메뉴 건너뛰기




Volumn 169, Issue 1, 2005, Pages 35-47

Proteomic and genomic characterization of chromatin complexes at a boundary

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; DNA; HISTONE; PROTEIN SUBUNIT;

EID: 17644367887     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.200502104     Document Type: Article
Times cited : (124)

References (70)
  • 1
    • 0028819762 scopus 로고
    • Two novel related yeast nucleoporins Nup170p and Nup157p: Complementation with the vertebrate homologue Nup155p and functional interactions with the yeast nuclear pore-membrane protein Pom152p
    • Aitchison, J.D., M.P. Rout, M. Marelli, G. Blobel, and R.W. Wozniak. 1995. Two novel related yeast nucleoporins Nup170p and Nup157p: complementation with the vertebrate homologue Nup155p and functional interactions with the yeast nuclear pore-membrane protein Pom152p. J. Cell Biol. 131:1133-1148.
    • (1995) J. Cell Biol. , vol.131 , pp. 1133-1148
    • Aitchison, J.D.1    Rout, M.P.2    Marelli, M.3    Blobel, G.4    Wozniak, R.W.5
  • 2
    • 0029845118 scopus 로고    scopus 로고
    • Kap104p: A karyopherin involved in the nuclear transport of messenger RNA binding proteins
    • Aitchison, J.D., G. Blobel, and M.P. Rout. 1996. Kap104p: a karyopherin involved in the nuclear transport of messenger RNA binding proteins. Science. 274:624-627.
    • (1996) Science , vol.274 , pp. 624-627
    • Aitchison, J.D.1    Blobel, G.2    Rout, M.P.3
  • 3
    • 0025825976 scopus 로고
    • Cloning DPB3, the gene encoding the third subunit of DNA polymerase II of Saccharomyces cerevisiae
    • Araki, H., R.K. Hamatake, A. Morrison, A.L. Johnson, L.H. Johnston, and A. Sugino. 1991. Cloning DPB3, the gene encoding the third subunit of DNA polymerase II of Saccharomyces cerevisiae. Nucleic Acids Res. 19:4867-4872.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 4867-4872
    • Araki, H.1    Hamatake, R.K.2    Morrison, A.3    Johnson, A.L.4    Johnston, L.H.5    Sugino, A.6
  • 6
    • 0035997356 scopus 로고    scopus 로고
    • ATP-dependent nucleosome remodeling
    • Becker, P.B., and W. Horz. 2002. ATP-dependent nucleosome remodeling. Annu. Rev. Biochem. 71:247-273.
    • (2002) Annu Rev Biochem , vol.71 , pp. 247-273
    • Becker, P.B.1    Horz, W.2
  • 7
    • 0035313801 scopus 로고    scopus 로고
    • Chromosomal boundaries in S. cerevisiae
    • Bi, X., and J.R. Broach. 2001. Chromosomal boundaries in S. cerevisiae. Curr. Opin. Genet. Dev. 11:199-204.
    • (2001) Curr. Opin. Genet. Dev. , vol.11 , pp. 199-204
    • Bi, X.1    Broach, J.R.2
  • 8
    • 0032744760 scopus 로고    scopus 로고
    • The yeast HML I silencer defines a heterochromatin domain boundary by directional establishment of silencing
    • Bi, X., M. Braunstein, G.J. Shei, and J.R. Broach. 1999. The yeast HML I silencer defines a heterochromatin domain boundary by directional establishment of silencing. Proc. Natl. Acad. Sci. USA. 96:11934-11939.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 11934-11939
    • Bi, X.1    Braunstein, M.2    Shei, G.J.3    Broach, J.R.4
  • 9
    • 0029953722 scopus 로고    scopus 로고
    • Efficient transcriptional silencing in Saccharomyces cerevisiae requires a heterochromatin histone acetylation pattern
    • Braunstein, M., R.E. Sobel, C.D. Allis, B.M. Turner, and J.R. Broach. 1996. Efficient transcriptional silencing in Saccharomyces cerevisiae requires a heterochromatin histone acetylation pattern. Mol. Cell. Biol. 16:4349-4356.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 4349-4356
    • Braunstein, M.1    Sobel, R.E.2    Allis, C.D.3    Turner, B.M.4    Broach, J.R.5
  • 11
    • 0037515466 scopus 로고    scopus 로고
    • The quaternary structure of DNA polymerase epsilon from Saccharomyces cerevisiae
    • Chilkova, O., B.H. Jonsson, and E. Johansson. 2003. The quaternary structure of DNA polymerase epsilon from Saccharomyces cerevisiae. J. Biol. Chem. 278:14082-14086.
    • (2003) J. Biol. Chem. , vol.278 , pp. 14082-14086
    • Chilkova, O.1    Jonsson, B.H.2    Johansson, E.3
  • 12
    • 0036532119 scopus 로고    scopus 로고
    • Breaking through to the other side: Silencers and barriers
    • Dhillon, N., and R.T. Kamakaka. 2002. Breaking through to the other side: silencers and barriers. Curr. Opin. Genet. Dev. 12:188-192.
    • (2002) Curr. Opin. Genet. Dev. , vol.12 , pp. 188-192
    • Dhillon, N.1    Kamakaka, R.T.2
  • 13
    • 0035254535 scopus 로고    scopus 로고
    • RNA polymerase III and RNA polymerase II promoter complexes are heterochromatin barriers in Saccharomyces cerevisiae
    • Donze, D., and R.T. Kamakaka. 2001. RNA polymerase III and RNA polymerase II promoter complexes are heterochromatin barriers in Saccharomyces cerevisiae. EMBO J. 20:520-531.
    • (2001) EMBO J. , vol.20 , pp. 520-531
    • Donze, D.1    Kamakaka, R.T.2
  • 14
    • 0033558878 scopus 로고    scopus 로고
    • The boundaries of the silenced HMR domain in Saccharomyces cerevisiae
    • Donze, D., C.R. Adams, J. Rine, and R.T. Kamakaka. 1999. The boundaries of the silenced HMR domain in Saccharomyces cerevisiae. Genes Dev. 13: 698-708.
    • (1999) Genes Dev. , vol.13 , pp. 698-708
    • Donze, D.1    Adams, C.R.2    Rine, J.3    Kamakaka, R.T.4
  • 15
    • 0032491540 scopus 로고    scopus 로고
    • Role of the putative zinc finger domain of Saccharomyces cerevisiae DNA polymerase epsilon in DNA replication and the S/M checkpoint pathway
    • Dua, R., D.L. Levy, and J.L. Campbell. 1998. Role of the putative zinc finger domain of Saccharomyces cerevisiae DNA polymerase epsilon in DNA replication and the S/M checkpoint pathway. J. Biol. Chem. 273:30046-30055.
    • (1998) J. Biol. Chem. , vol.273 , pp. 30046-30055
    • Dua, R.1    Levy, D.L.2    Campbell, J.L.3
  • 16
    • 0034666148 scopus 로고    scopus 로고
    • Subunit interactions within the Saccharomyces cerevisiae DNA polymerase epsilon (pol epsilon) complex. Demonstration of a dimeric pol epsilon
    • Dua, R., S. Edwards, D.L. Levy, and J.L. Campbell. 2000. Subunit interactions within the Saccharomyces cerevisiae DNA polymerase epsilon (pol epsilon) complex. Demonstration of a dimeric pol epsilon. J. Biol. Chem. 275:28816-28825.
    • (2000) J. Biol. Chem. , vol.275 , pp. 28816-28825
    • Dua, R.1    Edwards, S.2    Levy, D.L.3    Campbell, J.L.4
  • 17
    • 0037384875 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae DNA polymerase epsilon and polymerase sigma interact physically and functionally, suggesting a role for polymerase epsilon in sister chromatid cohesion
    • Edwards, S., C.M. Li, D.L. Levy, J. Brown, P.M. Snow, and J.L. Campbell. 2003. Saccharomyces cerevisiae DNA polymerase epsilon and polymerase sigma interact physically and functionally, suggesting a role for polymerase epsilon in sister chromatid cohesion. Mol. Cell. Biol. 23:2733-2748.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 2733-2748
    • Edwards, S.1    Li, C.M.2    Levy, D.L.3    Brown, J.4    Snow, P.M.5    Campbell, J.L.6
  • 18
    • 0345276461 scopus 로고    scopus 로고
    • Chromatin remodeling in vivo: Evidence for a nucleosome sliding mechanism
    • Fazzio, T.G., and T. Tsukiyama. 2003. Chromatin remodeling in vivo: evidence for a nucleosome sliding mechanism. Mol. Cell. 12:1333-1340.
    • (2003) Mol. Cell. , vol.12 , pp. 1333-1340
    • Fazzio, T.G.1    Tsukiyama, T.2
  • 20
    • 0035007681 scopus 로고    scopus 로고
    • An AAA family tree
    • Frohlich, K.U. 2001. An AAA family tree. J. Cell Sci. 114:1601-1602.
    • (2001) J. Cell Sci. , vol.114 , pp. 1601-1602
    • Frohlich, K.U.1
  • 22
    • 0021235437 scopus 로고
    • The purification and characterization of DNA topoisomerases I and II of the yeast Saccharomyces cerevisiae
    • Goto, T., P. Laipis, and J.C. Wang. 1984. The purification and characterization of DNA topoisomerases I and II of the yeast Saccharomyces cerevisiae. J. Biol. Chem. 259:10422-10429.
    • (1984) J. Biol. Chem. , vol.259 , pp. 10422-10429
    • Goto, T.1    Laipis, P.2    Wang, J.C.3
  • 23
    • 0032412476 scopus 로고    scopus 로고
    • Mating-type gene switching in Saccharomyces cerevisiae
    • Haber, J.E. 1998. Mating-type gene switching in Saccharomyces cerevisiae. Annu. Rev. Genet. 32:561-599.
    • (1998) Annu. Rev. Genet. , vol.32 , pp. 561-599
    • Haber, J.E.1
  • 24
    • 1642276329 scopus 로고    scopus 로고
    • Genetic and epigenetic regulation of the FLO gene family generates cell-surface variation in yeast
    • Halme, A., S. Bumgarner, C. Styles, and G.R. Fink. 2004. Genetic and epigenetic regulation of the FLO gene family generates cell-surface variation in yeast. Cell. 116:405-415.
    • (2004) Cell , vol.116 , pp. 405-415
    • Halme, A.1    Bumgarner, S.2    Styles, C.3    Fink, G.R.4
  • 25
    • 0025228710 scopus 로고
    • Purification and characterization of DNA polymerase II from the yeast Saccharomyces cerevisiae. Identification of the catalytic core and a possible holoenzyme form of the enzyme
    • Hamatake, R.K., H. Hasegawa, A.B. Clark, K. Bebenek, T.A. Kunkel, and A. Sugino. 1990. Purification and characterization of DNA polymerase II from the yeast Saccharomyces cerevisiae. Identification of the catalytic core and a possible holoenzyme form of the enzyme. J. Biol. Chem. 265:4072-4083.
    • (1990) J. Biol. Chem. , vol.265 , pp. 4072-4083
    • Hamatake, R.K.1    Hasegawa, H.2    Clark, A.B.3    Bebenek, K.4    Kunkel, T.A.5    Sugino, A.6
  • 26
    • 0035051062 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae CTF18 and CTF4 are required for sister chromatid cohesion
    • Hanna, J.S., E.S. Kroll, V. Lundblad, and P.A. Spencer. 2001. Saccharomyces cerevisiae CTF18 and CTF4 are required for sister chromatid cohesion. Mol. Cell. Biol. 21:3144-3158.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 3144-3158
    • Hanna, J.S.1    Kroll, E.S.2    Lundblad, V.3    Spencer, P.A.4
  • 28
    • 0035577668 scopus 로고    scopus 로고
    • Histone H3 specific acetyltransferases are essential for cell cycle progression
    • Howe, L., D. Auston, P. Grant, S. John, R.G. Cook, J.L. Workman, and L. Pillus. 2001. Histone H3 specific acetyltransferases are essential for cell cycle progression. Genes Dev. 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
  • 30
    • 0346363763 scopus 로고    scopus 로고
    • Noncompetitive counteractions of DNA polymerase epsilon and ISW2/yCHRAC for epigenetic inheritance of telomere position effect in Saccharomyces cerevisiae
    • Iida, T., and H. Araki. 2004. Noncompetitive counteractions of DNA polymerase epsilon and ISW2/yCHRAC for epigenetic inheritance of telomere position effect in Saccharomyces cerevisiae. Mol. Cell. Biol. 24:217-227.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 217-227
    • Iida, T.1    Araki, H.2
  • 31
    • 0037249320 scopus 로고    scopus 로고
    • Structural and dynamic functions establish chromatin domains
    • Ishii, K., and U.K. Laemmli. 2003. Structural and dynamic functions establish chromatin domains. Mol. Cell. 11:237-248.
    • (2003) Mol. Cell. , vol.11 , pp. 237-248
    • Ishii, K.1    Laemmli, U.K.2
  • 32
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • Jenuwein, T., and C.D. Allis. 2001. Translating the histone code. Science. 293:1074-1080.
    • (2001) Science , vol.293 , pp. 1074-1080
    • Jenuwein, T.1    Allis, C.D.2
  • 34
    • 0034657420 scopus 로고    scopus 로고
    • The something about silencing protein, Sas3, is the catalytic subunit of NuA3, a yTAF(II)30-containing HAT complex that interacts with the Spt16 subunit of the yeast CP (Cdc68/Pob3)-FACT complex
    • John, S., L. Howe, S.T. Tafrov, P.A. Grant, R. Sternglanz, and J.L. Workman. 2000. The something about silencing protein, Sas3, is the catalytic subunit of NuA3, a yTAF(II)30-containing HAT complex that interacts with the Spt16 subunit of the yeast CP (Cdc68/Pob3)-FACT complex. Genes Dev. 14:1196-1208.
    • (2000) Genes Dev. , vol.14 , pp. 1196-1208
    • John, S.1    Howe, L.2    Tafrov, S.T.3    Grant, P.A.4    Sternglanz, R.5    Workman, J.L.6
  • 35
    • 0345354678 scopus 로고    scopus 로고
    • Detection of secreted peptides by using hypothesis-driven multistage mass spectrometry
    • Kalkum, M., G.J. Lyon, and B.T. Chait. 2003. Detection of secreted peptides by using hypothesis-driven multistage mass spectrometry. Proc. Natl. Acad. Sci. USA. 100:2795-2800.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 2795-2800
    • Kalkum, M.1    Lyon, G.J.2    Chait, B.T.3
  • 36
    • 0036837670 scopus 로고    scopus 로고
    • High-resolution mapping of changes in histone-DNA contacts of nucleosomes remodeled by ISW2
    • Kassabov, S.R., N.M. Henry, M. Zofall, T. Tsukiyama, and B. Bartholomew. 2002. High-resolution mapping of changes in histone-DNA contacts of nucleosomes remodeled by ISW2. Mol. Cell. Biol. 22:7524-7534.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 7524-7534
    • Kassabov, S.R.1    Henry, N.M.2    Zofall, M.3    Tsukiyama, T.4    Bartholomew, B.5
  • 37
    • 0035281586 scopus 로고    scopus 로고
    • In vivo chromatin remodeling by yeast ISWI homologs Isw1p and Isw2p
    • Kent, N.A., N. Karabetsou, P.K. Politis, and J. Mellor. 2001. In vivo chromatin remodeling by yeast ISWI homologs Isw1p and Isw2p. Genes Dev. 15:619-626.
    • (2001) Genes Dev. , vol.15 , pp. 619-626
    • Kent, N.A.1    Karabetsou, N.2    Politis, P.K.3    Mellor, J.4
  • 38
    • 0034480770 scopus 로고    scopus 로고
    • Rapidly switchable matrix-assisted laser desorption/ionization and electrospray quadrupole-time-of-flight mass spectrometry for protein identification
    • Krutchinsky, A.N., W. Zhang, and B.T. Chait. 2000. Rapidly switchable matrix-assisted laser desorption/ionization and electrospray quadrupole-time-of-flight mass spectrometry for protein identification. J. Am. Soc. Mass Spectrom. 11:493-504.
    • (2000) J. Am. Soc. Mass Spectrom. , vol.11 , pp. 493-504
    • Krutchinsky, A.N.1    Zhang, W.2    Chait, B.T.3
  • 39
    • 0035499655 scopus 로고    scopus 로고
    • Automatic identification of proteins with a MALDI-quadrupole ion trap mass spectrometer
    • Krutchinsky, A.N., M. Kalkum, and B.T. Chait, 2001. Automatic identification of proteins with a MALDI-quadrupole ion trap mass spectrometer. Anal. Chem. 73:5066-5077.
    • (2001) Anal. Chem. , vol.73 , pp. 5066-5077
    • Krutchinsky, A.N.1    Kalkum, M.2    Chait, B.T.3
  • 40
    • 2942518343 scopus 로고    scopus 로고
    • Mapping global histone acetylation patterns to gene expression
    • Kurdistani, S.K., S. Tavazoie, and M. Grunstein. 2004. Mapping global histone acetylation patterns to gene expression. Cell. 117:721-733.
    • (2004) Cell , vol.117 , pp. 721-733
    • Kurdistani, S.K.1    Tavazoie, S.2    Grunstein, M.3
  • 41
    • 0037131524 scopus 로고    scopus 로고
    • Setting the boundaries of chromatin domains and nuclear organization
    • Labrador, M., and V.G. Corces. 2002. Setting the boundaries of chromatin domains and nuclear organization. Cell. 111:151-154.
    • (2002) Cell , vol.111 , pp. 151-154
    • Labrador, M.1    Corces, V.G.2
  • 42
    • 0034722387 scopus 로고    scopus 로고
    • Chromosomal addresses of the cohesin component Mcd1p
    • Laloraya, S., V. Guacci, and D, Koshland. 2000, Chromosomal addresses of the cohesin component Mcd1p. J Cell Biol. 151:1047-1056.
    • (2000) J Cell Biol. , vol.151 , pp. 1047-1056
    • Laloraya, S.1    Guacci, V.2    Koshland, D.3
  • 43
    • 0034934774 scopus 로고    scopus 로고
    • Promoter-specific binding of Rap1 revealed by genome-wide maps of protein-DNA association
    • Lieb, J.D., X. Liu, D. Botstein, and P.O. Brown, 2001. Promoter-specific binding of Rap1 revealed by genome-wide maps of protein-DNA association. Nat. Genet. 28:327-334.
    • (2001) Nat. Genet. , vol.28 , pp. 327-334
    • Lieb, J.D.1    Liu, X.2    Botstein, D.3    Brown, P.O.4
  • 44
    • 0035947084 scopus 로고    scopus 로고
    • Identification of RFC(Ctf18p, Ctf8p, Dcc 1p): An alternative RFC complex required for sister chromatid cohesion in S. cerevisiae
    • Mayer, M.L., S.P. Gygi, R. Aebersold, and P. Mieter, 2001. Identification of RFC(Ctf18p, Ctf8p, Dcc 1p): an alternative RFC complex required for sister chromatid cohesion in S. cerevisiae. Mol. Cell, 7:959-970.
    • (2001) Mol. Cell , vol.7 , pp. 959-970
    • Mayer, M.L.1    Gygi, S.P.2    Aebersold, R.3    Mieter, P.4
  • 45
    • 1642321066 scopus 로고    scopus 로고
    • Histone fold protein Dls1p is required for Isw2-dependent chromatin remodeling in vivo
    • McConnell, A.D., M.E. Gelbart, and T. Tsukiyama. 2004. Histone fold protein Dls1p is required for Isw2-dependent chromatin remodeling in vivo. Mol. Cell. Biol. 24:2605-2613.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 2605-2613
    • McConnell, A.D.1    Gelbart, M.E.2    Tsukiyama, T.3
  • 46
    • 0037423930 scopus 로고    scopus 로고
    • Conserved histone variant H2A.Z protects euchromatin from the ectopic spread of silent heterochromatin
    • Meneghini, M.D., M. Wu, and H.D. Madhani. 2003. Conserved histone variant H2A.Z protects euchromatin from the ectopic spread of silent heterochromatin. Cell. 112:725-736,
    • (2003) Cell , vol.112 , pp. 725-736
    • Meneghini, M.D.1    Wu, M.2    Madhani, H.D.3
  • 47
    • 0348184963 scopus 로고    scopus 로고
    • ATP-driven exchange of histone H2AZ variant catalyzed by SWR1 chromatin remodeling complex
    • Mizuguchi, G., X. Shen, J. Landry, W.H. Wu, S. Sen, and C. Wu, 2004. ATP-driven exchange of histone H2AZ variant catalyzed by SWR1 chromatin remodeling complex. Science. 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
  • 48
    • 0032561189 scopus 로고    scopus 로고
    • RNA polymerase II holoenzymes and sub-complexes
    • Myer, V.E., and R.A. Young. 1998. RNA polymerase II holoenzymes and sub-complexes. J. Biol. Chem. 273:27757-27760
    • (1998) J. Biol. Chem. , vol.273 , pp. 27757-27760
    • Myer, V.E.1    Young, R.A.2
  • 49
    • 0028979332 scopus 로고
    • DNA polymerase epsilon links the DNA replication machinery to the S phase checkpoint
    • Navas, T.A., Z. Zhou, and S.J. Elledge. 1995. DNA polymerase epsilon links the DNA replication machinery to the S phase checkpoint. Cell. 80:29-39.
    • (1995) Cell , vol.80 , pp. 29-39
    • Navas, T.A.1    Zhou, Z.2    Elledge, S.J.3
  • 50
    • 0034667778 scopus 로고    scopus 로고
    • Structure and function of the fourth subunit (Dpb4p) of DNA polymerase epsilon in Saccharomyces cerevisiae
    • Ohya, T., S. Maki, Y. Kawasaki, and A. Sugino. 2000. Structure and function of the fourth subunit (Dpb4p) of DNA polymerase epsilon in Saccharomyces cerevisiae. Nucleic Acids Res. 28:3846-3852.
    • (2000) Nucleic Acids Res. , vol.28 , pp. 3846-3852
    • Ohya, T.1    Maki, S.2    Kawasaki, Y.3    Sugino, A.4
  • 51
    • 0037008736 scopus 로고    scopus 로고
    • The DNA polymerase domain of pol(epsilon) is required for rapid, efficient, and highly accurate chromosomal DNA replication, telomere length maintenance, and normal cell senescence in Saccharomyces cerevisiae
    • Ohya, T., Y. Kawasaki, S. Hiraga, S. Kanbara, K. Nakajo, N. Nakashima, A. Suzuki, and A. Sugino. 2002. The DNA polymerase domain of pol(epsilon) is required for rapid, efficient, and highly accurate chromosomal DNA replication, telomere length maintenance, and normal cell senescence in Saccharomyces cerevisiae. J. Biol. Chem. 277:28099-28108.
    • (2002) J. Biol. Chem. , vol.277 , pp. 28099-28108
    • Ohya, T.1    Kawasaki, Y.2    Hiraga, S.3    Kanbara, S.4    Nakajo, K.5    Nakashima, N.6    Suzuki, A.7    Sugino, A.8
  • 52
    • 1342346506 scopus 로고    scopus 로고
    • Barrier proteins remodel and modify chromatin to restrict silenced domains
    • Oki, M., L. Valenzuela, T. Chiba, T. Ito, and R.T. Kamakaka. 2004. Barrier proteins remodel and modify chromatin to restrict silenced domains. Mol. Cell Biol. 24:1956-1967.
    • (2004) Mol. Cell Biol. , vol.24 , pp. 1956-1967
    • Oki, M.1    Valenzuela, L.2    Chiba, T.3    Ito, T.4    Kamakaka, R.T.5
  • 53
    • 0036849432 scopus 로고    scopus 로고
    • Checking on the fork: The DNA-replication stress-response pathway
    • Osborn, A.J., S.J. Elledge, and L. Zou. 2002. Checking on the fork: the DNA-replication stress-response pathway. Trends Cell Biol. 12:509-516.
    • (2002) Trends Cell Biol. , vol.12 , pp. 509-516
    • Osborn, A.J.1    Elledge, S.J.2    Zou, L.3
  • 54
    • 0036176982 scopus 로고    scopus 로고
    • The PWWP domain of mammalian DNA methyltransferase Dnmt3b defines a new family of DNA-binding folds
    • Qiu, C., K, Sawada, X. Zhang, and X. Cheng. 2002. The PWWP domain of mammalian DNA methyltransferase Dnmt3b defines a new family of DNA-binding folds. Nat. Struct. Biol. 9:217-224.
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 217-224
    • Qiu, C.1    Sawada, K.2    Zhang, X.3    Cheng, X.4
  • 55
    • 0034025190 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae PAU genes are induced by anaerobiosis
    • Rachidi, N., M.J. Martinez, P. Barre, and B. Blondin. 2000. Saccharomyces cerevisiae PAU genes are induced by anaerobiosis. Mol. Microbiol. 35:1421-1430.
    • (2000) Mol. Microbiol. , vol.35 , pp. 1421-1430
    • Rachidi, N.1    Martinez, M.J.2    Barre, P.3    Blondin, B.4
  • 57
    • 0030722506 scopus 로고    scopus 로고
    • A distinct nuclear import pathway used by ribosomal proteins
    • Rout, M.P., G. Blobel, and J.D. Aitchison, 1997. A distinct nuclear import pathway used by ribosomal proteins. Cell. 89:715-725.
    • (1997) Cell , vol.89 , pp. 715-725
    • Rout, M.P.1    Blobel, G.2    Aitchison, J.D.3
  • 58
    • 0034695924 scopus 로고    scopus 로고
    • The yeast nuclear pore complex: Composition, architecture, and transport mechanism
    • Rout, M.P., J.D. Aitchison, A. Suprapto, K. Hjertaas, Y. Zhao, and B.T. Chait. 2000. The yeast nuclear pore complex: composition, architecture, and transport mechanism. J. Cell Biol. 148:635-651.
    • (2000) J. Cell Biol. , vol.148 , pp. 635-651
    • Rout, M.P.1    Aitchison, J.D.2    Suprapto, A.3    Hjertaas, K.4    Zhao, Y.5    Chait, B.T.6
  • 59
    • 0037636027 scopus 로고    scopus 로고
    • The establishment, inheritance, and function of silenced chromatin in Saccharomyces cerevisiae
    • Rusche, L.N., A.L. Kirchmaier, and J. Rine. 2003, The establishment, inheritance, and function of silenced chromatin in Saccharomyces cerevisiae. Anna. Rev. Biochem. 72:481-516.
    • (2003) Anna. Rev. Biochem. , vol.72 , pp. 481-516
    • Rusche, L.N.1    Kirchmaier, A.L.2    Rine, J.3
  • 61
    • 0037402422 scopus 로고    scopus 로고
    • Mass spectrometric quantification of acetylation at specific lysines within the amino-terminal tail of histone H4
    • Smith, C.M., P.R. Gafken, Z. Zhang, D.E. Gottschling, J.B. Smith, and D.L. Smith. 2003. Mass spectrometric quantification of acetylation at specific lysines within the amino-terminal tail of histone H4. Anal. Biochem, 316:23-33.
    • (2003) Anal. Biochem , vol.316 , pp. 23-33
    • Smith, C.M.1    Gafken, P.R.2    Zhang, Z.3    Gottschling, D.E.4    Smith, J.B.5    Smith, D.L.6
  • 63
    • 0034603990 scopus 로고    scopus 로고
    • The PWWP domain: A potential protein-protein interaction domain in nuclear proteins influencing differentiation?
    • Stec, I., S.B. Nagl, G.J. van Ommen, and J.T. den Dunnen. 2000. The PWWP domain: a potential protein-protein interaction domain in nuclear proteins influencing differentiation? FEBS Lett. 473:1-5.
    • (2000) FEBS Lett. , vol.473 , pp. 1-5
    • Stec, I.1    Nagl, S.B.2    Van Ommen, G.J.3    Den Dunnen, J.T.4
  • 64
    • 0031027431 scopus 로고    scopus 로고
    • Sir2 and Sir4 interactions differ in core and extended telomeric heterochromatin in yeast
    • Strahl-Bolsinger, S., A. Hecht, K. Luo, and M. Grunstein. 1997. Sir2 and Sir4 interactions differ in core and extended telomeric heterochromatin in yeast. Genes Dev. 11:83-93.
    • (1997) Genes Dev. , vol.11 , pp. 83-93
    • Strahl-Bolsinger, S.1    Hecht, A.2    Luo, K.3    Grunstein, M.4
  • 65
    • 0036842129 scopus 로고    scopus 로고
    • Sir2p and Sas2p opposingly regulate acetylation of yeast histone H4 lysine 16 and spreading of heterochromatin
    • Suka, N., K. Luo, and M. Grunstein. 2002. Sir2p and Sas2p opposingly regulate acetylation of yeast histone H4 lysine 16 and spreading of heterochromatin. Nat. Genet. 32:378-383.
    • (2002) Nat. Genet. , vol.32 , pp. 378-383
    • Suka, N.1    Luo, K.2    Grunstein, M.3
  • 66
    • 0037077178 scopus 로고    scopus 로고
    • Dotl p modulates silencing in yeast by methylation of the nucleosome core
    • van Leeuwen, F., P.R. Gafken, and D.E. Gottschling. 2002. Dotl p modulates silencing in yeast by methylation of the nucleosome core. Cell. 109:745-756.
    • (2002) Cell , vol.109 , pp. 745-756
    • Van Leeuwen, F.1    Gafken, P.R.2    Gottschling, D.E.3
  • 67
    • 0037648396 scopus 로고    scopus 로고
    • Maintenance of chromatin states: An open-and-shut case
    • Vermaak, D., K. Ahmad, and S. Henikoff. 2003. Maintenance of chromatin states: an open-and-shut case. Curr. Opin. Cell Biol. 15:266-274.
    • (2003) Curr. Opin. Cell Biol. , vol.15 , pp. 266-274
    • Vermaak, D.1    Ahmad, K.2    Henikoff, S.3
  • 69
    • 0034724871 scopus 로고    scopus 로고
    • Steady-state levels of histone acetylation in Saccharomyces cerevisiae
    • Waterborg, J.H. 2000. Steady-state levels of histone acetylation in Saccharomyces cerevisiae. J. Biol. Chem. 275:13007-13011.
    • (2000) J. Biol. Chem. , vol.275 , pp. 13007-13011
    • Waterborg, J.H.1
  • 70
    • 0037009519 scopus 로고    scopus 로고
    • Structure and function of the BAH-containing domain of Ore lp in epigenetic silencing
    • Zhang, Z., M.K. Hayashi, O. Merkel, B. Stillman, and R.M. Xu. 2002. Structure and function of the BAH-containing domain of Ore lp in epigenetic silencing. EMBO J. 21:4600-4611.
    • (2002) EMBO J. , vol.21 , pp. 4600-4611
    • Zhang, Z.1    Hayashi, M.K.2    Merkel, O.3    Stillman, B.4    Xu, R.M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.