로고
    • Identification of ADP-ribosylated histones by the combined use of high-performance liquid chromatography and electrophoresis
    • Lindner H, Wesierska-Gadek J, Helliger W, Puschendorf B, Sauermann G. Identification of ADP-ribosylated histones by the combined use of high-performance liquid chromatography and electrophoresis. J Chromatogr 1989; 472: 243-9.
    • (1989) J Chromatogr , vol.472 , pp. 243-249
    • Lindner, H.1    Wesierska-Gadek, J.2    Helliger, W.3    Puschendorf, B.4    Sauermann, G.5
  • 10
    • 0032489520 scopus 로고    scopus 로고
    • DNA double-stranded breaks induce histone H2AX phosphorylation on serine 139
    • Rogakau EP, Pilch DR, Orr AH, Ivanova VS, Bonner WM. DNA double-stranded breaks induce histone H2AX phosphorylation on serine 139. J Biol Chem 1998; 273: 5858-68.
    • (1998) J Biol Chem , vol.273 , pp. 5858-5868
    • Rogakau, E.P.1    Pilch, D.R.2    Orr, A.H.3    Ivanova, V.S.4    Bonner, W.M.5
  • 11
    • 0035834693 scopus 로고    scopus 로고
    • ATM phosphorylates histone H2AX in response to DNA double-strand breaks
    • Burma S, Chen BP, Murphy M, Kurimasa A, Chen DJ. ATM phosphorylates histone H2AX in response to DNA double-strand breaks. J Biol Chem 2001; 276: 42462-7.
    • (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
  • 12
    • 0032861343 scopus 로고    scopus 로고
    • Megabase chromatin domains involved in DNA double-strand breaks in vivo
    • Rogakou EP, Boon C, Redon C, Bonner WM. Megabase chromatin domains involved in DNA double-strand breaks in vivo. J Cell Biol 1999; 146: 905-16.
    • (1999) J Cell Biol , vol.146 , pp. 905-916
    • Rogakou, E.P.1    Boon, C.2    Redon, C.3    Bonner, W.M.4
  • 13
    • 0034739853 scopus 로고    scopus 로고
    • p53 binding protein 1 (53BP1) is an early participant in the cellular response to DNA double-strand breaks
    • Schultz LB, Chehab NH, Malikzay A, Halazonetis TD. p53 binding protein 1 (53BP1) is an early participant in the cellular response to DNA double-strand breaks. J Cell Biol 2000; 151: 1381-90.
    • (2000) J Cell Biol , vol.151 , pp. 1381-1390
    • Schultz, L.B.1    Chehab, N.H.2    Malikzay, A.3    Halazonetis, T.D.4
  • 14
    • 0343280013 scopus 로고    scopus 로고
    • A critical role for histone H2AX in recruitment of repair factors to nuclear foci after DNA damage
    • Paull TT, Rogakou EP, Yamazaki V, Kirchgessner CU, Gellert M, Bonner WM. A critical role for histone H2AX in recruitment of repair factors to nuclear foci after DNA damage. Curr Biol 2000; 10: 886-95.
    • (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
  • 15
    • 0035097808 scopus 로고    scopus 로고
    • Recombinational DNA double-strand breaks in mice precede synopsis
    • Mahadevaiah SK, Turner JM, Baudat F, et al. Recombinational DNA double-strand breaks in mice precede synopsis. Nat Genet 2001; 27: 271-6.
    • (2001) Nat Genet , vol.27 , pp. 271-276
    • Mahadevaiah, S.K.1    Turner, J.M.2    Baudat, F.3
  • 16
    • 0034737439 scopus 로고    scopus 로고
    • Initiation of DNA fragmentation during opoptosis induces phosphorylation of H2AX histone at serine 139
    • Rogakou EP, Nieves-Neira W, Boor C, Pommier Y, Bonner WM. Initiation of DNA fragmentation during opoptosis induces phosphorylation of H2AX histone at serine 139. J Biol Chem 2000; 275: 9390-5.
    • (2000) J Biol Chem , vol.275 , pp. 9390-9395
    • Rogakou, E.P.1    Nieves-Neira, W.2    Boor, C.3    Pommier, Y.4    Bonner, W.M.5
  • 17
    • 0034623860 scopus 로고    scopus 로고
    • Response to RAG-mediated VDJ cleavage by NBS1 and gamma-H2AX
    • Chen HT, Bhandoola A, Difilippantonio MJ, et al. Response to RAG-mediated VDJ cleavage by NBS1 and gamma-H2AX. Science 2000; 290: 1962-5.
    • (2000) Science , vol.290 , pp. 1962-1965
    • Chen, H.T.1    Bhandoola, A.2    Difilippantonio, M.J.3
  • 18
    • 0035818990 scopus 로고    scopus 로고
    • AID is required to initiate Nbs1/gamma-H2AX focus formation and mutations at sites of class switching
    • Petersen S, Casellas R, Reina-San-Martin B, et al. AID is required to initiate Nbs1/gamma-H2AX focus formation and mutations at sites of class switching. Nature 2001; 414: 660-5.
    • (2001) Nature , vol.414 , pp. 660-665
    • Petersen, S.1    Casellas, R.2    Reina-San-Martin, B.3
  • 19
    • 0035930537 scopus 로고    scopus 로고
    • Histone H2AX is phosphorylated in an ATR-dependent manner in response to replicational stress
    • Ward IM, Chen J. Histone H2AX is phosphorylated in an ATR-dependent manner in response to replicational stress. J Biol Chem 2001; 276: 47759-62.
    • (2001) J Biol Chem , vol.276 , pp. 47759-47762
    • Ward, I.M.1    Chen, J.2
  • 20
    • 0020632051 scopus 로고
    • Minor histone 2A variants and ubiquinated forms in the native H2A:H2B dimer
    • Hatch CL, Bonner WM, Moudrianakis EN. Minor histone 2A variants and ubiquinated forms in the native H2A:H2B dimer. Science 1983; 221: 468-70.
    • (1983) Science , vol.221 , pp. 468-470
    • Hatch, C.L.1    Bonner, W.M.2    Moudrianakis, E.N.3
  • 21
    • 0026737922 scopus 로고
    • MacroH2A, a core histone containing a large nonhistone region
    • Pehrson JR, Fried VA. MacroH2A, a core histone containing a large nonhistone region. Science 1992; 257: 1398-400.
    • (1992) Science , vol.257 , pp. 1398-1400
    • Pehrson, J.R.1    Fried, V.A.2
  • 22
    • 0025815045 scopus 로고
    • DNA-dependent phosphorylation of histone H2A.X during nucleosome assembly in Xenopus laevis oocytes: Involvement of protein phosphorylation in nucleosome spacing
    • Kleinschmidt JA, Steinbeisser H. DNA-dependent phosphorylation of histone H2A.X during nucleosome assembly in Xenopus laevis oocytes: involvement of protein phosphorylation in nucleosome spacing. EMBO J 1991; 10: 3043-50.
    • (1991) EMBO J , vol.10 , pp. 3043-3050
    • Kleinschmidt, J.A.1    Steinbeisser, H.2
  • 23
    • 0028955149 scopus 로고
    • ATP-dependent reorganization of human sperm nuclear chromatin
    • Banerjee S, Smallwood A, Hulten M. ATP-dependent reorganization of human sperm nuclear chromatin. J Cell Sci 1995; 108: 755-65.
    • (1995) J Cell Sci , vol.108 , pp. 755-765
    • Banerjee, S.1    Smallwood, A.2    Hulten, M.3
  • 24
    • 0034700511 scopus 로고    scopus 로고
    • A role for Saccharomyces cerevisiae histone H2A in DNA repair
    • Downs JA, Lowndes NF, Jackson SP. A role for Saccharomyces cerevisiae histone H2A in DNA repair. Nature 2000; 408: 1001-4.
    • (2000) Nature , vol.408 , pp. 1001-1004
    • Downs, J.A.1    Lowndes, N.F.2    Jackson, S.P.3
  • 25
    • 0028139274 scopus 로고
    • Analysis of a histone H2A variant from fission yeast: Evidence for a role in chromosome stability
    • Carr AM, Dorrington SM, Hindley J, Phear GA, Aves SJ, Nurse P. Analysis of a histone H2A variant from fission yeast: evidence for a role in chromosome stability. Mol Gen Genet 1994; 245: 628-35.
    • (1994) Mol Gen Genet , vol.245 , pp. 628-635
    • Carr, A.M.1    Dorrington, S.M.2    Hindley, J.3    Phear, G.A.4    Aves, S.J.5    Nurse, P.6
  • 26
    • 0031742022 scopus 로고    scopus 로고
    • Comprehensive identification of cell cycle-regulated genes of the yeast Saccharomyces cerevisiae by microarray hybridization
    • Spellman PT, Sherlock G, Zhong MQ, et al. Comprehensive identification of cell cycle-regulated genes of the yeast Saccharomyces cerevisiae by microarray hybridization. Mol Biol Cell 1998; 9: 3273-97.
    • (1998) Mol Biol Cell , vol.9 , pp. 3273-3297
    • Spellman, P.T.1    Sherlock, G.2    Zhong, M.Q.3
  • 27
    • 0024283907 scopus 로고
    • Sequence and properties of the message encoding Tetrahymena hv1, a highly evolutionarily conserved histone H2A variant that is associated with active genes
    • White EM, Shapiro DL, Allis CD, Gorovsky MA. Sequence and properties of the message encoding Tetrahymena hv1, a highly evolutionarily conserved histone H2A variant that is associated with active genes. Nucleic Acids Res 1988; 16: 179-98.
    • (1988) Nucleic Acids Res , vol.16 , pp. 179-198
    • White, E.M.1    Shapiro, D.L.2    Allis, C.D.3    Gorovsky, M.A.4
  • 28
    • 0025125173 scopus 로고
    • The human histone H2A.Z gene. Sequence and regulation
    • Hatch CL, Bonner WM. The human histone H2A.Z gene. Sequence and regulation. J Biol Chem 1990; 265: 15211-8.
    • (1990) J Biol Chem , vol.265 , pp. 15211-15218
    • Hatch, C.L.1    Bonner, W.M.2
  • 29
    • 0034307468 scopus 로고    scopus 로고
    • Histone H2A.Z has a conserved function that is distinct from that of the major H2A sequence variants
    • Jackson JD, Gorovsky MA. Histone H2A.Z has a conserved function that is distinct from that of the major H2A sequence variants. Nucleic Acids Res 2000; 28: 3811-6.
    • (2000) Nucleic Acids Res , vol.28 , pp. 3811-3816
    • Jackson, J.D.1    Gorovsky, M.A.2
  • 30
    • 0034721645 scopus 로고    scopus 로고
    • Histone H2A.Z regulates transcription and is partially redundant with nucleosome remodeling complexes
    • Santisteban MS, Kalashnikova T, Smith MM. Histone H2A.Z regulates transcription and is partially redundant with nucleosome remodeling complexes. Cell 2000; 103: 411-22.
    • (2000) Cell , vol.103 , pp. 411-422
    • Santisteban, M.S.1    Kalashnikova, T.2    Smith, M.M.3
  • 31
    • 0029982345 scopus 로고    scopus 로고
    • Either of the major H2A genes but not an evolutionarily conserved H2A.F/ Z variant of Tetrahymena thermophila can function as the sole H2A gene in the yeast Saccharomyces cerevisiae
    • Liu X, Bowen J, Gorovsky MA. Either of the major H2A genes but not an evolutionarily conserved H2A.F/Z variant of Tetrahymena thermophila can function as the sole H2A gene in the yeast Saccharomyces cerevisiae. Mol Cell Biol 1996; 16: 2878-87.
    • (1996) Mol Cell Biol , vol.16 , pp. 2878-2887
    • Liu, X.1    Bowen, J.2    Gorovsky, M.A.3
  • 32
    • 0033578004 scopus 로고    scopus 로고
    • Regions of variant histone His2AVD required for Drosophila development
    • Clarkson MJ, Wells JR, Gibson F, Saint R, Tremethick DJ. Regions of variant histone His2AVD required for Drosophila development. Nature 1999; 399: 694-7.
    • (1999) Nature , vol.399 , pp. 694-697
    • Clarkson, M.J.1    Wells, J.R.2    Gibson, F.3    Saint, R.4    Tremethick, D.J.5
  • 33
    • 0035822687 scopus 로고    scopus 로고
    • Histone variant H2A.Z is required for early mammalian development
    • Faast R, Thonglairoam V, Schulz TC, et al. Histone variant H2A.Z is required for early mammalian development. Curr Biol 2001; 11: 1183-7.
    • (2001) Curr Biol , vol.11 , pp. 1183-1187
    • Faast, R.1    Thonglairoam, V.2    Schulz, T.C.3
  • 34
    • 0033664380 scopus 로고    scopus 로고
    • Crystal structure of a nucleosome core particle containing the variant histone H2A.Z
    • Suto RK, Clarkson MJ, Tremethick DJ, Luger K. Crystal structure of a nucleosome core particle containing the variant histone H2A.Z. Nat Struct Biol 2000; 7: 1121-4.
    • (2000) Nat Struct Biol , vol.7 , pp. 1121-1124
    • Suto, R.K.1    Clarkson, M.J.2    Tremethick, D.J.3    Luger, K.4
  • 35
    • 0035834777 scopus 로고    scopus 로고
    • Characterization of the stability and folding of H2A.Z chromatin particles: Implications for transcriptional activation
    • Abbott DN, Ivanova VS, Wong X, Bonner WM, Ausio J. Characterization of the stability and folding of H2A.Z chromatin particles: implications for transcriptional activation. J Biol Chem 2001; 276: 41945-9.
    • (2001) J Biol Chem , vol.276 , pp. 41945-41949
    • Abbott, D.N.1    Ivanova, V.S.2    Wong, X.3    Bonner, W.M.4    Ausio, J.5
  • 36
    • 0027759372 scopus 로고
    • Temporal and spatial association of histone H2A variant hv1 with transcriptionally competent chromatin during nuclear development in Tetrahymena thermophila
    • Stargell LA, Bowen J, Dadd CA, et al. Temporal and spatial association of histone H2A variant hv1 with transcriptionally competent chromatin during nuclear development in Tetrahymena thermophila. Genes Dev 1993; 7: 2641-51.
    • (1993) Genes Dev , vol.7 , pp. 2641-2651
    • Stargell, L.A.1    Bowen, J.2    Dadd, C.A.3
  • 37
    • 0023032792 scopus 로고
    • hv1 is an evolutionarily conserved H2A variant that is preferentially associated with active genes
    • Allis CO, Richman R, Gorovsky MA, et al. hv1 is an evolutionarily conserved H2A variant that is preferentially associated with active genes. J Biol Chem 1986; 261: 1941-8.
    • (1986) J Biol Chem , vol.261 , pp. 1941-1948
    • Allis, C.O.1    Richman, R.2    Gorovsky, M.A.3
  • 38
    • 0035725036 scopus 로고    scopus 로고
    • H2A.Z is required for global chromatin integrity and for recruitment of RNA polymerase II under specific conditions
    • Adam M, Robert F, Larochelle M, Gaudreou L. H2A.Z is required for global chromatin integrity and for recruitment of RNA polymerase II under specific conditions. Mol Cell Biol 2001; 21: 6270-9.
    • (2001) Mol Cell Biol , vol.21 , pp. 6270-6279
    • Adam, M.1    Robert, F.2    Larochelle, M.3    Gaudreou, L.4
  • 39
  • 40
    • 0033638234 scopus 로고    scopus 로고
    • A histone variant, Htz1p, and a Sir1p-like protein, Esc2p, mediate silencing at HMR
    • Dhillon N, Kamakaka RT. A histone variant, Htz1p, and a Sir1p-like protein, Esc2p, mediate silencing at HMR. Mol Cell 2000; 6: 769-80.
    • (2000) Mol Cell , vol.6 , pp. 769-780
    • Dhillon, N.1    Kamakaka, R.T.2
  • 41
    • 0030975594 scopus 로고    scopus 로고
    • Developmental and tissue expression patterns of histone macroH2A1 subtypes
    • Pehrson JR, Costanzi C, Dharia C. Developmental and tissue expression patterns of histone macroH2A1 subtypes. J Cell Biochem 1997; 65: 107-13.
    • (1997) J Cell Biochem , vol.65 , pp. 107-113
    • Pehrson, J.R.1    Costanzi, C.2    Dharia, C.3
  • 42
    • 0032507949 scopus 로고    scopus 로고
    • Histone macroH2A1 is concentrated in the inactive X chromosome of female mammals
    • Costanzi C, Pehrson JR. Histone macroH2A1 is concentrated in the inactive X chromosome of female mammals. Nature 1998; 393: 599-601.
    • (1998) Nature , vol.393 , pp. 599-601
    • Costanzi, C.1    Pehrson, J.R.2
  • 43
    • 0031467130 scopus 로고    scopus 로고
    • X-chromosome inactivation in mammals
    • Heard E, Clerc P, Avner P. X-chromosome inactivation in mammals. Annu Rev Genet 1997; 31: 571-610.
    • (1997) Annu Rev Genet , vol.31 , pp. 571-610
    • Heard, E.1    Clerc, P.2    Avner, P.3
  • 44
    • 0036532224 scopus 로고    scopus 로고
    • X-chromosome inactivation and the search for chromosome-wide silencers
    • Cohen DE, Lee JT. X-chromosome inactivation and the search for chromosome-wide silencers. Curr Opin Genet Dev 2002; 12: 219-24.
    • (2002) Curr Opin Genet Dev , vol.12 , pp. 219-224
    • Cohen, D.E.1    Lee, J.T.2
  • 45
    • 0033920964 scopus 로고    scopus 로고
    • Tsix et Xist, antisens et sens: Du verlan dans l'inactivation du chromosome X de la souris
    • Clerc P. Tsix et Xist, antisens et sens: du verlan dans l'inactivation du chromosome X de la souris. Med Sci 2000; 16: 818-9.
    • (2000) Med Sci , vol.16 , pp. 818-819
    • Clerc, P.1
  • 46
    • 0242692505 scopus 로고    scopus 로고
    • Encore l'inactivation du chromosome X chez la souris
    • Blanche J. Encore l'inactivation du chromosome X chez la souris. Med Sci 1998; 14: 976.
    • (1998) Med Sci , vol.14 , pp. 976
    • Blanche, J.1
  • 47
    • 0033611106 scopus 로고    scopus 로고
    • Histone macroH2A1.2 relocates to the inactive X chromosome after initiation and propagation of X-inactivation
    • Mermoud JE, Costanzi C, Pehrson JR, Brockdorff N. Histone macroH2A1.2 relocates to the inactive X chromosome after initiation and propagation of X-inactivation. J Cell Biol 1999; 147: 1399-408.
    • (1999) J Cell Biol , vol.147 , pp. 1399-1408
    • Mermoud, J.E.1    Costanzi, C.2    Pehrson, J.R.3    Brockdorff, N.4
  • 48
    • 0034605124 scopus 로고    scopus 로고
    • Dynamic relocalization of histone MacroH2A1 from centrosomes to inactive X chromosomes during X inactivation
    • Rasmussen TP, Mastrangelo MA, Eden A, Pehrson JR, Jaenisch R. Dynamic relocalization of histone MacroH2A1 from centrosomes to inactive X chromosomes during X inactivation. J Cell Biol 2000; 150: 1189-98.
    • (2000) J Cell Biol , vol.150 , pp. 1189-1198
    • Rasmussen, T.P.1    Mastrangelo, M.A.2    Eden, A.3    Pehrson, J.R.4    Jaenisch, R.5
  • 49
    • 0032805149 scopus 로고    scopus 로고
    • Conditional deletion of Xist disrupts histone macroH2A localization but not maintenance of X inactivation
    • Csankovszki G, Panning B, Bates B, Pehrson JR, Jaenisch R. Conditional deletion of Xist disrupts histone macroH2A localization but not maintenance of X inactivation. Nat Genet 1999; 22: 323-4.
    • (1999) Nat Genet , vol.22 , pp. 323-324
    • Csankovszki, G.1    Panning, B.2    Bates, B.3    Pehrson, J.R.4    Jaenisch, R.5
  • 50
    • 0034735914 scopus 로고    scopus 로고
    • Higher concentrations of histone macroH2A in the Barr body are correlated with higher nucleosome density
    • Perche PY, Vourc'h C, Konecny L, et al. Higher concentrations of histone macroH2A in the Barr body are correlated with higher nucleosome density. Curr Biol 2000; 10: 1531-4.
    • (2000) Curr Biol , vol.10 , pp. 1531-1534
    • Perche, P.Y.1    Vourc'h, C.2    Konecny, L.3
  • 51
    • 0032846669 scopus 로고    scopus 로고
    • Histone variants of H2A and H3 families are regulated during in vitro aging in the same manner cis during differentiation
    • Rogakou EP, Sekeri-Pataryas KE. Histone variants of H2A and H3 families are regulated during in vitro aging in the same manner cis during differentiation. Exp Gerontol 1999; 34: 741-54.
    • (1999) Exp Gerontol , vol.34 , pp. 741-754
    • Rogakou, E.P.1    Sekeri-Pataryas, K.E.2
  • 52
    • 0004142945 scopus 로고
    • New York: Academic Press
    • eéd. New York: Academic Press, 1992.
    • (1992) eÉd
    • Wolffe, A.1
  • 53
    • 0037711771 scopus 로고    scopus 로고
    • Histone H2AX phosphorylation is dispensable for the initial recognition of DNA breaks
    • Celeste A, Fernandez-Capetillo O, Kruhlak MJ, et al. Histone H2AX phosphorylation is dispensable for the initial recognition of DNA breaks. Nat Cell Biol 2003; 5: 675-9.
    • (2003) Nat Cell Biol , vol.5 , pp. 675-679
    • Celeste, A.1    Fernandez-Capetillo, O.2    Kruhlak, M.J.3
  • 54
    • 0037012845 scopus 로고    scopus 로고
    • Genomic instability in mice lacking histone H2AX
    • Celeste A, Petersen S, Romanienko PJ, et al. Genomic instability in mice lacking histone H2AX. Science 2002; 296: 922-7.
    • (2002) Science , vol.296 , pp. 922-927
    • Celeste, A.1    Petersen, S.2    Romanienko, P.J.3
  • 55
    • 0037423930 scopus 로고    scopus 로고
    • Conserved histone variant H2A.Z protects euchromatin from the ectopic spread of silent heterochromotin
    • Meneghini MD, Wu M, Madhani HD. Conserved histone variant H2A.Z protects euchromatin from the ectopic spread of silent heterochromotin. Cell 2003; 112: 725-36.
    • (2003) Cell , vol.112 , pp. 725-736
    • Meneghini, M.D.1    Wu, M.2    Madhani, H.D.3
  • 56
    • 0037961635 scopus 로고    scopus 로고
    • The histone variant macroH2A interferes with transcription factor binding and SWI/SNF nucleosome remodeling
    • Angelov D, Molla A, Perche PY, et al. The histone variant macroH2A interferes with transcription factor binding and SWI/SNF nucleosome remodeling. Mol Cell 2003; 11: 1033-41.
    • (2003) Mol Cell , vol.11 , pp. 1033-1041
    • Angelov, D.1    Molla, A.2    Perche, P.Y.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.