메뉴 건너뛰기




Volumn 3, Issue 1, 2013, Pages 75-84

Role of the checkpoint clamp in DNA damage response

Author keywords

Checkpoint clamp; DNA damage checkpoint; DNA repair; Rad9

Indexed keywords

ATM PROTEIN; CELL CYCLE PROTEIN; CHECKPOINT KINASE 1; CHECKPOINT KINASE 2; CYCLINE; MRE11 PROTEIN; PROTEIN RAD1; PROTEIN RAD9; REPLICATION FACTOR A;

EID: 84915774789     PISSN: None     EISSN: 2218273X     Source Type: Journal    
DOI: 10.3390/biom3010075     Document Type: Review
Times cited : (8)

References (69)
  • 1
    • 0034235463 scopus 로고    scopus 로고
    • Structure-based predictions of rad1, rad9, hus1 and rad17 participation in sliding clamp and clamp-loading complexes
    • Venclovas, C.; Thelen, M.P. Structure-based predictions of rad1, rad9, hus1 and rad17 participation in sliding clamp and clamp-loading complexes. Nucleic Acids Res. 2000, 28, 2481-2493.
    • (2000) Nucleic Acids Res , vol.28 , pp. 2481-2493
    • Venclovas, C.1    Thelen, M.P.2
  • 2
    • 0037452605 scopus 로고    scopus 로고
    • Loading of the human 9-1-1 checkpoint complex onto DNA by the checkpoint clamp loader hrad17-replication factor c complex in vitro
    • Bermudez, V.P.; Lindsey-Boltz, L.A.; Cesare, A.J.; Maniwa, Y.; Griffith, J.D.; Hurwitz, J.; Sancar, A. Loading of the human 9-1-1 checkpoint complex onto DNA by the checkpoint clamp loader hrad17-replication factor c complex in vitro. Proc. Natl. Acad. Sci. USA 2003, 100, 1633-1638.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 1633-1638
    • Bermudez, V.P.1    Lindsey-Boltz, L.A.2    Cesare, A.J.3    Maniwa, Y.4    Griffith, J.D.5    Hurwitz, J.6    Sancar, A.7
  • 3
    • 0036668474 scopus 로고    scopus 로고
    • Clamp and clamp loader structures of the human checkpoint protein complexes, rad9-1-1 and rad17-rfc
    • Shiomi, Y.; Shinozaki, A.; Nakada, D.; Sugimoto, K.; Usukura, J.; Obuse, C.; Tsurimoto, T. Clamp and clamp loader structures of the human checkpoint protein complexes, rad9-1-1 and rad17-rfc. Genes Cells 2002, 7, 861-868.
    • (2002) Genes Cells , vol.7 , pp. 861-868
    • Shiomi, Y.1    Shinozaki, A.2    Nakada, D.3    Sugimoto, K.4    Usukura, J.5    Obuse, C.6    Tsurimoto, T.7
  • 4
    • 0035854804 scopus 로고    scopus 로고
    • Reconstitution and molecular analysis of the hrad9-hhus1-hrad1 (9-1-1) DNA damage responsive checkpoint complex
    • Burtelow, M.A.; Roos-Mattjus, P.M.; Rauen, M.; Babendure, J.R.; Karnitz, L.M. Reconstitution and molecular analysis of the hrad9-hhus1-hrad1 (9-1-1) DNA damage responsive checkpoint complex. J. Bio. Chem. 2001, 276, 25903-25909.
    • (2001) J. Bio. Chem , vol.276 , pp. 25903-25909
    • Burtelow, M.A.1    Roos-Mattjus, P.M.2    Rauen, M.3    Babendure, J.R.4    Karnitz, L.M.5
  • 6
    • 67649111979 scopus 로고    scopus 로고
    • Crystal structure of the rad9-rad1-hus1 DNA damage checkpoint complex--implications for clamp loading and regulation
    • Dore, A.S.; Kilkenny, M.L.; Rzechorzek, N.J.; Pearl, L.H. Crystal structure of the rad9-rad1-hus1 DNA damage checkpoint complex--implications for clamp loading and regulation. Mol. Cell. 2009, 34, 735-745.
    • (2009) Mol. Cell , vol.34 , pp. 735-745
    • Dore, A.S.1    Kilkenny, M.L.2    Rzechorzek, N.J.3    Pearl, L.H.4
  • 7
    • 67449103064 scopus 로고    scopus 로고
    • Crystal structure of the human rad9-hus1-rad1 clamp
    • Sohn, S.Y.; Cho, Y. Crystal structure of the human rad9-hus1-rad1 clamp. J. Mol. Biol. 2009, 390, 490-502.
    • (2009) J. Mol. Biol , vol.390 , pp. 490-502
    • Sohn, S.Y.1    Cho, Y.2
  • 8
    • 68949137117 scopus 로고    scopus 로고
    • Structure and functional implications of the human rad9-hus1-rad1 cell cycle checkpoint complex
    • Xu, M.; Bai, L.; Gong, Y.; Xie, W.; Hang, H.; Jiang, T. Structure and functional implications of the human rad9-hus1-rad1 cell cycle checkpoint complex. J. Bio. Chem. 2009, 284, 20457-20461.
    • (2009) J. Bio. Chem , vol.284 , pp. 20457-20461
    • Xu, M.1    Bai, L.2    Gong, Y.3    Xie, W.4    Hang, H.5    Jiang, T.6
  • 9
    • 0025293914 scopus 로고
    • Mechanism of elongation of primed DNA by DNA polymerase delta, proliferating cell nuclear antigen, and activator 1
    • Lee, S.H.; Hurwitz, J. Mechanism of elongation of primed DNA by DNA polymerase delta, proliferating cell nuclear antigen, and activator 1. Proc. Natl. Acad. Sci. USA 1990, 87, 5672-5676.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 5672-5676
    • Lee, S.H.1    Hurwitz, J.2
  • 10
    • 0027425441 scopus 로고
    • Interaction of DNA polymerase delta, proliferating cell nuclear antigen, and synthetic oligonucleotide template-primers. Analysis by polyacrylamide gel electrophoresis-band mobility shift assay
    • Ng, L.; McConnell, M.; Tan, C.K.; Downey, K.M.; Fisher, P.A. Interaction of DNA polymerase delta, proliferating cell nuclear antigen, and synthetic oligonucleotide template-primers. Analysis by polyacrylamide gel electrophoresis-band mobility shift assay. J. Bio. Chem. 1993, 268, 13571-13576.
    • (1993) J. Bio. Chem , vol.268 , pp. 13571-13576
    • Ng, L.1    McConnell, M.2    Tan, C.K.3    Downey, K.M.4    Fisher, P.A.5
  • 11
    • 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.; Hubscher, U. Regulation of DNA replication and repair proteins through interaction with the front side of proliferating cell nuclear antigen. EMBO J. 1998, 17, 2412-2425.
    • (1998) EMBO J , vol.17 , pp. 2412-2425
    • Jonsson, Z.O.1    Hindges, R.2    Hubscher, U.3
  • 12
    • 0033538566 scopus 로고    scopus 로고
    • Architecture of the active DNA polymerase delta. Proliferating cell nuclear antigen. Template-primer complex
    • Mozzherin, D.J.; Tan, C.K.; Downey, K.M.; Fisher, P.A. Architecture of the active DNA polymerase delta. Proliferating cell nuclear antigen. Template-primer complex. J. Bio. Chem. 1999, 274, 19862-19867.
    • (1999) J. Bio. Chem , vol.274 , pp. 19862-19867
    • Mozzherin, D.J.1    Tan, C.K.2    Downey, K.M.3    Fisher, P.A.4
  • 13
    • 0035225868 scopus 로고    scopus 로고
    • Molecular mechanism of pcna-dependent base excision repair
    • Matsumoto, Y. Molecular mechanism of pcna-dependent base excision repair. Prog. Nucleic Acid Res. Mol. Biol. 2001, 68, 129-138.
    • (2001) Prog. Nucleic Acid Res. Mol. Biol , vol.68 , pp. 129-138
    • Matsumoto, Y.1
  • 14
    • 2242420935 scopus 로고    scopus 로고
    • Human DNA polymerase lambda functionally and physically interacts with proliferating cell nuclear antigen in normal and translesion DNA synthesis
    • Maga, G.; Villani, G.; Ramadan, K.; Shevelev, I.; Tanguy Le Gac, N.; Blanco, L.; Blanca, G.; Spadari, S.; Hubscher, U. Human DNA polymerase lambda functionally and physically interacts with proliferating cell nuclear antigen in normal and translesion DNA synthesis. J. Bio. Chem. 2002, 277, 48434-48440.
    • (2002) J. Bio. Chem , vol.277 , pp. 48434-48440
    • Maga, G.1    Villani, G.2    Ramadan, K.3    Shevelev, I.4    Tanguy Le Gac, N.5    Blanco, L.6    Blanca, G.7    Spadari, S.8    Hubscher, U.9
  • 16
    • 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.; 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. Bio. Chem. 1997, 272, 24522-24529.
    • (1997) J. Bio. Chem , vol.272 , pp. 24522-24529
    • Gary, R.1    Ludwig, D.L.2    Cornelius, H.L.3    McInnes, M.A.4    Park, M.S.5
  • 17
    • 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, D.J.; Mol, C.D.; Shen, B.; Tainer, J.A. Structure of the DNA repair and replication endonuclease and exonuclease fen-1: Coupling DNA and pcna binding to fen-1 activity. Cell 1998, 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
  • 18
    • 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.; Jentsch, S. Rad6-dependent DNA repair is linked to modification of pcna by ubiquitin and sumo. Nature 2002, 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
  • 20
    • 34948889415 scopus 로고    scopus 로고
    • The rad9-hus1-rad1 checkpoint clamp regulates interaction of topbp1 with atr
    • Lee, J.; Kumagai, A.; Dunphy, W.G. The rad9-hus1-rad1 checkpoint clamp regulates interaction of topbp1 with atr. J. Bio. Chem. 2007, 282, 28036-28044.
    • (2007) J. Bio. Chem , vol.282 , pp. 28036-28044
    • Lee, J.1    Kumagai, A.2    Dunphy, W.G.3
  • 21
    • 64049105391 scopus 로고    scopus 로고
    • Topbp1 and DNA polymerase-alpha directly recruit the 9-1-1 complex to stalled DNA replication forks
    • Yan, S.; Michael, W.M. Topbp1 and DNA polymerase-alpha directly recruit the 9-1-1 complex to stalled DNA replication forks. J. Cell. Biol. 2009, 184, 793-804.
    • (2009) J. Cell. Biol , vol.184 , pp. 793-804
    • Yan, S.1    Michael, W.M.2
  • 22
    • 34250705797 scopus 로고    scopus 로고
    • The rad9-hus1-rad1 (9-1-1) clamp activates checkpoint signaling via topbp1
    • Delacroix, S.; Wagner, J.M.; Kobayashi, M.; Yamamoto, K.; Karnitz, L.M. The rad9-hus1-rad1 (9-1-1) clamp activates checkpoint signaling via topbp1. Genes Dev. 2007, 21, 1472-1477.
    • (2007) Genes Dev , vol.21 , pp. 1472-1477
    • Delacroix, S.1    Wagner, J.M.2    Kobayashi, M.3    Yamamoto, K.4    Karnitz, L.M.5
  • 23
    • 0035449355 scopus 로고    scopus 로고
    • Cell cycle checkpoint signaling through the atm and atr kinases
    • Abraham, R.T. Cell cycle checkpoint signaling through the atm and atr kinases. Genes Dev. 2001, 15, 2177-2196.
    • (2001) Genes Dev , vol.15 , pp. 2177-2196
    • Abraham, R.T.1
  • 24
    • 34249337705 scopus 로고    scopus 로고
    • Cdc25 and wee1: Analogous opposites?
    • Perry, J.A.; Kornbluth, S. Cdc25 and wee1: Analogous opposites? Cell Div. 2007, 2, 12.
    • (2007) Cell Div , vol.2 , pp. 12
    • Perry, J.A.1    Kornbluth, S.2
  • 25
    • 3342986735 scopus 로고    scopus 로고
    • Disruption of the rad9/rad1/hus1 (9-1-1) complex leads to checkpoint signaling and replication defects
    • Bao, S.; Lu, T.; Wang, X.; Zheng, H.; Wang, L.E.; Wei, Q.; Hittelman, W.N.; Li, L. Disruption of the rad9/rad1/hus1 (9-1-1) complex leads to checkpoint signaling and replication defects. Oncogene 2004, 23, 5586-5593.
    • (2004) Oncogene , vol.23 , pp. 5586-5593
    • Bao, S.1    Lu, T.2    Wang, X.3    Zheng, H.4    Wang, L.E.5    Wei, Q.6    Hittelman, W.N.7    Li, L.8
  • 26
    • 33746408535 scopus 로고    scopus 로고
    • Rad17 phosphorylation is required for claspin recruitment and chk1 activation in response to replication stress
    • Wang, X.; Zou, L.; Lu, T.; Bao, S.; Hurov, K.E.; Hittelman, W.N.; Elledge, S.J.; Li, L. Rad17 phosphorylation is required for claspin recruitment and chk1 activation in response to replication stress. Mol. Cell. 2006, 23, 331-341.
    • (2006) Mol. Cell , vol.23 , pp. 331-341
    • Wang, X.1    Zou, L.2    Lu, T.3    Bao, S.4    Hurov, K.E.5    Hittelman, W.N.6    Elledge, S.J.7    Li, L.8
  • 29
    • 79953759105 scopus 로고    scopus 로고
    • Sensing of replication stress and mec1 activation act through two independent pathways involving the 9-1-1 complex and DNA polymerase epsilon
    • Puddu, F.; Piergiovanni, G.; Plevani, P.; Muzi-Falconi, M. Sensing of replication stress and mec1 activation act through two independent pathways involving the 9-1-1 complex and DNA polymerase epsilon. PLoS Genetics 2011, 7, e1002022.
    • (2011) PLoS Genetics , vol.7
    • Puddu, F.1    Piergiovanni, G.2    Plevani, P.3    Muzi-Falconi, M.4
  • 30
    • 71149093704 scopus 로고    scopus 로고
    • The unstructured C-terminal tail of the 9-1-1 clamp subunit ddc1 activates mec1/atr via two distinct mechanisms
    • Navadgi-Patil, V.M.; Burgers, P.M. The unstructured C-terminal tail of the 9-1-1 clamp subunit ddc1 activates mec1/atr via two distinct mechanisms. Mol. Cell. 2009, 36, 743-753.
    • (2009) Mol. Cell , vol.36 , pp. 743-753
    • Navadgi-Patil, V.M.1    Burgers, P.M.2
  • 31
    • 0032540927 scopus 로고    scopus 로고
    • Identification of a human homologue of the schizosaccharomyces pombe rad17+ checkpoint gene
    • Parker, A.E.; Van de Weyer, I.; Laus, M.C.; Verhasselt, P.; Luyten, W.H. Identification of a human homologue of the schizosaccharomyces pombe rad17+ checkpoint gene. J. Bio. Chem. 1998, 273, 18340-18346.
    • (1998) J. Bio. Chem , vol.273 , pp. 18340-18346
    • Parker, A.E.1    Van de Weyer, I.2    Laus, M.C.3    Verhasselt, P.4    Luyten, W.H.5
  • 32
    • 4243156107 scopus 로고    scopus 로고
    • Biochemical characterization of DNA damage checkpoint complexes: Clamp loader and clamp complexes with specificity for 5' recessed DNA
    • Ellison, V.; Stillman, B. Biochemical characterization of DNA damage checkpoint complexes: Clamp loader and clamp complexes with specificity for 5' recessed DNA. PLoS Biol. 2003, 1, E33.
    • (2003) PLoS Biol , vol.1
    • Ellison, V.1    Stillman, B.2
  • 33
    • 84860742574 scopus 로고    scopus 로고
    • Atm-dependent phosphorylation of the checkpoint clamp regulates repair pathways and maintains genomic stability
    • Shin, M.H.; Yuan, M.; Zhang, H.; Margolick, J.B.; Kai, M. Atm-dependent phosphorylation of the checkpoint clamp regulates repair pathways and maintains genomic stability. Cell Cycle 2012, 11, 1796-1803.
    • (2012) Cell Cycle , vol.11 , pp. 1796-1803
    • Shin, M.H.1    Yuan, M.2    Zhang, H.3    Margolick, J.B.4    Kai, M.5
  • 34
    • 85016374443 scopus 로고    scopus 로고
    • Department of Radiation Oncology, Johns Hopkins University, School of Medicine, Baltimore MD 21231, USA Unpublished Data
    • Kai, M., Tsui, E.,. Role of the checkpoint clamp in double-strand break repair. Department of Radiation Oncology, Johns Hopkins University, School of Medicine, Baltimore MD 21231, USA Unpublished Data, 2013.
    • (2013) Role of the checkpoint clamp in double-strand break repair
    • Kai, M.1    Tsui, E.2
  • 35
    • 4544281398 scopus 로고    scopus 로고
    • Choreography of the DNA damage response: Spatiotemporal relationships among checkpoint and repair proteins
    • Lisby, M.; Barlow, J.H.; Burgess, R.C.; Rothstein, R. Choreography of the DNA damage response: Spatiotemporal relationships among checkpoint and repair proteins. Cell 2004, 118, 699-713.
    • (2004) Cell , vol.118 , pp. 699-713
    • Lisby, M.1    Barlow, J.H.2    Burgess, R.C.3    Rothstein, R.4
  • 38
    • 1842431822 scopus 로고    scopus 로고
    • Direct activation of the atm protein kinase by the mre11/rad50/nbs1 complex
    • Lee, J.H.; Paull, T.T. Direct activation of the atm protein kinase by the mre11/rad50/nbs1 complex. Science 2004, 304, 93-96.
    • (2004) Science , vol.304 , pp. 93-96
    • Lee, J.H.1    Paull, T.T.2
  • 39
    • 17644409069 scopus 로고    scopus 로고
    • Atm activation by DNA double-strand breaks through the mre11-rad50-nbs1 complex
    • Lee, J.H.; Paull, T.T. Atm activation by DNA double-strand breaks through the mre11-rad50-nbs1 complex. Science 2005, 308, 551-554.
    • (2005) Science , vol.308 , pp. 551-554
    • Lee, J.H.1    Paull, T.T.2
  • 40
    • 0345564858 scopus 로고    scopus 로고
    • Replication protein a-mediated recruitment and activation of rad17 complexes
    • Zou, L.; Liu, D.; Elledge, S.J. Replication protein a-mediated recruitment and activation of rad17 complexes. Proc. Natl. Acad. Sci. USA 2003, 100, 13827-13832.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 13827-13832
    • Zou, L.1    Liu, D.2    Elledge, S.J.3
  • 41
    • 0037567268 scopus 로고    scopus 로고
    • Sensing DNA damage through atrip recognition of rpa-ssdna complexes
    • Zou, L.; Elledge, S.J. Sensing DNA damage through atrip recognition of rpa-ssdna complexes. Science 2003, 300, 1542-1548.
    • (2003) Science , vol.300 , pp. 1542-1548
    • Zou, L.1    Elledge, S.J.2
  • 43
    • 0032566753 scopus 로고    scopus 로고
    • The C-terminal (brct) domains of brca1 interact in vivo with ctip, a protein implicated in the ctbp pathway of transcriptional repression
    • Yu, X.; Wu, L.C.; Bowcock, A.M.; Aronheim, A.; Baer, R. The C-terminal (brct) domains of brca1 interact in vivo with ctip, a protein implicated in the ctbp pathway of transcriptional repression. J. Bio. Chem. 1998, 273, 25388-25392.
    • (1998) J. Bio. Chem , vol.273 , pp. 25388-25392
    • Yu, X.1    Wu, L.C.2    Bowcock, A.M.3    Aronheim, A.4    Baer, R.5
  • 44
    • 43149118369 scopus 로고    scopus 로고
    • Cell cycle-dependent complex formation of brca1. Ctip. Mrn is important for DNA double-strand break repair
    • Chen, L.; Nievera, C.J.; Lee, A.Y.; Wu, X. Cell cycle-dependent complex formation of brca1. Ctip. Mrn is important for DNA double-strand break repair. J. Bio. Chem. 2008, 283, 7713-7720.
    • (2008) J. Bio. Chem , vol.283 , pp. 7713-7720
    • Chen, L.1    Nievera, C.J.2    Lee, A.Y.3    Wu, X.4
  • 45
    • 67349246802 scopus 로고    scopus 로고
    • Ctip-brca1 modulates the choice of DNA double-strand-break repair pathway throughout the cell cycle
    • Yun, M.H.; Hiom, K. Ctip-brca1 modulates the choice of DNA double-strand-break repair pathway throughout the cell cycle. Nature 2009, 459, 460-463.
    • (2009) Nature , vol.459 , pp. 460-463
    • Yun, M.H.1    Hiom, K.2
  • 47
    • 68249116573 scopus 로고    scopus 로고
    • DNA end resection: Many nucleases make light work
    • Mimitou, E.P.; Symington, L.S. DNA end resection: Many nucleases make light work. DNA Repair 2009, 8, 983-995.
    • (2009) DNA Repair , vol.8 , pp. 983-995
    • Mimitou, E.P.1    Symington, L.S.2
  • 48
    • 59249107930 scopus 로고    scopus 로고
    • Interplay of mre11 nuclease with dna2 plus sgs1 in rad51-dependent recombinational repair
    • Budd, M.E.; Campbell, J.L. Interplay of mre11 nuclease with dna2 plus sgs1 in rad51-dependent recombinational repair. PLoS One 2009, 4, e4267.
    • (2009) PLoS One , vol.4
    • Budd, M.E.1    Campbell, J.L.2
  • 49
    • 53649104599 scopus 로고    scopus 로고
    • Sae2, exo1 and sgs1 collaborate in DNA double-strand break processing
    • Mimitou, E.P.; Symington, L.S. Sae2, exo1 and sgs1 collaborate in DNA double-strand break processing. Nature 2008, 455, 770-774.
    • (2008) Nature , vol.455 , pp. 770-774
    • Mimitou, E.P.1    Symington, L.S.2
  • 50
    • 51549095956 scopus 로고    scopus 로고
    • Sgs1 helicase and two nucleases dna2 and exo1 resect DNA double-strand break ends
    • Zhu, Z.; Chung, W.H.; Shim, E.Y.; Lee, S.E.; Ira, G. Sgs1 helicase and two nucleases dna2 and exo1 resect DNA double-strand break ends. Cell 2008, 134, 981-994.
    • (2008) Cell , vol.134 , pp. 981-994
    • Zhu, Z.1    Chung, W.H.2    Shim, E.Y.3    Lee, S.E.4    Ira, G.5
  • 52
    • 53649090109 scopus 로고    scopus 로고
    • DNA helicases sgs1 and blm promote DNA double-strand break resection
    • Gravel, S.; Chapman, J.R.; Magill, C.; Jackson, S.P. DNA helicases sgs1 and blm promote DNA double-strand break resection. Genes Dev. 2008, 22, 2767-2772.
    • (2008) Genes Dev , vol.22 , pp. 2767-2772
    • Gravel, S.1    Chapman, J.R.2    Magill, C.3    Jackson, S.P.4
  • 53
    • 27544459564 scopus 로고    scopus 로고
    • Analysis of the xenopus werner syndrome protein in DNA double-strand break repair
    • Yan, H.; McCane, J.; Toczylowski, T.; Chen, C. Analysis of the xenopus werner syndrome protein in DNA double-strand break repair. J. Cell. Biol. 2005, 171, 217-227.
    • (2005) J. Cell. Biol , vol.171 , pp. 217-227
    • Yan, H.1    McCane, J.2    Toczylowski, T.3    Chen, C.4
  • 54
    • 33845925546 scopus 로고    scopus 로고
    • Mechanistic analysis of a DNA end processing pathway mediated by the xenopus werner syndrome protein
    • Toczylowski, T.; Yan, H. Mechanistic analysis of a DNA end processing pathway mediated by the xenopus werner syndrome protein. J. Bio. Chem. 2006, 281, 33198-33205.
    • (2006) J. Bio. Chem , vol.281 , pp. 33198-33205
    • Toczylowski, T.1    Yan, H.2
  • 56
    • 66749120336 scopus 로고    scopus 로고
    • Cell cycle-dependent processing of DNA lesions controls localization of rad9 to sites of genotoxic stress
    • Warmerdam, D.O.; Freire, R.; Kanaar, R.; Smits, V.A. Cell cycle-dependent processing of DNA lesions controls localization of rad9 to sites of genotoxic stress. Cell Cycle 2009, 8, 1765-1774.
    • (2009) Cell Cycle , vol.8 , pp. 1765-1774
    • Warmerdam, D.O.1    Freire, R.2    Kanaar, R.3    Smits, V.A.4
  • 57
    • 84860742574 scopus 로고    scopus 로고
    • Atm-dependent phosphorylation of the checkpoint clamp regulates repair pathways and maintains genomic stability
    • Shin, M.H.; Yuan, M.; Zhang, H.; Margolick, J.B.; Kai, M. Atm-dependent phosphorylation of the checkpoint clamp regulates repair pathways and maintains genomic stability. Cell Cycle 2012, 11, 1796-1803.
    • (2012) Cell Cycle , vol.11 , pp. 1796-1803
    • Shin, M.H.1    Yuan, M.2    Zhang, H.3    Margolick, J.B.4    Kai, M.5
  • 59
    • 6344247481 scopus 로고    scopus 로고
    • Uterus hyperplasia and increased carcinogen-induced tumorigenesis in mice carrying a targeted mutation of the chk2 phosphorylation site in brca1
    • Kim, S.S.; Cao, L.; Li, C.; Xu, X.; Huber, L.J.; Chodosh, L.A.; Deng, C.X. Uterus hyperplasia and increased carcinogen-induced tumorigenesis in mice carrying a targeted mutation of the chk2 phosphorylation site in brca1. Mol. Cell. Biol. 2004, 24, 9498-9507.
    • (2004) Mol. Cell. Biol , vol.24 , pp. 9498-9507
    • Kim, S.S.1    Cao, L.2    Li, C.3    Xu, X.4    Huber, L.J.5    Chodosh, L.A.6    Deng, C.X.7
  • 60
    • 0037224965 scopus 로고    scopus 로고
    • Checkpoint activation regulates mutagenic translesion synthesis
    • Kai, M.; Wang, T.S. Checkpoint activation regulates mutagenic translesion synthesis. Genes Dev. 2003, 17, 64-76.
    • (2003) Genes Dev , vol.17 , pp. 64-76
    • Kai, M.1    Wang, T.S.2
  • 61
    • 0344741364 scopus 로고    scopus 로고
    • Checkpoint responses to replication stalling: Inducing tolerance and preventing mutagenesis
    • Kai, M.; Wang, T.S. Checkpoint responses to replication stalling: Inducing tolerance and preventing mutagenesis. Mutation Res. 2003, 532, 59-73.
    • (2003) Mutation Res , vol.532 , pp. 59-73
    • Kai, M.1    Wang, T.S.2
  • 62
    • 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.; 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. Bio. Chem. 2005, 280, 38657-38665.
    • (2005) J. Bio. 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
  • 63
    • 22144468371 scopus 로고    scopus 로고
    • The human checkpoint sensor and alternative DNA clamp rad9-rad1-hus1 modulates the activity of DNA ligase i, a component of the long-patch base excision repair machinery
    • Smirnova, E.; Toueille, M.; Markkanen, E.; Hubscher, U. The human checkpoint sensor and alternative DNA clamp rad9-rad1-hus1 modulates the activity of DNA ligase i, a component of the long-patch base excision repair machinery. Biochem. J. 2005, 389, 13-17.
    • (2005) Biochem. J , vol.389 , pp. 13-17
    • Smirnova, E.1    Toueille, M.2    Markkanen, E.3    Hubscher, U.4
  • 65
    • 27144495464 scopus 로고    scopus 로고
    • The two DNA clamps rad9/rad1/hus1 complex and proliferating cell nuclear antigen differentially regulate flap endonuclease 1 activity
    • Friedrich-Heineken, E.; Toueille, M.; Tannler, B.; Burki, C.; Ferrari, E.; Hottiger, M.O.; Hubscher, U. The two DNA clamps rad9/rad1/hus1 complex and proliferating cell nuclear antigen differentially regulate flap endonuclease 1 activity. J. Mol. Biol. 2005, 353, 980-989.
    • (2005) J. Mol. Biol , vol.353 , pp. 980-989
    • Friedrich-Heineken, E.1    Toueille, M.2    Tannler, B.3    Burki, C.4    Ferrari, E.5    Hottiger, M.O.6    Hubscher, U.7
  • 67
    • 0033548096 scopus 로고    scopus 로고
    • Proliferating cell nuclear antigen facilitates excision in long-patch base excision repair
    • Gary, R.; Kim, K.; Cornelius, H.L.; Park, M.S.; Matsumoto, Y. Proliferating cell nuclear antigen facilitates excision in long-patch base excision repair. J. Bio. Chem. 1999, 274, 4354-4363.
    • (1999) J. Bio. Chem , vol.274 , pp. 4354-4363
    • Gary, R.1    Kim, K.2    Cornelius, H.L.3    Park, M.S.4    Matsumoto, Y.5
  • 68
    • 0037163025 scopus 로고    scopus 로고
    • Direct interaction between mammalian DNA polymerase beta and proliferating cell nuclear antigen
    • Kedar, P.S.; Kim, S.J.; Robertson, A.; Hou, E.; Prasad, R.; Horton, J.K.; Wilson, S.H. Direct interaction between mammalian DNA polymerase beta and proliferating cell nuclear antigen. J. Bio. Chem. 2002, 277, 31115-31123.
    • (2002) J. Bio. Chem , vol.277 , pp. 31115-31123
    • Kedar, P.S.1    Kim, S.J.2    Robertson, A.3    Hou, E.4    Prasad, R.5    Horton, J.K.6    Wilson, S.H.7
  • 69
    • 0242389787 scopus 로고    scopus 로고
    • Structural basis for recruitment of translesion DNA polymerase pol iv/dinb to the beta-clamp
    • Bunting, K.A.; Roe, S.M.; Pearl, L.H. Structural basis for recruitment of translesion DNA polymerase pol iv/dinb to the beta-clamp. EMBO J. 2003, 22, 5883-5892.
    • (2003) EMBO J , vol.22 , pp. 5883-5892
    • Bunting, K.A.1    Roe, S.M.2    Pearl, L.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.