메뉴 건너뛰기




Volumn 512, Issue , 2012, Pages 57-69

A method to site-specifically incorporate methyl-lysine analogues into recombinant proteins

Author keywords

Aminoethylcysteine; Chromatin; Cysteine alkylation; Histones; Methyl lysine analogue; MLA

Indexed keywords

CYSTEINE; ETHYLAMINE; HISTONE; LYSINE DERIVATIVE; METHYL LYSINE ANALOGUE; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG;

EID: 84865341932     PISSN: 00766879     EISSN: 15577988     Source Type: Book Series    
DOI: 10.1016/B978-0-12-391940-3.00003-2     Document Type: Chapter
Times cited : (14)

References (25)
  • 3
    • 78650734995 scopus 로고    scopus 로고
    • Chromodomain-mediated oligomerization of HP1 suggests a nucleosome-bridging mechanism for heterochromatin assembly
    • D. Canzio, E.Y. Chang, S. Shankar, K.M. Kuchenbecker, M.D. Simon, and H.D. Madhani Chromodomain-mediated oligomerization of HP1 suggests a nucleosome-bridging mechanism for heterochromatin assembly Molecular Cell 41 2011 67 81
    • (2011) Molecular Cell , vol.41 , pp. 67-81
    • Canzio, D.1    Chang, E.Y.2    Shankar, S.3    Kuchenbecker, K.M.4    Simon, M.D.5    Madhani, H.D.6
  • 4
    • 63049138876 scopus 로고    scopus 로고
    • Polycomb proteins remain bound to chromatin and DNA during DNA replication in vitro
    • N.J. Francis, N.E. Follmer, M.D. Simon, G. Aghia, and J.D. Butler Polycomb proteins remain bound to chromatin and DNA during DNA replication in vitro Cell 137 2009 110 122
    • (2009) Cell , vol.137 , pp. 110-122
    • Francis, N.J.1    Follmer, N.E.2    Simon, M.D.3    Aghia, G.4    Butler, J.D.5
  • 5
    • 0042528729 scopus 로고    scopus 로고
    • Heterochromatin and epigenetic control of gene expression
    • S.I. Grewal, and D. Moazed Heterochromatin and epigenetic control of gene expression Science 301 2003 798 802
    • (2003) Science , vol.301 , pp. 798-802
    • Grewal, S.I.1    Moazed, D.2
  • 8
    • 58649102691 scopus 로고    scopus 로고
    • ING4 mediates crosstalk between histone H3 K4 trimethylation and H3 acetylation to attenuate cellular transformation
    • T. Hung, O. Binda, K.S. Champagne, A.J. Kuo, K. Johnson, and H.Y. Chang ING4 mediates crosstalk between histone H3 K4 trimethylation and H3 acetylation to attenuate cellular transformation Molecular Cell 33 2009 248 256
    • (2009) Molecular Cell , vol.33 , pp. 248-256
    • Hung, T.1    Binda, O.2    Champagne, K.S.3    Kuo, A.J.4    Johnson, K.5    Chang, H.Y.6
  • 9
    • 70349786358 scopus 로고    scopus 로고
    • A systematic evaluation of the compatibility of histones containing methyl-lysine analogues with biochemical reactions
    • G. Jia, W. Wang, H. Li, Z. Mao, G. Cai, and J. Sun A systematic evaluation of the compatibility of histones containing methyl-lysine analogues with biochemical reactions Cell Research 19 2009 1217 1220
    • (2009) Cell Research , vol.19 , pp. 1217-1220
    • Jia, G.1    Wang, W.2    Li, H.3    Mao, Z.4    Cai, G.5    Sun, J.6
  • 11
    • 33847076849 scopus 로고    scopus 로고
    • Chromatin modifications and their function
    • T. Kouzarides Chromatin modifications and their function Cell 128 2007 693 705
    • (2007) Cell , vol.128 , pp. 693-705
    • Kouzarides, T.1
  • 12
    • 80054914428 scopus 로고    scopus 로고
    • Purification and assay protocols for obtaining highly active Jumonji C demethylases
    • S. Krishnan, E. Collazo, P.A. Ortiz-Tello, and R.C. Trievel Purification and assay protocols for obtaining highly active Jumonji C demethylases Analytical Biochemistry 420 2012 48 53
    • (2012) Analytical Biochemistry , vol.420 , pp. 48-53
    • Krishnan, S.1    Collazo, E.2    Ortiz-Tello, P.A.3    Trievel, R.C.4
  • 14
    • 65549095078 scopus 로고    scopus 로고
    • Histone H3 lysine 36 dimethylation (H3K36me2) is sufficient to recruit the Rpd3s histone deacetylase complex and to repress spurious transcription
    • B. Li, J. Jackson, M.D. Simon, B. Fleharty, M. Gogol, and C. Seidel Histone H3 lysine 36 dimethylation (H3K36me2) is sufficient to recruit the Rpd3s histone deacetylase complex and to repress spurious transcription The Journal of Biological Chemistry 284 2009 7970 7976
    • (2009) The Journal of Biological Chemistry , vol.284 , pp. 7970-7976
    • Li, B.1    Jackson, J.2    Simon, M.D.3    Fleharty, B.4    Gogol, M.5    Seidel, C.6
  • 17
    • 0033039285 scopus 로고    scopus 로고
    • Preparation of nucleosome core particle from recombinant histones
    • K. Luger, T.J. Rechsteiner, and T.J. Richmond Preparation of nucleosome core particle from recombinant histones Methods in Enzymology 304 1999 3 19
    • (1999) Methods in Enzymology , vol.304 , pp. 3-19
    • Luger, K.1    Rechsteiner, T.J.2    Richmond, T.J.3
  • 18
    • 70349952171 scopus 로고    scopus 로고
    • Role of the polycomb protein EED in the propagation of repressive histone marks
    • R. Margueron, N. Justin, K. Ohno, M.L. Sharpe, J. Son, and W.J. Drury 3rd Role of the polycomb protein EED in the propagation of repressive histone marks Nature 461 2009 762 767
    • (2009) Nature , vol.461 , pp. 762-767
    • Margueron, R.1    Justin, N.2    Ohno, K.3    Sharpe, M.L.4    Son, J.5    Drury III, W.J.6
  • 21
    • 84856144675 scopus 로고    scopus 로고
    • Quantitative assessment of protein interaction with methyl-lysine analogues by hybrid computational and experimental approaches
    • D. Seeliger, S. Soeroes, R. Klingberg, D. Schwarzer, H. Grubmuller, and W. Fischle Quantitative assessment of protein interaction with methyl-lysine analogues by hybrid computational and experimental approaches ACS Chemical Biology 7 2012 150 154
    • (2012) ACS Chemical Biology , vol.7 , pp. 150-154
    • Seeliger, D.1    Soeroes, S.2    Klingberg, R.3    Schwarzer, D.4    Grubmuller, H.5    Fischle, W.6
  • 22
    • 0038047672 scopus 로고    scopus 로고
    • A native peptide ligation strategy for deciphering nucleosomal histone modifications
    • M.A. Shogren-Knaak, C.J. Fry, and C.L. Peterson A native peptide ligation strategy for deciphering nucleosomal histone modifications The Journal of Biological Chemistry 278 2003 15744 15748
    • (2003) The Journal of Biological Chemistry , vol.278 , pp. 15744-15748
    • Shogren-Knaak, M.A.1    Fry, C.J.2    Peterson, C.L.3
  • 23
    • 77950791132 scopus 로고    scopus 로고
    • Installation of site-specific methylation into histones using methyl lysine analogs
    • M.D. Simon Installation of site-specific methylation into histones using methyl lysine analogs Current Protocols in Molecular Biology 2010 1 10 Chapter 21 Unit 21.18
    • (2010) Current Protocols in Molecular Biology , pp. 1-10
    • Simon, M.D.1
  • 24
    • 33847386172 scopus 로고    scopus 로고
    • The site-specific installation of methyl-lysine analogs into recombinant histones
    • M.D. Simon, F. Chu, L.R. Racki, C.C. de la Cruz, A.L. Burlingame, and B. Panning The site-specific installation of methyl-lysine analogs into recombinant histones Cell 128 2007 1003 1012
    • (2007) Cell , vol.128 , pp. 1003-1012
    • Simon, M.D.1    Chu, F.2    Racki, L.R.3    De La Cruz, C.C.4    Burlingame, A.L.5    Panning, B.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.