메뉴 건너뛰기




Volumn 116, Issue 18, 2003, Pages 3677-3685

Phosphorylation of serine 10 in histone H3, what for?

Author keywords

Chromatin; Histone H3; Mitosis; Phosphorylation; Serine 10

Indexed keywords

DNA BINDING PROTEIN; HISTONE H3; PHOSPHATASE; SERINE;

EID: 0141613756     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: 10.1242/jcs.00735     Document Type: Article
Times cited : (397)

References (93)
  • 1
  • 2
    • 0035252654 scopus 로고    scopus 로고
    • Chromosomal passengers and the (aurora) ABCs of mitosis
    • Adams, R. R., Carmena, M. and Earnshaw, W. C. (2001a). Chromosomal passengers and the (aurora) ABCs of mitosis. Trends Cell Biol. 11, 49-54.
    • (2001) Trends Cell Biol. , vol.11 , pp. 49-54
    • Adams, R.R.1    Carmena, M.2    Earnshaw, W.C.3
  • 3
    • 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
    • Adams, R. R., Maiato, H., Earnshaw, W. C. and Carmena, M. (2001b). 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. 153, 865-880.
    • (2001) J. Cell Biol. , vol.153 , pp. 865-880
    • Adams, R.R.1    Maiato, H.2    Earnshaw, W.C.3    Carmena, M.4
  • 4
    • 0029911154 scopus 로고    scopus 로고
    • Vanadate triggers the transition from chromosome condensation to decondensation in a mitotic mutant (tsTM13) inactivation of p34cdc2/H1 kinase and dephosphorylation of mitosis-specific histone H3
    • Ajiro, K., Yasuda, H. and Tsuji, H. (1996a). Vanadate triggers the transition from chromosome condensation to decondensation in a mitotic mutant (tsTM13) inactivation of p34cdc2/H1 kinase and dephosphorylation of mitosis-specific histone H3. Eur. J. Biochem. 241, 923-930.
    • (1996) Eur. J. Biochem. , vol.241 , pp. 923-930
    • Ajiro, K.1    Yasuda, H.2    Tsuji, H.3
  • 5
    • 0029993122 scopus 로고    scopus 로고
    • Alteration of cell cycle-dependent histone phosphorylations by okadaic acid. Induction of mitosis-specific H3 phosphorylation and chromatin condensation in mammalian interphase cells
    • Ajiro, K., Yoda, K., Utsumi, K. and Nishikawa, Y. (1996b). Alteration of cell cycle-dependent histone phosphorylations by okadaic acid. Induction of mitosis-specific H3 phosphorylation and chromatin condensation in mammalian interphase cells. J. Biol. Chem. 271, 13197-13201.
    • (1996) J. Biol. Chem. , vol.271 , pp. 13197-13201
    • Ajiro, K.1    Yoda, K.2    Utsumi, K.3    Nishikawa, Y.4
  • 6
    • 0025837183 scopus 로고
    • The nucleosomal core histone octamer at 3.1 A resolution: A tripartite protein assembly and a left-handed superhelix
    • Arents, G., Burlingame, R. W., Wang, B. C., Love, W. E. and Moudrianakis, E. N. (1991). The nucleosomal core histone octamer at 3.1 A resolution: a tripartite protein assembly and a left-handed superhelix. Proc. Natl. Acad. Sci. USA 88, 10148-10152.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 10148-10152
    • Arents, G.1    Burlingame, R.W.2    Wang, B.C.3    Love, W.E.4    Moudrianakis, E.N.5
  • 7
    • 0031592931 scopus 로고    scopus 로고
    • The tails of histones H3 and H4 adopt a highly structured conformation in the nucleosome
    • Banéres, J. L., Martin, A. and Parello, J. (1997). The tails of histones H3 and H4 adopt a highly structured conformation in the nucleosome. J. Mol. Biol. 273, 503-508.
    • (1997) J. Mol. Biol. , vol.273 , pp. 503-508
    • Banéres, J.L.1    Martin, A.2    Parello, J.3
  • 8
    • 0033106222 scopus 로고    scopus 로고
    • The conserved protein kinase Ipl1 regulates microtubule binding to kinetochores in budding yeast
    • Biggins, S., Severin, F. F., Bhalla, N., Sassoon, I., Hyman, A. A. and Murray, A. W. (1999). The conserved protein kinase Ipl1 regulates microtubule binding to kinetochores in budding yeast. Genes Dev. 13, 532-544.
    • (1999) Genes Dev. , vol.13 , pp. 532-544
    • Biggins, S.1    Severin, F.F.2    Bhalla, N.3    Sassoon, I.4    Hyman, A.A.5    Murray, A.W.6
  • 10
    • 0036200147 scopus 로고    scopus 로고
    • Conserved organization of centromeric chromatin in flies and humans
    • Blower, M. D., Sullivan, B. A. and Karpen, G. H. (2002). Conserved organization of centromeric chromatin in flies and humans. Dev. Cell 2, 319-330.
    • (2002) Dev. Cell , vol.2 , pp. 319-330
    • Blower, M.D.1    Sullivan, B.A.2    Karpen, G.H.3
  • 11
    • 0036732808 scopus 로고    scopus 로고
    • Aurora B kinase exists in a complex with survivin and INCENP and its kinase activity is stimulated by survivin binding and phosphorylation
    • Bolton, M. A., Lan, W., Powers, S. E., McCleland, M. L., Kuang, J. and Stukenberg, P. T. (2002). Aurora B kinase exists in a complex with survivin and INCENP and its kinase activity is stimulated by survivin binding and phosphorylation. Mol. Cell. Biol. 13, 3064-3077.
    • (2002) Mol. Cell. Biol. , vol.13 , pp. 3064-3077
    • Bolton, M.A.1    Lan, W.2    Powers, S.E.3    McCleland, M.L.4    Kuang, J.5    Stukenberg, P.T.6
  • 13
    • 0027515186 scopus 로고
    • Isolation and characterization of chromosome-gain and increase-in-ploidy mutants in yeast
    • Chan, C. S. and Botstein, D. (1993). Isolation and characterization of chromosome-gain and increase-in-ploidy mutants in yeast. Genetics 135, 677-691.
    • (1993) Genetics , vol.135 , pp. 677-691
    • Chan, C.S.1    Botstein, D.2
  • 14
    • 0034644473 scopus 로고    scopus 로고
    • Signaling to chromatin through histone modifications
    • Cheung, P., Allis, C. D. and Sassone-Corsi, P. (2000a). Signaling to chromatin through histone modifications. Cell 103, 263-271.
    • (2000) Cell , vol.103 , pp. 263-271
    • Cheung, P.1    Allis, C.D.2    Sassone-Corsi, P.3
  • 15
    • 0033636595 scopus 로고    scopus 로고
    • Synergistic coupling of histone H3 phosphorylation and acetylation in response to epidermal growth factor stimulation
    • Cheung, P., Tanner, K. G., Cheung, W. L., Sassone-Corsi, P., Denu, J. M. and Allis, C. D. (2000b). Synergistic coupling of histone H3 phosphorylation and acetylation in response to epidermal growth factor stimulation. Mol. Cell 5, 905-915.
    • (2000) Mol. Cell , vol.5 , pp. 905-915
    • Cheung, P.1    Tanner, K.G.2    Cheung, W.L.3    Sassone-Corsi, P.4    Denu, J.M.5    Allis, C.D.6
  • 16
    • 0035431654 scopus 로고    scopus 로고
    • Domain organization at the centromere and neocentromere
    • Choo, K. H. (2001). Domain organization at the centromere and neocentromere. Dev. Cell 1, 165-177.
    • (2001) Dev. Cell , vol.1 , pp. 165-177
    • Choo, K.H.1
  • 17
    • 0034679625 scopus 로고    scopus 로고
    • Phosphoacetylation of histone H3 on c-fos- and c-jun-associated nucleosomes upon gene activation
    • Clayton, A. L., Rose, S., Barratt, M. J. and Mahadevan, L. C. (2000). Phosphoacetylation of histone H3 on c-fos- and c-jun-associated nucleosomes upon gene activation. EMBO J. 19, 3714-3726.
    • (2000) EMBO J. , vol.19 , pp. 3714-3726
    • Clayton, A.L.1    Rose, S.2    Barratt, M.J.3    Mahadevan, L.C.4
  • 19
    • 0034142381 scopus 로고    scopus 로고
    • Core histone N-termini play an essential role in mitotic chromosome condensation
    • de la Barre, A. E., Gerson, V., Gout, S., Creaven, M., Allis, C. D. and Dimitrov, S. (2000). Core histone N-termini play an essential role in mitotic chromosome condensation. EMBO J. 19, 379-391.
    • (2000) EMBO J. , vol.19 , pp. 379-391
    • de la Barre, A.E.1    Gerson, V.2    Gout, S.3    Creaven, M.4    Allis, C.D.5    Dimitrov, S.6
  • 20
    • 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
    • de la Barre, A. E., Angelov, D., Molla, A. and Dimitrov, S. (2001). The N-terminus of histone H2B, but not that of histone H3 or its phosphorylation, is essential for chromosome condensation. EMBO J. 20, 6383-6393.
    • (2001) EMBO J. , vol.20 , pp. 6383-6393
    • de la Barre, A.E.1    Angelov, D.2    Molla, A.3    Dimitrov, S.4
  • 22
    • 0035853261 scopus 로고    scopus 로고
    • Two mammalian mitotic aurora kinases: Who's who?
    • 2001
    • Descamps, S. and Prigent, C. (2001). Two mammalian mitotic aurora kinases: who's who? Sci. STKE 2001, E1.
    • (2001) Sci. STKE
    • Descamps, S.1    Prigent, C.2
  • 23
    • 0034604329 scopus 로고    scopus 로고
    • Mitotic histone H3 phosphorylation by the NIMA kinase in Aspergillus nidulans
    • De Souza, C. P., Osmani, A. H., Wu, L. P., Spotts, J. L. and Osmani, S. A. (2000). Mitotic histone H3 phosphorylation by the NIMA kinase in Aspergillus nidulans. Cell 102, 293-302.
    • (2000) Cell , vol.102 , pp. 293-302
    • De Souza, C.P.1    Osmani, A.H.2    Wu, L.P.3    Spotts, J.L.4    Osmani, S.A.5
  • 24
    • 0022551040 scopus 로고
    • Structure of hyperacetylated chromatin: Light scattering and flow linear dichroism study
    • Dimitrov, S., Makarov, V., Apostolova, T. and Pashev, I. (1986), Structure of hyperacetylated chromatin: light scattering and flow linear dichroism study. FEBS Lett. 197, 217-220.
    • (1986) FEBS Lett. , vol.197 , pp. 217-220
    • Dimitrov, S.1    Makarov, V.2    Apostolova, T.3    Pashev, I.4
  • 25
    • 0037446847 scopus 로고    scopus 로고
    • A novel mechanism for activation of the protein kinase aurora-A
    • Eyers, P. A., Erikson, E., Chen, L. G. and Maller, J. L. (2003). A novel mechanism for activation of the protein kinase aurora-A. Curr. Biol. 13, 691-697.
    • (2003) Curr. Biol. , vol.13 , pp. 691-697
    • Eyers, P.A.1    Erikson, E.2    Chen, L.G.3    Maller, J.L.4
  • 26
    • 0028304675 scopus 로고
    • Type 1 protein phosphatase acts in opposition to IpL1 protein kinase in regulating yeast chromosome segregation
    • Francisco, L., Wang, W. and Chan, C. S. (1994). Type 1 protein phosphatase acts in opposition to IpL1 protein kinase in regulating yeast chromosome segregation. Mol. Cell. Biol. 14, 4731-4740.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 4731-4740
    • Francisco, L.1    Wang, W.2    Chan, C.S.3
  • 27
    • 0029046603 scopus 로고
    • Modulation of chromatin folding by histone acetylation
    • Garcia-Ramirez, M., Rocchini, C. and Ausio, J. (1995). Modulation of chromatin folding by histone acetylation. J. Biol. Chem. 270, 17923-17928.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17923-17928
    • Garcia-Ramirez, M.1    Rocchini, C.2    Ausio, J.3
  • 28
    • 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
    • Giet, R. and Glover, D. M. (2001). 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. 152, 669-682.
    • (2001) J. Cell Biol. , vol.152 , pp. 669-682
    • Giet, R.1    Glover, D.M.2
  • 29
    • 0033226802 scopus 로고    scopus 로고
    • Aurora/Ipl1p-related kinases, a new oncogenic family of mitotic serine-threonine kinases
    • Giet, R. and Prigent, C. (1999). Aurora/Ipl1p-related kinases, a new oncogenic family of mitotic serine-threonine kinases. J. Cell Sci. 112, 3591-3601.
    • (1999) J. Cell Sci. , vol.112 , pp. 3591-3601
    • Giet, R.1    Prigent, C.2
  • 30
    • 0028938482 scopus 로고
    • Mutations in aurora prevent centrosome spearation leading to the formation of moonopolar spindles
    • Glover, D. M., Leibovitz, M. H., McLean, D. A. and Parry, H. (1995). Mutations in aurora prevent centrosome spearation leading to the formation of moonopolar spindles. Cell 81, 95-105.
    • (1995) Cell , vol.81 , pp. 95-105
    • Glover, D.M.1    Leibovitz, M.H.2    McLean, D.A.3    Parry, H.4
  • 31
    • 0030876766 scopus 로고    scopus 로고
    • A novel mammalian, mitotic spindle-associated kinase is related to yeast and fly chromosome segregation regulators
    • Gopalan, G., Chan, C. S. and Donovan, P. J. (1997). A novel mammalian, mitotic spindle-associated kinase is related to yeast and fly chromosome segregation regulators. J. Cell Biol. 138, 643-656.
    • (1997) J. Cell Biol. , vol.138 , pp. 643-656
    • Gopalan, G.1    Chan, C.S.2    Donovan, P.J.3
  • 33
    • 0036158780 scopus 로고    scopus 로고
    • Aurora-B phosphorylates Histone H3 at serine28 with regard to the mitotic chromosome condensation
    • Goto, H., Yasui, Y., Nigg, E. A. and Inagaki, M. (2002). Aurora-B phosphorylates Histone H3 at serine28 with regard to the mitotic chromosome condensation. Genes Cells 7, 11-17.
    • (2002) Genes Cells , vol.7 , pp. 11-17
    • Goto, H.1    Yasui, Y.2    Nigg, E.A.3    Inagaki, M.4
  • 34
    • 0014206261 scopus 로고
    • Tissue specificity of histone phosphorylation
    • Gutierrez, R. M. and Hnilica, L. S. (1967). Tissue specificity of histone phosphorylation. Science 157, 1324-1325.
    • (1967) Science , vol.157 , pp. 1324-1325
    • Gutierrez, R.M.1    Hnilica, L.S.2
  • 35
    • 0035962664 scopus 로고    scopus 로고
    • Histone H3 phosphorylation and cell division
    • Hans, F. and Dimitrov, S. (2001). Histone H3 phosphorylation and cell division. Oncogene 20, 3021-3027.
    • (2001) Oncogene , vol.20 , pp. 3021-3027
    • Hans, F.1    Dimitrov, S.2
  • 36
    • 0038746733 scopus 로고    scopus 로고
    • The small molecule Hesperidin reveals a role for Aurora-B in correcting kinetochore-microtubule attachment and in maintaining the spindle assembly checkpoint
    • Hauf, S., Cole, R. W., LaTerra, S., Zimmer, C., Schnapp, G., Walter, R., Heckel, A., van Meel, J., Rieder, C. L. and Peters, J. M. (2003). The small molecule Hesperidin reveals a role for Aurora-B in correcting kinetochore-microtubule attachment and in maintaining the spindle assembly checkpoint. J. Cell Biol. 161, 281-294.
    • (2003) J. Cell Biol. , vol.161 , pp. 281-294
    • Hauf, S.1    Cole, R.W.2    LaTerra, S.3    Zimmer, C.4    Schnapp, G.5    Walter, R.6    Heckel, A.7    van Meel, J.8    Rieder, C.L.9    Peters, J.M.10
  • 37
    • 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
    • Hendzel, M. J., Wei, Y., Mancini, M. A., van Hooser, A., Ranalli, T., Brinkley, B. R., Bazett-Jones, D. P. and Allis, C. D. (1997). 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 106, 348-360.
    • (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
  • 39
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • Jenuwein, T. and Allis, C. D. (2001). Translating the histone code. Science 293, 1074-1080.
    • (2001) Science , vol.293 , pp. 1074-1080
    • Jenuwein, T.1    Allis, C.D.2
  • 40
    • 0033786116 scopus 로고    scopus 로고
    • Phosphorylation of histone H3 is correlated with changes in the maintenance of sister chromatid cohesion during meiosis in maize, rather than the condensation of the chromatin
    • Kaszas, E. and Cande, W. Z. (2000). Phosphorylation of histone H3 is correlated with changes in the maintenance of sister chromatid cohesion during meiosis in maize, rather than the condensation of the chromatin. J. Cell Sci. 113, 3217-3226.
    • (2000) J. Cell Sci. , vol.113 , pp. 3217-3226
    • Kaszas, E.1    Cande, W.Z.2
  • 41
    • 0035824660 scopus 로고    scopus 로고
    • Interaction and feedback regulation between STK15/BTAK/Aurora-A kinase and protein phosphatase 1 through mitotic cell division cycle
    • Katayama, H., Zhou, H., Li, Q., Tatsuka, M. and Sen, S. (2001). Interaction and feedback regulation between STK15/BTAK/Aurora-A kinase and protein phosphatase 1 through mitotic cell division cycle. J. Biol. Chem. 276, 46219-46224.
    • (2001) J. Biol. Chem. , vol.276 , pp. 46219-46224
    • Katayama, H.1    Zhou, H.2    Li, Q.3    Tatsuka, M.4    Sen, S.5
  • 42
    • 0034710919 scopus 로고    scopus 로고
    • Dual roles of the 11S regulatory subcomplex in condensin functions
    • Kimura, K. and Hirano, T. (2000). Dual roles of the 11S regulatory subcomplex in condensin functions. Proc. Natl. Acad. Sci. USA 97, 11972-11977.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 11972-11977
    • Kimura, K.1    Hirano, T.2
  • 43
    • 0014349655 scopus 로고
    • Histone phosphorylation: Stimulation by adenosine 3′,5′-monophosphate
    • Langan, T. A. (1968). Histone phosphorylation: stimulation by adenosine 3′,5′-monophosphate. Science 162, 579-580.
    • (1968) Science , vol.162 , pp. 579-580
    • Langan, T.A.1
  • 44
    • 0036255653 scopus 로고    scopus 로고
    • Phosphorylation of histone H3 is functionally linked to retinoic acid receptor beta promoter activation
    • Lefebvre, B., Ozato, K. and Lefebvre, P. (2002). Phosphorylation of histone H3 is functionally linked to retinoic acid receptor beta promoter activation. EMBO Rep. 3, 335-340.
    • (2002) EMBO Rep. , vol.3 , pp. 335-340
    • Lefebvre, B.1    Ozato, K.2    Lefebvre, P.3
  • 45
    • 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 14
    • 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 14. 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
  • 46
    • 0035839135 scopus 로고    scopus 로고
    • Snf1 - A histone kinase that works in concert with histone acetytranferase Gcn5 to regulate transcription
    • Lo, W. S., Duggan, L., Tolga, N. C., Emre, Belotserkovskya, R., Lane, W. S., Shiekhattar, R. and Berger, S. L. (2001). Snf1 - a histone kinase that works in concert with histone acetytranferase Gcn5 to regulate transcription. Science 293, 1142-1146.
    • (2001) Science , vol.293 , pp. 1142-1146
    • Lo, W.S.1    Duggan, L.2    Tolga, N.C.3    Emre, A.4    Belotserkovskya, R.5    Lane, W.S.6    Shiekhattar, R.7    Berger, S.L.8
  • 47
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 A resolution
    • Luger, K., Mader, A. W., Richmond, R. K., Sargent, D. F. and Richmond, T. J. (1997). Crystal structure of the nucleosome core particle at 2.8 A resolution. Nature 389, 251-260.
    • (1997) Nature , vol.389 , pp. 251-260
    • Luger, K.1    Mader, A.W.2    Richmond, R.K.3    Sargent, D.F.4    Richmond, T.J.5
  • 48
    • 0036153807 scopus 로고    scopus 로고
    • ISWI remodeling complexes in Xenopus egg extracts: Identification as major chromosomal components that are regulated by INCENP-aurora B
    • MacCallum, D. E., Losada, A., Kobayashi, R. and Hirano, T. (2002). ISWI remodeling complexes in Xenopus egg extracts: identification as major chromosomal components that are regulated by INCENP-aurora B. Mol. Biol. Cell 13, 25-39.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 25-39
    • MacCallum, D.E.1    Losada, A.2    Kobayashi, R.3    Hirano, T.4
  • 49
    • 0021112111 scopus 로고
    • Histone hyperacetylation has little effect on the higher order folding of chromatin
    • McGhee, J. D., Nickol, J. M., Felsenfeld, J. and Rau, D. C. (1983). Histone hyperacetylation has little effect on the higher order folding of chromatin. Nucleic Acids Res. 11, 4065-4075.
    • (1983) Nucleic Acids Res. , vol.11 , pp. 4065-4075
    • McGhee, J.D.1    Nickol, J.M.2    Felsenfeld, J.3    Rau, D.C.4
  • 50
    • 0034813107 scopus 로고    scopus 로고
    • Mitogen-regulated RSK2-CBP interaction cntrols their kinase and acetylase activities
    • Merienne, K., Pannetiers, S., Harel-Bellan, A. and Sassone-Corsi, P. (2001). Mitogen-regulated RSK2-CBP interaction cntrols their kinase and acetylase activities. Mol. Cell. Biol. 21, 7089-7096.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 7089-7096
    • Merienne, K.1    Pannetiers, S.2    Harel-Bellan, A.3    Sassone-Corsi, P.4
  • 51
    • 0035854776 scopus 로고    scopus 로고
    • Chromatin-associated protein phosphatase 1 regulates aurora-B and histone H3 phosphorylation
    • Murnion, M. E., Adams, R. R., Callister, D. M., Allis, C. D., Earnshaw, W. C. and Swedlow, J. R. (2001). Chromatin-associated protein phosphatase 1 regulates aurora-B and histone H3 phosphorylation. J. Biol. Chem. 276, 26656-26665.
    • (2001) J. Biol. Chem. , vol.276 , pp. 26656-26665
    • Murnion, M.E.1    Adams, R.R.2    Callister, D.M.3    Allis, C.D.4    Earnshaw, W.C.5    Swedlow, J.R.6
  • 52
    • 0031741231 scopus 로고    scopus 로고
    • Persistent interactions of core histone tails with nucleosomal DNA following acetylation and transcription factor binding
    • Mutskov, V., Gerber, D., Angelov, D., Ausio, J., Workman, J. and Dimitrov, S. (1998). Persistent interactions of core histone tails with nucleosomal DNA following acetylation and transcription factor binding. Mol. Cell. Biol. 18, 6293-6304.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 6293-6304
    • Mutskov, V.1    Gerber, D.2    Angelov, D.3    Ausio, J.4    Workman, J.5    Dimitrov, S.6
  • 53
    • 0033639243 scopus 로고    scopus 로고
    • Phosphorylation of histone H3 correlates with transcriptionally active loci
    • Nowak, S. J. and Corces, V. G. (2000). Phosphorylation of histone H3 correlates with transcriptionally active loci. Genes Dev. 14, 3003-3013.
    • (2000) Genes Dev. , vol.14 , pp. 3003-3013
    • Nowak, S.J.1    Corces, V.G.2
  • 54
    • 0035844871 scopus 로고    scopus 로고
    • Functional analysis of kinetochore assembly in Caenorhabditis elegans
    • Oegema, K., Desai, A., Rybina, S., Kirkham, M. and Hyman, A. A. (2001). Functional analysis of kinetochore assembly in Caenorhabditis elegans. J. Cell Biol. 153, 1209-1226.
    • (2001) J. Cell Biol. , vol.153 , pp. 1209-1226
    • Oegema, K.1    Desai, A.2    Rybina, S.3    Kirkham, M.4    Hyman, A.A.5
  • 55
    • 0024294395 scopus 로고
    • Mitotic induction and maintenance by overexpression of a G2-specific gene that encodes a potential protein kinase
    • Osmani, S. A., Pu, R. T. and Morris, N. R. (1988). Mitotic induction and maintenance by overexpression of a G2-specific gene that encodes a potential protein kinase. Cell 53, 237-244.
    • (1988) Cell , vol.53 , pp. 237-244
    • Osmani, S.A.1    Pu, R.T.2    Morris, N.R.3
  • 56
    • 0025740935 scopus 로고
    • Crosslinking proteins to nucleic acids by ultraviolet laser irradiation
    • Pashev, I. G., Dimitrov, S. I. and Angelov, D. (1991). Crosslinking proteins to nucleic acids by ultraviolet laser irradiation. Trends Biochem. Sci. 16, 323-326.
    • (1991) Trends Biochem. Sci. , vol.16 , pp. 323-326
    • Pashev, I.G.1    Dimitrov, S.I.2    Angelov, D.3
  • 57
    • 0035694554 scopus 로고    scopus 로고
    • The S. pombe aurora-related kinase Ark1 associates with mitotic structures in a stage dependent manner and is required for chromosome segregation
    • Petersen, J., Paris, J., Willer, M., Philippe, M. and Hagan, I. M. (2001). The S. pombe aurora-related kinase Ark1 associates with mitotic structures in a stage dependent manner and is required for chromosome segregation. J. Cell Sci. 114, 4371-4384.
    • (2001) J. Cell Sci. , vol.114 , pp. 4371-4384
    • Petersen, J.1    Paris, J.2    Willer, M.3    Philippe, M.4    Hagan, I.M.5
  • 59
    • 0032802553 scopus 로고    scopus 로고
    • Cloning, mapping, and expression of ial, a novel Drosophila member of the Ipl1/aurora mitotic control kinase family
    • Reich, A., Yanai, A., Mesilaty-Gross, S., Chen-Moses, A., Wides, R. and Motro, B. (1999). Cloning, mapping, and expression of ial, a novel Drosophila member of the Ipl1/aurora mitotic control kinase family. DNA Cell Biol 18, 593-603.
    • (1999) DNA Cell Biol. , vol.18 , pp. 593-603
    • Reich, A.1    Yanai, A.2    Mesilaty-Gross, S.3    Chen-Moses, A.4    Wides, R.5    Motro, B.6
  • 60
    • 0034864042 scopus 로고    scopus 로고
    • Chromatin assembly and organization
    • Ridgway, P. and Almouzni, G. (2001). Chromatin assembly and organization. J. Cell Sci. 114, 2711-2712.
    • (2001) J. Cell Sci. , vol.114 , pp. 2711-2712
    • Ridgway, P.1    Almouzni, G.2
  • 61
    • 0037092044 scopus 로고    scopus 로고
    • The aurora kinase AIR-2 functions in the release of chromosome cohesion in Caenorhabditis elegans meiosis
    • Rogers, E., Bishop, J. D., Waddle, J. A., Schumacher, J. M. and Lin, R. (2002). The aurora kinase AIR-2 functions in the release of chromosome cohesion in Caenorhabditis elegans meiosis. J. Cell Biol. 157, 219-229.
    • (2002) J. Cell Biol. , vol.157 , pp. 219-229
    • Rogers, E.1    Bishop, J.D.2    Waddle, J.A.3    Schumacher, J.M.4    Lin, R.5
  • 62
    • 0036645394 scopus 로고    scopus 로고
    • Nercc1, a mammalian NIMA-family kinase, binds the ran GTPase and regulates mitotic progression
    • Roig, J., Mikhailov, A., Belham, C. and Avruch, J. (2002). Nercc1, a mammalian NIMA-family kinase, binds the ran GTPase and regulates mitotic progression. Genes Dev. 16, 1640-1658.
    • (2002) Genes Dev. , vol.16 , pp. 1640-1658
    • Roig, J.1    Mikhailov, A.2    Belham, C.3    Avruch, J.4
  • 63
    • 0036143654 scopus 로고    scopus 로고
    • p38-Dependent marking of inflammatory genes for increased NF-kappa B recruitment
    • Saccani, S., Pantano, S. and Natoli, G. (2002). p38-Dependent marking of inflammatory genes for increased NF-kappa B recruitment. Nat. Immunol. 3, 69-75.
    • (2002) Nat. Immunol. , vol.3 , pp. 69-75
    • Saccani, S.1    Pantano, S.2    Natoli, G.3
  • 66
    • 0345299208 scopus 로고    scopus 로고
    • Phosphorylation-induced rearrangement of the histone H3 NH2-terminal domain during mitotic chromosome condensation
    • Sauve, D. M., Anderson, H. J., Ray, J. M., James, W. M. and Roberge, M. (1999). Phosphorylation-induced rearrangement of the histone H3 NH2-terminal domain during mitotic chromosome condensation. J. Cell Biol. 145, 225-235.
    • (1999) J. Cell Biol. , vol.145 , pp. 225-235
    • Sauve, D.M.1    Anderson, H.J.2    Ray, J.M.3    James, W.M.4    Roberge, M.5
  • 67
    • 0037042207 scopus 로고    scopus 로고
    • Histone H3 phosphorylation during Xenopus oocyte maturation: Regulation by the MAP kinase/p90Rsk pathway and uncoupling from DNA condensation
    • Schmitt, A., Gutierrez, G. J., Lenart, P., Ellenberg, J. and Nebreda, A. R. (2002). Histone H3 phosphorylation during Xenopus oocyte maturation: regulation by the MAP kinase/p90Rsk pathway and uncoupling from DNA condensation. FEBS Lett. 518, 23-28.
    • (2002) FEBS Lett. , vol.518 , pp. 23-28
    • Schmitt, A.1    Gutierrez, G.J.2    Lenart, P.3    Ellenberg, J.4    Nebreda, A.R.5
  • 68
    • 0031673072 scopus 로고    scopus 로고
    • A highly conserved centrosomal kinase, AIR-1, is required for accurate cell cycle progression and segregation of developmental factors in Caenorhabditis elegans embryos
    • Schumacher, J. M., Ashcroft, N., Donovan, P. J. and Golden, A. (1998a). A highly conserved centrosomal kinase, AIR-1, is required for accurate cell cycle progression and segregation of developmental factors in Caenorhabditis elegans embryos. Development 125, 4391-4402.
    • (1998) Development , vol.125 , pp. 4391-4402
    • Schumacher, J.M.1    Ashcroft, N.2    Donovan, P.J.3    Golden, A.4
  • 69
    • 0032517860 scopus 로고    scopus 로고
    • AIR-2: An Aurora/Ipl1-related protein kinase associated with chromosomes and midbody microtubules is required for polar body extrusion and cytokinesis in Caenorhabditis elegans embryos
    • Schumacher, J. M., Golden, A. and Donovan, P. J. (1998b). AIR-2: An Aurora/Ipl1-related protein kinase associated with chromosomes and midbody microtubules is required for polar body extrusion and cytokinesis in Caenorhabditis elegans embryos. J. Cell Biol. 143, 1635-1646.
    • (1998) J. Cell Biol. , vol.143 , pp. 1635-1646
    • Schumacher, J.M.1    Golden, A.2    Donovan, P.J.3
  • 70
    • 0035839605 scopus 로고    scopus 로고
    • pEg2 aurora-A kinase, histone H3 phosphorylation, and chromosome assembly in Xenopus egg extract
    • Scrittori, L., Hans, F., Angelov, D., Charra, M., Prigent, C. and Dimitrov, S. (2001). pEg2 aurora-A kinase, histone H3 phosphorylation, and chromosome assembly in Xenopus egg extract. J. Biol. Chem. 276, 30002-30010.
    • (2001) J. Biol. Chem. , vol.276 , pp. 30002-30010
    • Scrittori, L.1    Hans, F.2    Angelov, D.3    Charra, M.4    Prigent, C.5    Dimitrov, S.6
  • 71
    • 0025061915 scopus 로고
    • Mitosis-specific histone H3 phosphorylation in vitro in nucleosome structures
    • Shibata, K., Inagaki, M. and Ajiro, K. (1990). Mitosis-specific histone H3 phosphorylation in vitro in nucleosome structures. Eur. J. Biochem. 192, 87-93.
    • (1990) Eur. J. Biochem. , vol.192 , pp. 87-93
    • Shibata, K.1    Inagaki, M.2    Ajiro, K.3
  • 72
    • 0018144234 scopus 로고
    • An H3 histone-specific kinase isolated from bovine thymus chromatin
    • Shoemaker, C. B. and Chalkley, R. (1978). An H3 histone-specific kinase isolated from bovine thymus chromatin. J. Biol. Chem. 252, 5802-5807.
    • (1978) J. Biol. Chem. , vol.252 , pp. 5802-5807
    • Shoemaker, C.B.1    Chalkley, R.2
  • 73
    • 0033637849 scopus 로고    scopus 로고
    • The survivin-like C. elegans BIR-1 protein acts with the Aurora-like kinase AIR-2 to affect chromosomes and the spindle midzone
    • Speliotes, E. K., Uren, A., Vaux, D. and Horvitz, H. R. (2000). The survivin-like C. elegans BIR-1 protein acts with the Aurora-like kinase AIR-2 to affect chromosomes and the spindle midzone. Mol. Cell 6, 211-223.
    • (2000) Mol. Cell , vol.6 , pp. 211-223
    • Speliotes, E.K.1    Uren, A.2    Vaux, D.3    Horvitz, H.R.4
  • 74
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications
    • Strahl, B. D. and Allis, C. D. (2000). The language of covalent histone modifications. Nature 403, 41-45.
    • (2000) Nature , vol.403 , pp. 41-45
    • Strahl, B.D.1    Allis, C.D.2
  • 76
    • 0020315745 scopus 로고
    • The in vitro phosphorylation of chromatin by the catalytic subunit of cAMP-dependent protein kinase
    • Taylor, S. S. (1982). The in vitro phosphorylation of chromatin by the catalytic subunit of cAMP-dependent protein kinase. J. Biol. Chem. 257, 6056-6063.
    • (1982) J. Biol. Chem. , vol.257 , pp. 6056-6063
    • Taylor, S.S.1
  • 77
    • 0032472915 scopus 로고    scopus 로고
    • AIM-1: A mammalian midbody-associated protein required for cytokinesis
    • Terada, Y., Tatsuka, M., Suzuki, F., Yasuda, Y., Fujita, S. and Otsu, M. (1998). AIM-1: a mammalian midbody-associated protein required for cytokinesis. EMBO J. 17, 667-676.
    • (1998) EMBO J. , vol.17 , pp. 667-676
    • Terada, Y.1    Tatsuka, M.2    Suzuki, F.3    Yasuda, Y.4    Fujita, S.5    Otsu, M.6
  • 78
    • 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
    • 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. EMBO J. 18, 4779-4793.
    • (1999) EMBO J. , vol.18 , 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
  • 81
    • 0003903126 scopus 로고
    • Berlin, Germany: Springer-Verlag
    • van Holde, K. (1988). Chromatin. Berlin, Germany: Springer-Verlag.
    • (1988) Chromatin
    • van Holde, K.1
  • 82
    • 0032442522 scopus 로고    scopus 로고
    • Histone H3 phosphorylation is required for the initiation, but not maintenance, of mammalian chromosome condensation
    • Van Hooser, A., Goodrich, D. W., Allis, C. D., Brinkley, B. R. and Mancini, M. A. (1998). Histone H3 phosphorylation is required for the initiation, but not maintenance, of mammalian chromosome condensation. J. Cell Sci. 111, 3497-3506.
    • (1998) J. Cell Sci. , vol.111 , pp. 3497-3506
    • Van Hooser, A.1    Goodrich, D.W.2    Allis, C.D.3    Brinkley, B.R.4    Mancini, M.A.5
  • 83
    • 0030871855 scopus 로고    scopus 로고
    • Apoptosis induced by gliotoxin is preceded by phosphorylation of histone H3 and enhanced sensitivity of chromatin to nuclease digestion
    • Waring, P., Khan, T. and Sjaarda, A. (1997). Apoptosis induced by gliotoxin is preceded by phosphorylation of histone H3 and enhanced sensitivity of chromatin to nuclease digestion. J. Biol. Chem. 272, 17929-17936.
    • (1997) J. Biol. Chem. , vol.272 , pp. 17929-17936
    • Waring, P.1    Khan, T.2    Sjaarda, A.3
  • 84
    • 0032560517 scopus 로고    scopus 로고
    • Phosphorylation of histone H3 at serine 10 is correlated with chromosome condensation during mitosis and meiosis in Tetrahymena
    • Wei, Y., Mizzen, C. A., Cook, R. G., Gorovsky, M. A. and Allis, C. D. (1998). Phosphorylation of histone H3 at serine 10 is correlated with chromosome condensation during mitosis and meiosis in Tetrahymena. Proc. Natl. Acad. Sci. USA 95, 7480-7484.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 7480-7484
    • Wei, Y.1    Mizzen, C.A.2    Cook, R.G.3    Gorovsky, M.A.4    Allis, C.D.5
  • 85
    • 0033515426 scopus 로고    scopus 로고
    • Phosphorylation of histone H3 is required for proper chromosome condensation and segregation
    • Wei, Y., Yu, L., Bowen, J., Gorovsky, M. A. and Allis, C. D. (1999). Phosphorylation of histone H3 is required for proper chromosome condensation and segregation. Cell 97, 99-109.
    • (1999) Cell , vol.97 , pp. 99-109
    • Wei, Y.1    Yu, L.2    Bowen, J.3    Gorovsky, M.A.4    Allis, C.D.5
  • 86
    • 0035313770 scopus 로고    scopus 로고
    • Higher-order structure of chromatin and chromosomes
    • Woodcock, C. L. and Dimitrov, S. (2001). Higher-order structure of chromatin and chromosomes. Curr. Opin. Genet. Dev. 11, 130-135.
    • (2001) Curr. Opin. Genet. Dev. , vol.11 , pp. 130-135
    • Woodcock, C.L.1    Dimitrov, S.2
  • 87
    • 0018830636 scopus 로고
    • Glucocorticoid-induced thymocyte apoptosis is associated with endogenous endonuclease activation
    • Wyllie, A. H. (1980). Glucocorticoid-induced thymocyte apoptosis is associated with endogenous endonuclease activation. Nature 284, 555-556.
    • (1980) Nature , vol.284 , pp. 555-556
    • Wyllie, A.H.1
  • 88
    • 0038511129 scopus 로고    scopus 로고
    • Histone H3 phosphorylation by IKK-alpha is critical for cytokine-induced gene expression
    • Yamamoto, Y., Verma, U. N., Prajapati, S., Kwak, Y. T. and Gaynor, R. B. (2003). Histone H3 phosphorylation by IKK-alpha is critical for cytokine-induced gene expression. Nature 423, 655-659.
    • (2003) Nature , vol.423 , pp. 655-659
    • Yamamoto, Y.1    Verma, U.N.2    Prajapati, S.3    Kwak, Y.T.4    Gaynor, R.B.5
  • 89
    • 0028904124 scopus 로고
    • The NIMA protein kinase is hyperphosphorylated and activated downstream of p34cdc2/cyclin B: Coordination of two mitosis promoting kinases
    • Ye, X. S., Xu, G., Pu, R. T., Fincher, R. R., McGuire, S. L., Osmani, A. H. and Osmani, S. A. (1995). The NIMA protein kinase is hyperphosphorylated and activated downstream of p34cdc2/cyclin B: coordination of two mitosis promoting kinases. EMBO J. 14, 986-994.
    • (1995) EMBO J. , vol.14 , pp. 986-994
    • Ye, X.S.1    Xu, G.2    Pu, R.T.3    Fincher, R.R.4    McGuire, S.L.5    Osmani, A.H.6    Osmani, S.A.7
  • 90
    • 0031148580 scopus 로고    scopus 로고
    • Biochemical differences between staurosporine-induced apoptosis and premature mitosis
    • Yoshida, M., Usui, T., Tsujimura, K., Inagaki, M., Beppu, T. and Horinouchi, S. (1997). Biochemical differences between staurosporine-induced apoptosis and premature mitosis. Exp. Cell Res. 232, 225-239.
    • (1997) Exp. Cell Res. , vol.232 , pp. 225-239
    • Yoshida, M.1    Usui, T.2    Tsujimura, K.3    Inagaki, M.4    Beppu, T.5    Horinouchi, S.6
  • 91
    • 0035945340 scopus 로고    scopus 로고
    • CENP-A is phosphorylated by Aurora B kinase and plays an unexpected role in completion of cytokinesis
    • Zeitlin, S. G., Shelby, R. D. and Sullivan, K. F. (2001). CENP-A is phosphorylated by Aurora B kinase and plays an unexpected role in completion of cytokinesis. J. Cell Biol. 155, 1147-1157.
    • (2001) J. Cell Biol. , vol.155 , pp. 1147-1157
    • Zeitlin, S.G.1    Shelby, R.D.2    Sullivan, K.F.3
  • 92
    • 0034647733 scopus 로고    scopus 로고
    • ERKs and p38 kinases mediate ultraviolet B-induced phosphorylation of histone H3 at serine 10
    • Zhong, S. P., Ma, W. Y. and Dong, Z. (2000). ERKs and p38 kinases mediate ultraviolet B-induced phosphorylation of histone H3 at serine 10. J. Biol. Chem. 275, 20980-20984.
    • (2000) J. Biol. Chem. , vol.275 , pp. 20980-20984
    • Zhong, S.P.1    Ma, W.Y.2    Dong, Z.3
  • 93
    • 0031714080 scopus 로고    scopus 로고
    • Tumour amplified kinase STK15/BTAK induces centrosome amplification, aneuploidy and transformation
    • Zhou, H., Kuang, J., Zhong, L., Kuo, W. L., Gray, J. W., Sahin, A., Brinkley, B. R. and Sen, S. (1998). Tumour amplified kinase STK15/BTAK induces centrosome amplification, aneuploidy and transformation. Nat. Genet. 20, 189-193.
    • (1998) Nat. Genet. , vol.20 , pp. 189-193
    • Zhou, H.1    Kuang, J.2    Zhong, L.3    Kuo, W.L.4    Gray, J.W.5    Sahin, A.6    Brinkley, B.R.7    Sen, S.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.