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Volumn 45, Issue 6, 2012, Pages 790-800

Inheritance of Silent rDNA Chromatin Is Mediated by PARP1 via Noncoding RNA

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE RIBOSE; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE 1; RIBOSOME DNA; RIBOSOME RNA; TIP5 PROTEIN; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG; UNTRANSLATED RNA;

EID: 84859051225     PISSN: 10972765     EISSN: 10974164     Source Type: Journal    
DOI: 10.1016/j.molcel.2012.01.024     Document Type: Article
Times cited : (127)

References (61)
  • 1
    • 0018599238 scopus 로고
    • Isolation and partial characterization of the ADP-ribosylated nuclear proteins from Ehrlich ascites tumor cells
    • Adamietz P., Klapproth K., Hilz H. Isolation and partial characterization of the ADP-ribosylated nuclear proteins from Ehrlich ascites tumor cells. Biochem. Biophys. Res. Commun. 1979, 91:1232-1238.
    • (1979) Biochem. Biophys. Res. Commun. , vol.91 , pp. 1232-1238
    • Adamietz, P.1    Klapproth, K.2    Hilz, H.3
  • 2
    • 0024781397 scopus 로고
    • DNA replication and poly(ADP-ribosyl)ation of chromatin
    • Anachkova B., Russev G., Poirier G.G. DNA replication and poly(ADP-ribosyl)ation of chromatin. Cytobios 1989, 58:19-28.
    • (1989) Cytobios , vol.58 , pp. 19-28
    • Anachkova, B.1    Russev, G.2    Poirier, G.G.3
  • 5
    • 63149116496 scopus 로고    scopus 로고
    • Combining affinity purification by ADP-ribose-binding macro domains with mass spectrometry to define the mammalian ADP-ribosyl proteome
    • Dani N., Stilla A., Marchegiani A., Tamburro A., Till S., Ladurner A.G., Corda D., Di Girolamo M. Combining affinity purification by ADP-ribose-binding macro domains with mass spectrometry to define the mammalian ADP-ribosyl proteome. Proc. Natl. Acad. Sci. USA 2009, 106:4243-4248.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 4243-4248
    • Dani, N.1    Stilla, A.2    Marchegiani, A.3    Tamburro, A.4    Till, S.5    Ladurner, A.G.6    Corda, D.7    Di Girolamo, M.8
  • 6
    • 0032522224 scopus 로고    scopus 로고
    • Functional association of poly(ADP-ribose) polymerase with DNA polymerase alpha-primase complex: a link between DNA strand break detection and DNA replication
    • Dantzer F., Nasheuer H.P., Vonesch J.L., de Murcia G., Ménissier-de Murcia J. Functional association of poly(ADP-ribose) polymerase with DNA polymerase alpha-primase complex: a link between DNA strand break detection and DNA replication. Nucleic Acids Res. 1998, 26:1891-1898.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 1891-1898
    • Dantzer, F.1    Nasheuer, H.P.2    Vonesch, J.L.3    de Murcia, G.4    Ménissier-de Murcia, J.5
  • 8
    • 0036710459 scopus 로고    scopus 로고
    • The functional role of poly(ADP-ribose)polymerase 1 as novel coactivator of NF-kappaB in inflammatory disorders
    • Hassa P.O., Hottiger M.O. The functional role of poly(ADP-ribose)polymerase 1 as novel coactivator of NF-kappaB in inflammatory disorders. Cell. Mol. Life Sci. 2002, 59:1534-1553.
    • (2002) Cell. Mol. Life Sci. , vol.59 , pp. 1534-1553
    • Hassa, P.O.1    Hottiger, M.O.2
  • 9
    • 38449088040 scopus 로고    scopus 로고
    • The diverse biological roles of mammalian PARPS, a small but powerful family of poly-ADP-ribose polymerases
    • Hassa P.O., Hottiger M.O. The diverse biological roles of mammalian PARPS, a small but powerful family of poly-ADP-ribose polymerases. Front. Biosci. 2008, 13:3046-3082.
    • (2008) Front. Biosci. , vol.13 , pp. 3046-3082
    • Hassa, P.O.1    Hottiger, M.O.2
  • 11
    • 0024406764 scopus 로고
    • The effect of poly(ADP-ribosyl)ation on native and H1-depleted chromatin. A role of poly(ADP-ribosyl)ation on core nucleosome structure
    • Huletsky A., de Murcia G., Muller S., Hengartner M., Ménard L., Lamarre D., Poirier G.G. The effect of poly(ADP-ribosyl)ation on native and H1-depleted chromatin. A role of poly(ADP-ribosyl)ation on core nucleosome structure. J. Biol. Chem. 1989, 264:8878-8886.
    • (1989) J. Biol. Chem. , vol.264 , pp. 8878-8886
    • Huletsky, A.1    de Murcia, G.2    Muller, S.3    Hengartner, M.4    Ménard, L.5    Lamarre, D.6    Poirier, G.G.7
  • 12
    • 79955500550 scopus 로고    scopus 로고
    • Broken silence restored-remodeling primes for deacetylation at replication forks
    • Jasencakova Z., Groth A. Broken silence restored-remodeling primes for deacetylation at replication forks. Mol. Cell 2011, 42:267-269.
    • (2011) Mol. Cell , vol.42 , pp. 267-269
    • Jasencakova, Z.1    Groth, A.2
  • 13
    • 77956648852 scopus 로고    scopus 로고
    • The roles of PARP1 in gene control and cell differentiation
    • Ji Y., Tulin A.V. The roles of PARP1 in gene control and cell differentiation. Curr. Opin. Genet. Dev. 2010, 20:512-518.
    • (2010) Curr. Opin. Genet. Dev. , vol.20 , pp. 512-518
    • Ji, Y.1    Tulin, A.V.2
  • 14
    • 0030667684 scopus 로고    scopus 로고
    • Cell cycle-dependent colocalization of BARD1 and BRCA1 proteins in discrete nuclear domains
    • Jin Y., Xu X.L., Yang M.C., Wei F., Ayi T.C., Bowcock A.M., Baer R. Cell cycle-dependent colocalization of BARD1 and BRCA1 proteins in discrete nuclear domains. Proc. Natl. Acad. Sci. USA 1997, 94:12075-12080.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 12075-12080
    • Jin, Y.1    Xu, X.L.2    Yang, M.C.3    Wei, F.4    Ayi, T.C.5    Bowcock, A.M.6    Baer, R.7
  • 15
    • 0018796405 scopus 로고
    • Nuclear protein modification and chromatin substructure. 3. Relationship between poly(adenosine diphosphate) ribosylation and different functional forms of chromatin
    • Jump D.B., Butt T.R., Smulson M. Nuclear protein modification and chromatin substructure. 3. Relationship between poly(adenosine diphosphate) ribosylation and different functional forms of chromatin. Biochemistry 1979, 18:983-990.
    • (1979) Biochemistry , vol.18 , pp. 983-990
    • Jump, D.B.1    Butt, T.R.2    Smulson, M.3
  • 16
    • 0037379179 scopus 로고    scopus 로고
    • Involvement of poly(ADP-Ribose) polymerase 1 and poly(ADP-Ribosyl)ation in regulation of centrosome function
    • Kanai M., Tong W.M., Sugihara E., Wang Z.Q., Fukasawa K., Miwa M. Involvement of poly(ADP-Ribose) polymerase 1 and poly(ADP-Ribosyl)ation in regulation of centrosome function. Mol. Cell. Biol. 2003, 23:2451-2462.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 2451-2462
    • Kanai, M.1    Tong, W.M.2    Sugihara, E.3    Wang, Z.Q.4    Fukasawa, K.5    Miwa, M.6
  • 18
    • 0021774471 scopus 로고
    • Monoclonal antibodies to poly(adenosine diphosphate ribose) recognize different structures
    • Kawamitsu H., Hoshino H., Okada H., Miwa M., Momoi H., Sugimura T. Monoclonal antibodies to poly(adenosine diphosphate ribose) recognize different structures. Biochemistry 1984, 23:3771-3777.
    • (1984) Biochemistry , vol.23 , pp. 3771-3777
    • Kawamitsu, H.1    Hoshino, H.2    Okada, H.3    Miwa, M.4    Momoi, H.5    Sugimura, T.6
  • 19
    • 10944227347 scopus 로고    scopus 로고
    • NAD+-dependent modulation of chromatin structure and transcription by nucleosome binding properties of PARP-1
    • Kim M.Y., Mauro S., Gévry N., Lis J.T., Kraus W.L. NAD+-dependent modulation of chromatin structure and transcription by nucleosome binding properties of PARP-1. Cell 2004, 119:803-814.
    • (2004) Cell , vol.119 , pp. 803-814
    • Kim, M.Y.1    Mauro, S.2    Gévry, N.3    Lis, J.T.4    Kraus, W.L.5
  • 20
    • 77950870459 scopus 로고    scopus 로고
    • Uncoupling of the transactivation and transrepression functions of PARP1 protein
    • Kotova E., Jarnik M., Tulin A.V. Uncoupling of the transactivation and transrepression functions of PARP1 protein. Proc. Natl. Acad. Sci. USA 2010, 107:6406-6411.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 6406-6411
    • Kotova, E.1    Jarnik, M.2    Tulin, A.V.3
  • 21
    • 0038682011 scopus 로고    scopus 로고
    • PARP goes transcription
    • Kraus W.L., Lis J.T. PARP goes transcription. Cell 2003, 113:677-683.
    • (2003) Cell , vol.113 , pp. 677-683
    • Kraus, W.L.1    Lis, J.T.2
  • 22
    • 77954274504 scopus 로고    scopus 로고
    • The PARP side of the nucleus: molecular actions, physiological outcomes, and clinical targets
    • Krishnakumar R., Kraus W.L. The PARP side of the nucleus: molecular actions, physiological outcomes, and clinical targets. Mol. Cell 2010, 39:8-24.
    • (2010) Mol. Cell , vol.39 , pp. 8-24
    • Krishnakumar, R.1    Kraus, W.L.2
  • 23
    • 38949198773 scopus 로고    scopus 로고
    • Reciprocal binding of PARP-1 and histone H1 at promoters specifies transcriptional outcomes
    • Krishnakumar R., Gamble M.J., Frizzell K.M., Berrocal J.G., Kininis M., Kraus W.L. Reciprocal binding of PARP-1 and histone H1 at promoters specifies transcriptional outcomes. Science 2008, 319:819-821.
    • (2008) Science , vol.319 , pp. 819-821
    • Krishnakumar, R.1    Gamble, M.J.2    Frizzell, K.M.3    Berrocal, J.G.4    Kininis, M.5    Kraus, W.L.6
  • 24
    • 0026651978 scopus 로고
    • Ethidium bromide provides a simple tool for identifying genuine DNA-independent protein associations
    • Lai J.S., Herr W. Ethidium bromide provides a simple tool for identifying genuine DNA-independent protein associations. Proc. Natl. Acad. Sci. USA 1992, 89:6958-6962.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 6958-6962
    • Lai, J.S.1    Herr, W.2
  • 25
    • 0015962328 scopus 로고
    • The relationship between cell growth, macromolecular synthesis and poly ADP-ribose polymerase in lymphoid cells
    • Lehmann A.R., Kirk-Bell S., Shall S., Whish W.J. The relationship between cell growth, macromolecular synthesis and poly ADP-ribose polymerase in lymphoid cells. Exp. Cell Res. 1974, 83:63-72.
    • (1974) Exp. Cell Res. , vol.83 , pp. 63-72
    • Lehmann, A.R.1    Kirk-Bell, S.2    Shall, S.3    Whish, W.J.4
  • 26
    • 0027157277 scopus 로고
    • ADP-ribosylation of nucleolar proteins in HeLa tumor cells
    • Leitinger N., Wesierska-Gadek J. ADP-ribosylation of nucleolar proteins in HeLa tumor cells. J. Cell. Biochem. 1993, 52:153-158.
    • (1993) J. Cell. Biochem. , vol.52 , pp. 153-158
    • Leitinger, N.1    Wesierska-Gadek, J.2
  • 27
    • 13244277994 scopus 로고    scopus 로고
    • The chromatin remodeling complex NoRC controls replication timing of rRNA genes
    • Li J., Santoro R., Koberna K., Grummt I. The chromatin remodeling complex NoRC controls replication timing of rRNA genes. EMBO J. 2005, 24:120-127.
    • (2005) EMBO J. , vol.24 , pp. 120-127
    • Li, J.1    Santoro, R.2    Koberna, K.3    Grummt, I.4
  • 28
    • 0023117437 scopus 로고
    • Release of core DNA from nucleosomal core particles following (ADP-ribose)n-modification in vitro
    • Mathis G., Althaus F.R. Release of core DNA from nucleosomal core particles following (ADP-ribose)n-modification in vitro. Biochem. Biophys. Res. Commun. 1987, 143:1049-1054.
    • (1987) Biochem. Biophys. Res. Commun. , vol.143 , pp. 1049-1054
    • Mathis, G.1    Althaus, F.R.2
  • 29
    • 33646147563 scopus 로고    scopus 로고
    • Intergenic transcripts regulate the epigenetic state of rRNA genes
    • Mayer C., Schmitz K.M., Li J., Grummt I., Santoro R. Intergenic transcripts regulate the epigenetic state of rRNA genes. Mol. Cell 2006, 22:351-361.
    • (2006) Mol. Cell , vol.22 , pp. 351-361
    • Mayer, C.1    Schmitz, K.M.2    Li, J.3    Grummt, I.4    Santoro, R.5
  • 30
    • 48649106585 scopus 로고    scopus 로고
    • The structure of NoRC-associated RNA is crucial for targeting the chromatin remodelling complex NoRC to the nucleolus
    • Mayer C., Neubert M., Grummt I. The structure of NoRC-associated RNA is crucial for targeting the chromatin remodelling complex NoRC to the nucleolus. EMBO Rep. 2008, 9:774-780.
    • (2008) EMBO Rep. , vol.9 , pp. 774-780
    • Mayer, C.1    Neubert, M.2    Grummt, I.3
  • 31
    • 14044273481 scopus 로고    scopus 로고
    • PARP-1 and PARP-2 interact with nucleophosmin/B23 and accumulate in transcriptionally active nucleoli
    • Meder V.S., Boeglin M., de Murcia G., Schreiber V. PARP-1 and PARP-2 interact with nucleophosmin/B23 and accumulate in transcriptionally active nucleoli. J. Cell Sci. 2005, 118:211-222.
    • (2005) J. Cell Sci. , vol.118 , pp. 211-222
    • Meder, V.S.1    Boeglin, M.2    de Murcia, G.3    Schreiber, V.4
  • 32
    • 80052172007 scopus 로고    scopus 로고
    • Histone ADP-ribosylation in DNA repair, replication and transcription
    • Messner S., Hottiger M.O. Histone ADP-ribosylation in DNA repair, replication and transcription. Trends Cell Biol. 2011, 21:534-542.
    • (2011) Trends Cell Biol. , vol.21 , pp. 534-542
    • Messner, S.1    Hottiger, M.O.2
  • 34
  • 35
    • 0017802365 scopus 로고
    • Purification of ADP-ribosylated nuclear proteins by covalent chromatography on dihydroxyboryl polyacrylamide beads and their characterization
    • Okayama H., Ueda K., Hayaishi O. Purification of ADP-ribosylated nuclear proteins by covalent chromatography on dihydroxyboryl polyacrylamide beads and their characterization. Proc. Natl. Acad. Sci. USA 1978, 75:1111-1115.
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 1111-1115
    • Okayama, H.1    Ueda, K.2    Hayaishi, O.3
  • 37
    • 46149108345 scopus 로고    scopus 로고
    • Rapid, transcription-independent loss of nucleosomes over a large chromatin domain at Hsp70 loci
    • Petesch S.J., Lis J.T. Rapid, transcription-independent loss of nucleosomes over a large chromatin domain at Hsp70 loci. Cell 2008, 134:74-84.
    • (2008) Cell , vol.134 , pp. 74-84
    • Petesch, S.J.1    Lis, J.T.2
  • 40
    • 59349083787 scopus 로고    scopus 로고
    • Delocalization of nucleolar poly(ADP-ribose) polymerase-1 to the nucleoplasm and its novel link to cellular sensitivity to DNA damage
    • Rancourt A., Satoh M.S. Delocalization of nucleolar poly(ADP-ribose) polymerase-1 to the nucleoplasm and its novel link to cellular sensitivity to DNA damage. DNA Repair (Amst.) 2009, 8:286-297.
    • (2009) DNA Repair (Amst.) , vol.8 , pp. 286-297
    • Rancourt, A.1    Satoh, M.S.2
  • 41
    • 0030854373 scopus 로고    scopus 로고
    • Random mutagenesis of the poly(ADP-ribose) polymerase catalytic domain reveals amino acids involved in polymer branching
    • Rolli V., O'Farrell M., Ménissier-de Murcia J., de Murcia G. Random mutagenesis of the poly(ADP-ribose) polymerase catalytic domain reveals amino acids involved in polymer branching. Biochemistry 1997, 36:12147-12154.
    • (1997) Biochemistry , vol.36 , pp. 12147-12154
    • Rolli, V.1    O'Farrell, M.2    Ménissier-de Murcia, J.3    de Murcia, G.4
  • 44
    • 24744448907 scopus 로고    scopus 로고
    • The silence of the ribosomal RNA genes
    • Santoro R. The silence of the ribosomal RNA genes. Cell. Mol. Life Sci. 2005, 62:2067-2079.
    • (2005) Cell. Mol. Life Sci. , vol.62 , pp. 2067-2079
    • Santoro, R.1
  • 45
    • 83455197111 scopus 로고    scopus 로고
    • The epigenetics of the nucleolus: structure and function of active and silent ribosomal RNA genes
    • Springer, New York, M.O.J. Olson (Ed.)
    • Santoro R. The epigenetics of the nucleolus: structure and function of active and silent ribosomal RNA genes. The Nucleolus 2011, 57-82. Springer, New York. First Edition. M.O.J. Olson (Ed.).
    • (2011) The Nucleolus , pp. 57-82
    • Santoro, R.1
  • 46
    • 0034791175 scopus 로고    scopus 로고
    • Molecular mechanisms mediating methylation-dependent silencing of ribosomal gene transcription
    • Santoro R., Grummt I. Molecular mechanisms mediating methylation-dependent silencing of ribosomal gene transcription. Mol. Cell 2001, 8:719-725.
    • (2001) Mol. Cell , vol.8 , pp. 719-725
    • Santoro, R.1    Grummt, I.2
  • 47
    • 15044362537 scopus 로고    scopus 로고
    • Epigenetic mechanism of rRNA gene silencing: temporal order of NoRC-mediated histone modification, chromatin remodeling, and DNA methylation
    • Santoro R., Grummt I. Epigenetic mechanism of rRNA gene silencing: temporal order of NoRC-mediated histone modification, chromatin remodeling, and DNA methylation. Mol. Cell. Biol. 2005, 25:2539-2546.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 2539-2546
    • Santoro, R.1    Grummt, I.2
  • 48
    • 0036844024 scopus 로고    scopus 로고
    • The nucleolar remodeling complex NoRC mediates heterochromatin formation and silencing of ribosomal gene transcription
    • Santoro R., Li J., Grummt I. The nucleolar remodeling complex NoRC mediates heterochromatin formation and silencing of ribosomal gene transcription. Nat. Genet. 2002, 32:393-396.
    • (2002) Nat. Genet. , vol.32 , pp. 393-396
    • Santoro, R.1    Li, J.2    Grummt, I.3
  • 49
    • 74249102765 scopus 로고    scopus 로고
    • Epigenetic engineering of ribosomal RNA genes enhances protein production
    • Santoro R., Lienemann P., Fussenegger M. Epigenetic engineering of ribosomal RNA genes enhances protein production. PLoS ONE 2009, 4:e6653.
    • (2009) PLoS ONE , vol.4
    • Santoro, R.1    Lienemann, P.2    Fussenegger, M.3
  • 50
    • 74149088040 scopus 로고    scopus 로고
    • Intergenic transcripts originating from a subclass of ribosomal DNA repeats silence ribosomal RNA genes in trans
    • Santoro R., Schmitz K.M., Sandoval J., Grummt I. Intergenic transcripts originating from a subclass of ribosomal DNA repeats silence ribosomal RNA genes in trans. EMBO Rep. 2010, 11:52-58.
    • (2010) EMBO Rep. , vol.11 , pp. 52-58
    • Santoro, R.1    Schmitz, K.M.2    Sandoval, J.3    Grummt, I.4
  • 51
    • 77958576363 scopus 로고    scopus 로고
    • Interaction of noncoding RNA with the rDNA promoter mediates recruitment of DNMT3b and silencing of rRNA genes
    • Schmitz K.M., Mayer C., Postepska A., Grummt I. Interaction of noncoding RNA with the rDNA promoter mediates recruitment of DNMT3b and silencing of rRNA genes. Genes Dev. 2010, 24:2264-2269.
    • (2010) Genes Dev. , vol.24 , pp. 2264-2269
    • Schmitz, K.M.1    Mayer, C.2    Postepska, A.3    Grummt, I.4
  • 53
    • 0029808055 scopus 로고    scopus 로고
    • The expression of poly(ADP-ribose) polymerase during differentiation-linked DNA replication reveals that it is a component of the multiprotein DNA replication complex
    • Simbulan-Rosenthal C.M., Rosenthal D.S., Hilz H., Hickey R., Malkas L., Applegren N., Wu Y., Bers G., Smulson M.E. The expression of poly(ADP-ribose) polymerase during differentiation-linked DNA replication reveals that it is a component of the multiprotein DNA replication complex. Biochemistry 1996, 35:11622-11633.
    • (1996) Biochemistry , vol.35 , pp. 11622-11633
    • Simbulan-Rosenthal, C.M.1    Rosenthal, D.S.2    Hilz, H.3    Hickey, R.4    Malkas, L.5    Applegren, N.6    Wu, Y.7    Bers, G.8    Smulson, M.E.9
  • 55
    • 59449101071 scopus 로고    scopus 로고
    • PARP-1 ensures regulation of replication fork progression by homologous recombination on damaged DNA
    • Sugimura K., Takebayashi S., Taguchi H., Takeda S., Okumura K. PARP-1 ensures regulation of replication fork progression by homologous recombination on damaged DNA. J. Cell Biol. 2008, 183:1203-1212.
    • (2008) J. Cell Biol. , vol.183 , pp. 1203-1212
    • Sugimura, K.1    Takebayashi, S.2    Taguchi, H.3    Takeda, S.4    Okumura, K.5
  • 57
    • 0037462597 scopus 로고    scopus 로고
    • Chromatin loosening by poly(ADP)-ribose polymerase (PARP) at Drosophila puff loci
    • Tulin A., Spradling A. Chromatin loosening by poly(ADP)-ribose polymerase (PARP) at Drosophila puff loci. Science 2003, 299:560-562.
    • (2003) Science , vol.299 , pp. 560-562
    • Tulin, A.1    Spradling, A.2
  • 58
    • 0037102454 scopus 로고    scopus 로고
    • The Drosophila heterochromatic gene encoding poly(ADP-ribose) polymerase (PARP) is required to modulate chromatin structure during development
    • Tulin A., Stewart D., Spradling A.C. The Drosophila heterochromatic gene encoding poly(ADP-ribose) polymerase (PARP) is required to modulate chromatin structure during development. Genes Dev. 2002, 16:2108-2119.
    • (2002) Genes Dev. , vol.16 , pp. 2108-2119
    • Tulin, A.1    Stewart, D.2    Spradling, A.C.3
  • 59
    • 35648955118 scopus 로고    scopus 로고
    • The DNA binding and catalytic domains of poly(ADP-ribose) polymerase 1 cooperate in the regulation of chromatin structure and transcription
    • Wacker D.A., Ruhl D.D., Balagamwala E.H., Hope K.M., Zhang T., Kraus W.L. The DNA binding and catalytic domains of poly(ADP-ribose) polymerase 1 cooperate in the regulation of chromatin structure and transcription. Mol. Cell. Biol. 2007, 27:7475-7485.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 7475-7485
    • Wacker, D.A.1    Ruhl, D.D.2    Balagamwala, E.H.3    Hope, K.M.4    Zhang, T.5    Kraus, W.L.6
  • 60
    • 2342524565 scopus 로고    scopus 로고
    • Ablation of PARP-1 does not interfere with the repair of DNA double-strand breaks, but compromises the reactivation of stalled replication forks
    • Yang Y.G., Cortes U., Patnaik S., Jasin M., Wang Z.Q. Ablation of PARP-1 does not interfere with the repair of DNA double-strand breaks, but compromises the reactivation of stalled replication forks. Oncogene 2004, 23:3872-3882.
    • (2004) Oncogene , vol.23 , pp. 3872-3882
    • Yang, Y.G.1    Cortes, U.2    Patnaik, S.3    Jasin, M.4    Wang, Z.Q.5
  • 61
    • 0037009366 scopus 로고    scopus 로고
    • The chromatin remodeling complex NoRC targets HDAC1 to the ribosomal gene promoter and represses RNA polymerase I transcription
    • Zhou Y., Santoro R., Grummt I. The chromatin remodeling complex NoRC targets HDAC1 to the ribosomal gene promoter and represses RNA polymerase I transcription. EMBO J. 2002, 21:4632-4640.
    • (2002) EMBO J. , vol.21 , pp. 4632-4640
    • Zhou, Y.1    Santoro, R.2    Grummt, I.3


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