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Volumn 1, Issue , 2007, Pages 27-68

Progress towards the anatomy of the eukaryotic DNA replication fork

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EID: 33750136263     PISSN: 18613373     EISSN: 18613381     Source Type: Book Series    
DOI: 10.1007/7050_016     Document Type: Article
Times cited : (16)

References (211)
  • 1
    • 0033529791 scopus 로고    scopus 로고
    • Differential assembly of cdc45p and DNA polymerases at early and late origins of DNA replication
    • Aparicio OM, Stout AM, Bell SP (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
  • 2
    • 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 OM, Weinstein DM, Bell SP (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
  • 3
    • 0029592020 scopus 로고
    • Dpb11, which interacts with DNA polymerase II(epsilon) in Saccharomyces cerevisiae, has a dual role in S-phase progression and at a cell cycle checkpoint
    • Araki H, Leem SH, Phongdara A, Sugino A (1995) Dpb11, which interacts with DNA polymerase II(epsilon) in Saccharomyces cerevisiae, has a dual role in S-phase progression and at a cell cycle checkpoint. Proc Natl Acad Sci USA 92:11791-11795
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 11791-11795
    • Araki, H.1    Leem, S.H.2    Phongdara, A.3    Sugino, A.4
  • 4
    • 0032134044 scopus 로고    scopus 로고
    • The HORMA domain: A common structural denominator in mitotic checkpoints, chromosome synapsis and DNA repair
    • Aravind L, Koonin EV (1998) The HORMA domain: A common structural denominator in mitotic checkpoints, chromosome synapsis and DNA repair. Trends Biochem Sci 23:284-286
    • (1998) Trends Biochem Sci , vol.23 , pp. 284-286
    • Aravind, L.1    Koonin, E.V.2
  • 6
    • 30344455639 scopus 로고    scopus 로고
    • PCNA functions as a molecular platform to trigger Cdt1 destruction and prevent re-replication
    • Arias EE, Walter JC (2006) PCNA functions as a molecular platform to trigger Cdt1 destruction and prevent re-replication. Nat Cell Biol 8:84-90
    • (2006) Nat Cell Biol , vol.8 , pp. 84-90
    • Arias, E.E.1    Walter, J.C.2
  • 7
    • 0033756041 scopus 로고    scopus 로고
    • The absence of ribonuclease H1 or H2 alters the sensitivity of Saccharomyces cerevisiae to hydroxyurea, caffeine and ethyl methanesulphonate: Implications for roles of RNases H in DNA replication and repair
    • Arudchandran A, Cerritelli S, Narimatsu S, Itaya M, Shin DY, Shimada Y, Crouch RJ (2000) The absence of ribonuclease H1 or H2 alters the sensitivity of Saccharomyces cerevisiae to hydroxyurea, caffeine and ethyl methanesulphonate: Implications for roles of RNases H in DNA replication and repair. Genes Cells 5:789-802
    • (2000) Genes Cells , vol.5 , pp. 789-802
    • Arudchandran, A.1    Cerritelli, S.2    Narimatsu, S.3    Itaya, M.4    Shin, D.Y.5    Shimada, Y.6    Crouch, R.J.7
  • 10
    • 0035169689 scopus 로고    scopus 로고
    • Crystal structure of a DNA-dependent RNA polymerase (DNA primase)
    • Augustin MA, Huber R, Kaiser JT (2001) Crystal structure of a DNA-dependent RNA polymerase (DNA primase). Nat Struct Biol 8:57-61
    • (2001) Nat Struct Biol , vol.8 , pp. 57-61
    • Augustin, M.A.1    Huber, R.2    Kaiser, J.T.3
  • 11
    • 0037449738 scopus 로고    scopus 로고
    • Okazaki fragment maturation in yeast. I. Distribution of functions between FEN1 AND DNA2
    • Ayyagari R, Gomes XV, Gordenin DA, Burgers PM (2003) Okazaki fragment maturation in yeast. I. Distribution of functions between FEN1 AND DNA2. J Biol Chem 278:1618-1625
    • (2003) J Biol Chem , vol.278 , pp. 1618-1625
    • Ayyagari, R.1    Gomes, X.V.2    Gordenin, D.A.3    Burgers, P.M.4
  • 12
    • 0035954737 scopus 로고    scopus 로고
    • RPA governs endonuclease switching during processing of Okazaki fragments in eukaryotes
    • Bae SH, Bae KH, Kim JA, Seo YS (2001a) RPA governs endonuclease switching during processing of Okazaki fragments in eukaryotes. Nature 412:456-461
    • (2001) Nature , vol.412 , pp. 456-461
    • Bae, S.H.1    Bae, K.H.2    Kim, J.A.3    Seo, Y.S.4
  • 13
    • 0037135632 scopus 로고    scopus 로고
    • Coupling of DNA helicase and endonuclease activities of yeast Dna2 facilitates Okazaki fragment processing
    • Bae SH, Kim DW, Kim J, Kim JH, Kim DH, Kim HD, Kang HY, Seo YS (2002) Coupling of DNA helicase and endonuclease activities of yeast Dna2 facilitates Okazaki fragment processing. J Biol Chem 277:26632-26641
    • (2002) J Biol Chem , vol.277 , pp. 26632-26641
    • Bae, S.H.1    Kim, D.W.2    Kim, J.3    Kim, J.H.4    Kim, D.H.5    Kim, H.D.6    Kang, H.Y.7    Seo, Y.S.8
  • 15
    • 0035997368 scopus 로고    scopus 로고
    • DNA replication in eukaryotic cells
    • Bell SP, Dutta A (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
  • 16
    • 0030016920 scopus 로고    scopus 로고
    • DNA ligase I is required for fetal liver erythropoiesis but is not essential for mammalian cell viability
    • Bentley D, Selfridge J, Millar JK, Samuel K, Hole N, Ansell JD, Melton DW (1996) DNA ligase I is required for fetal liver erythropoiesis but is not essential for mammalian cell viability. Nat Genet 13:489-491
    • (1996) Nat Genet , vol.13 , pp. 489-491
    • Bentley, D.1    Selfridge, J.2    Millar, J.K.3    Samuel, K.4    Hole, N.5    Ansell, J.D.6    Melton, D.W.7
  • 18
    • 0037184116 scopus 로고    scopus 로고
    • The influence of the Cdc27 subunit on the properties of the Schizosaccharomyces pombe DNA polymerase delta
    • Bermudez VP, MacNeill SA, Tappin I, Hurwitz J (2002) The influence of the Cdc27 subunit on the properties of the Schizosaccharomyces pombe DNA polymerase delta. J Biol Chem 277:36853-36862
    • (2002) J Biol Chem , vol.277 , pp. 36853-36862
    • Bermudez, V.P.1    MacNeill, S.A.2    Tappin, I.3    Hurwitz, J.4
  • 19
    • 3442896884 scopus 로고    scopus 로고
    • Replication Protein A phosphorylation and the cellular response to DNA damage
    • Binz SK, Sheehan AM, Wold MS (2004) Replication Protein A phosphorylation and the cellular response to DNA damage. DNA Repair (Amst) 3:1015-1024
    • (2004) DNA Repair (Amst) , vol.3 , pp. 1015-1024
    • Binz, S.K.1    Sheehan, A.M.2    Wold, M.S.3
  • 21
    • 0035796407 scopus 로고    scopus 로고
    • Control of chromosomal DNA replication in the early Xenopus embryo
    • Blow JJ (2001) Control of chromosomal DNA replication in the early Xenopus embryo. Embo J 20:3293-3297
    • (2001) Embo J , vol.20 , pp. 3293-3297
    • Blow, J.J.1
  • 22
    • 20344396122 scopus 로고    scopus 로고
    • Preventing re-replication of chromosomal DNA
    • Blow JJ, Dutta A (2005) Preventing re-replication of chromosomal DNA. Nat Rev Mol Cell Biol 6:476-486
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 476-486
    • Blow, J.J.1    Dutta, A.2
  • 23
    • 0346725950 scopus 로고    scopus 로고
    • The origin recognition complex and Sir4 protein recruit Sir1p to yeast silent chromatin through independent interactions requiring a common Sir1p domain
    • Bose ME, McConnell KH, Gardner-Aukema KA, Muller U, Weinreich M, Keck JL, Fox CA (2004) The origin recognition complex and Sir4 protein recruit Sir1p to yeast silent chromatin through independent interactions requiring a common Sir1p domain. Mol Cell Biol 24:774-786
    • (2004) Mol Cell Biol , vol.24 , pp. 774-786
    • Bose, M.E.1    McConnell, K.H.2    Gardner-Aukema, K.A.3    Muller, U.4    Weinreich, M.5    Keck, J.L.6    Fox, C.A.7
  • 25
    • 3042588011 scopus 로고    scopus 로고
    • Structural analysis of a eukaryotic sliding DNA clamp-clamp loader complex
    • Bowman GD, O'Donnell M, Kuriyan J (2004) Structural analysis of a eukaryotic sliding DNA clamp-clamp loader complex. Nature 429:724-730
    • (2004) Nature , vol.429 , pp. 724-730
    • Bowman, G.D.1    O'Donnell, M.2    Kuriyan, J.3
  • 26
    • 0029098312 scopus 로고
    • A yeast gene required for DNA replication encodes a protein with homology to DNA helicases
    • Budd ME, Campbell JL (1995) A yeast gene required for DNA replication encodes a protein with homology to DNA helicases. Proc Natl Acad Sci USA 92:7642-7646
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 7642-7646
    • Budd, M.E.1    Campbell, J.L.2
  • 27
    • 0031000629 scopus 로고    scopus 로고
    • A yeast replicative helicase, Dna2 helicase, interacts with yeast FEN-1 nuclease in carrying out its essential function
    • Budd ME, Campbell JL (1997) A yeast replicative helicase, Dna2 helicase, interacts with yeast FEN-1 nuclease in carrying out its essential function. Mol Cell Biol 17:2136-2142
    • (1997) Mol Cell Biol , vol.17 , pp. 2136-2142
    • Budd, M.E.1    Campbell, J.L.2
  • 28
    • 0031686246 scopus 로고    scopus 로고
    • Eukaryotic DNA polymerases in DNA replication and DNA repair
    • Burgers PM (1998) Eukaryotic DNA polymerases in DNA replication and DNA repair. Chromosoma 107:218-227
    • (1998) Chromosoma , vol.107 , pp. 218-227
    • Burgers, P.M.1
  • 29
    • 0032584599 scopus 로고    scopus 로고
    • Structure and processivity of two forms of saccharomyces cerevisiae DNA polymerase delta
    • Burgers PMJ, Gerik KJ (1998) Structure and processivity of two forms of saccharomyces cerevisiae DNA polymerase delta. J Biol Chem 273:19756-19762
    • (1998) J Biol Chem , vol.273 , pp. 19756-19762
    • Burgers, P.M.J.1    Gerik, K.J.2
  • 30
    • 0025931653 scopus 로고
    • Emetine allows identification of origins of mammalian DNA replication by imbalanced DNA synthesis, not through conservative nucleosome segregation
    • Burhans WC, Vassilev LT, Wu J, Sogo JM, Nallaseth FS, DePamphilis ML (1991) Emetine allows identification of origins of mammalian DNA replication by imbalanced DNA synthesis, not through conservative nucleosome segregation. Embo J 10:4351-4360
    • (1991) Embo J , vol.10 , pp. 4351-4360
    • Burhans, W.C.1    Vassilev, L.T.2    Wu, J.3    Sogo, J.M.4    Nallaseth, F.S.5    DePamphilis, M.L.6
  • 31
    • 18244371925 scopus 로고    scopus 로고
    • Functional uncoupling of MCM helicase and DNA polymerase activities activates the ATR-dependent checkpoint
    • Byun TS, Pacek M, Yee MC, Walter JC, Cimprich KA (2005) Functional uncoupling of MCM helicase and DNA polymerase activities activates the ATR-dependent checkpoint. Genes Dev 19:1040-1052
    • (2005) Genes Dev , vol.19 , pp. 1040-1052
    • Byun, T.S.1    Pacek, M.2    Yee, M.C.3    Walter, J.C.4    Cimprich, K.A.5
  • 32
    • 0345354684 scopus 로고    scopus 로고
    • Failure to produce mitochondrial DNA results in embryonic lethality in RNase H1 null mice
    • Cerritelli SM, Frolova EG, Feng C, Grinberg A, Love PE, Crouch RJ (2003) Failure to produce mitochondrial DNA results in embryonic lethality in RNase H1 null mice. Mol Cell 11:807-815
    • (2003) Mol Cell , vol.11 , pp. 807-815
    • Cerritelli, S.M.1    Frolova, E.G.2    Feng, C.3    Grinberg, A.4    Love, P.E.5    Crouch, R.J.6
  • 33
    • 0035115859 scopus 로고    scopus 로고
    • Cdc13 both positively and negatively regulates telomere replication
    • Chandra A, Hughes TR, Nugent CI, Lundblad V (2001) Cdc13 both positively and negatively regulates telomere replication. Genes Dev 15:404-414
    • (2001) Genes Dev , vol.15 , pp. 404-414
    • Chandra, A.1    Hughes, T.R.2    Nugent, C.I.3    Lundblad, V.4
  • 34
    • 0037515466 scopus 로고    scopus 로고
    • The quaternary structure of DNA polymerase epsilon from Saccharomyces cerevisiae
    • Chilkova O, Jonsson BH, Johansson E (2003) The quaternary structure of DNA polymerase epsilon from Saccharomyces cerevisiae. J Biol Chem 278:14082-14086
    • (2003) J Biol Chem , vol.278 , pp. 14082-14086
    • Chilkova, O.1    Jonsson, B.H.2    Johansson, E.3
  • 35
    • 0037174861 scopus 로고    scopus 로고
    • Protein phosphatase 2A regulates binding of Cdc45 to the prereplication complex
    • Chou DM, Petersen P, Walter JC, Walter G (2002) Protein phosphatase 2A regulates binding of Cdc45 to the prereplication complex. J Biol Chem 277:40520-40527
    • (2002) J Biol Chem , vol.277 , pp. 40520-40527
    • Chou, D.M.1    Petersen, P.2    Walter, J.C.3    Walter, G.4
  • 36
    • 0033546210 scopus 로고    scopus 로고
    • The organization of replication and transcription
    • Cook PR (1999) The organization of replication and transcription. Science 284:1790-1795
    • (1999) Science , vol.284 , pp. 1790-1795
    • Cook, P.R.1
  • 38
    • 30744457568 scopus 로고    scopus 로고
    • Getting a grip on licensing: Mechanism of stable Mcm2-7 loading onto replication origins
    • Cvetic CA, Walter JC (2006) Getting a grip on licensing: Mechanism of stable Mcm2-7 loading onto replication origins. Mol Cell 21:143-144
    • (2006) Mol Cell , vol.21 , pp. 143-144
    • Cvetic, C.A.1    Walter, J.C.2
  • 39
    • 0035336803 scopus 로고    scopus 로고
    • DNA replication: Building the perfect switch
    • Diffley JF (2001) DNA replication: Building the perfect switch. Curr Biol 11:R367-R370
    • (2001) Curr Biol , vol.11
    • Diffley, J.F.1
  • 40
    • 0036500535 scopus 로고    scopus 로고
    • The chromosome replication cycle
    • Diffley JF, Labib K (2002) The chromosome replication cycle. J Cell Sci 115:869-872
    • (2002) J Cell Sci , vol.115 , pp. 869-872
    • Diffley, J.F.1    Labib, K.2
  • 41
    • 0033529497 scopus 로고    scopus 로고
    • Analysis of the essential functions of the C-terminal Protein/Protein interaction domain of saccharomyces cerevisiae pol epsilon and its unexpected ability to support growth in the absence of the DNA polymerase domain
    • Dua R, Levy DL, Campbell JL (1999) Analysis of the essential functions of the C-terminal Protein/Protein interaction domain of saccharomyces cerevisiae pol epsilon and its unexpected ability to support growth in the absence of the DNA polymerase domain. J Biol Chem 274:22283-22288
    • (1999) J Biol Chem , vol.274 , pp. 22283-22288
    • Dua, R.1    Levy, D.L.2    Campbell, J.L.3
  • 42
    • 0037040871 scopus 로고    scopus 로고
    • In vivo reconstitution of Saccharomyces cerevisiae DNA polymerase epsilon in insect cells. Purification and characterization
    • Dua R, Levy DL, Li CM, Snow PM, Campbell JL (2002) In vivo reconstitution of Saccharomyces cerevisiae DNA polymerase epsilon in insect cells. Purification and characterization. J Biol Chem 277:7889-7896
    • (2002) J Biol Chem , vol.277 , pp. 7889-7896
    • Dua, R.1    Levy, D.L.2    Li, C.M.3    Snow, P.M.4    Campbell, J.L.5
  • 43
    • 33750111328 scopus 로고    scopus 로고
    • Chromosomal DNA Replication: On Replicases, Replisomes, and Bidirectional Replication Factories
    • In: Lankenau DH (ed) Springer, Berlin Heidelberg DOI: 10.1007/7050_012
    • Egel R (2006) Chromosomal DNA Replication: On Replicases, Replisomes, and Bidirectional Replication Factories. In: Lankenau DH (ed) Genome Integrity: Facets and Perspectives, vol 1. Springer, Berlin Heidelberg DOI: 10.1007/7050_012
    • (2006) Genome Integrity: Facets and Perspectives , vol.1
    • Egel, R.1
  • 44
    • 0036510055 scopus 로고    scopus 로고
    • The DNA damage-dependent intra-S phase checkpoint is regulated by parallel pathways
    • Falck J, Petrini JH, Williams BR, Lukas J, Bartek J (2002) The DNA damage-dependent intra-S phase checkpoint is regulated by parallel pathways. Nat Genet 30:290-294
    • (2002) Nat Genet , vol.30 , pp. 290-294
    • Falck, J.1    Petrini, J.H.2    Williams, B.R.3    Lukas, J.4    Bartek, J.5
  • 45
    • 0026540613 scopus 로고
    • Simian virus 40 large T antigen: The puzzle, the pieces, and the emerging picture
    • Fanning E (1992) Simian virus 40 large T antigen: The puzzle, the pieces, and the emerging picture. J Virol 66:1289-1293
    • (1992) J Virol , vol.66 , pp. 1289-1293
    • Fanning, E.1
  • 46
    • 0034955240 scopus 로고    scopus 로고
    • Schizosaccharomyces pombe cells lacking the amino-terminal catalytic domains of DNA polymerase epsilon are viable but require the DNA damage checkpoint control
    • Feng W, D'Urso G (2001) Schizosaccharomyces pombe cells lacking the amino-terminal catalytic domains of DNA polymerase epsilon are viable but require the DNA damage checkpoint control. Mol Cell Biol 21:4495-4504
    • (2001) Mol Cell Biol , vol.21 , pp. 4495-4504
    • Feng, W.1    D'Urso, G.2
  • 47
  • 48
    • 0034890460 scopus 로고    scopus 로고
    • Drosophila RNase H1 is essential for development but not for proliferation
    • Filippov V, Filippov M, Gill SS (2001) Drosophila RNase H1 is essential for development but not for proliferation. Mol Genet Genomics 265:771-777
    • (2001) Mol Genet Genomics , vol.265 , pp. 771-777
    • Filippov, V.1    Filippov, M.2    Gill, S.S.3
  • 49
    • 1542405310 scopus 로고    scopus 로고
    • Eukaryotic MCM proteins: Beyond replication initiation
    • table of contents
    • Forsburg SL (2004) Eukaryotic MCM proteins: Beyond replication initiation. Microbiol Mol Biol Rev 68:109-131, table of contents
    • (2004) Microbiol Mol Biol Rev , vol.68 , pp. 109-131
    • Forsburg, S.L.1
  • 50
    • 0036790008 scopus 로고    scopus 로고
    • The origin of DNA genomes and DNA replication proteins
    • Forterre P (2002) The origin of DNA genomes and DNA replication proteins. Curr Opin Microbiol 5:525-532
    • (2002) Curr Opin Microbiol , vol.5 , pp. 525-532
    • Forterre, P.1
  • 51
    • 1642351959 scopus 로고    scopus 로고
    • Distinct roles of DNA polymerases delta and epsilon at the replication fork in Xenopus egg extracts
    • Fukui T, Yamauchi K, Muroya T, Akiyama M, Maki H, Sugino A, Waga S (2004) Distinct roles of DNA polymerases delta and epsilon at the replication fork in Xenopus egg extracts. Genes Cells 9:179-191
    • (2004) Genes Cells , vol.9 , pp. 179-191
    • Fukui, T.1    Yamauchi, K.2    Muroya, T.3    Akiyama, M.4    Maki, H.5    Sugino, A.6    Waga, S.7
  • 52
    • 0037040932 scopus 로고    scopus 로고
    • Human DNA polymerase epsilon colocalizes with proliferating cell nuclear antigen and DNA replication late, but not early, in S phase
    • Fuss J, Linn S (2002) Human DNA polymerase epsilon colocalizes with proliferating cell nuclear antigen and DNA replication late, but not early, in S phase. J Biol Chem 277:8658-8666
    • (2002) J Biol Chem , vol.277 , pp. 8658-8666
    • Fuss, J.1    Linn, S.2
  • 53
    • 27544460716 scopus 로고    scopus 로고
    • Identification and functional analysis of TopBP1 and its homologs
    • Garcia V, Furuya K, Carr AM (2005) Identification and functional analysis of TopBP1 and its homologs. DNA Repair (Amst) 4:1227-1239
    • (2005) DNA Repair (Amst) , vol.4 , pp. 1227-1239
    • Garcia, V.1    Furuya, K.2    Carr, A.M.3
  • 54
    • 18044384092 scopus 로고    scopus 로고
    • DNA polymerases that propagate the eukaryotic DNA replication fork
    • Garg P, Burgers PM (2005) DNA polymerases that propagate the eukaryotic DNA replication fork. Crit Rev Biochem Mol Biol 40:115-128
    • (2005) Crit Rev Biochem Mol Biol , vol.40 , pp. 115-128
    • Garg, P.1    Burgers, P.M.2
  • 55
    • 21244448890 scopus 로고    scopus 로고
    • Proliferating cell nuclear antigen promotes translesion synthesis by DNA polymerase zeta
    • Garg P, Stith CM, Majka J, Burgers PM (2005) Proliferating cell nuclear antigen promotes translesion synthesis by DNA polymerase zeta. J Biol Chem 280:23446-23450
    • (2005) J Biol Chem , vol.280 , pp. 23446-23450
    • Garg, P.1    Stith, C.M.2    Majka, J.3    Burgers, P.M.4
  • 56
    • 0032584658 scopus 로고    scopus 로고
    • Characterization of the two small subunits of Saccharomyces cerevisiae DNA polymerase delta
    • Gerik KJ, Li X, Pautz A, Burgers PM (1998) Characterization of the two small subunits of Saccharomyces cerevisiae DNA polymerase delta. J Biol Chem 273:19747-19755
    • (1998) J Biol Chem , vol.273 , pp. 19747-19755
    • Gerik, K.J.1    Li, X.2    Pautz, A.3    Burgers, P.M.4
  • 58
    • 13444291950 scopus 로고    scopus 로고
    • Mapping and mutation of the conserved DNA polymerase interaction motif (DPIM) located in the C-terminal domain of fission yeast DNA polymerase delta subunit Cdc27
    • Gray FC, Pohler JR, Warbrick E, MacNeill SA (2004) Mapping and mutation of the conserved DNA polymerase interaction motif (DPIM) located in the C-terminal domain of fission yeast DNA polymerase delta subunit Cdc27. BMC Mol Biol 5:21
    • (2004) BMC Mol Biol , vol.5 , pp. 21
    • Gray, F.C.1    Pohler, J.R.2    Warbrick, E.3    MacNeill, S.A.4
  • 59
    • 2442564703 scopus 로고    scopus 로고
    • Pol12, the B subunit of DNA polymerase alpha, functions in both telomere capping and length regulation
    • Grossi S, Puglisi A, Dmitriev PV, Lopes M, Shore D (2004) Pol12, the B subunit of DNA polymerase alpha, functions in both telomere capping and length regulation. Genes Dev 18:992-1006
    • (2004) Genes Dev , vol.18 , pp. 992-1006
    • Grossi, S.1    Puglisi, A.2    Dmitriev, P.V.3    Lopes, M.4    Shore, D.5
  • 60
    • 0030592544 scopus 로고    scopus 로고
    • Structure of the C-terminal region of p21(WAF1/CIP1) complexed with human PCNA
    • Gulbis JM, Kelman Z, Hurwitz J, O'Donnell M, Kuriyan J (1996) Structure of the C-terminal region of p21(WAF1/CIP1) complexed with human PCNA. Cell 87:297-306
    • (1996) Cell , vol.87 , pp. 297-306
    • Gulbis, J.M.1    Kelman, Z.2    Hurwitz, J.3    O'Donnell, M.4    Kuriyan, J.5
  • 61
    • 0025228710 scopus 로고
    • Purification and characterization of DNA polymerase II from the yeast Saccharomyces cerevisiae. Identification of the catalytic core and a possible holoenzyme form of the enzyme
    • Hamatake RK, Hasegawa H, Clark AB, Bebenek K, Kunkel TA, Sugino A (1990) Purification and characterization of DNA polymerase II from the yeast Saccharomyces cerevisiae. Identification of the catalytic core and a possible holoenzyme form of the enzyme. J Biol Chem 265:4072-4083
    • (1990) J Biol Chem , vol.265 , pp. 4072-4083
    • Hamatake, R.K.1    Hasegawa, H.2    Clark, A.B.3    Bebenek, K.4    Kunkel, T.A.5    Sugino, A.6
  • 62
    • 0028281443 scopus 로고
    • The characterization of a mammalian DNA structure specific endonuclease
    • Harrington JJ, Lieber MR (1994a) The characterization of a mammalian DNA structure specific endonuclease. Embo J 13:1235-1246
    • (1994) Embo J , vol.13 , pp. 1235-1246
    • Harrington, J.J.1    Lieber, M.R.2
  • 63
    • 0028335180 scopus 로고
    • Functional domains within FEN-1 and RAD2 define a family of structure-specific endonucleases: Implications for nucleotide excision repair
    • Harrington JJ, Lieber MR (1994b) Functional domains within FEN-1 and RAD2 define a family of structure-specific endonucleases: Implications for nucleotide excision repair. Genes Dev 8:1344-1355
    • (1994) Genes Dev , vol.8 , pp. 1344-1355
    • Harrington, J.J.1    Lieber, M.R.2
  • 64
    • 0019871821 scopus 로고
    • Structure of chromatin at deoxyribonucleic acid replication forks: Location of the first nucleosomes on newly synthesized simian virus 40 deoxyribonucleic acid
    • Herman TM, DePamphilis ML, Wassarman PM (1981) Structure of chromatin at deoxyribonucleic acid replication forks: Location of the first nucleosomes on newly synthesized simian virus 40 deoxyribonucleic acid. Biochemistry 20:621-630
    • (1981) Biochemistry , vol.20 , pp. 621-630
    • Herman, T.M.1    DePamphilis, M.L.2    Wassarman, P.M.3
  • 65
    • 15944427098 scopus 로고    scopus 로고
    • DNA polymerases alpha, delta, and epsilon localize and function together at replication forks in Saccharomyces cerevisiae
    • Hiraga S, Hagihara-Hayashi A, Ohya T, Sugino A (2005) DNA polymerases alpha, delta, and epsilon localize and function together at replication forks in Saccharomyces cerevisiae. Genes Cells 10:297-309
    • (2005) Genes Cells , vol.10 , pp. 297-309
    • Hiraga, S.1    Hagihara-Hayashi, A.2    Ohya, T.3    Sugino, A.4
  • 66
    • 0037068455 scopus 로고    scopus 로고
    • RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO
    • Hoege C, Pfander B, Moldovan GL, Pyrowolakis G, Jentsch S (2002) RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO. Nature 419:135-141
    • (2002) Nature , vol.419 , pp. 135-141
    • Hoege, C.1    Pfander, B.2    Moldovan, G.L.3    Pyrowolakis, G.4    Jentsch, S.5
  • 67
    • 0032475933 scopus 로고    scopus 로고
    • Structure of the DNA repair and replication endonuclease and exonuclease FEN-1: Coupling DNA and PCNA binding to FEN-1 activity
    • Hosfield DJ, Mol CD, Shen B, Tainer JA (1998) Structure of the DNA repair and replication endonuclease and exonuclease FEN-1: Coupling DNA and PCNA binding to FEN-1 activity. Cell 95:135-146
    • (1998) Cell , vol.95 , pp. 135-146
    • Hosfield, D.J.1    Mol, C.D.2    Shen, B.3    Tainer, J.A.4
  • 68
    • 20844453952 scopus 로고    scopus 로고
    • Structural basis for origin recognition complex 1 protein-silence information regulator 1 protein interaction in epigenetic silencing
    • Hsu HC, Stillman B, Xu RM (2005) Structural basis for origin recognition complex 1 protein-silence information regulator 1 protein interaction in epigenetic silencing. Proc Natl Acad Sci USA 102:8519-8524
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 8519-8524
    • Hsu, H.C.1    Stillman, B.2    Xu, R.M.3
  • 69
    • 0033136582 scopus 로고    scopus 로고
    • Structural organization and splice variants of the POLE1 gene encoding the catalytic subunit of human DNA polymerase epsilon
    • Huang D, Pospiech H, Kesti T, Syväoja JE (1999a) Structural organization and splice variants of the POLE1 gene encoding the catalytic subunit of human DNA polymerase epsilon. Biochem J 339:657-665
    • (1999) Biochem J , vol.339 , pp. 657-665
    • Huang, D.1    Pospiech, H.2    Kesti, T.3    Syväoja, J.E.4
  • 70
    • 0032903092 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae protein YJR043C (Pol32) interacts with the catalytic subunit of DNA polymerase alpha and is required for cell cycle progression in G2/M
    • Huang ME, Le Douarin B, Henry C, Galibert F (1999b) The Saccharomyces cerevisiae protein YJR043C (Pol32) interacts with the catalytic subunit of DNA polymerase alpha and is required for cell cycle progression in G2/ M. Mol Gen Genet 260:541-550
    • (1999) Mol Gen Genet , vol.260 , pp. 541-550
    • Huang, M.E.1    Le Douarin, B.2    Henry, C.3    Galibert, F.4
  • 73
    • 0033562536 scopus 로고    scopus 로고
    • Isolation and identification of the third subunit of mammalian DNA polymerase delta by PCNA-affinity chromatography of mouse FM3A cell extracts
    • Hughes P, Tratner I, Ducoux M, Piard K, Baldacci G (1999) Isolation and identification of the third subunit of mammalian DNA polymerase delta by PCNA-affinity chromatography of mouse FM3A cell extracts. Nucleic Acids Res 27:2108-2114
    • (1999) Nucleic Acids Res , vol.27 , pp. 2108-2114
    • Hughes, P.1    Tratner, I.2    Ducoux, M.3    Piard, K.4    Baldacci, G.5
  • 74
    • 0031873411 scopus 로고    scopus 로고
    • The crystal structure of flap endonuclease-1 from Methanococcus jannaschii
    • Hwang KY, Baek K, Kim HY, Cho Y (1998) The crystal structure of flap endonuclease-1 from Methanococcus jannaschii. Nat Struct Biol 5:707-713
    • (1998) Nat Struct Biol , vol.5 , pp. 707-713
    • Hwang, K.Y.1    Baek, K.2    Kim, H.Y.3    Cho, Y.4
  • 76
    • 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
  • 77
    • 0034659412 scopus 로고    scopus 로고
    • Xenopus cdc7 function is dependent on licensing but not on XORC, XCdc6, or CDK activity and is required for XCdc45 loading
    • Jares P, Blow JJ (2000) Xenopus cdc7 function is dependent on licensing but not on XORC, XCdc6, or CDK activity and is required for XCdc45 loading. Genes Dev 14:1528-1540
    • (2000) Genes Dev , vol.14 , pp. 1528-1540
    • Jares, P.1    Blow, J.J.2
  • 79
    • 0035943342 scopus 로고    scopus 로고
    • Crystal structure of the processivity clamp loader gamma (gamma) complex of E. coli DNA polymerase III
    • Jeruzalmi D, O'Donnell M, Kuriyan J (2001a) Crystal structure of the processivity clamp loader gamma (gamma) complex of E. coli DNA polymerase III. Cell 106:429-441
    • (2001) Cell , vol.106 , pp. 429-441
    • Jeruzalmi, D.1    O'Donnell, M.2    Kuriyan, J.3
  • 80
    • 0035943399 scopus 로고    scopus 로고
    • Mechanism of processivity clamp opening by the delta subunit wrench of the clamp loader complex of E. coli DNA polymerase III
    • Jeruzalmi D, Yurieva O, Zhao Y, Young M, Stewart J, Hingorani M, O'Donnell M, Kuriyan J (2001b) Mechanism of processivity clamp opening by the delta subunit wrench of the clamp loader complex of E. coli DNA polymerase III. Cell 106:417-428
    • (2001) Cell , vol.106 , pp. 417-428
    • Jeruzalmi, D.1    Yurieva, O.2    Zhao, Y.3    Young, M.4    Stewart, J.5    Hingorani, M.6    O'Donnell, M.7    Kuriyan, J.8
  • 81
    • 0345826100 scopus 로고    scopus 로고
    • The Pol32 subunit of DNA polymerase delta contains separable domains for processive replication and proliferating cell nuclear antigen (PCNA) binding
    • Johansson E, Garg P, Burgers PM (2004) The Pol32 subunit of DNA polymerase delta contains separable domains for processive replication and proliferating cell nuclear antigen (PCNA) binding. J Biol Chem 279:1907-1915
    • (2004) J Biol Chem , vol.279 , pp. 1907-1915
    • Johansson, E.1    Garg, P.2    Burgers, P.M.3
  • 82
    • 0035941227 scopus 로고    scopus 로고
    • Structure of DNA polymerase delta from Saccharomyces cerevisiae
    • Johansson E, Majka J, Burgers PM (2001) Structure of DNA polymerase delta from Saccharomyces cerevisiae. J Biol Chem 276:43824-43828
    • (2001) J Biol Chem , vol.276 , pp. 43824-43828
    • Johansson, E.1    Majka, J.2    Burgers, P.M.3
  • 83
    • 0031658237 scopus 로고    scopus 로고
    • Sld2, which interacts with Dpb11 in Saccharomyces cerevisiae, is required for chromosomal DNA replication
    • Kamimura Y, Masumoto H, Sugino A, Araki H (1998) Sld2, which interacts with Dpb11 in Saccharomyces cerevisiae, is required for chromosomal DNA replication. Mol Cell Biol 18:6102-6109
    • (1998) Mol Cell Biol , vol.18 , pp. 6102-6109
    • Kamimura, Y.1    Masumoto, H.2    Sugino, A.3    Araki, H.4
  • 84
    • 0035901555 scopus 로고    scopus 로고
    • Sld3, which interacts with Cdc45 (Sld4), functions for chromosomal DNA replication in Saccharomyces cerevisiae
    • Kamimura Y, Tak YS, Sugino A, Araki H (2001) Sld3, which interacts with Cdc45 (Sld4), functions for chromosomal DNA replication in Saccharomyces cerevisiae. Embo J 20:2097-2107
    • (2001) Embo J , vol.20 , pp. 2097-2107
    • Kamimura, Y.1    Tak, Y.S.2    Sugino, A.3    Araki, H.4
  • 85
    • 0033941545 scopus 로고    scopus 로고
    • Genetic analyses of Schizosaccharomyces pombe dna2(+) reveal that dna2 plays an essential role in Okazaki fragment metabolism
    • Kang HY, Choi E, Bae SH, Lee KH, Gim BS, Kim HD, Park C, MacNeill SA, Seo YS (2000) Genetic analyses of Schizosaccharomyces pombe dna2(+) reveal that dna2 plays an essential role in Okazaki fragment metabolism. Genetics 155:1055-1067
    • (2000) Genetics , vol.155 , pp. 1055-1067
    • Kang, H.Y.1    Choi, E.2    Bae, S.H.3    Lee, K.H.4    Gim, B.S.5    Kim, H.D.6    Park, C.7    MacNeill, S.A.8    Seo, Y.S.9
  • 86
    • 13944256948 scopus 로고    scopus 로고
    • Ubiquitination of PCNA and the polymerase switch in human cells
    • Kannouche PL, Lehmann AR (2004) Ubiquitination of PCNA and the polymerase switch in human cells. Cell Cycle 3:1011-1013
    • (2004) Cell Cycle , vol.3 , pp. 1011-1013
    • Kannouche, P.L.1    Lehmann, A.R.2
  • 87
    • 1642545486 scopus 로고    scopus 로고
    • The protein components and mechanism of eukaryotic Okazaki fragment maturation
    • Kao HI, Bambara RA (2003) The protein components and mechanism of eukaryotic Okazaki fragment maturation. Crit Rev Biochem Mol Biol 38:433-452
    • (2003) Crit Rev Biochem Mol Biol , vol.38 , pp. 433-452
    • Kao, H.I.1    Bambara, R.A.2
  • 88
    • 10944271787 scopus 로고    scopus 로고
    • Dna2p helicase/nuclease is a tracking protein, like FEN1, for flap cleavage during Okazaki fragment maturation
    • Kao HI, Campbell JL, Bambara RA (2004a) Dna2p helicase/nuclease is a tracking protein, like FEN1, for flap cleavage during Okazaki fragment maturation. J Biol Chem 279:50840-50849
    • (2004) J Biol Chem , vol.279 , pp. 50840-50849
    • Kao, H.I.1    Campbell, J.L.2    Bambara, R.A.3
  • 89
    • 2442601582 scopus 로고    scopus 로고
    • On the roles of Saccharomyces cerevisiae Dna2p and Flap endonuclease 1 in Okazaki fragment processing
    • Kao HI, Veeraraghavan J, Polaczek P, Campbell JL, Bambara RA (2004b) On the roles of Saccharomyces cerevisiae Dna2p and Flap endonuclease 1 in Okazaki fragment processing. J Biol Chem 279:15014-15024
    • (2004) J Biol Chem , vol.279 , pp. 15014-15024
    • Kao, H.I.1    Veeraraghavan, J.2    Polaczek, P.3    Campbell, J.L.4    Bambara, R.A.5
  • 90
    • 4143107763 scopus 로고    scopus 로고
    • Did an early version of the eukaryal replisome enable the emergence of chromatin?
    • Kaufmann G, Nethanel T (2004) Did an early version of the eukaryal replisome enable the emergence of chromatin? Prog Nucleic Acid Res Mol Biol 77:173-209
    • (2004) Prog Nucleic Acid Res Mol Biol , vol.77 , pp. 173-209
    • Kaufmann, G.1    Nethanel, T.2
  • 91
    • 0000648854 scopus 로고
    • Excision of thymine dimers and other mismatched sequences by DNA polymerase of Escherichia coli
    • 224
    • Kelly RB, Atkinson MR, Huberman JA, Kornberg A (1969) Excision of thymine dimers and other mismatched sequences by DNA polymerase of Escherichia coli. Nature 224:224, 495-501
    • (1969) Nature , vol.224 , pp. 495-501
    • Kelly, R.B.1    Atkinson, M.R.2    Huberman, J.A.3    Kornberg, A.4
  • 92
    • 0032587610 scopus 로고    scopus 로고
    • DNA polymerase ε catalytic domains are dispensable for DNA replication, DNA repair, and cell viability
    • Kesti T, Flick K, Keränen S, Syväoja JE, Wittenberg C (1999) DNA polymerase ε catalytic domains are dispensable for DNA replication, DNA repair, and cell viability. Mol Cell 3:679-685
    • (1999) Mol Cell , vol.3 , pp. 679-685
    • Kesti, T.1    Flick, K.2    Keränen, S.3    Syväoja, J.E.4    Wittenberg, C.5
  • 93
    • 0027276552 scopus 로고
    • Molecular cloning of the cDNA for the catalytic subunit of human DNA polymerase epsilon
    • Kesti T, Frantti H, Syvaoja JE (1993) Molecular cloning of the cDNA for the catalytic subunit of human DNA polymerase epsilon. J Biol Chem 268:10238-10245
    • (1993) J Biol Chem , vol.268 , pp. 10238-10245
    • Kesti, T.1    Frantti, H.2    Syvaoja, J.E.3
  • 94
    • 0037436391 scopus 로고    scopus 로고
    • Interaction and assembly of murine prereplicative complex proteins in yeast and mouse cells
    • Kneissl M, Putter V, Szalay AA, Grummt F (2003) Interaction and assembly of murine prereplicative complex proteins in yeast and mouse cells. J Mol Biol 327:111-128
    • (2003) J Mol Biol , vol.327 , pp. 111-128
    • Kneissl, M.1    Putter, V.2    Szalay, A.A.3    Grummt, F.4
  • 95
    • 0033941641 scopus 로고    scopus 로고
    • Protein fold recognition using sequence profiles and its application in structural genomics
    • Koonin EV, Wolf YI, Aravind L (2000) Protein fold recognition using sequence profiles and its application in structural genomics. Adv Protein Chem 54:245-275
    • (2000) Adv Protein Chem , vol.54 , pp. 245-275
    • Koonin, E.V.1    Wolf, Y.I.2    Aravind, L.3
  • 96
    • 0003890119 scopus 로고
    • 2nd. Edition, W.H. Freeman & Company, New York
    • Kornberg A, Baker T (1992) DNA Replication, 2nd. Edition, W.H. Freeman & Company, New York
    • (1992) DNA Replication
    • Kornberg, A.1    Baker, T.2
  • 97
    • 0028618183 scopus 로고
    • Crystal structure of the eukaryotic DNA polymerase processivity factor PCNA
    • Krishna TS, Kong XP, Gary S, Burgers PM, Kuriyan J (1994) Crystal structure of the eukaryotic DNA polymerase processivity factor PCNA. Cell 79:1233-1243
    • (1994) Cell , vol.79 , pp. 1233-1243
    • Krishna, T.S.1    Kong, X.P.2    Gary, S.3    Burgers, P.M.4    Kuriyan, J.5
  • 98
    • 0034967855 scopus 로고    scopus 로고
    • Chromatin assembly during S phase: Contributions from histone deposition, DNA replication and the cell division cycle
    • Krude T, Keller C (2001) Chromatin assembly during S phase: contributions from histone deposition, DNA replication and the cell division cycle. Cell Mol Life Sci 58:665-672
    • (2001) Cell Mol Life Sci , vol.58 , pp. 665-672
    • Krude, T.1    Keller, C.2
  • 101
    • 0032054374 scopus 로고    scopus 로고
    • In vivo gap repair in Drosophila: A one-way street with many destinations
    • Lankenau DH, Gloor GB (1998) In vivo gap repair in Drosophila: A one-way street with many destinations. BioEssays 20:317-327
    • (1998) BioEssays , vol.20 , pp. 317-327
    • Lankenau, D.H.1    Gloor, G.B.2
  • 102
    • 0037219192 scopus 로고    scopus 로고
    • A rotary pumping model for helicase function of MCM proteins at a distance from replication forks
    • Laskey RA, Madine MA (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
  • 104
    • 0035793113 scopus 로고    scopus 로고
    • Processive DNA helicase activity of the minichromosome maintenance proteins 4, 6, and 7 complex requires forked DNA structures
    • Lee JK, Hurwitz J (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
  • 105
  • 108
    • 33750143155 scopus 로고
    • T4 DNA polymerase. Methods Enzymol 29:46-53 Lei M, Tye BK (2001) Initiating DNA synthesis: From recruiting to activating the MCM complex
    • Lehman IR (1974) T4 DNA polymerase. Methods Enzymol 29:46-53 Lei M, Tye BK (2001) Initiating DNA synthesis: From recruiting to activating the MCM complex. J Cell Sci 114:1447-1454
    • (1974) J Cell Sci , vol.114 , pp. 1447-1454
    • Lehman, I.R.1
  • 109
    • 0033975419 scopus 로고    scopus 로고
    • The bacterial replicative helicase DnaB evolved from a RecA duplication
    • Leipe DD, Aravind L, Grishin NV, Koonin EV (2000) The bacterial replicative helicase DnaB evolved from a RecA duplication. Genome Res 10:5-16
    • (2000) Genome Res , vol.10 , pp. 5-16
    • Leipe, D.D.1    Aravind, L.2    Grishin, N.V.3    Koonin, E.V.4
  • 110
    • 3943086339 scopus 로고    scopus 로고
    • Flap endonuclease 1: A central component of DNA metabolism
    • Liu Y, Kao HI, Bambara RA (2004) Flap endonuclease 1: A central component of DNA metabolism. Annu Rev Biochem 73:589-615
    • (2004) Annu Rev Biochem , vol.73 , pp. 589-615
    • Liu, Y.1    Kao, H.I.2    Bambara, R.A.3
  • 111
    • 25444485251 scopus 로고    scopus 로고
    • Modulation of replication protein A function by its hyperphosphorylation-induced conformational change involving DNA binding domain B
    • Liu Y, Kvaratskhelia M, Hess S, Qu Y, Zou Y (2005) Modulation of replication protein A function by its hyperphosphorylation-induced conformational change involving DNA binding domain B. J Biol Chem 280:32775-32783
    • (2005) J Biol Chem , vol.280 , pp. 32775-32783
    • Liu, Y.1    Kvaratskhelia, M.2    Hess, S.3    Qu, Y.4    Zou, Y.5
  • 112
    • 0037025362 scopus 로고    scopus 로고
    • Direct interaction of proliferating cell nuclear antigen with the small subunit of DNA polymerase delta
    • Lu X, Tan CK, Zhou JQ, You M, Carastro LM, Downey KM, So AG (2002) Direct interaction of proliferating cell nuclear antigen with the small subunit of DNA polymerase delta. J Biol Chem 277:24340-24345
    • (2002) J Biol Chem , vol.277 , pp. 24340-24345
    • Lu, X.1    Tan, C.K.2    Zhou, J.Q.3    You, M.4    Carastro, L.M.5    Downey, K.M.6    So, A.G.7
  • 113
    • 12344254254 scopus 로고    scopus 로고
    • Characterization of a novel ATR-dependent, Chk1-independent, intra-S-phase checkpoint that suppresses initiation of replication in Xenopus
    • Luciani MG, Oehlmann M, Blow JJ (2004) Characterization of a novel ATR-dependent, Chk1-independent, intra-S-phase checkpoint that suppresses initiation of replication in Xenopus. J Cell Sci 117:6019-6030
    • (2004) J Cell Sci , vol.117 , pp. 6019-6030
    • Luciani, M.G.1    Oehlmann, M.2    Blow, J.J.3
  • 114
    • 28244461615 scopus 로고    scopus 로고
    • Identification of full genes and proteins of MCM9, a novel, vertebrate-specific member of the MCM2-8 protein family
    • Lutzmann M, Maiorano D, Mechali M (2005) Identification of full genes and proteins of MCM9, a novel, vertebrate-specific member of the MCM2-8 protein family. Gene 362:51-56
    • (2005) Gene , vol.362 , pp. 51-56
    • Lutzmann, M.1    Maiorano, D.2    Mechali, M.3
  • 115
    • 26244431903 scopus 로고    scopus 로고
    • Right place, right time, and only once: Replication initiation in metazoans
    • Machida YJ, Hamlin JL, Dutta A (2005) Right place, right time, and only once: Replication initiation in metazoans. Cell 123:13-24
    • (2005) Cell , vol.123 , pp. 13-24
    • Machida, Y.J.1    Hamlin, J.L.2    Dutta, A.3
  • 116
    • 0029811325 scopus 로고    scopus 로고
    • The fission yeast Cdc1 protein, a homologue of the small subunit of DNA polymerase delta, binds to Pol3 and Cdc27
    • MacNeill S, Moreno S, Reynolds N, Nurse P, Fantes P (1996) The fission yeast Cdc1 protein, a homologue of the small subunit of DNA polymerase delta, binds to Pol3 and Cdc27. EMBO J 15:4613-4628
    • (1996) EMBO J , vol.15 , pp. 4613-4628
    • MacNeill, S.1    Moreno, S.2    Reynolds, N.3    Nurse, P.4    Fantes, P.5
  • 117
    • 0035153648 scopus 로고    scopus 로고
    • Geminin bans replication licence
    • Madine M, Laskey R (2001) Geminin bans replication licence. Nat Cell Biol 3:E49-50
    • (2001) Nat Cell Biol , vol.3
    • Madine, M.1    Laskey, R.2
  • 118
    • 0035947571 scopus 로고    scopus 로고
    • Replication protein A as a fidelity clamp for DNA polymerase alpha
    • Maga G, Frouin I, Spadari S, Hßcher U (2001) Replication protein A as a fidelity clamp for DNA polymerase alpha. J Biol Chem 276:18235-18242
    • (2001) J Biol Chem , vol.276 , pp. 18235-18242
    • Maga, G.1    Frouin, I.2    Spadari, S.3    Hßcher, U.4
  • 119
    • 0041885325 scopus 로고    scopus 로고
    • Proliferating cell nuclear antigen (PCNA): A dancer with many partners
    • Maga G, Hübscher U (2003) Proliferating cell nuclear antigen (PCNA): a dancer with many partners. J Cell Sci 116:3051-3060
    • (2003) J Cell Sci , vol.116 , pp. 3051-3060
    • Maga, G.1    Hübscher, U.2
  • 120
    • 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, Cuvier O, Danis E, Mechali M (2005a) 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
  • 121
    • 12544258483 scopus 로고    scopus 로고
    • Recombinant Cdt1 induces rereplication of G2 nuclei in Xenopus egg extracts
    • Maiorano D, Krasinska L, Lutzmann M, Mechali M (2005b) Recombinant Cdt1 induces rereplication of G2 nuclei in Xenopus egg extracts. Curr Biol 15:146-153
    • (2005) Curr Biol , vol.15 , pp. 146-153
    • Maiorano, D.1    Krasinska, L.2    Lutzmann, M.3    Mechali, M.4
  • 122
    • 11144266855 scopus 로고    scopus 로고
    • The PCNA-RFC families of DNA clamps and clamp loaders
    • Majka J, Burgers PM (2004) The PCNA-RFC families of DNA clamps and clamp loaders. Prog Nucleic Acid Res Mol Biol 78:227-260
    • (2004) Prog Nucleic Acid Res Mol Biol , vol.78 , pp. 227-260
    • Majka, J.1    Burgers, P.M.2
  • 125
    • 19744381512 scopus 로고    scopus 로고
    • Cell division and cancer
    • Marte B (2004) Cell division and cancer. Nature 432:293
    • (2004) Nature , vol.432 , pp. 293
    • Marte, B.1
  • 126
  • 127
    • 21344442139 scopus 로고    scopus 로고
    • Control of DNA replication: Regulation and activation of eukaryotic replicative helicase, MCM
    • Masai H, You Z, Arai K (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
  • 128
    • 0035883745 scopus 로고    scopus 로고
    • Replication protein A modulates its interface with the primed DNA template during RNA-DNA primer elongation in replicating SV40 chromosomes
    • Mass G, Nethanel T, Lavrik OI, Wold MS, Kaufmann G (2001) Replication protein A modulates its interface with the primed DNA template during RNA-DNA primer elongation in replicating SV40 chromosomes. Nucleic Acids Res 29:3892-3899
    • (2001) Nucleic Acids Res , vol.29 , pp. 3892-3899
    • Mass, G.1    Nethanel, T.2    Lavrik, O.I.3    Wold, M.S.4    Kaufmann, G.5
  • 129
    • 0037034048 scopus 로고    scopus 로고
    • S-Cdk-dependent phosphorylation of Sld2 essential for chromosomal DNA replication in budding yeast
    • Masumoto H, Muramatsu S, Kamimura Y, Araki H (2002) S-Cdk-dependent phosphorylation of Sld2 essential for chromosomal DNA replication in budding yeast. Nature 415:651-655
    • (2002) Nature , vol.415 , pp. 651-655
    • Masumoto, H.1    Muramatsu, S.2    Kamimura, Y.3    Araki, H.4
  • 130
    • 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, Sugino A, Araki H (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
  • 131
    • 0346102552 scopus 로고    scopus 로고
    • REC, a new member of the MCM-related protein family, is required for meiotic recombination in Drosophila
    • Matsubayashi H, Yamamoto MT (2003) REC, a new member of the MCM-related protein family, is required for meiotic recombination in Drosophila. Genes Genet Syst 78:363- 371
    • (2003) Genes Genet Syst , vol.78 , pp. 363-371
    • Matsubayashi, H.1    Yamamoto, M.T.2
  • 132
    • 0037295722 scopus 로고    scopus 로고
    • Identification of short "eukaryotic" Okazaki fragments synthesized from a prokaryotic replication origin
    • Matsunaga F, Norais C, Forterre P, Myllykallio H (2003) Identification of short "eukaryotic" Okazaki fragments synthesized from a prokaryotic replication origin EMBO Rep 4:154-158
    • (2003) EMBO Rep , vol.4 , pp. 154-158
    • Matsunaga, F.1    Norais, C.2    Forterre, P.3    Myllykallio, H.4
  • 133
    • 0032511148 scopus 로고    scopus 로고
    • Geminin, an inhibitor of DNA replication, is degraded during mitosis
    • McGarry TJ, Kirschner MW (1998) Geminin, an inhibitor of DNA replication, is degraded during mitosis. Cell 93:1043-1053
    • (1998) Cell , vol.93 , pp. 1043-1053
    • McGarry, T.J.1    Kirschner, M.W.2
  • 134
    • 0036529624 scopus 로고    scopus 로고
    • Physical and functional interactions of the tumor suppressor protein p53 and DNA polymerase α-primase
    • Melle C, Nasheuer HP (2002) Physical and functional interactions of the tumor suppressor protein p53 and DNA polymerase α-primase. Nucleic Acids Res 30:1493-1499
    • (2002) Nucleic Acids Res , vol.30 , pp. 1493-1499
    • Melle, C.1    Nasheuer, H.P.2
  • 135
    • 0034703330 scopus 로고    scopus 로고
    • Activation of the DNA replication checkpoint through RNA synthesis by primase
    • Michael WM, Ott R, Fanning E, Newport J (2000) Activation of the DNA replication checkpoint through RNA synthesis by primase. Science 289:2133-2137
    • (2000) Science , vol.289 , pp. 2133-2137
    • Michael, W.M.1    Ott, R.2    Fanning, E.3    Newport, J.4
  • 136
    • 0033936230 scopus 로고    scopus 로고
    • Central role for cdc45 in establishing an initiation complex of DNA replication in Xenopus egg extracts
    • Mimura S, Masuda T, Matsui T, Takisawa H (2000) Central role for cdc45 in establishing an initiation complex of DNA replication in Xenopus egg extracts. Genes Cells 5:439-452
    • (2000) Genes Cells , vol.5 , pp. 439-452
    • Mimura, S.1    Masuda, T.2    Matsui, T.3    Takisawa, H.4
  • 138
    • 0032747634 scopus 로고    scopus 로고
    • Molecular architecture of the mouse DNA polymerase alpha-primase complex
    • Mizuno T, Yamagishi K, Miyazawa H, Hanaoka F (1999) Molecular architecture of the mouse DNA polymerase alpha-primase complex. Mol Cell Biol 19:7886-7896
    • (1999) Mol Cell Biol , vol.19 , pp. 7886-7896
    • Mizuno, T.1    Yamagishi, K.2    Miyazawa, H.3    Hanaoka, F.4
  • 141
    • 0033538566 scopus 로고    scopus 로고
    • Architecture of the active DNA polymerase delta.proliferating cell nuclear antigen.template-primer complex
    • Mozzherin DJ, Tan CK, Downey KM, Fisher PA (1999) Architecture of the active DNA polymerase delta.proliferating cell nuclear antigen.template-primer complex. J Biol Chem 274:19862-19867
    • (1999) J Biol Chem , vol.274 , pp. 19862-19867
    • Mozzherin, D.J.1    Tan, C.K.2    Downey, K.M.3    Fisher, P.A.4
  • 142
    • 0029616338 scopus 로고
    • Calf 5′ to 3′ exo/endonuclease must slide from a 5′ end of the substrate to perform structure-specific cleavage
    • Murante RS, Rust L, Bambara RA (1995) Calf 5′ to 3′ exo/endonuclease must slide from a 5′ end of the substrate to perform structure-specific cleavage. J Biol Chem 270:30377-30383
    • (1995) J Biol Chem , vol.270 , pp. 30377-30383
    • Murante, R.S.1    Rust, L.2    Bambara, R.A.3
  • 143
    • 0035999969 scopus 로고    scopus 로고
    • SpSld3 is required for loading and maintenance of SpCdc45 on chromatin in DNA replication in fission yeast
    • Nakajima R, Masukata H (2002) SpSld3 is required for loading and maintenance of SpCdc45 on chromatin in DNA replication in fission yeast. Mol Biol Cell 13:1462-1472
    • (2002) Mol Biol Cell , vol.13 , pp. 1462-1472
    • Nakajima, R.1    Masukata, H.2
  • 144
    • 17144365007 scopus 로고    scopus 로고
    • Proliferating cell nuclear antigen (PCNA) may function as a double homotrimer complex in the mammalian cell
    • Naryzhny SN, Zhao H, Lee H (2005) Proliferating cell nuclear antigen (PCNA) may function as a double homotrimer complex in the mammalian cell. J Biol Chem 280:13888-13894
    • (2005) J Biol Chem , vol.280 , pp. 13888-13894
    • Naryzhny, S.N.1    Zhao, H.2    Lee, H.3
  • 145
    • 0003165637 scopus 로고    scopus 로고
    • DNA ligases
    • In: DePamphilis ML (ed) Cold Spring Harbor Laboratory Press, Cold Spring Harbor Laboratory, NY, USA
    • Nash R, Lindahl T (1996) DNA ligases. In: DePamphilis ML (ed) DNA Replication in Eukaryotic Cells. Cold Spring Harbor Laboratory Press, Cold Spring Harbor Laboratory, NY, USA, p 575-586
    • (1996) DNA Replication in Eukaryotic Cells , pp. 575-586
    • Nash, R.1    Lindahl, T.2
  • 148
    • 0026701992 scopus 로고
    • Assembly of simian virus 40 Okazaki pieces from DNA primers is reversibly arrested by ATP depletion
    • Nethanel T, Zlotkin T, Kaufmann G (1992) Assembly of simian virus 40 Okazaki pieces from DNA primers is reversibly arrested by ATP depletion. J Virol 66:6634-6640
    • (1992) J Virol , vol.66 , pp. 6634-6640
    • Nethanel, T.1    Zlotkin, T.2    Kaufmann, G.3
  • 149
    • 0023931298 scopus 로고
    • DNA repair synthesis in human fibroblasts requires DNA polymerase delta
    • Nishida C, Reinhard P, Linn S (1988) DNA repair synthesis in human fibroblasts requires DNA polymerase delta. J Biol Chem 263:501-510
    • (1988) J Biol Chem , vol.263 , pp. 501-510
    • Nishida, C.1    Reinhard, P.2    Linn, S.3
  • 150
    • 2142808749 scopus 로고    scopus 로고
    • The role of Cdc6 in ensuring complete genome licensing and S phase checkpoint activation
    • Oehlmann M, Score AJ, Blow JJ (2004) The role of Cdc6 in ensuring complete genome licensing and S phase checkpoint activation. J Cell Biol 165:181-190
    • (2004) J Cell Biol , vol.165 , pp. 181-190
    • Oehlmann, M.1    Score, A.J.2    Blow, J.J.3
  • 152
    • 32444450705 scopus 로고    scopus 로고
    • Localization of MCM2-7, Cdc45, and GINS to the site of DNA unwinding during eukaryotic DNA replication
    • Pacek M, Tutter AV, Kubota Y, Takisawa H, Walter JC (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
  • 153
    • 21244449061 scopus 로고    scopus 로고
    • Crosstalk between SUMO and ubiquitin on PCNA is mediated by recruitment of the helicase Srs2p
    • Papouli E, Chen S, Davies AA, Huttner D, Krejci L, Sung P, Ulrich HD (2005) Crosstalk between SUMO and ubiquitin on PCNA is mediated by recruitment of the helicase Srs2p. Mol Cell 19:123-133
    • (2005) Mol Cell , vol.19 , pp. 123-133
    • Papouli, E.1    Chen, S.2    Davies, A.A.3    Huttner, D.4    Krejci, L.5    Sung, P.6    Ulrich, H.D.7
  • 154
    • 0242413125 scopus 로고    scopus 로고
    • Cut5 is required for the binding of Atr and DNA polymerase alpha to genotoxin-damaged chromatin
    • Parrilla-Castellar ER, Karnitz LM (2003) Cut5 is required for the binding of Atr and DNA polymerase alpha to genotoxin-damaged chromatin. J Biol Chem 278:45507-45511
    • (2003) J Biol Chem , vol.278 , pp. 45507-45511
    • Parrilla-Castellar, E.R.1    Karnitz, L.M.2
  • 155
    • 9644289536 scopus 로고    scopus 로고
    • Human DNA ligase I completely encircles and partially unwinds nicked DNA
    • Pascal JM, O'Brien PJ, Tomkinson AE, Ellenberger T (2004) Human DNA ligase I completely encircles and partially unwinds nicked DNA. Nature 432:473-478
    • (2004) Nature , vol.432 , pp. 473-478
    • Pascal, J.M.1    O'Brien, P.J.2    Tomkinson, A.E.3    Ellenberger, T.4
  • 156
    • 30944452765 scopus 로고    scopus 로고
    • Evidence that errors made by DNA polymerase alpha are corrected by DNA polymerase delta
    • Pavlov YI, Frahm C, McElhinny SA, Niimi A, Suzuki M, Kunkel TA (2006) Evidence that errors made by DNA polymerase alpha are corrected by DNA polymerase delta. Curr Biol 16:202-207
    • (2006) Curr Biol , vol.16 , pp. 202-207
    • Pavlov, Y.I.1    Frahm, C.2    McElhinny, S.A.3    Niimi, A.4    Suzuki, M.5    Kunkel, T.A.6
  • 157
    • 0037593945 scopus 로고    scopus 로고
    • Human replication protein A: The C-terminal RPA70 and the central RPA32 domains are involved in the interactions with the 3′-end of a primertemplate DNA
    • Pestryakov PE, Weisshart K, Schlott B, Khodyreva SN, Kremmer E, Grosse F, Lavrik OI, Nasheuer HP (2003) Human replication protein A: The C-terminal RPA70 and the central RPA32 domains are involved in the interactions with the 3′-end of a primertemplate DNA. J Biol Chem 278:17515-17524
    • (2003) J Biol Chem , vol.278 , pp. 17515-17524
    • Pestryakov, P.E.1    Weisshart, K.2    Schlott, B.3    Khodyreva, S.N.4    Kremmer, E.5    Grosse, F.6    Lavrik, O.I.7    Nasheuer, H.P.8
  • 158
    • 0033556238 scopus 로고    scopus 로고
    • Phosphorylation of mammalian CDC6 by Cyclin A/CDK2 regulates its subcellular localization
    • Petersen BO, Lukas J, Sørensen CS, Bartek J, Helin K (1999) Phosphorylation of mammalian CDC6 by Cyclin A/CDK2 regulates its subcellular localization. Embo J 18:396-410
    • (1999) Embo J , vol.18 , pp. 396-410
    • Petersen, B.O.1    Lukas, J.2    Sørensen, C.S.3    Bartek, J.4    Helin, K.5
  • 159
    • 22944474665 scopus 로고    scopus 로고
    • SUMO-modified PCNA recruits Srs2 to prevent recombination during S phase
    • Pfander B, Moldovan GL, Sacher M, Hoege C, Jentsch S (2005) SUMO-modified PCNA recruits Srs2 to prevent recombination during S phase. Nature 436:428-433
    • (2005) Nature , vol.436 , pp. 428-433
    • Pfander, B.1    Moldovan, G.L.2    Sacher, M.3    Hoege, C.4    Jentsch, S.5
  • 160
    • 0037040170 scopus 로고    scopus 로고
    • Reconstitution of human DNA polymerase delta using recombinant baculoviruses: The p12 subunit potentiates DNA polymerizing activity of the four-subunit enzyme
    • Podust VN, Chang LS, Ott R, Dianov GL, Fanning E (2002) Reconstitution of human DNA polymerase delta using recombinant baculoviruses: The p12 subunit potentiates DNA polymerizing activity of the four-subunit enzyme. J Biol Chem 277:3894-3901
    • (2002) J Biol Chem , vol.277 , pp. 3894-3901
    • Podust, V.N.1    Chang, L.S.2    Ott, R.3    Dianov, G.L.4    Fanning, E.5
  • 162
    • 1542601166 scopus 로고    scopus 로고
    • DNA polymerase epsilon - More than a polymerase
    • Pospiech H, Syvaoja JE (2003) DNA polymerase epsilon - more than a polymerase. Scientific World Journal 3:87-104
    • (2003) Scientific World Journal , vol.3 , pp. 87-104
    • Pospiech, H.1    Syvaoja, J.E.2
  • 163
    • 3342926035 scopus 로고    scopus 로고
    • Human Orc2 localizes to centrosomes, centromeres and heterochromatin during chromosome inheritance
    • Prasanth SG, Prasanth KV, Siddiqui K, Spector DL, Stillman B (2004) Human Orc2 localizes to centrosomes, centromeres and heterochromatin during chromosome inheritance. Embo J 23:2651-2663
    • (2004) Embo J , vol.23 , pp. 2651-2663
    • Prasanth, S.G.1    Prasanth, K.V.2    Siddiqui, K.3    Spector, D.L.4    Stillman, B.5
  • 164
    • 0037047637 scopus 로고    scopus 로고
    • Orc6 involved in DNA replication, chromosome segregation, and cytokinesis
    • Prasanth SG, Prasanth KV, Stillman B (2002) Orc6 involved in DNA replication, chromosome segregation, and cytokinesis. Science 297:1026-1031
    • (2002) Science , vol.297 , pp. 1026-1031
    • Prasanth, S.G.1    Prasanth, K.V.2    Stillman, B.3
  • 165
    • 33750108921 scopus 로고    scopus 로고
    • DNA Polymerases and Diseases
    • In: Lankenau DH (ed) Springer, Berlin Heidelberg DOI: 10.1007/7050_005
    • Ramadan K, Maga G, Hübscher U (2006) DNA Polymerases and Diseases In: Lankenau DH (ed) Genome Integrity: Facets and Perspectives, vol 1. Springer, Berlin Heidelberg DOI: 10.1007/7050_005
    • (2006) Genome Integrity: Facets and Perspectives , vol.1
    • Ramadan, K.1    Maga, G.2    Hübscher, U.3
  • 166
    • 29544435484 scopus 로고    scopus 로고
    • Sequential ATP hydrolysis by Cdc6 and ORC directs loading of the Mcm2-7 helicase
    • Randell JC, Bowers JL, Rodriguez HK, Bell SP (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
  • 167
    • 6344284782 scopus 로고    scopus 로고
    • Mcm10 regulates the stability and chromatin association of DNA polymerase-alpha
    • Ricke RM, Bielinsky AK (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
  • 168
    • 33750102798 scopus 로고    scopus 로고
    • Facing Stalled Replication Forks: The Intricacies of Doing the Right Thing
    • In: Lankenau DH (ed) Springer, Berlin Heidelberg DOI: 10.1007/7050_003
    • Rudolph C, Schürer KA, Kramer W (2006) Facing Stalled Replication Forks: The Intricacies of Doing the Right Thing. In: Lankenau DH (ed) Genome Integrity: Facets and Perspectives, vol 1. Springer, Berlin Heidelberg DOI: 10.1007/7050_003
    • (2006) Genome Integrity: Facets and Perspectives , vol.1
    • Rudolph, C.1    Schürer, K.A.2    Kramer, W.3
  • 169
    • 0028581968 scopus 로고
    • Coupling of DNA replication and mitosis by fission yeast rad4/cut5
    • Saka Y, Fantes P, Yanagida M (1994) Coupling of DNA replication and mitosis by fission yeast rad4/cut5. J Cell Sci Suppl 18:57-61
    • (1994) J Cell Sci Suppl , vol.18 , pp. 57-61
    • Saka, Y.1    Fantes, P.2    Yanagida, M.3
  • 170
    • 0002277375 scopus 로고    scopus 로고
    • Mechanisms for priming DNA synthesis
    • In: DePamphilis ML (ed) Cold Spring Harbor Laboratory Press, Cold Spring Harbor Laboratory, NY, USA
    • Salas M, Miller JT, Leis J, DePamphilis ML (1996) Mechanisms for priming DNA synthesis. In: DePamphilis ML (ed) DNA Replication in Eukaryotic Cells. Cold Spring Harbor Laboratory Press, Cold Spring Harbor Laboratory, NY, USA, p 131-176
    • (1996) DNA Replication in Eukaryotic Cells , pp. 131-176
    • Salas, M.1    Miller, J.T.2    Leis, J.3    DePamphilis, M.L.4
  • 172
    • 10444252521 scopus 로고    scopus 로고
    • Geminin-Cdt1 balance is critical for genetic stability
    • Saxena S, Dutta A (2005) Geminin-Cdt1 balance is critical for genetic stability. Mutat Res 569:111-121
    • (2005) Mutat Res , vol.569 , pp. 111-121
    • Saxena, S.1    Dutta, A.2
  • 173
    • 0035851101 scopus 로고    scopus 로고
    • Multiple phosphorylation sites of DNA polymerase α-primase cooperate to regulate the initiation of DNA replication in vitro
    • Schub O, Rohaly G, Smith RW, Schneider A, Dehde S, Dornreiter I, Nasheuer HP (2001) Multiple phosphorylation sites of DNA polymerase α-primase cooperate to regulate the initiation of DNA replication in vitro. J Biol Chem 276:38076-38083
    • (2001) J Biol Chem , vol.276 , pp. 38076-38083
    • Schub, O.1    Rohaly, G.2    Smith, R.W.3    Schneider, A.4    Dehde, S.5    Dornreiter, I.6    Nasheuer, H.P.7
  • 174
    • 0035930346 scopus 로고    scopus 로고
    • Interactions between two catalytically distinct MCM subgroups are essential for coordinated ATP hydrolysis and DNA replication
    • Schwacha A, Bell SP (2001) Interactions between two catalytically distinct MCM subgroups are essential for coordinated ATP hydrolysis and DNA replication. Mol Cell 8:1093-1104
    • (2001) Mol Cell , vol.8 , pp. 1093-1104
    • Schwacha, A.1    Bell, S.P.2
  • 175
    • 0141835018 scopus 로고    scopus 로고
    • Functions of Eukaryotic DNA Polymerases
    • (26 February 2003)
    • Shcherbakova PV, Bebenek K, Kunkel TA (2003) Functions of Eukaryotic DNA Polymerases. Sci. SAGE KE 2003:rE3 (26 February 2003) http://sageke.sciencemag.org/cgi/content/full/sageke;2003/2008/re2003
    • (2003) Sci. SAGE KE , vol.2003
    • Shcherbakova, P.V.1    Bebenek, K.2    Kunkel, T.A.3
  • 176
    • 8644219655 scopus 로고    scopus 로고
    • Living with or without cyclins and cyclin-dependent kinases
    • Sherr CJ, Roberts JM (2004) Living with or without cyclins and cyclin-dependent kinases. Genes Dev 18:2699-2711
    • (2004) Genes Dev , vol.18 , pp. 2699-2711
    • Sherr, C.J.1    Roberts, J.M.2
  • 177
    • 0037063331 scopus 로고    scopus 로고
    • Control of complex formation of DNA polymerase alpha-primase and cell-free DNA replication by the C-terminal amino acids of the largest subunit p180
    • Smith RWP, Nasheuer HP (2002) Control of complex formation of DNA polymerase alpha-primase and cell-free DNA replication by the C-terminal amino acids of the largest subunit p180. FEBS Lett 527:143-146
    • (2002) FEBS Lett , vol.527 , pp. 143-146
    • Smith, R.W.P.1    Nasheuer, H.P.2
  • 178
    • 33750135685 scopus 로고    scopus 로고
    • Role of Human Topoisomerase I in DNA Repair and Apoptosis
    • In: Lankenau DH (ed) Springer, Berlin Heidelberg DOI: 10.1007/7050_004
    • Søe K, Rockstroh A, Grosse F (2006) Role of Human Topoisomerase I in DNA Repair and Apoptosis In: Lankenau DH (ed) Genome Integrity: Facets and Perspectives, vol 1. Springer, Berlin Heidelberg DOI: 10.1007/ 7050_004
    • (2006) Genome Integrity: Facets and Perspectives , vol.1
    • Søe, K.1    Rockstroh, A.2    Grosse, F.3
  • 179
    • 29544446184 scopus 로고    scopus 로고
    • ATPase-dependent cooperative binding of ORC and Cdc6 to origin DNA
    • Speck C, Chen Z, Li H, Stillman B (2005) ATPase-dependent cooperative binding of ORC and Cdc6 to origin DNA. Nat Struct Mol Biol
    • (2005) Nat Struct Mol Biol
    • Speck, C.1    Chen, Z.2    Li, H.3    Stillman, B.4
  • 180
    • 0141831006 scopus 로고    scopus 로고
    • Control of spontaneous and damage-induced mutagenesis by SUMO and ubiquitin conjugation
    • Stelter P, Ulrich HD (2003) Control of spontaneous and damage-induced mutagenesis by SUMO and ubiquitin conjugation. Nature 425:188-191
    • (2003) Nature , vol.425 , pp. 188-191
    • Stelter, P.1    Ulrich, H.D.2
  • 181
    • 14544277626 scopus 로고    scopus 로고
    • Origin recognition and the chromosome cycle
    • Stillman B (2005) Origin recognition and the chromosome cycle. FEBS Lett 579:877-884
    • (2005) FEBS Lett , vol.579 , pp. 877-884
    • Stillman, B.1
  • 182
    • 0029129140 scopus 로고
    • Yeast DNA polymerases and their role at the replication fork
    • Sugino A (1995) Yeast DNA polymerases and their role at the replication fork. Trends Biochem Sci 20:319-323
    • (1995) Trends Biochem Sci , vol.20 , pp. 319-323
    • Sugino, A.1
  • 183
    • 0037086650 scopus 로고    scopus 로고
    • Cell cycle-dependent regulation of the association between origin recognition proteins and somatic cell chromatin
    • Sun WH, Coleman TR, DePamphilis ML (2002) Cell cycle-dependent regulation of the association between origin recognition proteins and somatic cell chromatin. Embo J 21:1437-1446
    • (2002) Embo J , vol.21 , pp. 1437-1446
    • Sun, W.H.1    Coleman, T.R.2    DePamphilis, M.L.3
  • 184
    • 0024508332 scopus 로고
    • Characterization of a large form of DNA polymerase delta from HeLa cells that is insensitive to proliferating cell nuclear antigen
    • Syväoja J, Linn S (1989) Characterization of a large form of DNA polymerase delta from HeLa cells that is insensitive to proliferating cell nuclear antigen. J Biol Chem 264:2489-2497
    • (1989) J Biol Chem , vol.264 , pp. 2489-2497
    • Syväoja, J.1    Linn, S.2
  • 186
    • 0035147434 scopus 로고    scopus 로고
    • Repression of origin assembly in metaphase depends on inhibition of RLF-B/Cdt1 by geminin
    • Tada S, Li A, Maiorano D, Mechali M, Blow JJ (2001) Repression of origin assembly in metaphase depends on inhibition of RLF-B/Cdt1 by geminin. Nat Cell Biol 3:107-113
    • (2001) Nat Cell Biol , vol.3 , pp. 107-113
    • Tada, S.1    Li, A.2    Maiorano, D.3    Mechali, M.4    Blow, J.J.5
  • 187
    • 25844447786 scopus 로고    scopus 로고
    • Cdc7-Drf1 is a developmentally regulated protein kinase required for the initiation of vertebrate DNA replication
    • Takahashi TS, Walter JC (2005) Cdc7-Drf1 is a developmentally regulated protein kinase required for the initiation of vertebrate DNA replication. Genes Dev 19:2295-2300
    • (2005) Genes Dev , vol.19 , pp. 2295-2300
    • Takahashi, T.S.1    Walter, J.C.2
  • 188
    • 0019792035 scopus 로고
    • A nuclear antigen associated with cell proliferation and blast transformation
    • Takasaki Y, Deng JS, Tan EM (1981) A nuclear antigen associated with
    • (1981) J Exp Med , vol.154 , pp. 1899-1909
    • Takasaki, Y.1    Deng, J.S.2    Tan, E.M.3
  • 189
    • 0037847620 scopus 로고    scopus 로고
    • GINS, a novel multiprotein complex required for chromosomal DNA replication in budding yeast
    • Takayama Y, Kamimura Y, Okawa M, Muramatsu S, Sugino A, Araki H (2003) GINS, a novel multiprotein complex required for chromosomal DNA replication in budding yeast. Genes Dev 17:1153-1165
    • (2003) Genes Dev , vol.17 , pp. 1153-1165
    • Takayama, Y.1    Kamimura, Y.2    Okawa, M.3    Muramatsu, S.4    Sugino, A.5    Araki, H.6
  • 190
    • 0036125511 scopus 로고    scopus 로고
    • Interdependent nuclear accumulation of budding yeast Cdt1 and Mcm2-7 during G1 phase
    • Tanaka S, Diffley JF (2002) Interdependent nuclear accumulation of budding yeast Cdt1 and Mcm2-7 during G1 phase. Nat Cell Biol 4:198-207
    • (2002) Nat Cell Biol , vol.4 , pp. 198-207
    • Tanaka, S.1    Diffley, J.F.2
  • 191
    • 0034734323 scopus 로고    scopus 로고
    • Wigley DB DNA ligases in the repair and replication of DNA
    • Timson DJ, Singleton MR, Wigley DB (2000) DNA ligases in the repair and replication of DNA. Mutat Res 460:301-318
    • (2000) Mutat Res , vol.460 , pp. 301-318
    • Timson, D.J.1    Singleton, M.R.2
  • 192
    • 0242708802 scopus 로고    scopus 로고
    • Double-stranded DNA binding properties of Saccharomyces cerevisiae DNA polymerase epsilon and of the Dpb3p-Dpb4p subassembly
    • Tsubota T, Maki S, Kubota H, Sugino A, Maki H (2003) Double-stranded DNA binding properties of Saccharomyces cerevisiae DNA polymerase epsilon and of the Dpb3p-Dpb4p subassembly. Genes Cells 8:873-888
    • (2003) Genes Cells , vol.8 , pp. 873-888
    • Tsubota, T.1    Maki, S.2    Kubota, H.3    Sugino, A.4    Maki, H.5
  • 193
    • 0032881250 scopus 로고    scopus 로고
    • MCM proteins in DNA replication
    • Tye BK (1999) MCM proteins in DNA replication. Annu Rev Biochem 68:649-686
    • (1999) Annu Rev Biochem , vol.68 , pp. 649-686
    • Tye, B.K.1
  • 194
    • 25844437172 scopus 로고    scopus 로고
    • Mutual interactions between the SUMO and ubiquitin systems: A plea of no contest
    • Ulrich HD (2005) Mutual interactions between the SUMO and ubiquitin systems: A plea of no contest. Trends Cell Biol 15:525-532
    • (2005) Trends Cell Biol , vol.15 , pp. 525-532
    • Ulrich, H.D.1
  • 195
    • 0036863542 scopus 로고    scopus 로고
    • Histone acetylation regulates the time of replication origin firing
    • Vogelauer M, Rubbi L, Lucas I, Brewer BJ, Grunstein M (2002) Histone acetylation regulates the time of replication origin firing. Mol Cell 10:1223-1233
    • (2002) Mol Cell , vol.10 , pp. 1223-1233
    • Vogelauer, M.1    Rubbi, L.2    Lucas, I.3    Brewer, B.J.4    Grunstein, M.5
  • 196
    • 13444280146 scopus 로고    scopus 로고
    • Involvement of human MCM8 in prereplication complex assembly by recruiting hcdc6 to chromatin
    • Volkening M, Hoffmann I (2005) Involvement of human MCM8 in prereplication complex assembly by recruiting hcdc6 to chromatin. Mol Cell Biol 25:1560-1568
    • (2005) Mol Cell Biol , vol.25 , pp. 1560-1568
    • Volkening, M.1    Hoffmann, I.2
  • 197
    • 0031663505 scopus 로고    scopus 로고
    • The DNA replication fork in eukaryotic cells
    • Waga S, Stillman B (1998) The DNA replication fork in eukaryotic cells. Annu Rev Biochem 67:721-751
    • (1998) Annu Rev Biochem , vol.67 , pp. 721-751
    • Waga, S.1    Stillman, B.2
  • 198
    • 0033637837 scopus 로고    scopus 로고
    • Initiation of eukaryotic DNA replication: Origin unwinding and sequential chromatin association of Cdc45, RPA, and DNA polymerase alpha
    • Walter J, Newport J (2000) Initiation of eukaryotic DNA replication: origin unwinding and sequential chromatin association of Cdc45, RPA, and DNA polymerase alpha. Mol Cell 5:617-627
    • (2000) Mol Cell , vol.5 , pp. 617-627
    • Walter, J.1    Newport, J.2
  • 199
    • 0034671935 scopus 로고    scopus 로고
    • Evidence for sequential action of cdc7 and cdk2 protein kinases during initiation of DNA replication in xenopus egg extracts
    • Walter JC (2000) Evidence for sequential action of cdc7 and cdk2 protein kinases during initiation of DNA replication in xenopus egg extracts. J Biol Chem 275:39773-39778
    • (2000) J Biol Chem , vol.275 , pp. 39773-39778
    • Walter, J.C.1
  • 200
    • 0040952809 scopus 로고    scopus 로고
    • Proteinprotein interactions of the primase subunits p58 and p48 with simian virus 40 T antigen are required for efficient primer synthesis in a cell-free system
    • Weisshart K, Förster H, Kremmer E, Schlott B, Grosse F, Nasheuer HP (2000) Proteinprotein interactions of the primase subunits p58 and p48 with simian virus 40 T antigen are required for efficient primer synthesis in a cell-free system. J Biol Chem 275:17328-17337
    • (2000) J Biol Chem , vol.275 , pp. 17328-17337
    • Weisshart, K.1    Förster, H.2    Kremmer, E.3    Schlott, B.4    Grosse, F.5    Nasheuer, H.P.6
  • 202
    • 0014749933 scopus 로고
    • Studies on deoxyribonucleic acid polymerases from yeast. 1. Parial purification and properties of two DNA polymerases from mitochondria-free cell extracts
    • Wintersberger U, Wintersberger E (1970) Studies on deoxyribonucleic acid polymerases from yeast. 1. Parial purification and properties of two DNA polymerases from mitochondria-free cell extracts. Eur J Biochem 13:11-19
    • (1970) Eur J Biochem , vol.13 , pp. 11-19
    • Wintersberger, U.1    Wintersberger, E.2
  • 204
    • 0030908093 scopus 로고    scopus 로고
    • Replication protein A: A heterotrimeric, single-stranded DNA-binding protein required for eukaryotic DNA metabolism
    • Wold MS (1997) Replication protein A: A heterotrimeric, single-stranded DNA-binding protein required for eukaryotic DNA metabolism. Annu Rev Biochem 66:61-92
    • (1997) Annu Rev Biochem , vol.66 , pp. 61-92
    • Wold, M.S.1
  • 205
    • 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
  • 206
    • 0033230401 scopus 로고    scopus 로고
    • Multiple competition reactions for RPA order the assembly of the DNA polymerase delta holoenzyme
    • Yuzhakov A, Kelman Z, Hurwitz J, O'Donnell M (1999) Multiple competition reactions for RPA order the assembly of the DNA polymerase delta holoenzyme. Embo J 18:6189-6199
    • (1999) Embo J , vol.18 , pp. 6189-6199
    • Yuzhakov, A.1    Kelman, Z.2    Hurwitz, J.3    O'Donnell, M.4
  • 207
    • 0037117724 scopus 로고    scopus 로고
    • The p58 subunit of human DNA primase is important for primer initiation, elongation, and counting
    • Zerbe LK, Kuchta RD (2002) The p58 subunit of human DNA primase is important for primer initiation, elongation, and counting. Biochemistry 41:4891-4900
    • (2002) Biochemistry , vol.41 , pp. 4891-4900
    • Zerbe, L.K.1    Kuchta, R.D.2
  • 208
    • 0028912394 scopus 로고
    • A conserved region in the amino terminus of DNA polymerase delta is involved in proliferating cell nuclear antigen binding
    • Zhang SJ, Zeng XR, Zhang P, Toomey NL, Chuang RY, Chang LS, Lee MY (1995) A conserved region in the amino terminus of DNA polymerase delta is involved in proliferating cell nuclear antigen binding. J Biol Chem 270:7988-7992
    • (1995) J Biol Chem , vol.270 , pp. 7988-7992
    • Zhang, S.J.1    Zeng, X.R.2    Zhang, P.3    Toomey, N.L.4    Chuang, R.Y.5    Chang, L.S.6    Lee, M.Y.7
  • 210
    • 0037567268 scopus 로고    scopus 로고
    • Sensing DNA damage through ATRIP recognition of RPA-ssDNA complexes
    • Zou L, Elledge SJ (2003) Sensing DNA damage through ATRIP recognition of RPA-ssDNA complexes. Science 300:1542-1548
    • (2003) Science , vol.300 , pp. 1542-1548
    • Zou, L.1    Elledge, S.J.2


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