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Volumn 9, Issue 11, 2010, Pages 5827-5836

Systematic identification of methyllysine-driven interactions for histone and nonhistone targets

Author keywords

Chromatin binding modules; Epigenetics; Histone modification; Lysine methylation; Mass spectrometry; Multiple reaction monitoring; Peptide array

Indexed keywords

HETEROCHROMATIN PROTEIN 1; HISTONE; HISTONE H3; LYSINE DERIVATIVE; METHYLLYSINE; NONHISTONE PROTEIN; PROTEIN P53; UNCLASSIFIED DRUG;

EID: 78149374556     PISSN: 15353893     EISSN: 15353907     Source Type: Journal    
DOI: 10.1021/pr100597b     Document Type: Article
Times cited : (33)

References (46)
  • 1
    • 59349115177 scopus 로고    scopus 로고
    • Chemical mechanisms of histone lysine and arginine modifications
    • Smith, B. C.; Denu, J. M. Chemical mechanisms of histone lysine and arginine modifications Biochim. Biophys. Acta 2009, 1789 (1) 45-57
    • (2009) Biochim. Biophys. Acta , vol.1789 , Issue.1 , pp. 45-57
    • Smith, B.C.1    Denu, J.M.2
  • 2
    • 67650901198 scopus 로고    scopus 로고
    • Chromatin maps, histone modifications and leukemia
    • Neff, T.; Armstrong, S. A. Chromatin maps, histone modifications and leukemia Leukemia 2009, 23 (7) 1243-51
    • (2009) Leukemia , vol.23 , Issue.7 , pp. 1243-51
    • Neff, T.1    Armstrong, S.A.2
  • 3
    • 66349120902 scopus 로고    scopus 로고
    • Histone arginine methylations: Their roles in chromatin dynamics and transcriptional regulation
    • Litt, M.; Qiu, Y.; Huang, S. Histone arginine methylations: their roles in chromatin dynamics and transcriptional regulation Biosci. Rep. 2009, 29 (2) 131-41
    • (2009) Biosci. Rep. , vol.29 , Issue.2 , pp. 131-41
    • Litt, M.1    Qiu, Y.2    Huang, S.3
  • 4
    • 78651162036 scopus 로고
    • Acetylation and Methylation of Histones and Their Possible Role in the Regulation of Rna Synthesis
    • Allfrey, V. G.; Faulkner, R.; Mirsky, A. E. Acetylation and Methylation of Histones and Their Possible Role in the Regulation of Rna Synthesis Proc. Natl. Acad. Sci. U.S.A. 1964, 51, 786-94
    • (1964) Proc. Natl. Acad. Sci. U.S.A. , vol.51 , pp. 786-94
    • Allfrey, V.G.1    Faulkner, R.2    Mirsky, A.E.3
  • 5
    • 78149400026 scopus 로고    scopus 로고
    • Histone H3 lysine 4 (H3K4) methylation in development and differentiation
    • Eissenberg, J. C.; Shilatifard, A. Histone H3 lysine 4 (H3K4) methylation in development and differentiation Dev. Biol. 2009
    • (2009) Dev. Biol.
    • Eissenberg, J.C.1    Shilatifard, A.2
  • 6
    • 34249802072 scopus 로고    scopus 로고
    • Regulation and function of H3K9 methylation
    • Shinkai, Y. Regulation and function of H3K9 methylation Subcell Biochem. 2007, 41, 337-50
    • (2007) Subcell Biochem. , vol.41 , pp. 337-50
    • Shinkai, Y.1
  • 7
    • 33947315736 scopus 로고    scopus 로고
    • Cancer epigenomics: DNA methylomes and histone-modification maps
    • Esteller, M. Cancer epigenomics: DNA methylomes and histone-modification maps Nat. Rev. Genet. 2007, 8 (4) 286-98
    • (2007) Nat. Rev. Genet. , vol.8 , Issue.4 , pp. 286-98
    • Esteller, M.1
  • 8
    • 73449092853 scopus 로고    scopus 로고
    • SET7/9 mediated methylation of non-histone proteins in mammalian cells
    • Pradhan, S.; Chin, H. G.; Esteve, P. O.; Jacobsen, S. E. SET7/9 mediated methylation of non-histone proteins in mammalian cells Epigenetics 2009, 4 (6) 383-7
    • (2009) Epigenetics , vol.4 , Issue.6 , pp. 383-7
    • Pradhan, S.1    Chin, H.G.2    Esteve, P.O.3    Jacobsen, S.E.4
  • 9
    • 44349108499 scopus 로고    scopus 로고
    • The emerging field of dynamic lysine methylation of non-histone proteins
    • Huang, J.; Berger, S. L. The emerging field of dynamic lysine methylation of non-histone proteins Curr. Opin. Genet. Dev. 2008, 18 (2) 152-8
    • (2008) Curr. Opin. Genet. Dev. , vol.18 , Issue.2 , pp. 152-8
    • Huang, J.1    Berger, S.L.2
  • 11
    • 50149097809 scopus 로고    scopus 로고
    • A complex barcode underlies the heterogeneous response of p53 to stress
    • Murray-Zmijewski, F.; Slee, E. A.; Lu, X. A complex barcode underlies the heterogeneous response of p53 to stress Nat. Rev. Mol. Cell. Biol. 2008, 9 (9) 702-12
    • (2008) Nat. Rev. Mol. Cell. Biol. , vol.9 , Issue.9 , pp. 702-12
    • Murray-Zmijewski, F.1    Slee, E.A.2    Lu, X.3
  • 13
    • 34249299791 scopus 로고    scopus 로고
    • The complex language of chromatin regulation during transcription
    • Berger, S. L. The complex language of chromatin regulation during transcription Nature 2007, 447 (7143) 407-12
    • (2007) Nature , vol.447 , Issue.7143 , pp. 407-12
    • Berger, S.L.1
  • 14
    • 35848961668 scopus 로고    scopus 로고
    • How chromatin-binding modules interpret histone modifications: Lessons from professional pocket pickers
    • Taverna, S. D.; Li, H.; Ruthenburg, A. J.; Allis, C. D.; Patel, D. J. How chromatin-binding modules interpret histone modifications: lessons from professional pocket pickers Nat. Struct. Mol. Biol. 2007, 14 (11) 1025-40
    • (2007) Nat. Struct. Mol. Biol. , vol.14 , Issue.11 , pp. 1025-40
    • Taverna, S.D.1    Li, H.2    Ruthenburg, A.J.3    Allis, C.D.4    Patel, D.J.5
  • 15
    • 77954487796 scopus 로고    scopus 로고
    • Mechanism and regulation of acetylated histone binding by the tandem PHD finger of DPF3b
    • Zeng, L.; Zhang, Q.; Li, S.; Plotnikov, A. N.; Walsh, M. J.; Zhou, M. M. Mechanism and regulation of acetylated histone binding by the tandem PHD finger of DPF3b Nature 2010, 466 (7303) 258-62
    • (2010) Nature , vol.466 , Issue.7303 , pp. 258-62
    • Zeng, L.1    Zhang, Q.2    Li, S.3    Plotnikov, A.N.4    Walsh, M.J.5    Zhou, M.M.6
  • 16
    • 43749124629 scopus 로고    scopus 로고
    • A gateway to study protein lysine methylation
    • Trojer, P.; Reinberg, D. A gateway to study protein lysine methylation Nat. Chem. Biol. 2008, 4 (6) 332-4
    • (2008) Nat. Chem. Biol. , vol.4 , Issue.6 , pp. 332-4
    • Trojer, P.1    Reinberg, D.2
  • 17
    • 28044471827 scopus 로고    scopus 로고
    • Acetylation and deacetylation of non-histone proteins
    • Glozak, M. A.; Sengupta, N.; Zhang, X.; Seto, E. Acetylation and deacetylation of non-histone proteins Gene 2005, 363, 15-23
    • (2005) Gene , vol.363 , pp. 15-23
    • Glozak, M.A.1    Sengupta, N.2    Zhang, X.3    Seto, E.4
  • 18
    • 0001331640 scopus 로고
    • Multiple Reaction Monitoring in Mass Spectrometry Mass Spectrometry for Direct Analysis of Complex-Mixtures
    • Kondrat, R. W.; Mcclusky, G. A.; Cooks, R. G. Multiple Reaction Monitoring in Mass Spectrometry Mass Spectrometry for Direct Analysis of Complex-Mixtures Anal. Chem. 1978, 50 (14) 2017-21
    • (1978) Anal. Chem. , vol.50 , Issue.14 , pp. 2017-21
    • Kondrat, R.W.1    McClusky, G.A.2    Cooks, R.G.3
  • 19
    • 24044465136 scopus 로고    scopus 로고
    • Novel Src homology 3 domain-binding motifs identified from proteomic screen of a Pro-rich region
    • Jia, C. Y.; Nie, J.; Wu, C.; Li, C.; Li, S. S. Novel Src homology 3 domain-binding motifs identified from proteomic screen of a Pro-rich region Mol. Cell. Proteomics 2005, 4 (8) 1155-66
    • (2005) Mol. Cell. Proteomics , vol.4 , Issue.8 , pp. 1155-66
    • Jia, C.Y.1    Nie, J.2    Wu, C.3    Li, C.4    Li, S.S.5
  • 20
    • 0000312547 scopus 로고
    • Low-levels of ionizing-radiation and cancer - Are we underestimating the risk
    • Darby, S. C.; Reissland, J. A. Low-levels of ionizing-radiation and cancer-are we underestimating the risk J. R. Stat. Soc., Ser. A: Stat. Soc. 1981, 144, 298-331
    • (1981) J. R. Stat. Soc., Ser. A: Stat. Soc. , vol.144 , pp. 298-331
    • Darby, S.C.1    Reissland, J.A.2
  • 22
    • 30944452960 scopus 로고    scopus 로고
    • The PHD finger, a nuclear protein-interaction domain
    • Bienz, M. The PHD finger, a nuclear protein-interaction domain Trends Biochem. Sci. 2006, 31 (1) 35-40
    • (2006) Trends Biochem. Sci. , vol.31 , Issue.1 , pp. 35-40
    • Bienz, M.1
  • 23
    • 0037086355 scopus 로고    scopus 로고
    • Structure of HP1 chromodomain bound to a lysine 9-methylated histone H3 tail
    • Jacobs, S. A.; Khorasanizadeh, S. Structure of HP1 chromodomain bound to a lysine 9-methylated histone H3 tail Science 2002, 295 (5562) 2080-3
    • (2002) Science , vol.295 , Issue.5562 , pp. 2080-3
    • Jacobs, S.A.1    Khorasanizadeh, S.2
  • 24
    • 27844519267 scopus 로고    scopus 로고
    • HP1 binds specifically to Lys26-methylated histone H1.4, whereas simultaneous Ser27 phosphorylation blocks HP1 binding
    • Daujat, S.; Zeissler, U.; Waldmann, T.; Happel, N.; Schneider, R. HP1 binds specifically to Lys26-methylated histone H1.4, whereas simultaneous Ser27 phosphorylation blocks HP1 binding J. Biol. Chem. 2005, 280 (45) 38090-5
    • (2005) J. Biol. Chem. , vol.280 , Issue.45 , pp. 38090-5
    • Daujat, S.1    Zeissler, U.2    Waldmann, T.3    Happel, N.4    Schneider, R.5
  • 29
    • 33646438365 scopus 로고    scopus 로고
    • Recognition of histone H3 lysine-4 methylation by the double tudor domain of JMJD2A
    • Huang, Y.; Fang, J.; Bedford, M. T.; Zhang, Y.; Xu, R. M. Recognition of histone H3 lysine-4 methylation by the double tudor domain of JMJD2A Science 2006, 312 (5774) 748-51
    • (2006) Science , vol.312 , Issue.5774 , pp. 748-51
    • Huang, Y.1    Fang, J.2    Bedford, M.T.3    Zhang, Y.4    Xu, R.M.5
  • 30
    • 37849015924 scopus 로고    scopus 로고
    • Distinct binding modes specify the recognition of methylated histones H3K4 and H4K20 by JMJD2A-tudor
    • Lee, J.; Thompson, J. R.; Botuyan, M. V.; Mer, G. Distinct binding modes specify the recognition of methylated histones H3K4 and H4K20 by JMJD2A-tudor Nat. Struct. Mol. Biol. 2008, 15 (1) 109-11
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , Issue.1 , pp. 109-11
    • Lee, J.1    Thompson, J.R.2    Botuyan, M.V.3    Mer, G.4
  • 33
    • 46149116301 scopus 로고    scopus 로고
    • A SPOT on the chromatin landscape? Histone peptide arrays as a tool for epigenetic research
    • Nady, N.; Min, J.; Kareta, M. S.; Chedin, F.; Arrowsmith, C. H. A SPOT on the chromatin landscape? Histone peptide arrays as a tool for epigenetic research Trends Biochem. Sci. 2008, 33 (7) 305-13
    • (2008) Trends Biochem. Sci. , vol.33 , Issue.7 , pp. 305-13
    • Nady, N.1    Min, J.2    Kareta, M.S.3    Chedin, F.4    Arrowsmith, C.H.5
  • 34
    • 77953096072 scopus 로고    scopus 로고
    • Molecular interplay of the noncoding RNA ANRIL and methylated histone H3 lysine 27 by polycomb CBX7 in transcriptional silencing of INK4a
    • Yap, K. L.; Li, S.; Munoz-Cabello, A. M.; Raguz, S.; Zeng, L.; Mujtaba, S.; Gil, J.; Walsh, M. J.; Zhou, M. M. Molecular interplay of the noncoding RNA ANRIL and methylated histone H3 lysine 27 by polycomb CBX7 in transcriptional silencing of INK4a Mol. Cell 2010, 38 (5) 662-74
    • (2010) Mol. Cell , vol.38 , Issue.5 , pp. 662-74
    • Yap, K.L.1    Li, S.2    Munoz-Cabello, A.M.3    Raguz, S.4    Zeng, L.5    Mujtaba, S.6    Gil, J.7    Walsh, M.J.8    Zhou, M.M.9
  • 36
    • 77953121401 scopus 로고    scopus 로고
    • PELP1 is a reader of histone H3 methylation that facilitates oestrogen receptor-alpha target gene activation by regulating lysine demethylase 1 specificity
    • Nair, S. S.; Nair, B. C.; Cortez, V.; Chakravarty, D.; Metzger, E.; Schule, R.; Brann, D. W.; Tekmal, R. R.; Vadlamudi, R. K. PELP1 is a reader of histone H3 methylation that facilitates oestrogen receptor-alpha target gene activation by regulating lysine demethylase 1 specificity EMBO Rep. 2010, 11 (6) 438-44
    • (2010) EMBO Rep. , vol.11 , Issue.6 , pp. 438-44
    • Nair, S.S.1    Nair, B.C.2    Cortez, V.3    Chakravarty, D.4    Metzger, E.5    Schule, R.6    Brann, D.W.7    Tekmal, R.R.8    Vadlamudi, R.K.9
  • 39
    • 77950521594 scopus 로고    scopus 로고
    • PHF8 activates transcription of rRNA genes through H3K4me3 binding and H3K9me1/2 demethylation
    • Feng, W.; Yonezawa, M.; Ye, J.; Jenuwein, T.; Grummt, I. PHF8 activates transcription of rRNA genes through H3K4me3 binding and H3K9me1/2 demethylation Nat. Struct. Mol. Biol. 2010, 17 (4) 445-50
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , Issue.4 , pp. 445-50
    • Feng, W.1    Yonezawa, M.2    Ye, J.3    Jenuwein, T.4    Grummt, I.5
  • 40
    • 77951240318 scopus 로고    scopus 로고
    • Recognition of histone H3K4 trimethylation by the plant homeodomain of PHF2 modulates histone demethylation
    • Wen, H.; Li, J.; Song, T.; Lu, M.; Kan, P. Y.; Lee, M. G.; Sha, B.; Shi, X. Recognition of histone H3K4 trimethylation by the plant homeodomain of PHF2 modulates histone demethylation J. Biol. Chem. 2010, 285 (13) 9322-6
    • (2010) J. Biol. Chem. , vol.285 , Issue.13 , pp. 9322-6
    • Wen, H.1    Li, J.2    Song, T.3    Lu, M.4    Kan, P.Y.5    Lee, M.G.6    Sha, B.7    Shi, X.8
  • 42
    • 65149090563 scopus 로고    scopus 로고
    • Structure and site-specific recognition of histone H3 by the PHD finger of human autoimmune regulator
    • Chakravarty, S.; Zeng, L.; Zhou, M. M. Structure and site-specific recognition of histone H3 by the PHD finger of human autoimmune regulator Structure 2009, 17 (5) 670-9
    • (2009) Structure , vol.17 , Issue.5 , pp. 670-9
    • Chakravarty, S.1    Zeng, L.2    Zhou, M.M.3
  • 43
  • 45
    • 0037164736 scopus 로고    scopus 로고
    • Crosstalk between CARM1 methylation and CBP acetylation on histone H3
    • Daujat, S.; Bauer, U. M.; Shah, V.; Turner, B.; Berger, S.; Kouzarides, T. Crosstalk between CARM1 methylation and CBP acetylation on histone H3 Curr. Biol. 2002, 12 (24) 2090-7
    • (2002) Curr. Biol. , vol.12 , Issue.24 , pp. 2090-7
    • Daujat, S.1    Bauer, U.M.2    Shah, V.3    Turner, B.4    Berger, S.5    Kouzarides, T.6
  • 46
    • 33847047461 scopus 로고    scopus 로고
    • Epigenetics: A landscape takes shape
    • Goldberg, A. D.; Allis, C. D.; Bernstein, E. Epigenetics: a landscape takes shape Cell 2007, 128 (4) 635-8
    • (2007) Cell , vol.128 , Issue.4 , pp. 635-8
    • Goldberg, A.D.1    Allis, C.D.2    Bernstein, E.3


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