메뉴 건너뛰기




Volumn 13, Issue 2, 2014, Pages 240-248

DDB2 association with PCNA is required for its degradation after UV-induced DNA damage

Author keywords

DDB2; Nucleotide excision repair; P21CDKN1A; PCNA; UV damage

Indexed keywords

DAMAGE DNA BINDING PROTEIN SUBUNIT 2; DNA BINDING PROTEIN; PCNA INTERACTING PROTEIN; PCNA PROTEIN; PROTEIN; PROTEIN P21; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG; CDKN1A PROTEIN, HUMAN; CYCLIN DEPENDENT KINASE INHIBITOR 1A; CYCLINE; DDB2 PROTEIN, HUMAN; PROTEIN BINDING;

EID: 84892585403     PISSN: 15384101     EISSN: 15514005     Source Type: Journal    
DOI: 10.4161/cc.26987     Document Type: Article
Times cited : (20)

References (44)
  • 1
    • 0033538572 scopus 로고    scopus 로고
    • Characterization of DNA recognition by the human UV-damaged DNAbinding protein
    • PMID:10391953
    • Fujiwara Y, Masutani C, Mizukoshi T, Kondo J, Hanaoka F, Iwai S. Characterization of DNA recognition by the human UV-damaged DNAbinding protein. J Biol Chem 1999; 274:20027-33; PMID:10391953; http://dx.doi.org/10.1074/jbc. 274.28.20027
    • (1999) J Biol Chem , vol.274 , pp. 20027-20033
    • Fujiwara, Y.1    Masutani, C.2    Mizukoshi, T.3    Kondo, J.4    Hanaoka, F.5    Iwai, S.6
  • 2
    • 0037127293 scopus 로고    scopus 로고
    • DDB accumulates at DNA damage sites immediately after UV irradiation and directly stimulates nucleotide excision repair
    • DOI 10.1074/jbc.C100610200
    • Wakasugi M, Kawashima A, Morioka H, Linn S, Sancar A, Mori T, Nikaido O, Matsunaga T. DDB accumulates at DNA damage sites immediately after UV irradiation and directly stimulates nucleotide excision repair. J Biol Chem 2002; 277: 1637-40; PMID:11705987; http://dx.doi.org/10.1074/jbc.C100610200 (Pubitemid 34968731)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.3 , pp. 1637-1640
    • Wakasugi, M.1    Kawashima, A.2    Morioka, H.3    Linn, S.4    Sancar, A.5    Mori, T.6    Nikaido, O.7    Matsunaga, T.8
  • 3
    • 28944440380 scopus 로고    scopus 로고
    • DDB1-DDB2 (xeroderma pigmentosum group E) protein complex recognizes a cyclobutane pyrimidine dimer, mismatches, apurinic/apyrimidinic sites, and compound in DNA
    • DOI 10.1074/jbc.M507854200
    • Wittschieben BØ, Iwai S, Wood RD. DDB1-DDB2 (xeroderma pigmentosum group E) protein complex recognizes a cyclobutane pyrimidine dimer, mismatches, apurinic/apyrimidinic sites, and compound lesions in DNA. J Biol Chem 2005; 280: 39982-9; PMID:16223728; http://dx.doi.org/10.1074/jbc.M507854200 (Pubitemid 41782166)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.48 , pp. 39982-39989
    • Wittschieben, B.O.1    Iwai, S.2    Wood, R.D.3
  • 4
    • 84856298654 scopus 로고    scopus 로고
    • P21 cooperates with DDB2 protein in suppression of ultraviolet ray-induced skin malignancies
    • PMID:22167187
    • Stoyanova T, Roy N, Bhattacharjee S, Kopanja D, Valli T, Bagchi S, Raychaudhuri P. p21 cooperates with DDB2 protein in suppression of ultraviolet ray-induced skin malignancies. J Biol Chem 2012; 287: 3019-28; PMID:22167187; http://dx.doi.org/10.1074/jbc.M111.295816
    • (2012) J Biol Chem , vol.287 , pp. 3019-3028
    • Stoyanova, T.1    Roy, N.2    Bhattacharjee, S.3    Kopanja, D.4    Valli, T.5    Bagchi, S.6    Raychaudhuri, P.7
  • 5
    • 0035902108 scopus 로고    scopus 로고
    • Genome maintenance mechanisms for preventing cancer
    • DOI 10.1038/35077232
    • Hoeijmakers JH. Genome maintenance mechanisms for preventing cancer. Nature 2001; 411: 366-74; PMID:11357144; http://dx.doi.org/10.1038/35077232 (Pubitemid 32467046)
    • (2001) Nature , vol.411 , Issue.6835 , pp. 366-374
    • Hoeijmakers, J.H.J.1
  • 6
    • 77954696778 scopus 로고    scopus 로고
    • Overexpression of DDB2 enhances the sensitivity of human ovarian cancer cells to cisplatin by augmenting cellular apoptosis
    • PMID:20013802
    • Barakat BM, Wang QE, Han C, Milum K, Yin DT, Zhao Q, Wani G, Arafa SA, El-Mahdy MA, Wani AA. Overexpression of DDB2 enhances the sensitivity of human ovarian cancer cells to cisplatin by augmenting cellular apoptosis. Int J Cancer 2010; 127: 977-88; PMID:20013802
    • (2010) Int J Cancer , vol.127 , pp. 977-988
    • Barakat, B.M.1    Wang, Q.E.2    Han, C.3    Milum, K.4    Yin, D.T.5    Zhao, Q.6    Wani, G.7    Arafa, S.A.8    El-Mahdy, M.A.9    Wani, A.A.10
  • 7
    • 28544434877 scopus 로고    scopus 로고
    • Enhanced DDB2 expression protects mice from carcinogenic effects of chronic UV-B irradiation
    • DOI 10.1158/0008-5472.CAN-05-2295
    • Alekseev S, Kool H, Rebel H, Fousteri M, Moser J, Backendorf C, de Gruijl FR, Vrieling H, Mullenders LH. Enhanced DDB2 expression protects mice from carcinogenic effects of chronic UV-B irradiation. Cancer Res 2005; 65: 10298-306; PMID:16288018; http://dx.doi.org/10.1158/0008-5472.CAN-05-2295 (Pubitemid 41743722)
    • (2005) Cancer Research , vol.65 , Issue.22 , pp. 10298-10306
    • Alekseev, S.1    Kool, H.2    Rebel, H.3    Fousteri, M.4    Moser, J.5    Backendorf, C.6    De Gruijl, F.R.7    Vrieling, H.8    Mullenders, L.H.F.9
  • 10
    • 33744781568 scopus 로고    scopus 로고
    • Histone H3 and H4 ubiquitylation by the CUL4-DDB-ROC1 ubiquitin ligase facilitates cellular response to DNA damage
    • DOI 10.1016/j.molcel.2006.03.035, PII S1097276506002309
    • Wang H, Zhai L, Xu J, Joo HY, Jackson S, Erdjument-Bromage H, Tempst P, Xiong Y, Zhang Y. Histone H3 and H4 ubiquitylation by the CUL4- DDB-ROC1 ubiquitin ligase facilitates cellular response to DNA damage. Mol Cell 2006; 22:383-94; PMID:16678110; http://dx.doi.org/10.1016/j.molcel.2006.03.035 (Pubitemid 44308132)
    • (2006) Molecular Cell , vol.22 , Issue.3 , pp. 383-394
    • Wang, H.1    Zhai, L.2    Xu, J.3    Joo, H.-Y.4    Jackson, S.5    Erdjument-Bromage, H.6    Tempst, P.7    Xiong, Y.8    Zhang, Y.9
  • 11
    • 33644536070 scopus 로고    scopus 로고
    • The DDB1- CUL4ADDB2 ubiquitin ligase is deficient in xeroderma pigmentosum group e and targets histone H2A at UV-damaged DNA sites
    • PMID:16473935
    • Kapetanaki MG, Guerrero-Santoro J, Bisi DC, Hsieh CL, Rapić-Otrin V, Levine AS. The DDB1- CUL4ADDB2 ubiquitin ligase is deficient in xeroderma pigmentosum group E and targets histone H2A at UV-damaged DNA sites. Proc Natl Acad Sci U S A 2006; 103: 2588-93; PMID:16473935; http://dx.doi.org/10.1073/ pnas.0511160103
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 2588-2593
    • Kapetanaki, M.G.1    Guerrero-Santoro, J.2    Bisi, D.C.3    Hsieh, C.L.4    Rapić-Otrin, V.5    Levine, A.S.6
  • 13
    • 79960377998 scopus 로고    scopus 로고
    • XPB and XPD helicases in TFIIH orchestrate DNA duplex opening and damage verification to coordinate repair with transcription and cell cycle via CAK kinase
    • PMID:21571596
    • Fuss JO, Tainer JA. XPB and XPD helicases in TFIIH orchestrate DNA duplex opening and damage verification to coordinate repair with transcription and cell cycle via CAK kinase. DNA Repair (Amst) 2011; 10: 697-713; PMID:21571596; http://dx.doi.org/10.1016/j.dnarep.2011.04.028
    • (2011) DNA Repair (Amst) , vol.10 , pp. 697-713
    • Fuss, J.O.1    Tainer, J.A.2
  • 14
    • 41149125554 scopus 로고    scopus 로고
    • CDKN1A with PCNA regulates the histone acetyltransferase activity of p300 in nucleotide excision repair
    • DOI 10.1093/nar/gkn014
    • Cazzalini O, Perucca P, Savio M, Necchi D, Bianchi L, Stivala LA, Ducommun B, Scovassi AI, Prosperi E. Interaction of p21(CDKN1A) with PCNA regulates the histone acetyltransferase activity of p300 in nucleotide excision repair. Nucleic Acids Res 2008; 36: 1713-22; PMID:18263614; http://dx.doi.org/ 10.1093/nar/gkn014 (Pubitemid 351426120)
    • (2008) Nucleic Acids Research , vol.36 , Issue.5 , pp. 1713-1722
    • Cazzalini, O.1    Perucca, P.2    Savio, M.3    Necchi, D.4    Bianchi, L.5    Stivala, L.A.6    Ducommun, B.7    Scovassi, A.I.8    Prosperi, E.9
  • 15
    • 77951978240 scopus 로고    scopus 로고
    • Multiple roles of the cell cycle inhibitor p21(CDKN1A) in the DNA damage response
    • PMID:20096807
    • Cazzalini O, Scovassi AI, Savio M, Stivala LA, Prosperi E. Multiple roles of the cell cycle inhibitor p21(CDKN1A) in the DNA damage response. Mutat Res 2010; 704: 12-20; PMID:20096807; http://dx.doi.org/10.1016/j.mrrev.2010.01.009
    • (2010) Mutat Res , vol.704 , pp. 12-20
    • Cazzalini, O.1    Scovassi, A.I.2    Savio, M.3    Stivala, L.A.4    Prosperi, E.5
  • 16
    • 0242582360 scopus 로고    scopus 로고
    • The human proliferating cell nuclear antigen regulates transcriptional coactivator p300 activity and promotes transcriptional repression
    • DOI 10.1074/jbc.M303138200
    • Hong R, Chakravarti D. The human proliferating Cell nuclear antigen regulates transcriptional coactivator p300 activity and promotes transcriptional repression. J Biol Chem 2003; 278: 44505-13; PMID:12937166; http://dx.doi.org/10.1074/jbc.M303138200 (Pubitemid 37377203)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.45 , pp. 44505-44513
    • Hong, R.1    Chakravarti, D.2
  • 17
    • 84867205440 scopus 로고    scopus 로고
    • P300/CBP acetyl transferases interact with and acetylate the nucleotide excision repair factor XPG
    • PMID:22954786
    • Tillhon M, Cazzalini O, Nardo T, Necchi D, Sommatis S, Stivala LA, Scovassi AI, Prosperi E. p300/CBP acetyl transferases interact with and acetylate the nucleotide excision repair factor XPG. DNA Repair (Amst) 2012; 11: 844-52; PMID:22954786; http://dx.doi.org/10.1016/j.dnarep.2012.08.001
    • (2012) DNA Repair (Amst) , vol.11 , pp. 844-852
    • Tillhon, M.1    Cazzalini, O.2    Nardo, T.3    Necchi, D.4    Sommatis, S.5    Stivala, L.A.6    Scovassi, A.I.7    Prosperi, E.8
  • 18
    • 51949098691 scopus 로고    scopus 로고
    • PCNA-dependent regulation of p21 ubiquitylation and degradation via the CRL4Cdt2 ubiquitin ligase complex
    • PMID:18794347
    • Abbas T, Sivaprasad U, Terai K, Amador V, Pagano M, Dutta A. PCNA-dependent regulation of p21 ubiquitylation and degradation via the CRL4Cdt2 ubiquitin ligase complex. Genes Dev 2008; 22:2496-506; PMID:18794347; http://dx.doi.org/10.1101/gad.1676108
    • (2008) Genes Dev , vol.22 , pp. 2496-2506
    • Abbas, T.1    Sivaprasad, U.2    Terai, K.3    Amador, V.4    Pagano, M.5    Dutta, A.6
  • 19
    • 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
    • PMID:18703516
    • 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; 283:29045-52; PMID:18703516; http://dx.doi.org/10.1074/jbc.M806045200
    • (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
  • 20
    • 37549061452 scopus 로고    scopus 로고
    • The xeroderma pigmentosum group e gene product DDB2 activates nucleotide excision repair by regulating the level of p21Waf1/Cip1
    • PMID:17967871
    • Stoyanova T, Yoon T, Kopanja D, Mokyr MB, Raychaudhuri P. The xeroderma pigmentosum group E gene product DDB2 activates nucleotide excision repair by regulating the level of p21Waf1/Cip1. Mol Cell Biol 2008; 28: 177-87; PMID:17967871; http://dx.doi.org/10.1128/MCB.00880-07
    • (2008) Mol Cell Biol , vol.28 , pp. 177-187
    • Stoyanova, T.1    Yoon, T.2    Kopanja, D.3    Mokyr, M.B.4    Raychaudhuri, P.5
  • 23
    • 0034813575 scopus 로고    scopus 로고
    • The xeroderma pigmentosum group E gene product DDB2 is a specific target of cullin 4A in mammalian cells
    • DOI 10.1128/MCB.21.20.6738-6747.2001
    • Nag A, Bondar T, Shiv S, Raychaudhuri P. The xeroderma pigmentosum group E gene product DDB2 is a specific target of cullin 4A in mammalian cells. Mol Cell Biol 2001; 21: 6738-47; PMID:11564859; http://dx.doi.org/10.1128/MCB.21.20. 6738-6747.2001 (Pubitemid 32911236)
    • (2001) Molecular and Cellular Biology , vol.21 , Issue.20 , pp. 6738-6747
    • Nag, A.1    Bondar, T.2    Shiv, S.3    Raychaudhuri, P.4
  • 24
    • 0035930582 scopus 로고    scopus 로고
    • UV-damaged DNA-binding proteins are targets of CUL-4Amediated ubiquitination and degradation
    • PMID:11673459
    • Chen X, Zhang Y, Douglas L, Zhou P. UV-damaged DNA-binding proteins are targets of CUL-4Amediated ubiquitination and degradation. J Biol Chem 2001; 276: 48175-82; PMID:11673459
    • (2001) J Biol Chem , vol.276 , pp. 48175-48182
    • Chen, X.1    Zhang, Y.2    Douglas, L.3    Zhou, P.4
  • 25
    • 0032511893 scopus 로고    scopus 로고
    • Interaction with cyclin-dependent kinases and PCNA modulates proteasome-dependent degradation of p21
    • Cayrol C, Ducommun B. Interaction with cyclindependent kinases and PCNA modulates proteasome- dependent degradation of p21. Oncogene 1998; 17: 2437-44; PMID:9824154; http://dx.doi.org/10.1038/sj.onc.1202189 (Pubitemid 28544713)
    • (1998) Oncogene , vol.17 , Issue.19 , pp. 2437-2444
    • Cayrol, C.1    Ducommun, B.2
  • 26
    • 0347160176 scopus 로고    scopus 로고
    • P21CDKN1A does not interfere with loading of PCNA at DNA replication sites, but inhibits subsequent binding of DNA polymerase delta at the G1/S phase transition
    • PMID:14504476
    • Cazzalini O, Perucca P, Riva F, Stivala LA, Bianchi L, Vannini V, Ducommun B, Prosperi E. p21CDKN1A does not interfere with loading of PCNA at DNA replication sites, but inhibits subsequent binding of DNA polymerase delta at the G1/S phase transition. Cell Cycle 2003; 2: 596-603; PMID:14504476; http://dx.doi.org/10.4161/cc.2.6.502
    • (2003) Cell Cycle , vol.2 , pp. 596-603
    • Cazzalini, O.1    Perucca, P.2    Riva, F.3    Stivala, L.A.4    Bianchi, L.5    Vannini, V.6    Ducommun, B.7    Prosperi, E.8
  • 27
    • 0029016275 scopus 로고
    • Mechanism of inhibition of proliferating cell nuclear antigen-dependent DNA synthesis by the cyclin-dependent kinase inhibitor p21
    • PMID:7612628
    • Podust VN, Podust LM, Goubin F, Ducommun B, Hübscher U. Mechanism of inhibition of proliferating cell nuclear antigen-dependent DNA synthesis by the cyclin-dependent kinase inhibitor p21. Biochemistry 1995; 34: 8869-75; PMID:7612628; http://dx.doi.org/10.1021/bi00027a039
    • (1995) Biochemistry , vol.34 , pp. 8869-8875
    • Podust, V.N.1    Podust, L.M.2    Goubin, F.3    Ducommun, B.4    Hübscher, U.5
  • 29
    • 65649105790 scopus 로고    scopus 로고
    • CUL4A abrogation augments DNA damage response and protection against skin carcinogenesis
    • PMID:19481525
    • Liu L, Lee S, Zhang J, Peters SB, Hannah J, Zhang Y, Yin Y, Koff A, Ma L, Zhou P. CUL4A abrogation augments DNA damage response and protection against skin carcinogenesis. Mol Cell 2009; 34:451-60; PMID:19481525; http://dx.doi.org/10.1016/j.molcel.2009.04.020
    • (2009) Mol Cell , vol.34 , pp. 451-460
    • Liu, L.1    Lee, S.2    Zhang, J.3    Peters, S.B.4    Hannah, J.5    Zhang, Y.6    Yin, Y.7    Koff, A.8    Ma, L.9    Zhou, P.10
  • 30
    • 51949112601 scopus 로고    scopus 로고
    • The CRL4Cdt2 ubiquitin ligase targets the degradation of p21Cip1 to control replication licensing
    • PMID:18794348
    • Kim Y, Starostina NG, Kipreos ET. The CRL4Cdt2 ubiquitin ligase targets the degradation of p21Cip1 to control replication licensing. Genes Dev 2008; 22: 2507-19; PMID:18794348; http://dx.doi.org/10.1101/gad.1703708
    • (2008) Genes Dev , vol.22 , pp. 2507-2519
    • Kim, Y.1    Starostina, N.G.2    Kipreos, E.T.3
  • 31
    • 84859483427 scopus 로고    scopus 로고
    • Direct role for proliferating cell nuclear antigen in substrate recognition by the E3 ubiquitin ligase CRL4Cdt2
    • PMID:22303007
    • Havens CG, Shobnam N, Guarino E, Centore RC, Zou L, Kearsey SE, Walter JC. Direct role for proliferating cell nuclear antigen in substrate recognition by the E3 ubiquitin ligase CRL4Cdt2. J Biol Chem 2012; 287: 11410-21; PMID:22303007; http://dx.doi.org/10.1074/jbc.M111.337683
    • (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
  • 32
    • 80051525031 scopus 로고    scopus 로고
    • Mechanism of CRL4(Cdt2), a PCNA-dependent E3 ubiquitin ligase
    • PMID:21828267
    • Havens CG, Walter JC. Mechanism of CRL4(Cdt2), a PCNA-dependent E3 ubiquitin ligase. Genes Dev 2011; 25: 1568-82; PMID:21828267; http://dx.doi.org/10.1101/gad.2068611
    • (2011) Genes Dev , vol.25 , pp. 1568-1582
    • Havens, C.G.1    Walter, J.C.2
  • 33
    • 0001473365 scopus 로고    scopus 로고
    • The puzzle of PCNA's many partners
    • PMID:11056476
    • Warbrick E. The puzzle of PCNA's many partners. Bioessays 2000; 22: 997-1006; PMID:11056476; http://dx.doi.org/10.1002/1521-1878(200011)22: 11<997::AID-BIES6>3.0.CO;2-#
    • (2000) Bioessays , vol.22 , pp. 997-1006
    • Warbrick, E.1
  • 34
    • 34249066085 scopus 로고    scopus 로고
    • PCNA, The maestro of the replication fork
    • DOI 10.1016/j.cell.2007.05.003, PII S0092867407005946
    • Moldovan GL, Pfander B, Jentsch S. PCNA, the maestro of the replication fork. Cell 2007; 129:665-79; PMID:17512402; http://dx.doi.org/10.1016/j.cell. 2007.05.003 (Pubitemid 46802385)
    • (2007) Cell , vol.129 , Issue.4 , pp. 665-679
    • Moldovan, G.-L.1    Pfander, B.2    Jentsch, S.3
  • 35
    • 33744462103 scopus 로고    scopus 로고
    • The fellowship of the rings: Distinct pools of proliferating cell nuclear antigen trimer at work
    • DOI 10.1096/fj.05-5469hyp
    • Prosperi E. The fellowship of the rings: distinct pools of proliferating cell nuclear antigen trimer at work. FASEB J 2006; 20: 833-7; PMID:16675840; http://dx.doi.org/10.1096/fj.05-5469hyp (Pubitemid 44943941)
    • (2006) FASEB Journal , vol.20 , Issue.7 , pp. 833-837
    • Prosperi, E.1
  • 36
    • 73649125005 scopus 로고    scopus 로고
    • CRL4(Cdt2) E3 ubiquitin ligase monoubiquitinates PCNA to promote translesion DNA synthesis
    • PMID:20129063
    • Terai K, Abbas T, Jazaeri AA, Dutta A. CRL4(Cdt2) E3 ubiquitin ligase monoubiquitinates PCNA to promote translesion DNA synthesis. Mol Cell 2010; 37: 143-9; PMID:20129063; http://dx.doi.org/10.1016/j.molcel.2009.12.018
    • (2010) Mol Cell , vol.37 , pp. 143-149
    • Terai, K.1    Abbas, T.2    Jazaeri, A.A.3    Dutta, A.4
  • 37
    • 0037068455 scopus 로고    scopus 로고
    • RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO
    • DOI 10.1038/nature00991
    • Hoege C, Pfander B, Moldovan GL, Pyrowolakis G, Jentsch S. RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO. Nature 2002; 419: 135-41; PMID:12226657; http://dx.doi.org/10.1038/nature00991 (Pubitemid 35025438)
    • (2002) Nature , vol.419 , Issue.6903 , pp. 135-141
    • Hoege, C.1    Pfander, B.2    Moldovan, G.-L.3    Pyrowolakis, G.4    Jentsch, S.5
  • 38
    • 79960378814 scopus 로고    scopus 로고
    • Dynamics of mammalian NER proteins
    • PMID:21550320
    • Vermeulen W. Dynamics of mammalian NER proteins. DNA Repair (Amst) 2011; 10: 760-71; PMID:21550320; http://dx.doi.org/10.1016/j.dnarep.2011.04.015
    • (2011) DNA Repair (Amst) , vol.10 , pp. 760-771
    • Vermeulen, W.1
  • 39
    • 84873130772 scopus 로고    scopus 로고
    • Role of poly(ADPribose) polymerase-1 in the removal of UV-induced DNA lesions by nucleotide excision repair
    • PMID:23319653
    • Robu M, Shah RG, Petitclerc N, Brind'Amour J, Kandan-Kulangara F, Shah GM. Role of poly(ADPribose) polymerase-1 in the removal of UV-induced DNA lesions by nucleotide excision repair. Proc Natl Acad Sci U S A 2013; 110: 1658-63; PMID:23319653; http://dx.doi.org/10.1073/pnas.1209507110
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 1658-1663
    • Robu, M.1    Shah, R.G.2    Petitclerc, N.3    Brind'Amour, J.4    Kandan-Kulangara, F.5    Shah, G.M.6
  • 43
    • 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 δ or DNA ligase I
    • DOI 10.1016/j.yexcr.2003.10.025
    • Riva F, Savio M, Cazzalini O, Stivala LA, Scovassi IA, Cox LS, Ducommun B, 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 2004; 293: 357-67; PMID:14729473; http://dx.doi.org/10.1016/j.yexcr.2003.10.025 (Pubitemid 38083225)
    • (2004) Experimental Cell Research , vol.293 , Issue.2 , 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.