메뉴 건너뛰기




Volumn 65, Issue 5, 2012, Pages 263-265

Erratum: Inhibition of histone H3K9 methyltransferases by gliotoxin and related epipolythiodioxopiperazines (Journal of Antibiotics (2012) 65 (263-265) DOI: 10.1038/ja.2012.6);Inhibition of histone H3K9 methyltransferases by gliotoxin and related epipolythiodioxopiperazines

Author keywords

epipolythiodioxopiperazine (ETP); G9a; gliotoxin; histone H3K9 methylation; histone methyltransferase (HMT); inhibitor; Suv39h1

Indexed keywords

11,11' DIDEOXYVERTICILLIN A; BACTERIAL PROTEIN; BISDETHIOBIS(METHYLTHIO)ACETYLGLIOTOXIN; CHETOMIN; GLIOTOXIN; H3K9 PROTEIN; HISTONE LYSINE METHYLTRANSFERASE; PIPERAZINE DERIVATIVE; UNCLASSIFIED DRUG;

EID: 84861607876     PISSN: 00218820     EISSN: 18811469     Source Type: Journal    
DOI: 10.1038/ja.2014.101     Document Type: Erratum
Times cited : (29)

References (18)
  • 1
    • 0035839110 scopus 로고    scopus 로고
    • Transitions in distinct histone H3 methylation patterns at the heterochromatin domain boundaries
    • Noma, K., Allis, C. D. & Grewal, S. I. Transitions in distinct histone H3 methylation patterns at the heterochromatin domain boundaries. Science 293, 1150-1155 (2001).
    • (2001) Science , vol.293 , pp. 1150-1155
    • Noma, K.1    Allis, C.D.2    Grewal, S.I.3
  • 2
    • 0035816682 scopus 로고    scopus 로고
    • Set domain-containing protein, G9a, is a novel lysine-preferring mammalian histone methyltransferase with hyperactivity and specific selectivity to lysines 9 and 27 of histone H3
    • Tachibana, M., Sugimoto, K., Fukushima, T. & Shinkai, Y. Set domain-containing protein, G9a, is a novel lysine-preferring mammalian histone methyltransferase with hyperactivity and specific selectivity to lysines 9 and 27 of histone H3. J. Biol. Chem. 276, 25309-25317 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 25309-25317
    • Tachibana, M.1    Sugimoto, K.2    Fukushima, T.3    Shinkai, Y.4
  • 3
    • 0034632829 scopus 로고    scopus 로고
    • Regulation of chromatin structure by site-specific histone H3 methyltransferases
    • Rea, S. et al. Regulation of chromatin structure by site-specific histone H3 methyltransferases. Nature 406, 593-599 (2000).
    • (2000) Nature , vol.406 , pp. 593-599
    • Rea, S.1
  • 4
    • 20144388930 scopus 로고    scopus 로고
    • Histone methyltransferases G9a and GLP form heteromeric complexes and are both crucial for methylation of euchromatin at H3-K9
    • Tachibana, M. et al. Histone methyltransferases G9a and GLP form heteromeric complexes and are both crucial for methylation of euchromatin at H3-K9. Genes Dev. 19, 815-826 (2005).
    • (2005) Genes Dev. , vol.19 , pp. 815-826
    • Tachibana, M.1
  • 5
    • 33644846509 scopus 로고    scopus 로고
    • Epigenetic gene silencing in cancer - A mechanism for early oncogenic pathway addiction
    • Baylin, S. B. & Ohm, J. E. Epigenetic gene silencing in cancer - A mechanism for early oncogenic pathway addiction? Nat. Rev. Cancer 6, 107-116 (2006).
    • (2006) Nat. Rev. Cancer , vol.6 , pp. 107-116
    • Baylin, S.B.1    Ohm, J.E.2
  • 6
    • 77950678085 scopus 로고    scopus 로고
    • Coordinated chromatin control: Structural and functional linkage of DNA and histone methylation
    • Cheng, X. & Blumenthal, R. M. Coordinated chromatin control: Structural and functional linkage of DNA and histone methylation. Biochemistry 49, 2999-3008 (2010).
    • (2010) Biochemistry , vol.49 , pp. 2999-3008
    • Cheng, X.1    Blumenthal, R.M.2
  • 7
    • 56649103900 scopus 로고    scopus 로고
    • Deregulation of histone lysine methyltransferases contributes to oncogenic transformation of human bronchoepithelial cells
    • Watanabe, H. et al. Deregulation of histone lysine methyltransferases contributes to oncogenic transformation of human bronchoepithelial cells. Cancer Cell Int. 8, 15 (2008).
    • (2008) Cancer Cell Int. , vol.8 , pp. 15
    • Watanabe, H.1
  • 8
    • 77951233574 scopus 로고    scopus 로고
    • G9a and Glp methylate lysine 373 in the tumor suppressor p53
    • Huang,J.et al. G9a and Glp methylate lysine 373 in the tumor suppressor p53. J. Biol. Chem. 285, 9636-9641 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 9636-9641
    • Huang, J.1
  • 9
    • 78049307486 scopus 로고    scopus 로고
    • H3K9 histone methyltransferase G9a promotes lung cancer invasion and metastasis by silencing the cell adhesion molecule Ep-CAM
    • Chen,M.W.et al. H3K9 histone methyltransferase G9a promotes lung cancer invasion and metastasis by silencing the cell adhesion molecule Ep-CAM. Cancer Res. 70, 7830-7840 (2010).
    • (2010) Cancer Res. , vol.70 , pp. 7830-7840
    • Chen, M.W.1
  • 10
    • 30644474460 scopus 로고    scopus 로고
    • Identification of a specific inhibitor of the histone methyltransferase SU(VAR) 3-9
    • Greiner, D., Bonaldi, T., Eskeland, R., Roemer, E. & Imhof, A. Identification of a specific inhibitor of the histone methyltransferase SU(VAR)3-9. Nat. Chem. Biol. 1, 143-145 (2005).
    • (2005) Nat. Chem. Biol. , Issue.1 , pp. 143-145
    • Greiner, D.1    Bonaldi, T.2    Eskeland, R.3    Roemer, E.4    Imhof, A.5
  • 11
    • 33846783261 scopus 로고    scopus 로고
    • Reversal of H3K9me2 by a small-molecule inhibitor for the G9a histone methyltransferase
    • Kubicek, S. et al. Reversal of H3K9me2 by a small-molecule inhibitor for the G9a histone methyltransferase. Mol. Cell 25, 473-481 (2007).
    • (2007) Mol. Cell , vol.25 , pp. 473-481
    • Kubicek, S.1
  • 12
    • 62049083789 scopus 로고    scopus 로고
    • Structural basis for G9a-like protein lysine methyltransferase inhibition by BIX-01294
    • Chang, Y. et al. Structural basis for G9a-like protein lysine methyltransferase inhibition by BIX-01294. Nat. Struct. Mol. Biol. 16, 312-317 (2009).
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 312-317
    • Chang, Y.1
  • 13
    • 73249124141 scopus 로고    scopus 로고
    • Discovery of a 2,4-diamino-7-Aminoalkoxyquinazoline as a potent and selective inhibitor of histone lysine methyltransferase G9a
    • Liu, F. et al. Discovery of a 2,4-diamino-7-Aminoalkoxyquinazoline as a potent and selective inhibitor of histone lysine methyltransferase G9a. J. Med. Chem. 52, 7950-7953 (2009).
    • (2009) J. Med. Chem. , vol.52 , pp. 7950-7953
    • Liu, F.1
  • 14
    • 77955363182 scopus 로고    scopus 로고
    • Protein lysine methyltransferase G9a inhibitors: Design, syn thesis, and structure activity relationships of 2,4-diamino-7-Aminoalkoxy-quinazolines
    • Liu, F. et al. Protein lysine methyltransferase G9a inhibitors: Design, synthesis, and structure activity relationships of 2,4-diamino-7-Aminoalkoxy- quinazolines. J. Med. Chem. 53, 5844-5857 (2010).
    • (2010) J. Med. Chem. , vol.53 , pp. 5844-5857
    • Liu, F.1
  • 15
    • 79960493567 scopus 로고    scopus 로고
    • A chemical probe selectively inhibits G9a and GLP methyltransferase activity in cells
    • Vedadi, M. et al. A chemical probe selectively inhibits G9a and GLP methyltransferase activity in cells. Nat. Chem. Biol. 7, 566-574 (2011).
    • (2011) Nat. Chem. Biol. , vol.7 , pp. 566-574
    • Vedadi, M.1
  • 16
    • 77950229791 scopus 로고    scopus 로고
    • Total synthesis of (+)-chaetocin and its analogues: Their histone methyltransferase G9a inhibitory activity
    • Iwasa, E. et al. Total synthesis of (+)-chaetocin and its analogues: Their histone methyltransferase G9a inhibitory activity. J. Am. Chem. Soc. 132, 4078-4079 (2010).
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 4078-4079
    • Iwasa, E.1
  • 17
    • 0037083757 scopus 로고    scopus 로고
    • Set9, a novel histone H3 methyltransferase that facilitates transcription by precluding histone tail modifications required for heterochromatin formation
    • Nishioka, K. et al. Set9, a novel histone H3 methyltransferase that facilitates transcription by precluding histone tail modifications required for heterochromatin formation. Genes Dev. 16, 479-489 (2002).
    • (2002) Genes Dev. , vol.16 , pp. 479-489
    • Nishioka, K.1
  • 18
    • 17644412298 scopus 로고    scopus 로고
    • The epipolythiodioxopiperazine (ETP) class of fungal toxins: Distribution, mode of action, functions and biosynthesis
    • Gardiner, D. M., Waring, P. & Howlett, B. J. The epipolythiodioxopiperazine (ETP) class of fungal toxins: Distribution, mode of action, functions and biosynthesis. Microbiology 151, 1021-32 (2005).
    • (2005) Microbiology , vol.151 , pp. 1021-1032
    • Gardiner, D.M.1    Waring, P.2    Howlett, B.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.