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Volumn 9, Issue 1, 2010, Pages

Sometimes one just isn't enough: Do vertebrates contain an H2A.Z hyper-variant?

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; HISTONE H2AZ; HISTONE;

EID: 76749158455     PISSN: None     EISSN: 14754924     Source Type: Journal    
DOI: 10.1186/jbiol214     Document Type: Short Survey
Times cited : (2)

References (13)
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    • New developments in post-translational modifications and functions of histone H2A variants. AA Thambirajah T Ishibashi J Ausio, Biochem Cell Biol 2009 87 7-17
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    • Thambirajah, A.A.1    Ishibashi, T.2    Ausio, J.3
  • 2
    • 70349292569 scopus 로고    scopus 로고
    • Histone H2A.Z cooperates with RNAi and heterochromatin factors to suppress antisense RNAs
    • Histone H2A.Z cooperates with RNAi and heterochromatin factors to suppress antisense RNAs. M Zofall T Fischer K Zhang M Zhou B Cui TD Veenstra SI Grewal, Nature 2009 461 419 422
    • (2009) Nature , vol.461 , pp. 419-422
    • Zofall, M.1    Fischer, T.2    Zhang, K.3    Zhou, M.4    Cui, B.5    Veenstra, T.D.6    Grewal, S.I.7
  • 4
    • 34548777017 scopus 로고    scopus 로고
    • Monoubiquitylation of H2A.Z distinguishes its association with euchromatin or facultative heterochromatin
    • Monoubiquitylation of H2A.Z distinguishes its association with euchromatin or facultative heterochromatin. E Sarcinella PC Zuzarte PN Lau R Draker P Cheung, Mol Cell Biol 2007 27 6457 6486
    • (2007) Mol Cell Biol , vol.27 , pp. 6457-6486
    • Sarcinella, E.1    Zuzarte, P.C.2    Lau, P.N.3    Draker, R.4    Cheung, P.5
  • 5
    • 59649124496 scopus 로고    scopus 로고
    • Chromosome wide Rad51 spreading and SUMO-H2A.Z-dependent chromosome fixation in response to a persistent DNA double-strand break
    • Chromosome wide Rad51 spreading and SUMO-H2A.Z-dependent chromosome fixation in response to a persistent DNA double-strand break. M Kalocsay NJ Hiller S Jentsch, Mol Cell 2009 33 335 343
    • (2009) Mol Cell , vol.33 , pp. 335-343
    • Kalocsay, M.1    Hiller, N.J.2    Jentsch, S.3
  • 6
    • 38949091078 scopus 로고    scopus 로고
    • H2A.Z: View from the top
    • H2A.Z: view from the top. J Zlatanova A Thakar, Structure 2008 16 166 179
    • (2008) Structure , vol.16 , pp. 166-179
    • Zlatanova, J.1    Thakar, A.2
  • 7
    • 68449083728 scopus 로고    scopus 로고
    • The beauty of being a variant: H2A.Z and the SWR1 complex in plants
    • The beauty of being a variant: H2A.Z and the SWR1 complex in plants. R March-Díaz JC Reyes, Mol Plant 2009 2 565 577
    • (2009) Mol Plant , vol.2 , pp. 565-577
    • March-Díaz, R.1    Reyes, J.C.2
  • 9
    • 34250745886 scopus 로고    scopus 로고
    • Nucleosome stability mediated by histone variants H3.3 and H2A.Z
    • Nucleosome stability mediated by histone variants H3.3 and H2A.Z. C Jin G Felsenfeld, Genes Dev 2007 21 1519 1529
    • (2007) Genes Dev , vol.21 , pp. 1519-1529
    • Jin, C.1    Felsenfeld, G.2
  • 12
    • 60649120292 scopus 로고    scopus 로고
    • The evolutionary differentiation of two histone H2A.Z variants in chordates (H2A.Z-1 and H2A.Z-2) is mediated by a stepwise mutation process that affects three amino acid residues
    • The evolutionary differentiation of two histone H2A.Z variants in chordates (H2A.Z-1 and H2A.Z-2) is mediated by a stepwise mutation process that affects three amino acid residues. JM Eirín-Lápez R Gonzlez-Romero D Dryhurst T Ishibashi J Ausiá BMC Evol Biol 2009 9 31
    • (2009) BMC Evol Biol , vol.9 , pp. 31
    • Eirín-Lápez, J.M.1    Gonzlez-Romero, R.2    Dryhurst, D.3    Ishibashi, T.4    Ausiá, J.5
  • 13
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    • The histone variant H3.3 marks active chromatin by replication- independent nucleosome assembly
    • The histone variant H3.3 marks active chromatin by replication- independent nucleosome assembly. K Ahmad S Henikoff, Mol Cell 2002 9 1191 1200
    • (2002) Mol Cell , vol.9 , pp. 1191-1200
    • Ahmad, K.1    Henikoff, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.