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Volumn 2, Issue , 2012, Pages 313-317

Co-mutation of histone H2AX S139A with Y142A rescues Y142A-induced ionising radiation sensitivity

Author keywords

53BP1; DSB; H2AX; IR; S139; Y142

Indexed keywords

HISTONE H2AX;

EID: 84867441193     PISSN: 22115463     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.fob.2012.09.008     Document Type: Article
Times cited : (10)

References (18)
  • 1
    • 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., Bonner W.M. DNA double-stranded breaks induce histone H2AX phosphorylation on serine 139. J. Biol. Chem. 1998, 273(10):5858-5868.
    • (1998) J. Biol. Chem. , vol.273 , Issue.10 , pp. 5858-5868
    • Rogakou, E.P.1    Pilch, D.R.2    Orr, A.H.3    Ivanova, V.S.4    Bonner, W.M.5
  • 2
    • 77956416885 scopus 로고    scopus 로고
    • H2AX post-translational modifications in the ionizing radiation response and homologous recombination
    • Xie A., Odate S., Chandramouly G., Scully R. H2AX post-translational modifications in the ionizing radiation response and homologous recombination. Cell Cycle 2010, 9(17):3602-3610.
    • (2010) Cell Cycle , vol.9 , Issue.17 , pp. 3602-3610
    • Xie, A.1    Odate, S.2    Chandramouly, G.3    Scully, R.4
  • 4
    • 77953729074 scopus 로고    scopus 로고
    • Acetylation of H2AX on lysine 36 plays a key role in the DNA double-strand break repair pathway
    • Jiang X., Xu Y., Price B.D. Acetylation of H2AX on lysine 36 plays a key role in the DNA double-strand break repair pathway. FEBS Lett. 2010, 584(13):2926-2930.
    • (2010) FEBS Lett. , vol.584 , Issue.13 , pp. 2926-2930
    • Jiang, X.1    Xu, Y.2    Price, B.D.3
  • 6
    • 63849187827 scopus 로고    scopus 로고
    • Tyrosine dephosphorylation of H2AX modulates apoptosis and survival decisions
    • Cook P.J., Ju B.G., Telese F., Wang X., Glass C.K., Rosenfeld M.G. Tyrosine dephosphorylation of H2AX modulates apoptosis and survival decisions. Nature 2009, 458(7238):591-596.
    • (2009) Nature , vol.458 , Issue.7238 , pp. 591-596
    • Cook, P.J.1    Ju, B.G.2    Telese, F.3    Wang, X.4    Glass, C.K.5    Rosenfeld, M.G.6
  • 7
    • 67650230540 scopus 로고    scopus 로고
    • Dephosphorylation of the C-terminal tyrosyl residue of the DNA damage-related histone H2A.X is mediated by the protein phosphatase eyes absent
    • Krishnan N., Jeong D.G., Jung S.K., Ryu S.E., Xiao A., Allis C.D., Kim S.J., Tonks N.K. Dephosphorylation of the C-terminal tyrosyl residue of the DNA damage-related histone H2A.X is mediated by the protein phosphatase eyes absent. J. Biol. Chem. 2009, 284(24):16066-16070.
    • (2009) J. Biol. Chem. , vol.284 , Issue.24 , pp. 16066-16070
    • Krishnan, N.1    Jeong, D.G.2    Jung, S.K.3    Ryu, S.E.4    Xiao, A.5    Allis, C.D.6    Kim, S.J.7    Tonks, N.K.8
  • 8
    • 83255192184 scopus 로고    scopus 로고
    • A peek into the complex realm of histone phosphorylation
    • Banerjee T., Chakravarti D. A peek into the complex realm of histone phosphorylation. Mol. Cell Biol. 2011, 31(24):4858-4873.
    • (2011) Mol. Cell Biol. , vol.31 , Issue.24 , pp. 4858-4873
    • Banerjee, T.1    Chakravarti, D.2
  • 9
    • 77952908428 scopus 로고    scopus 로고
    • Phosphorylation of histone H2A.X by DNA-dependent protein kinase is not affected by core histone acetylation, but it alters nucleosome stability and histone H1 binding
    • Li A., Yu Y., Lee S.C., Ishibashi T., Lees-Miller S.P., Ausió J. Phosphorylation of histone H2A.X by DNA-dependent protein kinase is not affected by core histone acetylation, but it alters nucleosome stability and histone H1 binding. J. Biol. Chem. 2010, 285(23):17778-17788.
    • (2010) J. Biol. Chem. , vol.285 , Issue.23 , pp. 17778-17788
    • Li, A.1    Yu, Y.2    Lee, S.C.3    Ishibashi, T.4    Lees-Miller, S.P.5    Ausió, J.6
  • 14
    • 29244434544 scopus 로고    scopus 로고
    • MDC1 directly binds phosphorylated histone H2AX to regulate cellular responses to DNA double-strand breaks
    • Stucki M., Clapperton J.A., Mohammad D., Yaffe M.B., Smerdon S.J., Jackson S.P. MDC1 directly binds phosphorylated histone H2AX to regulate cellular responses to DNA double-strand breaks. Cell 2005, 123(7):1213-1226.
    • (2005) Cell , vol.123 , Issue.7 , pp. 1213-1226
    • Stucki, M.1    Clapperton, J.A.2    Mohammad, D.3    Yaffe, M.B.4    Smerdon, S.J.5    Jackson, S.P.6
  • 15
    • 25444465151 scopus 로고    scopus 로고
    • Structure of the BRCT repeat domain of MDC1 and its specificity for the free COOH-terminal end of the {gamma}-H2AX histone tail
    • Lee M.S., Edwards R.A., Thede G.L., Glover J.N. Structure of the BRCT repeat domain of MDC1 and its specificity for the free COOH-terminal end of the {gamma}-H2AX histone tail. J. Biol. Chem. 2005, 280:32053-32056.
    • (2005) J. Biol. Chem. , vol.280 , pp. 32053-32056
    • Lee, M.S.1    Edwards, R.A.2    Thede, G.L.3    Glover, J.N.4
  • 16
    • 0141780833 scopus 로고    scopus 로고
    • NFBD1/MDC1 regulates ionizing radiation-induced focus formation by DNA checkpoint signaling and repair factors
    • Xu X., Stern D.F. NFBD1/MDC1 regulates ionizing radiation-induced focus formation by DNA checkpoint signaling and repair factors. FASEB J. 2003, 17:1842-1848.
    • (2003) FASEB J. , vol.17 , pp. 1842-1848
    • Xu, X.1    Stern, D.F.2
  • 17
    • 0034739853 scopus 로고    scopus 로고
    • P53 binding protein 1 (53BP1) is an early participant in the cellular response to DNA double-strand breaks
    • Schultz L.B., Chehab N.H., Malikzay A., Halazonetis T.D. p53 binding protein 1 (53BP1) is an early participant in the cellular response to DNA double-strand breaks. J. Cell Biol. 2000, 151(7):1381-1390.
    • (2000) J. Cell Biol. , vol.151 , Issue.7 , pp. 1381-1390
    • Schultz, L.B.1    Chehab, N.H.2    Malikzay, A.3    Halazonetis, T.D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.