메뉴 건너뛰기




Volumn 1829, Issue 1, 2013, Pages 84-97

Transcription-associated histone modifications and cryptic transcription

Author keywords

Chromatin remodeling; Histone chaperone; Histone modifying enzyme; Intragenic transcription; RNA polymerase II; Transcription elongation

Indexed keywords

CHAPERONE; HISTONE ACETYLTRANSFERASE; HISTONE H2AZ; RNA POLYMERASE II;

EID: 84872398729     PISSN: 18749399     EISSN: 18764320     Source Type: Journal    
DOI: 10.1016/j.bbagrm.2012.08.008     Document Type: Review
Times cited : (160)

References (315)
  • 1
    • 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., Richmond T.J. Crystal structure of the nucleosome core particle at 2.8 A resolution. Nature 1997, 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
  • 2
    • 0015964401 scopus 로고
    • Spheroid chromatin units (v bodies)
    • Olins A.L., Olins D.E. Spheroid chromatin units (v bodies). Science 1974, 183:330-332.
    • (1974) Science , vol.183 , pp. 330-332
    • Olins, A.L.1    Olins, D.E.2
  • 3
    • 0026733468 scopus 로고
    • A nucleosome core is transferred out of the path of a transcribing polymerase
    • Clark D.J., Felsenfeld G. A nucleosome core is transferred out of the path of a transcribing polymerase. Cell 1992, 71:11-22.
    • (1992) Cell , vol.71 , pp. 11-22
    • Clark, D.J.1    Felsenfeld, G.2
  • 4
    • 0031451329 scopus 로고    scopus 로고
    • Mechanism of transcription through the nucleosome by eukaryotic RNA polymerase
    • Studitsky V.M., Kassavetis G.A., Geiduschek E.P., Felsenfeld G. Mechanism of transcription through the nucleosome by eukaryotic RNA polymerase. Science 1997, 278:1960-1963.
    • (1997) Science , vol.278 , pp. 1960-1963
    • Studitsky, V.M.1    Kassavetis, G.A.2    Geiduschek, E.P.3    Felsenfeld, G.4
  • 5
    • 78650566210 scopus 로고    scopus 로고
    • Pol II waiting in the starting gates: regulating the transition from transcription initiation into productive elongation
    • Nechaev S., Adelman K. Pol II waiting in the starting gates: regulating the transition from transcription initiation into productive elongation. Biochim. Biophys. Acta 2011, 1809:34-45.
    • (2011) Biochim. Biophys. Acta , vol.1809 , pp. 34-45
    • Nechaev, S.1    Adelman, K.2
  • 6
    • 67650725820 scopus 로고    scopus 로고
    • The biology of chromatin remodeling complexes
    • Clapier C.R., Cairns B.R. The biology of chromatin remodeling complexes. Annu. Rev. Biochem. 2009, 78:273-304.
    • (2009) Annu. Rev. Biochem. , vol.78 , pp. 273-304
    • Clapier, C.R.1    Cairns, B.R.2
  • 7
    • 78049246250 scopus 로고    scopus 로고
    • Fast signals and slow marks: the dynamics of histone modifications
    • Barth T.K., Imhof A. Fast signals and slow marks: the dynamics of histone modifications. Trends Biochem. Sci. 2010, 35:618-626.
    • (2010) Trends Biochem. Sci. , vol.35 , pp. 618-626
    • Barth, T.K.1    Imhof, A.2
  • 8
    • 15444376394 scopus 로고    scopus 로고
    • Replication-independent core histone dynamics at transcriptionally active loci in vivo
    • Thiriet C., Hayes J.J. Replication-independent core histone dynamics at transcriptionally active loci in vivo. Genes Dev. 2005, 19:677-682.
    • (2005) Genes Dev. , vol.19 , pp. 677-682
    • Thiriet, C.1    Hayes, J.J.2
  • 9
    • 33846663256 scopus 로고    scopus 로고
    • Continuous histone H2B and transcription-dependent histone H3 exchange in yeast cells outside of replication
    • Jamai A., Imoberdorf R.M., Strubin M. Continuous histone H2B and transcription-dependent histone H3 exchange in yeast cells outside of replication. Mol. Cell 2007, 25:345-355.
    • (2007) Mol. Cell , vol.25 , pp. 345-355
    • Jamai, A.1    Imoberdorf, R.M.2    Strubin, M.3
  • 10
    • 33947137710 scopus 로고    scopus 로고
    • Dynamics of replication-independent histone turnover in budding yeast
    • Dion M.F., Kaplan T., Kim M., Buratowski S., Friedman N., Rando O.J. Dynamics of replication-independent histone turnover in budding yeast. Science 2007, 315:1405-1408.
    • (2007) Science , vol.315 , pp. 1405-1408
    • Dion, M.F.1    Kaplan, T.2    Kim, M.3    Buratowski, S.4    Friedman, N.5    Rando, O.J.6
  • 11
    • 34547277498 scopus 로고    scopus 로고
    • Genome-wide replication-independent histone H3 exchange occurs predominantly at promoters and implicates H3 K56 acetylation and Asf1
    • Rufiange A., Jacques P.E., Bhat W., Robert F., Nourani A. Genome-wide replication-independent histone H3 exchange occurs predominantly at promoters and implicates H3 K56 acetylation and Asf1. Mol. Cell 2007, 27:393-405.
    • (2007) Mol. Cell , vol.27 , pp. 393-405
    • Rufiange, A.1    Jacques, P.E.2    Bhat, W.3    Robert, F.4    Nourani, A.5
  • 12
    • 0036203807 scopus 로고    scopus 로고
    • Nucleosome remodeling induced by RNA polymerase II: loss of the H2A/H2B dimer during transcription
    • Kireeva M.L., Walter W., Tchernajenko V., Bondarenko V., Kashlev M., Studitsky V.M. Nucleosome remodeling induced by RNA polymerase II: loss of the H2A/H2B dimer during transcription. Mol. Cell 2002, 9:541-552.
    • (2002) Mol. Cell , vol.9 , pp. 541-552
    • Kireeva, M.L.1    Walter, W.2    Tchernajenko, V.3    Bondarenko, V.4    Kashlev, M.5    Studitsky, V.M.6
  • 14
    • 10644222646 scopus 로고    scopus 로고
    • The histone chaperone Asf1p mediates global chromatin disassembly in vivo
    • Adkins M.W., Tyler J.K. The histone chaperone Asf1p mediates global chromatin disassembly in vivo. J. Biol. Chem. 2004, 279:52069-52074.
    • (2004) J. Biol. Chem. , vol.279 , pp. 52069-52074
    • Adkins, M.W.1    Tyler, J.K.2
  • 15
    • 33646141366 scopus 로고    scopus 로고
    • Asf1 mediates histone eviction and deposition during elongation by RNA polymerase II
    • Schwabish M.A., Struhl K. Asf1 mediates histone eviction and deposition during elongation by RNA polymerase II. Mol. Cell 2006, 22:415-422.
    • (2006) Mol. Cell , vol.22 , pp. 415-422
    • Schwabish, M.A.1    Struhl, K.2
  • 16
    • 15544369061 scopus 로고    scopus 로고
    • Distinct activities of CHD1 and ACF in ATP-dependent chromatin assembly
    • Lusser A., Urwin D.L., Kadonaga J.T. Distinct activities of CHD1 and ACF in ATP-dependent chromatin assembly. Nat. Struct. Mol. Biol. 2005, 12:160-166.
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 160-166
    • Lusser, A.1    Urwin, D.L.2    Kadonaga, J.T.3
  • 17
    • 34250831538 scopus 로고    scopus 로고
    • A genome-wide role for CHD remodelling factors and Nap1 in nucleosome disassembly
    • Walfridsson J., Khorosjutina O., Matikainen P., Gustafsson C.M., Ekwall K. A genome-wide role for CHD remodelling factors and Nap1 in nucleosome disassembly. EMBO J. 2007, 26:2868-2879.
    • (2007) EMBO J. , vol.26 , pp. 2868-2879
    • Walfridsson, J.1    Khorosjutina, O.2    Matikainen, P.3    Gustafsson, C.M.4    Ekwall, K.5
  • 18
    • 0242495784 scopus 로고    scopus 로고
    • Replication-independent assembly of nucleosome arrays in a novel yeast chromatin reconstitution system involves antisilencing factor Asf1p and chromodomain protein Chd1p
    • Robinson K.M., Schultz M.C. Replication-independent assembly of nucleosome arrays in a novel yeast chromatin reconstitution system involves antisilencing factor Asf1p and chromodomain protein Chd1p. Mol. Cell. Biol. 2003, 23:7937-7946.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 7937-7946
    • Robinson, K.M.1    Schultz, M.C.2
  • 19
    • 34247619728 scopus 로고    scopus 로고
    • Nap1: taking a closer look at a juggler protein of extraordinary skills
    • Zlatanova J., Seebart C., Tomschik M. Nap1: taking a closer look at a juggler protein of extraordinary skills. FASEB J. 2007, 21:1294-1310.
    • (2007) FASEB J. , vol.21 , pp. 1294-1310
    • Zlatanova, J.1    Seebart, C.2    Tomschik, M.3
  • 21
    • 27144510368 scopus 로고    scopus 로고
    • Genome-scale profiling of histone H3.3 replacement patterns
    • Mito Y., Henikoff J.G., Henikoff S. Genome-scale profiling of histone H3.3 replacement patterns. Nat. Genet. 2005, 37:1090-1097.
    • (2005) Nat. Genet. , vol.37 , pp. 1090-1097
    • Mito, Y.1    Henikoff, J.G.2    Henikoff, S.3
  • 22
    • 77952241644 scopus 로고    scopus 로고
    • New functions for an old variant: no substitute for histone H3.3
    • Elsaesser S.J., Goldberg A.D., Allis C.D. New functions for an old variant: no substitute for histone H3.3. Curr. Opin. Genet. Dev. 2010, 20:110-117.
    • (2010) Curr. Opin. Genet. Dev. , vol.20 , pp. 110-117
    • Elsaesser, S.J.1    Goldberg, A.D.2    Allis, C.D.3
  • 23
    • 0037423930 scopus 로고    scopus 로고
    • Conserved histone variant H2A.Z protects euchromatin from the ectopic spread of silent heterochromatin
    • Meneghini M.D., Wu M., Madhani H.D. Conserved histone variant H2A.Z protects euchromatin from the ectopic spread of silent heterochromatin. Cell 2003, 112:725-736.
    • (2003) Cell , vol.112 , pp. 725-736
    • Meneghini, M.D.1    Wu, M.2    Madhani, H.D.3
  • 24
  • 25
    • 77954670503 scopus 로고    scopus 로고
    • Reconciling the positive and negative roles of histone H2A.Z in gene transcription
    • Marques M., Laflamme L., Gervais A.L., Gaudreau L. Reconciling the positive and negative roles of histone H2A.Z in gene transcription. Epigenetics 2010, 5:267-272.
    • (2010) Epigenetics , vol.5 , pp. 267-272
    • Marques, M.1    Laflamme, L.2    Gervais, A.L.3    Gaudreau, L.4
  • 26
    • 0034721645 scopus 로고    scopus 로고
    • Histone H2A.Z regulats transcription and is partially redundant with nucleosome remodeling complexes
    • Santisteban M.S., Kalashnikova T., Smith M.M. Histone H2A.Z regulats transcription and is partially redundant with nucleosome remodeling complexes. Cell 2000, 103:411-422.
    • (2000) Cell , vol.103 , pp. 411-422
    • Santisteban, M.S.1    Kalashnikova, T.2    Smith, M.M.3
  • 27
    • 0035725036 scopus 로고    scopus 로고
    • H2A.Z is required for global chromatin integrity and for recruitment of RNA polymerase II under specific conditions
    • Adam M., Robert F., Larochelle M., Gaudreau L. H2A.Z is required for global chromatin integrity and for recruitment of RNA polymerase II under specific conditions. Mol. Cell. Biol. 2001, 21:6270-6279.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 6270-6279
    • Adam, M.1    Robert, F.2    Larochelle, M.3    Gaudreau, L.4
  • 28
    • 34047111213 scopus 로고    scopus 로고
    • Translational and rotational settings of H2A.Z nucleosomes across the Saccharomyces cerevisiae genome
    • Albert I., Mavrich T.N., Tomsho L.P., Qi J., Zanton S.J., Schuster S.C., Pugh B.F. Translational and rotational settings of H2A.Z nucleosomes across the Saccharomyces cerevisiae genome. Nature 2007, 446:572-576.
    • (2007) Nature , vol.446 , pp. 572-576
    • Albert, I.1    Mavrich, T.N.2    Tomsho, L.P.3    Qi, J.4    Zanton, S.J.5    Schuster, S.C.6    Pugh, B.F.7
  • 29
    • 29444454191 scopus 로고    scopus 로고
    • Preferential occupancy of histone variant H2AZ at inactive promoters influences local histone modifications and chromatin remodeling
    • Li B., Pattenden S.G., Lee D., Gutierrez J., Chen J., Seidel C., Gerton J., Workman J.L. Preferential occupancy of histone variant H2AZ at inactive promoters influences local histone modifications and chromatin remodeling. Proc. Natl. Acad. Sci. U. S. A. 2005, 102:18385-18390.
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 18385-18390
    • Li, B.1    Pattenden, S.G.2    Lee, D.3    Gutierrez, J.4    Chen, J.5    Seidel, C.6    Gerton, J.7    Workman, J.L.8
  • 30
    • 29144531244 scopus 로고    scopus 로고
    • Variant histone H2A.Z is globally localized to the promoters of inactive yeast genes and regulates nucleosome positioning
    • Guillemette B., Bataille A.R., Gevry N., Adam M., Blanchette M., Robert F., Gaudreau L. Variant histone H2A.Z is globally localized to the promoters of inactive yeast genes and regulates nucleosome positioning. PLoS Biol. 2005, 3:e384.
    • (2005) PLoS Biol. , vol.3
    • Guillemette, B.1    Bataille, A.R.2    Gevry, N.3    Adam, M.4    Blanchette, M.5    Robert, F.6    Gaudreau, L.7
  • 31
    • 26844489856 scopus 로고    scopus 로고
    • Genome-wide dynamics of Htz1, a histone H2A variant that poises repressed/basal promoters for activation through histone loss
    • Zhang H., Roberts D.N., Cairns B.R. Genome-wide dynamics of Htz1, a histone H2A variant that poises repressed/basal promoters for activation through histone loss. Cell 2005, 123:219-231.
    • (2005) Cell , vol.123 , pp. 219-231
    • Zhang, H.1    Roberts, D.N.2    Cairns, B.R.3
  • 35
    • 34247341747 scopus 로고    scopus 로고
    • H2A.Z-mediated localization of genes at the nuclear periphery confers epigenetic memory of previous transcriptional state
    • Brickner D.G., Cajigas I., Fondufe-Mittendorf Y., Ahmed S., Lee P.C., Widom J., Brickner J.H. H2A.Z-mediated localization of genes at the nuclear periphery confers epigenetic memory of previous transcriptional state. PLoS Biol. 2007, 5:e81.
    • (2007) PLoS Biol. , vol.5
    • Brickner, D.G.1    Cajigas, I.2    Fondufe-Mittendorf, Y.3    Ahmed, S.4    Lee, P.C.5    Widom, J.6    Brickner, J.H.7
  • 36
    • 73349098753 scopus 로고    scopus 로고
    • The euchromatic and heterochromatic landscapes are shaped by antagonizing effects of transcription on H2A.Z deposition
    • Hardy S., Jacques P.E., Gevry N., Forest A., Fortin M.E., Laflamme L., Gaudreau L., Robert F. The euchromatic and heterochromatic landscapes are shaped by antagonizing effects of transcription on H2A.Z deposition. PLoS Genet. 2009, 5:e1000687.
    • (2009) PLoS Genet. , vol.5
    • Hardy, S.1    Jacques, P.E.2    Gevry, N.3    Forest, A.4    Fortin, M.E.5    Laflamme, L.6    Gaudreau, L.7    Robert, F.8
  • 40
    • 0348184963 scopus 로고    scopus 로고
    • ATP-driven exchange of histone H2AZ variant catalyzed by SWR1 chromatin remodeling complex
    • Mizuguchi G., Shen X., Landry J., Wu W.H., Sen S., Wu C. ATP-driven exchange of histone H2AZ variant catalyzed by SWR1 chromatin remodeling complex. Science 2004, 303:343-348.
    • (2004) Science , vol.303 , pp. 343-348
    • Mizuguchi, G.1    Shen, X.2    Landry, J.3    Wu, W.H.4    Sen, S.5    Wu, C.6
  • 43
    • 33748698658 scopus 로고    scopus 로고
    • SAS-mediated acetylation of histone H4 Lys 16 is required for H2A.Z incorporation at subtelomeric regions in Saccharomyces cerevisiae
    • Shia W.J., Li B., Workman J.L. SAS-mediated acetylation of histone H4 Lys 16 is required for H2A.Z incorporation at subtelomeric regions in Saccharomyces cerevisiae. Genes Dev. 2006, 20:2507-2512.
    • (2006) Genes Dev. , vol.20 , pp. 2507-2512
    • Shia, W.J.1    Li, B.2    Workman, J.L.3
  • 44
    • 63349106258 scopus 로고    scopus 로고
    • Discriminating nucleosomes containing histone H2A.Z or H2A based on genetic and epigenetic information
    • Gervais A.L., Gaudreau L. Discriminating nucleosomes containing histone H2A.Z or H2A based on genetic and epigenetic information. BMC Mol. Biol. 2009, 10:18.
    • (2009) BMC Mol. Biol. , vol.10 , pp. 18
    • Gervais, A.L.1    Gaudreau, L.2
  • 45
    • 78651510784 scopus 로고    scopus 로고
    • Global regulation of H2A.Z localization by the INO80 chromatin-remodeling enzyme is essential for genome integrity
    • Papamichos-Chronakis M., Watanabe S., Rando O.J., Peterson C.L. Global regulation of H2A.Z localization by the INO80 chromatin-remodeling enzyme is essential for genome integrity. Cell 2011, 144:200-213.
    • (2011) Cell , vol.144 , pp. 200-213
    • Papamichos-Chronakis, M.1    Watanabe, S.2    Rando, O.J.3    Peterson, C.L.4
  • 46
    • 79952534189 scopus 로고    scopus 로고
    • Regulation of chromatin by histone modifications
    • Bannister A.J., Kouzarides T. Regulation of chromatin by histone modifications. Cell Res. 2011, 21:381-395.
    • (2011) Cell Res. , vol.21 , pp. 381-395
    • Bannister, A.J.1    Kouzarides, T.2
  • 47
    • 32444434989 scopus 로고    scopus 로고
    • Histone H4-K16 acetylation controls chromatin structure and protein interactions
    • Shogren-Knaak M., Ishii H., Sun J.M., Pazin M.J., Davie J.R., Peterson C.L. Histone H4-K16 acetylation controls chromatin structure and protein interactions. Science 2006, 311:844-847.
    • (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
  • 48
    • 79954416946 scopus 로고    scopus 로고
    • Readers of histone modifications
    • Yun M., Wu J., Workman J.L., Li B. Readers of histone modifications. Cell Res. 2011, 21:564-578.
    • (2011) Cell Res. , vol.21 , pp. 564-578
    • Yun, M.1    Wu, J.2    Workman, J.L.3    Li, B.4
  • 49
    • 78549287139 scopus 로고    scopus 로고
    • Keeping it in the family: diverse histone recognition by conserved structural folds
    • Yap K.L., Zhou M.M. Keeping it in the family: diverse histone recognition by conserved structural folds. Crit. Rev. Biochem. Mol. Biol. 2010, 45:488-505.
    • (2010) Crit. Rev. Biochem. Mol. Biol. , vol.45 , pp. 488-505
    • Yap, K.L.1    Zhou, M.M.2
  • 52
    • 34547925170 scopus 로고    scopus 로고
    • Hat1: the emerging cellular roles of a type B histone acetyltransferase
    • Parthun M.R. Hat1: the emerging cellular roles of a type B histone acetyltransferase. Oncogene 2007, 26:5319-5328.
    • (2007) Oncogene , vol.26 , pp. 5319-5328
    • Parthun, M.R.1
  • 53
    • 0027525970 scopus 로고
    • Studies of the DNA binding properties of histone H4 amino terminus. Thermal denaturation studies reveal that acetylation markedly reduces the binding constant of the H4 "tail" to DNA
    • Hong L., Schroth G.P., Matthews H.R., Yau P., Bradbury E.M. Studies of the DNA binding properties of histone H4 amino terminus. Thermal denaturation studies reveal that acetylation markedly reduces the binding constant of the H4 "tail" to DNA. J. Biol. Chem. 1993, 268:305-314.
    • (1993) J. Biol. Chem. , vol.268 , pp. 305-314
    • Hong, L.1    Schroth, G.P.2    Matthews, H.R.3    Yau, P.4    Bradbury, E.M.5
  • 54
    • 0031707751 scopus 로고    scopus 로고
    • Alteration of nucleosome structure as a mechanism of transcriptional regulation
    • Workman J.L., Kingston R.E. Alteration of nucleosome structure as a mechanism of transcriptional regulation. Annu. Rev. Biochem. 1998, 67:545-579.
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 545-579
    • Workman, J.L.1    Kingston, R.E.2
  • 55
    • 0035893240 scopus 로고    scopus 로고
    • Histone H3 lysine 4 methylation is mediated by Set1 and required for cell growth and rDNA silencing in Saccharomyces cerevisiae
    • Briggs S.D., Bryk M., Strahl B.D., Cheung W.L., Davie J.K., Dent S.Y., Winston F., Allis C.D. Histone H3 lysine 4 methylation is mediated by Set1 and required for cell growth and rDNA silencing in Saccharomyces cerevisiae. Genes Dev. 2001, 15:3286-3295.
    • (2001) Genes Dev. , vol.15 , pp. 3286-3295
    • Briggs, S.D.1    Bryk, M.2    Strahl, B.D.3    Cheung, W.L.4    Davie, J.K.5    Dent, S.Y.6    Winston, F.7    Allis, C.D.8
  • 56
    • 0037059029 scopus 로고    scopus 로고
    • Histone H3 lysine 4 methylation is mediated by Set1 and promotes maintenance of active chromatin states in fission yeast
    • Noma K., Grewal S.I. Histone H3 lysine 4 methylation is mediated by Set1 and promotes maintenance of active chromatin states in fission yeast. Proc. Natl. Acad. Sci. U. S. A. 2002, 99(Suppl. 4):16438-16445.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , Issue.SUPPL. 4 , pp. 16438-16445
    • Noma, K.1    Grewal, S.I.2
  • 57
    • 84861870951 scopus 로고    scopus 로고
    • The COMPASS family of histone H3K4 methylases: mechanisms of regulation in development and disease pathogenesis
    • Shilatifard A. The COMPASS family of histone H3K4 methylases: mechanisms of regulation in development and disease pathogenesis. Annu. Rev. Biochem. 2012, 81:65-95.
    • (2012) Annu. Rev. Biochem. , vol.81 , pp. 65-95
    • Shilatifard, A.1
  • 58
    • 0034695456 scopus 로고    scopus 로고
    • Rad6-dependent ubiquitination of histone H2B in yeast
    • Robzyk K., Recht J., Osley M.A. Rad6-dependent ubiquitination of histone H2B in yeast. Science 2000, 287:501-504.
    • (2000) Science , vol.287 , pp. 501-504
    • Robzyk, K.1    Recht, J.2    Osley, M.A.3
  • 61
    • 68849086180 scopus 로고    scopus 로고
    • Phosphorylation of the transcription elongation factor Spt5 by yeast Bur1 kinase stimulates recruitment of the PAF complex
    • Liu Y., Warfield L., Zhang C., Luo J., Allen J., Lang W.H., Ranish J., Shokat K.M., Hahn S. Phosphorylation of the transcription elongation factor Spt5 by yeast Bur1 kinase stimulates recruitment of the PAF complex. Mol. Cell. Biol. 2009, 29:4852-4863.
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 4852-4863
    • Liu, Y.1    Warfield, L.2    Zhang, C.3    Luo, J.4    Allen, J.5    Lang, W.H.6    Ranish, J.7    Shokat, K.M.8    Hahn, S.9
  • 62
    • 66349122952 scopus 로고    scopus 로고
    • Control of transcriptional elongation and cotranscriptional histone modification by the yeast BUR kinase substrate Spt5
    • Zhou K., Kuo W.H., Fillingham J., Greenblatt J.F. Control of transcriptional elongation and cotranscriptional histone modification by the yeast BUR kinase substrate Spt5. Proc. Natl. Acad. Sci. U. S. A. 2009, 106:6956-6961.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 6956-6961
    • Zhou, K.1    Kuo, W.H.2    Fillingham, J.3    Greenblatt, J.F.4
  • 67
    • 15244358670 scopus 로고    scopus 로고
    • Distinction and relationship between elongation rate and processivity of RNA polymerase II in vivo
    • Mason P.B., Struhl K. Distinction and relationship between elongation rate and processivity of RNA polymerase II in vivo. Mol. Cell 2005, 17:831-840.
    • (2005) Mol. Cell , vol.17 , pp. 831-840
    • Mason, P.B.1    Struhl, K.2
  • 69
    • 29644433964 scopus 로고    scopus 로고
    • Human but not yeast CHD1 binds directly and selectively to histone H3 methylated at lysine 4 via its tandem chromodomains
    • Sims R.J., Chen C.F., Santos-Rosa H., Kouzarides T., Patel S.S., Reinberg D. Human but not yeast CHD1 binds directly and selectively to histone H3 methylated at lysine 4 via its tandem chromodomains. J. Biol. Chem. 2005, 280:41789-41792.
    • (2005) J. Biol. Chem. , vol.280 , pp. 41789-41792
    • Sims, R.J.1    Chen, C.F.2    Santos-Rosa, H.3    Kouzarides, T.4    Patel, S.S.5    Reinberg, D.6
  • 74
    • 35349024178 scopus 로고    scopus 로고
    • A plant homeodomain in RAG-2 that binds Hypermethylated lysine 4 of histone H3 is necessary for efficient antigen-receptor-gene rearrangement
    • Liu Y., Subrahmanyam R., Chakraborty T., Sen R., Desiderio S. A plant homeodomain in RAG-2 that binds Hypermethylated lysine 4 of histone H3 is necessary for efficient antigen-receptor-gene rearrangement. Immunity 2007, 27:561-571.
    • (2007) Immunity , vol.27 , pp. 561-571
    • Liu, Y.1    Subrahmanyam, R.2    Chakraborty, T.3    Sen, R.4    Desiderio, S.5
  • 75
    • 0942290540 scopus 로고    scopus 로고
    • Rad6 plays a role in transcriptional activation through ubiquitylation of histone H2B
    • Kao C.F., Hillyer C., Tsukuda T., Henry K., Berger S., Osley M.A. Rad6 plays a role in transcriptional activation through ubiquitylation of histone H2B. Genes Dev. 2004, 18:184-195.
    • (2004) Genes Dev. , vol.18 , pp. 184-195
    • Kao, C.F.1    Hillyer, C.2    Tsukuda, T.3    Henry, K.4    Berger, S.5    Osley, M.A.6
  • 76
    • 80455162312 scopus 로고    scopus 로고
    • Genome-wide function of H2B ubiquitylation in promoter and genic regions
    • Batta K., Zhang Z., Yen K., Goffman D.B., Pugh B.F. Genome-wide function of H2B ubiquitylation in promoter and genic regions. Genes Dev. 2011, 25:2254-2265.
    • (2011) Genes Dev. , vol.25 , pp. 2254-2265
    • Batta, K.1    Zhang, Z.2    Yen, K.3    Goffman, D.B.4    Pugh, B.F.5
  • 78
    • 43149122898 scopus 로고    scopus 로고
    • Monoubiquitinated H2B is associated with the transcribed region of highly expressed genes in human cells
    • Minsky N., Shema E., Field Y., Schuster M., Segal E., Oren M. Monoubiquitinated H2B is associated with the transcribed region of highly expressed genes in human cells. Nat. Cell Biol. 2008, 10:483-488.
    • (2008) Nat. Cell Biol. , vol.10 , pp. 483-488
    • Minsky, N.1    Shema, E.2    Field, Y.3    Schuster, M.4    Segal, E.5    Oren, M.6
  • 79
    • 70349731733 scopus 로고    scopus 로고
    • Ubiquitination of histone H2B regulates chromatin dynamics by enhancing nucleosome stability
    • Chandrasekharan M.B., Huang F., Sun Z.W. Ubiquitination of histone H2B regulates chromatin dynamics by enhancing nucleosome stability. Proc. Natl. Acad. Sci. U. S. A. 2009, 106:16686-16691.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 16686-16691
    • Chandrasekharan, M.B.1    Huang, F.2    Sun, Z.W.3
  • 80
    • 0028235824 scopus 로고
    • Histone H2B (and H2A) ubiquitination allows normal histone octamer and core particle reconstitution
    • Davies N., Lindsey G.G. Histone H2B (and H2A) ubiquitination allows normal histone octamer and core particle reconstitution. Biochim. Biophys. Acta 1994, 1218:187-193.
    • (1994) Biochim. Biophys. Acta , vol.1218 , pp. 187-193
    • Davies, N.1    Lindsey, G.G.2
  • 82
    • 46149091721 scopus 로고    scopus 로고
    • H2B ubiquitylation plays a role in nucleosome dynamics during transcription elongation
    • Fleming A.B., Kao C.F., Hillyer C., Pikaart M., Osley M.A. H2B ubiquitylation plays a role in nucleosome dynamics during transcription elongation. Mol. Cell 2008, 31:57-66.
    • (2008) Mol. Cell , vol.31 , pp. 57-66
    • Fleming, A.B.1    Kao, C.F.2    Hillyer, C.3    Pikaart, M.4    Osley, M.A.5
  • 84
    • 33646691283 scopus 로고    scopus 로고
    • Histone H2B monoubiquitination functions cooperatively with FACT to regulate elongation by RNA polymerase II
    • Pavri R., Zhu B., Li G., Trojer P., Mandal S., Shilatifard A., Reinberg D. Histone H2B monoubiquitination functions cooperatively with FACT to regulate elongation by RNA polymerase II. Cell 2006, 125:703-717.
    • (2006) Cell , vol.125 , pp. 703-717
    • Pavri, R.1    Zhu, B.2    Li, G.3    Trojer, P.4    Mandal, S.5    Shilatifard, A.6    Reinberg, D.7
  • 91
    • 0037163016 scopus 로고    scopus 로고
    • Disruptor of telomeric silencing-1 is a chromatin-specific histone H3 methyltransferase
    • Lacoste N., Utley R.T., Hunter J.M., Poirier G.G., Cote J. Disruptor of telomeric silencing-1 is a chromatin-specific histone H3 methyltransferase. J. Biol. Chem. 2002, 277:30421-30424.
    • (2002) J. Biol. Chem. , vol.277 , pp. 30421-30424
    • Lacoste, N.1    Utley, R.T.2    Hunter, J.M.3    Poirier, G.G.4    Cote, J.5
  • 92
    • 0037098044 scopus 로고    scopus 로고
    • Lysine methylation within the globular domain of histone H3 by Dot1 is important for telomeric silencing and Sir protein association
    • Ng H.H., Feng Q., Wang H., Erdjument-Bromage H., Tempst P., Zhang Y., Struhl K. Lysine methylation within the globular domain of histone H3 by Dot1 is important for telomeric silencing and Sir protein association. Genes Dev. 2002, 16:1518-1527.
    • (2002) Genes Dev. , vol.16 , pp. 1518-1527
    • Ng, H.H.1    Feng, Q.2    Wang, H.3    Erdjument-Bromage, H.4    Tempst, P.5    Zhang, Y.6    Struhl, K.7
  • 93
  • 95
    • 0037144393 scopus 로고    scopus 로고
    • Ubiquitination of histone H2B by Rad6 is required for efficient Dot1-mediated methylation of histone H3 lysine 79
    • Ng H.H., Xu R.M., Zhang Y., Struhl K. Ubiquitination of histone H2B by Rad6 is required for efficient Dot1-mediated methylation of histone H3 lysine 79. J. Biol. Chem. 2002, 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
  • 96
    • 22544461653 scopus 로고    scopus 로고
    • Histone H2B ubiquitylation controls processive methylation but not monomethylation by Dot1 and Set1
    • Shahbazian M.D., Zhang K., Grunstein M. Histone H2B ubiquitylation controls processive methylation but not monomethylation by Dot1 and Set1. Mol. Cell 2005, 19:271-277.
    • (2005) Mol. Cell , vol.19 , pp. 271-277
    • Shahbazian, M.D.1    Zhang, K.2    Grunstein, M.3
  • 98
    • 44849100496 scopus 로고    scopus 로고
    • Chemically ubiquitylated histone H2B stimulates hDot1L-mediated intranucleosomal methylation
    • McGinty R.K., Kim J., Chatterjee C., Roeder R.G., Muir T.W. Chemically ubiquitylated histone H2B stimulates hDot1L-mediated intranucleosomal methylation. Nature 2008, 453:812-816.
    • (2008) Nature , vol.453 , pp. 812-816
    • McGinty, R.K.1    Kim, J.2    Chatterjee, C.3    Roeder, R.G.4    Muir, T.W.5
  • 99
    • 77949874828 scopus 로고    scopus 로고
    • Disulfide-directed histone ubiquitylation reveals plasticity in hDot1L activation
    • Chatterjee C., McGinty R.K., Fierz B., Muir T.W. Disulfide-directed histone ubiquitylation reveals plasticity in hDot1L activation. Nat. Chem. Biol. 2010, 6:267-269.
    • (2010) Nat. Chem. Biol. , vol.6 , pp. 267-269
    • Chatterjee, C.1    McGinty, R.K.2    Fierz, B.3    Muir, T.W.4
  • 100
    • 77956267115 scopus 로고    scopus 로고
    • A lysine-rich region in Dot1p is crucial for direct interaction with H2B ubiquitylation and high level methylation of H3K79
    • Oh S., Jeong K., Kim H., Kwon C.S., Lee D. A lysine-rich region in Dot1p is crucial for direct interaction with H2B ubiquitylation and high level methylation of H3K79. Biochem. Biophys. Res. Commun. 2010, 399:512-517.
    • (2010) Biochem. Biophys. Res. Commun. , vol.399 , pp. 512-517
    • Oh, S.1    Jeong, K.2    Kim, H.3    Kwon, C.S.4    Lee, D.5
  • 101
    • 1242271997 scopus 로고    scopus 로고
    • Proteasomal ATPases link ubiquitylation of histone H2B to methylation of histone H3
    • Ezhkova E., Tansey W.P. Proteasomal ATPases link ubiquitylation of histone H2B to methylation of histone H3. Mol. Cell 2004, 13:435-442.
    • (2004) Mol. Cell , vol.13 , pp. 435-442
    • Ezhkova, E.1    Tansey, W.P.2
  • 102
    • 79959960773 scopus 로고    scopus 로고
    • The diverse functions of Dot1 and H3K79 methylation
    • Nguyen A.T., Zhang Y. The diverse functions of Dot1 and H3K79 methylation. Genes Dev. 2011, 25:1345-1358.
    • (2011) Genes Dev. , vol.25 , pp. 1345-1358
    • Nguyen, A.T.1    Zhang, Y.2
  • 103
    • 0037452770 scopus 로고    scopus 로고
    • Lysine-79 of histone H3 is hypomethylated at silenced loci in yeast and mammalian cells: a potential mechanism for position-effect variegation
    • Ng H.H., Ciccone D.N., Morshead K.B., Oettinger M.A., Struhl K. Lysine-79 of histone H3 is hypomethylated at silenced loci in yeast and mammalian cells: a potential mechanism for position-effect variegation. Proc. Natl. Acad. Sci. U. S. A. 2003, 100:1820-1825.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 1820-1825
    • Ng, H.H.1    Ciccone, D.N.2    Morshead, K.B.3    Oettinger, M.A.4    Struhl, K.5
  • 107
    • 33846522525 scopus 로고    scopus 로고
    • The mixed-lineage leukemia fusion partner AF4 stimulates RNA polymerase II transcriptional elongation and mediates coordinated chromatin remodeling
    • Bitoun E., Oliver P.L., Davies K.E. The mixed-lineage leukemia fusion partner AF4 stimulates RNA polymerase II transcriptional elongation and mediates coordinated chromatin remodeling. Hum. Mol. Genet. 2007, 16:92-106.
    • (2007) Hum. Mol. Genet. , vol.16 , pp. 92-106
    • Bitoun, E.1    Oliver, P.L.2    Davies, K.E.3
  • 110
    • 82355181529 scopus 로고    scopus 로고
    • A novel disrupter of telomere silencing 1-like (DOT1L) interaction is required for signal transducer and activator of transcription 1 (STAT1)-activated gene expression
    • Shah S., Henriksen M.A. A novel disrupter of telomere silencing 1-like (DOT1L) interaction is required for signal transducer and activator of transcription 1 (STAT1)-activated gene expression. J. Biol. Chem. 2011, 286:41195-41204.
    • (2011) J. Biol. Chem. , vol.286 , pp. 41195-41204
    • Shah, S.1    Henriksen, M.A.2
  • 116
    • 0037147121 scopus 로고    scopus 로고
    • Association of the histone methyltransferase Set2 with RNA polymerase II plays a role in transcription elongation
    • Li J., Moazed D., Gygi S.P. Association of the histone methyltransferase Set2 with RNA polymerase II plays a role in transcription elongation. J. Biol. Chem. 2002, 277:49383-49388.
    • (2002) J. Biol. Chem. , vol.277 , pp. 49383-49388
    • Li, J.1    Moazed, D.2    Gygi, S.P.3
  • 118
    • 0037512273 scopus 로고    scopus 로고
    • The Set2 histone methyltransferase functions through the phosphorylated carboxyl-terminal domain of RNA polymerase II
    • Li B., Howe L., Anderson S., Yates J.R., Workman J.L. The Set2 histone methyltransferase functions through the phosphorylated carboxyl-terminal domain of RNA polymerase II. J. Biol. Chem. 2003, 278:8897-8903.
    • (2003) J. Biol. Chem. , vol.278 , pp. 8897-8903
    • Li, B.1    Howe, L.2    Anderson, S.3    Yates, J.R.4    Workman, J.L.5
  • 120
    • 84856285875 scopus 로고    scopus 로고
    • RNA polymerase II carboxyl-terminal domain phosphorylation regulates protein stability of the Set2 methyltransferase and histone H3 di- and trimethylation at lysine 36
    • Fuchs S.M., Kizer K.O., Braberg H., Krogan N.J., Strahl B.D. RNA polymerase II carboxyl-terminal domain phosphorylation regulates protein stability of the Set2 methyltransferase and histone H3 di- and trimethylation at lysine 36. J. Biol. Chem. 2012, 287:3249-3256.
    • (2012) J. Biol. Chem. , vol.287 , pp. 3249-3256
    • Fuchs, S.M.1    Kizer, K.O.2    Braberg, H.3    Krogan, N.J.4    Strahl, B.D.5
  • 121
    • 33748163064 scopus 로고    scopus 로고
    • Proline isomerization of histone H3 regulates lysine methylation and gene expression
    • Nelson C.J., Santos-Rosa H., Kouzarides T. Proline isomerization of histone H3 regulates lysine methylation and gene expression. Cell 2006, 126:905-916.
    • (2006) Cell , vol.126 , pp. 905-916
    • Nelson, C.J.1    Santos-Rosa, H.2    Kouzarides, T.3
  • 122
    • 27144458417 scopus 로고    scopus 로고
    • Dimethylation of histone H3 at lysine 36 demarcates regulatory and nonregulatory chromatin genome-wide
    • Rao B., Shibata Y., Strahl B.D., Lieb J.D. Dimethylation of histone H3 at lysine 36 demarcates regulatory and nonregulatory chromatin genome-wide. Mol. Cell. Biol. 2005, 25:9447-9459.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 9447-9459
    • Rao, B.1    Shibata, Y.2    Strahl, B.D.3    Lieb, J.D.4
  • 124
    • 29144468972 scopus 로고    scopus 로고
    • Eaf3 chromodomain interaction with methylated H3-K36 links histone deacetylation to Pol II elongation
    • Joshi A.A., Struhl K. Eaf3 chromodomain interaction with methylated H3-K36 links histone deacetylation to Pol II elongation. Mol. Cell 2005, 20:971-978.
    • (2005) Mol. Cell , vol.20 , pp. 971-978
    • Joshi, A.A.1    Struhl, K.2
  • 126
    • 34249099730 scopus 로고    scopus 로고
    • Combined action of PHD and chromo domains directs the Rpd3S HDAC to transcribed chromatin
    • Li B., Gogol M., Carey M., Lee D., Seidel C., Workman J.L. Combined action of PHD and chromo domains directs the Rpd3S HDAC to transcribed chromatin. Science 2007, 316:1050-1054.
    • (2007) Science , vol.316 , pp. 1050-1054
    • Li, B.1    Gogol, M.2    Carey, M.3    Lee, D.4    Seidel, C.5    Workman, J.L.6
  • 129
    • 84863654457 scopus 로고    scopus 로고
    • Psip1/Ledgf p52 binds methylated histone H3K36 and splicing factors and contributes to the regulation of alternative splicing
    • Pradeepa M.M., Sutherland H.G., Ule J., Grimes G.R., Bickmore W.A. Psip1/Ledgf p52 binds methylated histone H3K36 and splicing factors and contributes to the regulation of alternative splicing. PLoS Genet. 2012, 8:e1002717.
    • (2012) PLoS Genet. , vol.8
    • Pradeepa, M.M.1    Sutherland, H.G.2    Ule, J.3    Grimes, G.R.4    Bickmore, W.A.5
  • 132
    • 84856120332 scopus 로고    scopus 로고
    • Understanding the language of Lys36 methylation at histone H3
    • Wagner E.J., Carpenter P.B. Understanding the language of Lys36 methylation at histone H3. Nat. Rev. Mol. Cell Biol. 2012, 13:115-126.
    • (2012) Nat. Rev. Mol. Cell Biol. , vol.13 , pp. 115-126
    • Wagner, E.J.1    Carpenter, P.B.2
  • 133
    • 38549139593 scopus 로고    scopus 로고
    • Dynamic histone H3 methylation during gene induction: HYPB/Setd2 mediates all H3K36 trimethylation
    • Edmunds J.W., Mahadevan L.C., Clayton A.L. Dynamic histone H3 methylation during gene induction: HYPB/Setd2 mediates all H3K36 trimethylation. EMBO J. 2008, 27:406-420.
    • (2008) EMBO J. , vol.27 , pp. 406-420
    • Edmunds, J.W.1    Mahadevan, L.C.2    Clayton, A.L.3
  • 134
    • 10044266854 scopus 로고    scopus 로고
    • Coordination of transcription factor phosphorylation and histone methylation by the P-TEFb kinase during human immunodeficiency virus type 1 transcription
    • Zhou M., Deng L., Lacoste V., Park H.U., Pumfery A., Kashanchi F., Brady J.N., Kumar A. Coordination of transcription factor phosphorylation and histone methylation by the P-TEFb kinase during human immunodeficiency virus type 1 transcription. J. Virol. 2004, 78:13522-13533.
    • (2004) J. Virol. , vol.78 , pp. 13522-13533
    • Zhou, M.1    Deng, L.2    Lacoste, V.3    Park, H.U.4    Pumfery, A.5    Kashanchi, F.6    Brady, J.N.7    Kumar, A.8
  • 136
    • 0041828953 scopus 로고    scopus 로고
    • Transcription elongation factors repress transcription initiation from cryptic sites
    • Kaplan C.D., Laprade L., Winston F. Transcription elongation factors repress transcription initiation from cryptic sites. Science 2003, 301:1096-1099.
    • (2003) Science , vol.301 , pp. 1096-1099
    • Kaplan, C.D.1    Laprade, L.2    Winston, F.3
  • 137
    • 56849114880 scopus 로고    scopus 로고
    • Chromatin- and transcription-related factors repress transcription from within coding regions throughout the Saccharomyces cerevisiae genome
    • Cheung V., Chua G., Batada N.N., Landry C.R., Michnick S.W., Hughes T.R., Winston F. Chromatin- and transcription-related factors repress transcription from within coding regions throughout the Saccharomyces cerevisiae genome. PLoS Biol. 2008, 6:e277.
    • (2008) PLoS Biol. , vol.6
    • Cheung, V.1    Chua, G.2    Batada, N.N.3    Landry, C.R.4    Michnick, S.W.5    Hughes, T.R.6    Winston, F.7
  • 138
    • 34249874030 scopus 로고    scopus 로고
    • Infrequently transcribed long genes depend on the Set2/Rpd3S pathway for accurate transcription
    • Li B., Gogol M., Carey M., Pattenden S.G., Seidel C., Workman J.L. Infrequently transcribed long genes depend on the Set2/Rpd3S pathway for accurate transcription. Genes Dev. 2007, 21:1422-1430.
    • (2007) Genes Dev. , vol.21 , pp. 1422-1430
    • Li, B.1    Gogol, M.2    Carey, M.3    Pattenden, S.G.4    Seidel, C.5    Workman, J.L.6
  • 139
    • 69949159297 scopus 로고    scopus 로고
    • Pervasive transcription constitutes a new level of eukaryotic genome regulation
    • Berretta J., Morillon A. Pervasive transcription constitutes a new level of eukaryotic genome regulation. EMBO Rep. 2009, 10:973-982.
    • (2009) EMBO Rep. , vol.10 , pp. 973-982
    • Berretta, J.1    Morillon, A.2
  • 140
    • 84860362829 scopus 로고    scopus 로고
    • Active chromatin and noncoding RNAs: an intimate relationship
    • Flynn R.A., Chang H.Y. Active chromatin and noncoding RNAs: an intimate relationship. Curr. Opin. Genet. Dev. 2012, 22:172-178.
    • (2012) Curr. Opin. Genet. Dev. , vol.22 , pp. 172-178
    • Flynn, R.A.1    Chang, H.Y.2
  • 142
    • 60549114880 scopus 로고    scopus 로고
    • Widespread bidirectional promoters are the major source of cryptic transcripts in yeast
    • Neil H., Malabat C., d'Aubenton-Carafa Y., Xu Z., Steinmetz L.M., Jacquier A. Widespread bidirectional promoters are the major source of cryptic transcripts in yeast. Nature 2009, 457:1038-1042.
    • (2009) Nature , vol.457 , pp. 1038-1042
    • Neil, H.1    Malabat, C.2    d'Aubenton-Carafa, Y.3    Xu, Z.4    Steinmetz, L.M.5    Jacquier, A.6
  • 145
    • 78751659330 scopus 로고    scopus 로고
    • Nascent transcript sequencing visualizes transcription at nucleotide resolution
    • Churchman L.S., Weissman J.S. Nascent transcript sequencing visualizes transcription at nucleotide resolution. Nature 2011, 469:368-373.
    • (2011) Nature , vol.469 , pp. 368-373
    • Churchman, L.S.1    Weissman, J.S.2
  • 146
    • 36048951040 scopus 로고    scopus 로고
    • Antisense RNA stabilization induces transcriptional gene silencing via histone deacetylation in S. cerevisiae
    • Camblong J., Iglesias N., Fickentscher C., Dieppois G., Stutz F. Antisense RNA stabilization induces transcriptional gene silencing via histone deacetylation in S. cerevisiae. Cell 2007, 131:706-717.
    • (2007) Cell , vol.131 , pp. 706-717
    • Camblong, J.1    Iglesias, N.2    Fickentscher, C.3    Dieppois, G.4    Stutz, F.5
  • 147
  • 151
    • 77958530632 scopus 로고    scopus 로고
    • Features of cryptic promoters and their varied reliance on bromodomain-containing factors
    • Pattenden S.G., Gogol M.M., Workman J.L. Features of cryptic promoters and their varied reliance on bromodomain-containing factors. PLoS One 2010, 5:e12927.
    • (2010) PLoS One , vol.5
    • Pattenden, S.G.1    Gogol, M.M.2    Workman, J.L.3
  • 153
    • 84866497062 scopus 로고    scopus 로고
    • Set2 methylation of histone H3 lysine36 suppresses histone exchange on transcribed genes
    • (Epub ahead of print 22 August 2012).
    • S. Venkatesh, M. Smolle, H. Li, M. Gogol, M. Saint, S. Kumar, K. Natarajan, J.L. Workman, Set2 methylation of histone H3 lysine36 suppresses histone exchange on transcribed genes, Nature, (Epub ahead of print 22 August 2012). http://dx.doi.org/10.1038/nature11326.
    • Nature
    • Venkatesh, S.1    Smolle, M.2    Li, H.3    Gogol, M.4    Saint, M.5    Kumar, S.6    Natarajan, K.7    Workman, J.L.8
  • 154
    • 84862908952 scopus 로고    scopus 로고
    • The replication-independent histone H3-H4 chaperones HIR, ASF1, and RTT106 co-operate to maintain promoter fidelity
    • Silva A.C., Xu X., Kim H.S., Fillingham J., Kislinger T., Mennella T.A., Keogh M.C. The replication-independent histone H3-H4 chaperones HIR, ASF1, and RTT106 co-operate to maintain promoter fidelity. J. Biol. Chem. 2012, 287:1709-1718.
    • (2012) J. Biol. Chem. , vol.287 , pp. 1709-1718
    • Silva, A.C.1    Xu, X.2    Kim, H.S.3    Fillingham, J.4    Kislinger, T.5    Mennella, T.A.6    Keogh, M.C.7
  • 155
    • 0242579933 scopus 로고    scopus 로고
    • The FACT complex travels with elongating RNA polymerase II and is important for the fidelity of transcriptional initiation in vivo
    • Mason P.B., Struhl K. The FACT complex travels with elongating RNA polymerase II and is important for the fidelity of transcriptional initiation in vivo. Mol. Cell. Biol. 2003, 23:8323-8333.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 8323-8333
    • Mason, P.B.1    Struhl, K.2
  • 156
    • 80053978527 scopus 로고    scopus 로고
    • FACT, the Bur kinase pathway, and the histone co-repressor HirC have overlapping nucleosome-related roles in yeast transcription elongation
    • Stevens J.R., O'Donnell A.F., Perry T.E., Benjamin J.J., Barnes C.A., Johnston G.C., Singer R.A. FACT, the Bur kinase pathway, and the histone co-repressor HirC have overlapping nucleosome-related roles in yeast transcription elongation. PLoS One 2011, 6:e25644.
    • (2011) PLoS One , vol.6
    • Stevens, J.R.1    O'Donnell, A.F.2    Perry, T.E.3    Benjamin, J.J.4    Barnes, C.A.5    Johnston, G.C.6    Singer, R.A.7
  • 157
    • 55549138754 scopus 로고    scopus 로고
    • The Rtt106 histone chaperone is functionally linked to transcription elongation and is involved in the regulation of spurious transcription from cryptic promoters in yeast
    • Imbeault D., Gamar L., Rufiange A., Paquet E., Nourani A. The Rtt106 histone chaperone is functionally linked to transcription elongation and is involved in the regulation of spurious transcription from cryptic promoters in yeast. J. Biol. Chem. 2008, 283:27350-27354.
    • (2008) J. Biol. Chem. , vol.283 , pp. 27350-27354
    • Imbeault, D.1    Gamar, L.2    Rufiange, A.3    Paquet, E.4    Nourani, A.5
  • 158
    • 77951249838 scopus 로고    scopus 로고
    • A nucleosome surface formed by histone H4, H2A, and H3 residues is needed for proper histone H3 K36 methylation, histone acetylation, and repression of cryptic transcription
    • Du H.N., Briggs S.D. A nucleosome surface formed by histone H4, H2A, and H3 residues is needed for proper histone H3 K36 methylation, histone acetylation, and repression of cryptic transcription. J. Biol. Chem. 2010, 285:11704-11713.
    • (2010) J. Biol. Chem. , vol.285 , pp. 11704-11713
    • Du, H.N.1    Briggs, S.D.2
  • 159
    • 54349105157 scopus 로고    scopus 로고
    • Histone H3 K36 methylation is mediated by a trans-histone methylation pathway involving an interaction between Set2 and histone H4
    • Du H.N., Fingerman I.M., Briggs S.D. Histone H3 K36 methylation is mediated by a trans-histone methylation pathway involving an interaction between Set2 and histone H4. Genes Dev. 2008, 22:2786-2798.
    • (2008) Genes Dev. , vol.22 , pp. 2786-2798
    • Du, H.N.1    Fingerman, I.M.2    Briggs, S.D.3
  • 160
    • 80052330728 scopus 로고    scopus 로고
    • Identification of histone mutants that are defective for transcription-coupled nucleosome occupancy
    • Hainer S.J., Martens J.A. Identification of histone mutants that are defective for transcription-coupled nucleosome occupancy. Mol. Cell. Biol. 2011, 31:3557-3568.
    • (2011) Mol. Cell. Biol. , vol.31 , pp. 3557-3568
    • Hainer, S.J.1    Martens, J.A.2
  • 162
    • 65549095078 scopus 로고    scopus 로고
    • Histone H3 lysine 36 di-methylation (H3K36ME2) is sufficient to recruit the Rpd3S histone deacetylase complex and to repress spurious transcription
    • Li B., Jackson J., Simon M.D., Fleharty B., Gogol M., Seidel C., Workman J.L., Shilatifard A. Histone H3 lysine 36 di-methylation (H3K36ME2) is sufficient to recruit the Rpd3S histone deacetylase complex and to repress spurious transcription. J. Biol. Chem. 2009, 284:7970-7976.
    • (2009) J. Biol. Chem. , vol.284 , pp. 7970-7976
    • Li, B.1    Jackson, J.2    Simon, M.D.3    Fleharty, B.4    Gogol, M.5    Seidel, C.6    Workman, J.L.7    Shilatifard, A.8
  • 163
    • 77749261651 scopus 로고    scopus 로고
    • Histone H3K4 and K36 methylation, Chd1 and Rpd3S oppose the functions of Saccharomyces cerevisiae Spt4-Spt5 in transcription
    • Quan T.K., Hartzog G.A. Histone H3K4 and K36 methylation, Chd1 and Rpd3S oppose the functions of Saccharomyces cerevisiae Spt4-Spt5 in transcription. Genetics 2010, 184:321-334.
    • (2010) Genetics , vol.184 , pp. 321-334
    • Quan, T.K.1    Hartzog, G.A.2
  • 164
    • 0345698603 scopus 로고    scopus 로고
    • Chromatin remodeling protein Chd1 interacts with transcription elongation factors and localizes to transcribed genes
    • Simic R., Lindstrom D.L., Tran H.G., Roinick K.L., Costa P.J., Johnson A.D., Hartzog G.A., Arndt K.M. Chromatin remodeling protein Chd1 interacts with transcription elongation factors and localizes to transcribed genes. EMBO J. 2003, 22:1846-1856.
    • (2003) EMBO J. , vol.22 , pp. 1846-1856
    • Simic, R.1    Lindstrom, D.L.2    Tran, H.G.3    Roinick, K.L.4    Costa, P.J.5    Johnson, A.D.6    Hartzog, G.A.7    Arndt, K.M.8
  • 165
    • 79955008193 scopus 로고    scopus 로고
    • KDM5B regulates embryonic stem cell self-renewal and represses cryptic intragenic transcription
    • Xie L., Pelz C., Wang W., Bashar A., Varlamova O., Shadle S., Impey S. KDM5B regulates embryonic stem cell self-renewal and represses cryptic intragenic transcription. EMBO J. 2011, 30:1473-1484.
    • (2011) EMBO J. , vol.30 , pp. 1473-1484
    • Xie, L.1    Pelz, C.2    Wang, W.3    Bashar, A.4    Varlamova, O.5    Shadle, S.6    Impey, S.7
  • 166
    • 23944445861 scopus 로고    scopus 로고
    • BUR kinase selectively regulates H3 K4 trimethylation and H2B ubiquitylation through recruitment of the PAF elongation complex
    • Laribee R.N., Krogan N.J., Xiao T., Shibata Y., Hughes T.R., Greenblatt J.F., Strahl B.D. BUR kinase selectively regulates H3 K4 trimethylation and H2B ubiquitylation through recruitment of the PAF elongation complex. Curr. Biol. 2005, 15:1487-1493.
    • (2005) Curr. Biol. , vol.15 , pp. 1487-1493
    • Laribee, R.N.1    Krogan, N.J.2    Xiao, T.3    Shibata, Y.4    Hughes, T.R.5    Greenblatt, J.F.6    Strahl, B.D.7
  • 167
    • 27944450463 scopus 로고    scopus 로고
    • The Bur1/Bur2 complex is required for histone H2B monoubiquitination by Rad6/Bre1 and histone methylation by COMPASS
    • Wood A., Schneider J., Dover J., Johnston M., Shilatifard A. The Bur1/Bur2 complex is required for histone H2B monoubiquitination by Rad6/Bre1 and histone methylation by COMPASS. Mol. Cell 2005, 20:589-599.
    • (2005) Mol. Cell , vol.20 , pp. 589-599
    • Wood, A.1    Schneider, J.2    Dover, J.3    Johnston, M.4    Shilatifard, A.5
  • 168
    • 36248965214 scopus 로고    scopus 로고
    • Regulation of histone modification and cryptic transcription by the Bur1 and Paf1 complexes
    • Chu Y., Simic R., Warner M.H., Arndt K.M., Prelich G. Regulation of histone modification and cryptic transcription by the Bur1 and Paf1 complexes. EMBO J. 2007, 26:4646-4656.
    • (2007) EMBO J. , vol.26 , pp. 4646-4656
    • Chu, Y.1    Simic, R.2    Warner, M.H.3    Arndt, K.M.4    Prelich, G.5
  • 170
    • 79957543093 scopus 로고    scopus 로고
    • More than a splicing code: integrating the role of RNA, chromatin and non-coding RNA in alternative splicing regulation
    • Luco R.F., Misteli T. More than a splicing code: integrating the role of RNA, chromatin and non-coding RNA in alternative splicing regulation. Curr. Opin. Genet. Dev. 2011, 21:366-372.
    • (2011) Curr. Opin. Genet. Dev. , vol.21 , pp. 366-372
    • Luco, R.F.1    Misteli, T.2
  • 172
    • 0032965152 scopus 로고    scopus 로고
    • Esa1p is an essential histone acetyltransferase required for cell cycle progression
    • Clarke A.S., Lowell J.E., Jacobson S.J., Pillus L. Esa1p is an essential histone acetyltransferase required for cell cycle progression. Mol. Cell. Biol. 1999, 19:2515-2526.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 2515-2526
    • Clarke, A.S.1    Lowell, J.E.2    Jacobson, S.J.3    Pillus, L.4
  • 174
    • 0032467640 scopus 로고    scopus 로고
    • Tip60 acetylates six lysines of a specific class in core histones in vitro
    • Kimura A., Horikoshi M. Tip60 acetylates six lysines of a specific class in core histones in vitro. Genes Cells 1998, 3:789-800.
    • (1998) Genes Cells , vol.3 , pp. 789-800
    • Kimura, A.1    Horikoshi, M.2
  • 175
    • 0033556404 scopus 로고    scopus 로고
    • Overlapping but distinct patterns of histone acetylation by the human coactivators p300 and PCAF within nucleosomal substrates
    • Schiltz R.L., Mizzen C.A., Vassilev A., Cook R.G., Allis C.D., Nakatani Y. Overlapping but distinct patterns of histone acetylation by the human coactivators p300 and PCAF within nucleosomal substrates. J. Biol. Chem. 1999, 274:1189-1192.
    • (1999) J. Biol. Chem. , vol.274 , pp. 1189-1192
    • Schiltz, R.L.1    Mizzen, C.A.2    Vassilev, A.3    Cook, R.G.4    Allis, C.D.5    Nakatani, Y.6
  • 176
    • 0032518442 scopus 로고    scopus 로고
    • Nucleosomal DNA regulates the core-histone-binding subunit of the human Hat1 acetyltransferase
    • Verreault A., Kaufman P.D., Kobayashi R., Stillman B. Nucleosomal DNA regulates the core-histone-binding subunit of the human Hat1 acetyltransferase. Curr. Biol. 1998, 8:96-108.
    • (1998) Curr. Biol. , vol.8 , pp. 96-108
    • Verreault, A.1    Kaufman, P.D.2    Kobayashi, R.3    Stillman, B.4
  • 177
    • 0035105035 scopus 로고    scopus 로고
    • TUP1 utilizes histone H3/H2B-specific HDA1 deacetylase to repress gene activity in yeast
    • Wu J., Suka N., Carlson M., Grunstein M. TUP1 utilizes histone H3/H2B-specific HDA1 deacetylase to repress gene activity in yeast. Mol. Cell 2001, 7:117-126.
    • (2001) Mol. Cell , vol.7 , pp. 117-126
    • Wu, J.1    Suka, N.2    Carlson, M.3    Grunstein, M.4
  • 178
    • 0034839973 scopus 로고    scopus 로고
    • Highly specific antibodies determine histone acetylation site usage in yeast heterochromatin and euchromatin
    • Suka N., Suka Y., Carmen A.A., Wu J., Grunstein M. Highly specific antibodies determine histone acetylation site usage in yeast heterochromatin and euchromatin. Mol. Cell 2001, 8:473-479.
    • (2001) Mol. Cell , vol.8 , pp. 473-479
    • Suka, N.1    Suka, Y.2    Carmen, A.A.3    Wu, J.4    Grunstein, M.5
  • 179
    • 0034636554 scopus 로고    scopus 로고
    • ATF-2 has intrinsic histone acetyltransferase activity which is modulated by phosphorylation
    • Kawasaki H., Schiltz L., Chiu R., Itakura K., Taira K., Nakatani Y., Yokoyama K.K. ATF-2 has intrinsic histone acetyltransferase activity which is modulated by phosphorylation. Nature 2000, 405:195-200.
    • (2000) Nature , vol.405 , pp. 195-200
    • Kawasaki, H.1    Schiltz, L.2    Chiu, R.3    Itakura, K.4    Taira, K.5    Nakatani, Y.6    Yokoyama, K.K.7
  • 182
    • 24344448174 scopus 로고    scopus 로고
    • The histone H3 acetylase dGcn5 is a key player in Drosophila melanogaster metamorphosis
    • Carre C., Szymczak D., Pidoux J., Antoniewski C. The histone H3 acetylase dGcn5 is a key player in Drosophila melanogaster metamorphosis. Mol. Cell. Biol. 2005, 25:8228-8238.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 8228-8238
    • Carre, C.1    Szymczak, D.2    Pidoux, J.3    Antoniewski, C.4
  • 184
    • 64249111489 scopus 로고    scopus 로고
    • Dimethylation of H3K4 by Set1 recruits the Set3 histone deacetylase complex to 5' transcribed regions
    • Kim T., Buratowski S. Dimethylation of H3K4 by Set1 recruits the Set3 histone deacetylase complex to 5' transcribed regions. Cell 2009, 137:259-272.
    • (2009) Cell , vol.137 , pp. 259-272
    • Kim, T.1    Buratowski, S.2
  • 185
    • 33745835064 scopus 로고    scopus 로고
    • Dissecting the biological functions of Drosophila histone deacetylases by RNA interference and transcriptional profiling
    • Foglietti C., Filocamo G., Cundari E., De Rinaldis E., Lahm A., Cortese R., Steinkuhler C. Dissecting the biological functions of Drosophila histone deacetylases by RNA interference and transcriptional profiling. J. Biol. Chem. 2006, 281:17968-17976.
    • (2006) J. Biol. Chem. , vol.281 , pp. 17968-17976
    • Foglietti, C.1    Filocamo, G.2    Cundari, E.3    De Rinaldis, E.4    Lahm, A.5    Cortese, R.6    Steinkuhler, C.7
  • 187
    • 0033579559 scopus 로고    scopus 로고
    • Crystal structure of the histone acetyltransferase Hpa2: a tetrameric member of the Gcn5-related N-acetyltransferase superfamily
    • Angus-Hill M.L., Dutnall R.N., Tafrov S.T., Sternglanz R., Ramakrishnan V. Crystal structure of the histone acetyltransferase Hpa2: a tetrameric member of the Gcn5-related N-acetyltransferase superfamily. J. Mol. Biol. 1999, 294:1311-1325.
    • (1999) J. Mol. Biol. , vol.294 , pp. 1311-1325
    • Angus-Hill, M.L.1    Dutnall, R.N.2    Tafrov, S.T.3    Sternglanz, R.4    Ramakrishnan, V.5
  • 189
    • 0037930802 scopus 로고    scopus 로고
    • Sas4 and Sas5 are required for the histone acetyltransferase activity of Sas2 in the SAS complex
    • Sutton A., Shia W.J., Band D., Kaufman P.D., Osada S., Workman J.L., Sternglanz R. Sas4 and Sas5 are required for the histone acetyltransferase activity of Sas2 in the SAS complex. J. Biol. Chem. 2003, 278:16887-16892.
    • (2003) J. Biol. Chem. , vol.278 , pp. 16887-16892
    • Sutton, A.1    Shia, W.J.2    Band, D.3    Kaufman, P.D.4    Osada, S.5    Workman, J.L.6    Sternglanz, R.7
  • 190
    • 0035577668 scopus 로고    scopus 로고
    • Histone H3 specific acetyltransferases are essential for cell cycle progression
    • Howe L., Auston D., Grant P., John S., Cook R.G., Workman J.L., Pillus L. Histone H3 specific acetyltransferases are essential for cell cycle progression. Genes Dev. 2001, 15:3144-3154.
    • (2001) Genes Dev. , vol.15 , pp. 3144-3154
    • Howe, L.1    Auston, D.2    Grant, P.3    John, S.4    Cook, R.G.5    Workman, J.L.6    Pillus, L.7
  • 192
    • 79251587149 scopus 로고    scopus 로고
    • HBO1 is required for H3K14 acetylation and normal transcriptional activity during embryonic development
    • Kueh A.J., Dixon M.P., Voss A.K., Thomas T. HBO1 is required for H3K14 acetylation and normal transcriptional activity during embryonic development. Mol. Cell. Biol. 2011, 31:845-860.
    • (2011) Mol. Cell. Biol. , vol.31 , pp. 845-860
    • Kueh, A.J.1    Dixon, M.P.2    Voss, A.K.3    Thomas, T.4
  • 194
    • 77954487796 scopus 로고    scopus 로고
    • Mechanism and regulation of acetylated histone binding by the tandem PHD finger of DPF3b
    • Zeng L., Zhang Q., Li S., Plotnikov A.N., Walsh M.J., Zhou M.M. Mechanism and regulation of acetylated histone binding by the tandem PHD finger of DPF3b. Nature 2010, 466:258-262.
    • (2010) Nature , vol.466 , pp. 258-262
    • Zeng, L.1    Zhang, Q.2    Li, S.3    Plotnikov, A.N.4    Walsh, M.J.5    Zhou, M.M.6
  • 196
    • 76849084692 scopus 로고    scopus 로고
    • A role for Gcn5 in replication-coupled nucleosome assembly
    • Burgess R.J., Zhou H., Han J., Zhang Z. A role for Gcn5 in replication-coupled nucleosome assembly. Mol. Cell 2010, 37:469-480.
    • (2010) Mol. Cell , vol.37 , pp. 469-480
    • Burgess, R.J.1    Zhou, H.2    Han, J.3    Zhang, Z.4
  • 199
    • 65549113750 scopus 로고    scopus 로고
    • CBP/p300-mediated acetylation of histone H3 on lysine 56
    • Das C., Lucia M.S., Hansen K.C., Tyler J.K. CBP/p300-mediated acetylation of histone H3 on lysine 56. Nature 2009, 459:113-117.
    • (2009) Nature , vol.459 , pp. 113-117
    • Das, C.1    Lucia, M.S.2    Hansen, K.C.3    Tyler, J.K.4
  • 201
    • 18844413266 scopus 로고    scopus 로고
    • Acetylation in histone H3 globular domain regulates gene expression in yeast
    • Xu F., Zhang K., Grunstein M. Acetylation in histone H3 globular domain regulates gene expression in yeast. Cell 2005, 121:375-385.
    • (2005) Cell , vol.121 , pp. 375-385
    • Xu, F.1    Zhang, K.2    Grunstein, M.3
  • 204
    • 29544444195 scopus 로고    scopus 로고
    • ING tumor suppressor proteins are critical regulators of chromatin acetylation required for genome expression and perpetuation
    • Doyon Y., Cayrou C., Ullah M., Landry A.J., Cote V., Selleck W., Lane W.S., Tan S., Yang X.J., Cote J. ING tumor suppressor proteins are critical regulators of chromatin acetylation required for genome expression and perpetuation. Mol. Cell 2006, 21:51-64.
    • (2006) Mol. Cell , vol.21 , pp. 51-64
    • Doyon, Y.1    Cayrou, C.2    Ullah, M.3    Landry, A.J.4    Cote, V.5    Selleck, W.6    Lane, W.S.7    Tan, S.8    Yang, X.J.9    Cote, J.10
  • 206
    • 0031865050 scopus 로고    scopus 로고
    • Targeted recruitment of the Sin3-Rpd3 histone deacetylase complex generates a highly localized domain of repressed chromatin in vivo
    • Kadosh D., Struhl K. Targeted recruitment of the Sin3-Rpd3 histone deacetylase complex generates a highly localized domain of repressed chromatin in vivo. Mol. Cell. Biol. 1998, 18:5121-5127.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 5121-5127
    • Kadosh, D.1    Struhl, K.2
  • 207
    • 0033866836 scopus 로고    scopus 로고
    • Activation of transcription through histone H4 acetylation by MOF, an acetyltransferase essential for dosage compensation in Drosophila
    • Akhtar A., Becker P.B. Activation of transcription through histone H4 acetylation by MOF, an acetyltransferase essential for dosage compensation in Drosophila. Mol. Cell 2000, 5:367-375.
    • (2000) Mol. Cell , vol.5 , pp. 367-375
    • Akhtar, A.1    Becker, P.B.2
  • 210
    • 0034669210 scopus 로고    scopus 로고
    • The structural basis for the recognition of acetylated histone H4 by the bromodomain of histone acetyltransferase gcn5p
    • Owen D.J., Ornaghi P., Yang J.C., Lowe N., Evans P.R., Ballario P., Neuhaus D., Filetici P., Travers A.A. The structural basis for the recognition of acetylated histone H4 by the bromodomain of histone acetyltransferase gcn5p. EMBO J. 2000, 19:6141-6149.
    • (2000) EMBO J. , vol.19 , pp. 6141-6149
    • Owen, D.J.1    Ornaghi, P.2    Yang, J.C.3    Lowe, N.4    Evans, P.R.5    Ballario, P.6    Neuhaus, D.7    Filetici, P.8    Travers, A.A.9
  • 211
    • 0034677535 scopus 로고    scopus 로고
    • Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase
    • Imai S., Armstrong C.M., Kaeberlein M., Guarente L. Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase. Nature 2000, 403:795-800.
    • (2000) Nature , vol.403 , pp. 795-800
    • Imai, S.1    Armstrong, C.M.2    Kaeberlein, M.3    Guarente, L.4
  • 212
    • 34547875013 scopus 로고    scopus 로고
    • NAD+-dependent deacetylation of H4 lysine 16 by class III HDACs
    • Vaquero A., Sternglanz R., Reinberg D. NAD+-dependent deacetylation of H4 lysine 16 by class III HDACs. Oncogene 2007, 26:5505-5520.
    • (2007) Oncogene , vol.26 , pp. 5505-5520
    • Vaquero, A.1    Sternglanz, R.2    Reinberg, D.3
  • 215
    • 0037167839 scopus 로고    scopus 로고
    • Histone methylation by the Drosophila epigenetic transcriptional regulator Ash1
    • Beisel C., Imhof A., Greene J., Kremmer E., Sauer F. Histone methylation by the Drosophila epigenetic transcriptional regulator Ash1. Nature 2002, 419:857-862.
    • (2002) Nature , vol.419 , pp. 857-862
    • Beisel, C.1    Imhof, A.2    Greene, J.3    Kremmer, E.4    Sauer, F.5
  • 216
    • 79960643838 scopus 로고    scopus 로고
    • Drosophila Set1 is the major histone H3 lysine 4 trimethyltransferase with role in transcription
    • Ardehali M.B., Mei A., Zobeck K.L., Caron M., Lis J.T., Kusch T. Drosophila Set1 is the major histone H3 lysine 4 trimethyltransferase with role in transcription. EMBO J. 2011, 30:2817-2828.
    • (2011) EMBO J. , vol.30 , pp. 2817-2828
    • Ardehali, M.B.1    Mei, A.2    Zobeck, K.L.3    Caron, M.4    Lis, J.T.5    Kusch, T.6
  • 218
    • 0035694922 scopus 로고    scopus 로고
    • Purification and functional characterization of a histone H3-lysine 4-specific methyltransferase
    • Wang H., Cao R., Xia L., Erdjument-Bromage H., Borchers C., Tempst P., Zhang Y. Purification and functional characterization of a histone H3-lysine 4-specific methyltransferase. Mol. Cell 2001, 8:1207-1217.
    • (2001) Mol. Cell , vol.8 , pp. 1207-1217
    • Wang, H.1    Cao, R.2    Xia, L.3    Erdjument-Bromage, H.4    Borchers, C.5    Tempst, P.6    Zhang, Y.7
  • 233
    • 33746072542 scopus 로고    scopus 로고
    • Identification of three histone methyltransferases in Drosophila: dG9a is a suppressor of PEV and is required for gene silencing
    • Mis J., Ner S.S., Grigliatti T.A. Identification of three histone methyltransferases in Drosophila: dG9a is a suppressor of PEV and is required for gene silencing. Mol. Genet. Genomics 2006, 275:513-526.
    • (2006) Mol. Genet. Genomics , vol.275 , pp. 513-526
    • Mis, J.1    Ner, S.S.2    Grigliatti, T.A.3
  • 234
    • 0035816682 scopus 로고    scopus 로고
    • Set domain-containing protein, G9a, is a novel lysine-preferring mammalian histone methyltransferase with hyperactivity and specific selectivity to lysines 9 and 27 of histone H3
    • Tachibana M., Sugimoto K., Fukushima T., Shinkai Y. Set domain-containing protein, G9a, is a novel lysine-preferring mammalian histone methyltransferase with hyperactivity and specific selectivity to lysines 9 and 27 of histone H3. J. Biol. Chem. 2001, 276:25309-25317.
    • (2001) J. Biol. Chem. , vol.276 , pp. 25309-25317
    • Tachibana, M.1    Sugimoto, K.2    Fukushima, T.3    Shinkai, Y.4
  • 235
    • 0037052539 scopus 로고    scopus 로고
    • A complex with chromatin modifiers that occupies E2F- and Myc-responsive genes in G0 cells
    • Ogawa H., Ishiguro K., Gaubatz S., Livingston D.M., Nakatani Y. A complex with chromatin modifiers that occupies E2F- and Myc-responsive genes in G0 cells. Science 2002, 296:1132-1136.
    • (2002) Science , vol.296 , pp. 1132-1136
    • Ogawa, H.1    Ishiguro, K.2    Gaubatz, S.3    Livingston, D.M.4    Nakatani, Y.5
  • 236
    • 0037089626 scopus 로고    scopus 로고
    • SETDB1: a novel KAP-1-associated histone H3, lysine 9-specific methyltransferase that contributes to HP1-mediated silencing of euchromatic genes by KRAB zinc-finger proteins
    • Schultz D.C., Ayyanathan K., Negorev D., Maul G.G., Rauscher F.J. SETDB1: a novel KAP-1-associated histone H3, lysine 9-specific methyltransferase that contributes to HP1-mediated silencing of euchromatic genes by KRAB zinc-finger proteins. Genes Dev. 2002, 16:919-932.
    • (2002) Genes Dev. , vol.16 , pp. 919-932
    • Schultz, D.C.1    Ayyanathan, K.2    Negorev, D.3    Maul, G.G.4    Rauscher, F.J.5
  • 237
    • 0345275880 scopus 로고    scopus 로고
    • Inactivation of a histone methyltransferase by mutations in human cancers
    • Kim K.C., Geng L., Huang S. Inactivation of a histone methyltransferase by mutations in human cancers. Cancer Res. 2003, 63:7619-7623.
    • (2003) Cancer Res. , vol.63 , pp. 7619-7623
    • Kim, K.C.1    Geng, L.2    Huang, S.3
  • 242
    • 34347346108 scopus 로고    scopus 로고
    • Demethylation of histone H3K36 and H3K9 by Rph1: a vestige of an H3K9 methylation system in Saccharomyces cerevisiae?
    • Klose R.J., Gardner K.E., Liang G., Erdjument-Bromage H., Tempst P., Zhang Y. Demethylation of histone H3K36 and H3K9 by Rph1: a vestige of an H3K9 methylation system in Saccharomyces cerevisiae?. Mol. Cell. Biol. 2007, 27:3951-3961.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 3951-3961
    • Klose, R.J.1    Gardner, K.E.2    Liang, G.3    Erdjument-Bromage, H.4    Tempst, P.5    Zhang, Y.6
  • 243
    • 56849114113 scopus 로고    scopus 로고
    • Heterochromatin protein 1a stimulates histone H3 lysine 36 demethylation by the Drosophila KDM4A demethylase
    • Lin C.H., Li B., Swanson S., Zhang Y., Florens L., Washburn M.P., Abmayr S.M., Workman J.L. Heterochromatin protein 1a stimulates histone H3 lysine 36 demethylation by the Drosophila KDM4A demethylase. Mol. Cell 2008, 32:696-706.
    • (2008) Mol. Cell , vol.32 , pp. 696-706
    • Lin, C.H.1    Li, B.2    Swanson, S.3    Zhang, Y.4    Florens, L.5    Washburn, M.P.6    Abmayr, S.M.7    Workman, J.L.8
  • 245
    • 33646138230 scopus 로고    scopus 로고
    • JHDM2A, a JmjC-containing H3K9 demethylase, facilitates transcription activation by androgen receptor
    • Yamane K., Toumazou C., Tsukada Y., Erdjument-Bromage H., Tempst P., Wong J., Zhang Y. JHDM2A, a JmjC-containing H3K9 demethylase, facilitates transcription activation by androgen receptor. Cell 2006, 125:483-495.
    • (2006) Cell , vol.125 , pp. 483-495
    • Yamane, K.1    Toumazou, C.2    Tsukada, Y.3    Erdjument-Bromage, H.4    Tempst, P.5    Wong, J.6    Zhang, Y.7
  • 247
    • 77649152293 scopus 로고    scopus 로고
    • KDM7 is a dual demethylase for histone H3 Lys 9 and Lys 27 and functions in brain development
    • Tsukada Y., Ishitani T., Nakayama K.I. KDM7 is a dual demethylase for histone H3 Lys 9 and Lys 27 and functions in brain development. Genes Dev. 2010, 24:432-437.
    • (2010) Genes Dev. , vol.24 , pp. 432-437
    • Tsukada, Y.1    Ishitani, T.2    Nakayama, K.I.3
  • 250
    • 0037131523 scopus 로고    scopus 로고
    • Drosophila enhancer of Zeste/ESC complexes have a histone H3 methyltransferase activity that marks chromosomal Polycomb sites
    • Czermin B., Melfi R., McCabe D., Seitz V., Imhof A., Pirrotta V. Drosophila enhancer of Zeste/ESC complexes have a histone H3 methyltransferase activity that marks chromosomal Polycomb sites. Cell 2002, 111:185-196.
    • (2002) Cell , vol.111 , pp. 185-196
    • Czermin, B.1    Melfi, R.2    McCabe, D.3    Seitz, V.4    Imhof, A.5    Pirrotta, V.6
  • 251
    • 79952220410 scopus 로고    scopus 로고
    • EZH1 and EZH2 cogovern histone H3K27 trimethylation and are essential for hair follicle homeostasis and wound repair
    • Ezhkova E., Lien W.H., Stokes N., Pasolli H.A., Silva J.M., Fuchs E. EZH1 and EZH2 cogovern histone H3K27 trimethylation and are essential for hair follicle homeostasis and wound repair. Genes Dev. 2011, 25:485-498.
    • (2011) Genes Dev. , vol.25 , pp. 485-498
    • Ezhkova, E.1    Lien, W.H.2    Stokes, N.3    Pasolli, H.A.4    Silva, J.M.5    Fuchs, E.6
  • 252
    • 0043127085 scopus 로고    scopus 로고
    • Molecular basis for the discrimination of repressive methyl-lysine marks in histone H3 by Polycomb and HP1 chromodomains
    • Fischle W., Wang Y., Jacobs S.A., Kim Y., Allis C.D., Khorasanizadeh S. Molecular basis for the discrimination of repressive methyl-lysine marks in histone H3 by Polycomb and HP1 chromodomains. Genes Dev. 2003, 17:1870-1881.
    • (2003) Genes Dev. , vol.17 , pp. 1870-1881
    • Fischle, W.1    Wang, Y.2    Jacobs, S.A.3    Kim, Y.4    Allis, C.D.5    Khorasanizadeh, S.6
  • 253
  • 254
    • 34250820481 scopus 로고    scopus 로고
    • Trithorax-group protein ASH1 methylates histone H3 lysine 36
    • Tanaka Y., Katagiri Z., Kawahashi K., Kioussis D., Kitajima S. Trithorax-group protein ASH1 methylates histone H3 lysine 36. Gene 2007, 397:161-168.
    • (2007) Gene , vol.397 , pp. 161-168
    • Tanaka, Y.1    Katagiri, Z.2    Kawahashi, K.3    Kioussis, D.4    Kitajima, S.5
  • 258
    • 33746832077 scopus 로고    scopus 로고
    • Identification and characterization of Smyd2: a split SET/MYND domain-containing histone H3 lysine 36-specific methyltransferase that interacts with the Sin3 histone deacetylase complex
    • Brown M.A., Sims R.J., Gottlieb P.D., Tucker P.W. Identification and characterization of Smyd2: a split SET/MYND domain-containing histone H3 lysine 36-specific methyltransferase that interacts with the Sin3 histone deacetylase complex. Mol. Cancer 2006, 5:26.
    • (2006) Mol. Cancer , vol.5 , pp. 26
    • Brown, M.A.1    Sims, R.J.2    Gottlieb, P.D.3    Tucker, P.W.4
  • 259
    • 55249111484 scopus 로고    scopus 로고
    • Structural basis for the recognition of methylated histone H3K36 by the Eaf3 subunit of histone deacetylase complex Rpd3S
    • Xu C., Cui G., Botuyan M.V., Mer G. Structural basis for the recognition of methylated histone H3K36 by the Eaf3 subunit of histone deacetylase complex Rpd3S. Structure 2008, 16:1740-1750.
    • (2008) Structure , vol.16 , pp. 1740-1750
    • Xu, C.1    Cui, G.2    Botuyan, M.V.3    Mer, G.4
  • 261
    • 34347342789 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae histone demethylase Jhd1 fine-tunes the distribution of H3K36me2
    • Fang J., Hogan G.J., Liang G., Lieb J.D., Zhang Y. The Saccharomyces cerevisiae histone demethylase Jhd1 fine-tunes the distribution of H3K36me2. Mol. Cell. Biol. 2007, 27:5055-5065.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 5055-5065
    • Fang, J.1    Hogan, G.J.2    Liang, G.3    Lieb, J.D.4    Zhang, Y.5
  • 266
    • 52049085575 scopus 로고    scopus 로고
    • Functional characterization of the Drosophila Hmt4-20/Suv4-20 histone methyltransferase
    • Sakaguchi A., Karachentsev D., Seth-Pasricha M., Druzhinina M., Steward R. Functional characterization of the Drosophila Hmt4-20/Suv4-20 histone methyltransferase. Genetics 2008, 179:317-322.
    • (2008) Genetics , vol.179 , pp. 317-322
    • Sakaguchi, A.1    Karachentsev, D.2    Seth-Pasricha, M.3    Druzhinina, M.4    Steward, R.5
  • 269
    • 60549108739 scopus 로고    scopus 로고
    • Regulation of Set9-mediated H4K20 methylation by a PWWP domain protein
    • Wang Y., Reddy B., Thompson J., Wang H., Noma K., Yates J.R., Jia S. Regulation of Set9-mediated H4K20 methylation by a PWWP domain protein. Mol. Cell 2009, 33:428-437.
    • (2009) Mol. Cell , vol.33 , pp. 428-437
    • Wang, Y.1    Reddy, B.2    Thompson, J.3    Wang, H.4    Noma, K.5    Yates, J.R.6    Jia, S.7
  • 270
    • 82455175407 scopus 로고    scopus 로고
    • Histone H4 lysine 20 of Saccharomyces cerevisiae is monomethylated and functions in subtelomeric silencing
    • Edwards C.R., Dang W., Berger S.L. Histone H4 lysine 20 of Saccharomyces cerevisiae is monomethylated and functions in subtelomeric silencing. Biochemistry 2011, 50:10473-10483.
    • (2011) Biochemistry , vol.50 , pp. 10473-10483
    • Edwards, C.R.1    Dang, W.2    Berger, S.L.3
  • 272
    • 35348938519 scopus 로고    scopus 로고
    • JMJD6 is a histone arginine demethylase
    • Chang B., Chen Y., Zhao Y., Bruick R.K. JMJD6 is a histone arginine demethylase. Science 2007, 318:444-447.
    • (2007) Science , vol.318 , pp. 444-447
    • Chang, B.1    Chen, Y.2    Zhao, Y.3    Bruick, R.K.4
  • 273
    • 6344222803 scopus 로고    scopus 로고
    • Human SWI/SNF-associated PRMT5 methylates histone H3 arginine 8 and negatively regulates expression of ST7 and NM23 tumor suppressor genes
    • Pal S., Vishwanath S.N., Erdjument-Bromage H., Tempst P., Sif S. Human SWI/SNF-associated PRMT5 methylates histone H3 arginine 8 and negatively regulates expression of ST7 and NM23 tumor suppressor genes. Mol. Cell. Biol. 2004, 24:9630-9645.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 9630-9645
    • Pal, S.1    Vishwanath, S.N.2    Erdjument-Bromage, H.3    Tempst, P.4    Sif, S.5
  • 275
    • 78650233514 scopus 로고    scopus 로고
    • TDRD3 Is an effector molecule for arginine-methylated histone marks
    • Yang Y., Lu Y., Espejo A., Wu J., Xu W., Liang S., Bedford M.T. TDRD3 Is an effector molecule for arginine-methylated histone marks. Mol. Cell 2010, 40:1016-1023.
    • (2010) Mol. Cell , vol.40 , pp. 1016-1023
    • Yang, Y.1    Lu, Y.2    Espejo, A.3    Wu, J.4    Xu, W.5    Liang, S.6    Bedford, M.T.7
  • 279
    • 77950390899 scopus 로고    scopus 로고
    • H4R3 methylation facilitates beta-globin transcription by regulating histone acetyltransferase binding and H3 acetylation
    • Li X., Hu X., Patel B., Zhou Z., Liang S., Ybarra R., Qiu Y., Felsenfeld G., Bungert J., Huang S. H4R3 methylation facilitates beta-globin transcription by regulating histone acetyltransferase binding and H3 acetylation. Blood 2010, 115:2028-2037.
    • (2010) Blood , vol.115 , pp. 2028-2037
    • Li, X.1    Hu, X.2    Patel, B.3    Zhou, Z.4    Liang, S.5    Ybarra, R.6    Qiu, Y.7    Felsenfeld, G.8    Bungert, J.9    Huang, S.10
  • 280
    • 11844276610 scopus 로고    scopus 로고
    • Sterile 20 kinase phosphorylates histone H2B at serine 10 during hydrogen peroxide-induced apoptosis in S. cerevisiae
    • Ahn S.H., Cheung W.L., Hsu J.Y., Diaz R.L., Smith M.M., Allis C.D. Sterile 20 kinase phosphorylates histone H2B at serine 10 during hydrogen peroxide-induced apoptosis in S. cerevisiae. Cell 2005, 120:25-36.
    • (2005) Cell , vol.120 , pp. 25-36
    • Ahn, S.H.1    Cheung, W.L.2    Hsu, J.Y.3    Diaz, R.L.4    Smith, M.M.5    Allis, C.D.6
  • 282
    • 0035839135 scopus 로고    scopus 로고
    • Snf1-a histone kinase that works in concert with the histone acetyltransferase Gcn5 to regulate transcription
    • Lo W.S., Duggan L., Emre N.C., Belotserkovskya R., Lane W.S., Shiekhattar R., Berger S.L. Snf1-a histone kinase that works in concert with the histone acetyltransferase Gcn5 to regulate transcription. Science 2001, 293:1142-1146.
    • (2001) Science , vol.293 , pp. 1142-1146
    • Lo, W.S.1    Duggan, L.2    Emre, N.C.3    Belotserkovskya, R.4    Lane, W.S.5    Shiekhattar, R.6    Berger, S.L.7
  • 284
    • 0035906859 scopus 로고    scopus 로고
    • The JIL-1 tandem kinase mediates histone H3 phosphorylation and is required for maintenance of chromatin structure in Drosophila
    • Wang Y., Zhang W., Jin Y., Johansen J., Johansen K.M. The JIL-1 tandem kinase mediates histone H3 phosphorylation and is required for maintenance of chromatin structure in Drosophila. Cell 2001, 105:433-443.
    • (2001) Cell , vol.105 , pp. 433-443
    • Wang, Y.1    Zhang, W.2    Jin, Y.3    Johansen, J.4    Johansen, K.M.5
  • 285
    • 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., Glover D.M. 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, 152:669-682.
    • (2001) J. Cell Biol. , vol.152 , pp. 669-682
    • Giet, R.1    Glover, D.M.2
  • 289
    • 34547599505 scopus 로고    scopus 로고
    • PIM1-dependent phosphorylation of histone H3 at serine 10 is required for MYC-dependent transcriptional activation and oncogenic transformation
    • Zippo A., De Robertis A., Serafini R., Oliviero S. PIM1-dependent phosphorylation of histone H3 at serine 10 is required for MYC-dependent transcriptional activation and oncogenic transformation. Nat. Cell Biol. 2007, 9:932-944.
    • (2007) Nat. Cell Biol. , vol.9 , pp. 932-944
    • Zippo, A.1    De Robertis, A.2    Serafini, R.3    Oliviero, S.4
  • 292
    • 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., Berger S.L. Phosphorylation of serine 10 in histone H3 is functionally linked in vitro and in vivo to Gcn5-mediated acetylation at lysine 14. Mol. Cell 2000, 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
  • 294
    • 0042470618 scopus 로고    scopus 로고
    • Protein phosphatase 2A activity affects histone H3 phosphorylation and transcription in Drosophila melanogaster
    • Nowak S.J., Pai C.Y., Corces V.G. Protein phosphatase 2A activity affects histone H3 phosphorylation and transcription in Drosophila melanogaster. Mol. Cell. Biol. 2003, 23:6129-6138.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 6129-6138
    • Nowak, S.J.1    Pai, C.Y.2    Corces, V.G.3
  • 297
    • 38149098408 scopus 로고    scopus 로고
    • Histone H2A monoubiquitination represses transcription by inhibiting RNA polymerase II transcriptional elongation
    • Zhou W., Zhu P., Wang J., Pascual G., Ohgi K.A., Lozach J., Glass C.K., Rosenfeld M.G. Histone H2A monoubiquitination represses transcription by inhibiting RNA polymerase II transcriptional elongation. Mol. Cell 2008, 29:69-80.
    • (2008) Mol. Cell , vol.29 , pp. 69-80
    • Zhou, W.1    Zhu, P.2    Wang, J.3    Pascual, G.4    Ohgi, K.A.5    Lozach, J.6    Glass, C.K.7    Rosenfeld, M.G.8
  • 303
    • 34547730282 scopus 로고    scopus 로고
    • A histone H2A deubiquitinase complex coordinating histone acetylation and H1 dissociation in transcriptional regulation
    • Zhu P., Zhou W., Wang J., Puc J., Ohgi K.A., Erdjument-Bromage H., Tempst P., Glass C.K., Rosenfeld M.G. A histone H2A deubiquitinase complex coordinating histone acetylation and H1 dissociation in transcriptional regulation. Mol. Cell 2007, 27:609-621.
    • (2007) Mol. Cell , vol.27 , pp. 609-621
    • Zhu, P.1    Zhou, W.2    Wang, J.3    Puc, J.4    Ohgi, K.A.5    Erdjument-Bromage, H.6    Tempst, P.7    Glass, C.K.8    Rosenfeld, M.G.9
  • 304
    • 0037248593 scopus 로고    scopus 로고
    • A conserved RING finger protein required for histone H2B monoubiquitination and cell size control
    • Hwang W.W., Venkatasubrahmanyam S., Ianculescu A.G., Tong A., Boone C., Madhani H.D. A conserved RING finger protein required for histone H2B monoubiquitination and cell size control. Mol. Cell 2003, 11:261-266.
    • (2003) Mol. Cell , vol.11 , pp. 261-266
    • Hwang, W.W.1    Venkatasubrahmanyam, S.2    Ianculescu, A.G.3    Tong, A.4    Boone, C.5    Madhani, H.D.6
  • 305
    • 79953194432 scopus 로고    scopus 로고
    • E2 ligase dRad6 regulates DMP53 turnover in Drosophila
    • Chen S., Wei H.M., Lv W.W., Wang D.L., Sun F.L. E2 ligase dRad6 regulates DMP53 turnover in Drosophila. J. Biol. Chem. 2011, 286:9020-9030.
    • (2011) J. Biol. Chem. , vol.286 , pp. 9020-9030
    • Chen, S.1    Wei, H.M.2    Lv, W.W.3    Wang, D.L.4    Sun, F.L.5
  • 306
    • 13344260610 scopus 로고    scopus 로고
    • Bre1 is required for Notch signaling and histone modification
    • Bray S., Musisi H., Bienz M. Bre1 is required for Notch signaling and histone modification. Dev. Cell 2005, 8:279-286.
    • (2005) Dev. Cell , vol.8 , pp. 279-286
    • Bray, S.1    Musisi, H.2    Bienz, M.3
  • 307
  • 308
    • 27944454433 scopus 로고    scopus 로고
    • Monoubiquitination of human histone H2B: the factors involved and their roles in HOX gene regulation
    • Zhu B., Zheng Y., Pham A.D., Mandal S.S., Erdjument-Bromage H., Tempst P., Reinberg D. Monoubiquitination of human histone H2B: the factors involved and their roles in HOX gene regulation. Mol. Cell 2005, 20:601-611.
    • (2005) Mol. Cell , vol.20 , pp. 601-611
    • Zhu, B.1    Zheng, Y.2    Pham, A.D.3    Mandal, S.S.4    Erdjument-Bromage, H.5    Tempst, P.6    Reinberg, D.7
  • 311
    • 58149398016 scopus 로고    scopus 로고
    • Drosophila stem cells share a common requirement for the histone H2B ubiquitin protease scrawny
    • Buszczak M., Paterno S., Spradling A.C. Drosophila stem cells share a common requirement for the histone H2B ubiquitin protease scrawny. Science 2009, 323:248-251.
    • (2009) Science , vol.323 , pp. 248-251
    • Buszczak, M.1    Paterno, S.2    Spradling, A.C.3
  • 313
    • 38549131332 scopus 로고    scopus 로고
    • SAGA-mediated H2B deubiquitination controls the development of neuronal connectivity in the Drosophila visual system
    • Weake V.M., Lee K.K., Guelman S., Lin C.H., Seidel C., Abmayr S.M., Workman J.L. SAGA-mediated H2B deubiquitination controls the development of neuronal connectivity in the Drosophila visual system. EMBO J. 2008, 27:394-405.
    • (2008) EMBO J. , vol.27 , pp. 394-405
    • Weake, V.M.1    Lee, K.K.2    Guelman, S.3    Lin, C.H.4    Seidel, C.5    Abmayr, S.M.6    Workman, J.L.7
  • 314
    • 38149078715 scopus 로고    scopus 로고
    • The putative cancer stem cell marker USP22 is a subunit of the human SAGA complex required for activated transcription and cell-cycle progression
    • Zhang X.Y., Varthi M., Sykes S.M., Phillips C., Warzecha C., Zhu W., Wyce A., Thorne A.W., Berger S.L., McMahon S.B. The putative cancer stem cell marker USP22 is a subunit of the human SAGA complex required for activated transcription and cell-cycle progression. Mol. Cell 2008, 29:102-111.
    • (2008) Mol. Cell , vol.29 , pp. 102-111
    • Zhang, X.Y.1    Varthi, M.2    Sykes, S.M.3    Phillips, C.4    Warzecha, C.5    Zhu, W.6    Wyce, A.7    Thorne, A.W.8    Berger, S.L.9    McMahon, S.B.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.