메뉴 건너뛰기




Volumn 13, Issue 7, 2014, Pages 1724-1740

Modulation of the chromatin phosphoproteome by the haspin protein kinase

(18)  Maiolica, Alessio a   De Medina Redondo, Maria b   Schoof, Erwin M c   Chaikuad, Apirat d   Villa, Fabrizio e   Gatti, Marco f   Jeganathan, Siva g   Lou, Hua Jane h   Novy, Karel a   Hauri, Simon a   Toprak, Umut H b   Herzog, Franz i   Meraldi, Patrick b   Penengo, Lorenza f   Turk, Benjamin E h   Knapp, Stefan d   Linding, Rune c   Aebersoldab, Ruedi j  


Author keywords

[No Author keywords available]

Indexed keywords

CHROMATIN PHOSPHOPROTEOME; HASPIN PROTEIN KINASE; HISTONE H3; PHOSPHOPROTEIN; PROTEIN KINASE; PROTEOME; THREONINE; UNCLASSIFIED DRUG; AURKB PROTEIN, HUMAN; AURORA B KINASE; CHROMATIN; GSG2 PROTEIN, HUMAN; HISTONE; NUCLEAR PROTEIN; PROTEIN SERINE THREONINE KINASE; RNA BINDING PROTEIN; SERINE ARGININE RICH SPLICING FACTOR; SIGNAL PEPTIDE;

EID: 84904107780     PISSN: 15359476     EISSN: 15359484     Source Type: Journal    
DOI: 10.1074/mcp.M113.034819     Document Type: Article
Times cited : (41)

References (86)
  • 1
    • 0037032835 scopus 로고    scopus 로고
    • The protein kinase complement of the human genome
    • Manning, G. (2002) The protein kinase complement of the human genome. Science 298, 1912-1934
    • (2002) Science , vol.298 , pp. 1912-1934
    • Manning, G.1
  • 2
    • 34250878954 scopus 로고    scopus 로고
    • Mechanisms of specificity in protein phosphorylation
    • DOI 10.1038/nrm2203, PII NRM2203
    • Ubersax, J. A., and Ferrell, J. E. (2007) Mechanisms of specificity in protein phosphorylation. Nat. Rev. Mol. Cell. Biol. 8, 530-541 (Pubitemid 46985383)
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , Issue.7 , pp. 530-541
    • Ubersax, J.A.1    Ferrell Jr., J.E.2
  • 4
    • 0034924175 scopus 로고    scopus 로고
    • Haspin-like proteins: A new family of evolutionarily conserved putative eukaryotic protein kinases
    • Higgins, J. M. (2001) Haspin-like proteins: a new family of evolutionarily conserved putative eukaryotic protein kinases. Protein Sci. 10, 1677-1684
    • (2001) Protein Sci. , vol.10 , pp. 1677-1684
    • Higgins, J.M.1
  • 7
    • 13844252061 scopus 로고    scopus 로고
    • The kinase haspin is required for mitotic histone H3 Thr 3 phosphorylation and normal metaphase chromosome alignment
    • Dai, J. J., Sultan, S. S., Taylor, S. S. S., and Higgins, J. M. G. J. (2005) The kinase haspin is required for mitotic histone H3 Thr 3 phosphorylation and normal metaphase chromosome alignment. Gene Dev. 19, 472-488
    • (2005) Gene Dev. , vol.19 , pp. 472-488
    • Dai, J.J.1    Sultan, S.S.2    Taylor, S.S.S.3    Higgins, J.M.G.J.4
  • 8
    • 33845783921 scopus 로고    scopus 로고
    • Chromosomal Enrichment and Activation of the Aurora B Pathway Are Coupled to Spatially Regulate Spindle Assembly
    • DOI 10.1016/j.devcel.2006.11.001, PII S1534580706005065
    • Kelly, A. E., Sampath, S. C., Maniar, T. A., Woo, E. M., Chait, B. T., and Funabiki, H. (2007) Chromosomal enrichment and activation of the Aurora B pathway are coupled to spatially regulate spindle assembly. Dev. Cell 12, 31-43 (Pubitemid 46002596)
    • (2007) Developmental Cell , vol.12 , Issue.1 , pp. 31-43
    • Kelly, A.E.1    Sampath, S.C.2    Maniar, T.A.3    Woo, E.M.4    Chait, B.T.5    Funabiki, H.6
  • 10
    • 77957731584 scopus 로고    scopus 로고
    • Two histone marks establish the inner centromere and chromosome bi-orientation
    • Yamagishi, Y., Honda, T., Tanno, Y., and Watanabe, Y. (2010) Two histone marks establish the inner centromere and chromosome bi-orientation. Science 330, 239-243
    • (2010) Science , vol.330 , pp. 239-243
    • Yamagishi, Y.1    Honda, T.2    Tanno, Y.3    Watanabe, Y.4
  • 11
    • 84869139587 scopus 로고    scopus 로고
    • A small-molecule inhibitor of Haspin alters the kinetochore functions of Aurora B
    • De Antoni, A., Maffini, S., Knapp, S., Musacchio, A., and Santaguida, S. (2012) A small-molecule inhibitor of Haspin alters the kinetochore functions of Aurora B. J. Cell Biol. 199, 269-284
    • (2012) J. Cell Biol. , vol.199 , pp. 269-284
    • De Antoni, A.1    Maffini, S.2    Knapp, S.3    Musacchio, A.4    Santaguida, S.5
  • 14
    • 0017752811 scopus 로고
    • Role of nonhistone proteins in metaphase chromosome structure
    • Adolph, K. W., Cheng, S. M., and Laemmli, U. K. (1977) Role of nonhistone proteins in metaphase chromosome structure. Cell 12, 805-816 (Pubitemid 8224419)
    • (1977) Cell , vol.12 , Issue.3 , pp. 805-816
    • Adolph, K.W.1    Cheng, S.M.2    Laemmli, U.K.3
  • 15
    • 37149019996 scopus 로고    scopus 로고
    • The CENP-A NAC/CAD kinetochore complex controls chromosome congression and spindle bipolarity
    • The CENP-A NAC/CAD
    • The CENP-A NAC/CAD (2007) The CENP-A NAC/CAD kinetochore complex controls chromosome congression and spindle bipolarity. EMBO J. 26, 5033-5047
    • (2007) EMBO J. , vol.26 , pp. 5033-5047
  • 16
    • 84863793933 scopus 로고    scopus 로고
    • A novel ubiquitin mark at the N-terminal tail of histone H2As targeted by RNF168 ubiquitin ligase
    • Gatti, M., Pinato, S., Maspero, E., Soffientini, P., Polo, S., and Penengo, L. (2012) A novel ubiquitin mark at the N-terminal tail of histone H2As targeted by RNF168 ubiquitin ligase. Cell Cycle 11, 2538-2544
    • (2012) Cell Cycle , vol.11 , pp. 2538-2544
    • Gatti, M.1    Pinato, S.2    Maspero, E.3    Soffientini, P.4    Polo, S.5    Penengo, L.6
  • 19
    • 84857047339 scopus 로고    scopus 로고
    • PhosphoSitePlus: A comprehensive resource for investigating the structure and function of experimentally determined post-translational modifications in man and mouse
    • Hornbeck, P. V., Kornhauser, J. M., Tkachev, S., Zhang, B., Skrzypek, E., Murray, B., Latham, V., and Sullivan, M. (2012) PhosphoSitePlus: a comprehensive resource for investigating the structure and function of experimentally determined post-translational modifications in man and mouse. Nucleic Acids Res. 40, D261-D270
    • (2012) Nucleic Acids Res. , vol.40
    • Hornbeck, P.V.1    Kornhauser, J.M.2    Tkachev, S.3    Zhang, B.4    Skrzypek, E.5    Murray, B.6    Latham, V.7    Sullivan, M.8
  • 21
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4
    • Collaborative Computational Project, Number 4 (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr. 50, 760-763
    • (1994) Acta Crystallogr. , vol.50 , pp. 760-763
  • 26
    • 77956028057 scopus 로고    scopus 로고
    • Quantitative analysis of protein phosphorylation on a system-wide scale by mass spectrometry-based proteomics
    • Bodenmiller, B., and Aebersold, R. (2010) Quantitative analysis of protein phosphorylation on a system-wide scale by mass spectrometry-based proteomics. Methods Enzymol. 470, 317-334
    • (2010) Methods Enzymol. , vol.470 , pp. 317-334
    • Bodenmiller, B.1    Aebersold, R.2
  • 27
    • 33746930864 scopus 로고    scopus 로고
    • A uniform proteomics MS/MS analysis platform utilizing open XML file formats
    • Keller, A., Eng, J., Zhang, N., Li, X.-J., and Aebersold, R. (2005) A uniform proteomics MS/MS analysis platform utilizing open XML file formats. Mol. Sys. Biol. 1, 2005.0017
    • (2005) Mol. Sys. Biol. , vol.1
    • Keller, A.1    Eng, J.2    Zhang, N.3    Li, X.-J.4    Aebersold, R.5
  • 29
    • 33947366516 scopus 로고    scopus 로고
    • Development and validation of a spectral library searching method for peptide identification from MS/MS
    • DOI 10.1002/pmic.200600625
    • Lam, H., Deutsch, E. W., Eddes, J. S., Eng, J. K., King, N., Stein, S. E., and Aebersold, R. (2007) Development and validation of a spectral library searching method for peptide identification from MS/MS. Proteomics 7, 655-667 (Pubitemid 46453760)
    • (2007) Proteomics , vol.7 , Issue.5 , pp. 655-667
    • Lam, H.1    Deutsch, E.W.2    Eddes, J.S.3    Eng, J.K.4    King, N.5    Stein, S.E.6    Aebersold, R.7
  • 31
    • 4544341015 scopus 로고    scopus 로고
    • Linear models and empirical bayes methods for assessing differential expression in microarray experiments
    • Smyth, G. K. (2004) Linear models and empirical bayes methods for assessing differential expression in microarray experiments. Stat. Appl. Genet. Mol. Biol. 3, 1544-6115
    • (2004) Stat. Appl. Genet. Mol. Biol. , vol.3 , pp. 1544-6115
    • Smyth, G.K.1
  • 32
    • 60849139395 scopus 로고    scopus 로고
    • GOrilla: A tool for discovery and visualization of enriched GO terms in ranked gene lists
    • Eden, E., Navon, R., Steinfeld, I., Lipson, D., and Yakhini, Z. (2009) GOrilla: a tool for discovery and visualization of enriched GO terms in ranked gene lists. BMC Bioinformatics 10, 48
    • (2009) BMC Bioinformatics , vol.10 , pp. 48
    • Eden, E.1    Navon, R.2    Steinfeld, I.3    Lipson, D.4    Yakhini, Z.5
  • 34
    • 79551587720 scopus 로고    scopus 로고
    • Cytoscape 2.8: New features for data integration and network visualization
    • Smoot, M. E., Ono, K., Ruscheinski, J., Wang, P.-L., and Ideker, T. (2011) Cytoscape 2.8: new features for data integration and network visualization. Bioinformatics 27, 431-432
    • (2011) Bioinformatics , vol.27 , pp. 431-432
    • Smoot, M.E.1    Ono, K.2    Ruscheinski, J.3    Wang, P.-L.4    Ideker, T.5
  • 36
    • 79953062776 scopus 로고    scopus 로고
    • Abacus: A computational tool for extracting and pre-processing spectral count data for label-free quantitative proteomic analysis
    • Fermin, D., Basrur, V., Yocum, A. K., and Nesvizhskii, A. I. (2011) Abacus: a computational tool for extracting and pre-processing spectral count data for label-free quantitative proteomic analysis. Proteomics 11, 1340-1345
    • (2011) Proteomics , vol.11 , pp. 1340-1345
    • Fermin, D.1    Basrur, V.2    Yocum, A.K.3    Nesvizhskii, A.I.4
  • 38
    • 80052163881 scopus 로고    scopus 로고
    • A general framework for inhibitor resistance in protein kinases
    • Balzano, D., Santaguida, S., Musacchio, A., and Villa, F. (2011) A general framework for inhibitor resistance in protein kinases. Chem, Biol. 18, 966-975
    • (2011) Chem, Biol. , vol.18 , pp. 966-975
    • Balzano, D.1    Santaguida, S.2    Musacchio, A.3    Villa, F.4
  • 39
    • 77957725753 scopus 로고    scopus 로고
    • Survivin reads phosphorylated histone h3 threonine 3 to activate the mitotic kinase Aurora B
    • Kelly, A. E., Ghenoiu, C., Xue, J. Z., Zierhut, C., Kimura, H., and Funabiki, H. (2010) Survivin reads phosphorylated histone h3 threonine 3 to activate the mitotic kinase Aurora B. Science 330, 235-239
    • (2010) Science , vol.330 , pp. 235-239
    • Kelly, A.E.1    Ghenoiu, C.2    Xue, J.Z.3    Zierhut, C.4    Kimura, H.5    Funabiki, H.6
  • 40
    • 33847616949 scopus 로고    scopus 로고
    • Reproducible isolation of distinct, overlapping segments of the phosphoproteome
    • DOI 10.1038/nmeth1005, PII NMETH1005
    • Bodenmiller, B., Mueller, L. N., Mueller, M., Domon, B., and Aebersold, R. (2007) Reproducible isolation of distinct, overlapping segments of the phosphoproteome. Nat. Methods 4, 231-237 (Pubitemid 46358873)
    • (2007) Nature Methods , vol.4 , Issue.3 , pp. 231-237
    • Bodenmiller, B.1    Mueller, L.N.2    Mueller, M.3    Domon, B.4    Aebersold, R.5
  • 43
    • 34247333444 scopus 로고    scopus 로고
    • The spindle-assembly checkpoint in space and time
    • DOI 10.1038/nrm2163, PII NRM2163
    • Musacchio, A., and Salmon, E. D. (2007) The spindle-assembly checkpoint in space and time. Nature 8, 379-393 (Pubitemid 46643240)
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , Issue.5 , pp. 379-393
    • Musacchio, A.1    Salmon, E.D.2
  • 44
    • 37549071893 scopus 로고    scopus 로고
    • Molecular architecture of the kinetochore-microtubule interface
    • Cheeseman, I. M., and Desai, A. (2008) Molecular architecture of the kinetochore-microtubule interface. Nature 9, 33-46
    • (2008) Nature , vol.9 , pp. 33-46
    • Cheeseman, I.M.1    Desai, A.2
  • 46
    • 35848961668 scopus 로고    scopus 로고
    • How chromatin-binding modules interpret histone modifications: Lessons from professional pocket pickers
    • DOI 10.1038/nsmb1338, PII NSMB1338
    • Taverna, S. D., Li, H., Ruthenburg, A. J., Allis, C. D., and Patel, D. J. (2007) How chromatin-binding modules interpret histone modifications: lessons from professional pocket pickers. Nature Struct. Biol. 14, 1025-1040 (Pubitemid 350060344)
    • (2007) Nature Structural and Molecular Biology , vol.14 , Issue.11 , pp. 1025-1040
    • Taverna, S.D.1    Li, H.2    Ruthenburg, A.J.3    Allis, C.D.4    Patel, D.J.5
  • 47
    • 79959967141 scopus 로고    scopus 로고
    • Phosphorylation of H4 Ser 47 promotes HIRA-mediated nucleosome assembly
    • Kang, B., Pu, M., Hu, G., Wen, W., Dong, Z., Zhao, K., Stillman, B., and Zhang, Z. (2011) Phosphorylation of H4 Ser 47 promotes HIRA-mediated nucleosome assembly. Gene Dev. 25, 1359-1364
    • (2011) Gene Dev. , vol.25 , pp. 1359-1364
    • Kang, B.1    Pu, M.2    Hu, G.3    Wen, W.4    Dong, Z.5    Zhao, K.6    Stillman, B.7    Zhang, Z.8
  • 49
    • 84875699641 scopus 로고    scopus 로고
    • Kinase-substrate enrichment analysis provides insights into the heterogeneity of signaling pathway activation in leukemia cells
    • Casado, P., Rodriguez-Prados, J. C., Cosulich, S. C., Guichard, S., Vanhaesebroeck, B., Joel, S., and Cutillas, P. R. (2013) Kinase-substrate enrichment analysis provides insights into the heterogeneity of signaling pathway activation in leukemia cells. Sci. Signal. 6, rs6-rs6
    • (2013) Sci. Signal. , vol.6
    • Casado, P.1    Rodriguez-Prados, J.C.2    Cosulich, S.C.3    Guichard, S.4    Vanhaesebroeck, B.5    Joel, S.6    Cutillas, P.R.7
  • 52
    • 84878582352 scopus 로고    scopus 로고
    • Regulation of splicing by SR proteins and SR protein-specific kinases
    • Zhou, Z., and Fu, X.-D. (2013) Regulation of splicing by SR proteins and SR protein-specific kinases. Chromosoma 122, 191-207
    • (2013) Chromosoma , vol.122 , pp. 191-207
    • Zhou, Z.1    Fu, X.-D.2
  • 53
    • 52449095361 scopus 로고    scopus 로고
    • The RSK family of kinases: Emerging roles in cellular signalling
    • Anjum, R., and Blenis, J. (2008) The RSK family of kinases: emerging roles in cellular signalling. Nature 9, 747-758
    • (2008) Nature , vol.9 , pp. 747-758
    • Anjum, R.1    Blenis, J.2
  • 55
    • 0042622251 scopus 로고    scopus 로고
    • Scansite 2.0: Proteome-wide prediction of cell signaling interactions using short sequence motifs
    • Obenauer, J. C. (2003) Scansite 2.0: proteome-wide prediction of cell signaling interactions using short sequence motifs. Nucleic Acids Res. 31, 3635-3641
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3635-3641
    • Obenauer, J.C.1
  • 57
    • 79955539577 scopus 로고    scopus 로고
    • Induced ectopic kinetochore assembly bypasses the requirement for CENP-A nucleosomes
    • Gascoigne, K. E., Takeuchi, K., Suzuki, A., and Hori, T. (2011) Induced ectopic kinetochore assembly bypasses the requirement for CENP-A nucleosomes. Cell 29, 410-422
    • (2011) Cell , vol.29 , pp. 410-422
    • Gascoigne, K.E.1    Takeuchi, K.2    Suzuki, A.3    Hori, T.4
  • 58
    • 58549085778 scopus 로고    scopus 로고
    • An integrated workflow for charting the human interaction proteome: Insights into the PP2A system
    • Glatter, T., Wepf, A., Aebersold, R., and Gstaiger, M. (2009) An integrated workflow for charting the human interaction proteome: insights into the PP2A system. Mol. Sys. Biol. 5, 237
    • (2009) Mol. Sys. Biol. , vol.5 , pp. 237
    • Glatter, T.1    Wepf, A.2    Aebersold, R.3    Gstaiger, M.4
  • 60
    • 28344440877 scopus 로고    scopus 로고
    • Mitotic remodeling of the replicon and chromosome structure
    • DOI 10.1016/j.cell.2005.08.045, PII S0092867405009736
    • Lemaitre, J.-M., Danis, E., Pasero, P., Vassetzky, Y., and Méchali, M. (2005) Mitotic remodeling of the replicon and chromosome structure. Cell 123, 787-801 (Pubitemid 41721027)
    • (2005) Cell , vol.123 , Issue.5 , pp. 787-801
    • Lemaitre, J.-M.1    Danis, E.2    Pasero, P.3    Vassetzky, Y.4    Mechali, M.5
  • 61
    • 41449089409 scopus 로고    scopus 로고
    • RNA interference guides histone modification during the S phase of chromosomal replication
    • Kloc, A., Zaratiegui, M., Nora, E., and Martienssen, R. (2008) RNA interference guides histone modification during the S phase of chromosomal replication. Curr. Biol. 18, 490-495
    • (2008) Curr. Biol. , vol.18 , pp. 490-495
    • Kloc, A.1    Zaratiegui, M.2    Nora, E.3    Martienssen, R.4
  • 63
    • 2642536094 scopus 로고    scopus 로고
    • Direct binding of INHAT to H3 tails disrupted by modifications
    • DOI 10.1074/jbc.C400151200
    • Schneider, R., Bannister, A. J., Weise, C., and Kouzarides, T. (2004) Direct binding of INHAT to H3 tails disrupted by modifications. J. Biol. Chem. 279, 23859-23862 (Pubitemid 38725241)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.23 , pp. 23859-23862
    • Schneider, R.1    Bannister, A.J.2    Weise, C.3    Kouzarides, T.4
  • 64
    • 33746828109 scopus 로고    scopus 로고
    • Molecular recognition of histone H3 by the WD40 protein WDR5
    • DOI 10.1038/nsmb1116, PII NSMB1116
    • Couture, J.-F., Collazo, E., and Trievel, R. C. (2006) Molecular recognition of histone H3 by the WD40 protein WDR5. Nature Struct. Biol. 13, 698-703 (Pubitemid 44175162)
    • (2006) Nature Structural and Molecular Biology , vol.13 , Issue.8 , pp. 698-703
    • Couture, J.-F.1    Collazo, E.2    Trievel, R.C.3
  • 65
    • 66249141300 scopus 로고    scopus 로고
    • The solution structure of the first PHD finger of autoimmune regulator in complex with non-modified histone H3 tail reveals the antagonistic role of H3R2 methylation
    • Chignola, F., Gaetani, M., Rebane, A., Org, T., Mollica, L., Zucchelli, C., Spitaleri, A., Mannella, V., Peterson, P., and Musco, G. (2009) The solution structure of the first PHD finger of autoimmune regulator in complex with non-modified histone H3 tail reveals the antagonistic role of H3R2 methylation. Nucleic Acids Res. 37, 2951-2961
    • (2009) Nucleic Acids Res. , vol.37 , pp. 2951-2961
    • Chignola, F.1    Gaetani, M.2    Rebane, A.3    Org, T.4    Mollica, L.5    Zucchelli, C.6    Spitaleri, A.7    Mannella, V.8    Peterson, P.9    Musco, G.10
  • 66
    • 58649110597 scopus 로고    scopus 로고
    • Structural basis for the requirement of additional factors for MLL1 SET domain activity and recognition of epigenetic marks
    • Southall, S. M., Wong, P.-S., Odho, Z., Roe, S. M., and Wilson, J. R. (2009) Structural basis for the requirement of additional factors for MLL1 SET domain activity and recognition of epigenetic marks. Mol. Cell 33, 181-191
    • (2009) Mol. Cell , vol.33 , pp. 181-191
    • Southall, S.M.1    Wong, P.-S.2    Odho, Z.3    Roe, S.M.4    Wilson, J.R.5
  • 68
    • 70350007285 scopus 로고    scopus 로고
    • Phosphorylation of histone H3 at Thr3 is part of a combinatorial pattern that marks and configures mitotic chromatin
    • Markaki, Y., Christogianni, A., Politou, A. S., and Georgatos, S. D. (2009) Phosphorylation of histone H3 at Thr3 is part of a combinatorial pattern that marks and configures mitotic chromatin. J. Cell Sci. 122, 2809-2819
    • (2009) J. Cell Sci. , vol.122 , pp. 2809-2819
    • Markaki, Y.1    Christogianni, A.2    Politou, A.S.3    Georgatos, S.D.4
  • 71
    • 0033200205 scopus 로고    scopus 로고
    • The nucleosomal response associated with immediate-early gene induction is mediated via alternative MAP kinase cascades: MSK1 as a potential histone H3/HMG-14 kinase
    • DOI 10.1093/emboj/18.17.4779
    • Thomson, S., Clayton, A. L., Hazzalin, C. A., Rose, S., Barratt, M. J., and Mahadevan, L. C. (1999) The nucleosomal response associated with immediate-early gene induction is mediated via alternative MAP kinase cascades: MSK1 as a potential histone H3/HMG-14 kinase. The EMBO J. 18, 4779-4793 (Pubitemid 29415531)
    • (1999) EMBO Journal , vol.18 , Issue.17 , pp. 4779-4793
    • Thomson, S.1    Clayton, A.L.2    Hazzalin, C.A.3    Rose, S.4    Barratt, M.J.5    Mahadevan, L.C.6
  • 72
  • 73
    • 0035854684 scopus 로고    scopus 로고
    • HMGN3a and HMGN3b, two protein isoforms with a tissuespecific expression pattern, expand the cellular repertoire of nucleosome-binding proteins
    • West, K. L., Ito, Y., Birger, Y., Postnikov, Y., Shirakawa, H., and Bustin, M. (2001) HMGN3a and HMGN3b, two protein isoforms with a tissuespecific expression pattern, expand the cellular repertoire of nucleosome-binding proteins. J. Biol. Chem. 276, 25959-25969
    • (2001) J. Biol. Chem. , vol.276 , pp. 25959-25969
    • West, K.L.1    Ito, Y.2    Birger, Y.3    Postnikov, Y.4    Shirakawa, H.5    Bustin, M.6
  • 74
    • 0028876893 scopus 로고
    • Two classes of proteins dependent on either the presence or absence of thyroid hormone for interaction with the thyroid hormone receptor
    • Lee, J. W., Choi, H. S., Gyuris, J., and Brent, R. (1995) Two classes of proteins dependent on either the presence or absence of thyroid hormone for interaction with the thyroid hormone receptor. Mol Endocrinol. 9, 243-254
    • (1995) Mol Endocrinol. , vol.9 , pp. 243-254
    • Lee, J.W.1    Choi, H.S.2    Gyuris, J.3    Brent, R.4
  • 75
    • 80054698820 scopus 로고    scopus 로고
    • Rapid and Reproducible Single-Stage Phosphopeptide Enrichment of complex peptide mixtures: Application to general and phosphotyrosine-specific phosphoproteomics experiments
    • Kettenbach, A. N., and Gerber, S. A. (2011) Rapid and Reproducible Single-Stage Phosphopeptide Enrichment of complex peptide mixtures: application to general and phosphotyrosine-specific phosphoproteomics experiments. Anal. Chem. 83, 7635-7644
    • (2011) Anal. Chem. , vol.83 , pp. 7635-7644
    • Kettenbach, A.N.1    Gerber, S.A.2
  • 76
    • 0032507949 scopus 로고    scopus 로고
    • Histone macroH2A1 is concentrated in the inactive X chromosome of female mammals
    • DOI 10.1038/31275
    • Costanzi, C., and Pehrson, J. R. (1998) Histone macroH2A1 is concentrated in the inactive X chromosome of female mammals. Nature 393, 599-601 (Pubitemid 28319252)
    • (1998) Nature , vol.393 , Issue.6685 , pp. 599-601
    • Costanzi, C.1    Pehrson, J.R.2
  • 77
    • 77955452081 scopus 로고    scopus 로고
    • Multiple facets of the unique histone variant macroH2A: From genomics to cell biology
    • Gamble, M., and Kraus, W. L. (2010) Multiple facets of the unique histone variant macroH2A: From genomics to cell biology. Cell Cycle 9, 2568-2574
    • (2010) Cell Cycle , vol.9 , pp. 2568-2574
    • Gamble, M.1    Kraus, W.L.2
  • 78
    • 84866918096 scopus 로고    scopus 로고
    • The basic linker of macroH2A stabilizes DNA at the entry/exit site of the nucleosome
    • Chakravarthy, S., Patel, A., and Bowman, G. D. (2012) The basic linker of macroH2A stabilizes DNA at the entry/exit site of the nucleosome. Nucleic Acids Res. 40, 8285-8295
    • (2012) Nucleic Acids Res. , vol.40 , pp. 8285-8295
    • Chakravarthy, S.1    Patel, A.2    Bowman, G.D.3
  • 79
    • 79959870239 scopus 로고    scopus 로고
    • The linker region of macroH2A promotes self-association of nucleosomal arrays
    • Muthurajan, U. M., McBryant, S. J., Lu, X., Hansen, J. C., and Luger, K. (2011) The linker region of macroH2A promotes self-association of nucleosomal arrays. J. Biol. Chem. 286, 23852-23864
    • (2011) J. Biol. Chem. , vol.286 , pp. 23852-23864
    • Muthurajan, U.M.1    McBryant, S.J.2    Lu, X.3    Hansen, J.C.4    Luger, K.5
  • 80
    • 84876339351 scopus 로고    scopus 로고
    • CDK-dependent phosphorylation and nuclear exclusion coordinately control kinetochore assembly state
    • Gascoigne, K. E., and Cheeseman, I. M. (2013) CDK-dependent phosphorylation and nuclear exclusion coordinately control kinetochore assembly state. J. Cell Biol. 201, 23-32
    • (2013) J. Cell Biol. , vol.201 , pp. 23-32
    • Gascoigne, K.E.1    Cheeseman, I.M.2
  • 81
    • 78549233307 scopus 로고    scopus 로고
    • The function of spliceosome components in open mitosis
    • Hofmann, J. C., Husedzinovic, A., and Gruss, O. J. (2010) The function of spliceosome components in open mitosis. Nucleus 1, 447-459
    • (2010) Nucleus , vol.1 , pp. 447-459
    • Hofmann, J.C.1    Husedzinovic, A.2    Gruss, O.J.3
  • 82
    • 84875507786 scopus 로고    scopus 로고
    • Mitotic bookmarking by transcription factors
    • Kadauke, S., and Blobel, G. A. (2013) Mitotic bookmarking by transcription factors. Epigenetics & Chromatin 6, 1-1
    • (2013) Epigenetics & Chromatin , vol.6 , pp. 1-1
    • Kadauke, S.1    Blobel, G.A.2
  • 85
    • 69849105566 scopus 로고    scopus 로고
    • Non-coding murine centromeric transcripts associate with and potentiate Aurora B kinase
    • Ferri, F., Bouzinba-Segard, H., Velasco, G., Hube, F., and Francastel, C. (2009) Non-coding murine centromeric transcripts associate with and potentiate Aurora B kinase. Nucleic Acids Res. 37, 5071-5080
    • (2009) Nucleic Acids Res. , vol.37 , pp. 5071-5080
    • Ferri, F.1    Bouzinba-Segard, H.2    Velasco, G.3    Hube, F.4    Francastel, C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.