메뉴 건너뛰기




Volumn 30, Issue 8, 2005, Pages 437-444

Pumps, paradoxes and ploughshares: Mechanism of the MCM2-7 DNA helicase

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; DOUBLE STRANDED DNA; HELICASE; MINICHROMOSOME MAINTENANCE PROTEIN 2;

EID: 22744445013     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tibs.2005.06.007     Document Type: Article
Times cited : (130)

References (75)
  • 1
    • 0032881250 scopus 로고    scopus 로고
    • MCM proteins in DNA replication
    • B.K. Tye MCM proteins in DNA replication Annu. Rev. Biochem. 68 1999 649 686
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 649-686
    • Tye, B.K.1
  • 2
    • 0035253410 scopus 로고    scopus 로고
    • Is the MCM2-7 complex the eukaryotic DNA replication fork helicase?
    • K. Labib, and J.F. Diffley Is the MCM2-7 complex the eukaryotic DNA replication fork helicase? Curr. Opin. Genet. Dev. 11 2001 64 70
    • (2001) Curr. Opin. Genet. Dev. , vol.11 , pp. 64-70
    • Labib, K.1    Diffley, J.F.2
  • 3
    • 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
    • E.V. Koonin 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 1993 2541 2547
    • (1993) Nucleic Acids Res. , vol.21 , pp. 2541-2547
    • Koonin, E.V.1
  • 4
    • 0032969563 scopus 로고    scopus 로고
    • AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes
    • A.F. Neuwald AAA+: a class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes Genome Res. 9 1999 27 43
    • (1999) Genome Res. , vol.9 , pp. 27-43
    • Neuwald, A.F.1
  • 5
    • 0034634533 scopus 로고    scopus 로고
    • The hexameric eukaryotic MCM helicase: Building symmetry from nonidentical parts
    • B.K. Tye, and S. Sawyer The hexameric eukaryotic MCM helicase: building symmetry from nonidentical parts J. Biol. Chem. 275 2000 34833 34836
    • (2000) J. Biol. Chem. , vol.275 , pp. 34833-34836
    • Tye, B.K.1    Sawyer, S.2
  • 6
    • 0031184659 scopus 로고    scopus 로고
    • A globular complex formation by Nda1 and the other five members of the MCM protein family in fission yeast
    • Y. Adachi A globular complex formation by Nda1 and the other five members of the MCM protein family in fission yeast Genes Cells 2 1997 467 479
    • (1997) Genes Cells , vol.2 , pp. 467-479
    • Adachi, Y.1
  • 7
    • 0034647412 scopus 로고    scopus 로고
    • Electron microscopic observation and single-stranded DNA binding activity of the Mcm4,6,7 complex
    • M. Sato Electron microscopic observation and single-stranded DNA binding activity of the Mcm4,6,7 complex J. Mol. Biol. 300 2000 421 431
    • (2000) J. Mol. Biol. , vol.300 , pp. 421-431
    • Sato, M.1
  • 8
    • 0037336323 scopus 로고    scopus 로고
    • The structure and function of MCM from archaeal M. Thermoautotrophicum
    • R.J. Fletcher The structure and function of MCM from archaeal M. Thermoautotrophicum Nat. Struct. Biol. 10 2003 160 167
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 160-167
    • Fletcher, R.J.1
  • 9
    • 0030859463 scopus 로고    scopus 로고
    • A DNA helicase activity is associated with an MCM4, -6, and -7 protein complex
    • Y. Ishimi A DNA helicase activity is associated with an MCM4, -6, and -7 protein complex J. Biol. Chem. 272 1997 24508 24513
    • (1997) J. Biol. Chem. , vol.272 , pp. 24508-24513
    • Ishimi, Y.1
  • 10
    • 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
    • D.L. Kaplan 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 2003 49171 49182
    • (2003) J. Biol. Chem. , vol.278 , pp. 49171-49182
    • Kaplan, D.L.1
  • 11
    • 0035793113 scopus 로고    scopus 로고
    • Processive DNA helicase activity of the minichromosome maintenance proteins 4, 6, and 7 complex requires forked DNA structures
    • J.K. Lee, and J. Hurwitz Processive DNA helicase activity of the minichromosome maintenance proteins 4, 6, and 7 complex requires forked DNA structures Proc. Natl. Acad. Sci. U. S. A. 98 2001 54 59
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 54-59
    • Lee, J.K.1    Hurwitz, J.2
  • 12
    • 0034652354 scopus 로고    scopus 로고
    • A double-hexamer archaeal minichromosome maintenance protein is an ATP-dependent DNA helicase
    • J.P. Chong A double-hexamer archaeal minichromosome maintenance protein is an ATP-dependent DNA helicase Proc. Natl. Acad. Sci. U. S. A. 97 2000 1530 1535
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 1530-1535
    • Chong, J.P.1
  • 13
    • 0033593053 scopus 로고    scopus 로고
    • The single minichromosome maintenance protein of Methanobacterium thermoautotrophicum DeltaH contains DNA helicase activity
    • Z. Kelman The single minichromosome maintenance protein of Methanobacterium thermoautotrophicum DeltaH contains DNA helicase activity Proc. Natl. Acad. Sci. U. S. A. 96 1999 14783 14788
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 14783-14788
    • Kelman, Z.1
  • 14
    • 0034686021 scopus 로고    scopus 로고
    • The intrinsic DNA helicase activity of Methanobacterium thermoautotrophicum delta H minichromosome maintenance protein
    • D.F. Shechter The intrinsic DNA helicase activity of Methanobacterium thermoautotrophicum delta H minichromosome maintenance protein J. Biol. Chem. 275 2000 15049 15059
    • (2000) J. Biol. Chem. , vol.275 , pp. 15049-15059
    • Shechter, D.F.1
  • 15
    • 0030886099 scopus 로고    scopus 로고
    • Components and dynamics of DNA replication complexes in S. cerevisiae: Redistribution of MCM proteins and Cdc45p during S phase
    • O.M. Aparicio Components and dynamics of DNA replication complexes in S. cerevisiae: redistribution of MCM proteins and Cdc45p during S phase Cell 91 1997 59 69
    • (1997) Cell , vol.91 , pp. 59-69
    • Aparicio, O.M.1
  • 16
    • 0034595448 scopus 로고    scopus 로고
    • Uninterrupted MCM2-7 function required for DNA replication fork progression
    • K. Labib Uninterrupted MCM2-7 function required for DNA replication fork progression Science 288 2000 1643 1647
    • (2000) Science , vol.288 , pp. 1643-1647
    • Labib, K.1
  • 17
    • 5044236667 scopus 로고    scopus 로고
    • A requirement for MCM7 and Cdc45 in chromosome unwinding during eukaryotic DNA replication
    • M. Pacek, and J.C. Walter A requirement for MCM7 and Cdc45 in chromosome unwinding during eukaryotic DNA replication EMBO J. 23 2004 3667 3676
    • (2004) EMBO J. , vol.23 , pp. 3667-3676
    • Pacek, M.1    Walter, J.C.2
  • 18
    • 8544221940 scopus 로고    scopus 로고
    • DNA unwinding is an Mcm complex-dependent and ATP hydrolysis-dependent process
    • D. Shechter DNA unwinding is an Mcm complex-dependent and ATP hydrolysis-dependent process J. Biol. Chem. 279 2004 45586 45593
    • (2004) J. Biol. Chem. , vol.279 , pp. 45586-45593
    • Shechter, D.1
  • 19
    • 0037440013 scopus 로고    scopus 로고
    • Identification and functional characterization of a new member of the human Mcm protein family: HMcm8
    • D. Gozuacik Identification and functional characterization of a new member of the human Mcm protein family: hMcm8 Nucleic Acids Res. 31 2003 570 579
    • (2003) Nucleic Acids Res. , vol.31 , pp. 570-579
    • Gozuacik, D.1
  • 20
    • 13544252547 scopus 로고    scopus 로고
    • MCM8 is an MCM2-7-related protein that functions as a DNA helicase during replication elongation and not initiation
    • D. Maiorano MCM8 is an MCM2-7-related protein that functions as a DNA helicase during replication elongation and not initiation Cell 120 2005 315 328
    • (2005) Cell , vol.120 , pp. 315-328
    • Maiorano, D.1
  • 21
    • 0035997368 scopus 로고    scopus 로고
    • DNA replication in eukaryotic cells
    • S.P. Bell, and A. Dutta DNA replication in eukaryotic cells Annu. Rev. Biochem. 71 2002 333 374
    • (2002) Annu. Rev. Biochem. , vol.71 , pp. 333-374
    • Bell, S.P.1    Dutta, A.2
  • 22
    • 0344198460 scopus 로고    scopus 로고
    • Perpetuating the double helix: Molecular machines at eukaryotic DNA replication origins
    • J. Mendez, and B. Stillman Perpetuating the double helix: molecular machines at eukaryotic DNA replication origins Bioessays 25 2003 1158 1167
    • (2003) Bioessays , vol.25 , pp. 1158-1167
    • Mendez, J.1    Stillman, B.2
  • 23
    • 0038680253 scopus 로고    scopus 로고
    • Functional proteomic identification of DNA replication proteins by induced proteolysis in vivo
    • M. Kanemaki Functional proteomic identification of DNA replication proteins by induced proteolysis in vivo Nature 423 2003 720 724
    • (2003) Nature , vol.423 , pp. 720-724
    • Kanemaki, M.1
  • 24
    • 0037510025 scopus 로고    scopus 로고
    • A novel ring-like complex of Xenopus proteins essential for the initiation of DNA replication
    • Y. Kubota A novel ring-like complex of Xenopus proteins essential for the initiation of DNA replication Genes Dev. 17 2003 1141 1152
    • (2003) Genes Dev. , vol.17 , pp. 1141-1152
    • Kubota, Y.1
  • 25
    • 0033936230 scopus 로고    scopus 로고
    • Central role for cdc45 in establishing an initiation complex of DNA replication in Xenopus egg extracts
    • S. Mimura Central role for cdc45 in establishing an initiation complex of DNA replication in Xenopus egg extracts Genes Cells 5 2000 439 452
    • (2000) Genes Cells , vol.5 , pp. 439-452
    • Mimura, S.1
  • 26
    • 0033637837 scopus 로고    scopus 로고
    • Initiation of eukaryotic DNA replication: Origin unwinding and sequential chromatin association of Cdc45, RPA, and DNA polymerase α
    • J. Walter, and J. Newport Initiation of eukaryotic DNA replication: origin unwinding and sequential chromatin association of Cdc45, RPA, and DNA polymerase α Mol. Cell 5 2000 617 627
    • (2000) Mol. Cell , vol.5 , pp. 617-627
    • Walter, J.1    Newport, J.2
  • 27
    • 0034595211 scopus 로고    scopus 로고
    • DNA synthesis at individual replication forks requires the essential initiation factor Cdc45p
    • J.A. Tercero DNA synthesis at individual replication forks requires the essential initiation factor Cdc45p EMBO J. 19 2000 2082 2093
    • (2000) EMBO J. , vol.19 , pp. 2082-2093
    • Tercero, J.A.1
  • 28
    • 0034004129 scopus 로고    scopus 로고
    • Assembly of a complex containing Cdc45p, replication protein A, and Mcm2p at replication origins controlled by S-phase cyclin-dependent kinases and Cdc7p-Dbf4p Kinase
    • L. Zou, and B. Stillman Assembly of a complex containing Cdc45p, replication protein A, and Mcm2p at replication origins controlled by S-phase cyclin-dependent kinases and Cdc7p-Dbf4p Kinase Mol. Cell. Biol. 20 2000 3086 3096
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 3086-3096
    • Zou, L.1    Stillman, B.2
  • 29
    • 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
    • T. Masuda 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 2003 145 161
    • (2003) Genes Cells , vol.8 , pp. 145-161
    • Masuda, T.1
  • 30
    • 0037219192 scopus 로고    scopus 로고
    • A rotary pumping model for helicase function of MCM proteins at a distance from replication forks
    • R.A. Laskey, and M.A. Madine A rotary pumping model for helicase function of MCM proteins at a distance from replication forks EMBO Rep. 4 2003 26 30
    • (2003) EMBO Rep. , vol.4 , pp. 26-30
    • Laskey, R.A.1    Madine, M.A.2
  • 31
    • 0037366704 scopus 로고    scopus 로고
    • Bidirectional DNA unwinding by a ternary complex of T antigen, nucleolin and topoisomerase I
    • S. Seinsoth Bidirectional DNA unwinding by a ternary complex of T antigen, nucleolin and topoisomerase I EMBO Rep. 4 2003 263 268
    • (2003) EMBO Rep. , vol.4 , pp. 263-268
    • Seinsoth, S.1
  • 32
    • 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
    • R. Wessel 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 1992 804 815
    • (1992) J. Virol. , vol.66 , pp. 804-815
    • Wessel, R.1
  • 33
    • 0037160068 scopus 로고    scopus 로고
    • Characterization of simian virus 40 T-antigen double hexamers bound to a replication fork. the active form of the helicase
    • A.I. Alexandrov Characterization of simian virus 40 T-antigen double hexamers bound to a replication fork. The active form of the helicase J. Biol. Chem. 277 2002 44886 44897
    • (2002) J. Biol. Chem. , vol.277 , pp. 44886-44897
    • Alexandrov, A.I.1
  • 34
    • 0030840509 scopus 로고    scopus 로고
    • Dimerization of simian virus 40 T-antigen hexamers activates T-antigen DNA helicase activity
    • N.V. Smelkova, and J.A. Borowiec Dimerization of simian virus 40 T-antigen hexamers activates T-antigen DNA helicase activity J. Virol. 71 1997 8766 8773
    • (1997) J. Virol. , vol.71 , pp. 8766-8773
    • Smelkova, N.V.1    Borowiec, J.A.2
  • 35
    • 0032978966 scopus 로고    scopus 로고
    • Two regions of simian virus 40 T antigen determine cooperativity of double-hexamer assembly on the viral origin of DNA replication and promote hexamer interactions during bidirectional origin DNA unwinding
    • K. Weisshart Two regions of simian virus 40 T antigen determine cooperativity of double-hexamer assembly on the viral origin of DNA replication and promote hexamer interactions during bidirectional origin DNA unwinding J. Virol. 73 1999 2201 2211
    • (1999) J. Virol. , vol.73 , pp. 2201-2211
    • Weisshart, K.1
  • 36
    • 0038700763 scopus 로고    scopus 로고
    • Structure of the replicative helicase of the oncoprotein SV40 large tumour antigen
    • D. Li Structure of the replicative helicase of the oncoprotein SV40 large tumour antigen Nature 423 2003 512 518
    • (2003) Nature , vol.423 , pp. 512-518
    • Li, D.1
  • 37
    • 4444226952 scopus 로고    scopus 로고
    • Mechanisms of conformational change for a replicative hexameric helicase of SV40 large tumor antigen
    • D. Gai Mechanisms of conformational change for a replicative hexameric helicase of SV40 large tumor antigen Cell 119 2004 47 60
    • (2004) Cell , vol.119 , pp. 47-60
    • Gai, D.1
  • 38
    • 4444347924 scopus 로고    scopus 로고
    • Two heads are better than one: Regulation of DNA replication by hexameric helicases
    • R.A. Sclafani Two heads are better than one: regulation of DNA replication by hexameric helicases Genes Dev. 18 2004 2039 2045
    • (2004) Genes Dev. , vol.18 , pp. 2039-2045
    • Sclafani, R.A.1
  • 39
    • 0035812836 scopus 로고    scopus 로고
    • Structural analysis of DNA replication fork reversal by RecG
    • M.R. Singleton Structural analysis of DNA replication fork reversal by RecG Cell 107 2001 79 89
    • (2001) Cell , vol.107 , pp. 79-89
    • Singleton, M.R.1
  • 40
    • 0033515425 scopus 로고    scopus 로고
    • Crystal structures of complexes of PcrA DNA helicase with a DNA substrate indicate an inchworm mechanism
    • S.S. Velankar Crystal structures of complexes of PcrA DNA helicase with a DNA substrate indicate an inchworm mechanism Cell 97 1999 75 84
    • (1999) Cell , vol.97 , pp. 75-84
    • Velankar, S.S.1
  • 41
    • 0033573066 scopus 로고    scopus 로고
    • Crystal structure of UvrB, a DNA helicase adapted for nucleotide excision repair
    • K. Theis Crystal structure of UvrB, a DNA helicase adapted for nucleotide excision repair EMBO J. 18 1999 6899 6907
    • (1999) EMBO J. , vol.18 , pp. 6899-6907
    • Theis, K.1
  • 42
    • 9144271294 scopus 로고    scopus 로고
    • Crystal structure of RecBCD enzyme reveals a machine for processing DNA breaks
    • M.R. Singleton Crystal structure of RecBCD enzyme reveals a machine for processing DNA breaks Nature 432 2004 187 193
    • (2004) Nature , vol.432 , pp. 187-193
    • Singleton, M.R.1
  • 43
    • 4143151757 scopus 로고    scopus 로고
    • Twin DNA pumps of a hexameric helicase provide power to simultaneously melt two duplexes
    • D.L. Kaplan, and M. O'Donnell Twin DNA pumps of a hexameric helicase provide power to simultaneously melt two duplexes Mol. Cell 15 2004 453 465
    • (2004) Mol. Cell , vol.15 , pp. 453-465
    • Kaplan, D.L.1    O'Donnell, M.2
  • 44
    • 0031002795 scopus 로고    scopus 로고
    • Coordinate binding of ATP and origin DNA regulates the ATPase activity of the origin recognition complex
    • R.D. Klemm Coordinate binding of ATP and origin DNA regulates the ATPase activity of the origin recognition complex Cell 88 1997 493 502
    • (1997) Cell , vol.88 , pp. 493-502
    • Klemm, R.D.1
  • 45
    • 11144246103 scopus 로고    scopus 로고
    • Atomic force microscopic analysis of the binding of the Schizosaccharomyces pombe origin recognition complex and the spOrc4 protein with origin DNA
    • M. Gaczynska Atomic force microscopic analysis of the binding of the Schizosaccharomyces pombe origin recognition complex and the spOrc4 protein with origin DNA Proc. Natl. Acad. Sci. U. S. A. 101 2004 17952 17957
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 17952-17957
    • Gaczynska, M.1
  • 46
    • 0033634866 scopus 로고    scopus 로고
    • Structure and function of Cdc6/Cdc18: Implications for origin recognition and checkpoint control
    • J. Liu Structure and function of Cdc6/Cdc18: implications for origin recognition and checkpoint control Mol. Cell 6 2000 637 648
    • (2000) Mol. Cell , vol.6 , pp. 637-648
    • Liu, J.1
  • 47
    • 0032110626 scopus 로고    scopus 로고
    • Nucleotide-dependent prereplicative complex assembly by Cdc6p, a homolog of eukaryotic and prokaryotic clamp-loaders
    • G. Perkins, and J.F. Diffley Nucleotide-dependent prereplicative complex assembly by Cdc6p, a homolog of eukaryotic and prokaryotic clamp-loaders Mol. Cell 2 1998 23 32
    • (1998) Mol. Cell , vol.2 , pp. 23-32
    • Perkins, G.1    Diffley, J.F.2
  • 48
    • 10944235448 scopus 로고    scopus 로고
    • ATP hydrolysis by ORC catalyzes reiterative Mcm2-7 assembly at a defined origin of replication
    • J.L. Bowers ATP hydrolysis by ORC catalyzes reiterative Mcm2-7 assembly at a defined origin of replication Mol. Cell 16 2004 967 978
    • (2004) Mol. Cell , vol.16 , pp. 967-978
    • Bowers, J.L.1
  • 49
    • 3042588011 scopus 로고    scopus 로고
    • Structural analysis of a eukaryotic sliding DNA clamp-clamp loader complex
    • G.D. Bowman Structural analysis of a eukaryotic sliding DNA clamp-clamp loader complex Nature 429 2004 724 730
    • (2004) Nature , vol.429 , pp. 724-730
    • Bowman, G.D.1
  • 50
    • 3042642152 scopus 로고    scopus 로고
    • The clamp-loading complex for processive DNA replication
    • T. Miyata The clamp-loading complex for processive DNA replication Nat. Struct. Mol. Biol. 11 2004 632 636
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 632-636
    • Miyata, T.1
  • 51
    • 0030951331 scopus 로고    scopus 로고
    • Cdc6p-dependent loading of Mcm proteins onto pre-replicative chromatin in budding yeast
    • S. Donovan Cdc6p-dependent loading of Mcm proteins onto pre-replicative chromatin in budding yeast Proc. Natl. Acad. Sci. U. S. A. 94 1997 5611 5616
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 5611-5616
    • Donovan, S.1
  • 52
    • 0037031834 scopus 로고    scopus 로고
    • MCM2-7 complexes bind chromatin in a distributed pattern surrounding ORC in Xenopus egg extracts
    • M.C. Edwards MCM2-7 complexes bind chromatin in a distributed pattern surrounding ORC in Xenopus egg extracts J. Biol. Chem. 277 2002 33049 33057
    • (2002) J. Biol. Chem. , vol.277 , pp. 33049-33057
    • Edwards, M.C.1
  • 53
    • 0032770221 scopus 로고    scopus 로고
    • Changes in association of the Xenopus origin recognition complex with chromatin on licensing of replication origins
    • A. Rowles Changes in association of the Xenopus origin recognition complex with chromatin on licensing of replication origins J. Cell Sci. 112 1999 2011 2018
    • (1999) J. Cell Sci. , vol.112 , pp. 2011-2018
    • Rowles, A.1
  • 54
    • 0031022391 scopus 로고    scopus 로고
    • Cell cycle regulation of the replication licensing system: Involvement of a Cdk-dependent inhibitor
    • H.M. Mahbubani Cell cycle regulation of the replication licensing system: involvement of a Cdk-dependent inhibitor J. Cell Biol. 136 1997 125 135
    • (1997) J. Cell Biol. , vol.136 , pp. 125-135
    • Mahbubani, H.M.1
  • 55
    • 0033593053 scopus 로고    scopus 로고
    • The single minichromosome maintenance protein of Methanobacterium thermoautotrophicum DeltaH contains DNA helicase activity
    • Z. Kelman The single minichromosome maintenance protein of Methanobacterium thermoautotrophicum DeltaH contains DNA helicase activity Proc. Natl. Acad. Sci. U. S. A. 96 1999 14783 14788
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 14783-14788
    • Kelman, Z.1
  • 56
    • 0037459376 scopus 로고    scopus 로고
    • Chromosomal cohesin forms a ring
    • S. Gruber Chromosomal cohesin forms a ring Cell 112 2003 765 777
    • (2003) Cell , vol.112 , pp. 765-777
    • Gruber, S.1
  • 57
    • 0036242551 scopus 로고    scopus 로고
    • Molecular architecture of SMC proteins and the yeast cohesin complex
    • C.H. Haering Molecular architecture of SMC proteins and the yeast cohesin complex Mol. Cell 9 2002 773 788
    • (2002) Mol. Cell , vol.9 , pp. 773-788
    • Haering, C.H.1
  • 58
    • 0034674728 scopus 로고    scopus 로고
    • Premature structural changes at replication origins in a yeast MCM mutant
    • D.S. Geraghty Premature structural changes at replication origins in a yeast MCM mutant J. Biol. Chem. 275 2000 18011 18021
    • (2000) J. Biol. Chem. , vol.275 , pp. 18011-18021
    • Geraghty, D.S.1
  • 59
    • 1942501704 scopus 로고    scopus 로고
    • Primer utilization by DNA polymerase α-primase is influenced by its interaction with Mcm10p
    • K. Fien Primer utilization by DNA polymerase α-primase is influenced by its interaction with Mcm10p J. Biol. Chem. 279 2004 16144 16153
    • (2004) J. Biol. Chem. , vol.279 , pp. 16144-16153
    • Fien, K.1
  • 60
    • 0037418273 scopus 로고    scopus 로고
    • The Cdc23 (Mcm10) protein is required for the phosphorylation of minichromosome maintenance complex by the Dfp1-Hsk1 kinase
    • J.K. Lee The Cdc23 (Mcm10) protein is required for the phosphorylation of minichromosome maintenance complex by the Dfp1-Hsk1 kinase Proc. Natl. Acad. Sci. U. S. A. 100 2003 2334 2339
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 2334-2339
    • Lee, J.K.1
  • 61
    • 0034687677 scopus 로고    scopus 로고
    • Stepwise assembly of initiation proteins at budding yeast replication origins in vitro
    • T. Seki, and J.F. Diffley Stepwise assembly of initiation proteins at budding yeast replication origins in vitro Proc. Natl. Acad. Sci. U. S. A. 97 2000 14115 14120
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 14115-14120
    • Seki, T.1    Diffley, J.F.2
  • 62
    • 0025019702 scopus 로고
    • Binding and unwinding-how T antigen engages the SV40 origin of DNA replication
    • J.A. Borowiec Binding and unwinding-how T antigen engages the SV40 origin of DNA replication Cell 60 1990 181 184
    • (1990) Cell , vol.60 , pp. 181-184
    • Borowiec, J.A.1
  • 63
    • 0033598133 scopus 로고    scopus 로고
    • Mcm2, but not RPA, is a component of the mammalian early G1-phase prereplication complex
    • D.S. Dimitrova Mcm2, but not RPA, is a component of the mammalian early G1-phase prereplication complex J. Cell Biol. 146 1999 709 722
    • (1999) J. Cell Biol. , vol.146 , pp. 709-722
    • Dimitrova, D.S.1
  • 64
    • 0141557808 scopus 로고    scopus 로고
    • CpG methylation of DNA restricts prereplication complex assembly in Xenopus egg extracts
    • K.J. Harvey, and J. Newport CpG methylation of DNA restricts prereplication complex assembly in Xenopus egg extracts Mol. Cell. Biol. 23 2003 6769 6779
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 6769-6779
    • Harvey, K.J.1    Newport, J.2
  • 65
    • 0032544742 scopus 로고    scopus 로고
    • Human minichromosome maintenance proteins and human origin recognition complex 2 protein on chromatin
    • M. Ritzi Human minichromosome maintenance proteins and human origin recognition complex 2 protein on chromatin J. Biol. Chem. 273 1998 24543 24549
    • (1998) J. Biol. Chem. , vol.273 , pp. 24543-24549
    • Ritzi, M.1
  • 66
    • 0034711945 scopus 로고    scopus 로고
    • Mechanisms ensuring rapid and complete DNA replication despite random initiation in Xenopus early embryos
    • I. Lucas Mechanisms ensuring rapid and complete DNA replication despite random initiation in Xenopus early embryos J. Mol. Biol. 296 2000 769 786
    • (2000) J. Mol. Biol. , vol.296 , pp. 769-786
    • Lucas, I.1
  • 67
    • 0141856295 scopus 로고    scopus 로고
    • Fission yeast Cdc23/Mcm10 functions after pre-replicative complex formation to promote Cdc45 chromatin binding
    • J. Gregan Fission yeast Cdc23/Mcm10 functions after pre-replicative complex formation to promote Cdc45 chromatin binding Mol. Biol. Cell 14 2003 3876 3887
    • (2003) Mol. Biol. Cell , vol.14 , pp. 3876-3887
    • Gregan, J.1
  • 68
    • 6344284782 scopus 로고    scopus 로고
    • Mcm10 regulates the stability and chromatin association of DNA polymerase-α
    • R.M. Ricke, and A.K. Bielinsky Mcm10 regulates the stability and chromatin association of DNA polymerase-α Mol. Cell 16 2004 173 185
    • (2004) Mol. Cell , vol.16 , pp. 173-185
    • Ricke, R.M.1    Bielinsky, A.K.2
  • 69
    • 2942607401 scopus 로고    scopus 로고
    • Mcm10 and Cdc45 cooperate in origin activation in Saccharomyces cerevisiae
    • S.L. Sawyer Mcm10 and Cdc45 cooperate in origin activation in Saccharomyces cerevisiae J. Mol. Biol. 340 2004 195 202
    • (2004) J. Mol. Biol. , vol.340 , pp. 195-202
    • Sawyer, S.L.1
  • 70
    • 0036190356 scopus 로고    scopus 로고
    • Xenopus mcm10 binds to origins of DNA replication after mcm2-7 and stimulates origin binding of cdc45
    • J.A. Wohlschlegel Xenopus mcm10 binds to origins of DNA replication after mcm2-7 and stimulates origin binding of cdc45 Mol. Cell 9 2002 233 240
    • (2002) Mol. Cell , vol.9 , pp. 233-240
    • Wohlschlegel, J.A.1
  • 71
    • 0037034048 scopus 로고    scopus 로고
    • S-Cdk-dependent phosphorylation of Sld2 essential for chromosomal DNA replication in budding yeast
    • H. Masumoto S-Cdk-dependent phosphorylation of Sld2 essential for chromosomal DNA replication in budding yeast Nature 415 2002 651 655
    • (2002) Nature , vol.415 , pp. 651-655
    • Masumoto, H.1
  • 72
    • 0037006806 scopus 로고    scopus 로고
    • CDK phosphorylation of Drc1 regulates DNA replication in fission yeast
    • E. Noguchi CDK phosphorylation of Drc1 regulates DNA replication in fission yeast Curr. Biol. 12 2002 599 605
    • (2002) Curr. Biol. , vol.12 , pp. 599-605
    • Noguchi, E.1
  • 73
    • 0037900888 scopus 로고    scopus 로고
    • Xenopus Cut5 is essential for a CDK-dependent process in the initiation of DNA replication
    • Y. Hashimoto, and H. Takisawa Xenopus Cut5 is essential for a CDK-dependent process in the initiation of DNA replication EMBO J. 22 2003 2526 2535
    • (2003) EMBO J. , vol.22 , pp. 2526-2535
    • Hashimoto, Y.1    Takisawa, H.2
  • 74
    • 0037847620 scopus 로고    scopus 로고
    • GINS, a novel multiprotein complex required for chromosomal DNA replication in budding yeast
    • Y. Takayama GINS, a novel multiprotein complex required for chromosomal DNA replication in budding yeast Genes Dev. 17 2003 1153 1165
    • (2003) Genes Dev. , vol.17 , pp. 1153-1165
    • Takayama, Y.1
  • 75
    • 0037175392 scopus 로고    scopus 로고
    • The Xenopus Xmus101 protein is required for the recruitment of Cdc45 to origins of DNA replication
    • R.A. Van Hatten The Xenopus Xmus101 protein is required for the recruitment of Cdc45 to origins of DNA replication J. Cell Biol. 159 2002 541 547
    • (2002) J. Cell Biol. , vol.159 , pp. 541-547
    • Van Hatten, R.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.