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Volumn 129, Issue 4, 2007, Pages 665-679

PCNA, the Maestro of the Replication Fork

Author keywords

[No Author keywords available]

Indexed keywords

CYCLINE; DNA POLYMERASE;

EID: 34249066085     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cell.2007.05.003     Document Type: Review
Times cited : (1440)

References (105)
  • 2
    • 30344455639 scopus 로고    scopus 로고
    • PCNA functions as a molecular platform to trigger Cdt1 destruction and prevent re-replication
    • Arias E.E., and Walter J.C. PCNA functions as a molecular platform to trigger Cdt1 destruction and prevent re-replication. Nat. Cell Biol. 8 (2006) 84-90
    • (2006) Nat. Cell Biol. , vol.8 , pp. 84-90
    • Arias, E.E.1    Walter, J.C.2
  • 3
    • 0035951829 scopus 로고    scopus 로고
    • Interaction of CR6 (GADD45gamma) with proliferating cell nuclear antigen impedes negative growth control
    • Azam N., Vairapandi M., Zhang W., Hoffman B., and Liebermann D.A. Interaction of CR6 (GADD45gamma) with proliferating cell nuclear antigen impedes negative growth control. J. Biol. Chem. 276 (2001) 2766-2774
    • (2001) J. Biol. Chem. , vol.276 , pp. 2766-2774
    • Azam, N.1    Vairapandi, M.2    Zhang, W.3    Hoffman, B.4    Liebermann, D.A.5
  • 4
    • 33747823839 scopus 로고    scopus 로고
    • L2DTL/CDT2 and PCNA interact with p53 and regulate p53 polyubiquitination and protein stability through MDM2 and CUL4A/DDB1 complexes
    • Banks D., Wu M., Higa L.A., Gavrilova N., Quan J., Ye T., Kobayashi R., Sun H., and Zhang H. L2DTL/CDT2 and PCNA interact with p53 and regulate p53 polyubiquitination and protein stability through MDM2 and CUL4A/DDB1 complexes. Cell Cycle 5 (2006) 1719-1729
    • (2006) Cell Cycle , vol.5 , pp. 1719-1729
    • Banks, D.1    Wu, M.2    Higa, L.A.3    Gavrilova, N.4    Quan, J.5    Ye, T.6    Kobayashi, R.7    Sun, H.8    Zhang, H.9
  • 5
    • 0345276624 scopus 로고    scopus 로고
    • Regulation of alternative replication bypass pathways at stalled replication forks and its effects on genome stability: a yeast model
    • Barbour L., and Xiao W. Regulation of alternative replication bypass pathways at stalled replication forks and its effects on genome stability: a yeast model. Mutat. Res. 532 (2003) 137-155
    • (2003) Mutat. Res. , vol.532 , pp. 137-155
    • Barbour, L.1    Xiao, W.2
  • 6
    • 0035997368 scopus 로고    scopus 로고
    • DNA replication in eukaryotic cells
    • Bell S.P., and Dutta A. 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
  • 8
    • 0036144048 scopus 로고    scopus 로고
    • DNA methylation patterns and epigenetic memory
    • Bird A. DNA methylation patterns and epigenetic memory. Genes Dev. 16 (2002) 6-21
    • (2002) Genes Dev. , vol.16 , pp. 6-21
    • Bird, A.1
  • 9
    • 3042588011 scopus 로고    scopus 로고
    • Structural analysis of a eukaryotic sliding DNA clamp-clamp loader complex
    • Bowman G.D., O'Donnell M., and Kuriyan J. 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    O'Donnell, M.2    Kuriyan, J.3
  • 10
    • 9944227232 scopus 로고    scopus 로고
    • Structural and thermodynamic analysis of human PCNA with peptides derived from DNA polymerase-delta p66 subunit and flap endonuclease-1
    • Bruning J.B., and Shamoo Y. Structural and thermodynamic analysis of human PCNA with peptides derived from DNA polymerase-delta p66 subunit and flap endonuclease-1. Structure 12 (2004) 2209-2219
    • (2004) Structure , vol.12 , pp. 2209-2219
    • Bruning, J.B.1    Shamoo, Y.2
  • 11
    • 20744435871 scopus 로고    scopus 로고
    • Replication protein A-directed unloading of PCNA by the Ctf18 cohesion establishment complex
    • Bylund G.O., and Burgers P.M. Replication protein A-directed unloading of PCNA by the Ctf18 cohesion establishment complex. Mol. Cell. Biol. 25 (2005) 5445-5455
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 5445-5455
    • Bylund, G.O.1    Burgers, P.M.2
  • 12
    • 0742321956 scopus 로고    scopus 로고
    • Structural basis for FEN-1 substrate specificity and PCNA-mediated activation in DNA replication and repair
    • Chapados B.R., Hosfield D.J., Han S., Qiu J., Yelent B., Shen B., and Tainer J.A. Structural basis for FEN-1 substrate specificity and PCNA-mediated activation in DNA replication and repair. Cell 116 (2004) 39-50
    • (2004) Cell , vol.116 , pp. 39-50
    • Chapados, B.R.1    Hosfield, D.J.2    Han, S.3    Qiu, J.4    Yelent, B.5    Shen, B.6    Tainer, J.A.7
  • 13
    • 27444433046 scopus 로고    scopus 로고
    • Proliferating cell nuclear antigen recruits cyclin-dependent kinase inhibitor Xic1 to DNA and couples its proteolysis to DNA polymerase switching
    • Chuang L.C., and Yew P.R. Proliferating cell nuclear antigen recruits cyclin-dependent kinase inhibitor Xic1 to DNA and couples its proteolysis to DNA polymerase switching. J. Biol. Chem. 280 (2005) 35299-35309
    • (2005) J. Biol. Chem. , vol.280 , pp. 35299-35309
    • Chuang, L.C.1    Yew, P.R.2
  • 14
    • 0030770835 scopus 로고    scopus 로고
    • Human DNA-(cytosine-5) methyltransferase-PCNA complex as a target for p21WAF1
    • Chuang L.S., Ian H.I., Koh T.W., Ng H.H., Xu G., and Li B.F. Human DNA-(cytosine-5) methyltransferase-PCNA complex as a target for p21WAF1. Science 277 (1997) 1996-2000
    • (1997) Science , vol.277 , pp. 1996-2000
    • Chuang, L.S.1    Ian, H.I.2    Koh, T.W.3    Ng, H.H.4    Xu, G.5    Li, B.F.6
  • 15
    • 4544221279 scopus 로고    scopus 로고
    • Regulation of early events in chromosome replication
    • Diffley J.F. Regulation of early events in chromosome replication. Curr. Biol. 14 (2004) R778-R786
    • (2004) Curr. Biol. , vol.14
    • Diffley, J.F.1
  • 16
    • 0037251411 scopus 로고    scopus 로고
    • A heterotrimeric PCNA in the hyperthermophilic archaeon Sulfolobus solfataricus
    • Dionne I., Nookala R.K., Jackson S.P., Doherty A.J., and Bell S.D. A heterotrimeric PCNA in the hyperthermophilic archaeon Sulfolobus solfataricus. Mol. Cell 11 (2003) 275-282
    • (2003) Mol. Cell , vol.11 , pp. 275-282
    • Dionne, I.1    Nookala, R.K.2    Jackson, S.P.3    Doherty, A.J.4    Bell, S.D.5
  • 17
    • 0034738420 scopus 로고    scopus 로고
    • p21(WAF1/Cip1): more than a break to the cell cycle?
    • Dotto G.P. p21(WAF1/Cip1): more than a break to the cell cycle?. Biochim. Biophys. Acta 1471 (2000) M43-M56
    • (2000) Biochim. Biophys. Acta , vol.1471
    • Dotto, G.P.1
  • 18
    • 0035966116 scopus 로고    scopus 로고
    • Mediation of proliferating cell nuclear antigen (PCNA)-dependent DNA replication through a conserved p21(Cip1)-like PCNA-binding motif present in the third subunit of human DNA polymerase delta
    • Ducoux M., Urbach S., Baldacci G., Hubscher U., Koundrioukoff S., Christensen J., and Hughes P. Mediation of proliferating cell nuclear antigen (PCNA)-dependent DNA replication through a conserved p21(Cip1)-like PCNA-binding motif present in the third subunit of human DNA polymerase delta. J. Biol. Chem. 276 (2001) 49258-49266
    • (2001) J. Biol. Chem. , vol.276 , pp. 49258-49266
    • Ducoux, M.1    Urbach, S.2    Baldacci, G.3    Hubscher, U.4    Koundrioukoff, S.5    Christensen, J.6    Hughes, P.7
  • 21
    • 19444383801 scopus 로고    scopus 로고
    • Trading places: how do DNA polymerases switch during translesion DNA synthesis?
    • Friedberg E.C., Lehmann A.R., and Fuchs R.P. Trading places: how do DNA polymerases switch during translesion DNA synthesis?. Mol. Cell 18 (2005) 499-505
    • (2005) Mol. Cell , vol.18 , pp. 499-505
    • Friedberg, E.C.1    Lehmann, A.R.2    Fuchs, R.P.3
  • 22
  • 23
    • 0032912468 scopus 로고    scopus 로고
    • Role of Saccharomyces cerevisiae chromatin assembly factor-I in repair of ultraviolet radiation damage in vivo
    • Game J.C., and Kaufman P.D. Role of Saccharomyces cerevisiae chromatin assembly factor-I in repair of ultraviolet radiation damage in vivo. Genetics 151 (1999) 485-497
    • (1999) Genetics , vol.151 , pp. 485-497
    • Game, J.C.1    Kaufman, P.D.2
  • 24
    • 18044384092 scopus 로고    scopus 로고
    • DNA polymerases that propagate the eukaryotic DNA replication fork
    • Garg P., and Burgers P.M. DNA polymerases that propagate the eukaryotic DNA replication fork. Crit. Rev. Biochem. Mol. Biol. 40 (2005) 115-128
    • (2005) Crit. Rev. Biochem. Mol. Biol. , vol.40 , pp. 115-128
    • Garg, P.1    Burgers, P.M.2
  • 25
    • 29444454665 scopus 로고    scopus 로고
    • Ubiquitinated proliferating cell nuclear antigen activates translesion DNA polymerases eta and REV1
    • Garg P., and Burgers P.M. Ubiquitinated proliferating cell nuclear antigen activates translesion DNA polymerases eta and REV1. Proc. Natl. Acad. Sci. USA 102 (2005) 18361-18366
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 18361-18366
    • Garg, P.1    Burgers, P.M.2
  • 26
    • 8644285427 scopus 로고    scopus 로고
    • Idling by DNA polymerase delta maintains a ligatable nick during lagging-strand DNA replication
    • Garg P., Stith C.M., Sabouri N., Johansson E., and Burgers P.M. Idling by DNA polymerase delta maintains a ligatable nick during lagging-strand DNA replication. Genes Dev. 18 (2004) 2764-2773
    • (2004) Genes Dev. , vol.18 , pp. 2764-2773
    • Garg, P.1    Stith, C.M.2    Sabouri, N.3    Johansson, E.4    Burgers, P.M.5
  • 27
    • 0030767281 scopus 로고    scopus 로고
    • The DNA repair endonuclease XPG binds to proliferating cell nuclear antigen (PCNA) and shares sequence elements with the PCNA-binding regions of FEN-1 and cyclin-dependent kinase inhibitor p21
    • Gary R., Ludwig D.L., Cornelius H.L., MacInnes M.A., and Park M.S. The DNA repair endonuclease XPG binds to proliferating cell nuclear antigen (PCNA) and shares sequence elements with the PCNA-binding regions of FEN-1 and cyclin-dependent kinase inhibitor p21. J. Biol. Chem. 272 (1997) 24522-24529
    • (1997) J. Biol. Chem. , vol.272 , pp. 24522-24529
    • Gary, R.1    Ludwig, D.L.2    Cornelius, H.L.3    MacInnes, M.A.4    Park, M.S.5
  • 28
    • 0035860719 scopus 로고    scopus 로고
    • ATP utilization by yeast replication factor C. I. ATP-mediated interaction with DNA and with proliferating cell nuclear antigen
    • Gomes X.V., and Burgers P.M. ATP utilization by yeast replication factor C. I. ATP-mediated interaction with DNA and with proliferating cell nuclear antigen. J. Biol. Chem. 276 (2001) 34768-34775
    • (2001) J. Biol. Chem. , vol.276 , pp. 34768-34775
    • Gomes, X.V.1    Burgers, P.M.2
  • 30
    • 0030592544 scopus 로고    scopus 로고
    • Structure of the C-terminal region of p21(WAF1/CIP1) complexed with human PCNA
    • Gulbis J.M., Kelman Z., Hurwitz J., O'Donnell M., and Kuriyan J. Structure of the C-terminal region of p21(WAF1/CIP1) complexed with human PCNA. Cell 87 (1996) 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
  • 32
    • 33646254420 scopus 로고    scopus 로고
    • Ubiquitylation of yeast proliferating cell nuclear antigen and its implications for translesion DNA synthesis
    • Haracska L., Unk I., Prakash L., and Prakash S. Ubiquitylation of yeast proliferating cell nuclear antigen and its implications for translesion DNA synthesis. Proc. Natl. Acad. Sci. USA 103 (2006) 6477-6482
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 6477-6482
    • Haracska, L.1    Unk, I.2    Prakash, L.3    Prakash, S.4
  • 33
    • 0035869074 scopus 로고    scopus 로고
    • Transcription coactivator p300 binds PCNA and may have a role in DNA repair synthesis
    • Hasan S., Hassa P.O., Imhof R., and Hottiger M.O. Transcription coactivator p300 binds PCNA and may have a role in DNA repair synthesis. Nature 410 (2001) 387-391
    • (2001) Nature , vol.410 , pp. 387-391
    • Hasan, S.1    Hassa, P.O.2    Imhof, R.3    Hottiger, M.O.4
  • 34
    • 33644850958 scopus 로고    scopus 로고
    • Heterochromatin protein 1: don't judge the book by its cover!
    • Hediger F., and Gasser S.M. Heterochromatin protein 1: don't judge the book by its cover!. Curr. Opin. Genet. Dev. 16 (2006) 143-150
    • (2006) Curr. Opin. Genet. Dev. , vol.16 , pp. 143-150
    • Hediger, F.1    Gasser, S.M.2
  • 35
    • 25444495672 scopus 로고    scopus 로고
    • Evidence that DNA damage detection machinery participates in DNA repair
    • Helt C.E., Wang W., Keng P.C., and Bambara R.A. Evidence that DNA damage detection machinery participates in DNA repair. Cell Cycle 4 (2005) 529-532
    • (2005) Cell Cycle , vol.4 , pp. 529-532
    • Helt, C.E.1    Wang, W.2    Keng, P.C.3    Bambara, R.A.4
  • 36
    • 0042804874 scopus 로고    scopus 로고
    • Phosphorylation of human Fen1 by cyclin-dependent kinase modulates its role in replication fork regulation
    • Henneke G., Koundrioukoff S., and Hubscher U. Phosphorylation of human Fen1 by cyclin-dependent kinase modulates its role in replication fork regulation. Oncogene 22 (2003) 4301-4313
    • (2003) Oncogene , vol.22 , pp. 4301-4313
    • Henneke, G.1    Koundrioukoff, S.2    Hubscher, U.3
  • 37
    • 9744251005 scopus 로고    scopus 로고
    • Biochemistry and biology of mammalian DNA methyltransferases
    • Hermann A., Gowher H., and Jeltsch A. Biochemistry and biology of mammalian DNA methyltransferases. Cell. Mol. Life Sci. 61 (2004) 2571-2587
    • (2004) Cell. Mol. Life Sci. , vol.61 , pp. 2571-2587
    • Hermann, A.1    Gowher, H.2    Jeltsch, A.3
  • 38
    • 0037068455 scopus 로고    scopus 로고
    • RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO
    • Hoege C., Pfander B., Moldovan G.L., Pyrowolakis G., and Jentsch S. RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO. Nature 419 (2002) 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
  • 41
    • 0036785210 scopus 로고    scopus 로고
    • PCNA clamp facilitates action of DNA cytosine methyltransferase 1 on hemimethylated DNA
    • Iida T., Suetake I., Tajima S., Morioka H., Ohta S., Obuse C., and Tsurimoto T. PCNA clamp facilitates action of DNA cytosine methyltransferase 1 on hemimethylated DNA. Genes Cells 7 (2002) 997-1007
    • (2002) Genes Cells , vol.7 , pp. 997-1007
    • Iida, T.1    Suetake, I.2    Tajima, S.3    Morioka, H.4    Ohta, S.5    Obuse, C.6    Tsurimoto, T.7
  • 42
    • 0023236126 scopus 로고
    • The yeast DNA repair gene RAD6 encodes a ubiquitin-conjugating enzyme
    • Jentsch S., McGrath J.P., and Varshavsky A. The yeast DNA repair gene RAD6 encodes a ubiquitin-conjugating enzyme. Nature 329 (1987) 131-134
    • (1987) Nature , vol.329 , pp. 131-134
    • Jentsch, S.1    McGrath, J.P.2    Varshavsky, A.3
  • 43
    • 33646187811 scopus 로고    scopus 로고
    • The multifaceted mismatch-repair system
    • Jiricny J. The multifaceted mismatch-repair system. Nat. Rev. Mol. Cell Biol. 7 (2006) 335-346
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 335-346
    • Jiricny, J.1
  • 44
    • 22244478079 scopus 로고    scopus 로고
    • Cellular DNA replicases: components and dynamics at the replication fork
    • Johnson A., and O'Donnell M. Cellular DNA replicases: components and dynamics at the replication fork. Annu. Rev. Biochem. 74 (2005) 283-315
    • (2005) Annu. Rev. Biochem. , vol.74 , pp. 283-315
    • Johnson, A.1    O'Donnell, M.2
  • 45
    • 0039710446 scopus 로고    scopus 로고
    • Regulation of DNA replication and repair proteins through interaction with the front side of proliferating cell nuclear antigen
    • Jonsson Z.O., Hindges R., and Hubscher U. Regulation of DNA replication and repair proteins through interaction with the front side of proliferating cell nuclear antigen. EMBO J. 17 (1998) 2412-2425
    • (1998) EMBO J. , vol.17 , pp. 2412-2425
    • Jonsson, Z.O.1    Hindges, R.2    Hubscher, U.3
  • 46
    • 33746189409 scopus 로고    scopus 로고
    • Endonucleolytic function of MutLalpha in human mismatch repair
    • Kadyrov F.A., Dzantiev L., Constantin N., and Modrich P. Endonucleolytic function of MutLalpha in human mismatch repair. Cell 126 (2006) 297-308
    • (2006) Cell , vol.126 , pp. 297-308
    • Kadyrov, F.A.1    Dzantiev, L.2    Constantin, N.3    Modrich, P.4
  • 47
    • 2442417331 scopus 로고    scopus 로고
    • Interaction of human DNA polymerase eta with monoubiquitinated PCNA: a possible mechanism for the polymerase switch in response to DNA damage
    • Kannouche P.L., Wing J., and Lehmann A.R. Interaction of human DNA polymerase eta with monoubiquitinated PCNA: a possible mechanism for the polymerase switch in response to DNA damage. Mol. Cell 14 (2004) 491-500
    • (2004) Mol. Cell , vol.14 , pp. 491-500
    • Kannouche, P.L.1    Wing, J.2    Lehmann, A.R.3
  • 48
    • 27844555425 scopus 로고    scopus 로고
    • Physical and functional interaction of human nuclear uracil-DNA glycosylase with proliferating cell nuclear antigen
    • Ko R., and Bennett S.E. Physical and functional interaction of human nuclear uracil-DNA glycosylase with proliferating cell nuclear antigen. DNA Repair (Amst.) 4 (2005) 1421-1431
    • (2005) DNA Repair (Amst.) , vol.4 , pp. 1421-1431
    • Ko, R.1    Bennett, S.E.2
  • 49
    • 0034725635 scopus 로고    scopus 로고
    • A direct interaction between proliferating cell nuclear antigen (PCNA) and Cdk2 targets PCNA-interacting proteins for phosphorylation
    • Koundrioukoff S., Jonsson Z.O., Hasan S., de Jong R.N., van der Vliet P.C., Hottiger M.O., and Hubscher U. A direct interaction between proliferating cell nuclear antigen (PCNA) and Cdk2 targets PCNA-interacting proteins for phosphorylation. J. Biol. Chem. 275 (2000) 22882-22887
    • (2000) J. Biol. Chem. , vol.275 , pp. 22882-22887
    • Koundrioukoff, S.1    Jonsson, Z.O.2    Hasan, S.3    de Jong, R.N.4    van der Vliet, P.C.5    Hottiger, M.O.6    Hubscher, U.7
  • 50
    • 0036135016 scopus 로고    scopus 로고
    • Chromatin assembly factor I mutants defective for PCNA binding require Asf1/Hir proteins for silencing
    • Krawitz D.C., Kama T., and Kaufman P.D. Chromatin assembly factor I mutants defective for PCNA binding require Asf1/Hir proteins for silencing. Mol. Cell. Biol. 22 (2002) 614-625
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 614-625
    • Krawitz, D.C.1    Kama, T.2    Kaufman, P.D.3
  • 51
    • 0028100764 scopus 로고
    • Crystallization of proliferating cell nuclear antigen (PCNA) from Saccharomyces cerevisiae
    • Krishna T.S., Fenyo D., Kong X.P., Gary S., Chait B.T., Burgers P., and Kuriyan J. Crystallization of proliferating cell nuclear antigen (PCNA) from Saccharomyces cerevisiae. J. Mol. Biol. 241 (1994) 265-268
    • (1994) J. Mol. Biol. , vol.241 , pp. 265-268
    • Krishna, T.S.1    Fenyo, D.2    Kong, X.P.3    Gary, S.4    Chait, B.T.5    Burgers, P.6    Kuriyan, J.7
  • 52
    • 20444424939 scopus 로고    scopus 로고
    • Gross chromosomal rearrangements and elevated recombination at an inducible site-specific replication fork barrier
    • Lambert S., Watson A., Sheedy D.M., Martin B., and Carr A.M. Gross chromosomal rearrangements and elevated recombination at an inducible site-specific replication fork barrier. Cell 121 (2005) 689-702
    • (2005) Cell , vol.121 , pp. 689-702
    • Lambert, S.1    Watson, A.2    Sheedy, D.M.3    Martin, B.4    Carr, A.M.5
  • 53
    • 29144501653 scopus 로고    scopus 로고
    • Ubiquitin/SUMO modification of PCNA promotes replication fork progression in Xenopus laevis egg extracts
    • Leach C.A., and Michael W.M. Ubiquitin/SUMO modification of PCNA promotes replication fork progression in Xenopus laevis egg extracts. J. Cell Biol. 171 (2005) 947-954
    • (2005) J. Cell Biol. , vol.171 , pp. 947-954
    • Leach, C.A.1    Michael, W.M.2
  • 54
    • 28844442919 scopus 로고    scopus 로고
    • Analysis of interactions between mismatch repair initiation factors and the replication processivity factor PCNA
    • Lee S.D., and Alani E. Analysis of interactions between mismatch repair initiation factors and the replication processivity factor PCNA. J. Mol. Biol. 355 (2006) 175-184
    • (2006) J. Mol. Biol. , vol.355 , pp. 175-184
    • Lee, S.D.1    Alani, E.2
  • 55
    • 29544437558 scopus 로고    scopus 로고
    • Multiple mechanisms control chromosome integrity after replication fork uncoupling and restart at irreparable UV lesions
    • Lopes M., Foiani M., and Sogo J.M. Multiple mechanisms control chromosome integrity after replication fork uncoupling and restart at irreparable UV lesions. Mol. Cell 21 (2006) 15-27
    • (2006) Mol. Cell , vol.21 , pp. 15-27
    • Lopes, M.1    Foiani, M.2    Sogo, J.M.3
  • 56
    • 11144266855 scopus 로고    scopus 로고
    • The PCNA-RFC families of DNA clamps and clamp loaders
    • Majka J., and Burgers P.M. The PCNA-RFC families of DNA clamps and clamp loaders. Prog. Nucleic Acid Res. Mol. Biol. 78 (2004) 227-260
    • (2004) Prog. Nucleic Acid Res. Mol. Biol. , vol.78 , pp. 227-260
    • Majka, J.1    Burgers, P.M.2
  • 57
    • 0037036465 scopus 로고    scopus 로고
    • Proliferating cell nuclear antigen associates with histone deacetylase activity, integrating DNA replication and chromatin modification
    • Milutinovic S., Zhuang Q., and Szyf M. Proliferating cell nuclear antigen associates with histone deacetylase activity, integrating DNA replication and chromatin modification. J. Biol. Chem. 277 (2002) 20974-20978
    • (2002) J. Biol. Chem. , vol.277 , pp. 20974-20978
    • Milutinovic, S.1    Zhuang, Q.2    Szyf, M.3
  • 58
    • 33750083332 scopus 로고    scopus 로고
    • Mechanisms in eukaryotic mismatch repair
    • Modrich P. Mechanisms in eukaryotic mismatch repair. J. Biol. Chem. 281 (2006) 30305-30309
    • (2006) J. Biol. Chem. , vol.281 , pp. 30305-30309
    • Modrich, P.1
  • 59
    • 33747882922 scopus 로고    scopus 로고
    • PCNA Controls Establishment of Sister Chromatid Cohesion during S Phase
    • Moldovan G.L., Pfander B., and Jentsch S. PCNA Controls Establishment of Sister Chromatid Cohesion during S Phase. Mol. Cell 23 (2006) 723-732
    • (2006) Mol. Cell , vol.23 , pp. 723-732
    • Moldovan, G.L.1    Pfander, B.2    Jentsch, S.3
  • 60
    • 0032126647 scopus 로고    scopus 로고
    • DNA ligase I is recruited to sites of DNA replication by an interaction with proliferating cell nuclear antigen: identification of a common targeting mechanism for the assembly of replication factories
    • Montecucco A., Rossi R., Levin D.S., Gary R., Park M.S., Motycka T.A., Ciarrocchi G., Villa A., Biamonti G., and Tomkinson A.E. DNA ligase I is recruited to sites of DNA replication by an interaction with proliferating cell nuclear antigen: identification of a common targeting mechanism for the assembly of replication factories. EMBO J. 17 (1998) 3786-3795
    • (1998) EMBO J. , vol.17 , pp. 3786-3795
    • Montecucco, A.1    Rossi, R.2    Levin, D.S.3    Gary, R.4    Park, M.S.5    Motycka, T.A.6    Ciarrocchi, G.7    Villa, A.8    Biamonti, G.9    Tomkinson, A.E.10
  • 62
    • 33947127598 scopus 로고    scopus 로고
    • The histone chaperone Asf1 at the crossroads of chromatin and DNA checkpoint pathways
    • Mousson F., Ochsenbein F., and Mann C. The histone chaperone Asf1 at the crossroads of chromatin and DNA checkpoint pathways. Chromosoma 116 (2006) 79-93
    • (2006) Chromosoma , vol.116 , pp. 79-93
    • Mousson, F.1    Ochsenbein, F.2    Mann, C.3
  • 63
    • 0033212963 scopus 로고    scopus 로고
    • Heterochromatin dynamics in mouse cells: interaction between chromatin assembly factor 1 and HP1 proteins
    • Murzina N., Verreault A., Laue E., and Stillman B. Heterochromatin dynamics in mouse cells: interaction between chromatin assembly factor 1 and HP1 proteins. Mol. Cell 4 (1999) 529-540
    • (1999) Mol. Cell , vol.4 , pp. 529-540
    • Murzina, N.1    Verreault, A.2    Laue, E.3    Stillman, B.4
  • 64
    • 22244481613 scopus 로고    scopus 로고
    • The structure and function of SMC and kleisin complexes
    • Nasmyth K., and Haering C.H. The structure and function of SMC and kleisin complexes. Annu. Rev. Biochem. 74 (2005) 595-648
    • (2005) Annu. Rev. Biochem. , vol.74 , pp. 595-648
    • Nasmyth, K.1    Haering, C.H.2
  • 65
    • 0031865131 scopus 로고    scopus 로고
    • Functional sites of human PCNA which interact with p21 (Cip1/Waf1), DNA polymerase delta and replication factor C
    • Oku T., Ikeda S., Sasaki H., Fukuda K., Morioka H., Ohtsuka E., Yoshikawa H., and Tsurimoto T. Functional sites of human PCNA which interact with p21 (Cip1/Waf1), DNA polymerase delta and replication factor C. Genes Cells 3 (1998) 357-369
    • (1998) Genes Cells , vol.3 , pp. 357-369
    • Oku, T.1    Ikeda, S.2    Sasaki, H.3    Fukuda, K.4    Morioka, H.5    Ohtsuka, E.6    Yoshikawa, H.7    Tsurimoto, T.8
  • 68
    • 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 A.A., Huttner D., Krejci L., Sung P., and Ulrich H.D. Crosstalk between SUMO and ubiquitin on PCNA is mediated by recruitment of the helicase Srs2p. Mol. Cell 19 (2005) 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
  • 69
    • 9644289536 scopus 로고    scopus 로고
    • Human DNA ligase I completely encircles and partially unwinds nicked DNA
    • Pascal J.M., O'Brien P.J., Tomkinson A.E., and Ellenberger T. Human DNA ligase I completely encircles and partially unwinds nicked DNA. Nature 432 (2004) 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
  • 71
    • 22944474665 scopus 로고    scopus 로고
    • SUMO-modified PCNA recruits Srs2 to prevent recombination during S phase
    • Pfander B., Moldovan G.L., Sacher M., Hoege C., and Jentsch S. SUMO-modified PCNA recruits Srs2 to prevent recombination during S phase. Nature 436 (2005) 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
  • 73
    • 33644866511 scopus 로고    scopus 로고
    • Chromatin assembly: a basic recipe with various flavours
    • Polo S.E., and Almouzni G. Chromatin assembly: a basic recipe with various flavours. Curr. Opin. Genet. Dev. 16 (2006) 104-111
    • (2006) Curr. Opin. Genet. Dev. , vol.16 , pp. 104-111
    • Polo, S.E.1    Almouzni, G.2
  • 75
    • 0346461412 scopus 로고    scopus 로고
    • Distinct pools of proliferating cell nuclear antigen associated to DNA replication sites interact with the p125 subunit of DNA polymerase delta or DNA ligase I
    • Riva F., Savio M., Cazzalini O., Stivala L.A., Scovassi I.A., Cox L.S., Ducommun B., and Prosperi E. Distinct pools of proliferating cell nuclear antigen associated to DNA replication sites interact with the p125 subunit of DNA polymerase delta or DNA ligase I. Exp. Cell Res. 293 (2004) 357-367
    • (2004) Exp. Cell Res. , vol.293 , pp. 357-367
    • Riva, F.1    Savio, M.2    Cazzalini, O.3    Stivala, L.A.4    Scovassi, I.A.5    Cox, L.S.6    Ducommun, B.7    Prosperi, E.8
  • 76
    • 0033609369 scopus 로고    scopus 로고
    • Growth inhibition by CDK-cyclin and PCNA binding domains of p21 occurs by distinct mechanisms and is regulated by ubiquitin-proteasome pathway
    • Rousseau D., Cannella D., Boulaire J., Fitzgerald P., Fotedar A., and Fotedar R. Growth inhibition by CDK-cyclin and PCNA binding domains of p21 occurs by distinct mechanisms and is regulated by ubiquitin-proteasome pathway. Oncogene 18 (1999) 4313-4325
    • (1999) Oncogene , vol.18 , pp. 4313-4325
    • Rousseau, D.1    Cannella, D.2    Boulaire, J.3    Fitzgerald, P.4    Fotedar, A.5    Fotedar, R.6
  • 77
    • 33644616440 scopus 로고    scopus 로고
    • The 9-1-1 checkpoint clamp physically interacts with polzeta and is partially required for spontaneous polzeta-dependent mutagenesis in Saccharomyces cerevisiae
    • Sabbioneda S., Minesinger B.K., Giannattasio M., Plevani P., Muzi-Falconi M., and Jinks-Robertson S. The 9-1-1 checkpoint clamp physically interacts with polzeta and is partially required for spontaneous polzeta-dependent mutagenesis in Saccharomyces cerevisiae. J. Biol. Chem. 280 (2005) 38657-38665
    • (2005) J. Biol. Chem. , vol.280 , pp. 38657-38665
    • Sabbioneda, S.1    Minesinger, B.K.2    Giannattasio, M.3    Plevani, P.4    Muzi-Falconi, M.5    Jinks-Robertson, S.6
  • 79
    • 3943107573 scopus 로고    scopus 로고
    • Molecular mechanisms of mammalian DNA repair and the DNA damage checkpoints
    • Sancar A., Lindsey-Boltz L.A., Unsal-Kacmaz K., and Linn S. Molecular mechanisms of mammalian DNA repair and the DNA damage checkpoints. Annu. Rev. Biochem. 73 (2004) 39-85
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 39-85
    • Sancar, A.1    Lindsey-Boltz, L.A.2    Unsal-Kacmaz, K.3    Linn, S.4
  • 80
    • 4344685735 scopus 로고    scopus 로고
    • Methyl-CpG binding protein MBD1 couples histone H3 methylation at lysine 9 by SETDB1 to DNA replication and chromatin assembly
    • Sarraf S.A., and Stancheva I. Methyl-CpG binding protein MBD1 couples histone H3 methylation at lysine 9 by SETDB1 to DNA replication and chromatin assembly. Mol. Cell 15 (2004) 595-605
    • (2004) Mol. Cell , vol.15 , pp. 595-605
    • Sarraf, S.A.1    Stancheva, I.2
  • 82
    • 0035799281 scopus 로고    scopus 로고
    • Yeast histone deposition protein Asf1p requires Hir proteins and PCNA for heterochromatic silencing
    • Sharp J.A., Fouts E.T., Krawitz D.C., and Kaufman P.D. Yeast histone deposition protein Asf1p requires Hir proteins and PCNA for heterochromatic silencing. Curr. Biol. 11 (2001) 463-473
    • (2001) Curr. Biol. , vol.11 , pp. 463-473
    • Sharp, J.A.1    Fouts, E.T.2    Krawitz, D.C.3    Kaufman, P.D.4
  • 83
    • 0036102289 scopus 로고    scopus 로고
    • Solution structure of a yeast ubiquitin-like protein Smt3: the role of structurally less defined sequences in protein-protein recognitions
    • Sheng W., and Liao X. Solution structure of a yeast ubiquitin-like protein Smt3: the role of structurally less defined sequences in protein-protein recognitions. Protein Sci. 11 (2002) 1482-1491
    • (2002) Protein Sci. , vol.11 , pp. 1482-1491
    • Sheng, W.1    Liao, X.2
  • 84
    • 0024372060 scopus 로고
    • Purification and characterization of CAF-I, a human cell factor required for chromatin assembly during DNA replication in vitro
    • Smith S., and Stillman B. Purification and characterization of CAF-I, a human cell factor required for chromatin assembly during DNA replication in vitro. Cell 58 (1989) 15-25
    • (1989) Cell , vol.58 , pp. 15-25
    • Smith, S.1    Stillman, B.2
  • 85
    • 0141831006 scopus 로고    scopus 로고
    • Control of spontaneous and damage-induced mutagenesis by SUMO and ubiquitin conjugation
    • Stelter P., and Ulrich H.D. Control of spontaneous and damage-induced mutagenesis by SUMO and ubiquitin conjugation. Nature 425 (2003) 188-191
    • (2003) Nature , vol.425 , pp. 188-191
    • Stelter, P.1    Ulrich, H.D.2
  • 86
    • 0035816586 scopus 로고    scopus 로고
    • DNA ligase I and proliferating cell nuclear antigen form a functional complex
    • Tom S., Henricksen L.A., Park M.S., and Bambara R.A. DNA ligase I and proliferating cell nuclear antigen form a functional complex. J. Biol. Chem. 276 (2001) 24817-24825
    • (2001) J. Biol. Chem. , vol.276 , pp. 24817-24825
    • Tom, S.1    Henricksen, L.A.2    Park, M.S.3    Bambara, R.A.4
  • 87
    • 0035369734 scopus 로고    scopus 로고
    • Human APE2 protein is mostly localized in the nuclei and to some extent in the mitochondria, while nuclear APE2 is partly associated with proliferating cell nuclear antigen
    • Tsuchimoto D., Sakai Y., Sakumi K., Nishioka K., Sasaki M., Fujiwara T., and Nakabeppu Y. Human APE2 protein is mostly localized in the nuclei and to some extent in the mitochondria, while nuclear APE2 is partly associated with proliferating cell nuclear antigen. Nucleic Acids Res. 29 (2001) 2349-2360
    • (2001) Nucleic Acids Res. , vol.29 , pp. 2349-2360
    • Tsuchimoto, D.1    Sakai, Y.2    Sakumi, K.3    Nishioka, K.4    Sasaki, M.5    Fujiwara, T.6    Nakabeppu, Y.7
  • 88
  • 89
    • 0032497566 scopus 로고    scopus 로고
    • Cohesion between sister chromatids must be established during DNA replication
    • Uhlmann F., and Nasmyth K. Cohesion between sister chromatids must be established during DNA replication. Curr. Biol. 8 (1998) 1095-1101
    • (1998) Curr. Biol. , vol.8 , pp. 1095-1101
    • Uhlmann, F.1    Nasmyth, K.2
  • 90
    • 0034600851 scopus 로고    scopus 로고
    • Two RING finger proteins mediate cooperation between ubiquitin-conjugating enzymes in DNA repair
    • Ulrich H.D., and Jentsch S. Two RING finger proteins mediate cooperation between ubiquitin-conjugating enzymes in DNA repair. EMBO J. 19 (2000) 3388-3397
    • (2000) EMBO J. , vol.19 , pp. 3388-3397
    • Ulrich, H.D.1    Jentsch, S.2
  • 92
    • 0036707526 scopus 로고    scopus 로고
    • Stimulation of 3′→5′ exonuclease and 3′-phosphodiesterase activities of yeast apn2 by proliferating cell nuclear antigen
    • Unk I., Haracska L., Gomes X.V., Burgers P.M., Prakash L., and Prakash S. Stimulation of 3′→5′ exonuclease and 3′-phosphodiesterase activities of yeast apn2 by proliferating cell nuclear antigen. Mol. Cell. Biol. 22 (2002) 6480-6486
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 6480-6486
    • Unk, I.1    Haracska, L.2    Gomes, X.V.3    Burgers, P.M.4    Prakash, L.5    Prakash, S.6
  • 94
    • 0029922537 scopus 로고    scopus 로고
    • The differentiation primary response gene MyD118, related to GADD45, encodes for a nuclear protein which interacts with PCNA and p21WAF1/CIP1
    • Vairapandi M., Balliet A.G., Fornace Jr. A.J., Hoffman B., and Liebermann D.A. The differentiation primary response gene MyD118, related to GADD45, encodes for a nuclear protein which interacts with PCNA and p21WAF1/CIP1. Oncogene 12 (1996) 2579-2594
    • (1996) Oncogene , vol.12 , pp. 2579-2594
    • Vairapandi, M.1    Balliet, A.G.2    Fornace Jr., A.J.3    Hoffman, B.4    Liebermann, D.A.5
  • 96
    • 0028352434 scopus 로고
    • The p21 inhibitor of cyclin-dependent kinases controls DNA replication by interaction with PCNA
    • Waga S., Hannon G.J., Beach D., and Stillman B. The p21 inhibitor of cyclin-dependent kinases controls DNA replication by interaction with PCNA. Nature 369 (1994) 574-578
    • (1994) Nature , vol.369 , pp. 574-578
    • Waga, S.1    Hannon, G.J.2    Beach, D.3    Stillman, B.4
  • 98
    • 0029257341 scopus 로고
    • A small peptide inhibitor of DNA replication defines the site of interaction between the cyclin-dependent kinase inhibitor p21WAF1 and proliferating cell nuclear antigen
    • Warbrick E., Lane D.P., Glover D.M., and Cox L.S. A small peptide inhibitor of DNA replication defines the site of interaction between the cyclin-dependent kinase inhibitor p21WAF1 and proliferating cell nuclear antigen. Curr. Biol. 5 (1995) 275-282
    • (1995) Curr. Biol. , vol.5 , pp. 275-282
    • Warbrick, E.1    Lane, D.P.2    Glover, D.M.3    Cox, L.S.4
  • 99
    • 0030913166 scopus 로고    scopus 로고
    • Homologous regions of Fen1 and p21Cip1 compete for binding to the same site on PCNA: a potential mechanism to co-ordinate DNA replication and repair
    • Warbrick E., Lane D.P., Glover D.M., and Cox L.S. Homologous regions of Fen1 and p21Cip1 compete for binding to the same site on PCNA: a potential mechanism to co-ordinate DNA replication and repair. Oncogene 14 (1997) 2313-2321
    • (1997) Oncogene , vol.14 , pp. 2313-2321
    • Warbrick, E.1    Lane, D.P.2    Glover, D.M.3    Cox, L.S.4
  • 100
    • 6344288785 scopus 로고    scopus 로고
    • Rad18 guides poleta to replication stalling sites through physical interaction and PCNA monoubiquitination
    • Watanabe K., Tateishi S., Kawasuji M., Tsurimoto T., Inoue H., and Yamaizumi M. Rad18 guides poleta to replication stalling sites through physical interaction and PCNA monoubiquitination. EMBO J. 23 (2004) 3886-3896
    • (2004) EMBO J. , vol.23 , pp. 3886-3896
    • Watanabe, K.1    Tateishi, S.2    Kawasuji, M.3    Tsurimoto, T.4    Inoue, H.5    Yamaizumi, M.6
  • 101
    • 13844280351 scopus 로고    scopus 로고
    • Human 3-methyladenine-DNA glycosylase: effect of sequence context on excision, association with PCNA, and stimulation by AP endonuclease
    • Xia L., Zheng L., Lee H.W., Bates S.E., Federico L., Shen B., and O'Connor T.R. Human 3-methyladenine-DNA glycosylase: effect of sequence context on excision, association with PCNA, and stimulation by AP endonuclease. J. Mol. Biol. 346 (2005) 1259-1274
    • (2005) J. Mol. Biol. , vol.346 , pp. 1259-1274
    • Xia, L.1    Zheng, L.2    Lee, H.W.3    Bates, S.E.4    Federico, L.5    Shen, B.6    O'Connor, T.R.7
  • 102
    • 0035836496 scopus 로고    scopus 로고
    • A novel PCNA-binding motif identified by the panning of a random peptide display library
    • Xu H., Zhang P., Liu L., and Lee M.Y. A novel PCNA-binding motif identified by the panning of a random peptide display library. Biochemistry 40 (2001) 4512-4520
    • (2001) Biochemistry , vol.40 , pp. 4512-4520
    • Xu, H.1    Zhang, P.2    Liu, L.3    Lee, M.Y.4
  • 103
    • 33745187598 scopus 로고    scopus 로고
    • Mechanism of proliferating cell nuclear antigen clamp opening by replication factor C
    • Yao N.Y., Johnson A., Bowman G.D., Kuriyan J., and O'Donnell M. Mechanism of proliferating cell nuclear antigen clamp opening by replication factor C. J. Biol. Chem. 281 (2006) 17528-17539
    • (2006) J. Biol. Chem. , vol.281 , pp. 17528-17539
    • Yao, N.Y.1    Johnson, A.2    Bowman, G.D.3    Kuriyan, J.4    O'Donnell, M.5
  • 104
    • 0027440552 scopus 로고
    • Proliferating cell nuclear antigen and p21 are components of multiple cell cycle kinase complexes
    • Zhang H., Xiong Y., and Beach D. Proliferating cell nuclear antigen and p21 are components of multiple cell cycle kinase complexes. Mol. Biol. Cell 4 (1993) 897-906
    • (1993) Mol. Biol. Cell , vol.4 , pp. 897-906
    • Zhang, H.1    Xiong, Y.2    Beach, D.3
  • 105
    • 0034626734 scopus 로고    scopus 로고
    • PCNA connects DNA replication to epigenetic inheritance in yeast
    • Zhang Z., Shibahara K., and Stillman B. PCNA connects DNA replication to epigenetic inheritance in yeast. Nature 408 (2000) 221-225
    • (2000) Nature , vol.408 , pp. 221-225
    • Zhang, Z.1    Shibahara, K.2    Stillman, B.3


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