메뉴 건너뛰기




Volumn 1783, Issue 9, 2008, Pages 1595-1604

Crosstalk between Nap1 protein and Cds1 checkpoint kinase to maintain chromatin integrity

Author keywords

Cell cycle; Checkpoint; Chromatin; Fission yeast; Nap1

Indexed keywords

CHECKPOINT KINASE 1; CHECKPOINT KINASE 2; HISTONE H2AX; NUCLEAR PROTEIN; PROTEIN NAP1; UNCLASSIFIED DRUG; CELL CYCLE PROTEIN; CHAPERONE; NAP1 PROTEIN, S POMBE; NAP2 PROTEIN, S POMBE; PROTEIN SERINE THREONINE KINASE; SCHIZOSACCHAROMYCES POMBE PROTEIN;

EID: 49149130382     PISSN: 01674889     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2008.03.019     Document Type: Article
Times cited : (7)

References (58)
  • 1
    • 0018221572 scopus 로고
    • Nucleosomes are assembled by an acidic protein which binds histones and transfers them to DNA
    • Laskey R.A., Honda B.M., Mills A.D., and Finch J.T. Nucleosomes are assembled by an acidic protein which binds histones and transfers them to DNA. Nature 275 (1978) 416-420
    • (1978) Nature , vol.275 , pp. 416-420
    • Laskey, R.A.1    Honda, B.M.2    Mills, A.D.3    Finch, J.T.4
  • 2
    • 0020159426 scopus 로고
    • Soluble acidic complexes containing histones H3 and H4 in nuclei of Xenopus laevis oocytes
    • Kleinschmidt J.A., and Franke W.W. Soluble acidic complexes containing histones H3 and H4 in nuclei of Xenopus laevis oocytes. Cell 29 (1982) 799-809
    • (1982) Cell , vol.29 , pp. 799-809
    • Kleinschmidt, J.A.1    Franke, W.W.2
  • 4
    • 11844263936 scopus 로고    scopus 로고
    • The histone chaperone TAF-I/SET/INHAT is required for transcription in vitro of chromatin templates
    • Gamble M.J., Erdjument-Bromage H., Tempst P., Freedman L.P., and Fisher R.P. The histone chaperone TAF-I/SET/INHAT is required for transcription in vitro of chromatin templates. Mol. Cell. Biol. 25 (2005) 797-807
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 797-807
    • Gamble, M.J.1    Erdjument-Bromage, H.2    Tempst, P.3    Freedman, L.P.4    Fisher, R.P.5
  • 5
    • 0024372060 scopus 로고
    • Purification and characterization of CAF-I, a human cell factor required for chromatin assembly during DNA replication in vitro
    • Smith S., and Stillman B. Purification and characterization of CAF-I, a human cell factor required for chromatin assembly during DNA replication in vitro. Cell 58 (1989) 15-25
    • (1989) Cell , vol.58 , pp. 15-25
    • Smith, S.1    Stillman, B.2
  • 6
    • 0036091117 scopus 로고    scopus 로고
    • Chromatin assembly: cooperation between histone chaperones and ATP-dependent nucleosome remodeling machines
    • Tyler J.K. Chromatin assembly: cooperation between histone chaperones and ATP-dependent nucleosome remodeling machines. Eur. J. Biochem. 269 (2002) 2268-2274
    • (2002) Eur. J. Biochem. , vol.269 , pp. 2268-2274
    • Tyler, J.K.1
  • 7
    • 0037011167 scopus 로고    scopus 로고
    • A role for nucleosome assembly protein 1 in the nuclear transport of histones H2A and H2B
    • Mosammaparast N., Ewart C.S., and Pemberton L.F. A role for nucleosome assembly protein 1 in the nuclear transport of histones H2A and H2B. EMBO J. 21 (2002) 6527-6538
    • (2002) EMBO J. , vol.21 , pp. 6527-6538
    • Mosammaparast, N.1    Ewart, C.S.2    Pemberton, L.F.3
  • 9
    • 0021470855 scopus 로고
    • Purification and initial characterization of a protein which facilitates assembly of nucleosome-like structure from mammalian cells
    • Ishimi Y., Hirosumi J., Sato W., Sugasawa K., Yokota S., Hanaoka F., et al. Purification and initial characterization of a protein which facilitates assembly of nucleosome-like structure from mammalian cells. Eur. J. Biochem. 142 (1984) 431-439
    • (1984) Eur. J. Biochem. , vol.142 , pp. 431-439
    • Ishimi, Y.1    Hirosumi, J.2    Sato, W.3    Sugasawa, K.4    Yokota, S.5    Hanaoka, F.6
  • 10
    • 0025816844 scopus 로고
    • Identification and molecular cloning of yeast homolog of nucleosome assembly protein I which facilitates nucleosome assembly in vitro
    • Ishimi Y., and Kikuchi A. Identification and molecular cloning of yeast homolog of nucleosome assembly protein I which facilitates nucleosome assembly in vitro. J. Biol. Chem. 266 (1991) 7025-7029
    • (1991) J. Biol. Chem. , vol.266 , pp. 7025-7029
    • Ishimi, Y.1    Kikuchi, A.2
  • 11
    • 0034724563 scopus 로고    scopus 로고
    • NAP-2: histone chaperone function and phosphorylation state through the cell cycle
    • Rodriguez P., Pelletier J., Price G.B., and Zannis-Hadjopoulos M. NAP-2: histone chaperone function and phosphorylation state through the cell cycle. J. Mol. Biol. 298 (2000) 225-238
    • (2000) J. Mol. Biol. , vol.298 , pp. 225-238
    • Rodriguez, P.1    Pelletier, J.2    Price, G.B.3    Zannis-Hadjopoulos, M.4
  • 12
    • 33644753839 scopus 로고    scopus 로고
    • Chromatin remodeling by nucleosome disassembly in vitro
    • Lorch Y., Maier-Davis B., and Kornberg R.D. Chromatin remodeling by nucleosome disassembly in vitro. PNAS 103 (2006) 3090-3093
    • (2006) PNAS , vol.103 , pp. 3090-3093
    • Lorch, Y.1    Maier-Davis, B.2    Kornberg, R.D.3
  • 13
    • 15544369061 scopus 로고    scopus 로고
    • Distinct activities of CHD1 and ACF in ATP-dependent chromatin assembly
    • Lusser A., Urwin D.L., and Kadonaga J.T. Distinct activities of CHD1 and ACF in ATP-dependent chromatin assembly. Nat. Struct. Mol. Biol. 12 (2005) 160-166
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 160-166
    • Lusser, A.1    Urwin, D.L.2    Kadonaga, J.T.3
  • 14
    • 0033118950 scopus 로고    scopus 로고
    • Chromatin assembly: biochemical identities and genetic redundancy
    • Adams C.R., and Kamakaka R.T. Chromatin assembly: biochemical identities and genetic redundancy. Curr. Opin. Genet. Dev. 9 (1999) 185-190
    • (1999) Curr. Opin. Genet. Dev. , vol.9 , pp. 185-190
    • Adams, C.R.1    Kamakaka, R.T.2
  • 15
    • 0037311294 scopus 로고    scopus 로고
    • Histone chaperones and nucleosome assembly
    • Akey C.W., and Luger K. Histone chaperones and nucleosome assembly. Curr. Opin. Struct. Biol. 13 (2003) 6-14
    • (2003) Curr. Opin. Struct. Biol. , vol.13 , pp. 6-14
    • Akey, C.W.1    Luger, K.2
  • 17
    • 2642515598 scopus 로고    scopus 로고
    • A new fluorescence resonance energy transfer approach demonstrates that the histone variant H2AZ stabilizes the histone octamer within the nucleosome
    • Park Y.J., Dyer P.N., Tremethick D.J., and Luger K. A new fluorescence resonance energy transfer approach demonstrates that the histone variant H2AZ stabilizes the histone octamer within the nucleosome. J. Biol. Chem. 279 (2004) 24274-24282
    • (2004) J. Biol. Chem. , vol.279 , pp. 24274-24282
    • Park, Y.J.1    Dyer, P.N.2    Tremethick, D.J.3    Luger, K.4
  • 18
    • 0038054272 scopus 로고    scopus 로고
    • Genome-wide expression analysis of NAP1 in Saccharomyces cerevisiae
    • Ohkuni K., Shirahige K., and Kikuchi A. Genome-wide expression analysis of NAP1 in Saccharomyces cerevisiae. Biochem. Biophys. Res. Commun. 306 (2003) 5-9
    • (2003) Biochem. Biophys. Res. Commun. , vol.306 , pp. 5-9
    • Ohkuni, K.1    Shirahige, K.2    Kikuchi, A.3
  • 19
    • 0033898468 scopus 로고    scopus 로고
    • p300-mediated acetylation facilitates the transfer of histone H2A-H2B dimers from nucleosomes to a histone chaperone
    • Ito T., Ikehara T., Nakagawa T., Kraus W.L., and Muramatsu M. p300-mediated acetylation facilitates the transfer of histone H2A-H2B dimers from nucleosomes to a histone chaperone. Genes Dev. 14 (2000) 1899-1907
    • (2000) Genes Dev. , vol.14 , pp. 1899-1907
    • Ito, T.1    Ikehara, T.2    Nakagawa, T.3    Kraus, W.L.4    Muramatsu, M.5
  • 20
    • 0034462693 scopus 로고    scopus 로고
    • Functional interaction between nucleosome assembly proteins and p300/CREB-binding protein family coactivators
    • Shikama N., Chan H.M., Krstic-Demonacos M., Smith L., Lee C.W., Cairns W., et al. Functional interaction between nucleosome assembly proteins and p300/CREB-binding protein family coactivators. Mol. Cell. Biol. 20 (2000) 8933-8943
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 8933-8943
    • Shikama, N.1    Chan, H.M.2    Krstic-Demonacos, M.3    Smith, L.4    Lee, C.W.5    Cairns, W.6
  • 21
    • 0029080942 scopus 로고
    • Members of the NAP/SET family of proteins interact specifically with B-type cyclins
    • Kellogg D.R., Kikuchi A., Fujii-Nakata T., Turck C.W., and Murray A.W. Members of the NAP/SET family of proteins interact specifically with B-type cyclins. J. Cell Biol. 130 (1995) 661-673
    • (1995) J. Cell Biol. , vol.130 , pp. 661-673
    • Kellogg, D.R.1    Kikuchi, A.2    Fujii-Nakata, T.3    Turck, C.W.4    Murray, A.W.5
  • 22
    • 0028991340 scopus 로고
    • NAP1 acts with Clb1 to perform mitotic functions and to suppress polar bud growth in budding yeast
    • Kellogg D.R., and Murray A.W. NAP1 acts with Clb1 to perform mitotic functions and to suppress polar bud growth in budding yeast. J. Cell Biol. 130 (1995) 675-685
    • (1995) J. Cell Biol. , vol.130 , pp. 675-685
    • Kellogg, D.R.1    Murray, A.W.2
  • 23
    • 0035181837 scopus 로고    scopus 로고
    • The Sda1 protein is required for passage through start
    • Zimmerman Z.A., and Kellogg D.R. The Sda1 protein is required for passage through start. Mol. Biol. Cell 12 (2001) 201-219
    • (2001) Mol. Biol. Cell , vol.12 , pp. 201-219
    • Zimmerman, Z.A.1    Kellogg, D.R.2
  • 24
    • 0030742542 scopus 로고    scopus 로고
    • Control of mitotic events by Nap1 and the Gin4 kinase
    • Altman R., and Kellogg D. Control of mitotic events by Nap1 and the Gin4 kinase. J.Cell Biol. 138 (1997) 119-130
    • (1997) J.Cell Biol. , vol.138 , pp. 119-130
    • Altman, R.1    Kellogg, D.2
  • 25
    • 0029808466 scopus 로고    scopus 로고
    • Cell cycle checkpoints: preventing an identity crisis
    • Elledge S.J. Cell cycle checkpoints: preventing an identity crisis. Science 274 (1996) 1664-1672
    • (1996) Science , vol.274 , pp. 1664-1672
    • Elledge, S.J.1
  • 26
    • 0032004942 scopus 로고    scopus 로고
    • S-phase-specific activation of Cds1 kinase defines a subpathway of the checkpoint response in Schizosaccharomyces pombe
    • Lindsay H.D., Griffiths D.J.F., Edwards R.J., Christensen P.U., Murray J.M., Osman F., et al. S-phase-specific activation of Cds1 kinase defines a subpathway of the checkpoint response in Schizosaccharomyces pombe. Genes Dev. 12 (1998) 382-395
    • (1998) Genes Dev. , vol.12 , pp. 382-395
    • Lindsay, H.D.1    Griffiths, D.J.F.2    Edwards, R.J.3    Christensen, P.U.4    Murray, J.M.5    Osman, F.6
  • 27
  • 28
    • 0029664616 scopus 로고    scopus 로고
    • rad-dependent response of the chk1-encoded protein kinase at the DNA damage checkpoint
    • %
    • Walworth N.C., and Bernards R. rad-dependent response of the chk1-encoded protein kinase at the DNA damage checkpoint. Science 19 271 (1996) 353-356 %
    • (1996) Science , vol.19 , Issue.271 , pp. 353-356
    • Walworth, N.C.1    Bernards, R.2
  • 29
    • 0032496322 scopus 로고    scopus 로고
    • Replication checkpoint enforced by kinases Cds1 and Chk1
    • Boddy M.N., Furnari B., Mondesert O., and Russell P. Replication checkpoint enforced by kinases Cds1 and Chk1. Science 280 (1998) 909-912
    • (1998) Science , vol.280 , pp. 909-912
    • Boddy, M.N.1    Furnari, B.2    Mondesert, O.3    Russell, P.4
  • 30
    • 0032941746 scopus 로고    scopus 로고
    • Cdc25 inhibited in vivo and in vitro by checkpoint kinases Cds1 and Chk1
    • Furnari B., Blasina A., Boddy M.N., McGowan C.H., and Russell P. Cdc25 inhibited in vivo and in vitro by checkpoint kinases Cds1 and Chk1. Mol. Biol. Cell 10 (1999) 833-845
    • (1999) Mol. Biol. Cell , vol.10 , pp. 833-845
    • Furnari, B.1    Blasina, A.2    Boddy, M.N.3    McGowan, C.H.4    Russell, P.5
  • 31
    • 0035135161 scopus 로고    scopus 로고
    • Roles of the mitotic inhibitors Wee1 and Mik1 in the G2 DNA damage and replication checkpoints
    • Rhind N., and Russell P. Roles of the mitotic inhibitors Wee1 and Mik1 in the G2 DNA damage and replication checkpoints. Mol. Cell. Biol. 21 (2001) 1499-1508
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 1499-1508
    • Rhind, N.1    Russell, P.2
  • 32
    • 0000502113 scopus 로고    scopus 로고
    • DNA replication checkpoint
    • Boddy M.N., and Russell P. DNA replication checkpoint. Curr. Biol. 11 (2001) R953-R956
    • (2001) Curr. Biol. , vol.11
    • Boddy, M.N.1    Russell, P.2
  • 33
    • 17444416489 scopus 로고    scopus 로고
    • Replication checkpoint kinase Cds1 regulates Mus81 to preserve genome integrity during replication stress
    • Kai M., Boddy M.N., Russell P., and Wang T.S. Replication checkpoint kinase Cds1 regulates Mus81 to preserve genome integrity during replication stress. Genes Dev. 19 (2005) 919-932
    • (2005) Genes Dev. , vol.19 , pp. 919-932
    • Kai, M.1    Boddy, M.N.2    Russell, P.3    Wang, T.S.4
  • 34
    • 13944261496 scopus 로고    scopus 로고
    • Temporal separation of replication and recombination requires the intra-S checkpoint
    • Meister P., Taddei A., Vernis L., Poidevin M., Gasser S.M., and Baldacci G. Temporal separation of replication and recombination requires the intra-S checkpoint. J. Cell Biol. 168 (2005) 537-544
    • (2005) J. Cell Biol. , vol.168 , pp. 537-544
    • Meister, P.1    Taddei, A.2    Vernis, L.3    Poidevin, M.4    Gasser, S.M.5    Baldacci, G.6
  • 35
    • 6344249313 scopus 로고    scopus 로고
    • On the slowing of S phase in response to DNA damage in fission yeast
    • Kumar S., and Huberman J.A. On the slowing of S phase in response to DNA damage in fission yeast. J. Biol. Chem. 279 (2004) 43574-43580
    • (2004) J. Biol. Chem. , vol.279 , pp. 43574-43580
    • Kumar, S.1    Huberman, J.A.2
  • 36
    • 0034472434 scopus 로고    scopus 로고
    • Chk1 and Cds1: linchpins of the DNA damage and replication checkpoint pathways
    • Rhind N., and Russell P. Chk1 and Cds1: linchpins of the DNA damage and replication checkpoint pathways. J. Cell Sci. 113 (2000) 3889-3896
    • (2000) J. Cell Sci. , vol.113 , pp. 3889-3896
    • Rhind, N.1    Russell, P.2
  • 37
    • 0038730929 scopus 로고    scopus 로고
    • A central role for DNA replication forks in checkpoint activation and response
    • Tercero J.A., Longhese M.P., and Diffley J.F.X. A central role for DNA replication forks in checkpoint activation and response. Mol. Cell. 11 (2003) 1323-1336
    • (2003) Mol. Cell. , vol.11 , pp. 1323-1336
    • Tercero, J.A.1    Longhese, M.P.2    Diffley, J.F.X.3
  • 39
    • 0033781393 scopus 로고    scopus 로고
    • Schizosaccharomyces pombe Hsk1p is a potential Cds1p target required for genome integrity
    • Snaith H.A., Brown G.W., and Forsburg S.L. Schizosaccharomyces pombe Hsk1p is a potential Cds1p target required for genome integrity. Mol. Cell. Biol. 20 (2000) 7922-7932
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 7922-7932
    • Snaith, H.A.1    Brown, G.W.2    Forsburg, S.L.3
  • 40
    • 0034765174 scopus 로고    scopus 로고
    • Regulation of initiation of S phase, replication checkpoint signaling, and maintenance of mitotic chromosome structures during S phase by Hsk1 kinase in the fission yeast
    • Takeda T., Ogino K., Tatebayashi K., Ikeda H., Arai K.i., and Masai H. Regulation of initiation of S phase, replication checkpoint signaling, and maintenance of mitotic chromosome structures during S phase by Hsk1 kinase in the fission yeast. Mol. Biol. Cell. 12 (2001) 1257-1274
    • (2001) Mol. Biol. Cell. , vol.12 , pp. 1257-1274
    • Takeda, T.1    Ogino, K.2    Tatebayashi, K.3    Ikeda, H.4    Arai, K.i.5    Masai, H.6
  • 41
    • 34250831538 scopus 로고    scopus 로고
    • A genome-wide role for CHD remodelling factors and Nap1 in nucleosome disassembly
    • Walfridsson J., Khorosjutina O., Matikainen P., Gustafsson C.M., and Ekwall K. A genome-wide role for CHD remodelling factors and Nap1 in nucleosome disassembly. EMBO J. 26 (2007) 2868-2879
    • (2007) EMBO J. , vol.26 , pp. 2868-2879
    • Walfridsson, J.1    Khorosjutina, O.2    Matikainen, P.3    Gustafsson, C.M.4    Ekwall, K.5
  • 42
    • 0026025891 scopus 로고
    • Molecular genetic analysis of fission yeast Schizosaccharomyces pombe
    • Moreno S., Klar A., and Nurse P. Molecular genetic analysis of fission yeast Schizosaccharomyces pombe. Methods Enzymol. 194 (1991) 795-823
    • (1991) Methods Enzymol. , vol.194 , pp. 795-823
    • Moreno, S.1    Klar, A.2    Nurse, P.3
  • 45
    • 0027441494 scopus 로고
    • TATA box mutations in the Schizosaccharomyces pombe nmt1 promoter affect transcription efficiency but not the transcription start point or thiamine repressibility
    • Basi G., Schmid E., and Maundrell K. TATA box mutations in the Schizosaccharomyces pombe nmt1 promoter affect transcription efficiency but not the transcription start point or thiamine repressibility. Gene 123 (1993) 131-136
    • (1993) Gene , vol.123 , pp. 131-136
    • Basi, G.1    Schmid, E.2    Maundrell, K.3
  • 46
    • 0028059299 scopus 로고
    • Temporal order of S phase and mitosis in fission yeast is determined by the state of the p34cdc2-mitotic B cyclin complex
    • Hayles J., Fisher D., Woollard A., and Nurse P. Temporal order of S phase and mitosis in fission yeast is determined by the state of the p34cdc2-mitotic B cyclin complex. Cell 78 (1994) 813-822
    • (1994) Cell , vol.78 , pp. 813-822
    • Hayles, J.1    Fisher, D.2    Woollard, A.3    Nurse, P.4
  • 48
    • 0023105676 scopus 로고
    • Binding mode of nucleosome-assembly protein (AP-I) and histones
    • Ishimi Y., Kojima M., Yamada M., and Hanaoka F. Binding mode of nucleosome-assembly protein (AP-I) and histones. Eur. J. Biochem. 162 (1987) 19-24
    • (1987) Eur. J. Biochem. , vol.162 , pp. 19-24
    • Ishimi, Y.1    Kojima, M.2    Yamada, M.3    Hanaoka, F.4
  • 50
    • 0028256218 scopus 로고
    • Analysis of the Schizosaccharomyces pombe cyclin puc1: evidence for a role in cell cycle exit
    • Forsburg S.L., and Nurse P. Analysis of the Schizosaccharomyces pombe cyclin puc1: evidence for a role in cell cycle exit. J. Cell. Sci. 107 (1994) 601-613
    • (1994) J. Cell. Sci. , vol.107 , pp. 601-613
    • Forsburg, S.L.1    Nurse, P.2
  • 51
    • 0034000124 scopus 로고    scopus 로고
    • The puc1 cyclin regulates the G1 phase of the fission yeast cell cycle in response to cell size
    • Martin-Castellanos C., Blanco M.A., de Prada J.M., and Moreno S. The puc1 cyclin regulates the G1 phase of the fission yeast cell cycle in response to cell size. Mol. Biol. Cell. 11 (2000) 543-554
    • (2000) Mol. Biol. Cell. , vol.11 , pp. 543-554
    • Martin-Castellanos, C.1    Blanco, M.A.2    de Prada, J.M.3    Moreno, S.4
  • 52
    • 0029868069 scopus 로고    scopus 로고
    • Cig2, a B-type cyclin, promotes the onset of S in Schizosaccharomyces pombe
    • Mondesert O., McGowan C.H., and Russell P. Cig2, a B-type cyclin, promotes the onset of S in Schizosaccharomyces pombe. Mol. Cell. Biol. 16 (1996) 1527-1533
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 1527-1533
    • Mondesert, O.1    McGowan, C.H.2    Russell, P.3
  • 53
    • 2442483802 scopus 로고    scopus 로고
    • Requirement of the SCFPop1/Pop2 ubiquitin ligase for degradation of the fission yeast S phase cyclin Cig2
    • Yamano H., Kominami K., Harrison C., Kitamura K., Katayama S., Dhut S., et al. Requirement of the SCFPop1/Pop2 ubiquitin ligase for degradation of the fission yeast S phase cyclin Cig2. J. Biol. Chem. 279 (2004) 18974-18980
    • (2004) J. Biol. Chem. , vol.279 , pp. 18974-18980
    • Yamano, H.1    Kominami, K.2    Harrison, C.3    Kitamura, K.4    Katayama, S.5    Dhut, S.6
  • 54
    • 0025109181 scopus 로고
    • Real-time visualization of cell cycle-dependent changes in microtubule dynamics in cytoplasmic extracts
    • Belmont L.D., Hyman A.A., Sawin K.E., and Mitchison T.J. Real-time visualization of cell cycle-dependent changes in microtubule dynamics in cytoplasmic extracts. Cell 62 (1990) 579-589
    • (1990) Cell , vol.62 , pp. 579-589
    • Belmont, L.D.1    Hyman, A.A.2    Sawin, K.E.3    Mitchison, T.J.4
  • 55
    • 0026775358 scopus 로고
    • Control of microtubule dynamics and length by cyclin A- and cyclin B-dependent kinases in Xenopus egg extracts
    • Verde F., Dogterom M., Stelzer E., Karsenti E., and Leibler S. Control of microtubule dynamics and length by cyclin A- and cyclin B-dependent kinases in Xenopus egg extracts. J. Cell Biol. 118 (1992) 1097-1108
    • (1992) J. Cell Biol. , vol.118 , pp. 1097-1108
    • Verde, F.1    Dogterom, M.2    Stelzer, E.3    Karsenti, E.4    Leibler, S.5
  • 56
    • 0032249331 scopus 로고    scopus 로고
    • On growth and form: control of cell morphogenesis in fission yeast
    • Verde F. On growth and form: control of cell morphogenesis in fission yeast. Current Opinion in Microbiology 1 (1998/12) 712-718
    • (1998) Current Opinion in Microbiology , vol.1 , pp. 712-718
    • Verde, F.1
  • 57
    • 33751292143 scopus 로고    scopus 로고
    • Cytoplasmic microtubule organization in fission yeast
    • Sawin K.E., and Tran P.T. Cytoplasmic microtubule organization in fission yeast. Yeast 23 (2006) 1001-1024
    • (2006) Yeast , vol.23 , pp. 1001-1024
    • Sawin, K.E.1    Tran, P.T.2
  • 58
    • 22144448593 scopus 로고    scopus 로고
    • Histone H2A phosphorylation in DNA double-strand break repair
    • Foster E.R., and Downs J.A. Histone H2A phosphorylation in DNA double-strand break repair. FEBS J. 272 (2005) 3231-3240
    • (2005) FEBS J. , vol.272 , pp. 3231-3240
    • Foster, E.R.1    Downs, J.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.