메뉴 건너뛰기




Volumn 73, Issue 4, 2009, Pages 652-683

The Mcm complex: Unwinding the mechanism of a replicative helicase

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; HELICASE; MINICHROMOSOME MAINTENANCE PROTEIN; MINICHROMOSOME MAINTENANCE PROTEIN 2; MINICHROMOSOME MAINTENANCE PROTEIN 3; MINICHROMOSOME MAINTENANCE PROTEIN 4; MINICHROMOSOME MAINTENANCE PROTEIN 5; MINICHROMOSOME MAINTENANCE PROTEIN 6; MINICHROMOSOME MAINTENANCE PROTEIN 7; SINGLE STRANDED DNA;

EID: 71449107031     PISSN: 10922172     EISSN: None     Source Type: Journal    
DOI: 10.1128/MMBR.00019-09     Document Type: Review
Times cited : (252)

References (280)
  • 1
    • 4043175756 scopus 로고    scopus 로고
    • The X-ray structure of the papillomavirus helicase in complex with its molecular matchmaker E2
    • Abbate, E. A., J. M. Berger, and M. R. Botchan. 2004. The X-ray structure of the papillomavirus helicase in complex with its molecular matchmaker E2. Genes Dev. 18:1981-1996.
    • (2004) Genes Dev. , vol.18 , pp. 1981-1996
    • Abbate, E.A.1    Berger, J.M.2    Botchan, M.R.3
  • 2
    • 0031184659 scopus 로고    scopus 로고
    • A globular complex formation by Nda1 and the other five members of the MCM protein family in fission yeast
    • Adachi, Y., J. Usukura, and M. Yanagida. 1997. A globular complex formation by Nda1 and the other five members of the MCM protein family in fission yeast. Genes Cells 2:467-479. (Pubitemid 127688595)
    • (1997) Genes to Cells , vol.2 , Issue.7 , pp. 467-479
    • Adachi, Y.1    Usukura, J.2    Yanagida, M.3
  • 3
    • 0033529791 scopus 로고    scopus 로고
    • Differential assembly of Cdc45p and DNA polymerases at early and late origins of DNA replication
    • Aparicio, O. M., A. M. Stout, and S. P. Bell. 1999. Differential assembly of Cdc45p and DNA polymerases at early and late origins of DNA replication. Proc. Natl. Acad. Sci. USA 96:9130-9135.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 9130-9135
    • Aparicio, O.M.1    Stout, A.M.2    Bell, S.P.3
  • 4
    • 0030886099 scopus 로고    scopus 로고
    • Components and dynamics of DNA replication complexes in S. cerevisiae: Redistribution of MCM proteins and Cdc45p during S phase
    • Aparicio, O. M., D. M. Weinstein, and S. P. Bell. 1997. Components and dynamics of DNA replication complexes in S. cerevisiae: redistribution of MCM proteins and Cdc45p during S phase. Cell 91:59-69.
    • (1997) Cell , vol.91 , pp. 59-69
    • Aparicio, O.M.1    Weinstein, D.M.2    Bell, S.P.3
  • 5
    • 34247606471 scopus 로고    scopus 로고
    • Cdc45-MCM-GINS, a new power player for DNA replication
    • DOI 10.1186/1747-1028-1-18
    • Aparicio, T., A. Ibarra, and J. Méndez. 2006. Cdc45-MCM-GINS, a new power player for DNA replication. Cell Div. 1:18. (Pubitemid 46731036)
    • (2006) Cell Division , vol.1 , pp. 18
    • Aparicio, T.1    Ibarra, A.2    Mendez, J.3
  • 6
    • 33947127410 scopus 로고    scopus 로고
    • Strength in numbers: Preventing rereplication via multiple mechanisms in eukaryotic cells
    • Arias, E. E., and J. C. Walter. 2007. Strength in numbers: preventing rereplication via multiple mechanisms in eukaryotic cells. Genes Dev. 21:497-518.
    • (2007) Genes Dev. , vol.21 , pp. 497-518
    • Arias, E.E.1    Walter, J.C.2
  • 7
    • 57649119780 scopus 로고    scopus 로고
    • Biochemical characterization of the minichromosome maintenance (MCM) protein of the crenarchaeote Aeropyrum pernix and its interactions with the origin recognition complex (ORC) proteins
    • Atanassova, N., and I. Grainge. 2008. Biochemical characterization of the minichromosome maintenance (MCM) protein of the crenarchaeote Aeropyrum pernix and its interactions with the origin recognition complex (ORC) proteins. Biochemistry 47:13362-13370.
    • (2008) Biochemistry , vol.47 , pp. 13362-13370
    • Atanassova, N.1    Grainge, I.2
  • 8
    • 59649110896 scopus 로고    scopus 로고
    • Insights into the architecture of the replicative helicase from the structure of an archaeal MCM homolog
    • Bae, B., Y. H. Chen, A. Costa, S. Onesti, J. S. Brunzelle, Y. Lin, I. K. Cann, and S. K. Nair. 2009. Insights into the architecture of the replicative helicase from the structure of an archaeal MCM homolog. Structure 17:211-222.
    • (2009) Structure , vol.17 , pp. 211-222
    • Bae, B.1    Chen, Y.H.2    Costa, A.3    Onesti, S.4    Brunzelle, J.S.5    Lin, Y.6    Cann, I.K.7    Nair, S.K.8
  • 9
    • 0842324624 scopus 로고    scopus 로고
    • MCM proteins: DNA damage, mutagenesis and repair
    • Bailis, J. M., and S. L. Forsburg. 2004. MCM proteins: DNA damage, mutagenesis and repair. Curr. Opin. Genet. Dev. 14:17-21.
    • (2004) Curr. Opin. Genet. Dev. , vol.14 , pp. 17-21
    • Bailis, J.M.1    Forsburg, S.L.2
  • 10
    • 40749107055 scopus 로고    scopus 로고
    • Minichromosome maintenance proteins interact with checkpoint and recombination proteins to promote S-phase genome stability
    • Bailis, J. M., D. D. Luche, T. Hunter, and S. L. Forsburg. 2008. Minichromosome maintenance proteins interact with checkpoint and recombination proteins to promote S-phase genome stability. Mol. Cell. Biol. 28:1724-1738.
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 1724-1738
    • Bailis, J.M.1    Luche, D.D.2    Hunter, T.3    Forsburg, S.L.4
  • 12
    • 59049088137 scopus 로고    scopus 로고
    • Intersubunit allosteric communication mediated by a conserved loop in the MCM helicase
    • Barry, E. R., J. E. Lovett, A. Costa, S. M. Lea, and S. D. Bell. 2009. Intersubunit allosteric communication mediated by a conserved loop in the MCM helicase. Proc. Natl. Acad. Sci. USA 106:1051-1056.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 1051-1056
    • Barry, E.R.1    Lovett, J.E.2    Costa, A.3    Lea, S.M.4    Bell, S.D.5
  • 13
    • 33847376397 scopus 로고    scopus 로고
    • Archaeal MCM has separable processivity, substrate choice and helicase domains
    • Barry, E. R., A. T. McGeoch, Z. Kelman, and S. D. Bell. 2007. Archaeal MCM has separable processivity, substrate choice and helicase domains. Nucleic Acids Res. 35:988-998.
    • (2007) Nucleic Acids Res. , vol.35 , pp. 988-998
    • Barry, E.R.1    McGeoch, A.T.2    Kelman, Z.3    Bell, S.D.4
  • 14
    • 0035997368 scopus 로고    scopus 로고
    • DNA replication in eukaryotic cells
    • Bell, S. P., and A. Dutta. 2002. DNA replication in eukaryotic cells. Annu. Rev. Biochem. 71:333-374.
    • (2002) Annu. Rev. Biochem. , vol.71 , pp. 333-374
    • Bell, S.P.1    Dutta, A.2
  • 15
    • 0025755256 scopus 로고
    • Dynamic light scattering investigations of RecA self-assembly and interactions with single strand DNA
    • Benight, A. S., D. H. Wilson, D. M. Budzynski, and R. F. Goldstein. 1991. Dynamic light scattering investigations of RecA self-assembly and interactions with single strand DNA. Biochimie 73:143-155.
    • (1991) Biochimie , vol.73 , pp. 143-155
    • Benight, A.S.1    Wilson, D.H.2    Budzynski, D.M.3    Goldstein, R.F.4
  • 16
    • 50249180325 scopus 로고    scopus 로고
    • SnapShot: Nucleic acid helicases and translocases
    • Berger, J. M. 2008. SnapShot: nucleic acid helicases and translocases. Cell 134:888-888.e1.
    • (2008) Cell , vol.134
    • Berger, J.M.1
  • 17
    • 0034635137 scopus 로고    scopus 로고
    • Mapping protein-protein interactions within a stable complex of DNA primase and DnaB helicase from Bacillus stearothermophilus
    • Bird, L. E., H. Pan, P. Soultanas, and D. B. Wigley. 2000. Mapping protein-protein interactions within a stable complex of DNA primase and DnaB helicase from Bacillus stearothermophilus. Biochemistry 39:171-182.
    • (2000) Biochemistry , vol.39 , pp. 171-182
    • Bird, L.E.1    Pan, H.2    Soultanas, P.3    Wigley, D.B.4
  • 18
    • 44349172245 scopus 로고    scopus 로고
    • Hexameric ring structure of the N-terminal domain of Mycobacterium tuberculosis DnaB helicase
    • DOI 10.1111/j.1742-4658.2008.06460.x
    • Biswas, T., and O. V. Tsodikov. 2008. Hexameric ring structure of the N-terminal domain of Mycobacterium tuberculosis DnaB helicase. FEBS J. 275:3064-3071. (Pubitemid 351743582)
    • (2008) FEBS Journal , vol.275 , Issue.12 , pp. 3064-3071
    • Biswas, T.1    Tsodikov, O.V.2
  • 19
    • 14344265036 scopus 로고    scopus 로고
    • The Mcm467 complex of Saccharomyces cerevisiae is preferentially activated by autonomously replicating DNA sequences
    • DOI 10.1021/bi0491649
    • Biswas-Fiss, E. E., S. M. Khopde, and S. B. Biswas. 2005. The Mcm467 complex of Saccharomyces cerevisiae is preferentially activated by autonomously replicating DNA sequences. Biochemistry 44:2916-2925. (Pubitemid 40293666)
    • (2005) Biochemistry , vol.44 , Issue.8 , pp. 2916-2925
    • Biswas-Fiss, E.E.1    Khopde, S.M.2    Biswas, S.B.3
  • 20
    • 0023904730 scopus 로고
    • A role for the nuclear envelope in controlling DNA replication within the cell cycle
    • Blow, J. J., and R. A. Laskey. 1988. A role for the nuclear envelope in controlling DNA replication within the cell cycle. Nature 332:546-548.
    • (1988) Nature , vol.332 , pp. 546-548
    • Blow, J.J.1    Laskey, R.A.2
  • 21
    • 33845686801 scopus 로고    scopus 로고
    • Structure of the origin-binding domain of simian virus 40 large T antigen bound to DNA
    • DOI 10.1038/sj.emboj.7601452, PII 7601452
    • Bochkareva, E., D. Martynowski, A. Seitova, and A. Bochkarev. 2006. Structure of the origin-binding domain of simian virus 40 large T antigen bound to DNA. EMBO J. 25:5961-5969. (Pubitemid 44967777)
    • (2006) EMBO Journal , vol.25 , Issue.24 , pp. 5961-5969
    • Bochkareva, E.1    Martynowski, D.2    Seitova, A.3    Bochkarev, A.4
  • 22
    • 52649096993 scopus 로고    scopus 로고
    • Subunit organization of Mcm2-7 and the unequal role of active sites in ATP hydrolysis and viability
    • Bochman, M. L., S. P. Bell, and A. Schwacha. 2008. Subunit organization of Mcm2-7 and the unequal role of active sites in ATP hydrolysis and viability. Mol. Cell. Biol. 28:5865-5873.
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 5865-5873
    • Bochman, M.L.1    Bell, S.P.2    Schwacha, A.3
  • 23
    • 36349008252 scopus 로고    scopus 로고
    • Differences in the single-stranded DNA binding activities of MCM2-7 and MCM467: MCM2 and 5 define a slow ATP-dependent step
    • Bochman, M. L., and A. Schwacha. 2007. Differences in the single-stranded DNA binding activities of MCM2-7 and MCM467: MCM2 and 5 define a slow ATP-dependent step. J. Biol. Chem. 282:33795-33804.
    • (2007) J. Biol. Chem. , vol.282 , pp. 33795-33804
    • Bochman, M.L.1    Schwacha, A.2
  • 24
    • 47349114465 scopus 로고    scopus 로고
    • The Mcm2-7 complex has in vitro helicase activity
    • Bochman, M. L., and A. Schwacha. 2008. The Mcm2-7 complex has in vitro helicase activity. Mol. Cell 31:287-293.
    • (2008) Mol. Cell , vol.31 , pp. 287-293
    • Bochman, M.L.1    Schwacha, A.2
  • 26
    • 10944235448 scopus 로고    scopus 로고
    • ATP hydrolysis by ORC catalyzes reiterative Mcm2-7 assembly at a defined origin of replication
    • Bowers, J. L., J. C. Randell, S. Chen, and S. P. Bell. 2004. ATP hydrolysis by ORC catalyzes reiterative Mcm2-7 assembly at a defined origin of replication. Mol. Cell 16:967-978.
    • (2004) Mol. Cell , vol.16 , pp. 967-978
    • Bowers, J.L.1    Randell, J.C.2    Chen, S.3    Bell, S.P.4
  • 27
    • 0024284091 scopus 로고
    • Duplex opening by dnaA protein at novel sequences in initiation of replication at the origin of the E. coli chromosome
    • Bramhill, D., and A. Kornberg. 1988. Duplex opening by dnaA protein at novel sequences in initiation of replication at the origin of the E. coli chromosome. Cell 52:743-755.
    • (1988) Cell , vol.52 , pp. 743-755
    • Bramhill, D.1    Kornberg, A.2
  • 28
    • 27544445683 scopus 로고    scopus 로고
    • The DNA damage response during DNA replication
    • Branzei, D., and M. Foiani. 2005. The DNA damage response during DNA replication. Curr. Opin. Cell Biol. 17:568-575.
    • (2005) Curr. Opin. Cell Biol. , vol.17 , pp. 568-575
    • Branzei, D.1    Foiani, M.2
  • 29
    • 34249946978 scopus 로고    scopus 로고
    • Interplay of replication checkpoints and repair proteins at stalled replication forks
    • DOI 10.1016/j.dnarep.2007.02.018, PII S1568786407000699, Replication Fork Repair Processes
    • Branzei, D., and M. Foiani. 2007. Interplay of replication checkpoints and repair proteins at stalled replication forks. DNA Repair (Amsterdam) 6:994-1003. (Pubitemid 46880479)
    • (2007) DNA Repair , vol.6 , Issue.7 , pp. 994-1003
    • Branzei, D.1    Foiani, M.2
  • 31
    • 0027214787 scopus 로고
    • Negative cooperativity in the binding of nucleotides to Escherichia coli replicative helicase DnaB protein. Interactions with fluorescent nucleotide analogs
    • Bujalowski, W., and M. M. Klonowska. 1993. Negative cooperativity in the binding of nucleotides to Escherichia coli replicative helicase DnaB protein. Interactions with fluorescent nucleotide analogs. Biochemistry 32:5888-5900.
    • (1993) Biochemistry , vol.32 , pp. 5888-5900
    • Bujalowski, W.1    Klonowska, M.M.2
  • 32
    • 23944507608 scopus 로고    scopus 로고
    • Molecular anatomy and regulation of a stable replisome at a paused eukaryotic DNA replication fork
    • DOI 10.1101/gad.337205
    • Calzada, A., B. Hodgson, M. Kanemaki, A. Bueno, and K. Labib. 2005. Molecular anatomy and regulation of a stable replisome at a paused eukaryotic DNA replication fork. Genes Dev. 19:1905-1919. (Pubitemid 41186991)
    • (2005) Genes and Development , vol.19 , Issue.16 , pp. 1905-1919
    • Calzada, A.1    Hodgson, B.2    Kanemaki, M.3    Bueno, A.4    Labib, K.5
  • 33
    • 4444381255 scopus 로고    scopus 로고
    • Biochemical characterization of Cdc6/Orc1 binding to the replication origin of the euryarchaeon Methanothermobacter thermoautotrophicus
    • Capaldi, S. A., and J. M. Berger. 2004. Biochemical characterization of Cdc6/Orc1 binding to the replication origin of the euryarchaeon Methanothermobacter thermoautotrophicus. Nucleic Acids Res. 32:4821-4832.
    • (2004) Nucleic Acids Res. , vol.32 , pp. 4821-4832
    • Capaldi, S.A.1    Berger, J.M.2
  • 34
    • 0037023748 scopus 로고    scopus 로고
    • Physical and functional interaction between the mini-chromosome maintenance-like DNA helicase and the single-stranded DNA binding protein from the crenarchaeon Sulfolobus solfataricus
    • Carpentieri, F., M. De Felice, M. De Falco, M. Rossi, and F. M. Pisani. 2002. Physical and functional interaction between the mini-chromosome maintenance-like DNA helicase and the single-stranded DNA binding protein from the crenarchaeon Sulfolobus solfataricus. J. Biol. Chem. 277:12118-12127.
    • (2002) J. Biol. Chem. , vol.277 , pp. 12118-12127
    • Carpentieri, F.1    De Felice, M.2    De Falco, M.3    Rossi, M.4    Pisani, F.M.5
  • 35
    • 34547874631 scopus 로고    scopus 로고
    • Crystal structure of the GINS complex and functional insights into its role in DNA replication
    • Chang, Y. P., G. Wang, V. Bermudez, J. Hurwitz, and X. S. Chen. 2007. Crystal structure of the GINS complex and functional insights into its role in DNA replication. Proc. Natl. Acad. Sci. USA 104:12685-12690.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 12685-12690
    • Chang, Y.P.1    Wang, G.2    Bermudez, V.3    Hurwitz, J.4    Chen, X.S.5
  • 36
    • 33744769406 scopus 로고    scopus 로고
    • The two helicases of herpes simplex virus type 1 (HSV-1)
    • DOI 10.2741/1964
    • Chattopadhyay, S., Y. Chen, and S. K. Weller. 2006. The two helicases of herpes simplex virus type 1 (HSV-1). Front. Biosci. 11:2213-2223. (Pubitemid 43822554)
    • (2006) Frontiers in Bioscience , vol.11 , Issue.SUPPL. 1 , pp. 2213-2223
    • Chattopadhyay, S.1    Chen, Y.2    Weller, S.K.3
  • 37
    • 36249005517 scopus 로고    scopus 로고
    • Orc6 is required for dynamic recruitment of Cdt1 during repeated Mcm2-7 loading
    • DOI 10.1101/gad.1596807
    • Chen, S., M. A. de Vries, and S. P. Bell. 2007. Orc6 is required for dynamic recruitment of Cdt1 during repeated Mcm2-7 loading. Genes Dev. 21:2897-2907. (Pubitemid 350133438)
    • (2007) Genes and Development , vol.21 , Issue.22 , pp. 2897-2907
    • Chen, S.1    De Vries, M.A.2    Bell, S.P.3
  • 38
    • 64649100384 scopus 로고    scopus 로고
    • Mechanism of ATP-driven PCNA clamp loading by S. cerevisiae RFC
    • Chen, S., M. K. Levin, M. Sakato, Y. Zhou, and M. M. Hingorani. 2009. Mechanism of ATP-driven PCNA clamp loading by S. cerevisiae RFC. J. Mol. Biol. 388:431-442.
    • (2009) J. Mol. Biol. , vol.388 , pp. 431-442
    • Chen, S.1    Levin, M.K.2    Sakato, M.3    Zhou, Y.4    Hingorani, M.M.5
  • 40
    • 34249875398 scopus 로고    scopus 로고
    • Crystal structure of the human GINS complex
    • DOI 10.1101/gad.1548107
    • Choi, J. M., H. S. Lim, J. J. Kim, O. K. Song, and Y. Cho. 2007. Crystal structure of the human GINS complex. Genes Dev. 21:1316-1321. (Pubitemid 46871035)
    • (2007) Genes and Development , vol.21 , Issue.11 , pp. 1316-1321
    • Jung, M.C.1    Hye, S.L.2    Jeong, J.K.3    Song, O.-K.4    Cho, Y.5
  • 41
    • 0030310075 scopus 로고    scopus 로고
    • DNA replication licensing factor
    • Chong, J. P., and J. J. Blow. 1996. DNA replication licensing factor. Prog. Cell Cycle Res. 2:83-90.
    • (1996) Prog. Cell Cycle Res. , vol.2 , pp. 83-90
    • Chong, J.P.1    Blow, J.J.2
  • 42
    • 0034652354 scopus 로고    scopus 로고
    • A double-hexamer archaeal minichromosome maintenance protein is an ATP-dependent DNA helicase
    • Chong, J. P., M. K. Hayashi, M. N. Simon, R. M. Xu, and B. Stillman. 2000. A double-hexamer archaeal minichromosome maintenance protein is an ATP-dependent DNA helicase. Proc. Natl. Acad. Sci. USA 97:1530-1535.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 1530-1535
    • Chong, J.P.1    Hayashi, M.K.2    Simon, M.N.3    Xu, R.M.4    Stillman, B.5
  • 43
    • 0029670238 scopus 로고    scopus 로고
    • The role of MCM/P1 proteins in the licensing of DNA replication
    • Chong, J. P., P. Thommes, and J. J. Blow. 1996. The role of MCM/P1 proteins in the licensing of DNA replication. Trends Biochem. Sci. 21:102-106.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 102-106
    • Chong, J.P.1    Thommes, P.2    Blow, J.J.3
  • 44
    • 0038308585 scopus 로고    scopus 로고
    • Drosophila MCM10 interacts with members of the prereplication complex and is required for proper chromosome condensation
    • Christensen, T. W., and B. K. Tye. 2003. Drosophila MCM10 interacts with members of the prereplication complex and is required for proper chromosome condensation. Mol. Biol. Cell 14:2206-2215.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 2206-2215
    • Christensen, T.W.1    Tye, B.K.2
  • 46
    • 27644594271 scopus 로고    scopus 로고
    • Crosstalk between primase subunits can act to regulate primer synthesis in trans
    • Corn, J. E., P. J. Pease, G. L. Hura, and J. M. Berger. 2005. Crosstalk between primase subunits can act to regulate primer synthesis in trans. Mol. Cell 20:391-401.
    • (2005) Mol. Cell , vol.20 , pp. 391-401
    • Corn, J.E.1    Pease, P.J.2    Hura, G.L.3    Berger, J.M.4
  • 47
    • 3042798440 scopus 로고    scopus 로고
    • Minichromosome maintenance proteins are direct targets of the ATM and ATR checkpoint kinases
    • Cortez, D., G. Glick, and S. J. Elledge. 2004. Minichromosome maintenance proteins are direct targets of the ATM and ATR checkpoint kinases. Proc. Natl. Acad. Sci. USA 101:10078-10083.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 10078-10083
    • Cortez, D.1    Glick, G.2    Elledge, S.J.3
  • 48
    • 39449123549 scopus 로고    scopus 로고
    • The MCM complex: (just) a replicative helicase?
    • Costa, A., and S. Onesti. 2008. The MCM complex: (just) a replicative helicase? Biochem. Soc. Trans. 36:136-140.
    • (2008) Biochem. Soc. Trans. , vol.36 , pp. 136-140
    • Costa, A.1    Onesti, S.2
  • 49
    • 33845648483 scopus 로고    scopus 로고
    • Structural basis of the Methanothermobacter thermautotrophicus MCM helicase activity
    • DOI 10.1093/nar/gkl708
    • Costa, A., T. Pape, M. van Heel, P. Brick, A. Patwardhan, and S. Onesti. 2006. Structural basis of the Methanothermobacter thermautotrophicus MCM helicase activity. Nucleic Acids Res. 34:5829-5838. (Pubitemid 44941162)
    • (2006) Nucleic Acids Research , vol.34 , Issue.20 , pp. 5829-5838
    • Costa, A.1    Pape, T.2    Van Heel, M.3    Brick, P.4    Patwardhan, A.5    Onesti, S.6
  • 50
    • 33749266161 scopus 로고    scopus 로고
    • Structural studies of the archaeal MCM complex in different functional states
    • Costa, A., T. Pape, M. van Heel, P. Brick, A. Patwardhan, and S. Onesti. 2006. Structural studies of the archaeal MCM complex in different functional states. J. Struct. Biol. 156:210-219.
    • (2006) J. Struct. Biol. , vol.156 , pp. 210-219
    • Costa, A.1    Pape, T.2    Van Heel, M.3    Brick, P.4    Patwardhan, A.5    Onesti, S.6
  • 52
    • 0032871542 scopus 로고    scopus 로고
    • The yeast Saccharomyces cerevisiae does not sequester chloride but can express a functional mammalian chloride channel
    • Coury, L. A., J. E. McGeoch, G. Guidotti, and J. L. Brodsky. 1999. The yeast Saccharomyces cerevisiae does not sequester chloride but can express a functional mammalian chloride channel. FEMS Microbiol. Lett. 179:327-332.
    • (1999) FEMS Microbiol. Lett. , vol.179 , pp. 327-332
    • Coury, L.A.1    McGeoch, J.E.2    Guidotti, G.3    Brodsky, J.L.4
  • 53
    • 30744451401 scopus 로고    scopus 로고
    • DNA-induced switch from independent to sequential dTTP hydrolysis in the bacteriophage T7 DNA helicase
    • Crampton, D. J., S. Mukherjee, and C. C. Richardson. 2006. DNA-induced switch from independent to sequential dTTP hydrolysis in the bacteriophage T7 DNA helicase. Mol. Cell 21:165-174.
    • (2006) Mol. Cell , vol.21 , pp. 165-174
    • Crampton, D.J.1    Mukherjee, S.2    Richardson, C.C.3
  • 54
    • 0035578028 scopus 로고    scopus 로고
    • Nearest neighbour analysis of MCM protein complexes in Drosophila melanogaster
    • Crevel, G., A. Ivetic, K. Ohno, M. Yamaguchi, and S. Cotterill. 2001. Nearest neighbour analysis of MCM protein complexes in Drosophila melanogaster. Nucleic Acids Res. 29:4834-4842. (Pubitemid 33133555)
    • (2001) Nucleic Acids Research , vol.29 , Issue.23 , pp. 4834-4842
    • Crevel, G.1    Ivetic, A.2    Ohno, K.3    Yamaguchi, M.4    Cotterill, S.5
  • 55
    • 12244265093 scopus 로고    scopus 로고
    • DNA replication origins in the Schizosaccharomyces pombe genome
    • Dai, J., R. Y. Chuang, and T. J. Kelly. 2005. DNA replication origins in the Schizosaccharomyces pombe genome. Proc. Natl. Acad. Sci. USA 102:337-342.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 337-342
    • Dai, J.1    Chuang, R.Y.2    Kelly, T.J.3
  • 56
    • 0030845932 scopus 로고    scopus 로고
    • Characterization of Cdc47p-minichromosome maintenance complexes in Saccharomyces cerevisiae: Identification of Cdc45p as a subunit
    • Dalton, S., and B. Hopwood. 1997. Characterization of Cdc47p-minichromosome maintenance complexes in Saccharomyces cerevisiae: identification of Cdc45p as a subunit. Mol. Cell. Biol. 17:5867-5875.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 5867-5875
    • Dalton, S.1    Hopwood, B.2
  • 58
    • 0038475879 scopus 로고    scopus 로고
    • Reconstitution of the Mcm2-7p heterohexamer, subunit arrangement, and ATP site architecture
    • Davey, M. J., C. Indiani, and M. O'Donnell. 2003. Reconstitution of the Mcm2-7p heterohexamer, subunit arrangement, and ATP site architecture. J. Biol. Chem. 278:4491-4499.
    • (2003) J. Biol. Chem. , vol.278 , pp. 4491-4499
    • Davey, M.J.1    Indiani, C.2    O'Donnell, M.3
  • 59
    • 0042200759 scopus 로고    scopus 로고
    • Replicative helicase loaders: Ring breakers and ring makers
    • Davey, M. J., and M. O'Donnell. 2003. Replicative helicase loaders: ring breakers and ring makers. Curr. Biol. 13:R594-R596.
    • (2003) Curr. Biol. , vol.13
    • Davey, M.J.1    O'Donnell, M.2
  • 60
    • 33846001361 scopus 로고    scopus 로고
    • The human GINS complex binds to and specifically stimulates human DNA polymerase α-primase
    • DOI 10.1038/sj.embor.7400870, PII 7400870
    • De Falco, M., E. Ferrari, M. De Felice, M. Rossi, U. Hubscher, and F. M. Pisani. 2007. The human GINS complex binds to and specifically stimulates human DNA polymerase alpha-primase. EMBO Rep. 8:99-103. (Pubitemid 46043807)
    • (2007) EMBO Reports , vol.8 , Issue.1 , pp. 99-103
    • De Falco, M.1    Ferrari, E.2    De Felice, M.3    Rossi, M.4    Hubscher, U.5    Pisani, F.M.6
  • 61
  • 62
    • 5644225579 scopus 로고    scopus 로고
    • A CDC6-like factor from the archaea Sulfolobus solfataricus promotes binding of the mini-chromosome maintenance complex to DNA
    • De Felice, M., L. Esposito, B. Pucci, M. De Falco, M. Rossi, and F. M. Pisani. 2004. A CDC6-like factor from the archaea Sulfolobus solfataricus promotes binding of the mini-chromosome maintenance complex to DNA. J. Biol. Chem. 279:43008-43012.
    • (2004) J. Biol. Chem. , vol.279 , pp. 43008-43012
    • De Felice, M.1    Esposito, L.2    Pucci, B.3    De Falco, M.4    Rossi, M.5    Pisani, F.M.6
  • 63
    • 33644865778 scopus 로고    scopus 로고
    • Biochemical characterization of two Cdc6/ORC1-like proteins from the crenarchaeon Sulfolobus solfataricus
    • DOI 10.1007/s00792-005-0473-0
    • De Felice, M., L. Esposito, M. Rossi, and F. M. Pisani. 2006. Biochemical characterization of two Cdc6/ORC1-like proteins from the crenarchaeon Sulfolobus solfataricus. Extremophiles 10:61-70. (Pubitemid 43375564)
    • (2006) Extremophiles , vol.10 , Issue.1 , pp. 61-70
    • De Felice, M.1    Esposito, L.2    Rossi, M.3    Pisani, F.M.4
  • 64
    • 33749121811 scopus 로고    scopus 로고
    • Mechanisms of a ring shaped helicase
    • Donmez, I., and S. S. Patel. 2006. Mechanisms of a ring shaped helicase. Nucleic Acids Res. 34:4216-4224.
    • (2006) Nucleic Acids Res. , vol.34 , pp. 4216-4224
    • Donmez, I.1    Patel, S.S.2
  • 65
    • 0030951331 scopus 로고    scopus 로고
    • Cdc6p-dependent loading of Mcm proteins onto pre-replicative chromatin in budding yeast
    • Donovan, S., J. Harwood, L. S. Drury, and J. F. Diffley. 1997. Cdc6p-dependent loading of Mcm proteins onto pre-replicative chromatin in budding yeast. Proc. Natl. Acad. Sci. USA 94:5611-5616.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 5611-5616
    • Donovan, S.1    Harwood, J.2    Drury, L.S.3    Diffley, J.F.4
  • 66
    • 34548530410 scopus 로고    scopus 로고
    • Replication origin recognition and deformation by a heterodimeric archaeal Orc1 complex
    • Dueber, E. L., J. E. Corn, S. D. Bell, and J. M. Berger. 2007. Replication origin recognition and deformation by a heterodimeric archaeal Orc1 complex. Science 317:1210-1213.
    • (2007) Science , vol.317 , pp. 1210-1213
    • Dueber, E.L.1    Corn, J.E.2    Bell, S.D.3    Berger, J.M.4
  • 67
    • 0037031834 scopus 로고    scopus 로고
    • MCM2-7 complexes bind chromatin in a distributed pattern surrounding the origin recognition complex in Xenopus egg extracts
    • Edwards, M. C., A. V. Tutter, C. Cvetic, C. H. Gilbert, T. A. Prokhorova, and J. C. Walter. 2002. MCM2-7 complexes bind chromatin in a distributed pattern surrounding the origin recognition complex in Xenopus egg extracts. J. Biol. Chem. 277:33049-33057.
    • (2002) J. Biol. Chem. , vol.277 , pp. 33049-33057
    • Edwards, M.C.1    Tutter, A.V.2    Cvetic, C.3    Gilbert, C.H.4    Prokhorova, T.A.5    Walter, J.C.6
  • 68
    • 69949144606 scopus 로고    scopus 로고
    • Novel DNA-binding properties of the MCMm10 protein from Saccharomyces cerevisiae
    • Eisenberg, S., G. Korza, J. Carson, I. Liachko, and B. K. Tye. 2009. Novel DNA-binding properties of the MCMm10 protein from Saccharomyces cerevisiae. J. Biol. Chem. 284:25412-25420.
    • (2009) J. Biol. Chem. , vol.284 , pp. 25412-25420
    • Eisenberg, S.1    Korza, G.2    Carson, J.3    Liachko, I.4    Tye, B.K.5
  • 69
    • 33746375404 scopus 로고    scopus 로고
    • Mechanism of DNA translocation in a replicative hexameric helicase
    • DOI 10.1038/nature04943, PII NATURE04943
    • Enemark, E. J., and L. Joshua-Tor. 2006. Mechanism of DNA translocation in a replicative hexameric helicase. Nature 442:270-275. (Pubitemid 44114897)
    • (2006) Nature , vol.442 , Issue.7100 , pp. 270-275
    • Enemark, E.J.1    Joshua-Tor, L.2
  • 71
    • 33745041480 scopus 로고    scopus 로고
    • Evolutionary relationships and structural mechanisms of AAA+ proteins
    • Erzberger, J. P., and J. M. Berger. 2006. Evolutionary relationships and structural mechanisms of AAA+ proteins. Annu. Rev. Biophys. Biomol. Struct. 35:93-114.
    • (2006) Annu. Rev. Biophys. Biomol. Struct. , vol.35 , pp. 93-114
    • Erzberger, J.P.1    Berger, J.M.2
  • 72
    • 33746860263 scopus 로고    scopus 로고
    • Structural basis for ATP-dependent DnaA assembly and replication-origin remodeling
    • Erzberger, J. P., M. L. Mott, and J. M. Berger. 2006. Structural basis for ATP-dependent DnaA assembly and replication-origin remodeling. Nat. Struct. Mol. Biol. 13:676-683.
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 676-683
    • Erzberger, J.P.1    Mott, M.L.2    Berger, J.M.3
  • 73
    • 0026724311 scopus 로고
    • Structure and function of simian virus 40 large tumor antigen
    • Fanning, E., and R. Knippers. 1992. Structure and function of simian virus 40 large tumor antigen. Annu. Rev. Biochem. 61:55-85.
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 55-85
    • Fanning, E.1    Knippers, R.2
  • 74
    • 33947130956 scopus 로고    scopus 로고
    • Polyomaviruses
    • M. L. DePamphilis (ed.), Cold Spring Harbor Laboratory Press, Cold Spring Harbor Laboratory, NY
    • Fanning, E., and J. M. Pipas. 2006. Polyomaviruses, p. 627-644. In M. L. DePamphilis (ed.), DNA replication and human disease. Cold Spring Harbor Laboratory Press, Cold Spring Harbor Laboratory, NY.
    • (2006) DNA Replication and Human Disease , pp. 627-644
    • Fanning, E.1    Pipas, J.M.2
  • 75
    • 33746817874 scopus 로고    scopus 로고
    • Fission yeast Mcm10p contains primase activity
    • Fien, K., and J. Hurwitz. 2006. Fission yeast Mcm10p contains primase activity. J. Biol. Chem. 281:22248-22260.
    • (2006) J. Biol. Chem. , vol.281 , pp. 22248-22260
    • Fien, K.1    Hurwitz, J.2
  • 77
    • 30744462819 scopus 로고    scopus 로고
    • Biochemical activities of the BOB1 mutant in Methanobacterium thermoautotrophicum MCM
    • Fletcher, R. J., and X. S. Chen. 2006. Biochemical activities of the BOB1 mutant in Methanobacterium thermoautotrophicum MCM. Biochemistry 45:462-467.
    • (2006) Biochemistry , vol.45 , pp. 462-467
    • Fletcher, R.J.1    Chen, X.S.2
  • 78
    • 29644436609 scopus 로고    scopus 로고
    • Double hexamer disruption and biochemical activities of Methanobacterium thermoautotrophicum MCM
    • Fletcher, R. J., J. Shen, Y. Gomez-Llorente, C. S. Martin, J. M. Carazo, and X. S. Chen. 2005. Double hexamer disruption and biochemical activities of Methanobacterium thermoautotrophicum MCM. J. Biol. Chem. 280:42405-42410.
    • (2005) J. Biol. Chem. , vol.280 , pp. 42405-42410
    • Fletcher, R.J.1    Shen, J.2    Gomez-Llorente, Y.3    Martin, C.S.4    Carazo, J.M.5    Chen, X.S.6
  • 79
    • 52249092176 scopus 로고    scopus 로고
    • Identification of amino acids important for the biochemical activity of Methanothermobacter thermautotrophicus MCM
    • Fletcher, R. J., J. Shen, L. G. Holden, and X. S. Chen. 2008. Identification of amino acids important for the biochemical activity of Methanothermobacter thermautotrophicus MCM. Biochemistry 47:9981-9986.
    • (2008) Biochemistry , vol.47 , pp. 9981-9986
    • Fletcher, R.J.1    Shen, J.2    Holden, L.G.3    Chen, X.S.4
  • 80
    • 1542405310 scopus 로고    scopus 로고
    • Eukaryotic MCM proteins: Beyond replication initiation
    • Forsburg, S. L. 2004. Eukaryotic MCM proteins: beyond replication initiation. Microbiol. Mol. Biol. Rev. 68:109-131.
    • (2004) Microbiol. Mol. Biol. Rev. , vol.68 , pp. 109-131
    • Forsburg, S.L.1
  • 81
    • 39449086412 scopus 로고    scopus 로고
    • The MCM helicase: Linking checkpoints to the replication fork
    • Forsburg, S. L. 2008. The MCM helicase: linking checkpoints to the replication fork. Biochem. Soc. Trans. 36:114-119.
    • (2008) Biochem. Soc. Trans. , vol.36 , pp. 114-119
    • Forsburg, S.L.1
  • 82
    • 61849173573 scopus 로고    scopus 로고
    • Incorporation into the prereplicative complex activates the Mcm2-7 helicase for Cdc7-Dbf4 phosphorylation
    • Francis, L. I., J. C. Randell, T. J. Takara, L. Uchima, and S. P. Bell. 2009. Incorporation into the prereplicative complex activates the Mcm2-7 helicase for Cdc7-Dbf4 phosphorylation. Genes Dev. 23:643-654.
    • (2009) Genes Dev. , vol.23 , pp. 643-654
    • Francis, L.I.1    Randell, J.C.2    Takara, T.J.3    Uchima, L.4    Bell, S.P.5
  • 83
    • 0023664708 scopus 로고
    • In vitro assembly of a prepriming complex at the origin of the Escherichia coli chromosome
    • Funnell, B. E., T. A. Baker, and A. Kornberg. 1987. In vitro assembly of a prepriming complex at the origin of the Escherichia coli chromosome. J. Biol. Chem. 262:10327-10334.
    • (1987) J. Biol. Chem. , vol.262 , pp. 10327-10334
    • Funnell, B.E.1    Baker, T.A.2    Kornberg, A.3
  • 84
    • 4444226952 scopus 로고    scopus 로고
    • Mechanisms of conformational change for a replicative hexameric helicase of SV40 large tumor antigen
    • DOI 10.1016/j.cell.2004.09.017, PII S0092867404008906
    • Gai, D., R. Zhao, D. Li, C. V. Finkielstein, and X. S. Chen. 2004. Mechanisms of conformational change for a replicative hexameric helicase of SV40 large tumor antigen. Cell 119:47-60. (Pubitemid 39349319)
    • (2004) Cell , vol.119 , Issue.1 , pp. 47-60
    • Gai, D.1    Zhao, R.2    Li, D.3    Finkielstein, C.V.4    Chen, X.S.5
  • 85
    • 33645717628 scopus 로고    scopus 로고
    • GINS maintains association of Cdc45 with MCM in replisome progression complexes at eukaryotic DNA replication forks
    • Gambus, A., R. C. Jones, A. Sanchez-Diaz, M. Kanemaki, F. van Deursen, R. D. Edmondson, and K. Labib. 2006. GINS maintains association of Cdc45 with MCM in replisome progression complexes at eukaryotic DNA replication forks. Nat. Cell Biol. 8:358-366.
    • (2006) Nat. Cell Biol. , vol.8 , pp. 358-366
    • Gambus, A.1    Jones, R.C.2    Sanchez-Diaz, A.3    Kanemaki, M.4    Van Deursen, F.5    Edmondson, R.D.6    Labib, K.7
  • 86
    • 34548529079 scopus 로고    scopus 로고
    • Structural basis of DNA replication origin recognition by an ORC protein
    • Gaudier, M., B. S. Schuwirth, S. L. Westcott, and D. B. Wigley. 2007. Structural basis of DNA replication origin recognition by an ORC protein. Science 317:1213-1216.
    • (2007) Science , vol.317 , pp. 1213-1216
    • Gaudier, M.1    Schuwirth, B.S.2    Westcott, S.L.3    Wigley, D.B.4
  • 87
    • 35748962910 scopus 로고    scopus 로고
    • The Hsp70 chaperone machines of Escherichia coli: A paradigm for the repartition of chaperone functions
    • Genevaux, P., C. Georgopoulos, and W. L. Kelley. 2007. The Hsp70 chaperone machines of Escherichia coli: a paradigm for the repartition of chaperone functions. Mol. Microbiol. 66:840-857.
    • (2007) Mol. Microbiol. , vol.66 , pp. 840-857
    • Genevaux, P.1    Georgopoulos, C.2    Kelley, W.L.3
  • 88
    • 0034674728 scopus 로고    scopus 로고
    • Premature structural changes at replication origins in a yeast minichromosome maintenance (MCM) mutant
    • Geraghty, D. S., M. Ding, N. H. Heintz, and D. S. Pederson. 2000. Premature structural changes at replication origins in a yeast minichromosome maintenance (MCM) mutant. J. Biol. Chem. 275:18011-18021.
    • (2000) J. Biol. Chem. , vol.275 , pp. 18011-18021
    • Geraghty, D.S.1    Ding, M.2    Heintz, N.H.3    Pederson, D.S.4
  • 89
    • 3042852862 scopus 로고    scopus 로고
    • Reconstitution of licensed replication origins on Xenopus sperm nuclei using purified proteins
    • Gillespie, P. J., A. Li, and J. J. Blow. 2001. Reconstitution of licensed replication origins on Xenopus sperm nuclei using purified proteins. BMC Biochem. 2:15.
    • (2001) BMC Biochem. , vol.2 , pp. 15
    • Gillespie, P.J.1    Li, A.2    Blow, J.J.3
  • 90
    • 0036242688 scopus 로고    scopus 로고
    • Different phenotypes in vivo are associated with ATPase motif mutations in Schizosaccharomyces pombe minichromosome maintenance proteins
    • Gomez, E. B., M. G. Catlett, and S. L. Forsburg. 2002. Different phenotypes in vivo are associated with ATPase motif mutations in Schizosaccharomyces pombe minichromosome maintenance proteins. Genetics 160:1305-1318.
    • (2002) Genetics , vol.160 , pp. 1305-1318
    • Gomez, E.B.1    Catlett, M.G.2    Forsburg, S.L.3
  • 91
    • 28844449554 scopus 로고    scopus 로고
    • Polymorphism and double hexamer structure in the archaeal minichromosome maintenance (MCM) helicase from Methanobacterium thermoautotrophicum
    • Gomez-Llorente, Y., R. J. Fletcher, X. S. Chen, J. M. Carazo, and C. San Martin. 2005. Polymorphism and double hexamer structure in the archaeal minichromosome maintenance (MCM) helicase from Methanobacterium thermoautotrophicum. J. Biol. Chem. 280:40909-40915.
    • (2005) J. Biol. Chem. , vol.280 , pp. 40909-40915
    • Gomez-Llorente, Y.1    Fletcher, R.J.2    Chen, X.S.3    Carazo, J.M.4    San Martin, C.5
  • 93
    • 0034868902 scopus 로고    scopus 로고
    • Autophosphorylation of archaeal Cdc6 homologues is regulated by DNA
    • DOI 10.1128/JB.183.18.5459-5464.2001
    • Grabowski, B., and Z. Kelman. 2001. Autophosphorylation of archaeal Cdc6 homologues is regulated by DNA. J. Bacteriol. 183:5459-5464. (Pubitemid 32802623)
    • (2001) Journal of Bacteriology , vol.183 , Issue.18 , pp. 5459-5464
    • Grabowski, B.1    Kelman, Z.2
  • 95
    • 0344012482 scopus 로고    scopus 로고
    • Biochemical analysis of components of the pre-replication complex of Archaeoglobus fulgidus
    • DOI 10.1093/nar/gkg662
    • Grainge, I., S. Scaife, and D. B. Wigley. 2003. Biochemical analysis of components of the pre-replication complex of Archaeoglobus fulgidus. Nucleic Acids Res. 31:4888-4898. (Pubitemid 37441854)
    • (2003) Nucleic Acids Research , vol.31 , Issue.16 , pp. 4888-4898
    • Grainge, I.1    Scaife, S.2    Wigley, D.B.3
  • 98
    • 58149196304 scopus 로고    scopus 로고
    • Biochemical characterization of the minichromosome maintenance protein from the archaeon Thermoplasma acidophilum
    • Haugland, G. T., C. R. Rollor, N. K. Birkeland, and Z. Kelman. 2009. Biochemical characterization of the minichromosome maintenance protein from the archaeon Thermoplasma acidophilum. Extremophiles 13:81-88.
    • (2009) Extremophiles , vol.13 , pp. 81-88
    • Haugland, G.T.1    Rollor, C.R.2    Birkeland, N.K.3    Kelman, Z.4
  • 99
    • 55249100551 scopus 로고    scopus 로고
    • Thermoplasma acidophilum Cdc6 protein stimulates MCM helicase activity by regulating its ATPase activity
    • Haugland, G. T., N. Sakakibara, A. L. Pey, C. R. Rollor, N. K. Birkeland, and Z. Kelman. 2008. Thermoplasma acidophilum Cdc6 protein stimulates MCM helicase activity by regulating its ATPase activity. Nucleic Acids Res. 36:5602-5609.
    • (2008) Nucleic Acids Res. , vol.36 , pp. 5602-5609
    • Haugland, G.T.1    Sakakibara, N.2    Pey, A.L.3    Rollor, C.R.4    Birkeland, N.K.5    Kelman, Z.6
  • 100
    • 33845407668 scopus 로고    scopus 로고
    • Stimulation of MCM helicase activity by a Cdc6 protein in the archaeon Thermoplasma acidophilum
    • Haugland, G. T., J. H. Shin, N. K. Birkeland, and Z. Kelman. 2006. Stimulation of MCM helicase activity by a Cdc6 protein in the archaeon Thermoplasma acidophilum. Nucleic Acids Res. 34:6337-6344.
    • (2006) Nucleic Acids Res. , vol.34 , pp. 6337-6344
    • Haugland, G.T.1    Shin, J.H.2    Birkeland, N.K.3    Kelman, Z.4
  • 101
    • 33845330910 scopus 로고    scopus 로고
    • Replisome assembly and the direct restart of stalled replication forks
    • Heller, R. C., and K. J. Marians. 2006. Replisome assembly and the direct restart of stalled replication forks. Nat. Rev. Mol. Cell Biol. 7:932-943.
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 932-943
    • Heller, R.C.1    Marians, K.J.2
  • 102
    • 0025821897 scopus 로고
    • A group of interacting yeast DNA replication genes
    • Hennessy, K. M., A. Lee, E. Chen, and D. Botstein. 1991. A group of interacting yeast DNA replication genes. Genes Dev. 5:958-969. (Pubitemid 21906010)
    • (1991) Genes and Development , vol.5 , Issue.6 , pp. 958-969
    • Hennessy, K.M.1    Lee, A.2    Chen, E.3    Botstein, D.4
  • 103
    • 0030045742 scopus 로고    scopus 로고
    • Cooperative interactions of nucleotide ligands are linked to oligomerization and DNA binding in bacteriophage T7 gene 4 helicases
    • Hingorani, M. M., and S. S. Patel. 1996. Cooperative interactions of nucleotide ligands are linked to oligomerization and DNA binding in bacteriophage T7 gene 4 helicases. Biochemistry 35:2218-2228.
    • (1996) Biochemistry , vol.35 , pp. 2218-2228
    • Hingorani, M.M.1    Patel, S.S.2
  • 104
    • 0030987298 scopus 로고    scopus 로고
    • The dTTPase mechanism of T7 DNA helicase resembles the binding change mechanism of the F1-ATPase
    • Hingorani, M. M., M. T. Washington, K. C. Moore, and S. S. Patel. 1997. The dTTPase mechanism of T7 DNA helicase resembles the binding change mechanism of the F1-ATPase. Proc. Natl. Acad. Sci. USA 94:5012-5017.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 5012-5017
    • Hingorani, M.M.1    Washington, M.T.2    Moore, K.C.3    Patel, S.S.4
  • 105
    • 0034656366 scopus 로고    scopus 로고
    • Mcm10 and the MCM2-7 complex interact to initiate DNA synthesis and to release replication factors from origins
    • Homesley, L., M. Lei, Y. Kawasaki, S. Sawyer, T. Christensen, and B. K. Tye. 2000. Mcm10 and the MCM2-7 complex interact to initiate DNA synthesis and to release replication factors from origins. Genes Dev. 14:913-926. (Pubitemid 30253001)
    • (2000) Genes and Development , vol.14 , Issue.8 , pp. 913-926
    • Homesley, L.1    Lei, M.2    Kawasaki, Y.3    Sawyer, S.4    Christensen, T.5    Tye, B.K.6
  • 106
    • 0032567761 scopus 로고    scopus 로고
    • Identification of a preinitiation step in DNA replication that is independent of origin recognition complex and cdc6, but dependent on cdk2
    • Hua, X. H., and J. Newport. 1998. Identification of a preinitiation step in DNA replication that is independent of origin recognition complex and cdc6, but dependent on cdk2. J. Cell Biol. 140:271-281.
    • (1998) J. Cell Biol. , vol.140 , pp. 271-281
    • Hua, X.H.1    Newport, J.2
  • 107
    • 48249084972 scopus 로고    scopus 로고
    • Excess MCM proteins protect human cells from replicative stress by licensing backup origins of replication
    • Ibarra, A., E. Schwob, and J. Mendez. 2008. Excess MCM proteins protect human cells from replicative stress by licensing backup origins of replication. Proc. Natl. Acad. Sci. USA 105:8956-8961.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 8956-8961
    • Ibarra, A.1    Schwob, E.2    Mendez, J.3
  • 108
    • 0034669196 scopus 로고    scopus 로고
    • The acidic pin of RuvA modulates Holliday junction binding and processing by the RuvABC resolvasome
    • Ingleston, S. M., G. J. Sharples, and R. G. Lloyd. 2000. The acidic pin of RuvA modulates Holliday junction binding and processing by the RuvABC resolvasome. EMBO J. 19:6266-6274.
    • (2000) EMBO J. , vol.19 , pp. 6266-6274
    • Ingleston, S.M.1    Sharples, G.J.2    Lloyd, R.G.3
  • 109
    • 0030859463 scopus 로고    scopus 로고
    • A DNA helicase activity is associated with an MCM4, -6, and -7 protein complex
    • Ishimi, Y. 1997. A DNA helicase activity is associated with an MCM4, -6, and -7 protein complex. J. Biol. Chem. 272:24508-24513.
    • (1997) J. Biol. Chem. , vol.272 , pp. 24508-24513
    • Ishimi, Y.1
  • 110
    • 0029817835 scopus 로고    scopus 로고
    • Binding of human minichromosome maintenance proteins with histone H3
    • Ishimi, Y., S. Ichinose, A. Omori, K. Sato, and H. Kimura. 1996. Binding of human minichromosome maintenance proteins with histone H3. J. Biol. Chem. 271:24115-24122.
    • (1996) J. Biol. Chem. , vol.271 , pp. 24115-24122
    • Ishimi, Y.1    Ichinose, S.2    Omori, A.3    Sato, K.4    Kimura, H.5
  • 111
    • 0035860801 scopus 로고    scopus 로고
    • Phosphorylation of Mcm4 at specific sites by cyclin-dependent kinase leads to loss of Mcm4,6,7 helicase activity
    • Ishimi, Y., and Y. Komamura-Kohno. 2001. Phosphorylation of Mcm4 at specific sites by cyclin-dependent kinase leads to loss of Mcm4,6,7 helicase activity. J. Biol. Chem. 276:34428-34433.
    • (2001) J. Biol. Chem. , vol.276 , pp. 34428-34433
    • Ishimi, Y.1    Komamura-Kohno, Y.2
  • 112
    • 0043092109 scopus 로고    scopus 로고
    • Identification of MCM4 as a target of the DNA replication block checkpoint system
    • Ishimi, Y., Y. Komamura-Kohno, H. J. Kwon, K. Yamada, and M. Nakanishi. 2003. Identification of MCM4 as a target of the DNA replication block checkpoint system. J. Biol. Chem. 278:24644-24650.
    • (2003) J. Biol. Chem. , vol.278 , pp. 24644-24650
    • Ishimi, Y.1    Komamura-Kohno, Y.2    Kwon, H.J.3    Yamada, K.4    Nakanishi, M.5
  • 113
    • 1642325936 scopus 로고    scopus 로고
    • Evolutionary history and higher order classification of AAA+ ATPases
    • Iyer, L. M., D. D. Leipe, E. V. Koonin, and L. Aravind. 2004. Evolutionary history and higher order classification of AAA+ ATPases. J. Struct. Biol. 146:11-31.
    • (2004) J. Struct. Biol. , vol.146 , pp. 11-31
    • Iyer, L.M.1    Leipe, D.D.2    Koonin, E.V.3    Aravind, L.4
  • 114
    • 34547491445 scopus 로고    scopus 로고
    • The evolutionary history of proteins involved in pre-replication complex assembly
    • M. L. DePamphilis (ed.), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Iyer, L. M., and L. Aravind. 2006. The evolutionary history of proteins involved in pre-replication complex assembly, p. 751-757. In M. L. DePamphilis (ed.), DNA replication and human disease. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (2006) DNA Replication and Human Disease , pp. 751-757
    • Iyer, L.M.1    Aravind, L.2
  • 115
    • 33646754407 scopus 로고    scopus 로고
    • Minichromosome maintenance helicase activity is controlled by N- And C-terminal motifs and requires the ATPase domain helix-2 insert
    • Jenkinson, E. R., and J. P. Chong. 2006. Minichromosome maintenance helicase activity is controlled by N- and C-terminal motifs and requires the ATPase domain helix-2 insert. Proc. Natl. Acad. Sci. USA 103:7613-7618.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 7613-7618
    • Jenkinson, E.R.1    Chong, J.P.2
  • 116
    • 0035943342 scopus 로고    scopus 로고
    • Crystal structure of the processivity clamp loader gamma (γ) complex of E. coli DNA polymerase III
    • DOI 10.1016/S0092-8674(01)00463-9
    • Jeruzalmi, D., M. O'Donnell, and J. Kuriyan. 2001. Crystal structure of the processivity clamp loader gamma (gamma) complex of E. coli DNA polymerase III. Cell 106:429-441. (Pubitemid 32786987)
    • (2001) Cell , vol.106 , Issue.4 , pp. 429-441
    • Jeruzalmi, D.1    O'Donnell, M.2    Kuriyan, J.3
  • 117
    • 34547725203 scopus 로고    scopus 로고
    • Divergent functions of multiple eukaryote-like Orc1/Cdc6 proteins on modulating the loading of the MCM helicase onto the origins of the hyperthermophilic archaeon Sulfolobus solfataricus P2
    • Jiang, P. X., J. Wang, Y. Feng, and Z. G. He. 2007. Divergent functions of multiple eukaryote-like Orc1/Cdc6 proteins on modulating the loading of the MCM helicase onto the origins of the hyperthermophilic archaeon Sulfolobus solfataricus P2. Biochem. Biophys. Res. Commun. 361:651-658.
    • (2007) Biochem. Biophys. Res. Commun. , vol.361 , pp. 651-658
    • Jiang, P.X.1    Wang, J.2    Feng, Y.3    He, Z.G.4
  • 118
    • 0038606975 scopus 로고    scopus 로고
    • A new member of the MCM protein family encoded by the human MCM8 gene, located contrapodal to GCD10 at chromosome band 20p12.3-13
    • Johnson, E. M., Y. Kinoshita, and D. C. Daniel. 2003. A new member of the MCM protein family encoded by the human MCM8 gene, located contrapodal to GCD10 at chromosome band 20p12.3-13. Nucleic Acids Res. 31:2915-2925.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 2915-2925
    • Johnson, E.M.1    Kinoshita, Y.2    Daniel, D.C.3
  • 119
    • 34247629049 scopus 로고    scopus 로고
    • Structure of the human GINS complex and its assembly and functional interface in replication initiation
    • Kamada, K., Y. Kubota, T. Arata, Y. Shindo, and F. Hanaoka. 2007. Structure of the human GINS complex and its assembly and functional interface in replication initiation. Nat. Struct. Mol. Biol. 14:388-396.
    • (2007) Nat. Struct. Mol. Biol. , vol.14 , pp. 388-396
    • Kamada, K.1    Kubota, Y.2    Arata, T.3    Shindo, Y.4    Hanaoka, F.5
  • 120
    • 0035901555 scopus 로고    scopus 로고
    • Sld3, which interacts with Cdc45 (Sld4), functions for chromosomal DNA replication in saccharomyces cerevisiae
    • DOI 10.1093/emboj/20.8.2097
    • Kamimura, Y., Y. S. Tak, A. Sugino, and H. Araki. 2001. Sld3, which interacts with Cdc45 (Sld4), functions for chromosomal DNA replication in Saccharomyces cerevisiae. EMBO J. 20:2097-2107. (Pubitemid 32397411)
    • (2001) EMBO Journal , vol.20 , Issue.8 , pp. 2097-2107
    • Kamimura, Y.1    Tak, Y.-S.2    Sugino, A.3    Araki, H.4
  • 121
    • 57649171240 scopus 로고    scopus 로고
    • Mcm subunits can assemble into two different active unwinding complexes
    • Kanter, D. M., I. Bruck, and D. L. Kaplan. 2008. Mcm subunits can assemble into two different active unwinding complexes. J. Biol. Chem. 283:31172-31182.
    • (2008) J. Biol. Chem. , vol.283 , pp. 31172-31182
    • Kanter, D.M.1    Bruck, I.2    Kaplan, D.L.3
  • 122
    • 0347157844 scopus 로고    scopus 로고
    • Mcm4,6,7 uses a "pump in ring" mechanism to unwind DNA by steric exclusion and actively translocate along a duplex
    • Kaplan, D. L., M. J. Davey, and M. O'Donnell. 2003. Mcm4,6,7 uses a "pump in ring" mechanism to unwind DNA by steric exclusion and actively translocate along a duplex. J. Biol. Chem. 278:49171-49182.
    • (2003) J. Biol. Chem. , vol.278 , pp. 49171-49182
    • Kaplan, D.L.1    Davey, M.J.2    O'Donnell, M.3
  • 123
    • 0036753338 scopus 로고    scopus 로고
    • DnaB drives DNA branch migration and dislodges proteins while encircling two DNA strands
    • Kaplan, D. L., and M. O'Donnell. 2002. DnaB drives DNA branch migration and dislodges proteins while encircling two DNA strands. Mol. Cell 10:647-657.
    • (2002) Mol. Cell , vol.10 , pp. 647-657
    • Kaplan, D.L.1    O'Donnell, M.2
  • 124
    • 4143151757 scopus 로고    scopus 로고
    • Twin DNA pumps of a hexameric helicase provide power to simultaneously melt two duplexes
    • Kaplan, D. L., and M. O'Donnell. 2004. Twin DNA pumps of a hexameric helicase provide power to simultaneously melt two duplexes. Mol. Cell 15:453-465.
    • (2004) Mol. Cell , vol.15 , pp. 453-465
    • Kaplan, D.L.1    O'Donnell, M.2
  • 125
    • 3142618515 scopus 로고    scopus 로고
    • Biochemical characterization of the Methanothermobacter thermautotrophicus minichromosome maintenance (MCM) helicase N-terminal domains
    • Kasiviswanathan, R., J. H. Shin, E. Melamud, and Z. Kelman. 2004. Biochemical characterization of the Methanothermobacter thermautotrophicus minichromosome maintenance (MCM) helicase N-terminal domains. J. Biol. Chem. 279:28358-28366.
    • (2004) J. Biol. Chem. , vol.279 , pp. 28358-28366
    • Kasiviswanathan, R.1    Shin, J.H.2    Melamud, E.3    Kelman, Z.4
  • 126
    • 0042865938 scopus 로고    scopus 로고
    • S-phase checkpoint proteins Tof1 and Mrc1 form a stable replication-pausing complex
    • DOI 10.1038/nature01900
    • Katou, Y., Y. Kanoh, M. Bando, H. Noguchi, H. Tanaka, T. Ashikari, K. Sugimoto, and K. Shirahige. 2003. S-phase checkpoint proteins Tof1 and Mrc1 form a stable replication-pausing complex. Nature 424:1078-1083. (Pubitemid 37064311)
    • (2003) Nature , vol.424 , Issue.6952 , pp. 1078-1083
    • Katou, Y.1    Kanoh, Y.2    Bando, M.3    Noguchi, H.4    Tanaka, H.5    Ashikari, T.6    Sugimoto, K.7    Shirahige, K.8
  • 127
    • 0035981231 scopus 로고    scopus 로고
    • Yeast Replicative DNA Polymerases and Their Role at the Replication Fork
    • Kawasaki, Y., and A. Sugino. 2001. Yeast replicative DNA polymerases and their role at the replication fork. Mol. Cells 12:277-285. (Pubitemid 33666007)
    • (2001) Molecules and Cells , vol.12 , Issue.3 , pp. 277-285
    • Kawasaki, Y.1    Sugino, A.2
  • 128
    • 0038687925 scopus 로고    scopus 로고
    • Archaea: An archetype for replication initiation studies?
    • Kelman, L. M., and Z. Kelman. 2003. Archaea: an archetype for replication initiation studies? Mol. Microbiol. 48:605-615.
    • (2003) Mol. Microbiol. , vol.48 , pp. 605-615
    • Kelman, L.M.1    Kelman, Z.2
  • 129
    • 0033593053 scopus 로고    scopus 로고
    • The single minichromosome maintenance protein of Methanobacterium thermoautotrophicum DeltaH contains DNA helicase activity
    • Kelman, Z., J. K. Lee, and J. Hurwitz. 1999. The single minichromosome maintenance protein of Methanobacterium thermoautotrophicum DeltaH contains DNA helicase activity. Proc. Natl. Acad. Sci. USA 96:14783-14788.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 14783-14788
    • Kelman, Z.1    Lee, J.K.2    Hurwitz, J.3
  • 130
    • 27844542206 scopus 로고    scopus 로고
    • Archaeal DNA replication and repair
    • Kelman, Z., and M. F. White. 2005. Archaeal DNA replication and repair. Curr. Opin. Microbiol. 8:669-676.
    • (2005) Curr. Opin. Microbiol. , vol.8 , pp. 669-676
    • Kelman, Z.1    White, M.F.2
  • 131
    • 0030278503 scopus 로고    scopus 로고
    • Mouse MCM proteins: Complex formation and transportation to the nucleus
    • Kimura, H., T. Ohtomo, M. Yamaguchi, A. Ishii, and K. Sugimoto. 1996. Mouse MCM proteins: complex formation and transportation to the nucleus. Genes Cells 1:977-993. (Pubitemid 126670803)
    • (1996) Genes to Cells , vol.1 , Issue.11 , pp. 977-993
    • Kimura, H.1    Ohtomo, T.2    Yamaguchi, M.3    Ishii, A.4    Sugimoto, K.5
  • 132
    • 0020405207 scopus 로고
    • The Escherichia coli dnaC gene product. III. Properties of the dnaB-dnaC protein complex
    • Kobori, J. A., and A. Kornberg. 1982. The Escherichia coli dnaC gene product. III. Properties of the dnaB-dnaC protein complex. J. Biol. Chem. 257:13770-13775.
    • (1982) J. Biol. Chem. , vol.257 , pp. 13770-13775
    • Kobori, J.A.1    Kornberg, A.2
  • 133
    • 33644781968 scopus 로고    scopus 로고
    • Site-specific phosphorylation of MCM4 during the cell cycle in mammalian cells
    • DOI 10.1111/j.1742-4658.2006.05146.x
    • Komamura-Kohno, Y., K. Karasawa-Shimizu, T. Saitoh, M. Sato, F. Hanaoka, S. Tanaka, and Y. Ishimi. 2006. Site-specific phosphorylation of MCM4 during the cell cycle in mammalian cells. FEBS J. 273:1224-1239. (Pubitemid 43345042)
    • (2006) FEBS Journal , vol.273 , Issue.6 , pp. 1224-1239
    • Komamura-Kohno, Y.1    Karasawa-Shimizu, K.2    Saitoh, T.3    Sato, M.4    Hanaoka, F.5    Tanaka, S.6    Ishimi, Y.7
  • 134
    • 70249118531 scopus 로고    scopus 로고
    • The direct binding of Mrc1, a checkpoint mediator, to Mcm6, a replication helicase, is essential for the replication checkpoint against methyl methanesulfonate-induced stress
    • Komata, M., M. Bando, H. Araki, and K. Shirahige. 2009. The direct binding of Mrc1, a checkpoint mediator, to Mcm6, a replication helicase, is essential for the replication checkpoint against methyl methanesulfonate-induced stress. Mol. Cell. Biol. 29:5008-5019.
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 5008-5019
    • Komata, M.1    Bando, M.2    Araki, H.3    Shirahige, K.4
  • 135
    • 0027267908 scopus 로고
    • A common set of conserved motifs in a vast variety of putative nucleic acid-dependent ATPases including MCM proteins involved in the initiation of eukaryotic DNA replication
    • Koonin, E. V. 1993. A common set of conserved motifs in a vast variety of putative nucleic acid-dependent ATPases including MCM proteins involved in the initiation of eukaryotic DNA replication. Nucleic Acids Res. 21:2541-2547.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 2541-2547
    • Koonin, E.V.1
  • 137
    • 0037510025 scopus 로고    scopus 로고
    • A novel ring-like complex of Xenopus proteins essential for the initiation of DNA replication
    • DOI 10.1101/gad.1070003
    • Kubota, Y., Y. Takase, Y. Komori, Y. Hashimoto, T. Arata, Y. Kamimura, H. Araki, and H. Takisawa. 2003. A novel ring-like complex of Xenopus proteins essential for the initiation of DNA replication. Genes Dev. 17:1141-1152. (Pubitemid 36534988)
    • (2003) Genes and Development , vol.17 , Issue.9 , pp. 1141-1152
    • Kubota, Y.1    Takase, Y.2    Komori, Y.3    Hashimoto, Y.4    Arata, T.5    Kamimura, Y.6    Araki, H.7    Takisawa, H.8
  • 138
    • 33749463157 scopus 로고    scopus 로고
    • Phosphorylation of MCM4 at sites inactivating DNA helicase activity of the MCM4-MCM6-MCM7 complex during Epstein-Barr virus productive replication
    • DOI 10.1128/JVI.00678-06
    • Kudoh, A., T. Daikoku, Y. Ishimi, Y. Kawaguchi, N. Shirata, S. Iwahori, H. Isomura, and T. Tsurumi. 2006. Phosphorylation of MCM4 at sites inactivating DNA helicase activity of the MCM4-MCM6-MCM7 complex during Epstein-Barr virus productive replication. J. Virol. 80:10064-10072. (Pubitemid 44522600)
    • (2006) Journal of Virology , vol.80 , Issue.20 , pp. 10064-10072
    • Kudoh, A.1    Daikoku, T.2    Ishimi, Y.3    Kawaguchi, Y.4    Shirata, N.5    Iwahori, S.6    Isomura, H.7    Tsurumi, T.8
  • 139
    • 0033224310 scopus 로고    scopus 로고
    • G1-phase and B-type cyclins exclude the DNA-replication factor Mcm4 from the nucleus
    • Labib, K., J. F. Diffley, and S. E. Kearsey. 1999. G1-phase and B-type cyclins exclude the DNA-replication factor Mcm4 from the nucleus. Nat. Cell Biol. 1:415-422.
    • (1999) Nat. Cell Biol. , vol.1 , pp. 415-422
    • Labib, K.1    Diffley, J.F.2    Kearsey, S.E.3
  • 140
    • 0034595448 scopus 로고    scopus 로고
    • Uninterrupted MCM2-7 function required for DNA replication fork progression
    • Labib, K., J. A. Tercero, and J. F. Diffley. 2000. Uninterrupted MCM2-7 function required for DNA replication fork progression. Science 288:1643-1647.
    • (2000) Science , vol.288 , pp. 1643-1647
    • Labib, K.1    Tercero, J.A.2    Diffley, J.F.3
  • 142
    • 0037219192 scopus 로고    scopus 로고
    • A rotary pumping model for helicase function of MCM proteins at a distance from replication forks
    • Laskey, R. A., and M. A. Madine. 2003. A rotary pumping model for helicase function of MCM proteins at a distance from replication forks. EMBO Rep. 4:26-30.
    • (2003) EMBO Rep. , vol.4 , pp. 26-30
    • Laskey, R.A.1    Madine, M.A.2
  • 143
    • 0034282727 scopus 로고    scopus 로고
    • Regulation of origin recognition complex conformation and ATPase activity: Differential effects of single-stranded and double-stranded DNA binding
    • Lee, D. G., A. M. Makhov, R. D. Klemm, J. D. Griffith, and S. P. Bell. 2000. Regulation of origin recognition complex conformation and ATPase activity: differential effects of single-stranded and double-stranded DNA binding. EMBO J. 19:4774-4782.
    • (2000) EMBO J. , vol.19 , pp. 4774-4782
    • Lee, D.G.1    Makhov, A.M.2    Klemm, R.D.3    Griffith, J.D.4    Bell, S.P.5
  • 144
    • 0034705520 scopus 로고    scopus 로고
    • Isolation and characterization of various complexes of the minichromosome maintenance proteins of Schizosaccharomyces pombe
    • Lee, J. K., and J. Hurwitz. 2000. Isolation and characterization of various complexes of the minichromosome maintenance proteins of Schizosaccharomyces pombe. J. Biol. Chem. 275:18871-18878.
    • (2000) J. Biol. Chem. , vol.275 , pp. 18871-18878
    • Lee, J.K.1    Hurwitz, J.2
  • 145
    • 0035793113 scopus 로고    scopus 로고
    • Processive DNA helicase activity of the minichromosome maintenance proteins 4, 6, and 7 complex requires forked DNA structures
    • Lee, J. K., and J. Hurwitz. 2001. Processive DNA helicase activity of the minichromosome maintenance proteins 4, 6, and 7 complex requires forked DNA structures. Proc. Natl. Acad. Sci. USA 98:54-59.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 54-59
    • Lee, J.K.1    Hurwitz, J.2
  • 146
    • 0031435940 scopus 로고    scopus 로고
    • Mcm2 is a target of regulation by Cdc7-Dbf4 during the initiation of DNA synthesis
    • Lei, M., Y. Kawasaki, M. R. Young, M. Kihara, A. Sugino, and B. K. Tye. 1997. Mcm2 is a target of regulation by Cdc7-Dbf4 during the initiation of DNA synthesis. Genes Dev. 11:3365-3374.
    • (1997) Genes Dev. , vol.11 , pp. 3365-3374
    • Lei, M.1    Kawasaki, Y.2    Young, M.R.3    Kihara, M.4    Sugino, A.5    Tye, B.K.6
  • 147
    • 0023219316 scopus 로고
    • Replacement of potassium chloride by potassium glutamate dramatically enhances protein-DNA interactions in vitro
    • Leirmo, S., C. Harrison, D. S. Cayley, R. R. Burgess, and M. T. Record, Jr. 1987. Replacement of potassium chloride by potassium glutamate dramatically enhances protein-DNA interactions in vitro. Biochemistry 26:2095-2101.
    • (1987) Biochemistry , vol.26 , pp. 2095-2101
    • Leirmo, S.1    Harrison, C.2    Cayley, D.S.3    Burgess, R.R.4    Record Jr., M.T.5
  • 148
    • 55749083888 scopus 로고    scopus 로고
    • Functional conservation of beta-hairpin DNA binding domains in the Mcm protein of Methanobacterium thermoautotrophicum and the Mcm5 protein of Saccharomyces cerevisiae
    • Leon, R. P., M. Tecklenburg, and R. A. Sclafani. 2008. Functional conservation of beta-hairpin DNA binding domains in the Mcm protein of Methanobacterium thermoautotrophicum and the Mcm5 protein of Saccharomyces cerevisiae. Genetics 179:1757-1768.
    • (2008) Genetics , vol.179 , pp. 1757-1768
    • Leon, R.P.1    Tecklenburg, M.2    Sclafani, R.A.3
  • 150
    • 26244435980 scopus 로고    scopus 로고
    • CDK phosphorylation of a novel NLS-NES module distributed between two subunits of the Mcm2-7 complex prevents chromosomal rereplication
    • Liku, M. E., V. Q. Nguyen, A. W. Rosales, K. Irie, and J. J. Li. 2005. CDK phosphorylation of a novel NLS-NES module distributed between two subunits of the Mcm2-7 complex prevents chromosomal rereplication. Mol. Biol. Cell 16:5026-5039.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 5026-5039
    • Liku, M.E.1    Nguyen, V.Q.2    Rosales, A.W.3    Irie, K.4    Li, J.J.5
  • 151
    • 45849094037 scopus 로고    scopus 로고
    • Phosphorylation of MCM3 on Ser-112 regulates its incorporation into the MCM2-7 complex
    • Lin, D. I., P. Aggarwal, and J. A. Diehl. 2008. Phosphorylation of MCM3 on Ser-112 regulates its incorporation into the MCM2-7 complex. Proc. Natl. Acad. Sci. USA 105:8079-8084.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 8079-8084
    • Lin, D.I.1    Aggarwal, P.2    Diehl, J.A.3
  • 152
    • 0033634866 scopus 로고    scopus 로고
    • Structure and function of Cdc6/Cdc18: Implications for origin recognition and checkpoint control
    • Liu, J., C. L. Smith, D. DeRyckere, K. DeAngelis, G. S. Martin, and J. M. Berger. 2000. Structure and function of Cdc6/Cdc18: implications for origin recognition and checkpoint control. Mol. Cell 6:637-648.
    • (2000) Mol. Cell , vol.6 , pp. 637-648
    • Liu, J.1    Smith, C.L.2    Deryckere, D.3    Deangelis, K.4    Martin, G.S.5    Berger, J.M.6
  • 153
    • 45549086385 scopus 로고    scopus 로고
    • Structural analysis of the Sulfolobus solfataricus MCM protein N-terminal domain
    • Liu, W., B. Pucci, M. Rossi, F. M. Pisani, and R. Ladenstein. 2008. Structural analysis of the Sulfolobus solfataricus MCM protein N-terminal domain. Nucleic Acids Res. 36:3235-3243.
    • (2008) Nucleic Acids Res. , vol.36 , pp. 3235-3243
    • Liu, W.1    Pucci, B.2    Rossi, M.3    Pisani, F.M.4    Ladenstein, R.5
  • 154
    • 33947251128 scopus 로고    scopus 로고
    • Adjacent residues in the E1 initiator beta-hairpin define different roles of the beta-hairpin in Ori melting, helicase loading, and helicase activity
    • Liu, X., S. Schuck, and A. Stenlund. 2007. Adjacent residues in the E1 initiator beta-hairpin define different roles of the beta-hairpin in Ori melting, helicase loading, and helicase activity. Mol. Cell 25:825-837.
    • (2007) Mol. Cell , vol.25 , pp. 825-837
    • Liu, X.1    Schuck, S.2    Stenlund, A.3
  • 155
    • 64549101067 scopus 로고    scopus 로고
    • Ancient diversification of eukaryotic MCM DNA replication proteins
    • Liu, Y., T. A. Richards, and S. J. Aves. 2009. Ancient diversification of eukaryotic MCM DNA replication proteins. BMC Evol. Biol. 9:60.
    • (2009) BMC Evol. Biol. , vol.9 , pp. 60
    • Liu, Y.1    Richards, T.A.2    Aves, S.J.3
  • 157
    • 53149135030 scopus 로고    scopus 로고
    • Mrc1 and DNA polymerase epsilon function together in linking DNA replication and the S phase checkpoint
    • Lou, H., M. Komata, Y. Katou, Z. Guan, C. C. Reis, M. Budd, K. Shirahige, and J. L. Campbell. 2008. Mrc1 and DNA polymerase epsilon function together in linking DNA replication and the S phase checkpoint. Mol. Cell 32:106-117.
    • (2008) Mol. Cell , vol.32 , pp. 106-117
    • Lou, H.1    Komata, M.2    Katou, Y.3    Guan, Z.4    Reis, C.C.5    Budd, M.6    Shirahige, K.7    Campbell, J.L.8
  • 158
    • 47349113682 scopus 로고    scopus 로고
    • MCM9 binds Cdt1 and is required for the assembly of prereplication complexes
    • Lutzmann, M., and M. Mechali. 2008. MCM9 binds Cdt1 and is required for the assembly of prereplication complexes. Mol. Cell 31:190-200.
    • (2008) Mol. Cell , vol.31 , pp. 190-200
    • Lutzmann, M.1    Mechali, M.2
  • 159
    • 59749096849 scopus 로고    scopus 로고
    • The haloarchaeal chromosome replication machinery
    • MacNeill, S. A. 2009. The haloarchaeal chromosome replication machinery. Biochem. Soc. Trans. 37:108-113.
    • (2009) Biochem. Soc. Trans. , vol.37 , pp. 108-113
    • MacNeill, S.A.1
  • 160
    • 0029036901 scopus 로고
    • MCM3 complex required for cell cycle regulation of DNA replication in vertebrate cells
    • Madine, M. A., C. Y. Khoo, A. D. Mills, and R. A. Laskey. 1995. MCM3 complex required for cell cycle regulation of DNA replication in vertebrate cells. Nature 375:421-424.
    • (1995) Nature , vol.375 , pp. 421-424
    • Madine, M.A.1    Khoo, C.Y.2    Mills, A.D.3    Laskey, R.A.4
  • 161
    • 0021342031 scopus 로고
    • Mutants of S. cerevisiae defective in the maintenance of minichromosomes
    • Maine, G. T., P. Sinha, and B. K. Tye. 1984. Mutants of S. cerevisiae defective in the maintenance of minichromosomes. Genetics 106:365-385.
    • (1984) Genetics , vol.106 , pp. 365-385
    • Maine, G.T.1    Sinha, P.2    Tye, B.K.3
  • 162
    • 13544252547 scopus 로고    scopus 로고
    • MCM8 is an MCM2-7-related protein that functions as a DNA helicase during replication elongation and not initiation
    • Maiorano, D., O. Cuvier, E. Danis, and M. Mechali. 2005. MCM8 is an MCM2-7-related protein that functions as a DNA helicase during replication elongation and not initiation. Cell 120:315-328.
    • (2005) Cell , vol.120 , pp. 315-328
    • Maiorano, D.1    Cuvier, O.2    Danis, E.3    Mechali, M.4
  • 165
    • 33645094195 scopus 로고    scopus 로고
    • Influence of chromatin and single strand binding proteins on the activity of an archaeal MCM
    • Marsh, V. L., A. T. McGeoch, and S. D. Bell. 2006. Influence of chromatin and single strand binding proteins on the activity of an archaeal MCM. J. Mol. Biol. 357:1345-1350.
    • (2006) J. Mol. Biol. , vol.357 , pp. 1345-1350
    • Marsh, V.L.1    McGeoch, A.T.2    Bell, S.D.3
  • 166
    • 27144474906 scopus 로고    scopus 로고
    • Rebuilt AAA+ motors reveal operating principles for ATP-fuelled machines
    • Martin, A., T. A. Baker, and R. T. Sauer. 2005. Rebuilt AAA+ motors reveal operating principles for ATP-fuelled machines. Nature 437:1115-1120.
    • (2005) Nature , vol.437 , pp. 1115-1120
    • Martin, A.1    Baker, T.A.2    Sauer, R.T.3
  • 167
    • 0034683026 scopus 로고    scopus 로고
    • Dbf4 motifs: Conserved motifs in activation subunits for Cdc7 kinases essential for S-phase
    • Masai, H., and K. Arai. 2000. Dbf4 motifs: conserved motifs in activation subunits for Cdc7 kinases essential for S-phase. Biochem. Biophys. Res. Commun. 275:228-232.
    • (2000) Biochem. Biophys. Res. Commun. , vol.275 , pp. 228-232
    • Masai, H.1    Arai, K.2
  • 169
    • 21344442139 scopus 로고    scopus 로고
    • Control of DNA replication: Regulation and activation of eukaryotic replicative helicase, MCM
    • Masai, H., Z. You, and K. Arai. 2005. Control of DNA replication: regulation and activation of eukaryotic replicative helicase, MCM. IUBMB Life 57:323-335.
    • (2005) IUBMB Life , vol.57 , pp. 323-335
    • Masai, H.1    You, Z.2    Arai, K.3
  • 170
    • 0037323011 scopus 로고    scopus 로고
    • CDK- and Cdc45-dependent priming of the MCM complex on chromatin during S-phase in Xenopus egg extracts: Possible activation of MCM helicase by association with Cdc45
    • Masuda, T., S. Mimura, and H. Takisawa. 2003. CDK- and Cdc45-dependent priming of the MCM complex on chromatin during S-phase in Xenopus egg extracts: possible activation of MCM helicase by association with Cdc45. Genes Cells 8:145-161.
    • (2003) Genes Cells , vol.8 , pp. 145-161
    • Masuda, T.1    Mimura, S.2    Takisawa, H.3
  • 171
    • 0034028908 scopus 로고    scopus 로고
    • Dpb11 controls the association between DNA polymerases alpha and epsilon and the autonomously replicating sequence region of budding yeast
    • Masumoto, H., A. Sugino, and H. Araki. 2000. Dpb11 controls the association between DNA polymerases alpha and epsilon and the autonomously replicating sequence region of budding yeast. Mol. Cell. Biol. 20:2809-2817.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 2809-2817
    • Masumoto, H.1    Sugino, A.2    Araki, H.3
  • 172
    • 33846007717 scopus 로고    scopus 로고
    • Crystal structure of the human AAA+ protein RuvBL1
    • Matias, P. M., S. Gorynia, P. Donner, and M. A. Carrondo. 2006. Crystal structure of the human AAA+ protein RuvBL1. J. Biol. Chem. 281:38918-38929.
    • (2006) J. Biol. Chem. , vol.281 , pp. 38918-38929
    • Matias, P.M.1    Gorynia, S.2    Donner, P.3    Carrondo, M.A.4
  • 173
    • 12944319325 scopus 로고    scopus 로고
    • Eukaryotic/archaeal primase and MCM proteins encoded in a bacteriophage genome
    • McGeoch, A. T., and S. D. Bell. 2005. Eukaryotic/archaeal primase and MCM proteins encoded in a bacteriophage genome. Cell 120:167-168.
    • (2005) Cell , vol.120 , pp. 167-168
    • McGeoch, A.T.1    Bell, S.D.2
  • 174
    • 26944435616 scopus 로고    scopus 로고
    • Organization of the archaeal MCM complex on DNA and implications for the helicase mechanism
    • McGeoch, A. T., M. A. Trakselis, R. A. Laskey, and S. D. Bell. 2005. Organization of the archaeal MCM complex on DNA and implications for the helicase mechanism. Nat. Struct. Mol. Biol. 12:756-762.
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 756-762
    • McGeoch, A.T.1    Trakselis, M.A.2    Laskey, R.A.3    Bell, S.D.4
  • 175
    • 33646193384 scopus 로고    scopus 로고
    • Crystal structure of the simian virus 40 large T-antigen origin-binding domain
    • Meinke, G., P. A. Bullock, and A. Bohm. 2006. Crystal structure of the simian virus 40 large T-antigen origin-binding domain. J. Virol. 80:4304-4312.
    • (2006) J. Virol. , vol.80 , pp. 4304-4312
    • Meinke, G.1    Bullock, P.A.2    Bohm, A.3
  • 177
    • 0030974160 scopus 로고    scopus 로고
    • A lesion in the DNA replication initiation factor Mcm10 induces pausing of elongation forks through chromosomal replication origins in Saccharomyces cerevisiae
    • Merchant, A. M., Y. Kawasaki, Y. Chen, M. Lei, and B. K. Tye. 1997. A lesion in the DNA replication initiation factor Mcm10 induces pausing of elongation forks through chromosomal replication origins in Saccharomyces cerevisiae. Mol. Cell. Biol. 17:3261-3271.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 3261-3271
    • Merchant, A.M.1    Kawasaki, Y.2    Chen, Y.3    Lei, M.4    Tye, B.K.5
  • 178
    • 0020120095 scopus 로고
    • Cold-sensitive cell-division-cycle mutants of yeast: Isolation, properties, and pseudoreversion studies
    • Moir, D., S. E. Stewart, B. C. Osmond, and D. Botstein. 1982. Cold-sensitive cell-division-cycle mutants of yeast: isolation, properties, and pseudoreversion studies. Genetics 100:547-563.
    • (1982) Genetics , vol.100 , pp. 547-563
    • Moir, D.1    Stewart, S.E.2    Osmond, B.C.3    Botstein, D.4
  • 180
    • 35348971984 scopus 로고    scopus 로고
    • ATPase site architecture and helicase mechanism of an archaeal MCM
    • Moreau, M. J., A. T. McGeoch, A. R. Lowe, L. S. Itzhaki, and S. D. Bell. 2007. ATPase site architecture and helicase mechanism of an archaeal MCM. Mol. Cell 28:304-314.
    • (2007) Mol. Cell , vol.28 , pp. 304-314
    • Moreau, M.J.1    McGeoch, A.T.2    Lowe, A.R.3    Itzhaki, L.S.4    Bell, S.D.5
  • 181
    • 36749051222 scopus 로고    scopus 로고
    • Regulatory evolution in proteins by turnover and lineage-specific changes of cyclin-dependent kinase consensus sites
    • Moses, A. M., M. E. Liku, J. J. Li, and R. Durbin. 2007. Regulatory evolution in proteins by turnover and lineage-specific changes of cyclin-dependent kinase consensus sites. Proc. Natl. Acad. Sci. USA 104:17713-17718.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 17713-17718
    • Moses, A.M.1    Liku, M.E.2    Li, J.J.3    Durbin, R.4
  • 182
    • 34247271405 scopus 로고    scopus 로고
    • DNA replication initiation: Mechanisms and regulation in bacteria
    • Mott, M. L., and J. M. Berger. 2007. DNA replication initiation: mechanisms and regulation in bacteria. Nat. Rev. Microbiol. 5:343-354.
    • (2007) Nat. Rev. Microbiol. , vol.5 , pp. 343-354
    • Mott, M.L.1    Berger, J.M.2
  • 183
    • 55649098814 scopus 로고    scopus 로고
    • Structural synergy and molecular crosstalk between bacterial helicase loaders and replication initiators
    • Mott, M. L., J. P. Erzberger, M. M. Coons, and J. M. Berger. 2008. Structural synergy and molecular crosstalk between bacterial helicase loaders and replication initiators. Cell 135:623-634.
    • (2008) Cell , vol.135 , pp. 623-634
    • Mott, M.L.1    Erzberger, J.P.2    Coons, M.M.3    Berger, J.M.4
  • 184
    • 33745925880 scopus 로고    scopus 로고
    • Isolation of the Cdc45/Mcm2-7/GINS (CMG) complex, a candidate for the eukaryotic DNA replication fork helicase
    • Moyer, S. E., P. W. Lewis, and M. R. Botchan. 2006. Isolation of the Cdc45/Mcm2-7/GINS (CMG) complex, a candidate for the eukaryotic DNA replication fork helicase. Proc. Natl. Acad. Sci. USA 103:10236-10241.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 10236-10241
    • Moyer, S.E.1    Lewis, P.W.2    Botchan, M.R.3
  • 185
    • 0029053298 scopus 로고
    • A human homologue of the yeast replication protein Cdc21. Interactions with other Mcm proteins
    • Musahl, C., D. Schulte, R. Burkhart, and R. Knippers. 1995. A human homologue of the yeast replication protein Cdc21. Interactions with other Mcm proteins. Eur. J. Biochem. 230:1096-1101.
    • (1995) Eur. J. Biochem. , vol.230 , pp. 1096-1101
    • Musahl, C.1    Schulte, D.2    Burkhart, R.3    Knippers, R.4
  • 186
  • 187
    • 0027443434 scopus 로고
    • The structure and function of yeast ARS elements
    • Newlon, C. S., and J. F. Theis. 1993. The structure and function of yeast ARS elements. Curr. Opin. Genet. Dev. 3:752-758.
    • (1993) Curr. Opin. Genet. Dev. , vol.3 , pp. 752-758
    • Newlon, C.S.1    Theis, J.F.2
  • 188
    • 0034708063 scopus 로고    scopus 로고
    • Clb/Cdc28 kinases promote nuclear export of the replication initiator proteins Mcm2-7
    • Nguyen, V. Q., C. Co, K. Irie, and J. J. Li. 2000. Clb/Cdc28 kinases promote nuclear export of the replication initiator proteins Mcm2-7. Curr. Biol. 10:195-205.
    • (2000) Curr. Biol. , vol.10 , pp. 195-205
    • Nguyen, V.Q.1    Co, C.2    Irie, K.3    Li, J.J.4
  • 189
    • 0035963372 scopus 로고    scopus 로고
    • Cyclin-dependent kinases prevent DNA re-replication through multiple mechanisms
    • Nguyen, V. Q., C. Co, and J. J. Li. 2001. Cyclin-dependent kinases prevent DNA re-replication through multiple mechanisms. Nature 411:1068-1073.
    • (2001) Nature , vol.411 , pp. 1068-1073
    • Nguyen, V.Q.1    Co, C.2    Li, J.J.3
  • 190
    • 0342368778 scopus 로고    scopus 로고
    • Hierarchy of S-phase-promoting factors: Yeast Dbf4-Cdc7 kinase requires prior S-phase cyclin-dependent kinase activation
    • Nougarede, R., F. Della Seta, P. Zarzov, and E. Schwob. 2000. Hierarchy of S-phase-promoting factors: yeast Dbf4-Cdc7 kinase requires prior S-phase cyclin-dependent kinase activation. Mol. Cell. Biol. 20:3795-3806.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 3795-3806
    • Nougarede, R.1    Della Seta, F.2    Zarzov, P.3    Schwob, E.4
  • 192
    • 32444450705 scopus 로고    scopus 로고
    • Localization of MCM2-7, Cdc45, and GINS to the site of DNA unwinding during eukaryotic DNA replication
    • Pacek, M., A. V. Tutter, Y. Kubota, H. Takisawa, and J. C. Walter. 2006. Localization of MCM2-7, Cdc45, and GINS to the site of DNA unwinding during eukaryotic DNA replication. Mol. Cell 21:581-587.
    • (2006) Mol. Cell , vol.21 , pp. 581-587
    • Pacek, M.1    Tutter, A.V.2    Kubota, Y.3    Takisawa, H.4    Walter, J.C.5
  • 193
    • 0348133607 scopus 로고    scopus 로고
    • Hexameric ring structure of the full-length archaeal MCM protein complex
    • Pape, T., H. Meka, S. Chen, G. Vicentini, M. van Heel, and S. Onesti. 2003. Hexameric ring structure of the full-length archaeal MCM protein complex. EMBO Rep. 4:1079-1083.
    • (2003) EMBO Rep. , vol.4 , pp. 1079-1083
    • Pape, T.1    Meka, H.2    Chen, S.3    Vicentini, G.4    Van Heel, M.5    Onesti, S.6
  • 194
    • 36549076396 scopus 로고    scopus 로고
    • Knockdown of human MCM10 exhibits delayed and incomplete chromosome replication
    • Park, J. H., S. W. Bang, Y. Jeon, S. Kang, and D. S. Hwang. 2008. Knockdown of human MCM10 exhibits delayed and incomplete chromosome replication. Biochem. Biophys. Res. Commun. 365:575-582.
    • (2008) Biochem. Biophys. Res. Commun. , vol.365 , pp. 575-582
    • Park, J.H.1    Bang, S.W.2    Jeon, Y.3    Kang, S.4    Hwang, D.S.5
  • 195
    • 1642307235 scopus 로고    scopus 로고
    • Multiple roles of replication forks in S phase checkpoints: Sensors, effectors and targets
    • Pasero, P., K. Shimada, and B. P. Duncker. 2003. Multiple roles of replication forks in S phase checkpoints: sensors, effectors and targets. Cell Cycle 2:568-572.
    • (2003) Cell Cycle , vol.2 , pp. 568-572
    • Pasero, P.1    Shimada, K.2    Duncker, B.P.3
  • 196
    • 0032760517 scopus 로고    scopus 로고
    • Nuclear localization of Schizosaccharomyces pombe Mcm2/Cdc19p requires MCM complex assembly
    • Pasion, S. G., and S. L. Forsburg. 1999. Nuclear localization of Schizosaccharomyces pombe Mcm2/Cdc19p requires MCM complex assembly. Mol. Biol. Cell 10:4043-4057.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 4043-4057
    • Pasion, S.G.1    Forsburg, S.L.2
  • 197
    • 0033786801 scopus 로고    scopus 로고
    • Structure and function of hexameric helicases
    • Patel, S. S., and K. M. Picha. 2000. Structure and function of hexameric helicases. Annu. Rev. Biochem. 69:651-697.
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 651-697
    • Patel, S.S.1    Picha, K.M.2
  • 198
    • 0029085781 scopus 로고
    • A checkpoint regulates the rate of progression through S phase in S. cerevisiae in response to DNA damage
    • Paulovich, A. G., and L. H. Hartwell. 1995. A checkpoint regulates the rate of progression through S phase in S. cerevisiae in response to DNA damage. Cell 82:841-847.
    • (1995) Cell , vol.82 , pp. 841-847
    • Paulovich, A.G.1    Hartwell, L.H.2
  • 199
    • 0032896662 scopus 로고    scopus 로고
    • MCM21 and MCM22, two novel genes of the yeast Saccharomyces cerevisiae are required for chromosome transmission
    • Poddar, A., N. Roy, and P. Sinha. 1999. MCM21 and MCM22, two novel genes of the yeast Saccharomyces cerevisiae are required for chromosome transmission. Mol. Microbiol. 31:349-360.
    • (1999) Mol. Microbiol. , vol.31 , pp. 349-360
    • Poddar, A.1    Roy, N.2    Sinha, P.3
  • 200
    • 0035965990 scopus 로고    scopus 로고
    • The zinc finger domain of the archaeal minichromosome maintenance protein is required for helicase activity
    • Poplawski, A., B. Grabowski, S. E. Long, and Z. Kelman. 2001. The zinc finger domain of the archaeal minichromosome maintenance protein is required for helicase activity. J. Biol. Chem. 276:49371-49377.
    • (2001) J. Biol. Chem. , vol.276 , pp. 49371-49377
    • Poplawski, A.1    Grabowski, B.2    Long, S.E.3    Kelman, Z.4
  • 201
    • 0034723198 scopus 로고    scopus 로고
    • Sequential MCM/P1 subcomplex assembly is required to form a heterohexamer with replication licensing activity
    • Prokhorova, T. A., and J. J. Blow. 2000. Sequential MCM/P1 subcomplex assembly is required to form a heterohexamer with replication licensing activity. J. Biol. Chem. 275:2491-2498.
    • (2000) J. Biol. Chem. , vol.275 , pp. 2491-2498
    • Prokhorova, T.A.1    Blow, J.J.2
  • 202
    • 63849101707 scopus 로고    scopus 로고
    • Recombination at DNA replication fork barriers is not universal and is differentially regulated by Swi1
    • Pryce, D. W., S. Ramayah, A. Jaendling, and R. J. McFarlane. 2009. Recombination at DNA replication fork barriers is not universal and is differentially regulated by Swi1. Proc. Natl. Acad. Sci. USA 106:4770-4775.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 4770-4775
    • Pryce, D.W.1    Ramayah, S.2    Jaendling, A.3    McFarlane, R.J.4
  • 204
    • 10344252316 scopus 로고    scopus 로고
    • Amino acids of the Sulfolobus solfataricus mini-chromosome maintenance-like DNA helicase involved in DNA binding/remodeling
    • Pucci, B., M. De Felice, M. Rossi, S. Onesti, and F. M. Pisani. 2004. Amino acids of the Sulfolobus solfataricus mini-chromosome maintenance-like DNA helicase involved in DNA binding/remodeling. J. Biol. Chem. 279:49222-49228.
    • (2004) J. Biol. Chem. , vol.279 , pp. 49222-49228
    • Pucci, B.1    De Felice, M.2    Rossi, M.3    Onesti, S.4    Pisani, F.M.5
  • 205
    • 29544435484 scopus 로고    scopus 로고
    • Sequential ATP hydrolysis by Cdc6 and ORC directs loading of the Mcm2-7 helicase
    • Randell, J. C., J. L. Bowers, H. K. Rodriguez, and S. P. Bell. 2006. Sequential ATP hydrolysis by Cdc6 and ORC directs loading of the Mcm2-7 helicase. Mol. Cell 21:29-39.
    • (2006) Mol. Cell , vol.21 , pp. 29-39
    • Randell, J.C.1    Bowers, J.L.2    Rodriguez, H.K.3    Bell, S.P.4
  • 206
    • 1842509904 scopus 로고    scopus 로고
    • DNA topology, not DNA sequence, is a critical determinant for Drosophila ORC-DNA binding
    • DOI 10.1038/sj.emboj.7600077
    • Remus, D., E. L. Beall, and M. R. Botchan. 2004. DNA topology, not DNA sequence, is a critical determinant for Drosophila ORC-DNA binding. EMBO J. 23:897-907. (Pubitemid 38418756)
    • (2004) EMBO Journal , vol.23 , Issue.4 , pp. 897-907
    • Remus, D.1    Beall, E.L.2    Botchan, M.R.3
  • 207
    • 6344284782 scopus 로고    scopus 로고
    • Mcm10 regulates the stability and chromatin association of DNA polymerase-alpha
    • Ricke, R. M., and A. K. Bielinsky. 2004. Mcm10 regulates the stability and chromatin association of DNA polymerase-alpha. Mol. Cell 16:173-185.
    • (2004) Mol. Cell , vol.16 , pp. 173-185
    • Ricke, R.M.1    Bielinsky, A.K.2
  • 209
    • 36348987861 scopus 로고    scopus 로고
    • MCM forked substrate specificity involves dynamic interaction with the 5′-tail
    • Rothenberg, E., M. A. Trakselis, S. D. Bell, and T. Ha. 2007. MCM forked substrate specificity involves dynamic interaction with the 5′-tail. J. Biol. Chem. 282:34229-34234.
    • (2007) J. Biol. Chem. , vol.282 , pp. 34229-34234
    • Rothenberg, E.1    Trakselis, M.A.2    Bell, S.D.3    Ha, T.4
  • 210
    • 0032770221 scopus 로고    scopus 로고
    • Changes in association of the Xenopus origin recognition complex with chromatin on licensing of replication origins
    • Rowles, A., S. Tada, and J. J. Blow. 1999. Changes in association of the Xenopus origin recognition complex with chromatin on licensing of replication origins. J. Cell Sci. 112(Pt. 12):2011-2018. (Pubitemid 29338825)
    • (1999) Journal of Cell Science , vol.112 , Issue.12 , pp. 2011-2018
    • Rowles, A.1    Tada, S.2    Blow, J.J.3
  • 211
    • 0030694361 scopus 로고    scopus 로고
    • The mcm17 mutation of yeast shows a size-dependent segregational defect of a mini-chromosome
    • Roy, N., A. Poddar, A. Lohia, and P. Sinha. 1997. The mcm17 mutation of yeast shows a size-dependent segregational defect of a mini-chromosome. Curr. Genet. 32:182-189.
    • (1997) Curr. Genet. , vol.32 , pp. 182-189
    • Roy, N.1    Poddar, A.2    Lohia, A.3    Sinha, P.4
  • 212
    • 49949083837 scopus 로고    scopus 로고
    • DNA binding to RecD: Role of the 1B domain in SF1B helicase activity
    • Saikrishnan, K., S. P. Griffiths, N. Cook, R. Court, and D. B. Wigley. 2008. DNA binding to RecD: role of the 1B domain in SF1B helicase activity. EMBO J. 27:2222-2229.
    • (2008) EMBO J. , vol.27 , pp. 2222-2229
    • Saikrishnan, K.1    Griffiths, S.P.2    Cook, N.3    Court, R.4    Wigley, D.B.5
  • 213
    • 40249118477 scopus 로고    scopus 로고
    • Coupling of DNA binding and helicase activity is mediated by a conserved loop in the MCM protein
    • DOI 10.1093/nar/gkm1160
    • Sakakibara, N., R. Kasiviswanathan, E. Melamud, M. Han, F. P. Schwarz, and Z. Kelman. 2008. Coupling of DNA binding and helicase activity is mediated by a conserved loop in the MCM protein. Nucleic Acids Res. 36:1309-1320. (Pubitemid 351330946)
    • (2008) Nucleic Acids Research , vol.36 , Issue.4 , pp. 1309-1320
    • Sakakibara, N.1    Kasiviswanathan, R.2    Melamud, E.3    Han, M.4    Schwarz, F.P.5    Kelman, Z.6
  • 215
    • 0016737258 scopus 로고
    • Ten proteins required for conversion of phiX174 single-stranded DNA to duplex form in vitro. Resolution and reconstitution
    • Schekman, R., J. H. Weiner, A. Weiner, and A. Kornberg. 1975. Ten proteins required for conversion of phiX174 single-stranded DNA to duplex form in vitro. Resolution and reconstitution. J. Biol. Chem. 250:5859-5865.
    • (1975) J. Biol. Chem. , vol.250 , pp. 5859-5865
    • Schekman, R.1    Weiner, J.H.2    Weiner, A.3    Kornberg, A.4
  • 216
    • 27644484567 scopus 로고    scopus 로고
    • Assembly of a double hexameric helicase
    • Schuck, S., and A. Stenlund. 2005. Assembly of a double hexameric helicase. Mol. Cell 20:377-389.
    • (2005) Mol. Cell , vol.20 , pp. 377-389
    • Schuck, S.1    Stenlund, A.2
  • 217
    • 0030066302 scopus 로고    scopus 로고
    • Properties of the human nuclear protein p85Mcm. Expression, nuclear localization and interaction with other Mcm proteins
    • Schulte, D., A. Richter, R. Burkhart, C. Musahl, and R. Knippers. 1996. Properties of the human nuclear protein p85Mcm. Expression, nuclear localization and interaction with other Mcm proteins. Eur. J. Biochem. 235:144-151.
    • (1996) Eur. J. Biochem. , vol.235 , pp. 144-151
    • Schulte, D.1    Richter, A.2    Burkhart, R.3    Musahl, C.4    Knippers, R.5
  • 218
    • 0035930346 scopus 로고    scopus 로고
    • Interactions between two catalytically distinct MCM subgroups are essential for coordinated ATP hydrolysis and DNA replication
    • DOI 10.1016/S1097-2765(01)00389-6
    • Schwacha, A., and S. P. Bell. 2001. Interactions between two catalytically distinct MCM subgroups are essential for coordinated ATP hydrolysis and DNA replication. Mol. Cell 8:1093-1104. (Pubitemid 34031811)
    • (2001) Molecular Cell , vol.8 , Issue.5 , pp. 1093-1104
    • Schwacha, A.1    Bell, S.P.2
  • 219
    • 0033947670 scopus 로고    scopus 로고
    • Cdc7p-Dbf4p becomes famous in the cell cycle
    • Sclafani, R. A. 2000. Cdc7p-Dbf4p becomes famous in the cell cycle. J. Cell Sci. 113(Pt. 12):2111-2117.
    • (2000) J. Cell Sci. , vol.113 , Issue.PART 12 , pp. 2111-2117
    • Sclafani, R.A.1
  • 220
    • 0036263094 scopus 로고    scopus 로고
    • The mcm5-bob1 bypass of Cdc7p/Dbf4p in DNA replication depends on both Cdk1-independent and Cdk1-dependent steps in Saccharomyces cerevisiae
    • Sclafani, R. A., M. Tecklenburg, and A. Pierce. 2002. The mcm5-bob1 bypass of Cdc7p/Dbf4p in DNA replication depends on both Cdk1-independent and Cdk1-dependent steps in Saccharomyces cerevisiae. Genetics 161:47-57.
    • (2002) Genetics , vol.161 , pp. 47-57
    • Sclafani, R.A.1    Tecklenburg, M.2    Pierce, A.3
  • 221
    • 0034687677 scopus 로고    scopus 로고
    • Stepwise assembly of initiation proteins at budding yeast replication origins in vitro
    • Seki, T., and J. F. Diffley. 2000. Stepwise assembly of initiation proteins at budding yeast replication origins in vitro. Proc. Natl. Acad. Sci. USA 97:14115-14120.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 14115-14120
    • Seki, T.1    Diffley, J.F.2
  • 222
    • 0034686021 scopus 로고    scopus 로고
    • The intrinsic DNA helicase activity of Methanobacterium thermoautotrophicum delta H minichromosome maintenance protein
    • Shechter, D. F., C. Y. Ying, and J. Gautier. 2000. The intrinsic DNA helicase activity of Methanobacterium thermoautotrophicum delta H minichromosome maintenance protein. J. Biol. Chem. 275:15049-15059.
    • (2000) J. Biol. Chem. , vol.275 , pp. 15049-15059
    • Shechter, D.F.1    Ying, C.Y.2    Gautier, J.3
  • 223
    • 0031869382 scopus 로고    scopus 로고
    • Multiple domains of fission yeast Cdc19p (MCM2) are required for its association with the core MCM complex
    • Sherman, D. A., S. G. Pasion, and S. L. Forsburg. 1998. Multiple domains of fission yeast Cdc19p (MCM2) are required for its association with the core MCM complex. Mol. Biol. Cell 9:1833-1845.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 1833-1845
    • Sherman, D.A.1    Pasion, S.G.2    Forsburg, S.L.3
  • 224
    • 33749075373 scopus 로고    scopus 로고
    • Cdc7-Dbf4 phosphorylates MCM proteins via a docking site-mediated mechanism to promote S phase progression
    • Sheu, Y. J., and B. Stillman. 2006. Cdc7-Dbf4 phosphorylates MCM proteins via a docking site-mediated mechanism to promote S phase progression. Mol. Cell 24:101-113.
    • (2006) Mol. Cell , vol.24 , pp. 101-113
    • Sheu, Y.J.1    Stillman, B.2
  • 226
    • 44349119246 scopus 로고    scopus 로고
    • The Methanothermobacter thermautotrophicus Cdc6-2 protein, the putative helicase loader, dissociates the minichromosome maintenance helicase
    • Shin, J. H., G. Y. Heo, and Z. Kelman. 2008. The Methanothermobacter thermautotrophicus Cdc6-2 protein, the putative helicase loader, dissociates the minichromosome maintenance helicase. J. Bacteriol. 190:4091-4094.
    • (2008) J. Bacteriol. , vol.190 , pp. 4091-4094
    • Shin, J.H.1    Heo, G.Y.2    Kelman, Z.3
  • 227
    • 1542782549 scopus 로고    scopus 로고
    • Substrate requirements for duplex DNA translocation by the eukaryal and archaeal minichromosome maintenance helicases
    • Shin, J. H., Y. Jiang, B. Grabowski, J. Hurwitz, and Z. Kelman. 2003. Substrate requirements for duplex DNA translocation by the eukaryal and archaeal minichromosome maintenance helicases. J. Biol. Chem. 278:49053-49062.
    • (2003) J. Biol. Chem. , vol.278 , pp. 49053-49062
    • Shin, J.H.1    Jiang, Y.2    Grabowski, B.3    Hurwitz, J.4    Kelman, Z.5
  • 228
    • 33748752207 scopus 로고    scopus 로고
    • The replicative helicases of bacteria, archaea and eukarya can unwind RNA-DNA hybrid substrates
    • Shin, J. H., and Z. Kelman. 2006. The replicative helicases of bacteria, archaea and eukarya can unwind RNA-DNA hybrid substrates. J. Biol. Chem. 281:26914-26921.
    • (2006) J. Biol. Chem. , vol.281 , pp. 26914-26921
    • Shin, J.H.1    Kelman, Z.2
  • 229
    • 33947545128 scopus 로고    scopus 로고
    • Archaeal minichromosome maintenance (MCM) helicase can unwind DNA bound by archaeal histones and transcription factors
    • Shin, J. H., T. J. Santangelo, Y. Xie, J. N. Reeve, and Z. Kelman. 2007. Archaeal minichromosome maintenance (MCM) helicase can unwind DNA bound by archaeal histones and transcription factors. J. Biol. Chem. 282:4908-4915.
    • (2007) J. Biol. Chem. , vol.282 , pp. 4908-4915
    • Shin, J.H.1    Santangelo, T.J.2    Xie, Y.3    Reeve, J.N.4    Kelman, Z.5
  • 230
    • 0032942212 scopus 로고    scopus 로고
    • Systematic identification, classification, and characterization of the open reading frames which encode novel helicase-related proteins in Saccharomyces cerevisiae by gene disruption and Northern analysis
    • DOI 10.1002/(SICI)1097-0061(199902)15:3<219::AID-YEA349>3.0.CO;2-3
    • Shiratori, A., T. Shibata, M. Arisawa, F. Hanaoka, Y. Murakami, and T. Eki. 1999. Systematic identification, classification, and characterization of the open reading frames which encode novel helicase-related proteins in Saccharomyces cerevisiae by gene disruption and Northern analysis. Yeast 15:219-253. (Pubitemid 29083957)
    • (1999) Yeast , vol.15 , Issue.3 , pp. 219-253
    • Shiratori, A.1    Shibata, T.2    Arisawa, M.3    Hanaoka, F.4    Murakami, Y.5    Eki, T.6
  • 231
  • 232
    • 34548638261 scopus 로고    scopus 로고
    • Structure and mechanism of helicases and nucleic acid translocases
    • Singleton, M. R., M. S. Dillingham, and D. B. Wigley. 2007. Structure and mechanism of helicases and nucleic acid translocases. Annu. Rev. Biochem. 76:23-50.
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 23-50
    • Singleton, M.R.1    Dillingham, M.S.2    Wigley, D.B.3
  • 233
    • 0034625236 scopus 로고    scopus 로고
    • Crystal structure of T7 gene 4 ring helicase indicates a mechanism for sequential hydrolysis of nucleotides
    • Singleton, M. R., M. R. Sawaya, T. Ellenberger, and D. B. Wigley. 2000. Crystal structure of T7 gene 4 ring helicase indicates a mechanism for sequential hydrolysis of nucleotides. Cell 101:589-600.
    • (2000) Cell , vol.101 , pp. 589-600
    • Singleton, M.R.1    Sawaya, M.R.2    Ellenberger, T.3    Wigley, D.B.4
  • 234
    • 33750477997 scopus 로고    scopus 로고
    • Structural Insights into RNA-Dependent Ring Closure and ATPase Activation by the Rho Termination Factor
    • DOI 10.1016/j.cell.2006.08.051, PII S0092867406012797
    • Skordalakes, E., and J. M. Berger. 2006. Structural insights into RNA-dependent ring closure and ATPase activation by the Rho termination factor. Cell 127:553-564. (Pubitemid 44647425)
    • (2006) Cell , vol.127 , Issue.3 , pp. 553-564
    • Skordalakes, E.1    Berger, J.M.2
  • 235
    • 0037178740 scopus 로고    scopus 로고
    • Fork reversal and ssDNA accumulation at stalled replication forks owing to checkpoint defects
    • Sogo, J. M., M. Lopes, and M. Foiani. 2002. Fork reversal and ssDNA accumulation at stalled replication forks owing to checkpoint defects. Science 297:599-602.
    • (2002) Science , vol.297 , pp. 599-602
    • Sogo, J.M.1    Lopes, M.2    Foiani, M.3
  • 236
    • 29544446184 scopus 로고    scopus 로고
    • ATPase-dependent cooperative binding of ORC and Cdc6 to origin DNA
    • Speck, C., Z. Chen, H. Li, and B. Stillman. 2005. ATPase-dependent cooperative binding of ORC and Cdc6 to origin DNA. Nat. Struct. Mol. Biol. 12:965-971.
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 965-971
    • Speck, C.1    Chen, Z.2    Li, H.3    Stillman, B.4
  • 237
    • 67650683478 scopus 로고    scopus 로고
    • ATP binding and hydrolysis by Mcm2 regulate DNA binding by Mcm complexes
    • Stead, B. E., C. D. Sorbara, C. J. Brandl, and M. J. Davey. 2009. ATP binding and hydrolysis by Mcm2 regulate DNA binding by Mcm complexes. J. Mol. Biol. 391:301-313.
    • (2009) J. Mol. Biol. , vol.391 , pp. 301-313
    • Stead, B.E.1    Sorbara, C.D.2    Brandl, C.J.3    Davey, M.J.4
  • 238
    • 0031945518 scopus 로고    scopus 로고
    • Negative regulation of DNA replication by the retinoblastoma protein is mediated by its association with MCM7
    • Sterner, J. M., S. Dew-Knight, C. Musahl, S. Kornbluth, and J. M. Horowitz. 1998. Negative regulation of DNA replication by the retinoblastoma protein is mediated by its association with MCM7. Mol. Cell. Biol. 18:2748-2757.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 2748-2757
    • Sterner, J.M.1    Dew-Knight, S.2    Musahl, C.3    Kornbluth, S.4    Horowitz, J.M.5
  • 239
    • 0032500539 scopus 로고    scopus 로고
    • Sequential hydrolysis of ATP molecules bound in interacting catalytic sites of Escherichia coli transcription termination protein Rho
    • Stitt, B. L., and Y. Xu. 1998. Sequential hydrolysis of ATP molecules bound in interacting catalytic sites of Escherichia coli transcription termination protein Rho. J. Biol. Chem. 273:26477-26486.
    • (1998) J. Biol. Chem. , vol.273 , pp. 26477-26486
    • Stitt, B.L.1    Xu, Y.2
  • 240
    • 0026500416 scopus 로고
    • The structure of the E. coli recA protein monomer and polymer
    • Story, R. M., I. T. Weber, and T. A. Steitz. 1992. The structure of the E. coli recA protein monomer and polymer. Nature 355:318-325.
    • (1992) Nature , vol.355 , pp. 318-325
    • Story, R.M.1    Weber, I.T.2    Steitz, T.A.3
  • 242
    • 24044463869 scopus 로고    scopus 로고
    • Mrc1 is required for normal progression of replication forks throughout chromatin in S. cerevisiae
    • Szyjka, S. J., C. J. Viggiani, and O. M. Aparicio. 2005. Mrc1 is required for normal progression of replication forks throughout chromatin in S. cerevisiae. Mol. Cell 19:691-697.
    • (2005) Mol. Cell , vol.19 , pp. 691-697
    • Szyjka, S.J.1    Viggiani, C.J.2    Aparicio, O.M.3
  • 243
    • 0028052205 scopus 로고
    • Fission yeast minichromosome loss mutants mis cause lethal aneuploidy and replication abnormality
    • Takahashi, K., H. Yamada, and M. Yanagida. 1994. Fission yeast minichromosome loss mutants mis cause lethal aneuploidy and replication abnormality. Mol. Biol. Cell 5:1145-1158.
    • (1994) Mol. Biol. Cell , vol.5 , pp. 1145-1158
    • Takahashi, K.1    Yamada, H.2    Yanagida, M.3
  • 244
    • 22744445013 scopus 로고    scopus 로고
    • Pumps, paradoxes and ploughshares: Mechanism of the MCM2-7 DNA helicase
    • Takahashi, T. S., D. B. Wigley, and J. C. Walter. 2005. Pumps, paradoxes and ploughshares: mechanism of the MCM2-7 DNA helicase. Trends Biochem. Sci. 30:437-444.
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 437-444
    • Takahashi, T.S.1    Wigley, D.B.2    Walter, J.C.3
  • 245
    • 0037847620 scopus 로고    scopus 로고
    • GINS, a novel multiprotein complex required for chromosomal DNA replication in budding yeast
    • DOI 10.1101/gad.1065903
    • Takayama, Y., Y. Kamimura, M. Okawa, S. Muramatsu, A. Sugino, and H. Araki. 2003. GINS, a novel multiprotein complex required for chromosomal DNA replication in budding yeast. Genes Dev. 17:1153-1165. (Pubitemid 36534989)
    • (2003) Genes and Development , vol.17 , Issue.9 , pp. 1153-1165
    • Takayama, Y.1    Kamimura, Y.2    Okawa, M.3    Muramatsu, S.4    Sugino, A.5    Araki, H.6
  • 246
    • 33748357745 scopus 로고    scopus 로고
    • Functional cooperation between FACT and MCM helicase facilitates initiation of chromatin DNA replication
    • Tan, B. C., C. T. Chien, S. Hirose, and S. C. Lee. 2006. Functional cooperation between FACT and MCM helicase facilitates initiation of chromatin DNA replication. EMBO J. 25:3975-3985.
    • (2006) EMBO J. , vol.25 , pp. 3975-3985
    • Tan, B.C.1    Chien, C.T.2    Hirose, S.3    Lee, S.C.4
  • 247
    • 33846330909 scopus 로고    scopus 로고
    • CDK-dependent phosphorylation of Sld2 and Sld3 initiates DNA replication in budding yeast
    • DOI 10.1038/nature05465, PII NATURE05465
    • Tanaka, S., T. Umemori, K. Hirai, S. Muramatsu, Y. Kamimura, and H. Araki. 2007. CDK-dependent phosphorylation of Sld2 and Sld3 initiates DNA replication in budding yeast. Nature 445:328-332. (Pubitemid 46122821)
    • (2007) Nature , vol.445 , Issue.7125 , pp. 328-332
    • Tanaka, S.1    Umemori, T.2    Hirai, K.3    Muramatsu, S.4    Kamimura, Y.5    Araki, H.6
  • 248
    • 0035797444 scopus 로고    scopus 로고
    • Regulation of DNA replication fork progression through damaged DNA by the Mec1/Rad53 checkpoint
    • Tercero, J. A., and J. F. Diffley. 2001. Regulation of DNA replication fork progression through damaged DNA by the Mec1/Rad53 checkpoint. Nature 412:553-557.
    • (2001) Nature , vol.412 , pp. 553-557
    • Tercero, J.A.1    Diffley, J.F.2
  • 249
    • 0034595211 scopus 로고    scopus 로고
    • DNA synthesis at individual replication forks requires the essential initiation factor Cdc45p
    • Tercero, J. A., K. Labib, and J. F. Diffley. 2000. DNA synthesis at individual replication forks requires the essential initiation factor Cdc45p. EMBO J. 19:2082-2093.
    • (2000) EMBO J. , vol.19 , pp. 2082-2093
    • Tercero, J.A.1    Labib, K.2    Diffley, J.F.3
  • 250
    • 0038730929 scopus 로고    scopus 로고
    • A central role for DNA replication forks in checkpoint activation and response
    • DOI 10.1016/S1097-2765(03)00169-2
    • Tercero, J. A., M. P. Longhese, and J. F. Diffley. 2003. A central role for DNA replication forks in checkpoint activation and response. Mol. Cell 11:1323-1336. (Pubitemid 36645150)
    • (2003) Molecular Cell , vol.11 , Issue.5 , pp. 1323-1336
    • Tercero, J.A.1    Longhese, M.P.2    Diffley, J.F.X.3
  • 251
    • 0040894991 scopus 로고    scopus 로고
    • The RLF-M component of the replication licensing system forms complexes containing all six MCM/P1 polypeptides
    • DOI 10.1093/emboj/16.11.3312
    • Thommes, P., Y. Kubota, H. Takisawa, and J. J. Blow. 1997. The RLF-M component of the replication licensing system forms complexes containing all six MCM/P1 polypeptides. EMBO J. 16:3312-3319. (Pubitemid 27234968)
    • (1997) EMBO Journal , vol.16 , Issue.11 , pp. 3312-3319
    • Thommes, P.1    Kubota, Y.2    Takisawa, H.3    Julian Blow, J.4
  • 252
    • 0028143584 scopus 로고
    • Physiological concentrations of purines and pyrimidines
    • Traut, T. W. 1994. Physiological concentrations of purines and pyrimidines. Mol. Cell. Biochem. 140:1-22.
    • (1994) Mol. Cell. Biochem. , vol.140 , pp. 1-22
    • Traut, T.W.1
  • 253
    • 0026844470 scopus 로고
    • The SRF and MCM1 transcription factors
    • Treisman, R., and G. Ammerer. 1992. The SRF and MCM1 transcription factors. Curr. Opin. Genet. Dev. 2:221-226.
    • (1992) Curr. Opin. Genet. Dev. , vol.2 , pp. 221-226
    • Treisman, R.1    Ammerer, G.2
  • 254
    • 10644290908 scopus 로고    scopus 로고
    • Interaction between human MCM7 and Rad17 proteins is required for replication checkpoint signaling
    • Tsao, C. C., C. Geisen, and R. T. Abraham. 2004. Interaction between human MCM7 and Rad17 proteins is required for replication checkpoint signaling. EMBO J. 23:4660-4669.
    • (2004) EMBO J. , vol.23 , pp. 4660-4669
    • Tsao, C.C.1    Geisen, C.2    Abraham, R.T.3
  • 255
    • 0034646401 scopus 로고    scopus 로고
    • Insights into DNA replication from the third domain of life
    • Tye, B. K. 2000. Insights into DNA replication from the third domain of life. Proc. Natl. Acad. Sci. USA 97:2399-2401.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 2399-2401
    • Tye, B.K.1
  • 256
    • 33644822237 scopus 로고    scopus 로고
    • Structural basis for the cooperative assembly of large T antigen on the origin of replication
    • Valle, M., X. S. Chen, L. E. Donate, E. Fanning, and J. M. Carazo. 2006. Structural basis for the cooperative assembly of large T antigen on the origin of replication. J. Mol. Biol. 357:1295-1305.
    • (2006) J. Mol. Biol. , vol.357 , pp. 1295-1305
    • Valle, M.1    Chen, X.S.2    Donate, L.E.3    Fanning, E.4    Carazo, J.M.5
  • 257
    • 43249095257 scopus 로고    scopus 로고
    • ATP-dependent chromatin remodeling shapes the DNA replication landscape
    • Vincent, J. A., T. J. Kwong, and T. Tsukiyama. 2008. ATP-dependent chromatin remodeling shapes the DNA replication landscape. Nat. Struct. Mol. Biol. 15:477-484.
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 477-484
    • Vincent, J.A.1    Kwong, T.J.2    Tsukiyama, T.3
  • 258
    • 59749098081 scopus 로고    scopus 로고
    • Methanococcus maripaludis: An archaeon with multiple functional MCM proteins?
    • Walters, A. D., and J. P. Chong. 2009. Methanococcus maripaludis: an archaeon with multiple functional MCM proteins? Biochem. Soc. Trans. 37:1-6.
    • (2009) Biochem. Soc. Trans. , vol.37 , pp. 1-6
    • Walters, A.D.1    Chong, J.P.2
  • 259
    • 0025767169 scopus 로고
    • ATP induces the assembly of polyoma large tumor antigen into hexamers
    • Wang, E. H., and C. Prives. 1991. ATP induces the assembly of polyoma large tumor antigen into hexamers. Virology 184:399-403.
    • (1991) Virology , vol.184 , pp. 399-403
    • Wang, E.H.1    Prives, C.2
  • 262
    • 0026501124 scopus 로고
    • Simian virus 40 T-antigen DNA helicase is a hexamer which forms a binary complex during bidirectional unwinding from the viral origin of DNA replication
    • Wessel, R., J. Schweizer, and H. Stahl. 1992. Simian virus 40 T-antigen DNA helicase is a hexamer which forms a binary complex during bidirectional unwinding from the viral origin of DNA replication. J. Virol. 66:804-815.
    • (1992) J. Virol. , vol.66 , pp. 804-815
    • Wessel, R.1    Schweizer, J.2    Stahl, H.3
  • 263
    • 0023906245 scopus 로고
    • Simian virus 40 large T antigen DNA helicase. Characterization of the ATPase-dependent DNA unwinding activity and its substrate requirements
    • Wiekowski, M., M. W. Schwarz, and H. Stahl. 1988. Simian virus 40 large T antigen DNA helicase. Characterization of the ATPase-dependent DNA unwinding activity and its substrate requirements. J. Biol. Chem. 263:436-442.
    • (1988) J. Biol. Chem. , vol.263 , pp. 436-442
    • Wiekowski, M.1    Schwarz, M.W.2    Stahl, H.3
  • 264
    • 33747432986 scopus 로고    scopus 로고
    • Excess Mcm2-7 license dormant origins of replication that can be used under conditions of replicative stress
    • Woodward, A. M., T. Gohler, M. G. Luciani, M. Oehlmann, X. Ge, A. Gartner, D. A. Jackson, and J. J. Blow. 2006. Excess Mcm2-7 license dormant origins of replication that can be used under conditions of replicative stress. J. Cell Biol. 173:673-683.
    • (2006) J. Cell Biol. , vol.173 , pp. 673-683
    • Woodward, A.M.1    Gohler, T.2    Luciani, M.G.3    Oehlmann, M.4    Ge, X.5    Gartner, A.6    Jackson, D.A.7    Blow, J.J.8
  • 265
    • 0015748441 scopus 로고
    • Studies on in vitro DNA synthesis. Isolation of DNA B gene product from Escherichia coli
    • Wright, M., S. Wickner, and J. Hurwitz. 1973. Studies on in vitro DNA synthesis. Isolation of DNA B gene product from Escherichia coli. Proc. Natl. Acad. Sci. USA 70:3120-3124.
    • (1973) Proc. Natl. Acad. Sci. USA , vol.70 , pp. 3120-3124
    • Wright, M.1    Wickner, S.2    Hurwitz, J.3
  • 266
    • 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., J. G. Aparicio, T. Chen, J. D. Barnett, E. G. Jennings, R. A. Young, S. P. Bell, and O. M. Aparicio. 2001. Genome-wide distribution of ORC and MCM proteins in S. cerevisiae: high-resolution mapping of replication origins. Science 294:2357-2360.
    • (2001) Science , vol.294 , pp. 2357-2360
    • Wyrick, J.J.1    Aparicio, J.G.2    Chen, T.3    Barnett, J.D.4    Jennings, E.G.5    Young, R.A.6    Bell, S.P.7    Aparicio, O.M.8
  • 268
    • 1842861596 scopus 로고    scopus 로고
    • Three-dimensional structural views of branch migration and resolution in DNA homologous recombination
    • Yamada, K., M. Ariyoshi, and K. Morikawa. 2004. Three-dimensional structural views of branch migration and resolution in DNA homologous recombination. Curr. Opin. Struct. Biol. 14:130-137.
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , pp. 130-137
    • Yamada, K.1    Ariyoshi, M.2    Morikawa, K.3
  • 269
    • 0025806273 scopus 로고
    • Mcm2 and Mcm37 two proteins important for ARS activity, are related in structure and function
    • Yan, H., S. Gibson, and B. K. Tye. 1991. Mcm2 and Mcm3, two proteins important for ARS activity, are related in structure and function. Genes Dev. 5:944-957. (Pubitemid 21906009)
    • (1991) Genes and Development , vol.5 , Issue.6 , pp. 944-957
    • Yan, H.1    Gibson, S.2    Tye, B.K.3
  • 270
    • 29244451896 scopus 로고    scopus 로고
    • The ATPase activity of MCM2-7 is dispensable for pre-RC assembly but is required for DNA unwinding
    • Ying, C. Y., and J. Gautier. 2005. The ATPase activity of MCM2-7 is dispensable for pre-RC assembly but is required for DNA unwinding. EMBO J. 24:4334-4344.
    • (2005) EMBO J. , vol.24 , pp. 4334-4344
    • Ying, C.Y.1    Gautier, J.2
  • 271
    • 18044379915 scopus 로고    scopus 로고
    • Identification of a novel cell-cycle-induced MCM family protein MCM9
    • Yoshida, K. 2005. Identification of a novel cell-cycle-induced MCM family protein MCM9. Biochem. Biophys. Res. Commun. 331:669-674.
    • (2005) Biochem. Biophys. Res. Commun. , vol.331 , pp. 669-674
    • Yoshida, K.1
  • 272
    • 38349122463 scopus 로고    scopus 로고
    • The GINS complex from Pyrococcus furiosus stimulates the MCM helicase activity
    • Yoshimochi, T., R. Fujikane, M. Kawanami, F. Matsunaga, and Y. Ishino. 2008. The GINS complex from Pyrococcus furiosus stimulates the MCM helicase activity. J. Biol. Chem. 283:1601-1609.
    • (2008) J. Biol. Chem. , vol.283 , pp. 1601-1609
    • Yoshimochi, T.1    Fujikane, R.2    Kawanami, M.3    Matsunaga, F.4    Ishino, Y.5
  • 273
    • 0037044725 scopus 로고    scopus 로고
    • Roles of Mcm7 and Mcm4 subunits in the DNA helicase activity of the mouse Mcm4/6/7 complex
    • You, Z., Y. Ishimi, H. Masai, and F. Hanaoka. 2002. Roles of Mcm7 and Mcm4 subunits in the DNA helicase activity of the mouse Mcm4/6/7 complex. J. Biol. Chem. 277:42471-42479.
    • (2002) J. Biol. Chem. , vol.277 , pp. 42471-42479
    • You, Z.1    Ishimi, Y.2    Masai, H.3    Hanaoka, F.4
  • 274
    • 0344011592 scopus 로고    scopus 로고
    • Thymine-rich single-stranded DNA activates Mcm4/6/7 helicase on Y-fork and bubble-like substrates
    • DOI 10.1093/emboj/cdg576
    • You, Z., Y. Ishimi, T. Mizuno, K. Sugasawa, F. Hanaoka, and H. Masai. 2003. Thymine-rich single-stranded DNA activates Mcm4/6/7 helicase on Y-fork and bubble-like substrates. EMBO J. 22:6148-6160. (Pubitemid 37463257)
    • (2003) EMBO Journal , vol.22 , Issue.22 , pp. 6148-6160
    • You, Z.1    Ishimi, Y.2    Mizuno, T.3    Sugasawa, K.4    Hanaoka, F.5    Masai, H.6
  • 275
    • 0033499708 scopus 로고    scopus 로고
    • Biochemical analysis of the intrinsic Mcm4-Mcm6-Mcm7 DNA helicase activity
    • You, Z., Y. Komamura, and Y. Ishimi. 1999. Biochemical analysis of the intrinsic Mcm4-Mcm6-Mcm7 DNA helicase activity. Mol. Cell. Biol. 19:8003-8015.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 8003-8015
    • You, Z.1    Komamura, Y.2    Ishimi, Y.3
  • 276
    • 0029984117 scopus 로고    scopus 로고
    • The hexameric E. coli DnaB helicase can exist in different quaternary states
    • Yu, X., M. J. Jezewska, W. Bujalowski, and E. H. Egelman. 1996. The hexameric E. coli DnaB helicase can exist in different quaternary states. J. Mol. Biol. 259:7-14.
    • (1996) J. Mol. Biol. , vol.259 , pp. 7-14
    • Yu, X.1    Jezewska, M.J.2    Bujalowski, W.3    Egelman, E.H.4
  • 277
    • 0036668640 scopus 로고    scopus 로고
    • The Methanobacterium thermoautotrophicum MCM protein can form heptameric rings
    • DOI 10.1093/embo-reports/kvf160
    • Yu, X., M. S. VanLoock, A. Poplawski, Z. Kelman, T. Xiang, B. K. Tye, and E. H. Egelman. 2002. The Methanobacterium thermoautotrophicum MCM protein can form heptameric rings. EMBO Rep. 3:792-797. (Pubitemid 34966020)
    • (2002) EMBO Reports , vol.3 , Issue.8 , pp. 792-797
    • Yu, X.1    Vanloock, M.S.2    Poplawski, A.3    Kelman, Z.4    Xiang, T.5    Tye, B.K.6    Egelman, E.H.7
  • 278
    • 3242770626 scopus 로고    scopus 로고
    • Pairwise interactions of the six human MCM protein subunits
    • Yu, Z., D. Feng, and C. Liang. 2004. Pairwise interactions of the six human MCM protein subunits. J. Mol. Biol. 340:1197-1206.
    • (2004) J. Mol. Biol. , vol.340 , pp. 1197-1206
    • Yu, Z.1    Feng, D.2    Liang, C.3
  • 279
    • 33846328709 scopus 로고    scopus 로고
    • Phosphorylation of Sld2 and Sld3 by cyclin-dependent kinases promotes DNA replication in budding yeast
    • DOI 10.1038/nature05432, PII NATURE05432
    • Zegerman, P., and J. F. Diffley. 2007. Phosphorylation of Sld2 and Sld3 by cyclin-dependent kinases promotes DNA replication in budding yeast. Nature 445:281-285. (Pubitemid 46122811)
    • (2007) Nature , vol.445 , Issue.7125 , pp. 281-285
    • Zegerman, P.1    Diffley, J.F.X.2
  • 280
    • 0024316732 scopus 로고
    • Initiation of λ DNA replication with purified host- And bacteriophage-encoded proteins: The role of the dnaK, dnaJ and grpE heat shock proteins
    • Zylicz, M., D. Ang, K. Liberek, and C. Georgopoulos. 1989. Initiation of lambda DNA replication with purified host- and bacteriophage-encoded proteins: the role of the dnaK, dnaJ and grpE heat shock proteins. EMBO J. 8:1601-1608. (Pubitemid 19274387)
    • (1989) EMBO Journal , vol.8 , Issue.5 , pp. 1601-1608
    • Zylicz, M.1    Ang, D.2    Liberek, K.3    Georgopoulos, C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.