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Volumn 289, Issue 33, 2014, Pages 23043-23055

Thymine DNA glycosylase is a CRL4Cdt2 substrate

Author keywords

[No Author keywords available]

Indexed keywords

CELL PROLIFERATION; ENZYMES; SUBSTRATES;

EID: 84905966945     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.574194     Document Type: Article
Times cited : (36)

References (67)
  • 1
    • 79551564537 scopus 로고    scopus 로고
    • Cdt2: Master coordinator of cell cycle progression and genome stability
    • Cdt2: master coordinator of cell cycle progression and genome stability. Cell Cycle 10, 241-249
    • (2011) Cell Cycle , vol.10 , pp. 241-249
    • Abbas, T.1    Dutta, A.2
  • 2
    • 80051525031 scopus 로고    scopus 로고
    • Cdt2, a PCNA-dependent E3 ubiquitin ligase
    • Cdt2, a PCNA-dependent E3 ubiquitin ligase. Genes Dev. 25, 1568-1582
    • (2011) Genes Dev. , vol.25 , pp. 1568-1582
    • Havens, C.G.1    Walter, J.C.2
  • 3
    • 33747873322 scopus 로고    scopus 로고
    • A Family of Diverse Cul4-Ddb1-Interacting Proteins Includes Cdt2, which Is Required for S Phase Destruction of the Replication Factor Cdt1
    • DOI 10.1016/j.molcel.2006.08.010, PII S1097276506005703
    • Jin, J., Arias, E. E., Chen, J., Harper, J. W., and Walter, J. C. (2006) A family of diverse Cul4-Ddb1-interacting proteins includes Cdt2, which is required for S phase destruction of the replication factor Cdt1. Mol. Cell 23, 709-721 (Pubitemid 44292562)
    • (2006) Molecular Cell , vol.23 , Issue.5 , pp. 709-721
    • Jin, J.1    Arias, E.E.2    Chen, J.3    Harper, J.W.4    Walter, J.C.5
  • 4
    • 33747831132 scopus 로고    scopus 로고
    • L2DTL/CDT2 interacts with the CUL4/DDB1 complex and PCNA and regulates CDT1 proteolysis in response to DNA damage
    • Higa, L. A., Banks, D., Wu, M., Kobayashi, R., Sun, H., and Zhang, H. (2006) L2DTL/CDT2 interacts with the CUL4/DDB1 complex and PCNA and regulates CDT1 proteolysis in response to DNA damage. Cell Cycle 5, 1675-1680 (Pubitemid 44285255)
    • (2006) Cell Cycle , vol.5 , Issue.15 , pp. 1675-1680
    • Higa, L.A.1    Banks, D.2    Wu, M.3    Kobayashi, R.4    Sun, H.5    Zhang, H.6
  • 5
    • 33750495610 scopus 로고    scopus 로고
    • DNA damage induces Cdt1 proteolysis in fission yeast through a pathway dependent on Cdt2 and Ddb1
    • DOI 10.1038/sj.embor.7400827, PII 7400827
    • Ralph, E., Boye, E., and Kearsey, S. E. (2006) DNA damage induces Cdt1 proteolysis in fission yeast through a pathway dependent on Cdt2 and Ddb1. EMBO Rep. 7, 1134-1139 (Pubitemid 44660570)
    • (2006) EMBO Reports , vol.7 , Issue.11 , pp. 1134-1139
    • Ralph, E.1    Boye, E.2    Kearsey, S.E.3
  • 8
    • 77957378110 scopus 로고    scopus 로고
    • Cdt2 regulates cell proliferation and histone gene expression by targeting PR-Set7/Set8 for degradation
    • Cdt2 regulates cell proliferation and histone gene expression by targeting PR-Set7/Set8 for degradation. Mol. Cell 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
  • 16
    • 0038185375 scopus 로고    scopus 로고
    • Cop9/signalosome subunits and Pcu4 regulate ribonucleotide reductase by both checkpoint-dependent and -independent mechanisms
    • DOI 10.1101/gad.1090803
    • Liu, C., Powell, K. A., Mundt, K., Wu, L., Carr, A. M., and Caspari, T. (2003) Cop9/signalosome subunits and Pcu4 regulate ribonucleotide reductase by both checkpoint-dependent and -independent mechanisms. Genes Dev. 17, 1130-1140 (Pubitemid 36534987)
    • (2003) Genes and Development , vol.17 , Issue.9 , pp. 1130-1140
    • Liu, C.1    Powell, K.A.2    Mundt, K.3    Wu, L.4    Carr, A.M.5    Caspari, T.6
  • 18
    • 77956635549 scopus 로고    scopus 로고
    • Cdt2 ubiquitin ligase mediates the proteolysis of cyclin-dependent kinase inhibitor Xic1 through a direct association with PCNA
    • Cdt2 ubiquitin ligase mediates the proteolysis of cyclin-dependent kinase inhibitor Xic1 through a direct association with PCNA. Mol. Cell. Biol. 30, 4120-4133
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 4120-4133
    • Kim, D.H.1    Budhavarapu, V.N.2    Herrera, C.R.3    Nam, H.W.4    Kim, Y.S.5    Yew, P.R.6
  • 19
    • 33646504727 scopus 로고    scopus 로고
    • PCNA is a cofactor for CDT1 degradation by CUL4/DDB1-mediated N-terminal ubiquitination
    • DOI 10.1074/jbc.M512705200
    • Senga, T., Sivaprasad, U., Zhu, W., Park, J. H., Arias, E. E., Walter, J. C., and Dutta, A. (2006) PCNA is a cofactor for Cdt1 degradation by CUL4/DDB1-mediated N-terminal ubiquitination. J. Biol. Chem. 281, 6246-6252 (Pubitemid 43847555)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.10 , pp. 6246-6252
    • Senga, T.1    Sivaprasad, U.2    Zhu, W.3    Jong, J.P.4    Arias, E.E.5    Walter, J.C.6    Dutta, A.7
  • 20
    • 0035976980 scopus 로고    scopus 로고
    • 1 and is destabilized after initiation of S-phase
    • 1 and is destabilized after initiation of S-phase. J. Biol. Chem. 276, 44905-44911
    • (2001) J. Biol. Chem. , vol.276 , pp. 44905-44911
    • Nishitani, H.1
  • 21
    • 34249066085 scopus 로고    scopus 로고
    • PCNA, the Maestro of the Replication Fork
    • DOI 10.1016/j.cell.2007.05.003, PII S0092867407005946
    • Moldovan, G.-L., Pfander, B., and Jentsch, S. (2007) PCNA, the maestro of the replication fork. Cell 129, 665-679 (Pubitemid 46802385)
    • (2007) Cell , vol.129 , Issue.4 , pp. 665-679
    • Moldovan, G.-L.1    Pfander, B.2    Jentsch, S.3
  • 25
    • 0037086643 scopus 로고    scopus 로고
    • Modification of the human thymine-DNA glycosylase by ubiquitin-like proteins facilitates enzymatic turnover
    • DOI 10.1093/emboj/21.6.1456
    • Hardeland, U., Steinacher, R., Jiricny, J., and Schär, P. (2002) Modification of the human thymine-DNA glycosylase by ubiquitin-like proteins facilitates enzymatic turnover. EMBO J. 21, 1456-1464 (Pubitemid 34246524)
    • (2002) EMBO Journal , vol.21 , Issue.6 , pp. 1456-1464
    • Hardeland, U.1    Steinacher, R.2    Jiricny, J.3    Schar, P.4
  • 26
    • 79351468704 scopus 로고    scopus 로고
    • SUMO-1 regulates the conformational dynamics of thymine-DNA glycosylase regulatory domain and competes with its DNA binding activity
    • Smet-Nocca, C., Wieruszeski, J.-M., Léger, H., Eilebrecht, S., and Benecke, A. (2011) SUMO-1 regulates the conformational dynamics of thymine-DNA glycosylase regulatory domain and competes with its DNA binding activity. BMC Biochem. 12, 4
    • (2011) BMC Biochem. , vol.12 , pp. 4
    • Smet-Nocca, C.1    Wieruszeski, J.-M.2    Léger, H.3    Eilebrecht, S.4    Benecke, A.5
  • 28
    • 34547101263 scopus 로고    scopus 로고
    • Cell cycle regulation as a mechanism for functional separation of the apparently redundant uracil DNA glycosylases TDG and UNG2
    • DOI 10.1093/nar/gkm337
    • Hardeland, U., Kunz, C., Focke, F., Szadkowski, M., and Schär, P. (2007) Cell cycle regulation as a mechanism for functional separation of the apparently redundant uracil DNA glycosylases TDG and UNG2. Nucleic Acids Res. 35, 3859-3867 (Pubitemid 47244677)
    • (2007) Nucleic Acids Research , vol.35 , Issue.11 , pp. 3859-3867
    • Hardeland, U.1    Kunz, C.2    Focke, F.3    Szadkowski, M.4    Schar, P.5
  • 29
    • 84892763878 scopus 로고    scopus 로고
    • Reversing DNA methylation: Mechanisms, genomics, and biological functions
    • Wu, H., and Zhang, Y. (2014) Reversing DNA methylation: mechanisms, genomics, and biological functions. Cell 156, 45-68
    • (2014) Cell , vol.156 , pp. 45-68
    • Wu, H.1    Zhang, Y.2
  • 31
    • 80052461558 scopus 로고    scopus 로고
    • Tet proteins can convert 5-methylcytosine to 5-formylcytosine and 5-carboxylcytosine
    • Ito, S., Shen, L., Dai, Q., Wu, S. C., Collins, L. B., Swenberg, J. A., He, C., and Zhang, Y. (2011) Tet proteins can convert 5-methylcytosine to 5-formylcytosine and 5-carboxylcytosine. Science 333, 1300-1303
    • (2011) Science , vol.333 , pp. 1300-1303
    • Ito, S.1    Shen, L.2    Dai, Q.3    Wu, S.C.4    Collins, L.B.5    Swenberg, J.A.6    He, C.7    Zhang, Y.8
  • 32
    • 79955538247 scopus 로고    scopus 로고
    • Hydroxylation of 5-methylcytosine by TET1 promotes active DNA demethylation in the adult brain
    • Guo, J. U., Su, Y., Zhong, C., Ming, G.-L., and Song, H. (2011) Hydroxylation of 5-methylcytosine by TET1 promotes active DNA demethylation in the adult brain. Cell 145, 423-434
    • (2011) Cell , vol.145 , pp. 423-434
    • Guo, J.U.1    Su, Y.2    Zhong, C.3    Ming, G.-L.4    Song, H.5
  • 35
    • 84862776719 scopus 로고    scopus 로고
    • Thymine DNA glycosylase specifically recognizes 5-carboxylcytosine- modified DNA
    • Zhang, L., Lu, X., Lu, J., Liang, H., Dai, Q., Xu, G.-L., Luo, C., Jiang, H., and He, C. (2012) Thymine DNA glycosylase specifically recognizes 5-carboxylcytosine-modified DNA. Nat. Chem. Biol. 8, 328-330
    • (2012) Nat. Chem. Biol. , vol.8 , pp. 328-330
    • Zhang, L.1    Lu, X.2    Lu, J.3    Liang, H.4    Dai, Q.5    Xu, G.-L.6    Luo, C.7    Jiang, H.8    He, C.9
  • 36
    • 80053917872 scopus 로고    scopus 로고
    • Thymine DNA glycosylase can rapidly excise 5-formylcytosine and 5-carboxylcytosine: Potential implications for active demethylation of CpG sites
    • Maiti, A., and Drohat, A. C. (2011) Thymine DNA glycosylase can rapidly excise 5-formylcytosine and 5-carboxylcytosine: potential implications for active demethylation of CpG sites. J. Biol. Chem. 286, 35334-35338
    • (2011) J. Biol. Chem. , vol.286 , pp. 35334-35338
    • Maiti, A.1    Drohat, A.C.2
  • 37
    • 79952763586 scopus 로고    scopus 로고
    • Reprogramming of the paternal genome upon fertilization involves genome-wide oxidation of 5-methylcytosine
    • Iqbal, K., Jin, S.-G., Pfeifer, G. P., and Szabó, P. E. (2011) Reprogramming of the paternal genome upon fertilization involves genome-wide oxidation of 5-methylcytosine. Proc. Natl. Acad. Sci. U.S.A. 108, 3642-3647
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 3642-3647
    • Iqbal, K.1    Jin, S.-G.2    Pfeifer, G.P.3    Szabó, P.E.4
  • 38
    • 82655187105 scopus 로고    scopus 로고
    • Generation and replication-dependent dilution of 5fC and 5caC during mouse preimplantation development
    • Inoue, A., Shen, L., Dai, Q., He, C., and Zhang, Y. (2011) Generation and replication-dependent dilution of 5fC and 5caC during mouse preimplantation development. Cell Res. 21, 1670-1676
    • (2011) Cell Res. , vol.21 , pp. 1670-1676
    • Inoue, A.1    Shen, L.2    Dai, Q.3    He, C.4    Zhang, Y.5
  • 39
    • 80054097425 scopus 로고    scopus 로고
    • Replication-dependent loss of 5-hydroxymethylcytosine in mouse preimplantation embryos
    • Inoue, A., and Zhang, Y. (2011) Replication-dependent loss of 5-hydroxymethylcytosine in mouse preimplantation embryos. Science 334, 194-194
    • (2011) Science , vol.334 , pp. 194-194
    • Inoue, A.1    Zhang, Y.2
  • 40
    • 10644282845 scopus 로고    scopus 로고
    • Activation-induced cytidine deaminase deaminates 5-methylcytosine in DNA and is expressed in pluripotent tissues: Implications for epigenetic reprogramming
    • DOI 10.1074/jbc.M407695200
    • Morgan, H. D., Dean, W., Coker, H. A., Reik, W., and Petersen-Mahrt, S. K. (2004) Activation-induced cytidine deaminase deaminates 5-methylcytosine in DNA and is expressed in pluripotent tissues: implications for epigenetic reprogramming. J. Biol. Chem. 279, 52353-52360 (Pubitemid 39656611)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.50 , pp. 52353-52360
    • Morgan, H.D.1    Dean, W.2    Coker, H.A.3    Reik, W.4    Petersen-Mahrt, S.K.5
  • 41
    • 57649196594 scopus 로고    scopus 로고
    • DNA demethylation in zebrafish involves the coupling of a deaminase, a glycosylase, and Gadd45
    • Rai, K., Huggins, I. J., James, S. R., Karpf, A. R., Jones, D. A., and Cairns, B. R. (2008) DNA demethylation in zebrafish involves the coupling of a deaminase, a glycosylase, and Gadd45. Cell 135, 1201-1212
    • (2008) Cell , vol.135 , pp. 1201-1212
    • Rai, K.1    Huggins, I.J.2    James, S.R.3    Karpf, A.R.4    Jones, D.A.5    Cairns, B.R.6
  • 43
    • 77249148019 scopus 로고    scopus 로고
    • Genome-wide erasure of DNA methylation in mouse primordial germ cells is affected by AID deficiency
    • Popp, C., Dean, W., Feng, S., Cokus, S. J., Andrews, S., Pellegrini, M., Jacobsen, S. E., and Reik, W. (2010) Genome-wide erasure of DNA methylation in mouse primordial germ cells is affected by AID deficiency. Nature 463, 1101-1105
    • (2010) Nature , vol.463 , pp. 1101-1105
    • Popp, C.1    Dean, W.2    Feng, S.3    Cokus, S.J.4    Andrews, S.5    Pellegrini, M.6    Jacobsen, S.E.7    Reik, W.8
  • 45
    • 68349151239 scopus 로고    scopus 로고
    • DNA replication in nucleus-free Xenopus egg extracts
    • Lebofsky, R., Takahashi, T., and Walter, J. C. (2009) DNA replication in nucleus-free Xenopus egg extracts. Methods Mol. Biol. 521, 229-252
    • (2009) Methods Mol. Biol. , vol.521 , pp. 229-252
    • Lebofsky, R.1    Takahashi, T.2    Walter, J.C.3
  • 46
    • 0242361583 scopus 로고    scopus 로고
    • DNA damage-induced replication arrest in Xenopus egg extracts
    • Stokes, M. P. (2003) DNA damage-induced replication arrest in Xenopus egg extracts. J. Cell Biol. 163, 245-255
    • (2003) J. Cell Biol. , vol.163 , pp. 245-255
    • Stokes, M.P.1
  • 47
    • 30344455639 scopus 로고    scopus 로고
    • PCNA functions as a molecular platform to trigger Cdt1 destruction and prevent re-replication
    • DOI 10.1038/ncb1346, PII N1346
    • Arias, E. E., and Walter, J. C. (2006) PCNA functions as a molecular platform to trigger Cdt1 destruction and prevent re-replication. Nat. Cell Biol. 8, 84-90 (Pubitemid 43064801)
    • (2006) Nature Cell Biology , vol.8 , Issue.1 , pp. 84-90
    • Arias, E.E.1    Walter, J.C.2
  • 48
    • 0034704221 scopus 로고    scopus 로고
    • Inhibition of eukaryotic DNA replication by geminin binding to Cdt1
    • Wohlschlegel, J. A. (2000) Inhibition of eukaryotic DNA replication by geminin binding to Cdt1. Science 290, 2309-2312
    • (2000) Science , vol.290 , pp. 2309-2312
    • Wohlschlegel, J.A.1
  • 52
    • 45449113739 scopus 로고    scopus 로고
    • Bacterial expression and purification of interleukin-2 tyrosine kinase: Single step separation of the chaperonin impurity
    • Joseph, R. E., and Andreotti, A. H. (2008) Bacterial expression and purification of interleukin-2 tyrosine kinase: single step separation of the chaperonin impurity. Protein Expr. Purif. 60, 194-197
    • (2008) Protein Expr. Purif. , vol.60 , pp. 194-197
    • Joseph, R.E.1    Andreotti, A.H.2
  • 53
    • 11844273174 scopus 로고    scopus 로고
    • Replication-dependent destruction of Cdt1 limits DNA replication to a single round per cell cycle in Xenopus egg extracts
    • DOI 10.1101/gad.1255805
    • Arias, E. E., and Walter, J. C. (2005) Replication-dependent destruction of Cdt1 limits DNA replication to a single round per cell cycle in Xenopus egg extracts. Genes Dev. 19, 114-126 (Pubitemid 40095821)
    • (2005) Genes and Development , vol.19 , Issue.1 , pp. 114-126
    • Arias, E.E.1    Walter, J.C.2
  • 54
    • 0032015702 scopus 로고    scopus 로고
    • Regulated chromosomal DNA replication in the absence of a nucleus
    • Walter, J., Sun, L., and Newport, J. (1998) Regulated chromosomal DNA replication in the absence of a nucleus. Mol. Cell 1, 519-529 (Pubitemid 128374688)
    • (1998) Molecular Cell , vol.1 , Issue.4 , pp. 519-529
    • Walter, J.1    Sun, L.2    Newport, J.3
  • 55
    • 0033637837 scopus 로고    scopus 로고
    • Initiation of eukaryotic DNA replication: Origin unwinding and sequential chromatin association of Cdc45, RPA, and DNA polymerase α
    • Walter, J., and Newport, J. (2000) Initiation of eukaryotic DNA replication: origin unwinding and sequential chromatin association of Cdc45, RPA, and DNA polymerase α. Mol. Cell 5, 617-627
    • (2000) Mol. Cell , vol.5 , pp. 617-627
    • Walter, J.1    Newport, J.2
  • 56
    • 0025284348 scopus 로고
    • Completion of DNA replication is monitored by a feedback system that controls the initiation of mitosis in vitro: Studies in Xenopus
    • Dasso, M., and Newport, J. W. (1990) Completion of DNA replication is monitored by a feedback system that controls the initiation of mitosis in vitro: studies in Xenopus. Cell 61, 811-823
    • (1990) Cell , vol.61 , pp. 811-823
    • Dasso, M.1    Newport, J.W.2
  • 57
    • 0034721829 scopus 로고    scopus 로고
    • Separating substrate recognition from base hydrolysis in human thymine DNA glycosylase by mutational analysis
    • Hardeland, U., Bentele, M., Jiricny, J., and Schär, P. (2000) Separating substrate recognition from base hydrolysis in human thymine DNA glycosylase by mutational analysis. J. Biol. Chem. 275, 33449-33456
    • (2000) J. Biol. Chem. , vol.275 , pp. 33449-33456
    • Hardeland, U.1    Bentele, M.2    Jiricny, J.3    Schär, P.4
  • 58
    • 33644746214 scopus 로고    scopus 로고
    • Germ layers to organs: Using Xenopus to study "later" development
    • DOI 10.1016/j.semcdb.2005.11.002, PII S1084952105001138
    • Blitz, I. L., Andelfinger, G., and Horb, M. E. (2006) Germ layers to organs: using Xenopus to study "later" development. Semin. Cell Dev. Biol. 17, 133-145 (Pubitemid 43344470)
    • (2006) Seminars in Cell and Developmental Biology , vol.17 , Issue.1 , pp. 133-145
    • Blitz, I.L.1    Andelfinger, G.2    Horb, M.E.3
  • 60
    • 0036184090 scopus 로고    scopus 로고
    • Association of CBP/p300 acetylase and thymine DNA glycosylase links DNA repair and transcription
    • DOI 10.1016/S1097-2765(02)00453-7
    • Tini, M., Benecke, A., Um, S.-J., Torchia, J., Evans, R. M., and Chambon, P. (2002) Association of CBP/p300 acetylase and thymine DNA glycosylase links DNA repair and transcription. Mol. Cell 9, 265-277 (Pubitemid 34195553)
    • (2002) Molecular Cell , vol.9 , Issue.2 , pp. 265-277
    • Tini, M.1    Benecke, A.2    Um, S.-J.3    Torchia, J.4    Evans, R.M.5    Chambon, P.6
  • 61
    • 77950347722 scopus 로고    scopus 로고
    • Opposing regulatory roles of phosphorylation and acetylation in DNA mispair processing by thymine DNA glycosylase
    • Mohan, R. D., Litchfield, D. W., Torchia, J., and Tini, M. (2010) Opposing regulatory roles of phosphorylation and acetylation in DNA mispair processing by thymine DNA glycosylase. Nucleic Acids Res. 38, 1135-1148
    • (2010) Nucleic Acids Res. , vol.38 , pp. 1135-1148
    • Mohan, R.D.1    Litchfield, D.W.2    Torchia, J.3    Tini, M.4
  • 62
    • 0036499523 scopus 로고    scopus 로고
    • DNA methylation at promoter regions regulates the timing of gene activation in Xenopus laevis embryos
    • DOI 10.1006/dbio.2001.0560
    • Stancheva, I., El-Maarri, O., Walter, J., Niveleau, A., and Meehan, R. R. (2002) DNA methylation at promoter regions regulates the timing of gene activation in Xenopus laevis embryos. Dev. Biol. 243, 155-165 (Pubitemid 34208410)
    • (2002) Developmental Biology , vol.243 , Issue.1 , pp. 155-165
    • Stancheva, I.1    El-Maarri, O.2    Walter, J.3    Niveleau, A.4    Meehan, R.R.5
  • 64
    • 0033513096 scopus 로고    scopus 로고
    • Translation of maternal TATA-binding protein mRNA potentiates basal but not activated transcription in Xenopus embryos at the midblastula transition
    • Veenstra, G. J., Destrée, O. H., and Wolffe, A. P. (1999) Translation of maternal TATA-binding protein mRNA potentiates basal but not activated transcription in Xenopus embryos at the midblastula transition. Mol. Cell. Biol. 19, 7972-7982 (Pubitemid 30413992)
    • (1999) Molecular and Cellular Biology , vol.19 , Issue.12 , pp. 7972-7982
    • Veenstra, G.J.C.1    Destree, O.H.J.2    Wolffe, A.P.3
  • 66
    • 79954452308 scopus 로고    scopus 로고
    • Mapping gene expression in two Xenopus species: Evolutionary constraints and developmental flexibility
    • Yanai, I., Peshkin, L., Jorgensen, P., and Kirschner, M. W. (2011) Mapping gene expression in two Xenopus species: evolutionary constraints and developmental flexibility. Dev. Cell 20, 483-496
    • (2011) Dev. Cell , vol.20 , pp. 483-496
    • Yanai, I.1    Peshkin, L.2    Jorgensen, P.3    Kirschner, M.W.4
  • 67
    • 84905996782 scopus 로고    scopus 로고
    • Cdt2 E3 ubiquitin ligase and proliferating cell nuclear antigen (PCNA) cooperate to degrade thymine DNA glycosylase in S phase
    • Cdt2 E3 ubiquitin ligase and proliferating cell nuclear antigen (PCNA) cooperate to degrade thymine DNA glycosylase in S phase. J. Biol. Chem. 289, 23056-23064
    • (2014) J. Biol. Chem. , vol.289 , pp. 23056-23064
    • Shibata, E.1    Dar, A.2    Dutta, A.3


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