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Volumn 52, Issue 1, 2012, Pages 79-92

Lysine methylation and the regulation of p53

Author keywords

[No Author keywords available]

Indexed keywords

LYSINE; PROTEIN P53;

EID: 84867587970     PISSN: 00711365     EISSN: None     Source Type: Journal    
DOI: 10.1042/BSE0520079     Document Type: Article
Times cited : (12)

References (37)
  • 1
    • 68849093989 scopus 로고    scopus 로고
    • Tumour suppression by p53: The importance of apoptosis and cellular senescence
    • Zuckerman, V., Wolyniec, K., Sionov, R.V., Haupt, S. and Haupt, Y. (2009) Tumour suppression by p53: the importance of apoptosis and cellular senescence. J. Pathol. 210, 3-15
    • (2009) J. Pathol. , vol.210 , pp. 3-15
    • Zuckerman, V.1    Wolyniec, K.2    Sionov, R.V.3    Haupt, S.4    Haupt, Y.5
  • 2
    • 65549120715 scopus 로고    scopus 로고
    • Modes of p53 regulation
    • Kruse, J.P. and Gu, W. (2009) Modes of p53 regulation. Cell 137, 609-622
    • (2009) Cell , vol.137 , pp. 609-622
    • Kruse, J.P.1    Gu, W.2
  • 5
    • 27544446991 scopus 로고    scopus 로고
    • Life in the balance: How BH3-only proteins induce apoptosis
    • Willis, S.N. and Adams, J.M. (2005) Life in the balance: how BH3-only proteins induce apoptosis. Curr. Opin. Cell Biol. 17, 617-625
    • (2005) Curr. Opin. Cell Biol. , vol.17 , pp. 617-625
    • Willis, S.N.1    Adams, J.M.2
  • 6
    • 0034915032 scopus 로고    scopus 로고
    • Control of p53 ubiquitination and nuclear export by MDM2 and ARF
    • Zhang, Y. and Xiong, Y. (2001) Control of p53 ubiquitination and nuclear export by MDM2 and ARF. Cell Growth Differ. 12, 175-186
    • (2001) Cell Growth Differ. , vol.12 , pp. 175-186
    • Zhang, Y.1    Xiong, Y.2
  • 8
    • 78049302116 scopus 로고    scopus 로고
    • P53 post-translational modification: Deregulated in tumorigenesis
    • Dai, C. and Gu, W. (2010) p53 post-translational modification: deregulated in tumorigenesis. Trends Mol. Med. 16, 528-536
    • (2010) Trends Mol. Med. , vol.16 , pp. 528-536
    • Dai, C.1    Gu, W.2
  • 9
    • 0030667702 scopus 로고    scopus 로고
    • DNA damage-induced phosphorylation of p53 alleviates inhibition by MDM2
    • Shieh, S.Y., Ikeda, M., Taya, Y. and Prives, C. (1997) DNA damage-induced phosphorylation of p53 alleviates inhibition by MDM2. Cell 91, 325-334
    • (1997) Cell , vol.91 , pp. 325-334
    • Shieh, S.Y.1    Ikeda, M.2    Taya, Y.3    Prives, C.4
  • 10
    • 27644589675 scopus 로고    scopus 로고
    • The diverse functions of histone lysine methylation
    • Martin, C. and Zhang, Y. (2005) The diverse functions of histone lysine methylation. Nat. Rev. Mol. Cell Biol. 6, 838-849
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 838-849
    • Martin, C.1    Zhang, Y.2
  • 11
    • 33947513027 scopus 로고    scopus 로고
    • Regulation of histone methylation by demethylimination and demethylation
    • Klose, R.J. and Zhang, Y. (2007) Regulation of histone methylation by demethylimination and demethylation. Nat. Rev. Mol. Cell Biol. 8, 307-318
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 307-318
    • Klose, R.J.1    Zhang, Y.2
  • 12
    • 78549287139 scopus 로고    scopus 로고
    • Keeping it in the family: Diverse histone recognition by conserved structural folds
    • Yap, K.L. and Zhou, M.M. (2010) Keeping it in the family: diverse histone recognition by conserved structural folds. Crit. Rev. Biochem. Mol. Biol. 45, 488-505
    • (2010) Crit. Rev. Biochem. Mol. Biol. , vol.45 , pp. 488-505
    • Yap, K.L.1    Zhou, M.M.2
  • 17
    • 80051733486 scopus 로고    scopus 로고
    • The methyltransferase Set7/9 (Setd7) is dispensable for the p53-mediated DNA damage response in vivo
    • Campaner, S., Spreafico, F., Burgold, T., Doni, M., Rosato, U., Amati, B. and Testa, G. (2011) The methyltransferase Set7/9 (Setd7) is dispensable for the p53-mediated DNA damage response in vivo. Mol. Cell 43, 681-688
    • (2011) Mol. Cell , vol.43 , pp. 681-688
    • Campaner, S.1    Spreafico, F.2    Burgold, T.3    Doni, M.4    Rosato, U.5    Amati, B.6    Testa, G.7
  • 18
    • 80051733367 scopus 로고    scopus 로고
    • P53- dependent transcription and tumor suppression are not affected in Set7/9-deficient mice
    • Lehnertz, B., Rogalski, J.C., Schulze, F.M., Yi, L., Lin, S., Kast, J. and Rossi, F.M.V. (2011) p53- dependent transcription and tumor suppression are not affected in Set7/9-deficient mice. Mol. Cell 43, 673-680
    • (2011) Mol. Cell , vol.43 , pp. 673-680
    • Lehnertz, B.1    Rogalski, J.C.2    Schulze, F.M.3    Yi, L.4    Lin, S.5    Kast, J.6    Rossi, F.M.V.7
  • 23
    • 58049203867 scopus 로고    scopus 로고
    • Role for 53BP1 Tudor domain recognition of p53 dimethylated at lysine 382 in DNA damage signalling
    • Kachirskaia, I., Shi, X., Yamaguchi, H., Tanoue, K., Wen, H., Wang, E.W., Appella, E. and Gozani, O. (2008) Role for 53BP1 Tudor domain recognition of p53 dimethylated at lysine 382 in DNA damage signalling. J. Biol. Chem. 50, 34660-34666
    • (2008) J. Biol. Chem. , vol.50 , pp. 34660-34666
    • Kachirskaia, I.1    Shi, X.2    Yamaguchi, H.3    Tanoue, K.4    Wen, H.5    Wang, E.W.6    Appella, E.7    Gozani, O.8
  • 27
    • 33845668241 scopus 로고    scopus 로고
    • Tip60-dependent acetylation of p53 modulates the decision between cell-cycle arrest and apoptosis
    • Tang, Y., Luo, J., Zhang, W. and Gu, W. (2006) Tip60-dependent acetylation of p53 modulates the decision between cell-cycle arrest and apoptosis. Mol. Cell 24, 827-839
    • (2006) Mol. Cell , vol.24 , pp. 827-839
    • Tang, Y.1    Luo, J.2    Zhang, W.3    Gu, W.4
  • 31
    • 35848936709 scopus 로고    scopus 로고
    • Cross-regulation of histone modifications
    • Latham, J.A. and Dent, S.Y.R. (2007) Cross-regulation of histone modifications. Nat. Struct. Mol. Biol. 14, 1017-1024
    • (2007) Nat. Struct. Mol. Biol. , vol.14 , pp. 1017-1024
    • Latham, J.A.1    Dent, S.Y.R.2
  • 32
    • 0032540088 scopus 로고    scopus 로고
    • Regulation of the p53 protein by protein kinase Cα and protein kinase Cζ
    • Youmell, M., Park, S.J., Basu, S. and Price, B.D. (1998) Regulation of the p53 protein by protein kinase Cα and protein kinase Cζ. Biochem. Biophys. Res. Commun. 245, 514-518
    • (1998) Biochem. Biophys. Res. Commun. , vol.245 , pp. 514-518
    • Youmell, M.1    Park, S.J.2    Basu, S.3    Price, B.D.4
  • 33
    • 78751629039 scopus 로고    scopus 로고
    • Interplay between lysine methylation and Cdk phosphorylation in growth control by the retinoblastoma protein
    • Carr, S.M., Munro, S., Kessler, B., Oppermann, U. and La Thangue, N.B. (2011) Interplay between lysine methylation and Cdk phosphorylation in growth control by the retinoblastoma protein. EMBO J. 30, 317-327
    • (2011) EMBO J. , vol.30 , pp. 317-327
    • Carr, S.M.1    Munro, S.2    Kessler, B.3    Oppermann, U.4    La Thangue, N.B.5
  • 35
    • 77951623834 scopus 로고    scopus 로고
    • Lysine methylation regulates the pRb tumour suppressor protein
    • Munro, S., Khaire, N., Inche, A., Carr, S.M. and La Thangue, N.B. (2010) Lysine methylation regulates the pRb tumour suppressor protein. Oncogene 29, 2357-2367
    • (2010) Oncogene , vol.29 , pp. 2357-2367
    • Munro, S.1    Khaire, N.2    Inche, A.3    Carr, S.M.4    La Thangue, N.B.5
  • 37
    • 77954274181 scopus 로고    scopus 로고
    • Lysine methylation regulates E2F1-induced cell death
    • Kontaki, H. and Talianidis, I. (2010) Lysine methylation regulates E2F1-induced cell death. Mol. Cell 39, 152-160
    • (2010) Mol. Cell , vol.39 , pp. 152-160
    • Kontaki, H.1    Talianidis, I.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.