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Volumn 19, Issue 10, 2009, Pages 1217-1220

A systematic evaluation of the compatibility of histones containing methyl-lysine analogues with biochemical reactions

Author keywords

[No Author keywords available]

Indexed keywords

DRUG DERIVATIVE; EHMT2 PROTEIN, HUMAN; HISTOCOMPATIBILITY ANTIGEN; HISTONE; HISTONE DEMETHYLASE; HISTONE LYSINE METHYLTRANSFERASE; HISTONE METHYLTRANSFERASE; LYSINE;

EID: 70349786358     PISSN: 10010602     EISSN: 17487838     Source Type: Journal    
DOI: 10.1038/cr.2009.110     Document Type: Article
Times cited : (19)

References (10)
  • 1
    • 36248982297 scopus 로고    scopus 로고
    • Allis CD, Jenuwein T, Reinberg D, eds. Epigenetics. Cold Spring Harbor Laboratory Press: New York
    • Allis CD, Jenuwein T, Reinberg D. In: Allis CD, Jenuwein T, Reinberg D, eds. Epigenetics. Cold Spring Harbor Laboratory Press: New York 2006:23-56.
    • (2006) , pp. 23-56
    • Allis, C.D.1    Jenuwein, T.2    Reinberg, D.3
  • 2
    • 33847386172 scopus 로고    scopus 로고
    • The site-specific installation of methyl-lysine analogs into recombinant histones
    • Simon MD, Chu F, Racki LR, et al. The site-specific installation of methyl-lysine analogs into recombinant histones. Cell 2007; 128:1003-1012.
    • (2007) Cell , vol.128 , pp. 1003-1012
    • Simon, M.D.1    Chu, F.2    Racki, L.R.3
  • 3
    • 33845666681 scopus 로고    scopus 로고
    • The ankyrin repeats of G9a and GLP histone methyltransferases are mono- and dimethyllysine binding modules
    • Botuyan MV, Lee J, Ward IM, et al. Structural basis for the methylation state-specific recognition of histone H4-K20 by 53BP1 and Crb2 in DNA repair. Cell 2006; 127:1361-1373.
    • (2006) Cell , vol.127 , pp. 245-250
    • Botuyan, M.V.1    Lee, J.2    Ward, I.M.3
  • 4
    • 40949148102 scopus 로고    scopus 로고
    • The ankyrin repeats of G9a and GLP histone methyltransferases are mono- and dimethyllysine binding modules
    • Collins RE, Northrop JP, Horton JR, et al. The ankyrin repeats of G9a and GLP histone methyltransferases are mono- and dimethyllysine binding modules. Nat Struct Mol Biol 2008; 15:245-250.
    • (2008) Nat Struct Mol Biol , vol.15 , pp. 245-250
    • Collins, R.E.1    Northrop, J.P.2    Horton, J.R.3
  • 5
    • 38549139593 scopus 로고    scopus 로고
    • Dynamic histone H3 methylation during gene induction: HYPB/Setd2 mediates all H3K36 trimethylation
    • Edmunds JW, Mahadevan LC, Clayton AL. Dynamic histone H3 methylation during gene induction: HYPB/Setd2 mediates all H3K36 trimethylation. EMBO J 2008; 27:406-420.
    • (2008) EMBO J , vol.27 , pp. 406-420
    • Edmunds, J.W.1    Mahadevan, L.C.2    Clayton, A.L.3
  • 6
    • 67650120109 scopus 로고    scopus 로고
    • Heterogeneous nuclear ribo- nucleoprotein L is a subunit of human KMT3a/Set2 complex required for H3 Lys-36 trimethylation activity
    • Yuan W, Xie J, Long C, et al. Heterogeneous nuclear ribo- nucleoprotein L is a subunit of human KMT3a/Set2 complex required for H3 Lys-36 trimethylation activity in vivo. J Biol Chem 2009; 284:15701-15707.
    • (2009) In Vivo. J Biol Chem , vol.284 , pp. 15701-15707
    • Yuan, W.1    Xie, J.2    Long, C.3
  • 7
    • 48749102722 scopus 로고    scopus 로고
    • A chromatin-wide transition to H4K20 monomethylation impairs genome integrity and programmed DNA rearrangements in the mouse
    • Schotta G, Sengupta R, Kubicek S, et al. A chromatin-wide transition to H4K20 monomethylation impairs genome integrity and programmed DNA rearrangements in the mouse. Genes Dev 2008; 22:2048-2061.
    • (2008) Genes Dev , vol.22 , pp. 2048-2061
    • Schotta, G.1    Sengupta, R.2    Kubicek, S.3
  • 8
    • 24944520025 scopus 로고    scopus 로고
    • Molecular regulation of histone H3 trimethylation by COMPASS and the regulation of gene expression
    • Schneider J, Wood A, Lee JS, et al. Molecular regulation of histone H3 trimethylation by COMPASS and the regulation of gene expression. Mol Cell 2005; 19: 849-856.
    • (2005) Mol Cell , vol.19 , pp. 849-856
    • Schneider, J.1    Wood, A.2    Lee, J.S.3
  • 9
    • 34548644772 scopus 로고    scopus 로고
    • The histone H3 lysine-27 demethylase Jmjd3 links inflammation to inhibition of polycomb-mediated gene silencing
    • De Santa F, Totaro MG, Prosperini E, Notarbartolo S, Testa G, Natoli G. The histone H3 lysine-27 demethylase Jmjd3 links inflammation to inhibition of polycomb-mediated gene silencing. Cell 2007; 130:1083-1094.
    • (2007) Cell , vol.130 , pp. 1083-1094
    • De Santa, F.1    Totaro, M.G.2    Prosperini, E.3    Notarbartolo, S.4    Testa, G.5    Natoli, G.6
  • 10
    • 32844454603 scopus 로고    scopus 로고
    • Histone demethylation by a family of JmjC domain-containing proteins
    • Tsukada Y, Fang J, Erdjument-Bromage H, et al. Histone demethylation by a family of JmjC domain-containing proteins. Nature 2006; 439:811-816.
    • (2006) Nature , vol.439 , pp. 811-816
    • Tsukada, Y.1    Fang, J.2    Erdjument-Bromage, H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.