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Volumn 17, Issue 4, 2010, Pages 430-437

Dynamic changes in histone acetylation regulate origins of DNA replication

Author keywords

[No Author keywords available]

Indexed keywords

HISTONE H3; HISTONE H4;

EID: 77950519650     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb.1780     Document Type: Article
Times cited : (152)

References (60)
  • 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 389, 251-260 (1997).
    • (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
    • 33847076248 scopus 로고    scopus 로고
    • Chromatin challenges during DNA replication and repair
    • Groth, A., Rocha, W., Verreault, A. & Almouzni, G. Chromatin challenges during DNA replication and repair. Cell 128, 721-733 (2007).
    • (2007) Cell , vol.128 , pp. 721-733
    • Groth, A.1    Rocha, W.2    Verreault, A.3    Almouzni, G.4
  • 3
    • 33847070442 scopus 로고    scopus 로고
    • The role of chromatin during transcription
    • Li, B., Carey, M. & Workman, J.L. The role of chromatin during transcription. Cell 128, 707-719 (2007).
    • (2007) Cell , vol.128 , pp. 707-719
    • Li, B.1    Carey, M.2    Workman, J.L.3
  • 4
    • 33847076849 scopus 로고    scopus 로고
    • Chromatin modifcations and their function
    • Kouzarides, T. Chromatin modifcations and their function. Cell 128, 693-705 (2007).
    • (2007) Cell , vol.128 , pp. 693-705
    • Kouzarides, T.1
  • 5
    • 0018671664 scopus 로고
    • And characterisation of a yeast chromosomal replicator
    • Stinchcomb, D.T., Struhl, K. & Davis, R.W. Isolation and characterisation of a yeast chromosomal replicator. Nature 282, 39-43 (1979).
    • (1979) Nature , vol.282 , pp. 39-43
    • Stinchcomb, D.T.1    Struhl, K.2    Isolation, W.D.R.3
  • 6
    • 0035997368 scopus 로고    scopus 로고
    • DNA replication in eukaryotic cells
    • Bell, S.P. & Dutta, A. DNA replication in eukaryotic cells. Annu. Rev. Biochem. 71, 333-374 (2002).
    • (2002) Annu. Rev. Biochem. , vol.71 , pp. 333-374
    • Bell, S.P.1    Dutta, A.2
  • 7
    • 0026091743 scopus 로고
    • The chromatin structure of Saccharomyces cerevisiae autonomously replicating sequences changes during the cell division cycle
    • Brown, J.A., Holmes, S.G. & Smith, M.M. The chromatin structure of Saccharomyces cerevisiae autonomously replicating sequences changes during the cell division cycle. Mol. Cell. Biol. 11, 5301-5311 (1991).
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 5301-5311
    • Brown, J.A.1    Holmes, S.G.2    Smith, M.M.3
  • 8
    • 0025067370 scopus 로고
    • Nucleosome positioning can affect the function of a cis-acting DNA element in vivo
    • Simpson, R.T. Nucleosome positioning can affect the function of a cis-acting DNA element in vivo. Nature 343, 387-389 (1990).
    • (1990) Nature , vol.343 , pp. 387-389
    • Simpson, R.T.1
  • 9
    • 0026571672 scopus 로고
    • A position effect on the time of replication origin activation in yeast
    • Ferguson, B.M. & Fangman, W.L. A position effect on the time of replication origin activation in yeast. Cell 68, 333-339 (1992).
    • (1992) Cell , vol.68 , pp. 333-339
    • Ferguson, B.M.1    Fangman, W.L.2
  • 10
    • 0033556028 scopus 로고    scopus 로고
    • Telomeric chromatin modulates replication timing near chromosome ends
    • Stevenson, J.B. & Gottschling, D.E. Telomeric chromatin modulates replication timing near chromosome ends. Genes Dev. 13, 146-151 (1999).
    • (1999) Genes Dev. , vol.13 , pp. 146-151
    • Stevenson, J.B.1    Gottschling, D.E.2
  • 11
    • 2442660397 scopus 로고    scopus 로고
    • The Rpd3-Sin3 histone deacetylase regulates replication timing and enables intra-S origin control in Saccharomyces cerevisiae
    • Aparicio, J.G., Viggiani, C.J., Gibson, D.G. & Aparicio, O.M. The Rpd3-Sin3 histone deacetylase regulates replication timing and enables intra-S origin control in Saccharomyces cerevisiae. Mol. Cell. Biol. 24, 4769-4780 (2004).
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 4769-4780
    • Aparicio, J.G.1    Viggiani, C.J.2    Gibson, D.G.3    Aparicio, O.M.4
  • 12
    • 0036863542 scopus 로고    scopus 로고
    • Histone acetylation regulates the time of replication origin fring
    • Vogelauer, M., Rubbi, L., Lucas, I., Brewer, B.J. & Grunstein, M. Histone acetylation regulates the time of replication origin fring. Mol. Cell 10, 1223-1233 (2002).
    • (2002) Mol. Cell , vol.10 , pp. 1223-1233
    • Vogelauer, M.1    Rubbi, L.2    Lucas, I.3    Brewer, B.J.4    Grunstein, M.5
  • 13
    • 0033551686 scopus 로고    scopus 로고
    • Histone acetyltransferase HBO1 interacts with the ORC1 subunit of the human initiator protein
    • Iizuka, M. & Stillman, B. Histone acetyltransferase HBO1 interacts with the ORC1 subunit of the human initiator protein. J. Biol. Chem. 274, 23027-23034 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 23027-23034
    • Iizuka, M.1    Stillman, B.2
  • 14
    • 0035805606 scopus 로고    scopus 로고
    • Replication factors MCM2 and ORC1 interact with the histone acetyltransferase HBO1
    • Burke, T.W., Cook, J.G., Asano, M. & Nevins, J.R. Replication factors MCM2 and ORC1 interact with the histone acetyltransferase HBO1. J. Biol. Chem. 276, 15397-15408 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 15397-15408
    • Burke, T.W.1    Cook, J.G.2    Asano, M.3    Nevins, J.R.4
  • 15
    • 0036791653 scopus 로고    scopus 로고
    • Single-molecule analysis reveals clustering and epigenetic regulation of replication origins at the yeast rDNA locus
    • Pasero, P., Bensimon, A. & Schwob, E. Single-molecule analysis reveals clustering and epigenetic regulation of replication origins at the yeast rDNA locus. Genes Dev. 16, 2479-2484 (2002).
    • (2002) Genes Dev. , vol.16 , pp. 2479-2484
    • Pasero, P.1    Bensimon, A.2    Schwob, E.3
  • 16
    • 1842682915 scopus 로고    scopus 로고
    • +-dependent Sir2p histone deacetylase is a negative regulator of chromosomal DNA replication
    • +-dependent Sir2p histone deacetylase is a negative regulator of chromosomal DNA replication. Genes Dev. 18, 769-781 (2004).
    • (2004) Genes Dev. , vol.18 , pp. 769-781
    • Pappas, D.L.1    Frisch, R.2    Weinreich, M.3
  • 17
    • 0035812808 scopus 로고    scopus 로고
    • Replication dynamics of the yeast genome
    • Raghuraman, M.K. et al. Replication dynamics of the yeast genome. Science 294, 115-121 (2001).
    • (2001) Science , vol.294 , pp. 115-121
    • Raghuraman, M.K.1
  • 18
    • 0035861492 scopus 로고    scopus 로고
    • Genome-wide distribution of ORC and MCM proteins in S. cerevisiae: High-resolution mapping of replication origins
    • Wyrick, J.J. et al. Genome-wide distribution of ORC and MCM proteins in S. cerevisiae: high-resolution mapping of replication origins. Science 294, 2357-2360 (2001).
    • (2001) Science , vol.294 , pp. 2357-2360
    • Wyrick, J.J.1
  • 19
    • 0033636595 scopus 로고    scopus 로고
    • Synergistic coupling of histone H3 phosphorylation and acetylation in response to epidermal growth factor stimulation
    • Cheung, P. et al. Synergistic coupling of histone H3 phosphorylation and acetylation in response to epidermal growth factor stimulation. Mol. Cell 5, 905-915 (2000).
    • (2000) Mol. Cell , vol.5 , pp. 905-915
    • Cheung, P.1
  • 20
    • 0035954274 scopus 로고    scopus 로고
    • Methylation of histone H4 at arginine 3 occurs in vivo and is mediated by the nuclear receptor coactivator PRMT1
    • Strahl, B.D. et al. Methylation of histone H4 at arginine 3 occurs in vivo and is mediated by the nuclear receptor coactivator PRMT1. Curr. Biol. 11, 996-1000 (2001).
    • (2001) Curr. Biol. , vol.11 , pp. 996-1000
    • Strahl, B.D.1
  • 21
    • 0141483484 scopus 로고    scopus 로고
    • Identifcation of novel histone post-translational modifcations by peptide mass fngerprinting
    • Zhang, L., Eugeni, E.E., Parthun, M.R. & Freitas, M.A. Identifcation of novel histone post-translational modifcations by peptide mass fngerprinting. Chromosoma 112, 77-86 (2003).
    • (2003) Chromosoma , vol.112 , pp. 77-86
    • Zhang, L.1    Eugeni, E.E.2    Parthun, M.R.3    Freitas, M.A.4
  • 22
    • 15944416371 scopus 로고    scopus 로고
    • Histone H4 lysine 91 acetylation a core domain modifcation associated with chromatin assembly
    • Ye, J. et al. Histone H4 lysine 91 acetylation a core domain modifcation associated with chromatin assembly. Mol. Cell 18, 123-130 (2005).
    • (2005) Mol. Cell , vol.18 , pp. 123-130
    • Ye, J.1
  • 23
    • 33847768829 scopus 로고    scopus 로고
    • Long-distance combinatorial linkage between methylation and acetylation on histone H3 N termini
    • Taverna, S.D. et al. Long-distance combinatorial linkage between methylation and acetylation on histone H3 N termini. Proc. Natl. Acad. Sci. USA 104, 2086-2091 (2007).
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 2086-2091
    • Taverna, S.D.1
  • 24
    • 0020053188 scopus 로고
    • Replication, and chromatin structure of TRP1 RI circle, a multiple-copy synthetic plasmid derived from Saccharomyces cerevisiae chromosomal DNA
    • Zakian, V.A. & Scott, J.F. Construction, replication, and chromatin structure of TRP1 RI circle, a multiple-copy synthetic plasmid derived from Saccharomyces cerevisiae chromosomal DNA. Mol. Cell. Biol. 2, 221-232 (1982).
    • (1982) Mol. Cell. Biol. , vol.2 , pp. 221-232
    • Zakian, V.A.1    Construction, F.S.J.2
  • 25
    • 0021691970 scopus 로고
    • Nuclease digestion of circular TRP1ARS1 chromatin reveals positioned nucleosomes separated by nuclease-sensitive regions
    • Thoma, F., Bergman, L.W. & Simpson, R.T. Nuclease digestion of circular TRP1ARS1 chromatin reveals positioned nucleosomes separated by nuclease-sensitive regions. J. Mol. Biol. 177, 715-733 (1984).
    • (1984) J. Mol. Biol. , vol.177 , pp. 715-733
    • Thoma, F.1    Bergman, L.W.2    Simpson, R.T.3
  • 26
    • 0034142029 scopus 로고    scopus 로고
    • The organized chromatin domain of the repressed yeast a cell-specifc gene STE6 contains two molecules of the corepressor Tup1p per nucleosome
    • Ducker, C.E. & Simpson, R.T. The organized chromatin domain of the repressed yeast a cell-specifc gene STE6 contains two molecules of the corepressor Tup1p per nucleosome. EMBO J. 19, 400-409 (2000).
    • (2000) EMBO J. , vol.19 , pp. 400-409
    • Ducker, C.E.1    Simpson, R.T.2
  • 28
    • 25144434235 scopus 로고    scopus 로고
    • A topological interaction between cohesin rings and a circular minichromosome
    • Ivanov, D. & Nasmyth, K. A topological interaction between cohesin rings and a circular minichromosome. Cell 122, 849-860 (2005).
    • (2005) Cell , vol.122 , pp. 849-860
    • Ivanov, D.1    Nasmyth, K.2
  • 29
    • 3142702204 scopus 로고    scopus 로고
    • Matching proteins with tandem mass spectra
    • Craig, R. & Beavis, R.C. TANDEM: matching proteins with tandem mass spectra. Bioinformatics 20, 1466-1467 (2004).
    • (2004) Bioinformatics , vol.20 , pp. 1466-1467
    • Craig, R.1    Tandem, C.B.R.2
  • 30
    • 0023646792 scopus 로고
    • The localization of replication origins on ARS plasmids in S. cerevisiae
    • Brewer, B.J. & Fangman, W.L. The localization of replication origins on ARS plasmids in S. cerevisiae. Cell 51, 463-471 (1987).
    • (1987) Cell , vol.51 , pp. 463-471
    • Brewer, B.J.1    Fangman, W.L.2
  • 31
    • 34147177521 scopus 로고    scopus 로고
    • Organismal differences in post-translational modifcations in histones H3 and H4
    • Garcia, B.A. et al. Organismal differences in post-translational modifcations in histones H3 and H4. J. Biol. Chem. 282, 7641-7655 (2007).
    • (2007) J. Biol. Chem. , vol.282 , pp. 7641-7655
    • Garcia, B.A.1
  • 32
    • 0036809640 scopus 로고    scopus 로고
    • Transcriptional inhibition of genes with severe histone h3 hypoacetylation in the coding region
    • Kristjuhan, A. et al. Transcriptional inhibition of genes with severe histone h3 hypoacetylation in the coding region. Mol. Cell 10, 925-933 (2002).
    • (2002) Mol. Cell , vol.10 , pp. 925-933
    • Kristjuhan, A.1
  • 33
    • 0036170767 scopus 로고    scopus 로고
    • Set2 is a nucleosomal histone H3-selective methyltransferase that mediates transcriptional repression
    • Strahl, B.D. et al. Set2 is a nucleosomal histone H3-selective methyltransferase that mediates transcriptional repression. Mol. Cell. Biol. 22, 1298-1306 (2002).
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 1298-1306
    • Strahl, B.D.1
  • 34
    • 23944462969 scopus 로고    scopus 로고
    • Genome-wide map of nucleosome acetylation and methylation in yeast
    • Pokholok, D.K. et al. Genome-wide map of nucleosome acetylation and methylation in yeast. Cell 122, 517-527 (2005).
    • (2005) Cell , vol.122 , pp. 517-527
    • Pokholok, D.K.1
  • 35
    • 27744577727 scopus 로고    scopus 로고
    • Histone H3 methylation by Set2 directs deacetylation of coding regions by Rpd3S to suppress spurious intragenic transcription
    • Carrozza, M.J. et al. Histone H3 methylation by Set2 directs deacetylation of coding regions by Rpd3S to suppress spurious intragenic transcription. Cell 123, 581-592 (2005).
    • (2005) Cell , vol.123 , pp. 581-592
    • Carrozza, M.J.1
  • 36
    • 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 436, 294-298 (2005).
    • (2005) Nature , vol.436 , pp. 294-298
    • Masumoto, H.1    Hawke, D.2    Kobayashi, R.3    Verreault, A.4
  • 37
    • 47549092547 scopus 로고    scopus 로고
    • Acetylation of histone H3 lysine 56 regulates replication-coupled nucleosome assembly
    • Li, Q. et al. Acetylation of histone H3 lysine 56 regulates replication-coupled nucleosome assembly. Cell 134, 244-255 (2008).
    • (2008) Cell , vol.134 , pp. 244-255
    • Li, Q.1
  • 38
    • 33745496607 scopus 로고    scopus 로고
    • Cell cycle and checkpoint regulation of histone H3 K56 acetylation by Hst3 and Hst4
    • Maas, N.L., Miller, K.M., DeFazio, L.G. & Toczyski, D.P. Cell cycle and checkpoint regulation of histone H3 K56 acetylation by Hst3 and Hst4. Mol. Cell 23, 109-119 (2006).
    • (2006) Mol. Cell , vol.23 , pp. 109-119
    • Maas, N.L.1    Miller, K.M.2    Defazio, L.G.3    Toczyski, D.P.4
  • 39
    • 57149124836 scopus 로고    scopus 로고
    • Cell cycle-and chaperone-mediated regulation of H3K56ac incorporation in yeast
    • Kaplan, T. et al. Cell cycle-and chaperone-mediated regulation of H3K56ac incorporation in yeast. PLoS Genet. 4, e1000270 (2008).
    • (2008) PLoS Genet. , vol.4
    • Kaplan, T.1
  • 40
    • 0029123092 scopus 로고
    • Histone H4 and the maintenance of genome integrity
    • Megee, P.C., Morgan, B.A. & Smith, M.M. Histone H4 and the maintenance of genome integrity. Genes Dev. 9, 1716-1727 (1995).
    • (1995) Genes Dev. , vol.9 , pp. 1716-1727
    • Megee, P.C.1    Morgan, B.A.2    Smith, M.M.3
  • 41
    • 0025093599 scopus 로고
    • Genetic analysis of histone H4: Essential role of lysines subject to reversible acetylation
    • Megee, P.C., Morgan, B.A., Mittman, B.A. & Smith, M.M. Genetic analysis of histone H4: essential role of lysines subject to reversible acetylation. Science 247, 841-845 (1990).
    • (1990) Science , vol.247 , pp. 841-845
    • Megee, P.C.1    Morgan, B.A.2    Mittman, B.A.3    Smith, M.M.4
  • 42
    • 0037402422 scopus 로고    scopus 로고
    • Mass spectrometric quantifcation of acetylation at specifc lysines within the amino-terminal tail of histone H4
    • Smith, C.M. et al. Mass spectrometric quantifcation of acetylation at specifc lysines within the amino-terminal tail of histone H4. Anal. Biochem. 316, 23-33 (2003).
    • (2003) Anal. Biochem. , vol.316 , pp. 23-33
    • Smith, C.M.1
  • 43
    • 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. 32, 378-383 (2002).
    • (2002) Nat. Genet. , vol.32 , pp. 378-383
    • Suka, N.1    Luo, K.2    Grunstein, M.3
  • 44
    • 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. 32, 370-377 (2002).
    • (2002) Nat. Genet. , vol.32 , pp. 370-377
    • Kimura, A.1    Umehara, T.2    Horikoshi, M.3
  • 45
    • 0032845169 scopus 로고    scopus 로고
    • Minichromosome maintenance as a genetic assay for defects in DNA replication
    • Tye, B.K. Minichromosome maintenance as a genetic assay for defects in DNA replication. Methods 18, 329-334 (1999).
    • (1999) Methods , vol.18 , pp. 329-334
    • Tye, B.K.1
  • 46
    • 0026506383 scopus 로고
    • Addition of extra origins of replication to a minichromosome suppresses its mitotic loss in cdc6 and cdc14 mutants of Saccharomyces cerevisiae
    • Hogan, E. & Koshland, D. Addition of extra origins of replication to a minichromosome suppresses its mitotic loss in cdc6 and cdc14 mutants of Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA 89, 3098-3102 (1992).
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 3098-3102
    • Hogan, E.1    Koshland, D.2
  • 47
    • 72849116829 scopus 로고    scopus 로고
    • Quantitative proteomic analysis of purifed yeast kinetochores identifes a PP1 regulatory subunit
    • Akiyoshi, B., Nelson, C.R., Ranish, J.A. & Biggins, S. Quantitative proteomic analysis of purifed yeast kinetochores identifes a PP1 regulatory subunit. Genes Dev. 23, 2887-2899 (2009).
    • (2009) Genes Dev. , vol.23 , pp. 2887-2899
    • Akiyoshi, B.1    Nelson, C.R.2    Ranish, J.A.3    Biggins, S.4
  • 48
    • 27644467857 scopus 로고    scopus 로고
    • Insights into the role of histone H3 and histone H4 core modifable residues in Saccharomyces cerevisiae
    • Hyland, E.M. et al. Insights into the role of histone H3 and histone H4 core modifable residues in Saccharomyces cerevisiae. Mol. Cell. Biol. 25, 10060-10070 (2005).
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 10060-10070
    • Hyland, E.M.1
  • 49
    • 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. USA 106, 16686-16691 (2009).
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 16686-16691
    • Chandrasekharan, M.B.1    Huang, F.2    Sun, Z.W.3
  • 50
    • 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 31, 57-66 (2008).
    • (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
  • 51
    • 67651245131 scopus 로고    scopus 로고
    • H3 k36 methylation helps determine the timing of cdc45 association with replication origins
    • Pryde, F. et al. H3 k36 methylation helps determine the timing of cdc45 association with replication origins. PLoS One 4, e5882 (2009).
    • (2009) PLoS One , vol.4
    • Pryde, F.1
  • 52
    • 33745743449 scopus 로고    scopus 로고
    • Tracking of controlled Escherichia coli replication fork stalling and restart at repressor-bound DNA in vivo
    • Possoz, C., Filipe, S.R., Grainge, I. & Sherratt, D.J. Tracking of controlled Escherichia coli replication fork stalling and restart at repressor-bound DNA in vivo. EMBO J. 25, 2596-2604 (2006).
    • (2006) EMBO J. , vol.25 , pp. 2596-2604
    • Possoz, C.1    Filipe, S.R.2    Grainge, I.3    Sherratt, D.J.4
  • 53
    • 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, T.A., Schultz, M.C., 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. 10, 686-699 (1996).
    • (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
  • 54
    • 0024370763 scopus 로고
    • The genetic control of direct-repeat recombination in Saccharomyces: The effect of rad52 and rad1 on mitotic recombination at GAL10, a transcriptionally regulated gene
    • Thomas, B.J. & Rothstein, R. The genetic control of direct-repeat recombination in Saccharomyces: the effect of rad52 and rad1 on mitotic recombination at GAL10, a transcriptionally regulated gene. Genetics 123, 725-738 (1989).
    • (1989) Genetics , vol.123 , pp. 725-738
    • Thomas, B.J.1    Rothstein, R.2
  • 55
    • 0032161269 scopus 로고    scopus 로고
    • A suppressor of two essential checkpoint genes identifies a novel protein that negatively affects dNTP pools
    • Zhao, X., Muller, E.G. & Rothstein, R. A suppressor of two essential checkpoint genes identifes a novel protein that negatively affects dNTP pools. Mol. Cell 2, 329-340 (1998). (Pubitemid 128379273)
    • (1998) Molecular Cell , vol.2 , Issue.3 , pp. 329-340
    • Zhao, X.1    Muller, E.G.D.2    Rothstein, R.3
  • 56
    • 43249095257 scopus 로고    scopus 로고
    • ATP-dependent chromatin remodeling shapes the DNA replication landscape
    • DOI 10.1038/nsmb.1419, PII NSMB1419
    • Vincent, J.A., Kwong, T.J. & Tsukiyama, T. ATP-dependent chromatin remodeling shapes the DNA replication landscape. Nat. Struct. Mol. Biol. 15, 477-484 (2008). (Pubitemid 351653590)
    • (2008) Nature Structural and Molecular Biology , vol.15 , Issue.5 , pp. 477-484
    • Vincent, J.A.1    Kwong, T.J.2    Tsukiyama, T.3
  • 57
    • 0037108887 scopus 로고    scopus 로고
    • Empirical statistical model to estimate the accuracy of peptide identifications made by MS/MS and database search
    • DOI 10.1021/ac025747h
    • Keller, A., Nesvizhskii, A.I., Kolker, E. & Aebersold, R. Empirical statistical model to estimate the accuracy of peptide identifcations made by MS/MS and database search. Anal. Chem. 74, 5383-5392 (2002). (Pubitemid 35215372)
    • (2002) Analytical Chemistry , vol.74 , Issue.20 , pp. 5383-5392
    • Keller, A.1    Nesvizhskii, A.I.2    Kolker, E.3    Aebersold, R.4
  • 60
    • 0347416973 scopus 로고    scopus 로고
    • Branch Migrating Sister Chromatid Junctions Form at Replication Origins through Rad51/Rad52-Independent Mechanisms
    • DOI 10.1016/S1097-2765(03)00473-8
    • Lopes, M., Cotta-Ramusino, C., Liberi, G. & Foiani, M. Branch migrating sister chromatid junctions form at replication origins through Rad51/Rad52-independent mechanisms. Mol. Cell 12, 1499-1510 (2003). (Pubitemid 38037018)
    • (2003) Molecular Cell , vol.12 , Issue.6 , pp. 1499-1510
    • Lopes, M.1    Cotta-Ramusino, C.2    Liberi, G.3    Foiani, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.