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Volumn 15, Issue 6, 2010, Pages 553-594

Global analysis of functional relationships between histone point mutations and the effects of histone deacetylase inhibitors

Author keywords

[No Author keywords available]

Indexed keywords

CORE PROTEIN; HISTONE; HISTONE DEACETYLASE INHIBITOR; MUTANT PROTEIN; PEPTIDE LIBRARY; HISTONE DEACETYLASE;

EID: 77954155784     PISSN: 13569597     EISSN: 13652443     Source Type: Journal    
DOI: 10.1111/j.1365-2443.2010.01408.x     Document Type: Article
Times cited : (6)

References (95)
  • 1
    • 27944493925 scopus 로고    scopus 로고
    • Scale-free networks in cell biology
    • Albert R. Scale-free networks in cell biology. J. Cell Sci. 2005, 118:4947-4957.
    • (2005) J. Cell Sci. , vol.118 , pp. 4947-4957
    • Albert, R.1
  • 2
    • 0034721164 scopus 로고    scopus 로고
    • Error and attack tolerance of complex networks
    • Albert R, Jeong H, Barabasi AL. Error and attack tolerance of complex networks. Nature 2000, 406:378-382.
    • (2000) Nature , vol.406 , pp. 378-382
    • Albert, R.1    Jeong, H.2    Barabasi, A.L.3
  • 3
    • 2942612843 scopus 로고    scopus 로고
    • Ordered cooperative functions of PRMT1, p300, and CARM1 in transcriptional activation by p53
    • An W, Kim J, Roeder RG. Ordered cooperative functions of PRMT1, p300, and CARM1 in transcriptional activation by p53. Cell 2004, 117:735-748.
    • (2004) Cell , vol.117 , pp. 735-748
    • An, W.1    Kim, J.2    Roeder, R.G.3
  • 4
    • 0026672441 scopus 로고
    • Genetic interaction between transcription elongation factor TFIIS and RNA polymerase II
    • Archambault J, Lacroute F, Ruet A, Friesen JD. Genetic interaction between transcription elongation factor TFIIS and RNA polymerase II. Mol. Cell. Biol. 1992, 12:4142-4152.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 4142-4152
    • Archambault, J.1    Lacroute, F.2    Ruet, A.3    Friesen, J.D.4
  • 5
    • 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 RW, Wang BC, Love WE, Moudrianakis EN. The nucleosomal core histone octamer at 3.1 A resolution: a tripartite protein assembly and a left-handed superhelix. Proc. Natl Acad. Sci. USA 1991, 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
  • 6
    • 0027431478 scopus 로고
    • Topography of the histone octamer surface: repeating structural motifs utilized in the docking of nucleosomal DNA
    • Arents G, Moudrianakis EN. Topography of the histone octamer surface: repeating structural motifs utilized in the docking of nucleosomal DNA. Proc. Natl Acad. Sci. USA 1993, 90:10489-10493.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 10489-10493
    • Arents, G.1    Moudrianakis, E.N.2
  • 7
    • 10944233962 scopus 로고    scopus 로고
    • Recruitment of the INO80 complex by H2A phosphorylation links ATP-dependent chromatin remodeling with DNA double-strand break repair
    • van Attikum H, Fritsch O, Hohn B, Gasser SM. Recruitment of the INO80 complex by H2A phosphorylation links ATP-dependent chromatin remodeling with DNA double-strand break repair. Cell 2004, 119:777-788.
    • (2004) Cell , vol.119 , pp. 777-788
    • van Attikum, H.1    Fritsch, O.2    Hohn, B.3    Gasser, S.M.4
  • 8
    • 28444456705 scopus 로고    scopus 로고
    • The histone code at DNA breaks: a guide to repair?
    • van Attikum H, Gasser SM. The histone code at DNA breaks: a guide to repair? Nat. Rev. Mol. Cell Biol. 2005, 6:757-765.
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 757-765
    • van Attikum, H.1    Gasser, S.M.2
  • 9
    • 0742305866 scopus 로고    scopus 로고
    • Network biology: understanding the cell's functional organization
    • Barabási AL, Oltvai ZN. Network biology: understanding the cell's functional organization. Nat. Rev. Genet. 2004, 5:101-113.
    • (2004) Nat. Rev. Genet. , vol.5 , pp. 101-113
    • Barabási, A.L.1    Oltvai, Z.N.2
  • 10
    • 33845666681 scopus 로고    scopus 로고
    • Structural basis for the methylation state-specific recognition of histone H4-K20 by 53BP1 and Crb2 in DNA repair
    • Botuyan MV, Lee J, Ward IM, Kim JE, Thompson JR, Chen J, Mer G. Structural basis for the methylation state-specific recognition of histone H4-K20 by 53BP1 and Crb2 in DNA repair. Cell 2006, 127:1361-1373.
    • (2006) Cell , vol.127 , pp. 1361-1373
    • Botuyan, M.V.1    Lee, J.2    Ward, I.M.3    Kim, J.E.4    Thompson, J.R.5    Chen, J.6    Mer, G.7
  • 12
    • 33745520486 scopus 로고    scopus 로고
    • The sirtuins hst3 and Hst4p preserve genome integrity by controlling histone h3 lysine 56 deacetylation
    • Celic I, Masumoto H, Griffith WP, Meluh P, Cotter RJ, Boeke JD, Verreault A. The sirtuins hst3 and Hst4p preserve genome integrity by controlling histone h3 lysine 56 deacetylation. Curr. Biol. 2006, 16:1280-1289.
    • (2006) Curr. Biol. , vol.16 , pp. 1280-1289
    • Celic, I.1    Masumoto, H.2    Griffith, W.P.3    Meluh, P.4    Cotter, R.J.5    Boeke, J.D.6    Verreault, A.7
  • 13
    • 47549105301 scopus 로고    scopus 로고
    • Acetylated lysine 56 on histone H3 drives chromatin assembly after repair and signals for the completion of repair
    • Chen CC, Carson JJ, Feser J, Tamburini B, Zabaronick S, Linger J, Tyler JK. Acetylated lysine 56 on histone H3 drives chromatin assembly after repair and signals for the completion of repair. Cell 2008, 134:231-243.
    • (2008) Cell , vol.134 , pp. 231-243
    • Chen, C.C.1    Carson, J.J.2    Feser, J.3    Tamburini, B.4    Zabaronick, S.5    Linger, J.6    Tyler, J.K.7
  • 14
    • 0036500834 scopus 로고    scopus 로고
    • Reverse engineering of biological complexity
    • Csete ME, Doyle JC. Reverse engineering of biological complexity. Science 2002, 295:1664-1669.
    • (2002) Science , vol.295 , pp. 1664-1669
    • Csete, M.E.1    Doyle, J.C.2
  • 16
    • 36048958965 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: overview and perspectives
    • Dokmanovic M, Clarke C, Marks PA. Histone deacetylase inhibitors: overview and perspectives. Mol. Cancer Res. 2007, 5:981-989.
    • (2007) Mol. Cancer Res. , vol.5 , pp. 981-989
    • Dokmanovic, M.1    Clarke, C.2    Marks, P.A.3
  • 17
    • 0025736044 scopus 로고
    • Yeast histone H4 N-terminal sequence is required for promoter activation in vivo
    • Durrin LK, Mann RK, Kayne PS, Grunstein M. Yeast histone H4 N-terminal sequence is required for promoter activation in vivo. Cell 1991, 65:1023-1031.
    • (1991) Cell , vol.65 , pp. 1023-1031
    • Durrin, L.K.1    Mann, R.K.2    Kayne, P.S.3    Grunstein, M.4
  • 18
    • 33745686603 scopus 로고    scopus 로고
    • What properties characterize the hub proteins of the protein-protein interaction network of Saccharomyces cerevisiae?
    • Ekman D, Light S, Björklund AK, Elofsson A. What properties characterize the hub proteins of the protein-protein interaction network of Saccharomyces cerevisiae? Genome Biol. 2006, 7:R45.
    • (2006) Genome Biol. , vol.7
    • Ekman, D.1    Light, S.2    Björklund, A.K.3    Elofsson, A.4
  • 19
    • 0035101733 scopus 로고    scopus 로고
    • Dynamic interaction of DNA damage checkpoint protein Rad53 with chromatin assembly factor Asf1
    • Emili A, Schieltz DM, Yates JR, Hartwell LH. Dynamic interaction of DNA damage checkpoint protein Rad53 with chromatin assembly factor Asf1. Mol. Cell 2001, 7:13-20.
    • (2001) Mol. Cell , vol.7 , pp. 13-20
    • Emili, A.1    Schieltz, D.M.2    Yates, J.R.3    Hartwell, L.H.4
  • 20
    • 0026633013 scopus 로고
    • 6-Azauracil inhibition of GTP biosynthesis in Saccharomyces cerevisiae
    • Exinger F, Lacroute F. 6-Azauracil inhibition of GTP biosynthesis in Saccharomyces cerevisiae. Curr. Genet. 1992, 22:9-11.
    • (1992) Curr. Genet. , vol.22 , pp. 9-11
    • Exinger, F.1    Lacroute, F.2
  • 21
    • 67949102053 scopus 로고    scopus 로고
    • Recent progress in the biology and physiology of sirtuins
    • Finkel T, Deng CX, Mostoslavsky R. Recent progress in the biology and physiology of sirtuins. Nature 2009, 460:587-591.
    • (2009) Nature , vol.460 , pp. 587-591
    • Finkel, T.1    Deng, C.X.2    Mostoslavsky, R.3
  • 23
    • 0037173615 scopus 로고    scopus 로고
    • Functional profiling of the Saccharomyces cerevisiae genome
    • Giaever G, Chu AM, Ni L. Functional profiling of the Saccharomyces cerevisiae genome. Nature 2002, 418:387-391.
    • (2002) Nature , vol.418 , pp. 387-391
    • Giaever, G.1    Chu, A.M.2    Ni, L.3
  • 24
    • 1842578986 scopus 로고    scopus 로고
    • Molecular evolution of the histone deacetylase family: functional implications of phylogenetic analysis
    • Gregoretti IV, Lee YM, Goodson HV. Molecular evolution of the histone deacetylase family: functional implications of phylogenetic analysis. J. Mol. Biol. 2004, 338:17-31.
    • (2004) J. Mol. Biol. , vol.338 , pp. 17-31
    • Gregoretti, I.V.1    Lee, Y.M.2    Goodson, H.V.3
  • 25
    • 0036947243 scopus 로고    scopus 로고
    • Immunosuppressant-like effects of phenylbutyrate on growth inhibition of Saccharomyces cerevisiae
    • Grzanowski A, Needleman R, Brusilow WS. Immunosuppressant-like effects of phenylbutyrate on growth inhibition of Saccharomyces cerevisiae. Curr. Genet. 2002, 41:142-149.
    • (2002) Curr. Genet. , vol.41 , pp. 142-149
    • Grzanowski, A.1    Needleman, R.2    Brusilow, W.S.3
  • 26
    • 33845868198 scopus 로고    scopus 로고
    • Sirtuins as potential targets for metabolic syndrome
    • Guarente L. Sirtuins as potential targets for metabolic syndrome. Nature 2006, 444:868-874.
    • (2006) Nature , vol.444 , pp. 868-874
    • Guarente, L.1
  • 27
    • 57749170458 scopus 로고    scopus 로고
    • The many roles of histone deacetylases in development and physiology: implications for disease and therapy
    • Haberland M, Montgomery RL, Olson EN. The many roles of histone deacetylases in development and physiology: implications for disease and therapy. Nat. Rev. Genet. 2009, 10:32-42.
    • (2009) Nat. Rev. Genet. , vol.10 , pp. 32-42
    • Haberland, M.1    Montgomery, R.L.2    Olson, E.N.3
  • 29
    • 0024472603 scopus 로고
    • A receptor for the immunosuppressant FK506 is a cis-trans peptidyl-prolyl isomerase
    • Harding MW, Galat A, Uehling DE, Schreiber SL. A receptor for the immunosuppressant FK506 is a cis-trans peptidyl-prolyl isomerase. Nature 1989, 341:758-760.
    • (1989) Nature , vol.341 , pp. 758-760
    • Harding, M.W.1    Galat, A.2    Uehling, D.E.3    Schreiber, S.L.4
  • 30
    • 67649476233 scopus 로고    scopus 로고
    • Theoretical framework for the histone modification network: modifications in the unstructured histone tails form a robust scale-free network
    • Hayashi Y, Senda T, Sano N, Horikoshi M. Theoretical framework for the histone modification network: modifications in the unstructured histone tails form a robust scale-free network. Genes Cells 2009, 14:789-806.
    • (2009) Genes Cells , vol.14 , pp. 789-806
    • Hayashi, Y.1    Senda, T.2    Sano, N.3    Horikoshi, M.4
  • 31
    • 0032725567 scopus 로고    scopus 로고
    • Relationship between the subcellular localization and structures of catalytic domains of FKBP-type PPIases
    • Himukai R, Kuzuhara T, Horikoshi M. Relationship between the subcellular localization and structures of catalytic domains of FKBP-type PPIases. J. Biochem. 1999, 126:879-888.
    • (1999) J. Biochem. , vol.126 , pp. 879-888
    • Himukai, R.1    Kuzuhara, T.2    Horikoshi, M.3
  • 32
    • 0023732753 scopus 로고
    • Mechanism of action of a yeast activator: direct effect of GAL4 derivatives on mammalian TFIID-promoter interactions
    • Horikoshi M, Carey MF, Kakidani H, Roeder RG. Mechanism of action of a yeast activator: direct effect of GAL4 derivatives on mammalian TFIID-promoter interactions. Cell 1988, 54:665-669.
    • (1988) Cell , vol.54 , pp. 665-669
    • Horikoshi, M.1    Carey, M.F.2    Kakidani, H.3    Roeder, R.G.4
  • 36
    • 32944469082 scopus 로고    scopus 로고
    • A decade of histone acetylation: marking eukaryotic chromosomes with specific codes
    • Kimura A, Matsubara K, Horikoshi M. A decade of histone acetylation: marking eukaryotic chromosomes with specific codes. J. Biochem. 2005, 138:647-662.
    • (2005) J. Biochem. , vol.138 , pp. 647-662
    • Kimura, A.1    Matsubara, K.2    Horikoshi, M.3
  • 37
    • 0036843170 scopus 로고    scopus 로고
    • Chromosomal gradient of histone acetylation established by Sas2p and Sir2p functions as a shield against gene silencing
    • Kimura A, Umehara T, Horikoshi M. Chromosomal gradient of histone acetylation established by Sas2p and Sir2p functions as a shield against gene silencing. Nat. Genet. 2002, 32:370-377.
    • (2002) Nat. Genet. , vol.32 , pp. 370-377
    • Kimura, A.1    Umehara, T.2    Horikoshi, M.3
  • 38
    • 0036500993 scopus 로고    scopus 로고
    • Systems biology: a brief overview
    • Kitano H. Systems biology: a brief overview. Science 2002, 295:1662-1664.
    • (2002) Science , vol.295 , pp. 1662-1664
    • Kitano, H.1
  • 39
    • 0016221697 scopus 로고
    • Chromatin structure: a repeating unit of histones and DNA
    • Kornberg RD. Chromatin structure: a repeating unit of histones and DNA. Science 1974, 184:868-871.
    • (1974) Science , vol.184 , pp. 868-871
    • Kornberg, R.D.1
  • 40
    • 33847076849 scopus 로고    scopus 로고
    • Chromatin modifications and their function
    • Kouzarides T. Chromatin modifications and their function. Cell 2007, 128:693-705.
    • (2007) Cell , vol.128 , pp. 693-705
    • Kouzarides, T.1
  • 42
    • 1442286922 scopus 로고    scopus 로고
    • A nuclear FK506-binding protein is a histone chaperone regulating rDNA silencing
    • Kuzuhara T, Horikoshi M. A nuclear FK506-binding protein is a histone chaperone regulating rDNA silencing. Nat. Struct. Mol. Biol. 2004, 11:275-283.
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 275-283
    • Kuzuhara, T.1    Horikoshi, M.2
  • 43
    • 0037672689 scopus 로고    scopus 로고
    • An epigenetic road map for histone lysine methylation
    • Lachner M, O'Sullivan RJ, Jenuwein T. An epigenetic road map for histone lysine methylation. J. Cell Sci. 2003, 116:2117-2124.
    • (2003) J. Cell Sci. , vol.116 , pp. 2117-2124
    • Lachner, M.1    O'Sullivan, R.J.2    Jenuwein, T.3
  • 44
    • 0030862060 scopus 로고    scopus 로고
    • Two new S-phase-specific genes from Saccharomyces cerevisiae
    • Le S, Davis C, Konopka JB, Sternglanz R. Two new S-phase-specific genes from Saccharomyces cerevisiae. Yeast 1997, 13:1029-1042.
    • (1997) Yeast , vol.13 , pp. 1029-1042
    • Le, S.1    Davis, C.2    Konopka, J.B.3    Sternglanz, R.4
  • 46
    • 0037174671 scopus 로고    scopus 로고
    • Transcriptional regulatory networks in Saccharomyces cerevisiae
    • Lee TI, Rinaldi NJ, Robert F. Transcriptional regulatory networks in Saccharomyces cerevisiae. Science 2002, 298:799-804.
    • (2002) Science , vol.298 , pp. 799-804
    • Lee, T.I.1    Rinaldi, N.J.2    Robert, F.3
  • 48
    • 0029878216 scopus 로고    scopus 로고
    • Yeast histone H3 and H4 amino termini are important for nucleosome assembly in vivo and in vitro: redundant and position-independent functions in assembly but not in gene regulation
    • Ling X, Harkness TA, Schultz MC, Fisher-Adams G, Grunstein M. Yeast histone H3 and H4 amino termini are important for nucleosome assembly in vivo and in vitro: redundant and position-independent functions in assembly but not in gene regulation. Genes Dev. 1996, 10:686-699.
    • (1996) Genes Dev. , vol.10 , pp. 686-699
    • Ling, X.1    Harkness, T.A.2    Schultz, M.C.3    Fisher-Adams, G.4    Grunstein, M.5
  • 49
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 Å resolution
    • Luger K, Mäder AW, Richmond RK, Sargent DF, Richmond TJ. Crystal structure of the nucleosome core particle at 2.8 Å resolution. Nature 1997, 389:251-260.
    • (1997) Nature , vol.389 , pp. 251-260
    • Luger, K.1    Mäder, A.W.2    Richmond, R.K.3    Sargent, D.F.4    Richmond, T.J.5
  • 50
    • 22444448143 scopus 로고    scopus 로고
    • A role for cell-cycle-regulated histone H3 lysine 56 acetylation in the DNA damage response
    • Masumoto H, Hawke D, Kobayashi R, Verreault A. A role for cell-cycle-regulated histone H3 lysine 56 acetylation in the DNA damage response. Nature 2005, 436:294-298.
    • (2005) Nature , vol.436 , pp. 294-298
    • Masumoto, H.1    Hawke, D.2    Kobayashi, R.3    Verreault, A.4
  • 51
    • 33845880445 scopus 로고    scopus 로고
    • Global analysis of functional surfaces of core histones with comprehensive point mutants
    • Matsubara K, Sano N, Umehara T, Horikoshi M. Global analysis of functional surfaces of core histones with comprehensive point mutants. Genes Cells 2007, 12:13-33.
    • (2007) Genes Cells , vol.12 , pp. 13-33
    • Matsubara, K.1    Sano, N.2    Umehara, T.3    Horikoshi, M.4
  • 52
    • 58149333884 scopus 로고    scopus 로고
    • Pnc1p-mediated nicotinamide clearance modifies the epigenetic properties of rDNA silencing in Saccharomyces cerevisiae
    • McClure JM, Gallo CM, Smith DL, Matecic M, Hontz RD, Buck SW, Racette FG, Smith JS. Pnc1p-mediated nicotinamide clearance modifies the epigenetic properties of rDNA silencing in Saccharomyces cerevisiae. Genetics 2008, 180:797-810.
    • (2008) Genetics , vol.180 , pp. 797-810
    • McClure, J.M.1    Gallo, C.M.2    Smith, D.L.3    Matecic, M.4    Hontz, R.D.5    Buck, S.W.6    Racette, F.G.7    Smith, J.S.8
  • 53
    • 33645002813 scopus 로고    scopus 로고
    • Acetylation of H2AZ Lys 14 is associated with genome-wide gene activity in yeast
    • Millar CB, Xu F, Zhang K, Grunstein M. Acetylation of H2AZ Lys 14 is associated with genome-wide gene activity in yeast. Genes Dev. 2006, 20:711-722.
    • (2006) Genes Dev. , vol.20 , pp. 711-722
    • Millar, C.B.1    Xu, F.2    Zhang, K.3    Grunstein, M.4
  • 54
    • 30344477367 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors and the promise of epigenetic (and more) treatments for cancer
    • Minucci S, Pelicci PG. Histone deacetylase inhibitors and the promise of epigenetic (and more) treatments for cancer. Nat. Rev. Cancer 2006, 6:38-51.
    • (2006) Nat. Rev. Cancer , vol.6 , pp. 38-51
    • Minucci, S.1    Pelicci, P.G.2
  • 55
    • 34548569327 scopus 로고    scopus 로고
    • Diverse roles for histone H2A modifications in DNA damage response pathways in yeast
    • Moore JD, Yazgan O, Ataian Y, Krebs JE. Diverse roles for histone H2A modifications in DNA damage response pathways in yeast. Genetics 2007, 176:15-25.
    • (2007) Genetics , vol.176 , pp. 15-25
    • Moore, J.D.1    Yazgan, O.2    Ataian, Y.3    Krebs, J.E.4
  • 57
    • 0034100123 scopus 로고    scopus 로고
    • A human homologue of yeast anti-silencing factor has histone chaperone activity
    • Munakata T, Adachi N, Yokoyama N, Kuzuhara T, Horikoshi M. A human homologue of yeast anti-silencing factor has histone chaperone activity. Genes Cells 2000, 5:221-233.
    • (2000) Genes Cells , vol.5 , pp. 221-233
    • Munakata, T.1    Adachi, N.2    Yokoyama, N.3    Kuzuhara, T.4    Horikoshi, M.5
  • 60
    • 33847226680 scopus 로고    scopus 로고
    • Structure and function of the histone chaperone CIA/ASF1 complexed with histones H3 and H4
    • Natsume R, Eitoku M, Akai Y, Sano N, Horikoshi M, Senda T. Structure and function of the histone chaperone CIA/ASF1 complexed with histones H3 and H4. Nature 2007, 446:338-341.
    • (2007) Nature , vol.446 , pp. 338-341
    • Natsume, R.1    Eitoku, M.2    Akai, Y.3    Sano, N.4    Horikoshi, M.5    Senda, T.6
  • 61
    • 33748163064 scopus 로고    scopus 로고
    • Proline isomerization of histone H3 regulates lysine methylation and gene expression
    • Nelson CJ, 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
  • 63
    • 0037174638 scopus 로고    scopus 로고
    • Systems biology. Life's complexity pyramid
    • Oltvai ZN, Barabási AL. Systems biology. Life's complexity pyramid. Science 2002, 298:763-764.
    • (2002) Science , vol.298 , pp. 763-764
    • Oltvai, Z.N.1    Barabási, A.L.2
  • 65
    • 35649016107 scopus 로고    scopus 로고
    • Regulation of gene transcription by the histone H2A N-terminal domain
    • Parra MA, Wyrick JJ. Regulation of gene transcription by the histone H2A N-terminal domain. Mol. Cell. Biol. 2007, 27:7641-7648.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 7641-7648
    • Parra, M.A.1    Wyrick, J.J.2
  • 66
    • 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
  • 67
    • 0017409010 scopus 로고
    • Isolation and characterization of MMS-sensitive mutants of Saccharomyces cerevisiae
    • Prakash L, Prakash S. Isolation and characterization of MMS-sensitive mutants of Saccharomyces cerevisiae. Genetics 1977, 86:33-55.
    • (1977) Genetics , vol.86 , pp. 33-55
    • Prakash, L.1    Prakash, S.2
  • 68
    • 13444267442 scopus 로고    scopus 로고
    • Chd1 chromodomain links histone H3 methylation with SAGA- and SLIK-dependent acetylation
    • Pray-Grant MG, Daniel JA, Schieltz D, Yates JR, Grant PA. Chd1 chromodomain links histone H3 methylation with SAGA- and SLIK-dependent acetylation. Nature 2005, 433:434-438.
    • (2005) Nature , vol.433 , pp. 434-438
    • Pray-Grant, M.G.1    Daniel, J.A.2    Schieltz, D.3    Yates, J.R.4    Grant, P.A.5
  • 69
    • 0023683667 scopus 로고
    • How eukaryotic transcriptional activators work
    • Ptashne M. How eukaryotic transcriptional activators work. Nature 1988, 335:683-689.
    • (1988) Nature , vol.335 , pp. 683-689
    • Ptashne, M.1
  • 70
    • 0034695456 scopus 로고    scopus 로고
    • Rad6-dependent ubiquitination of histone H2B in yeast
    • Robzyk K, Recht J, Osley MA. 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
  • 71
    • 50549209851 scopus 로고
    • Hydroxyurea: a specific inhibitor of deoxyribonucleic acid synthesis
    • Rosenkranz HS, Levy JA. Hydroxyurea: a specific inhibitor of deoxyribonucleic acid synthesis. Biochim. Biophys. Acta 1965, 95:181-183.
    • (1965) Biochim. Biophys. Acta , vol.95 , pp. 181-183
    • Rosenkranz, H.S.1    Levy, J.A.2
  • 72
  • 73
    • 8844248619 scopus 로고    scopus 로고
    • Methylation of histone H4 lysine 20 controls recruitment of Crb2 to sites of DNA damage
    • Sanders SL, Portoso M, Mata J, Bähler J, Allshire RC, Kouzarides T. Methylation of histone H4 lysine 20 controls recruitment of Crb2 to sites of DNA damage. Cell 2004, 119:603-614.
    • (2004) Cell , vol.119 , pp. 603-614
    • Sanders, S.L.1    Portoso, M.2    Mata, J.3    Bähler, J.4    Allshire, R.C.5    Kouzarides, T.6
  • 74
    • 0022500042 scopus 로고
    • Yeast histone H2A and H2B amino termini have interchangeable functions
    • Schuster T, Han M, Grunstein M. Yeast histone H2A and H2B amino termini have interchangeable functions. Cell 1986, 45:445-451.
    • (1986) Cell , vol.45 , pp. 445-451
    • Schuster, T.1    Han, M.2    Grunstein, M.3
  • 75
    • 0024556318 scopus 로고
    • Monofunctional alkylating agentinduced S-phase-dependent DNA damage
    • Schwartz JL. Monofunctional alkylating agentinduced S-phase-dependent DNA damage. Mutat. Res. 1989, 216:111-118.
    • (1989) Mutat. Res. , vol.216 , pp. 111-118
    • Schwartz, J.L.1
  • 76
    • 34547890019 scopus 로고    scopus 로고
    • Functions of site-specific histone acetylation and deacetylation
    • Shahbazian MD, Grunstein M. Functions of site-specific histone acetylation and deacetylation. Annu. Rev. Biochem. 2007, 76:75-100.
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 75-100
    • Shahbazian, M.D.1    Grunstein, M.2
  • 77
    • 33745868054 scopus 로고    scopus 로고
    • ING2 PHD domain links histone H3 lysine 4 methylation to active gene repression
    • Shi X, Hong T, Walter KL. ING2 PHD domain links histone H3 lysine 4 methylation to active gene repression. Nature 2006, 442:96-99.
    • (2006) Nature , vol.442 , pp. 96-99
    • Shi, X.1    Hong, T.2    Walter, K.L.3
  • 78
    • 0024442393 scopus 로고
    • A cytosolic binding protein for the immunosuppressant FK506 has peptidyl-prolyl isomerase activity but is distinct from cyclophilin
    • Siekierka JJ, Hung SH, Poe M, Lin CS, Sigal NH. A cytosolic binding protein for the immunosuppressant FK506 has peptidyl-prolyl isomerase activity but is distinct from cyclophilin. Nature 1989, 341:755-757.
    • (1989) Nature , vol.341 , pp. 755-757
    • Siekierka, J.J.1    Hung, S.H.2    Poe, M.3    Lin, C.S.4    Sigal, N.H.5
  • 79
    • 0024291679 scopus 로고
    • Transcriptional activation. Acid blobs and negative noodles
    • Sigler PB. Transcriptional activation. Acid blobs and negative noodles. Nature 1988, 333:210-212.
    • (1988) Nature , vol.333 , pp. 210-212
    • Sigler, P.B.1
  • 80
    • 0021659582 scopus 로고
    • Effects of Ty insertions on HIS4 transcription in Saccharomyces cerevisiae
    • Silverman SJ, Fink GR. Effects of Ty insertions on HIS4 transcription in Saccharomyces cerevisiae. Mol. Cell. Biol. 1984, 4:1246-1251.
    • (1984) Mol. Cell. Biol. , vol.4 , pp. 1246-1251
    • Silverman, S.J.1    Fink, G.R.2
  • 81
    • 0022292635 scopus 로고
    • In vitro mutagenesis
    • Smith M. In vitro mutagenesis. Annu. Rev. Genet. 1985, 19:423-462.
    • (1985) Annu. Rev. Genet. , vol.19 , pp. 423-462
    • Smith, M.1
  • 82
    • 0036842129 scopus 로고    scopus 로고
    • Sir2p and Sas2p opposingly regulate acetylation of yeast histone H4 lysine16 and spreading of heterochromatin
    • Suka N, Luo K, Grunstein M. Sir2p and Sas2p opposingly regulate acetylation of yeast histone H4 lysine16 and spreading of heterochromatin. Nat. Genet. 2002, 32:378-383.
    • (2002) Nat. Genet. , vol.32 , pp. 378-383
    • Suka, N.1    Luo, K.2    Grunstein, M.3
  • 84
    • 0016729499 scopus 로고
    • Hydroxyurea
    • Timson J. Hydroxyurea. Mutat. Res. 1975, 32:115-132.
    • (1975) Mutat. Res. , vol.32 , pp. 115-132
    • Timson, J.1
  • 86
    • 0035903534 scopus 로고    scopus 로고
    • Structure of the yeast nucleosome core particle reveals fundamental changes in internucleosome interactions
    • White CL, Suto RK, Luger K. Structure of the yeast nucleosome core particle reveals fundamental changes in internucleosome interactions. EMBO J. 2001, 20:5207-5218.
    • (2001) EMBO J. , vol.20 , pp. 5207-5218
    • White, C.L.1    Suto, R.K.2    Luger, K.3
  • 87
    • 0032749078 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm
    • Wright PE, Dyson HJ. Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm. J. Mol. Biol. 1999, 293:321-331.
    • (1999) J. Mol. Biol. , vol.293 , pp. 321-331
    • Wright, P.E.1    Dyson, H.J.2
  • 88
    • 33845726097 scopus 로고    scopus 로고
    • Methylating agents and DNA repair responses: methylated bases and sources of strand breaks
    • Wyatt MD, Pittman DL. Methylating agents and DNA repair responses: methylated bases and sources of strand breaks. Chem. Res. Toxicol. 2006, 19:1580-1594.
    • (2006) Chem. Res. Toxicol. , vol.19 , pp. 1580-1594
    • Wyatt, M.D.1    Pittman, D.L.2
  • 89
    • 0035116375 scopus 로고    scopus 로고
    • SPT genes: key players in the regulation of transcription, chromatin structure and other cellular processes
    • Yamaguchi Y, Narita T, Inukai N, Wada T, Handa H. SPT genes: key players in the regulation of transcription, chromatin structure and other cellular processes. J. Biochem. 2001, 129:185-191.
    • (2001) J. Biochem. , vol.129 , pp. 185-191
    • Yamaguchi, Y.1    Narita, T.2    Inukai, N.3    Wada, T.4    Handa, H.5
  • 91
    • 39749127166 scopus 로고    scopus 로고
    • The Rpd3/Hda1 family of lysine deacetylases: from bacteria and yeast to mice and men
    • Yang XJ, Seto E. The Rpd3/Hda1 family of lysine deacetylases: from bacteria and yeast to mice and men. Nat. Rev. Mol. Cell Biol. 2008, 9:206-218.
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 206-218
    • Yang, X.J.1    Seto, E.2
  • 93
    • 0141483484 scopus 로고    scopus 로고
    • Identification of novel histone post-translational modifications by peptide mass fingerprinting
    • Zhang L, Eugeni EE, Parthun MR, Freitas MA. Identification of novel histone post-translational modifications by peptide mass fingerprinting. Chromosoma 2003, 112:77-86.
    • (2003) Chromosoma , vol.112 , pp. 77-86
    • Zhang, L.1    Eugeni, E.E.2    Parthun, M.R.3    Freitas, M.A.4
  • 94
    • 23244448558 scopus 로고    scopus 로고
    • The PHD finger/bromodomain of NoRC interacts with acetylated histone H4K16 and is sufficient for rDNA silencing
    • Zhou Y, Grummt I. The PHD finger/bromodomain of NoRC interacts with acetylated histone H4K16 and is sufficient for rDNA silencing. Curr. Biol. 2005, 15:1434-1438.
    • (2005) Curr. Biol. , vol.15 , pp. 1434-1438
    • Zhou, Y.1    Grummt, I.2
  • 95
    • 70149112313 scopus 로고    scopus 로고
    • Histone crosstalk between H3S10ph and H4K16ac generates a histone code that mediates transcription elongation
    • Zippo A, Serafini R, Rocchigiani M, Pennacchini S, Krepelova A, Oliviero S. Histone crosstalk between H3S10ph and H4K16ac generates a histone code that mediates transcription elongation. Cell 2009, 138:1122-1136.
    • (2009) Cell , vol.138 , pp. 1122-1136
    • Zippo, A.1    Serafini, R.2    Rocchigiani, M.3    Pennacchini, S.4    Krepelova, A.5    Oliviero, S.6


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