메뉴 건너뛰기




Volumn 6, Issue 3, 2015, Pages 451-468

Regulation of unperturbed DNA replication by ubiquitylation

Author keywords

DNA replication; Posttranslational modification; Proteasomal degradation; Re replication; Replisome; Termination; Ubiquitylation

Indexed keywords

CELL CYCLE PROTEIN 6; CELL PROTEIN; CULLIN; CULLIN RING LIGASE 1; CULLIN RING LIGASE 4; CULLIN RING LIGASE 4 CDT2; CYCLIN D; CYCLIN DEPENDENT KINASE 2; CYCLIN DEPENDENT KINASE 4; CYCLIN DEPENDENT KINASE 6; CYCLIN E; CYCLINE; DNA; DNA DIRECTED DNA POLYMERASE ALPHA; DNA DIRECTED DNA POLYMERASE DELTA; HISTONE H3; HISTONE H4; MINICHROMOSOME MAINTENANCE PROTEIN 7; ORIGIN RECOGNITION COMPLEX 1; ORIGIN RECOGNITION COMPLEX 1-6; PEVONEDISTAT; PROTEASOME; PROTEIN P21; PROTEIN P27; PROTEIN SPT16; REPLICATION LICENSING FACTOR CDT1; S PHASE KINASE ASSOCIATED PROTEIN 2; UBIQUITIN PROTEIN LIGASE; UNCLASSIFIED DRUG; UNINDEXED DRUG; UVOMORULIN;

EID: 84934768282     PISSN: None     EISSN: 20734425     Source Type: Journal    
DOI: 10.3390/genes6030451     Document Type: Review
Times cited : (15)

References (115)
  • 2
    • 77953915005 scopus 로고    scopus 로고
    • Ubiquitin signalling in DNA replication and repair
    • Ulrich, H.D.; Walden, H. Ubiquitin signalling in DNA replication and repair. Nat. Rev. Mol. Cell Biol. 2010, 11, 479-489.
    • (2010) Nat. Rev. Mol. Cell Biol , vol.11 , pp. 479-489
    • Ulrich, H.D.1    Walden, H.2
  • 3
    • 84901628233 scopus 로고    scopus 로고
    • Helicase loading: How to build a MCM2-7 double-hexamer
    • Riera, A.; Tognetti, S.; Speck, C. Helicase loading: How to build a MCM2-7 double-hexamer. Semin. Cell Dev. Biol. 2014, 30, 104-109.
    • (2014) Semin. Cell Dev. Biol , vol.30 , pp. 104-109
    • Riera, A.1    Tognetti, S.2    Speck, C.3
  • 4
    • 12444311754 scopus 로고    scopus 로고
    • Anaphase-promoting complex-dependent proteolysis of cell cycle regulators and genomic instability of cancer cells
    • Wasch, R.; Engelbert, D. Anaphase-promoting complex-dependent proteolysis of cell cycle regulators and genomic instability of cancer cells. Oncogene 2005, 24, 1-10.
    • (2005) Oncogene , vol.24 , pp. 1-10
    • Wasch, R.1    Engelbert, D.2
  • 6
    • 0030693087 scopus 로고    scopus 로고
    • CDC20 and CDH1: A family of substrate-specific activators of APC-dependent proteolysis
    • Visintin, R.; Prinz, S.; Amon, A. CDC20 and CDH1: A family of substrate-specific activators of APC-dependent proteolysis. Science 1997, 278, 460-463.
    • (1997) Science , vol.278 , pp. 460-463
    • Visintin, R.1    Prinz, S.2    Amon, A.3
  • 7
    • 0034654399 scopus 로고    scopus 로고
    • The KEN box: An APC recognition signal distinct from the D box targeted by Cdh1
    • Pfleger, C.M.; Kirschner, M.W. The KEN box: An APC recognition signal distinct from the D box targeted by Cdh1. Genes Dev. 2000, 14, 655-665.
    • (2000) Genes Dev , vol.14 , pp. 655-665
    • Pfleger, C.M.1    Kirschner, M.W.2
  • 8
    • 44849107340 scopus 로고    scopus 로고
    • Mitotic CDKs control the metaphase-anaphase transition and trigger spindle elongation
    • Rahal, R.; Amon, A. Mitotic CDKs control the metaphase-anaphase transition and trigger spindle elongation. Genes Dev. 2008, 22, 1534-1548.
    • (2008) Genes Dev , vol.22 , pp. 1534-1548
    • Rahal, R.1    Amon, A.2
  • 9
    • 0344578064 scopus 로고    scopus 로고
    • APC(Cdc20) promotes exit from mitosis by destroying the anaphase inhibitor Pds1 and cyclin Clb5
    • Shirayama, M.; Toth, A.; Galova, M.; Nasmyth, K. APC(Cdc20) promotes exit from mitosis by destroying the anaphase inhibitor Pds1 and cyclin Clb5. Nature 1999, 402, 203-207.
    • (1999) Nature , vol.402 , pp. 203-207
    • Shirayama, M.1    Toth, A.2    Galova, M.3    Nasmyth, K.4
  • 10
    • 0033545694 scopus 로고    scopus 로고
    • Inhibitory phosphorylation of the APC regulator Hct1 is controlled by the kinase Cdc28 and the phosphatase Cdc14
    • Jaspersen, S.L.; Charles, J.F.; Morgan, D.O. Inhibitory phosphorylation of the APC regulator Hct1 is controlled by the kinase Cdc28 and the phosphatase Cdc14. Curr. Biol. 1999, 9, 227-236.
    • (1999) Curr. Biol , vol.9 , pp. 227-236
    • Jaspersen, S.L.1    Charles, J.F.2    Morgan, D.O.3
  • 11
    • 77956484794 scopus 로고    scopus 로고
    • Regulated degradation of the APC coactivator Cdc20
    • Robbins, J.A.; Cross, F.R. Regulated degradation of the APC coactivator Cdc20. Cell Div. 2010, 5, doi:10.1186/1747-1028-5-23.
    • (2010) Cell Div , vol.5
    • Robbins, J.A.1    Cross, F.R.2
  • 13
    • 1642378661 scopus 로고    scopus 로고
    • Control of the SCF (Skp2-Cks1) ubiquitin ligase by the APC/C (Cdh1) ubiquitin ligase
    • Bashir, T.; Dorrello, N.V.; Amador, V.; Guardavaccaro, D.; Pagano, M. Control of the SCF (Skp2-Cks1) ubiquitin ligase by the APC/C (Cdh1) ubiquitin ligase. Nature 2004, 428, 190-193.
    • (2004) Nature , vol.428 , pp. 190-193
    • Bashir, T.1    Dorrello, N.V.2    Amador, V.3    Guardavaccaro, D.4    Pagano, M.5
  • 14
    • 0027769876 scopus 로고
    • A new regulatory motif in cell-cycle control causing specific inhibition of cyclin D/CDK4
    • Serrano, M.; Hannon, G.J.; Beach, D. A new regulatory motif in cell-cycle control causing specific inhibition of cyclin D/CDK4. Nature 1993, 366, 704-707.
    • (1993) Nature , vol.366 , pp. 704-707
    • Serrano, M.1    Hannon, G.J.2    Beach, D.3
  • 15
    • 1642399624 scopus 로고    scopus 로고
    • Degradation of the SCF component Skp2 in cell-cycle phase G1 by the anaphase-promoting complex
    • Wei, W.; Ayad, N.G.; Wan, Y.; Zhang, G.J.; Kirschner, M.W.; Kaelin, W.G., Jr. Degradation of the SCF component Skp2 in cell-cycle phase G1 by the anaphase-promoting complex. Nature 2004, 428, 194-198.
    • (2004) Nature , vol.428 , pp. 194-198
    • Wei, W.1    Ayad, N.G.2    Wan, Y.3    Zhang, G.J.4    Kirschner, M.W.5    Kaelin, W.G.6
  • 17
    • 25144525540 scopus 로고    scopus 로고
    • CDKs promote DNA replication origin licensing in human cells by protecting Cdc6 from APC/C-dependent proteolysis
    • Mailand, N.; Diffley, J.F. CDKs promote DNA replication origin licensing in human cells by protecting Cdc6 from APC/C-dependent proteolysis. Cell 2005, 122, 915-926.
    • (2005) Cell , vol.122 , pp. 915-926
    • Mailand, N.1    Diffley, J.F.2
  • 18
    • 0032511148 scopus 로고    scopus 로고
    • Geminin, an inhibitor of DNA replication, is degraded during mitosis
    • McGarry, T.J.; Kirschner, M.W. Geminin, an inhibitor of DNA replication, is degraded during mitosis. Cell 1998, 93, 1043-1053.
    • (1998) Cell , vol.93 , pp. 1043-1053
    • McGarry, T.J.1    Kirschner, M.W.2
  • 19
    • 0035895622 scopus 로고    scopus 로고
    • Pathways governing G1/S transition and their response to DNA damage
    • Bartek, J.; Lukas, J. Pathways governing G1/S transition and their response to DNA damage. FEBS Letters 2001, 490, 117-122.
    • (2001) FEBS Letters , vol.490 , pp. 117-122
    • Bartek, J.1    Lukas, J.2
  • 20
    • 47149085982 scopus 로고    scopus 로고
    • P21 and p27: Roles in carcinogenesis and drug resistance
    • Abukhdeir, A.M.; Park, B.H. P21 and p27: Roles in carcinogenesis and drug resistance. Exp. Rev. Mol. Med. 2008, 10, doi:10.1017/S1462399408000744.
    • (2008) Exp. Rev. Mol. Med , vol.10
    • Abukhdeir, A.M.1    Park, B.H.2
  • 21
    • 67650657199 scopus 로고    scopus 로고
    • Ubiquitin-mediated control of oncogene and tumor suppressor gene products
    • Kitagawa, K.; Kotake, Y.; Kitagawa, M. Ubiquitin-mediated control of oncogene and tumor suppressor gene products. Cancer Sci. 2009, 100, 1374-1381.
    • (2009) Cancer Sci , vol.100 , pp. 1374-1381
    • Kitagawa, K.1    Kotake, Y.2    Kitagawa, M.3
  • 22
    • 78649653568 scopus 로고    scopus 로고
    • Structural assembly of cullin-RING ubiquitin ligase complexes
    • Zimmerman, E.S.; Schulman, B.A.; Zheng, N. Structural assembly of cullin-RING ubiquitin ligase complexes. Curr. Opin. Struct. Biol. 2010, 20, 714-721.
    • (2010) Curr. Opin. Struct. Biol , vol.20 , pp. 714-721
    • Zimmerman, E.S.1    Schulman, B.A.2    Zheng, N.3
  • 24
    • 84879880079 scopus 로고    scopus 로고
    • Regulation of APC(Cdh1) E3 ligase activity by the Fbw7/cyclin E signaling axis contributes to the tumor suppressor function of Fbw7
    • Lau, A.W.; Inuzuka, H.; Fukushima, H.; Wan, L.; Liu, P.; Gao, D.; Sun, Y.; Wei, W. Regulation of APC(Cdh1) E3 ligase activity by the Fbw7/cyclin E signaling axis contributes to the tumor suppressor function of Fbw7. Cell Res. 2013, 23, 947-961.
    • (2013) Cell Res , vol.23 , pp. 947-961
    • Lau, A.W.1    Inuzuka, H.2    Fukushima, H.3    Wan, L.4    Liu, P.5    Gao, D.6    Sun, Y.7    Wei, W.8
  • 25
    • 84883287460 scopus 로고    scopus 로고
    • SCF-mediated Cdh1 degradation defines a negative feedback system that coordinates cell-cycle progression
    • Fukushima, H.; Ogura, K.; Wan, L.; Lu, Y.; Li, V.; Gao, D.; Liu, P.; Lau, A.W.; Wu, T.; Kirschner, M.W.; et al. SCF-mediated Cdh1 degradation defines a negative feedback system that coordinates cell-cycle progression. Cell Rep. 2013, 4, 803-816.
    • (2013) Cell Rep , vol.4 , pp. 803-816
    • Fukushima, H.1    Ogura, K.2    Wan, L.3    Lu, Y.4    Li, V.5    Gao, D.6    Liu, P.7    Lau, A.W.8    Wu, T.9    Kirschner, M.W.10
  • 26
    • 31044453144 scopus 로고    scopus 로고
    • The evi5 oncogene regulates cyclin accumulation by stabilizing the anaphase-promoting complex inhibitor emi1
    • Eldridge, A.G.; Loktev, A.V.; Hansen, D.V.; Verschuren, E.W.; Reimann, J.D.; Jackson, P.K. The evi5 oncogene regulates cyclin accumulation by stabilizing the anaphase-promoting complex inhibitor emi1. Cell 2006, 124, 367-380.
    • (2006) Cell , vol.124 , pp. 367-380
    • Eldridge, A.G.1    Loktev, A.V.2    Hansen, D.V.3    Verschuren, E.W.4    Reimann, J.D.5    Jackson, P.K.6
  • 27
    • 10344247126 scopus 로고    scopus 로고
    • Autonomous regulation of the anaphase-promoting complex couples mitosis to S-phase entry
    • Rape, M.; Kirschner, M.W. Autonomous regulation of the anaphase-promoting complex couples mitosis to S-phase entry. Nature 2004, 432, 588-595.
    • (2004) Nature , vol.432 , pp. 588-595
    • Rape, M.1    Kirschner, M.W.2
  • 29
    • 0035812709 scopus 로고    scopus 로고
    • Phosphorylation-dependent ubiquitination of cyclin E by the SCFFbw7 ubiquitin ligase
    • Koepp, D.M.; Schaefer, L.K.; Ye, X.; Keyomarsi, K.; Chu, C.; Harper, J.W.; Elledge, S.J. Phosphorylation-dependent ubiquitination of cyclin E by the SCFFbw7 ubiquitin ligase. Science 2001, 294, 173-177.
    • (2001) Science , vol.294 , pp. 173-177
    • Koepp, D.M.1    Schaefer, L.K.2    Ye, X.3    Keyomarsi, K.4    Chu, C.5    Harper, J.W.6    Elledge, S.J.7
  • 30
    • 0033130137 scopus 로고    scopus 로고
    • Interaction between ubiquitin-protein ligase SCFSKP2 and E2F-1 underlies the regulation of E2F-1 degradation
    • Marti, A.; Wirbelauer, C.; Scheffner, M.; Krek, W. Interaction between ubiquitin-protein ligase SCFSKP2 and E2F-1 underlies the regulation of E2F-1 degradation. Nat. Cell Biol. 1999, 1, 14-19.
    • (1999) Nat. Cell Biol , vol.1 , pp. 14-19
    • Marti, A.1    Wirbelauer, C.2    Scheffner, M.3    Krek, W.4
  • 31
    • 79551564537 scopus 로고    scopus 로고
    • CRL4Cdt2: Master coordinator of cell cycle progression and genome stability
    • Abbas, T.; Dutta, A. CRL4Cdt2: master coordinator of cell cycle progression and genome stability. Cell Cycle 2011, 10, 241-249.
    • (2011) Cell Cycle , vol.10 , pp. 241-249
    • Abbas, T.1    Dutta, A.2
  • 32
    • 80051525031 scopus 로고    scopus 로고
    • Mechanism of CRL4(Cdt2), a PCNA-dependent E3 ubiquitin ligase
    • Havens, C.G.; Walter, J.C. Mechanism of CRL4(Cdt2), a PCNA-dependent E3 ubiquitin ligase. Genes Dev. 2011, 25, 1568-1582.
    • (2011) Genes Dev , vol.25 , pp. 1568-1582
    • Havens, C.G.1    Walter, J.C.2
  • 33
    • 34249066085 scopus 로고    scopus 로고
    • PCNA, the maestro of the replication fork
    • Moldovan, G.L.; Pfander, B.; Jentsch, S. PCNA, the maestro of the replication fork. Cell 2007, 129, 665-679.
    • (2007) Cell , vol.129 , pp. 665-679
    • Moldovan, G.L.1    Pfander, B.2    Jentsch, S.3
  • 34
    • 67649641658 scopus 로고    scopus 로고
    • Docking of a specialized PIP Box onto chromatin-bound PCNA creates a degron for the ubiquitin ligase CRL4Cdt2
    • Havens, C.G.; Walter, J.C. Docking of a specialized PIP Box onto chromatin-bound PCNA creates a degron for the ubiquitin ligase CRL4Cdt2. Mol. Cell 2009, 35, 93-104.
    • (2009) Mol. Cell , vol.35 , pp. 93-104
    • Havens, C.G.1    Walter, J.C.2
  • 35
    • 84859483427 scopus 로고    scopus 로고
    • Direct role for proliferating cell nuclear antigen in substrate recognition by the E3 ubiquitin ligase CRL4Cdt2
    • Havens, C.G.; Shobnam, N.; Guarino, E.; Centore, R.C.; Zou, L.; Kearsey, S.E.; Walter, J.C. Direct role for proliferating cell nuclear antigen in substrate recognition by the E3 ubiquitin ligase CRL4Cdt2. J. Biol. Chem. 2012, 287, 11410-11421.
    • (2012) J. Biol. Chem , vol.287 , pp. 11410-11421
    • Havens, C.G.1    Shobnam, N.2    Guarino, E.3    Centore, R.C.4    Zou, L.5    Kearsey, S.E.6    Walter, J.C.7
  • 36
    • 0038185375 scopus 로고    scopus 로고
    • Cop9/signalosome subunits and Pcu4 regulate ribonucleotide reductase by both checkpoint-dependent and -independent mechanisms
    • Liu, C.; Powell, K.A.; Mundt, K.; Wu, L.; Carr, A.M.; Caspari, T. Cop9/signalosome subunits and Pcu4 regulate ribonucleotide reductase by both checkpoint-dependent and -independent mechanisms. Genes Dev. 2003, 17, 1130-1140.
    • (2003) Genes Dev , vol.17 , pp. 1130-1140
    • Liu, C.1    Powell, K.A.2    Mundt, K.3    Wu, L.4    Carr, A.M.5    Caspari, T.6
  • 37
    • 27844432597 scopus 로고    scopus 로고
    • Transactivation of Schizosaccharomyces pombe cdt2+ stimulates a Pcu4-Ddb1-CSN ubiquitin ligase
    • Liu, C.; Poitelea, M.; Watson, A.; Yoshida, S.H.; Shimoda, C.; Holmberg, C.; Nielsen, O.; Carr, A.M. Transactivation of Schizosaccharomyces pombe cdt2+ stimulates a Pcu4-Ddb1-CSN ubiquitin ligase. EMBO J. 2005, 24, 3940-3951.
    • (2005) EMBO J , vol.24 , pp. 3940-3951
    • Liu, C.1    Poitelea, M.2    Watson, A.3    Yoshida, S.H.4    Shimoda, C.5    Holmberg, C.6    Nielsen, O.7    Carr, A.M.8
  • 38
    • 57049097607 scopus 로고    scopus 로고
    • Intrinsic negative cell cycle regulation provided by PIP box- and Cul4Cdt2-mediated destruction of E2f1 during S phase
    • Shibutani, S.T.; de la Cruz, A.F.; Tran, V.; Turbyfill, W.J., 3rd.; Reis, T.; Edgar, B.A.; Duronio, R.J. Intrinsic negative cell cycle regulation provided by PIP box- and Cul4Cdt2-mediated destruction of E2f1 during S phase. Dev. Cell. 2008, 15, 890-900.
    • (2008) Dev. Cell , vol.15 , pp. 890-900
    • Shibutani, S.T.1    de la Cruz, A.F.2    Tran, V.3    Turbyfill, W.J.4    Reis, T.5    Edgar, B.A.6    Duronio, R.J.7
  • 39
    • 18344393150 scopus 로고    scopus 로고
    • The E2F transcriptional network: Old acquaintances with new faces
    • Dimova, D.K.; Dyson, N.J. The E2F transcriptional network: Old acquaintances with new faces. Oncogene 2005, 24, 2810-2826.
    • (2005) Oncogene , vol.24 , pp. 2810-2826
    • Dimova, D.K.1    Dyson, N.J.2
  • 41
    • 34547101263 scopus 로고    scopus 로고
    • Cell cycle regulation as a mechanism for functional separation of the apparently redundant uracil DNA glycosylases TDG and UNG2
    • Hardeland, U.; Kunz, C.; Focke, F.; Szadkowski, M.; Schar, P. Cell cycle regulation as a mechanism for functional separation of the apparently redundant uracil DNA glycosylases TDG and UNG2. Nucleic Acids Res. 2007, 35, 3859-3867.
    • (2007) Nucleic Acids Res , vol.35 , pp. 3859-3867
    • Hardeland, U.1    Kunz, C.2    Focke, F.3    Szadkowski, M.4    Schar, P.5
  • 42
    • 84905996782 scopus 로고    scopus 로고
    • CRL4Cdt2 E3 ubiquitin ligase and proliferating cell nuclear antigen (PCNA) cooperate to degrade thymine DNA glycosylase in S phase
    • Shibata, E.; Dar, A.; Dutta, A. CRL4Cdt2 E3 ubiquitin ligase and proliferating cell nuclear antigen (PCNA) cooperate to degrade thymine DNA glycosylase in S phase. J. Biol. Chem. 2014, 289, 23056-23064.
    • (2014) J. Biol. Chem , vol.289 , pp. 23056-23064
    • Shibata, E.1    Dar, A.2    Dutta, A.3
  • 44
    • 20344396122 scopus 로고    scopus 로고
    • Preventing re-replication of chromosomal DNA
    • Blow, J.J.; Dutta, A. Preventing re-replication of chromosomal DNA. Nat. Rev. Mol. Cell Biol. 2005, 6, 476-486.
    • (2005) Nat. Rev. Mol. Cell Biol , vol.6 , pp. 476-486
    • Blow, J.J.1    Dutta, A.2
  • 45
    • 30344455639 scopus 로고    scopus 로고
    • PCNA functions as a molecular platform to trigger Cdt1 destruction and prevent re-replication
    • Arias, E.E.; Walter, J.C. PCNA functions as a molecular platform to trigger Cdt1 destruction and prevent re-replication. Nat. Cell Biol. 2006, 8, 84-90.
    • (2006) Nat. Cell Biol , vol.8 , pp. 84-90
    • Arias, E.E.1    Walter, J.C.2
  • 46
    • 2342442851 scopus 로고    scopus 로고
    • Cyclin-dependent kinases phosphorylate human Cdt1 and induce its degradation
    • Liu, E.; Li, X.; Yan, F.; Zhao, Q.; Wu, X. Cyclin-dependent kinases phosphorylate human Cdt1 and induce its degradation. J. Biol. Chem. 2004, 279, 17283-17288.
    • (2004) J. Biol. Chem , vol.279 , pp. 17283-17288
    • Liu, E.1    Li, X.2    Yan, F.3    Zhao, Q.4    Wu, X.5
  • 47
    • 2442427423 scopus 로고    scopus 로고
    • Cdt1 phosphorylation by cyclin A-dependent kinases negatively regulates its function without affecting geminin binding
    • Sugimoto, N.; Tatsumi, Y.; Tsurumi, T.; Matsukage, A.; Kiyono, T.; Nishitani, H.; Fujita, M. Cdt1 phosphorylation by cyclin A-dependent kinases negatively regulates its function without affecting geminin binding. J. Biol. Chem. 2004, 279, 19691-19697.
    • (2004) J. Biol. Chem , vol.279 , pp. 19691-19697
    • Sugimoto, N.1    Tatsumi, Y.2    Tsurumi, T.3    Matsukage, A.4    Kiyono, T.5    Nishitani, H.6    Fujita, M.7
  • 48
    • 3142766071 scopus 로고    scopus 로고
    • Proteolysis of DNA replication licensing factor Cdt1 in S-phase is performed independently of geminin through its N-terminal region
    • Nishitani, H.; Lygerou, Z.; Nishimoto, T. Proteolysis of DNA replication licensing factor Cdt1 in S-phase is performed independently of geminin through its N-terminal region. J. Biol. Chem. 2004, 279, 30807-30816.
    • (2004) J. Biol. Chem , vol.279 , pp. 30807-30816
    • Nishitani, H.1    Lygerou, Z.2    Nishimoto, T.3
  • 50
    • 20744458539 scopus 로고    scopus 로고
    • Degradation of Cdt1 during S phase is Skp2-independent and is required for efficient progression of mammalian cells through S phase
    • Takeda, D.Y.; Parvin, J.D.; Dutta, A. Degradation of Cdt1 during S phase is Skp2-independent and is required for efficient progression of mammalian cells through S phase. J. Biol. Chem. 2005, 280, 23416-23423.
    • (2005) J. Biol. Chem , vol.280 , pp. 23416-23423
    • Takeda, D.Y.1    Parvin, J.D.2    Dutta, A.3
  • 51
    • 84903519467 scopus 로고    scopus 로고
    • SCF-FBXO31 E3 ligase targets DNA replication factor Cdt1 for proteolysis in the G2 phase of cell cycle to prevent re-replication
    • Johansson, P.; Jeffery, J.; Al-Ejeh, F.; Schulz, R.B.; Callen, D.F.; Kumar, R.; Khanna, K.K. SCF-FBXO31 E3 ligase targets DNA replication factor Cdt1 for proteolysis in the G2 phase of cell cycle to prevent re-replication. J. Biol. Chem. 2014, 289, 18514-18525.
    • (2014) J. Biol. Chem , vol.289 , pp. 18514-18525
    • Johansson, P.1    Jeffery, J.2    Al-Ejeh, F.3    Schulz, R.B.4    Callen, D.F.5    Kumar, R.6    Khanna, K.K.7
  • 52
    • 0034624819 scopus 로고    scopus 로고
    • The cyclin-dependent kinase Cdc28p regulates distinct modes of Cdc6p proteolysis during the budding yeast cell cycle
    • Drury, L.S.; Perkins, G.; Diffley, J.F. The cyclin-dependent kinase Cdc28p regulates distinct modes of Cdc6p proteolysis during the budding yeast cell cycle. Curr. Biol. 2000, 10, 231-240.
    • (2000) Curr. Biol , vol.10 , pp. 231-240
    • Drury, L.S.1    Perkins, G.2    Diffley, J.F.3
  • 53
    • 0032865839 scopus 로고    scopus 로고
    • Phosphorylation controls timing of Cdc6p destruction: A biochemical analysis
    • Elsasser, S.; Chi, Y.; Yang, P.; Campbell, J.L. Phosphorylation controls timing of Cdc6p destruction: A biochemical analysis. Mol. Biol. Cell. 1999, 10, 3263-3277.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 3263-3277
    • Elsasser, S.1    Chi, Y.2    Yang, P.3    Campbell, J.L.4
  • 54
    • 0030950644 scopus 로고    scopus 로고
    • Fission yeast WD-repeat protein pop1 regulates genome ploidy through ubiquitin-proteasome-mediated degradation of the CDK inhibitor Rum1 and the S-phase initiator Cdc18
    • Kominami, K.; Toda, T. Fission yeast WD-repeat protein pop1 regulates genome ploidy through ubiquitin-proteasome-mediated degradation of the CDK inhibitor Rum1 and the S-phase initiator Cdc18. Genes Dev. 1997, 11, 1548-1560.
    • (1997) Genes Dev , vol.11 , pp. 1548-1560
    • Kominami, K.1    Toda, T.2
  • 55
    • 0031921561 scopus 로고    scopus 로고
    • Human CDC6/Cdc18 associates with Orc1 and cyclin-cdk and is selectively eliminated from the nucleus at the onset of S phase
    • Saha, P.; Chen, J.; Thome, K.C.; Lawlis, S.J.; Hou, Z.H.; Hendricks, M.; Parvin, J.D.; Dutta, A. Human CDC6/Cdc18 associates with Orc1 and cyclin-cdk and is selectively eliminated from the nucleus at the onset of S phase. Mol. Cell Biol. 1998, 18, 2758-2767.
    • (1998) Mol. Cell Biol , vol.18 , pp. 2758-2767
    • Saha, P.1    Chen, J.2    Thome, K.C.3    Lawlis, S.J.4    Hou, Z.H.5    Hendricks, M.6    Parvin, J.D.7    Dutta, A.8
  • 56
    • 40549089206 scopus 로고    scopus 로고
    • Control of the Cdc6 replication licensing factor in metazoa: The role of nuclear export and the CUL4 ubiquitin ligase
    • Kim, J.; Kipreos, E.T. Control of the Cdc6 replication licensing factor in metazoa: The role of nuclear export and the CUL4 ubiquitin ligase. Cell Cycle. 2008, 7, 146-150.
    • (2008) Cell Cycle , vol.7 , pp. 146-150
    • Kim, J.1    Kipreos, E.T.2
  • 57
    • 84903363884 scopus 로고    scopus 로고
    • PIP-box-mediated degradation prohibits re-accumulation of Cdc6 during S phase
    • Clijsters, L.; Wolthuis, R. PIP-box-mediated degradation prohibits re-accumulation of Cdc6 during S phase. J. Cell Sci. 2014, 127, 1336-1345.
    • (2014) J. Cell Sci , vol.127 , pp. 1336-1345
    • Clijsters, L.1    Wolthuis, R.2
  • 58
    • 57049133181 scopus 로고    scopus 로고
    • CDK inhibitor p21 is degraded by a proliferating cell nuclear antigen-coupled Cul4-DDB1Cdt2 pathway during S phase and after UV irradiation
    • Nishitani, H.; Shiomi, Y.; Iida, H.; Michishita, M.; Takami, T.; Tsurimoto, T. CDK inhibitor p21 is degraded by a proliferating cell nuclear antigen-coupled Cul4-DDB1Cdt2 pathway during S phase and after UV irradiation. J. Biol. Chem. 2008, 283, 29045-29052.
    • (2008) J. Biol. Chem , vol.283 , pp. 29045-29052
    • Nishitani, H.1    Shiomi, Y.2    Iida, H.3    Michishita, M.4    Takami, T.5    Tsurimoto, T.6
  • 59
    • 0036208817 scopus 로고    scopus 로고
    • Human origin recognition complex large subunit is degraded by ubiquitin-mediated proteolysis after initiation of DNA replication
    • Mendez, J.; Zou-Yang, X.H.; Kim, S.Y.; Hidaka, M.; Tansey, W.P.; Stillman, B. Human origin recognition complex large subunit is degraded by ubiquitin-mediated proteolysis after initiation of DNA replication. Mol. Cell 2002, 9, 481-491.
    • (2002) Mol. Cell , vol.9 , pp. 481-491
    • Mendez, J.1    Zou-Yang, X.H.2    Kim, S.Y.3    Hidaka, M.4    Tansey, W.P.5    Stillman, B.6
  • 60
    • 0142071671 scopus 로고    scopus 로고
    • The ORC1 cycle in human cells: II. Dynamic changes in the human ORC complex during the cell cycle
    • Ohta, S.; Tatsumi, Y.; Fujita, M.; Tsurimoto, T.; Obuse, C. The ORC1 cycle in human cells: II. Dynamic changes in the human ORC complex during the cell cycle. J. Biol. Chem. 2003, 278, 41535-41540.
    • (2003) J. Biol. Chem , vol.278 , pp. 41535-41540
    • Ohta, S.1    Tatsumi, Y.2    Fujita, M.3    Tsurimoto, T.4    Obuse, C.5
  • 61
    • 84867263331 scopus 로고    scopus 로고
    • Orc2 protects ORCA from ubiquitin-mediated degradation
    • Shen, Z.; Prasanth, S.G. Orc2 protects ORCA from ubiquitin-mediated degradation. Cell Cycle. 2012, 11, 3578-3589.
    • (2012) Cell Cycle , vol.11 , pp. 3578-3589
    • Shen, Z.1    Prasanth, S.G.2
  • 62
    • 78149281634 scopus 로고    scopus 로고
    • The histone H4 Lys 20 methyltransferase PR-Set7 regulates replication origins in mammalian cells
    • Tardat, M.; Brustel, J.; Kirsh, O.; Lefevbre, C.; Callanan, M.; Sardet, C.; Julien, E. The histone H4 Lys 20 methyltransferase PR-Set7 regulates replication origins in mammalian cells. Nat. Cell Biol. 2010, 12, 1086-1093.
    • (2010) Nat. Cell Biol , vol.12 , pp. 1086-1093
    • Tardat, M.1    Brustel, J.2    Kirsh, O.3    Lefevbre, C.4    Callanan, M.5    Sardet, C.6    Julien, E.7
  • 63
    • 77957378110 scopus 로고    scopus 로고
    • CRL4(Cdt2) regulates cell proliferation and histone gene expression by targeting PR-Set7/Set8 for degradation
    • Abbas, T.; Shibata, E.; Park, J.; Jha, S.; Karnani, N.; Dutta, A. CRL4(Cdt2) regulates cell proliferation and histone gene expression by targeting PR-Set7/Set8 for degradation. Mol. Cell 2010, 40, 9-21.
    • (2010) Mol. Cell , vol.40 , pp. 9-21
    • Abbas, T.1    Shibata, E.2    Park, J.3    Jha, S.4    Karnani, N.5    Dutta, A.6
  • 64
  • 65
    • 84875806981 scopus 로고    scopus 로고
    • CRL1-FBXO11 promotes Cdt2 ubiquitylation and degradation and regulates Pr-Set7/Set8-mediated cellular migration
    • Abbas, T.; Mueller, A,C.; Shibata, E.; Keaton, M.; Rossi, M.; Dutta, A. CRL1-FBXO11 promotes Cdt2 ubiquitylation and degradation and regulates Pr-Set7/Set8-mediated cellular migration. Mol. Cell 2013, 49, 1147-1158.
    • (2013) Mol. Cell , vol.49 , pp. 1147-1158
    • Abbas, T.1    Mueller A, C.2    Shibata, E.3    Keaton, M.4    Rossi, M.5    Dutta, A.6
  • 66
    • 84907857808 scopus 로고    scopus 로고
    • 14-3-3 proteins play a role in the cell cycle by shielding cdt2 from ubiquitin-mediated degradation
    • Dar, A.; Wu, D.; Lee, N.; Shibata, E.; Dutta, A. 14-3-3 proteins play a role in the cell cycle by shielding cdt2 from ubiquitin-mediated degradation. Mol. Cell Biol. 2014, 34, 4049-4061.
    • (2014) Mol. Cell Biol , vol.34 , pp. 4049-4061
    • Dar, A.1    Wu, D.2    Lee, N.3    Shibata, E.4    Dutta, A.5
  • 67
  • 68
    • 84901643336 scopus 로고    scopus 로고
    • Replisome components-Post-translational modifications and their effects
    • Zech, J; Dalgaard, J.Z. Replisome components-Post-translational modifications and their effects. Semin. Cell Dev. Biol. 2014, 30, 144-153.
    • (2014) Semin. Cell Dev. Biol , vol.30 , pp. 144-153
    • Zech, J.1    Dalgaard, J.Z.2
  • 70
    • 29144501653 scopus 로고    scopus 로고
    • Ubiquitin/SUMO modification of PCNA promotes replication fork progression in Xenopus laevis egg extracts
    • Leach, C.A.; Michael, W.M. Ubiquitin/SUMO modification of PCNA promotes replication fork progression in Xenopus laevis egg extracts. J. Cell Biol. 2005, 171, 947-954.
    • (2005) J. Cell Biol , vol.171 , pp. 947-954
    • Leach, C.A.1    Michael, W.M.2
  • 71
    • 84901617265 scopus 로고    scopus 로고
    • MCM10: One tool for all-Integrity, maintenance and damage control
    • Thu, Y.M.; Bielinsky, A.K. MCM10: One tool for all-Integrity, maintenance and damage control. Semin. Cell Dev. Biol. 2014, 30, 121-130.
    • (2014) Semin. Cell Dev. Biol , vol.30 , pp. 121-130
    • Thu, Y.M.1    Bielinsky, A.K.2
  • 72
    • 6344284782 scopus 로고    scopus 로고
    • Mcm10 regulates the stability and chromatin association of DNA polymerase-alpha
    • Ricke, R.M.; Bielinsky, A.K. Mcm10 regulates the stability and chromatin association of DNA polymerase-alpha. Mol. Cell 2004, 16, 173-185.
    • (2004) Mol. Cell , vol.16 , pp. 173-185
    • Ricke, R.M.1    Bielinsky, A.K.2
  • 73
    • 33745469893 scopus 로고    scopus 로고
    • Interaction between PCNA and diubiquitinated Mcm10 is essential for cell growth in budding yeast
    • Das-Bradoo, S.; Ricke, R.M.; Bielinsky, A.K. Interaction between PCNA and diubiquitinated Mcm10 is essential for cell growth in budding yeast. Mol. Cell Biol. 2006, 26, 4806-4817.
    • (2006) Mol. Cell Biol , vol.26 , pp. 4806-4817
    • Das-Bradoo, S.1    Ricke, R.M.2    Bielinsky, A.K.3
  • 74
    • 33748294308 scopus 로고    scopus 로고
    • The p66 and p12 subunits of DNA polymerase delta are modified by ubiquitin and ubiquitin-like proteins
    • Liu, G.; Warbrick, E. The p66 and p12 subunits of DNA polymerase delta are modified by ubiquitin and ubiquitin-like proteins. Biochem. Biophys. Res. Commun. 2006, 349, 360-366.
    • (2006) Biochem. Biophys. Res. Commun , vol.349 , pp. 360-366
    • Liu, G.1    Warbrick, E.2
  • 75
    • 84873495712 scopus 로고    scopus 로고
    • Coordinated degradation of replisome components ensures genome stability upon replication stress in the absence of the replication fork protection complex
    • Roseaulin, L.C.; Noguchi, C.; Martinez, E.; Ziegler, M.A.; Toda, T.; Noguchi, E. Coordinated degradation of replisome components ensures genome stability upon replication stress in the absence of the replication fork protection complex. PLoS Genet. 2013, 9, e1003213.
    • (2013) PLoS Genet , vol.9
    • Roseaulin, L.C.1    Noguchi, C.2    Martinez, E.3    Ziegler, M.A.4    Toda, T.5    Noguchi, E.6
  • 76
    • 84883222131 scopus 로고    scopus 로고
    • Proteasome-dependent degradation of replisome components regulates faithful DNA replication
    • Roseaulin, L.C.; Noguchi, C.; Noguchi, E. Proteasome-dependent degradation of replisome components regulates faithful DNA replication. Cell Cycle 2013, 12, 2564-2569.
    • (2013) Cell Cycle , vol.12 , pp. 2564-2569
    • Roseaulin, L.C.1    Noguchi, C.2    Noguchi, E.3
  • 77
    • 77954852162 scopus 로고    scopus 로고
    • Ubiquitylation of FACT by the cullin-E3 ligase Rtt101 connects FACT to DNA replication
    • Han, J.; Li, Q.; McCullough, L.; Kettelkamp, C.; Formosa, T.; Zhang, Z. Ubiquitylation of FACT by the cullin-E3 ligase Rtt101 connects FACT to DNA replication. Genes Dev. 2010, 24, 1485-1490.
    • (2010) Genes Dev , vol.24 , pp. 1485-1490
    • Han, J.1    Li, Q.2    McCullough, L.3    Kettelkamp, C.4    Formosa, T.5    Zhang, Z.6
  • 78
    • 33746856074 scopus 로고    scopus 로고
    • de FACTo nucleosome dynamics.
    • Reinberg, D.; Sims, R.J., 3rd. de FACTo nucleosome dynamics. J. Biol. Chem. 2006, 281, 23297-23301.
    • (2006) J. Biol. Chem. , vol.281 , pp. 23297-23301
    • Reinberg, D.1    Sims, R.J.2
  • 80
    • 33748357745 scopus 로고    scopus 로고
    • Functional cooperation between FACT and MCM helicase facilitates initiation of chromatin DNA replication
    • Tan, B.C.; Chien, C.T.; Hirose, S.; Lee, S.C. Functional cooperation between FACT and MCM helicase facilitates initiation of chromatin DNA replication. EMBO J. 2006, 25, 3975-3985.
    • (2006) EMBO J , vol.25 , pp. 3975-3985
    • Tan, B.C.1    Chien, C.T.2    Hirose, S.3    Lee, S.C.4
  • 81
    • 77049107080 scopus 로고    scopus 로고
    • Restoring chromatin after replication: How new and old histone marks come together. Semin
    • Jasencakova, Z.; Groth, A. Restoring chromatin after replication: How new and old histone marks come together. Semin. Cell Dev. Biol. 2010, 21, 231-237.
    • (2010) Cell Dev. Biol , vol.21 , pp. 231-237
    • Jasencakova, Z.1    Groth, A.2
  • 82
    • 84857430552 scopus 로고    scopus 로고
    • Chromatin replication and epigenome maintenance
    • Alabert, C.; Groth, A. Chromatin replication and epigenome maintenance. Nat. Rev. Mol. Cell Biol. 2012, 13, 153-167.
    • (2012) Nat. Rev. Mol. Cell Biol , vol.13 , pp. 153-167
    • Alabert, C.1    Groth, A.2
  • 83
    • 0022482135 scopus 로고
    • Normal stoichiometry of histone dimer sets is necessary for high fidelity of mitotic chromosome transmission
    • Meeks-Wagner, D.; Hartwell, L.H. Normal stoichiometry of histone dimer sets is necessary for high fidelity of mitotic chromosome transmission. Cell 1986, 44, 43-52.
    • (1986) Cell , vol.44 , pp. 43-52
    • Meeks-Wagner, D.1    Hartwell, L.H.2
  • 84
    • 77950579010 scopus 로고    scopus 로고
    • Hsk1- and SCF(Pof3)-dependent proteolysis of S. pombe Ams2 ensures histone homeostasis and centromere function
    • Takayama, Y.; Mamnun, Y.M.; Trickey, M.; Dhut, S.; Masuda, F.; Yamano, H.; Toda, T.; Saitoh, S. Hsk1- and SCF(Pof3)-dependent proteolysis of S. pombe Ams2 ensures histone homeostasis and centromere function. Dev Cell. 2010, 18, 385-396.
    • (2010) Dev Cell , vol.18 , pp. 385-396
    • Takayama, Y.1    Mamnun, Y.M.2    Trickey, M.3    Dhut, S.4    Masuda, F.5    Yamano, H.6    Toda, T.7    Saitoh, S.8
  • 85
    • 84872316033 scopus 로고    scopus 로고
    • Anaphase-promoting complex/cyclosome-mediated proteolysis of Ams2 in the G1 phase ensures the coupling of histone gene expression to DNA replication in fission yeast
    • Trickey, M.; Fujimitsu, K.; Yamano, H. Anaphase-promoting complex/cyclosome-mediated proteolysis of Ams2 in the G1 phase ensures the coupling of histone gene expression to DNA replication in fission yeast. J. Biol. Chem. 2013, 288, 928-937.
    • (2013) J. Biol. Chem , vol.288 , pp. 928-937
    • Trickey, M.1    Fujimitsu, K.2    Yamano, H.3
  • 86
    • 0344688414 scopus 로고    scopus 로고
    • A Rad53 kinase-dependent surveillance mechanism that regulates histone protein levels in S. cerevisiae
    • Gunjan, A.; Verreault, A. A Rad53 kinase-dependent surveillance mechanism that regulates histone protein levels in S. cerevisiae. Cell 2003, 115, 537-549.
    • (2003) Cell , vol.115 , pp. 537-549
    • Gunjan, A.1    Verreault, A.2
  • 87
    • 68249094946 scopus 로고    scopus 로고
    • Histone levels are regulated by phosphorylation and ubiquitylation-dependent proteolysis
    • Singh, R.K.; Kabbaj, M.H.; Paik, J.; Gunjan, A. Histone levels are regulated by phosphorylation and ubiquitylation-dependent proteolysis. Nat. Cell Biol. 2009, 11, 925-933.
    • (2009) Nat. Cell Biol , vol.11 , pp. 925-933
    • Singh, R.K.1    Kabbaj, M.H.2    Paik, J.3    Gunjan, A.4
  • 88
    • 84860516339 scopus 로고    scopus 로고
    • Novel E3 ubiquitin ligases that regulate histone protein levels in the budding yeast Saccharomyces cerevisiae
    • Singh, R.K.; Gonzalez, M.; Kabbaj, M.H.; Gunjan, A. Novel E3 ubiquitin ligases that regulate histone protein levels in the budding yeast Saccharomyces cerevisiae. PLoS ONE 2012, 7, e36295.
    • (2012) PLoS ONE , vol.7
    • Singh, R.K.1    Gonzalez, M.2    Kabbaj, M.H.3    Gunjan, A.4
  • 89
    • 15044354179 scopus 로고    scopus 로고
    • Characterization of E3Histone, a novel testis ubiquitin protein ligase which ubiquitinates histones
    • Liu, Z.; Oughtred, R.; Wing, S.S. Characterization of E3Histone, a novel testis ubiquitin protein ligase which ubiquitinates histones. Mol. Cell Biol. 2005, 25, 2819-2831.
    • (2005) Mol. Cell Biol , vol.25 , pp. 2819-2831
    • Liu, Z.1    Oughtred, R.2    Wing, S.S.3
  • 90
    • 84887899338 scopus 로고    scopus 로고
    • A Cul4 E3 ubiquitin ligase regulates histone hand-off during nucleosome assembly
    • Han, J.; Zhang, H.; Wang, Z.; Zhou, H.; Zhang, Z. A Cul4 E3 ubiquitin ligase regulates histone hand-off during nucleosome assembly. Cell 2013, 155, 817-829.
    • (2013) Cell , vol.155 , pp. 817-829
    • Han, J.1    Zhang, H.2    Wang, Z.3    Zhou, H.4    Zhang, Z.5
  • 91
    • 46149091721 scopus 로고    scopus 로고
    • H2B ubiquitylation plays a role in nucleosome dynamics during transcription elongation
    • Fleming, A.B.; Kao, C.F.; Hillyer, C.; Pikaart, M.; Osley, M.A. H2B ubiquitylation plays a role in nucleosome dynamics during transcription elongation. Mol. Cell 2008, 31, 57-66.
    • (2008) Mol. Cell , vol.31 , pp. 57-66
    • Fleming, A.B.1    Kao, C.F.2    Hillyer, C.3    Pikaart, M.4    Osley, M.A.5
  • 92
    • 15444373985 scopus 로고    scopus 로고
    • The DNA damage checkpoint response requires histone H2B ubiquitination by Rad6-Bre1 and H3 methylation by Dot1
    • Giannattasio, M.; Lazzaro, F.; Plevani, P.; Muzi-Falconi, M. The DNA damage checkpoint response requires histone H2B ubiquitination by Rad6-Bre1 and H3 methylation by Dot1. J. Biol. Chem. 2005, 280, 9879-9886.
    • (2005) J. Biol. Chem , vol.280 , pp. 9879-9886
    • Giannattasio, M.1    Lazzaro, F.2    Plevani, P.3    Muzi-Falconi, M.4
  • 93
    • 63049135667 scopus 로고    scopus 로고
    • The role of RAD6 in recombinational repair, checkpoints and meiosis via histone modification
    • Game, J.C.; Chernikova, S.B. The role of RAD6 in recombinational repair, checkpoints and meiosis via histone modification. DNA Repair 2009, 8, 470-482.
    • (2009) DNA Repair , vol.8 , pp. 470-482
    • Game, J.C.1    Chernikova, S.B.2
  • 94
    • 77958102720 scopus 로고    scopus 로고
    • Deficiency in Bre1 impairs homologous recombination repair and cell cycle checkpoint response to radiation damage in mammalian cells
    • Chernikova, S.B.; Dorth, J.A.; Razorenova, O.V; Game, J.C.; Brown, J.M. Deficiency in Bre1 impairs homologous recombination repair and cell cycle checkpoint response to radiation damage in mammalian cells. Radiat. Res. 2010, 174, 558-565.
    • (2010) Radiat. Res , vol.174 , pp. 558-565
    • Chernikova, S.B.1    Dorth, J.A.2    Razorenova, O.V.3    Game, J.C.4    Brown, J.M.5
  • 95
    • 80052288217 scopus 로고    scopus 로고
    • Chromatin signaling to kinetochores: Transregulation of Dam1 methylation by histone H2B ubiquitination
    • Latham, J.A.; Chosed, R.J.; Wang, S.; Dent, S.Y. Chromatin signaling to kinetochores: Transregulation of Dam1 methylation by histone H2B ubiquitination. Cell 2011, 146, 709-719.
    • (2011) Cell , vol.146 , pp. 709-719
    • Latham, J.A.1    Chosed, R.J.2    Wang, S.3    Dent, S.Y.4
  • 96
    • 84870912857 scopus 로고    scopus 로고
    • A role for H2B ubiquitylation in DNA replication
    • Trujillo, K.M.; Osley, M.A. A role for H2B ubiquitylation in DNA replication. Mol. Cell 2012, 48, 734-746.
    • (2012) Mol. Cell , vol.48 , pp. 734-746
    • Trujillo, K.M.1    Osley, M.A.2
  • 98
    • 79955069748 scopus 로고    scopus 로고
    • Recruitment of Dnmt1 roles of the SRA protein Np95 (Uhrf1) and other factors
    • Sharif, J.; Koseki, H. Recruitment of Dnmt1 roles of the SRA protein Np95 (Uhrf1) and other factors. Prog. Mol. Biol. Transl. Sci. 2011, 101, 289-310.
    • (2011) Prog. Mol. Biol. Transl. Sci , vol.101 , pp. 289-310
    • Sharif, J.1    Koseki, H.2
  • 99
    • 84928110660 scopus 로고    scopus 로고
    • Conserved linker regions and their regulation determine multiple chromatin-binding modes of UHRF1
    • Tauber, M.; Fischle, W. Conserved linker regions and their regulation determine multiple chromatin-binding modes of UHRF1. Nucleus 2015, 6, 123-132.
    • (2015) Nucleus , vol.6 , pp. 123-132
    • Tauber, M.1    Fischle, W.2
  • 100
    • 84908248970 scopus 로고    scopus 로고
    • Cdc48 and a ubiquitin ligase drive disassembly of the CMG helicase at the end of DNA replication
    • Maric, M.; Maculins, T.; De Piccoli, G.; Labib, K. Cdc48 and a ubiquitin ligase drive disassembly of the CMG helicase at the end of DNA replication. Science 2014, 346, doi:10.1126/science.1253596.
    • (2014) Science , vol.346
    • Maric, M.1    Maculins, T.2    De Piccoli, G.3    Labib, K.4
  • 101
    • 84908257634 scopus 로고    scopus 로고
    • Polyubiquitylation drives replisome disassembly at the termination of DNA replication
    • Moreno, S.P.; Bailey, R.; Campion, N.; Herron, S.; Gambus, A. Polyubiquitylation drives replisome disassembly at the termination of DNA replication. Science 2014, 346, 477-481.
    • (2014) Science , vol.346 , pp. 477-481
    • Moreno, S.P.1    Bailey, R.2    Campion, N.3    Herron, S.4    Gambus, A.5
  • 102
    • 0025314878 scopus 로고
    • An abundant and ubiquitous homo-oligomeric ring-shaped ATPase particle related to the putative vesicle fusion proteins Sec18p and NSF
    • Peters, J.M.; Walsh, M.J.; Franke, W.W. An abundant and ubiquitous homo-oligomeric ring-shaped ATPase particle related to the putative vesicle fusion proteins Sec18p and NSF. EMBO J. 1990, 9, 1757-1767.
    • (1990) EMBO J , vol.9 , pp. 1757-1767
    • Peters, J.M.1    Walsh, M.J.2    Franke, W.W.3
  • 105
    • 84886387458 scopus 로고    scopus 로고
    • Role of p97/VCP (Cdc48) in genome stability
    • Vaz, B.; Halder, S.; Ramadan, K. Role of p97/VCP (Cdc48) in genome stability. Front. Genet. 2013, 4, doi:10.3389/fgene.2013.00060.
    • (2013) Front. Genet , vol.4
    • Vaz, B.1    Halder, S.2    Ramadan, K.3
  • 106
    • 30744451400 scopus 로고    scopus 로고
    • Functional division of substrate processing cofactors of the ubiquitinselective Cdc48 chaperone
    • Rumpf, S.; Jentsch, S. Functional division of substrate processing cofactors of the ubiquitinselective Cdc48 chaperone. Mol. Cell 2006, 21, 261-269.
    • (2006) Mol. Cell , vol.21 , pp. 261-269
    • Rumpf, S.1    Jentsch, S.2
  • 107
    • 70450265298 scopus 로고    scopus 로고
    • The amino-terminal TPR domain of Dia2 tethers SCF(Dia2) to the replisome progression complex
    • Morohashi, H.; Maculins, T.; Labib, K. The amino-terminal TPR domain of Dia2 tethers SCF(Dia2) to the replisome progression complex. Curr. Biol. 2009, 19, 1943-1949.
    • (2009) Curr. Biol , vol.19 , pp. 1943-1949
    • Morohashi, H.1    Maculins, T.2    Labib, K.3
  • 110
    • 71249158149 scopus 로고    scopus 로고
    • SCF(Dia2) regulates DNA replication forks during S-phase in budding yeast
    • Mimura, S.; Komata, M.; Kishi, T.; Shirahige, K.; Kamura, T. SCF(Dia2) regulates DNA replication forks during S-phase in budding yeast. EMBO J. 2009, 28, 3693-3705.
    • (2009) EMBO J , vol.28 , pp. 3693-3705
    • Mimura, S.1    Komata, M.2    Kishi, T.3    Shirahige, K.4    Kamura, T.5
  • 111
    • 79251473377 scopus 로고    scopus 로고
    • Will the ubiquitin system furnish as many drug targets as protein kinases?
    • Cohen, P.; Tcherpakov, M. Will the ubiquitin system furnish as many drug targets as protein kinases? Cell 2010, 143, 686-693.
    • (2010) Cell , vol.143 , pp. 686-693
    • Cohen, P.1    Tcherpakov, M.2
  • 112
    • 84874995996 scopus 로고    scopus 로고
    • Cullin-RING Ligases as attractive anti-cancer targets
    • Zhao, Y.; Sun, Y. Cullin-RING Ligases as attractive anti-cancer targets. Curr. Pharm. Des. 2013, 19, 3215-3225.
    • (2013) Curr. Pharm. Des , vol.19 , pp. 3215-3225
    • Zhao, Y.1    Sun, Y.2
  • 114
    • 78650355357 scopus 로고    scopus 로고
    • NEDD8-targeting drug MLN4924 elicits DNA rereplication by stabilizing Cdt1 in S phase, triggering checkpoint activation, apoptosis, and senescence in cancer cells
    • Lin, J.J.; Milhollen, M.A.; Smith, P.G.; Narayanan, U.; Dutta, A. NEDD8-targeting drug MLN4924 elicits DNA rereplication by stabilizing Cdt1 in S phase, triggering checkpoint activation, apoptosis, and senescence in cancer cells. Cancer Res. 2010, 70, 10310-10320.
    • (2010) Cancer Res , vol.70 , pp. 10310-10320
    • Lin, J.J.1    Milhollen, M.A.2    Smith, P.G.3    Narayanan, U.4    Dutta, A.5
  • 115
    • 67449119401 scopus 로고    scopus 로고
    • Targeting NEDD8-activated cullin-RING ligases for the treatment of cancer
    • Soucy, T.A.; Smith, P.G.; Rolfe, M. Targeting NEDD8-activated cullin-RING ligases for the treatment of cancer. Clin. Cancer Res. 2009, 15, 3912-3916.
    • (2009) Clin. Cancer Res , vol.15 , pp. 3912-3916
    • Soucy, T.A.1    Smith, P.G.2    Rolfe, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.