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Volumn 13, Issue 3, 2014, Pages 440-452

Mitotic phosphorylation of histone H3 threonine 80

Author keywords

Chromatin condensation; Histone phosphorylation; Mitosis

Indexed keywords

ALANINE; ALPHA TUBULIN; AURORA B KINASE; GLUTAMIC ACID; HISTONE H2A; HISTONE H3; HISTONE H4; THREONINE; ANTIBODY; CHROMATIN; HISTONE; NUCLEOSOME; PROTEIN BINDING;

EID: 84896817379     PISSN: 15384101     EISSN: 15514005     Source Type: Journal    
DOI: 10.4161/cc.27269     Document Type: Article
Times cited : (31)

References (51)
  • 1
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 A resolution
    • PMID:9305837
    • Luger K, Mäder AW, Richmond RK, Sargent DF, Richmond TJ. Crystal structure of the nucleosome core particle at 2.8 A resolution. Nature 1997; 389:251-60; PMID:9305837; http://dx.doi.org/10.1038/38444
    • (1997) Nature , vol.389 , pp. 251-260
    • Luger, K.1    Mäder, A.W.2    Richmond, R.K.3    Sargent, D.F.4    Richmond, T.J.5
  • 2
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • PMID:11498575
    • Jenuwein T, Allis CD. Translating the histone code. Science 2001; 293:1074-80; PMID:11498575; http://dx.doi.org/10.1126/science.1063127
    • (2001) Science , vol.293 , pp. 1074-1080
    • Jenuwein, T.1    Allis, C.D.2
  • 3
    • 84878924943 scopus 로고    scopus 로고
    • Scratching the (lateral) surface of chromatin regulation by histone modifications
    • PMID:23739170
    • Tropberger P, Schneider R. Scratching the (lateral) surface of chromatin regulation by histone modifications. Nat Struct Mol Biol 2013; 20:657-61; PMID:23739170; http://dx.doi.org/10.1038/nsmb.2581
    • (2013) Nat Struct Mol Biol , vol.20 , pp. 657-661
    • Tropberger, P.1    Schneider, R.2
  • 5
    • 0030828073 scopus 로고    scopus 로고
    • Mitosis-specific phosphorylation of histone H3 initiates primarily within pericentromeric heterochromatin during G2 and spreads in an ordered fashion coincident with mitotic chromosome condensation
    • PMID:9362543
    • Hendzel MJ, Wei Y, Mancini MA, Van Hooser A, Ranalli T, Brinkley BR, Bazett-Jones DP, Allis CD. Mitosis-specific phosphorylation of histone H3 initiates primarily within pericentromeric heterochromatin during G2 and spreads in an ordered fashion coincident with mitotic chromosome condensation. Chromosoma 1997; 106:348-60; PMID:9362543; http://dx.doi.org/10.1007/ s004120050256
    • (1997) Chromosoma , vol.106 , pp. 348-360
    • Hendzel, M.J.1    Wei, Y.2    Mancini, M.A.3    Van Hooser, A.4    Ranalli, T.5    Brinkley, B.R.6    Bazett-Jones, D.P.7    Allis, C.D.8
  • 6
    • 0037324194 scopus 로고    scopus 로고
    • Novel mitosis-specific phosphorylation of histone H3 at Thr11 mediated by Dlk/ZIP kinase
    • PMID:12560483
    • Preuss U, Landsberg G, Scheidtmann KH. Novel mitosis-specific phosphorylation of histone H3 at Thr11 mediated by Dlk/ZIP kinase. Nucleic Acids Res 2003; 31:878-85; PMID:12560483; http://dx.doi.org/10.1093/nar/gkg176
    • (2003) Nucleic Acids Res , vol.31 , pp. 878-885
    • Preuss, U.1    Landsberg, G.2    Scheidtmann, K.H.3
  • 7
    • 0033520367 scopus 로고    scopus 로고
    • Identification of a novel phosphorylation site on histone H3 coupled with mitotic chromosome condensation
    • PMID:10464286
    • Goto H, Tomono Y, Ajiro K, Kosako H, Fujita M, Sakurai M, Okawa K, Iwamatsu A, Okigaki T, Takahashi T, et al. Identification of a novel phosphorylation site on histone H3 coupled with mitotic chromosome condensation. J Biol Chem 1999; 274:25543-9; PMID:10464286; http://dx.doi.org/10.1074/jbc. 274.36.25543
    • (1999) J Biol Chem , vol.274 , pp. 25543-25549
    • Goto, H.1    Tomono, Y.2    Ajiro, K.3    Kosako, H.4    Fujita, M.5    Sakurai, M.6    Okawa, K.7    Iwamatsu, A.8    Okigaki, T.9    Takahashi, T.10
  • 9
    • 84861665777 scopus 로고    scopus 로고
    • Identification of combinatorial patterns of post-translational modifications on individual histones in the mouse brain
    • PMID:22693562
    • Tweedie-Cullen RY, Brunner AM, Grossmann J, Mohanna S, Sichau D, Nanni P, Panse C, Mansuy IM. Identification of combinatorial patterns of post-translational modifications on individual histones in the mouse brain. PLoS One 2012; 7:e36980; PMID:22693562; http://dx.doi.org/10.1371/journal.pone. 0036980
    • (2012) PLoS One , vol.7
    • Tweedie-Cullen, R.Y.1    Brunner, A.M.2    Grossmann, J.3    Mohanna, S.4    Sichau, D.5    Nanni, P.6    Panse, C.7    Mansuy, I.M.8
  • 10
    • 70449426592 scopus 로고    scopus 로고
    • Comprehensive mapping of post-translational modifications on synaptic, nuclear, and histone proteins in the adult mouse brain
    • PMID:19737024
    • Tweedie-Cullen RY, Reck JM, Mansuy IM. Comprehensive mapping of post-translational modifications on synaptic, nuclear, and histone proteins in the adult mouse brain. J Proteome Res 2009; 8:4966-82; PMID:19737024; http://dx.doi.org/10.1021/pr9003739
    • (2009) J Proteome Res , vol.8 , pp. 4966-4982
    • Tweedie-Cullen, R.Y.1    Reck, J.M.2    Mansuy, I.M.3
  • 11
    • 77956643239 scopus 로고    scopus 로고
    • Quantitative interaction proteomics and genome-wide profiling of epigenetic histone marks and their readers
    • PMID:20850016
    • Vermeulen M, Eberl HC, Matarese F, Marks H, Denissov S, Butter F, Lee KK, Olsen JV, Hyman AA, Stunnenberg HG, et al. Quantitative interaction proteomics and genome-wide profiling of epigenetic histone marks and their readers. Cell 2010; 142:967-80; PMID:20850016; http://dx.doi.org/10.1016/j.cell.2010.08.020
    • (2010) Cell , vol.142 , pp. 967-980
    • Vermeulen, M.1    Eberl, H.C.2    Matarese, F.3    Marks, H.4    Denissov, S.5    Butter, F.6    Lee, K.K.7    Olsen, J.V.8    Hyman, A.A.9    Stunnenberg, H.G.10
  • 14
    • 0034604354 scopus 로고    scopus 로고
    • Mitotic phosphorylation of histone H3 is governed by Ipl1/aurora kinase and Glc7/PP1 phosphatase in budding yeast and nematodes
    • PMID:10975519
    • Hsu JY, Sun ZW, Li X, Reuben M, Tatchell K, Bishop DK, Grushcow JM, Brame CJ, Caldwell JA, Hunt DF, et al. Mitotic phosphorylation of histone H3 is governed by Ipl1/aurora kinase and Glc7/PP1 phosphatase in budding yeast and nematodes. Cell 2000; 102:279-91; PMID:10975519; http://dx.doi.org/10.1016/ S0092-8674(00)00034-9
    • (2000) Cell , vol.102 , pp. 279-291
    • Hsu, J.Y.1    Sun, Z.W.2    Li, X.3    Reuben, M.4    Tatchell, K.5    Bishop, D.K.6    Grushcow, J.M.7    Brame, C.J.8    Caldwell, J.A.9    Hunt, D.F.10
  • 15
    • 0035911159 scopus 로고    scopus 로고
    • Drosophila aurora B kinase is required for histone H3 phosphorylation and condensin recruitment during chromosome condensation and to organize the central spindle during cytokinesis
    • PMID:11266459
    • Giet R, Glover DM. Drosophila aurora B kinase is required for histone H3 phosphorylation and condensin recruitment during chromosome condensation and to organize the central spindle during cytokinesis. J Cell Biol 2001; 152:669-82; PMID:11266459; http://dx.doi.org/10.1083/jcb.152.4.669
    • (2001) J Cell Biol , vol.152 , pp. 669-682
    • Giet, R.1    Glover, D.M.2
  • 16
    • 0035858865 scopus 로고    scopus 로고
    • Essential roles of Drosophila inner centromere protein (INCENP) and aurora B in histone H3 phosphorylation, metaphase chromosome alignment, kinetochore disjunction, and chromosome segregation
    • PMID:11352945
    • Adams RR, Maiato H, Earnshaw WC, Carmena M. Essential roles of Drosophila inner centromere protein (INCENP) and aurora B in histone H3 phosphorylation, metaphase chromosome alignment, kinetochore disjunction, and chromosome segregation. J Cell Biol 2001; 153:865-80; PMID:11352945; http://dx.doi.org/10. 1083/jcb.153.4.865
    • (2001) J Cell Biol , vol.153 , pp. 865-880
    • Adams, R.R.1    Maiato, H.2    Earnshaw, W.C.3    Carmena, M.4
  • 17
    • 77957725753 scopus 로고    scopus 로고
    • Survivin reads phosphorylated histone H3 threonine 3 to activate the mitotic kinase Aurora B
    • PMID:20705815
    • Kelly AE, Ghenoiu C, Xue JZ, Zierhut C, Kimura H, Funabiki H. Survivin reads phosphorylated histone H3 threonine 3 to activate the mitotic kinase Aurora B. Science 2010; 330:235-9; PMID:20705815; http://dx.doi.org/10.1126/ science.1189505
    • (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
  • 18
    • 28844475262 scopus 로고    scopus 로고
    • Histone H3 serine 10 phosphorylation by Aurora B causes HP1 dissociation from heterochromatin
    • PMID:16222244
    • Hirota T, Lipp JJ, Toh BH, Peters JM. Histone H3 serine 10 phosphorylation by Aurora B causes HP1 dissociation from heterochromatin. Nature 2005; 438:1176-80; PMID:16222244; http://dx.doi.org/10.1038/nature04254
    • (2005) Nature , vol.438 , pp. 1176-1180
    • Hirota, T.1    Lipp, J.J.2    Toh, B.H.3    Peters, J.M.4
  • 20
    • 0033515426 scopus 로고    scopus 로고
    • Phosphorylation of histone H3 is required for proper chromosome condensation and segregation
    • PMID:10199406
    • Wei Y, Yu L, Bowen J, Gorovsky MA, Allis CD. Phosphorylation of histone H3 is required for proper chromosome condensation and segregation. Cell 1999; 97:99-109; PMID:10199406; http://dx.doi.org/10.1016/S0092-8674(00)80718-7
    • (1999) Cell , vol.97 , pp. 99-109
    • Wei, Y.1    Yu, L.2    Bowen, J.3    Gorovsky, M.A.4    Allis, C.D.5
  • 21
    • 0036153807 scopus 로고    scopus 로고
    • ISWI remodeling complexes in Xenopus egg extracts: Identification as major chromosomal components that are regulated by INCENP-aurora B
    • PMID:11809820
    • MacCallum DE, Losada A, Kobayashi R, Hirano T. ISWI remodeling complexes in Xenopus egg extracts: identification as major chromosomal components that are regulated by INCENP-aurora B. Mol Biol Cell 2002; 13:25-39; PMID:11809820; http://dx.doi.org/10.1091/mbc.01-09-0441
    • (2002) Mol Biol Cell , vol.13 , pp. 25-39
    • MacCallum, D.E.1    Losada, A.2    Kobayashi, R.3    Hirano, T.4
  • 22
    • 0035890134 scopus 로고    scopus 로고
    • The N-terminus of histone H2B, but not that of histone H3 or its phosphorylation, is essential for chromosome condensation
    • PMID:11707409
    • de la Barre AE, Angelov D, Molla A, Dimitrov S. The N-terminus of histone H2B, but not that of histone H3 or its phosphorylation, is essential for chromosome condensation. EMBO J 2001; 20:6383-93; PMID:11707409; http://dx.doi.org/10.1093/emboj/20.22.6383
    • (2001) EMBO J , vol.20 , pp. 6383-6393
    • De La Barre, A.E.1    Angelov, D.2    Molla, A.3    Dimitrov, S.4
  • 23
    • 0037172665 scopus 로고    scopus 로고
    • Methylation of H3-lysine 79 is mediated by a new family of HMTases without a SET domain
    • PMID:12123582
    • Feng Q, Wang H, Ng HH, Erdjument-Bromage H, Tempst P, Struhl K, Zhang Y. Methylation of H3-lysine 79 is mediated by a new family of HMTases without a SET domain. Curr Biol 2002; 12:1052-8; PMID:12123582; http://dx.doi.org/10.1016/ S0960-9822(02)00901-6
    • (2002) Curr Biol , vol.12 , pp. 1052-1058
    • Feng, Q.1    Wang, H.2    Ng, H.H.3    Erdjument-Bromage, H.4    Tempst, P.5    Struhl, K.6    Zhang, Y.7
  • 24
    • 0037077178 scopus 로고    scopus 로고
    • Dot1p modulates silencing in yeast by methylation of the nucleosome core
    • PMID:12086673
    • van Leeuwen F, Gafken PR, Gottschling DE. Dot1p modulates silencing in yeast by methylation of the nucleosome core. Cell 2002; 109:745-56; PMID:12086673; http://dx.doi.org/10.1016/S0092-8674(02)00759-6
    • (2002) Cell , vol.109 , pp. 745-756
    • Van Leeuwen, F.1    Gafken, P.R.2    Gottschling, D.E.3
  • 25
    • 13744259076 scopus 로고    scopus 로고
    • Characterization of the grappa gene, the Drosophila histone H3 lysine 79 methyltransferase
    • PMID:15371351
    • Shanower GA, Muller M, Blanton JL, Honti V, Gyurkovics H, Schedl P. Characterization of the grappa gene, the Drosophila histone H3 lysine 79 methyltransferase. Genetics 2005; 169:173-84; PMID:15371351; http://dx.doi.org/10.1534/genetics.104.033191
    • (2005) Genetics , vol.169 , pp. 173-184
    • Shanower, G.A.1    Muller, M.2    Blanton, J.L.3    Honti, V.4    Gyurkovics, H.5    Schedl, P.6
  • 26
  • 27
    • 79952074043 scopus 로고    scopus 로고
    • Regulation of the DNA damage response and gene expression by the Dot1L histone methyltransferase and the 53Bp1 tumour suppressor
    • PMID:21383990
    • FitzGerald J, Moureau S, Drogaris P, O'Connell E, Abshiru N, Verreault A, Thibault P, Grenon M, Lowndes NF. Regulation of the DNA damage response and gene expression by the Dot1L histone methyltransferase and the 53Bp1 tumour suppressor. PLoS One 2011; 6:e14714; PMID:21383990; http://dx.doi.org/10.1371/ journal.pone.0014714
    • (2011) PLoS One , vol.6
    • FitzGerald, J.1    Moureau, S.2    Drogaris, P.3    O'Connell, E.4    Abshiru, N.5    Verreault, A.6    Thibault, P.7    Grenon, M.8    Lowndes, N.F.9
  • 28
    • 0018355091 scopus 로고
    • Role of spindle microtubules in the control of cell cycle timing
    • PMID:572367
    • Sluder G. Role of spindle microtubules in the control of cell cycle timing. J Cell Biol 1979; 80:674-91; PMID:572367; http://dx.doi.org/10.1083/jcb. 80.3.674
    • (1979) J Cell Biol , vol.80 , pp. 674-691
    • Sluder, G.1
  • 30
    • 32944477078 scopus 로고    scopus 로고
    • Condensin I stabilizes chromosomes mechanically through a dynamic interaction in live cells
    • PMID:16488867
    • Gerlich D, Hirota T, Koch B, Peters JM, Ellenberg J. Condensin I stabilizes chromosomes mechanically through a dynamic interaction in live cells. Curr Biol 2006; 16:333-44; PMID:16488867; http://dx.doi.org/10.1016/j.cub.2005. 12.040
    • (2006) Curr Biol , vol.16 , pp. 333-344
    • Gerlich, D.1    Hirota, T.2    Koch, B.3    Peters, J.M.4    Ellenberg, J.5
  • 31
    • 84877774804 scopus 로고    scopus 로고
    • Rewiring of human lung cell lineage and mitotic networks in lung adenocarcinomas
    • PMID:23591868
    • Kim IJ, Quigley D, To MD, Pham P, Lin K, Jo B, Jen KY, Raz D, Kim J, Mao JH, et al. Rewiring of human lung cell lineage and mitotic networks in lung adenocarcinomas. Nat Commun 2013; 4:1701; PMID:23591868; http://dx.doi.org/10. 1038/ncomms2660
    • (2013) Nat Commun , vol.4 , pp. 1701
    • Kim, I.J.1    Quigley, D.2    To, M.D.3    Pham, P.4    Lin, K.5    Jo, B.6    Jen, K.Y.7    Raz, D.8    Kim, J.9    Mao, J.H.10
  • 32
    • 37549026472 scopus 로고    scopus 로고
    • Mitotic histone H3 phosphorylation by vaccinia-related kinase 1 in mammalian cells
    • PMID:17938195
    • Kang TH, Park DY, Choi YH, Kim KJ, Yoon HS, Kim KT. Mitotic histone H3 phosphorylation by vaccinia-related kinase 1 in mammalian cells. Mol Cell Biol 2007; 27:8533-46; PMID:17938195; http://dx.doi.org/10.1128/MCB.00018-07
    • (2007) Mol Cell Biol , vol.27 , pp. 8533-8546
    • Kang, T.H.1    Park, D.Y.2    Choi, Y.H.3    Kim, K.J.4    Yoon, H.S.5    Kim, K.T.6
  • 34
    • 21844436803 scopus 로고    scopus 로고
    • X-ray structure of a tetranucleosome and its implications for the chromatin fibre
    • PMID:16001076
    • Schalch T, Duda S, Sargent DF, Richmond TJ. X-ray structure of a tetranucleosome and its implications for the chromatin fibre. Nature 2005; 436:138-41; PMID:16001076; http://dx.doi.org/10.1038/nature03686
    • (2005) Nature , vol.436 , pp. 138-141
    • Schalch, T.1    Duda, S.2    Sargent, D.F.3    Richmond, T.J.4
  • 35
    • 84859421494 scopus 로고    scopus 로고
    • Human mitotic chromosomes consist predominantly of irregularly folded nucleosome fibres without a 30-nm chromatin structure
    • PMID:22343941
    • Nishino Y, Eltsov M, Joti Y, Ito K, Takata H, Takahashi Y, Hihara S, Frangakis AS, Imamoto N, Ishikawa T, et al. Human mitotic chromosomes consist predominantly of irregularly folded nucleosome fibres without a 30-nm chromatin structure. EMBO J 2012; 31:1644-53; PMID:22343941; http://dx.doi.org/10.1038/ emboj.2012.35
    • (2012) EMBO J , vol.31 , pp. 1644-1653
    • Nishino, Y.1    Eltsov, M.2    Joti, Y.3    Ito, K.4    Takata, H.5    Takahashi, Y.6    Hihara, S.7    Frangakis, A.S.8    Imamoto, N.9    Ishikawa, T.10
  • 36
    • 32444434989 scopus 로고    scopus 로고
    • Histone H4-K16 acetylation controls chromatin structure and protein interactions
    • PMID:16469925
    • Shogren-Knaak M, Ishii H, Sun JM, Pazin MJ, Davie JR, Peterson CL. Histone H4-K16 acetylation controls chromatin structure and protein interactions. Science 2006; 311:844-7; PMID:16469925; http://dx.doi.org/10.1126/ science.1124000
    • (2006) Science , vol.311 , pp. 844-847
    • Shogren-Knaak, M.1    Ishii, H.2    Sun, J.M.3    Pazin, M.J.4    Davie, J.R.5    Peterson, C.L.6
  • 37
    • 0032489012 scopus 로고    scopus 로고
    • TRF2 protects human telomeres from end-to-end fusions
    • PMID:9476899
    • van Steensel B, Smogorzewska A, de Lange T. TRF2 protects human telomeres from end-to-end fusions. Cell 1998; 92:401-13; PMID:9476899; http://dx.doi.org/10.1016/S0092-8674(00)80932-0
    • (1998) Cell , vol.92 , pp. 401-413
    • Van Steensel, B.1    Smogorzewska, A.2    De Lange, T.3
  • 38
    • 67349227137 scopus 로고    scopus 로고
    • Replication stress induces sister-chromatid bridging at fragile site loci in mitosis
    • PMID:19465922
    • Chan KL, Palmai-Pallag T, Ying S, Hickson ID. Replication stress induces sister-chromatid bridging at fragile site loci in mitosis. Nat Cell Biol 2009; 11:753-60; PMID:19465922; http://dx.doi.org/10.1038/ncb1882
    • (2009) Nat Cell Biol , vol.11 , pp. 753-760
    • Chan, K.L.1    Palmai-Pallag, T.2    Ying, S.3    Hickson, I.D.4
  • 39
    • 51549087123 scopus 로고    scopus 로고
    • Probing nucleosome function: A highly versatile library of synthetic histone H3 and H4 mutants
    • PMID:18805098
    • Dai J, Hyland EM, Yuan DS, Huang H, Bader JS, Boeke JD. Probing nucleosome function: a highly versatile library of synthetic histone H3 and H4 mutants. Cell 2008; 134:1066-78; PMID:18805098; http://dx.doi.org/10.1016/j. cell.2008.07.019
    • (2008) Cell , vol.134 , pp. 1066-1078
    • Dai, J.1    Hyland, E.M.2    Yuan, D.S.3    Huang, H.4    Bader, J.S.5    Boeke, J.D.6
  • 40
  • 41
    • 33750844590 scopus 로고    scopus 로고
    • Mitotic chromosome structure and condensation
    • PMID:17046228
    • Belmont AS. Mitotic chromosome structure and condensation. Curr Opin Cell Biol 2006; 18:632-8; PMID:17046228; http://dx.doi.org/10.1016/j.ceb.2006.09.007
    • (2006) Curr Opin Cell Biol , vol.18 , pp. 632-638
    • Belmont, A.S.1
  • 42
    • 0037365635 scopus 로고    scopus 로고
    • Structure, function and evolution of haspin and haspin-related proteins, a distinctive group of eukaryotic protein kinases
    • PMID:12737306
    • Higgins JM. Structure, function and evolution of haspin and haspin-related proteins, a distinctive group of eukaryotic protein kinases. Cell Mol Life Sci 2003; 60:446-62; PMID:12737306; http://dx.doi.org/10.1007/ s000180300038
    • (2003) Cell Mol Life Sci , vol.60 , pp. 446-462
    • Higgins, J.M.1
  • 43
    • 13844252061 scopus 로고    scopus 로고
    • The kinase haspin is required for mitotic histone H3 Thr 3 phosphorylation and normal metaphase chromosome alignment
    • PMID:15681610
    • Dai J, Sultan S, Taylor SS, Higgins JM. The kinase haspin is required for mitotic histone H3 Thr 3 phosphorylation and normal metaphase chromosome alignment. Genes Dev 2005; 19:472-88; PMID:15681610; http://dx.doi.org/10.1101/ gad.1267105
    • (2005) Genes Dev , vol.19 , pp. 472-488
    • Dai, J.1    Sultan, S.2    Taylor, S.S.3    Higgins, J.M.4
  • 44
    • 0344837759 scopus 로고    scopus 로고
    • Structure of the catalytic domain of human DOT1L, a non-SET domain nucleosomal histone methyltransferase
    • PMID:12628190
    • Min J, Feng Q, Li Z, Zhang Y, Xu RM. Structure of the catalytic domain of human DOT1L, a non-SET domain nucleosomal histone methyltransferase. Cell 2003; 112:711-23; PMID:12628190; http://dx.doi.org/10.1016/S0092-8674(03)00114-4
    • (2003) Cell , vol.112 , pp. 711-723
    • Min, J.1    Feng, Q.2    Li, Z.3    Zhang, Y.4    Xu, R.M.5
  • 45
    • 69249119365 scopus 로고    scopus 로고
    • Mapping the local protein interactome of the NuA3 histone acetyltransferase
    • PMID:19621382
    • Smart SK, Mackintosh SG, Edmondson RD, Taverna SD, Tackett AJ. Mapping the local protein interactome of the NuA3 histone acetyltransferase. Protein Sci 2009; 18:1987-97; PMID:19621382; http://dx.doi.org/10.1002/pro.212
    • (2009) Protein Sci , vol.18 , pp. 1987-1997
    • Smart, S.K.1    Mackintosh, S.G.2    Edmondson, R.D.3    Taverna, S.D.4    Tackett, A.J.5
  • 46
    • 26844556166 scopus 로고    scopus 로고
    • I-DIRT, a general method for distinguishing between specific and nonspecific protein interactions
    • PMID:16212429
    • Tackett AJ, DeGrasse JA, Sekedat MD, Oeffinger M, Rout MP, Chait BT. I-DIRT, a general method for distinguishing between specific and nonspecific protein interactions. J Proteome Res 2005; 4:1752-6; PMID:16212429; http://dx.doi.org/10.1021/pr050225e
    • (2005) J Proteome Res , vol.4 , pp. 1752-1756
    • Tackett, A.J.1    DeGrasse, J.A.2    Sekedat, M.D.3    Oeffinger, M.4    Rout, M.P.5    Chait, B.T.6
  • 48
    • 84864308665 scopus 로고    scopus 로고
    • ChAP-MS: A method for identification of proteins and histone posttranslational modifications at a single genomic locus
    • PMID:22840409
    • Byrum SD, Raman A, Taverna SD, Tackett AJ. ChAP-MS: a method for identification of proteins and histone posttranslational modifications at a single genomic locus. Cell Rep 2012; 2:198-205; PMID:22840409; http://dx.doi.org/10.1016/j.celrep.2012.06.019
    • (2012) Cell Rep , vol.2 , pp. 198-205
    • Byrum, S.D.1    Raman, A.2    Taverna, S.D.3    Tackett, A.J.4
  • 49
    • 84864310426 scopus 로고    scopus 로고
    • Quantitative analysis of histone exchange for transcriptionally active chromatin
    • PMID:21884633
    • Byrum SD, Taverna SD, Tackett AJ. Quantitative analysis of histone exchange for transcriptionally active chromatin. J Clin Bioinforma 2011; 1:17; PMID:21884633; http://dx.doi.org/10.1186/2043-9113-1-17
    • (2011) J Clin Bioinforma , vol.1 , pp. 17
    • Byrum, S.D.1    Taverna, S.D.2    Tackett, A.J.3
  • 50
    • 0033039285 scopus 로고    scopus 로고
    • Preparation of nucleosome core particle from recombinant histones
    • PMID:10372352
    • Luger K, Rechsteiner TJ, Richmond TJ. Preparation of nucleosome core particle from recombinant histones. Methods Enzymol 1999; 304:3-19; PMID:10372352; http://dx.doi.org/10.1016/S0076-6879(99)04003-3
    • (1999) Methods Enzymol , vol.304 , pp. 3-19
    • Luger, K.1    Rechsteiner, T.J.2    Richmond, T.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.