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Volumn 12, Issue 8, 2013, Pages 2048-2059

Discovery of histone modification crosstalk networks by stable isotope labeling of amino acids in cell culture mass spectrometry (SILAC MS)

Author keywords

[No Author keywords available]

Indexed keywords

HISTONE; AMINO ACID; PEPTIDE; SACCHAROMYCES CEREVISIAE PROTEIN;

EID: 84881114088     PISSN: 15359476     EISSN: 15359484     Source Type: Journal    
DOI: 10.1074/mcp.M112.026716     Document Type: Article
Times cited : (32)

References (63)
  • 1
    • 33847076849 scopus 로고    scopus 로고
    • Chromatin modifications and their function
    • Kouzarides, T. (2007) Chromatin Modifications and Their Function. Cell 128, 693-705
    • (2007) Cell , vol.128 , pp. 693-705
    • Kouzarides, T.1
  • 2
    • 35848951163 scopus 로고    scopus 로고
    • Covalent modifications of histones during development and disease pathogenesis
    • Bhaumik, S. R., Smith, E., and Shilatifard, A. (2007) Covalent modifications of histones during development and disease pathogenesis. Nat. Struct. Mol. Biol. 14, 1008-1016
    • (2007) Nat. Struct. Mol. Biol. , vol.14 , pp. 1008-1016
    • Bhaumik, S.R.1    Smith, E.2    Shilatifard, A.3
  • 3
    • 79952534189 scopus 로고    scopus 로고
    • Regulation of chromatin by histone modifications
    • Bannister, A. J., and Kouzarides, T. (2011) Regulation of chromatin by histone modifications. Cell Res. 21, 381-395
    • (2011) Cell Res. , vol.21 , pp. 381-395
    • Bannister, A.J.1    Kouzarides, T.2
  • 4
    • 0036312462 scopus 로고    scopus 로고
    • Trans-tail histone modifications: Wedge or bridge? Nat
    • Henry, K. W., and Berger, S. L. (2002) Trans-tail histone modifications: wedge or bridge? Nat. Struct. Mol. Biol. 9, 565-566
    • (2002) Struct. Mol. Biol. , vol.9 , pp. 565-566
    • Henry, K.W.1    Berger, S.L.2
  • 5
    • 77957369358 scopus 로고    scopus 로고
    • Histone H2B ubiquitination and beyond: Regulation of nucleosome stability, chromatin dynamics and the trans-histone H3 methylation
    • Chandrasekharan, M. B., Huang, F., and Sun, Z. W. (2010) Histone H2B ubiquitination and beyond: Regulation of nucleosome stability, chromatin dynamics and the trans-histone H3 methylation. Epigenetics 5, 460-468
    • (2010) Epigenetics , vol.5 , pp. 460-468
    • Chandrasekharan, M.B.1    Huang, F.2    Sun, Z.W.3
  • 6
    • 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
  • 8
    • 33645804789 scopus 로고    scopus 로고
    • Methylation of histone H3 mediates the association of the NuA3 histone acetyltransferase with chromatin
    • Martin, D. G., Grimes, D. E., Baetz, K., and Howe, L. (2006) Methylation of Histone H3 Mediates the Association of the NuA3 Histone Acetyltransferase with Chromatin. Mol. Cell. Biol. 26, 3018-3028
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 3018-3028
    • Martin, D.G.1    Grimes, D.E.2    Baetz, K.3    Howe, L.4
  • 9
    • 27644588839 scopus 로고    scopus 로고
    • A histone code in meiosis: The histone kinase, NHK-1, is required for proper chromosomal architecture in Drosophila oocytes
    • Ivanovska, I., Khandan, T., Ito, T., and Orr-Weaver, T. L. (2005) A histone code in meiosis: the histone kinase, NHK-1, is required for proper chromosomal architecture in Drosophila oocytes. Genes Develop. 19, 2571-2582
    • (2005) Genes Develop. , vol.19 , pp. 2571-2582
    • Ivanovska, I.1    Khandan, T.2    Ito, T.3    Orr-Weaver, T.L.4
  • 10
    • 34547949573 scopus 로고    scopus 로고
    • A charge-based interaction between histone H4 and Dot1 is required for H3K79 methylation and telomere silencing: Identification of a new trans-histone pathway
    • Fingerman, I. M., Li, H.-C., and Briggs, S. D. (2007) A charge-based interaction between histone H4 and Dot1 is required for H3K79 methylation and telomere silencing: identification of a new trans-histone pathway. Genes Develop. 21, 2018-2029
    • (2007) Genes Develop. , vol.21 , pp. 2018-2029
    • Fingerman, I.M.1    Li, H.-C.2    Briggs, S.D.3
  • 11
    • 58149151514 scopus 로고    scopus 로고
    • Controlling histone methylation via trans-histone pathways
    • Fingerman, I. M., Du, H. N., and Briggs, S. D. (2008) Controlling histone methylation via trans-histone pathways. Epigenetics 3, 237-242
    • (2008) Epigenetics , vol.3 , pp. 237-242
    • Fingerman, I.M.1    Du, H.N.2    Briggs, S.D.3
  • 12
    • 21744433162 scopus 로고    scopus 로고
    • Ubp10/Dot4p regulates the persistence of ubiquitinated histone H2B: Distinct roles in telomeric silencing and general chromatin
    • Gardner, R. G., Nelson, Z. W., and Gottschling, D. E. (2005) Ubp10/Dot4p Regulates the Persistence of Ubiquitinated Histone H2B: Distinct Roles in Telomeric Silencing and General Chromatin. Mol. Cell. Biol. 25, 6123-6139
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 6123-6139
    • Gardner, R.G.1    Nelson, Z.W.2    Gottschling, D.E.3
  • 14
    • 22544461653 scopus 로고    scopus 로고
    • Histone H2B ubiquitylation controls processive methylation but not monomethylation by Dot1 and Se t1
    • Shahbazian, M. D., Zhang, K., and Grunstein, M. (2005) Histone H2B ubiquitylation controls processive methylation but not monomethylation by Dot1 and Se t1. Mol. Cell. 19, 271-277
    • (2005) Mol. Cell. , vol.19 , pp. 271-277
    • Shahbazian, M.D.1    Zhang, K.2    Grunstein, M.3
  • 15
    • 0037144393 scopus 로고    scopus 로고
    • Ubiquitination of histone H2B by Rad6 is required for efficient Dot1-mediated methylation of histone H3 lysine
    • Ng, H. H., Xu, R. M., Zhang, Y., and Struhl, K. (2002) Ubiquitination of histone H2B by Rad6 is required for efficient Dot1-mediated methylation of histone H3 lysine J. Biol. Chem. 277, 34655-34657
    • (2002) J. Biol. Chem. , vol.277 , pp. 34655-34657
    • Ng, H.H.1    Xu, R.M.2    Zhang, Y.3    Struhl, K.4
  • 16
    • 55549101555 scopus 로고    scopus 로고
    • Ubiquitylation of the COMPASS component Swd2 links H2B ubiquitylation to H3K4 trimethylation
    • Vitaliano-Prunier, A., Menant, A., Hobeika, M., Géli, V., Gwizdek, C., and Dargemont, C. (2008) Ubiquitylation of the COMPASS component Swd2 links H2B ubiquitylation to H3K4 trimethylation. Nat. Cell. Biol. 10, 1365-1371
    • (2008) Nat. Cell. Biol. , vol.10 , pp. 1365-1371
    • Vitaliano-Prunier, A.1    Menant, A.2    Hobeika, M.3    Géli, V.4    Gwizdek, C.5    Dargemont, C.6
  • 19
    • 0037019333 scopus 로고    scopus 로고
    • Ubiquitination of histone H2B regulates H3 methylation and gene silencing in yeast
    • Sun, Z. W., and Allis, C. D. (2002) Ubiquitination of histone H2B regulates H3 methylation and gene silencing in yeast. Nature 418, 104-108
    • (2002) Nature , vol.418 , pp. 104-108
    • Sun, Z.W.1    Allis, C.D.2
  • 20
    • 79961047028 scopus 로고    scopus 로고
    • H2B ubiquitylation and H3 lysine 4 methylation prevent ectopic silencing of euchromatic loci important for the cellular response to heat
    • Leung, A., Cajigas, I., Jia, P., Ezhkova, E., Brickner, J. H., Zhao, Z., Geng, F., and Tansey, W. P. Histone H2B ubiquitylation and H3 lysine 4 methylation prevent ectopic silencing of euchromatic loci important for the cellular response to heat. Mol. Biol. Cell 22, 2741-2753
    • Mol. Biol. Cell , vol.22 , pp. 2741-2753
    • Leung, A.1    Cajigas, I.2    Jia, P.3    Ezhkova, E.4    Brickner, J.H.5    Zhao, Z.6    Geng, F.7    Histone, P.T.W.8
  • 21
    • 79959256141 scopus 로고    scopus 로고
    • Decoding the trans-histone crosstalk: Methods to analyze H2B ubiquitination, H3 methylation and their regulatory factors
    • Chandrasekharan, M. B., Huang, F., and Sun, Z. W. (2011) Decoding the trans-histone crosstalk: Methods to analyze H2B ubiquitination, H3 methylation and their regulatory factors. Methods 54, 304-314
    • (2011) Methods , vol.54 , pp. 304-314
    • Chandrasekharan, M.B.1    Huang, F.2    Sun, Z.W.3
  • 23
    • 34547949573 scopus 로고    scopus 로고
    • A charge-based interaction between histone H4 and Dot1 is required for H3K79 methylation and telomere silencing: Identification of a new trans-histone pathway
    • Fingerman, I. M., Li, H. C., and Briggs, S. D. (2007) A charge-based interaction between histone H4 and Dot1 is required for H3K79 methylation and telomere silencing: identification of a new trans-histone pathway. Genes Dev. 21, 2018-2029
    • (2007) Genes Dev. , vol.21 , pp. 2018-2029
    • Fingerman, I.M.1    Li, H.C.2    Briggs, S.D.3
  • 25
    • 77954371390 scopus 로고    scopus 로고
    • Novel trans-Tail Regulation of H2B Ubiquitylation and H3K4 Methylation by the N Terminus of Histone H2A
    • Zheng, S., Wyrick, J. J., and Reese, J. C. (2010) Novel trans-Tail Regulation of H2B Ubiquitylation and H3K4 Methylation by the N Terminus of Histone H2A. Mol. Cell. Biol. 30, 3635-3645
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 3635-3645
    • Zheng, S.1    Wyrick, J.J.2    Reese, J.C.3
  • 26
    • 34247172850 scopus 로고    scopus 로고
    • Histone modifications in response to DNA damage
    • Altaf, M., Saksouk, N., and Côté, J. (2007) Histone modifications in response to DNA damage. Mutat. Res. 618, 81-90
    • (2007) Mutat. Res. , vol.618 , pp. 81-90
    • Altaf, M.1    Saksouk, N.2    Côté, J.3
  • 27
    • 0033638105 scopus 로고    scopus 로고
    • Phosphorylation of serine 10 in histone H3 Is functionally linked in vitro and in vivo to Gcn5-mediated acetylation at lysine
    • Lo, W. S., Trievel, R. C., Rojas, J. R., Duggan, L., Hsu, J. Y., Allis, C. D., Marmorstein, R., and Berger, S. L. (2000) Phosphorylation of serine 10 in histone H3 Is functionally linked in vitro and in vivo to Gcn5-mediated acetylation at lysine Mol. Cell 5, 917-926
    • (2000) Mol. Cell , vol.5 , pp. 917-926
    • Lo, W.S.1    Trievel, R.C.2    Rojas, J.R.3    Duggan, L.4    Hsu, J.Y.5    Allis, C.D.6    Marmorstein, R.7    Berger, S.L.8
  • 28
    • 70149112313 scopus 로고    scopus 로고
    • Histone crosstalk between H3S10ph and H4K16ac generates a histone code that mediates transcription elongation
    • Zippo, A., Serafini, R., Rocchigiani, M., Pennacchini, S., Krepelova, A., and Oliviero, S. (2009) Histone crosstalk between H3S10ph and H4K16ac generates a histone code that mediates transcription elongation. Cell 138, 1122-1136
    • (2009) Cell , vol.138 , pp. 1122-1136
    • Zippo, A.1    Serafini, R.2    Rocchigiani, M.3    Pennacchini, S.4    Krepelova, A.5    Oliviero, S.6
  • 29
    • 33748163064 scopus 로고    scopus 로고
    • Proline isomerization of histone H3 regulates lysine methylation and gene expression
    • Nelson, C. J., Santos-Rosa, H., and Kouzarides, T. (2006) Proline isomerization of histone H3 regulates lysine methylation and gene expression. Cell 126, 905-916
    • (2006) Cell , vol.126 , pp. 905-916
    • Nelson, C.J.1    Santos-Rosa, H.2    Kouzarides, T.3
  • 30
    • 33745520486 scopus 로고    scopus 로고
    • The sirtuins hst3 and Hst4p preserve genome integrity by controlling histone h3 lysine 56 deacetylation
    • Celic, I., Masumoto, H., Griffith, W. P., Meluh, P., Cotter, R. J., Boeke, J. D., and Verreault, A. (2006) The sirtuins hst3 and Hst4p preserve genome integrity by controlling histone h3 lysine 56 deacetylation. Curr. Biol. 16, 1280-1289
    • (2006) Curr. Biol. , vol.16 , pp. 1280-1289
    • Celic, I.1    Masumoto, H.2    Griffith, W.P.3    Meluh, P.4    Cotter, R.J.5    Boeke, J.D.6    Verreault, A.7
  • 31
    • 33745496607 scopus 로고    scopus 로고
    • Cell cycle and checkpoint regulation of histone H3 K56 acetylation by Hst3 and Hs t4
    • Maas, N. L., Miller, K. M., DeFazio, L. G., and Toczyski, D. P. (2006) Cell cycle and checkpoint regulation of histone H3 K56 acetylation by Hst3 and Hs t4. Mol Cell 23, 109-119
    • (2006) Mol Cell , vol.23 , pp. 109-119
    • Maas, N.L.1    Miller, K.M.2    Defazio, L.G.3    Toczyski, D.P.4
  • 32
    • 22444448143 scopus 로고    scopus 로고
    • A role for cell-cycle-regulated histone H3 lysine 56 acetylation in the DNA damage response
    • Masumoto, H., Hawke, D., Kobayashi, R., and Verreault, A. (2005) A role for cell-cycle-regulated histone H3 lysine 56 acetylation in the DNA damage response. Nature 436, 294-298
    • (2005) Nature , vol.436 , pp. 294-298
    • Masumoto, H.1    Hawke, D.2    Kobayashi, R.3    Verreault, A.4
  • 33
    • 1242342240 scopus 로고    scopus 로고
    • Histone H3.3 is enriched in covalent modifications associated with active chromatin
    • McKittrick, E., Gafken, P. R., Ahmad, K., and Henikoff, S. (2004) Histone H3.3 is enriched in covalent modifications associated with active chromatin. Proc. Natl. Acad. Sci. U.S.A. 101, 1525-1530
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 1525-1530
    • McKittrick, E.1    Gafken, P.R.2    Ahmad, K.3    Henikoff, S.4
  • 34
    • 33846023720 scopus 로고    scopus 로고
    • Rtt109 is required for proper H3K56 acetylation: A chromatin mark associated with the elongating RNA polymerase III
    • Schneider, J., Bajwa, P., Johnson, F. C., Bhaumik, S. R., and Shilatifard, A. (2006) Rtt109 is required for proper H3K56 acetylation: A chromatin mark associated with the elongating RNA polymerase III. J. Biol. Chem. 281, 37270-37274
    • (2006) J. Biol. Chem. , vol.281 , pp. 37270-37274
    • Schneider, J.1    Bajwa, P.2    Johnson, F.C.3    Bhaumik, S.R.4    Shilatifard, A.5
  • 35
    • 0037077178 scopus 로고    scopus 로고
    • Dot1p modulates silencing in yeast by methylation of the nucleosome core
    • van Leeuwen, F., Gafken, P. R., and Gottschling, D. E. (2002) Dot1p modulates silencing in yeast by methylation of the nucleosome core. Cell 109, 745-756
    • (2002) Cell , vol.109 , pp. 745-756
    • Van Leeuwen, F.1    Gafken, P.R.2    Gottschling, D.E.3
  • 36
    • 18844413266 scopus 로고    scopus 로고
    • Acetylation in histone H3 globular domain regulates gene expression in yeast
    • Xu, F., Zhang, K., and Grunstein, M. (2005) Acetylation in histone H3 globular domain regulates gene expression in yeast. Cell 121, 375-385
    • (2005) Cell , vol.121 , pp. 375-385
    • Xu, F.1    Zhang, K.2    Grunstein, M.3
  • 38
    • 34347258162 scopus 로고    scopus 로고
    • The Rtt109-Vps75 histone acetyltransferase complex acetylates non-nucleosomal histone H3
    • Han, J., Zhou, H., Li, Z., Xu, R. M., and Zhang, Z. (2007) The Rtt109-Vps75 histone acetyltransferase complex acetylates non-nucleosomal histone H3. J. Biol. Chem. 282, 14158-14164
    • (2007) J. Biol. Chem. , vol.282 , pp. 14158-14164
    • Han, J.1    Zhou, H.2    Li, Z.3    Xu, R.M.4    Zhang, Z.5
  • 39
    • 35348970835 scopus 로고    scopus 로고
    • Acetylation of lysine 56 of histone H3 catalyzed by RTT109 and regulated by ASF1 is required for replisome integrity
    • Han, J., Zhou, H., Li, Z., Xu, R. M., and Zhang, Z. (2007) Acetylation of lysine 56 of histone H3 catalyzed by RTT109 and regulated by ASF1 is required for replisome integrity. J. Biol. Chem. 282, 28587-28596
    • (2007) J. Biol. Chem. , vol.282 , pp. 28587-28596
    • Han, J.1    Zhou, H.2    Li, Z.3    Xu, R.M.4    Zhang, Z.5
  • 40
    • 33846818840 scopus 로고    scopus 로고
    • Yeast Rtt109 promotes genome stability by acetylating histone H3 on lysine
    • Driscoll, R., Hudson, A., and Jackson, S. P. (2007) Yeast Rtt109 promotes genome stability by acetylating histone H3 on lysine Science 315, 649-652
    • (2007) Science , vol.315 , pp. 649-652
    • Driscoll, R.1    Hudson, A.2    Jackson, S.P.3
  • 41
    • 33846796258 scopus 로고    scopus 로고
    • Rtt109 acetylates histone H3 lysine 56 and functions in DNA replication
    • Han, J., Zhou, H., Horazdovsky, B., Zhang, K., Xu, R. M., and Zhang, Z. (2007) Rtt109 acetylates histone H3 lysine 56 and functions in DNA replication. Science 315, 653-655
    • (2007) Science , vol.315 , pp. 653-655
    • Han, J.1    Zhou, H.2    Horazdovsky, B.3    Zhang, K.4    Xu, R.M.5    Zhang, Z.6
  • 44
    • 69249221533 scopus 로고    scopus 로고
    • Cell cycle-dependent deacetylation of telomeric histone H3 lysine K56 by human SIR T6
    • Michishita, E., McCord, R. A., Boxer, L. D., Barber, M. F., Hong, T., Gozani, O., and Chua, K. F. (2009) Cell cycle-dependent deacetylation of telomeric histone H3 lysine K56 by human SIR T6. Cell Cycle 8, 2664-2666
    • (2009) Cell Cycle , vol.8 , pp. 2664-2666
    • Michishita, E.1    McCord, R.A.2    Boxer, L.D.3    Barber, M.F.4    Hong, T.5    Gozani, O.6    Chua, K.F.7
  • 45
    • 48249148195 scopus 로고    scopus 로고
    • Acetylation in the globular core of histone H3 on lysine-56 promotes chromatin disassembly during transcriptional activation
    • Williams, S. K., Truong, D., and Tyler, J. K. (2008) Acetylation in the globular core of histone H3 on lysine-56 promotes chromatin disassembly during transcriptional activation. Proc. Natl. Acad. Sci. U.S.A. 105, 9000-9005
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 9000-9005
    • Williams, S.K.1    Truong, D.2    Tyler, J.K.3
  • 47
    • 34748909429 scopus 로고    scopus 로고
    • Sir2 deacetylates histone H3 lysine 56 to regulate telomeric heterochromatin structure in yeast
    • Xu, F., Zhang, Q., Zhang, K., Xie, W., and Grunstein, M. (2007) Sir2 deacetylates histone H3 lysine 56 to regulate telomeric heterochromatin structure in yeast. Mol. Cell 27, 890-900
    • (2007) Mol. Cell , vol.27 , pp. 890-900
    • Xu, F.1    Zhang, Q.2    Zhang, K.3    Xie, W.4    Grunstein, M.5
  • 48
    • 58149293992 scopus 로고    scopus 로고
    • HST3/HST4-dependent deacetylation of lysine 56 of histone H3 in silent chromatin
    • Yang, B., Miller, A., and Kirchmaier, A. L. (2008) HST3/HST4-dependent deacetylation of lysine 56 of histone H3 in silent chromatin. Mol. Biol. Cell 19, 4993-5005
    • (2008) Mol. Biol. Cell , vol.19 , pp. 4993-5005
    • Yang, B.1    Miller, A.2    Kirchmaier, A.L.3
  • 49
    • 33845329203 scopus 로고    scopus 로고
    • Functional and quantitative proteomics using SILAC
    • Mann, M. (2006) Functional and quantitative proteomics using SILAC. Nat. Rev. Mol. Cell Biol. 7, 952-958
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 952-958
    • Mann, M.1
  • 50
    • 0036583926 scopus 로고    scopus 로고
    • Stable Isotope Labeling by Amino Acids in Cell Culture, SILAC, as a Simple and Accurate Approach to Expression Proteomics
    • Ong, S.-E., Blagoev, B., Kratchmarova, I., Kristensen, D. B., Steen, H., Pandey, A., and Mann, M. (2002) Stable Isotope Labeling by Amino Acids in Cell Culture, SILAC, as a Simple and Accurate Approach to Expression Proteomics. Mol. Cell. Proteomics 1, 376-386
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 376-386
    • Ong, S.-E.1    Blagoev, B.2    Kratchmarova, I.3    Kristensen, D.B.4    Steen, H.5    Pandey, A.6    Mann, M.7
  • 53
    • 79960281535 scopus 로고    scopus 로고
    • SILAC-based proteomic analysis to dissect the "histone modification signature" of human breast cancer cells
    • Cuomo, A., Moretti, S., Minucci, S., and Bonaldi, T. (2011) SILAC-based proteomic analysis to dissect the "histone modification signature" of human breast cancer cells. Amino Acids 41, 387-399
    • (2011) Amino Acids , vol.41 , pp. 387-399
    • Cuomo, A.1    Moretti, S.2    Minucci, S.3    Bonaldi, T.4
  • 54
    • 0033826256 scopus 로고    scopus 로고
    • Type B histone acetyltransferase Hat1p participates in telomeric silencing
    • Kelly, T. J., Qin, S., Gottschling, D. E., and Parthun, M. R. (2000) Type B histone acetyltransferase Hat1p participates in telomeric silencing. Mol. Cell. Biol. 20, 7051-7058
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 7051-7058
    • Kelly, T.J.1    Qin, S.2    Gottschling, D.E.3    Parthun, M.R.4
  • 55
    • 25144455418 scopus 로고    scopus 로고
    • H2B (Ser10) phosphorylation is induced during apoptosis and meiosis in S
    • Ahn, S. H., Henderson, K. A., Keeney, S., and Allis, C. D. (2005) H2B (Ser10) phosphorylation is induced during apoptosis and meiosis in S. cerevisiae. Cell Cycle 4, 780-783
    • (2005) Cerevisiae. Cell Cycle , vol.4 , pp. 780-783
    • Ahn, S.H.1    Henderson, K.A.2    Keeney, S.3    Allis, C.D.4
  • 56
    • 33847028358 scopus 로고    scopus 로고
    • Quantitative profiling of histone post-translational modifications by stable isotope labeling
    • Knapp, A. R., Ren, C., Su, X., Lucas, D. M., Byrd, J. C., Freitas, M. A., and Parthun, M. R. (2007) Quantitative profiling of histone post-translational modifications by stable isotope labeling. Methods 41, 312-319
    • (2007) Methods , vol.41 , pp. 312-319
    • Knapp, A.R.1    Ren, C.2    Su, X.3    Lucas, D.M.4    Byrd, J.C.5    Freitas, M.A.6    Parthun, M.R.7
  • 57
    • 33847630405 scopus 로고    scopus 로고
    • Target-decoy search strategy for increased confidence in large-scale protein identifications by mass spectrometry
    • Elias, J. E., and Gygi, S. P. (2007) Target-decoy search strategy for increased confidence in large-scale protein identifications by mass spectrometry. Nat. Meth. 4, 207-214
    • (2007) Nat. Meth. , vol.4 , pp. 207-214
    • Elias, J.E.1    Gygi, S.P.2
  • 60
    • 26244462329 scopus 로고    scopus 로고
    • Robust linear regression using Theil's method
    • Glaister, P. (2005) Robust linear regression using Theil's method. J. Chem. Ed. 82, 1472
    • (2005) J. Chem. Ed. , vol.82 , pp. 1472
    • Glaister, P.1
  • 61
    • 70449624833 scopus 로고    scopus 로고
    • Unambiguous determination of isobaric histone modifications by reversed-phase retention time and high-mass accuracy
    • Yang, L., Tu, S., Ren, C., Bulloch, E. M. M., Liao, C.-L., Tsai, M.-D., and Freitas, M. A. (2010) Unambiguous determination of isobaric histone modifications by reversed-phase retention time and high-mass accuracy. Anal. Biochem. 396, 13-22
    • (2010) Anal. Biochem. , vol.396 , pp. 13-22
    • Yang, L.1    Tu, S.2    Ren, C.3    Bulloch, E.M.M.4    Liao, C.-L.5    Tsai, M.-D.6    Freitas, M.A.7
  • 62
    • 40849106789 scopus 로고    scopus 로고
    • Histone ubiquitination: Triggering gene activity
    • Weake, V. M., and Workman, J. L. (2008) Histone Ubiquitination: Triggering Gene Activity. Mol. Cell 29, 653-663
    • (2008) Mol. Cell , vol.29 , pp. 653-663
    • Weake, V.M.1    Workman, J.L.2
  • 63
    • 33746324216 scopus 로고    scopus 로고
    • Chromatin modifications by methylation and ubiquitination: Implications in the regulation of gene expression
    • Shilatifard, A. (2006) Chromatin modifications by methylation and ubiquitination: implications in the regulation of gene expression. Ann. Rev. Biochem. 75, 243-269
    • (2006) Ann. Rev. Biochem. , vol.75 , pp. 243-269
    • Shilatifard, A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.