메뉴 건너뛰기




Volumn 18, Issue 8, 2013, Pages 851-873

Biological and therapeutic relevance of nonreplicative DNA polymerases to cancer

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA TOCOTRIENOL; BETULIC ACID; BIOLOGICAL MARKER; BLEOMYCIN; CARBOPLATIN; CHLORMETHINE; CISPLATIN; CYTARABINE; CYTOTOXIC AGENT; DNA DIRECTED DNA POLYMERASE BETA; DNA DIRECTED DNA POLYMERASE ETA; DNA POLYMERASE; DNA POLYMERASE IOTA; DNA POLYMERASE KAPPA; DNA POLYMERASE LAMBDA; DNA POLYMERASE MU; DNA POLYMERASE THETA; DNA POLYMERASE ZETA; ETOPOSIDE; GEMCITABINE; MELPHALAN; MESYLIC ACID METHYL ESTER; METHYLFUNICONE; NONREPLICATIVE DNA POLYMERASE; OLEANOLIC ACID; OXALIPLATIN; PLATINUM DERIVATIVE; STIGMASTEROL; TEMOZOLOMIDE; UNCLASSIFIED DRUG; UNINDEXED DRUG;

EID: 84873866621     PISSN: 15230864     EISSN: 15577716     Source Type: Journal    
DOI: 10.1089/ars.2011.4203     Document Type: Review
Times cited : (17)

References (274)
  • 1
    • 33645244521 scopus 로고    scopus 로고
    • The in vivo characterization of translesion synthesis across UV-induced lesions in Saccharomyces cerevisiae: Insights into Pol zeta-and Pol eta-dependent frameshift mutagenesis
    • Abdulovic AL and Jinks-Robertson S. The in vivo characterization of translesion synthesis across UV-induced lesions in Saccharomyces cerevisiae: insights into Pol zeta-and Pol eta-dependent frameshift mutagenesis. Genetics 172: 1487-1498, 2006.
    • (2006) Genetics , vol.172 , pp. 1487-1498
    • Abdulovic, A.L.1    Jinks-Robertson, S.2
  • 2
    • 33845427432 scopus 로고    scopus 로고
    • Complex formation with Rev1 enhances the proficiency of Sac-charomyces cerevisiae DNA polymerase zeta for mismatch extension and for extension opposite from DNA lesions
    • Acharya N, Johnson RE, Prakash S, and Prakash L. Complex formation with Rev1 enhances the proficiency of Sac-charomyces cerevisiae DNA polymerase zeta for mismatch extension and for extension opposite from DNA lesions. Mol Cell Biol 26: 9555-9563, 2006.
    • (2006) Mol Cell Biol , vol.26 , pp. 9555-9563
    • Acharya, N.1    Johnson, R.E.2    Prakash, S.3    Prakash, L.4
  • 5
    • 27544489816 scopus 로고    scopus 로고
    • A role for polymerase eta in the cellular tolerance to cisplatin-induced damage
    • Albertella MR, Green CM, Lehmann AR, and O'Connor MJ. A role for polymerase eta in the cellular tolerance to cisplatin-induced damage. Cancer Res 65: 9799-9806, 2005.
    • (2005) Cancer Res , vol.65 , pp. 9799-9806
    • Albertella, M.R.1    Green, C.M.2    Lehmann, A.R.3    O'Connor, M.J.4
  • 6
    • 16244375578 scopus 로고    scopus 로고
    • The over-expression of specialized DNA polymerases in cancer
    • Albertella MR, Lau A, and O'Connor MJ. The over-expression of specialized DNA polymerases in cancer. DNA Repair (Amst) 4: 583-593, 2005.
    • (2005) DNA Repair (Amst) , vol.4 , pp. 583-593
    • Albertella, M.R.1    Lau, A.2    O'Connor, M.J.3
  • 7
    • 0035803497 scopus 로고    scopus 로고
    • DNA polymerase beta is the major dRP lyase involved in repair of oxidative base lesions in DNA by mammalian cell extracts
    • Allinson SL, Dianova, II, and Dianov GL. DNA polymerase beta is the major dRP lyase involved in repair of oxidative base lesions in DNA by mammalian cell extracts. EMBO J 20: 6919-6926, 2001.
    • (2001) EMBO J , vol.20 , pp. 6919-6926
    • Allinson, S.L.1    Dianova, I.I.2    Dianov, G.L.3
  • 9
    • 38049123477 scopus 로고    scopus 로고
    • Eukaryotic DNA damage tolerance and translesion synthesis through covalent modifications of PCNA
    • Andersen PL, Xu F, and Xiao W. Eukaryotic DNA damage tolerance and translesion synthesis through covalent modifications of PCNA. Cell Res 18: 162-173, 2008.
    • (2008) Cell Res , vol.18 , pp. 162-173
    • Andersen, P.L.1    Xu, F.2    Xiao, W.3
  • 10
    • 33646183367 scopus 로고    scopus 로고
    • DNA damage responses and their many interactions with the replication fork
    • Andreassen PR, Ho GP, and D'Andrea AD. DNA damage responses and their many interactions with the replication fork. Carcinogenesis 27: 883-892, 2006.
    • (2006) Carcinogenesis , vol.27 , pp. 883-892
    • Andreassen, P.R.1    Ho, G.P.2    D'Andrea, A.D.3
  • 15
    • 0345060496 scopus 로고    scopus 로고
    • Efficiency of extension of mismatched primer termini across from cisplatin and oxaliplatin ad-ducts by human DNA polymerases beta and eta in vitro
    • Bassett E, Vaisman A, Havener JM, Masutani C, Hanaoka F, and Chaney SG. Efficiency of extension of mismatched primer termini across from cisplatin and oxaliplatin ad-ducts by human DNA polymerases beta and eta in vitro. Biochemistry 42: 14197-14206, 2003.
    • (2003) Biochemistry , vol.42 , pp. 14197-14206
    • Bassett, E.1    Vaisman, A.2    Havener, J.M.3    Masutani, C.4    Hanaoka, F.5    Chaney, S.G.6
  • 17
    • 70450257567 scopus 로고    scopus 로고
    • DNA polymerase beta substrate specificity: Side chain modulation of the "a-rule"
    • Beard WA, Shock DD, Batra VK, Pedersen LC, and Wilson SH. DNA polymerase beta substrate specificity: side chain modulation of the "A-rule". J Biol Chem 284: 31680-31689, 2009.
    • (2009) J Biol Chem , vol.284 , pp. 31680-31689
    • Beard, W.A.1    Shock, D.D.2    Batra, V.K.3    Pedersen, L.C.4    Wilson, S.H.5
  • 18
    • 0037041029 scopus 로고    scopus 로고
    • Loss of DNA polymerase beta stacking interactions with templating purines, but not pyrimidines, alters catalytic efficiency and fidelity
    • Beard WA, Shock DD, Yang XP, DeLauder SF, and Wilson SH. Loss of DNA polymerase beta stacking interactions with templating purines, but not pyrimidines, alters catalytic efficiency and fidelity. J Biol Chem 277: 8235-8242, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 8235-8242
    • Beard, W.A.1    Shock, D.D.2    Yang, X.P.3    Delauder, S.F.4    Wilson, S.H.5
  • 19
    • 0028803178 scopus 로고
    • Purification and domain-mapping of mammalian DNA polymerase beta
    • Beard WA and Wilson SH. Purification and domain-mapping of mammalian DNA polymerase beta. Methods Enzymol 262: 98-107, 1995.
    • (1995) Methods Enzymol , vol.262 , pp. 98-107
    • Beard, W.A.1    Wilson, S.H.2
  • 20
    • 33644634986 scopus 로고    scopus 로고
    • Structure and mechanism of DNA polymerase beta
    • Beard WA and Wilson SH. Structure and mechanism of DNA polymerase beta. Chem Rev 106: 361-382, 2006.
    • (2006) Chem Rev , vol.106 , pp. 361-382
    • Beard, W.A.1    Wilson, S.H.2
  • 23
    • 0035834632 scopus 로고    scopus 로고
    • Fidelity of uracil-initiated base excision DNA repair in DNA polymerase beta-proficient and-deficient mouse embryonic fibroblast cell extracts
    • Bennett SE, Sung JS, and Mosbaugh DW. Fidelity of uracil-initiated base excision DNA repair in DNA polymerase beta-proficient and-deficient mouse embryonic fibroblast cell extracts. J Biol Chem 276: 42588-42600, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 42588-42600
    • Bennett, S.E.1    Sung, J.S.2    Mosbaugh, D.W.3
  • 24
    • 0041620605 scopus 로고    scopus 로고
    • DNA polymerase beta can incorporate ribonu-cleotides during DNA synthesis of undamaged and CPD-damaged DNA
    • Bergoglio V, Ferrari E, Hubscher U, Cazaux C, and Hoffmann JS. DNA polymerase beta can incorporate ribonu-cleotides during DNA synthesis of undamaged and CPD-damaged DNA. J Mol Biol 331: 1017-1023, 2003.
    • (2003) J Mol Biol , vol.331 , pp. 1017-1023
    • Bergoglio, V.1    Ferrari, E.2    Hubscher, U.3    Cazaux, C.4    Hoffmann, J.S.5
  • 25
    • 0041931065 scopus 로고    scopus 로고
    • Immunoglobulin kappa light chain gene rearrangement is impaired in mice deficient for DNA polymerase mu
    • Bertocci B, De Smet A, Berek C, Weill JC, and Reynaud CA. Immunoglobulin kappa light chain gene rearrangement is impaired in mice deficient for DNA polymerase mu. Immunity 19: 203-211, 2003.
    • (2003) Immunity , vol.19 , pp. 203-211
    • Bertocci, B.1    De Smet, A.2    Berek, C.3    Weill, J.C.4    Reynaud, C.A.5
  • 26
    • 33745997776 scopus 로고    scopus 로고
    • Nonoverlapping functions of DNA polymerases mu, lambda, and terminal deoxynucleotidyltransferase during immunoglobulin V(D)
    • Bertocci B, De Smet A, Weill JC, and Reynaud CA. Nonoverlapping functions of DNA polymerases mu, lambda, and terminal deoxynucleotidyltransferase during immunoglobulin V(D)J recombination in vivo. Immunity 25: 31-41, 2006.
    • (2006) J Recombination in Vivo. Immunity , vol.25 , pp. 31-41
    • Bertocci, B.1    De Smet, A.2    Weill, J.C.3    Reynaud, C.A.4
  • 29
    • 4444337946 scopus 로고    scopus 로고
    • Human DNA polymerases lambda and beta show different efficiencies of translesion DNA synthesis past abasic sites and alternative mechanisms for frameshift generation
    • Blanca G, Villani G, Shevelev I, Ramadan K, Spadari S, Hubscher U, and Maga G. Human DNA polymerases lambda and beta show different efficiencies of translesion DNA synthesis past abasic sites and alternative mechanisms for frameshift generation. Biochemistry 43: 11605-11615, 2004.
    • (2004) Biochemistry , vol.43 , pp. 11605-11615
    • Blanca, G.1    Villani, G.2    Shevelev, I.3    Ramadan, K.4    Spadari, S.5    Hubscher, U.6    Maga, G.7
  • 31
    • 77957909760 scopus 로고    scopus 로고
    • DNA polymerases beta and lambda mediate overlapping and independent roles in base excision repair in mouse embryonic fibro-blasts
    • Braithwaite EK, Kedar PS, Stumpo DJ, Bertocci B, Freed-man JH, Samson LD, and Wilson SH. DNA polymerases beta and lambda mediate overlapping and independent roles in base excision repair in mouse embryonic fibro-blasts. PLoS One 5: e12229, 2010.
    • (2010) PLoS One , vol.5
    • Braithwaite, E.K.1    Kedar, P.S.2    Stumpo, D.J.3    Bertocci, B.4    Freed-Man, J.H.5    Samson, L.D.6    Wilson, S.H.7
  • 32
    • 7944233608 scopus 로고    scopus 로고
    • Rad18/Rad5/Mms2-mediated polyubiquitination of PCNA is implicated in replication completion during replication stress
    • Branzei D, Seki M, and Enomoto T. Rad18/Rad5/Mms2-mediated polyubiquitination of PCNA is implicated in replication completion during replication stress. Genes Cells 9: 1031-1042, 2004.
    • (2004) Genes Cells , vol.9 , pp. 1031-1042
    • Branzei, D.1    Seki, M.2    Enomoto, T.3
  • 33
    • 57849155774 scopus 로고    scopus 로고
    • Template dependent human DNA polymerases
    • Brieba LG. Template dependent human DNA polymerases. Curr Top Med Chem 8: 1312-1326, 2008.
    • (2008) Curr Top Med Chem , vol.8 , pp. 1312-1326
    • Brieba, L.G.1
  • 36
    • 78650415862 scopus 로고    scopus 로고
    • Efficiency and fidelity of human DNA polymerases lambda and beta during gap-filling DNA synthesis
    • Brown JA, Pack LR, Sanman LE, and Suo Z. Efficiency and fidelity of human DNA polymerases lambda and beta during gap-filling DNA synthesis. DNA Repair (Amst) 10: 24-33, 2011.
    • (2011) DNA Repair (Amst) , vol.10 , pp. 24-33
    • Brown, J.A.1    Pack, L.R.2    Sanman, L.E.3    Suo, Z.4
  • 37
    • 77957917034 scopus 로고    scopus 로고
    • Identification of critical residues for the tight binding of both correct and incorrect nucleotides to human DNA polymerase lambda
    • Brown JA, Pack LR, Sherrer SM, Kshetry AK, Newmister SA, Fowler JD, Taylor JS, and Suo Z. Identification of critical residues for the tight binding of both correct and incorrect nucleotides to human DNA polymerase lambda. J Mol Biol 403: 505-515, 2010.
    • (2010) J Mol Biol , vol.403 , pp. 505-515
    • Brown, J.A.1    Pack, L.R.2    Sherrer, S.M.3    Kshetry, A.K.4    Newmister, S.A.5    Fowler, J.D.6    Taylor, J.S.7    Suo, Z.8
  • 38
    • 62449189462 scopus 로고    scopus 로고
    • Ubiquitination and deubiquitination of PCNA in response to stalling of the replication fork
    • Brown S, Niimi A, and Lehmann AR. Ubiquitination and deubiquitination of PCNA in response to stalling of the replication fork. Cell Cycle 8: 689-692, 2009.
    • (2009) Cell Cycle , vol.8 , pp. 689-692
    • Brown, S.1    Niimi, A.2    Lehmann, A.R.3
  • 41
    • 78651380166 scopus 로고    scopus 로고
    • Structural analysis of the conserved ubiqui-tin-binding motifs (UBMs) of the translesion polymerase iota in complex with ubiquitin
    • Burschowsky D, Rudolf F, Rabut G, Herrmann T, Peter M, and Wider G. Structural analysis of the conserved ubiqui-tin-binding motifs (UBMs) of the translesion polymerase iota in complex with ubiquitin. J Biol Chem 286: 1364-1373, 2011.
    • (2011) J Biol Chem , vol.286 , pp. 1364-1373
    • Burschowsky, D.1    Rudolf, F.2    Rabut, G.3    Herrmann, T.4    Peter, M.5    Wider, G.6
  • 42
    • 0141731310 scopus 로고    scopus 로고
    • Base excision repair deficiency caused by polymerase beta haploinsufficiency: Accelerated DNA damage and increased mutational response to carcinogens
    • Cabelof DC, Guo Z, Raffoul JJ, Sobol RW, Wilson SH, Richardson A, and Heydari AR. Base excision repair deficiency caused by polymerase beta haploinsufficiency: accelerated DNA damage and increased mutational response to carcinogens. Cancer Res 63: 5799-5807, 2003.
    • (2003) Cancer Res , vol.63 , pp. 5799-5807
    • Cabelof, D.C.1    Guo, Z.2    Raffoul, J.J.3    Sobol, R.W.4    Wilson, S.H.5    Richardson, A.6    Heydari, A.R.7
  • 44
    • 0032514636 scopus 로고    scopus 로고
    • Overexpression of DNA poly-merase beta in cell results in a mutator phenotype and a decreased sensitivity to anticancer drugs
    • Canitrot Y, Cazaux C, Frechet M, Bouayadi K, Lesca C, Salles B, and Hoffmann JS. Overexpression of DNA poly-merase beta in cell results in a mutator phenotype and a decreased sensitivity to anticancer drugs. Proc Natl Acad Sci USA 95: 12586-12590, 1998.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 12586-12590
    • Canitrot, Y.1    Cazaux, C.2    Frechet, M.3    Bouayadi, K.4    Lesca, C.5    Salles, B.6    Hoffmann, J.S.7
  • 45
    • 0345620782 scopus 로고    scopus 로고
    • Overexpression of DNA polymerase beta: A genomic instability enhancer process
    • Canitrot Y, Frechet M, Servant L, Cazaux C, and Hoffmann JS. Overexpression of DNA polymerase beta: a genomic instability enhancer process. FASEB J 13: 1107-1111, 1999.
    • (1999) FASEB J , vol.13 , pp. 1107-1111
    • Canitrot, Y.1    Frechet, M.2    Servant, L.3    Cazaux, C.4    Hoffmann, J.S.5
  • 46
    • 0033812619 scopus 로고    scopus 로고
    • Nucleotide excision repair DNA synthesis by excess DNA polymerase beta: A potential source of genetic instability in cancer cells
    • Canitrot Y, Hoffmann JS, Calsou P, Hayakawa H, Salles B, and Cazaux C. Nucleotide excision repair DNA synthesis by excess DNA polymerase beta: a potential source of genetic instability in cancer cells. FASEB J 14: 1765-1774, 2000.
    • (2000) FASEB J , vol.14 , pp. 1765-1774
    • Canitrot, Y.1    Hoffmann, J.S.2    Calsou, P.3    Hayakawa, H.4    Salles, B.5    Cazaux, C.6
  • 47
    • 77957757791 scopus 로고    scopus 로고
    • The R438W polymorphism of human DNA polymerase lambda triggers cellular sensitivity to camptothecin by compromising the homologous recombination repair pathway
    • Capp JP, Boudsocq F, Bergoglio V, Trouche D, Cazaux C, Blanco L, Hoffmann JS, and Canitrot Y. The R438W polymorphism of human DNA polymerase lambda triggers cellular sensitivity to camptothecin by compromising the homologous recombination repair pathway. Carcinogenesis 31: 1742-1747, 2010.
    • (2010) Carcinogenesis , vol.31 , pp. 1742-1747
    • Capp, J.P.1    Boudsocq, F.2    Bergoglio, V.3    Trouche, D.4    Cazaux, C.5    Blanco, L.6    Hoffmann, J.S.7    Canitrot, Y.8
  • 49
    • 34547135486 scopus 로고    scopus 로고
    • Involvement of DNA poly-merase mu in the repair of a specific subset of DNA double-strand breaks in mammalian cells
    • Capp JP, Boudsocq F, Besnard AG, Lopez BS, Cazaux C, Hoffmann JS, and Canitrot Y. Involvement of DNA poly-merase mu in the repair of a specific subset of DNA double-strand breaks in mammalian cells. Nucleic Acids Res 35: 3551-3560, 2007.
    • (2007) Nucleic Acids Res , vol.35 , pp. 3551-3560
    • Capp, J.P.1    Boudsocq, F.2    Besnard, A.G.3    Lopez, B.S.4    Cazaux, C.5    Hoffmann, J.S.6    Canitrot, Y.7
  • 51
    • 34548379865 scopus 로고    scopus 로고
    • Overexpression of DNA polymerase beta results in an increased rate of frameshift mutations during base excision repair
    • Chan K, Houlbrook S, Zhang QM, Harrison M, Hickson ID, and Dianov GL. Overexpression of DNA polymerase beta results in an increased rate of frameshift mutations during base excision repair. Mutagenesis 22: 183-188, 2007.
    • (2007) Mutagenesis , vol.22 , pp. 183-188
    • Chan, K.1    Houlbrook, S.2    Zhang, Q.M.3    Harrison, M.4    Hickson, I.D.5    Dianov, G.L.6
  • 52
    • 77957369329 scopus 로고    scopus 로고
    • Dual roles for DNA polymerase theta in alternative end-joining repair of double-strand breaks in Drosophila
    • Chan SH, Yu AM, and McVey M. Dual roles for DNA polymerase theta in alternative end-joining repair of double-strand breaks in Drosophila. PLoS Genet 6: e1001005, 2010.
    • (2010) PLoS Genet , vol.6
    • Chan, S.H.1    Yu, A.M.2    McVey, M.3
  • 53
    • 10644245994 scopus 로고    scopus 로고
    • Recognition and processing of cisplatin-and oxaliplatin-DNA adducts
    • Chaney SG, Campbell SL, Bassett E, and Wu Y. Recognition and processing of cisplatin-and oxaliplatin-DNA adducts. Crit Rev Oncol Hematol 53: 3-11, 2005.
    • (2005) Crit Rev Oncol Hematol , vol.53 , pp. 3-11
    • Chaney, S.G.1    Campbell, S.L.2    Bassett, E.3    Wu, Y.4
  • 54
    • 78049376599 scopus 로고    scopus 로고
    • Lack of DNA polymerase mu affects the kinetics of DNA double-strand break repair and impacts on cellular senescence
    • Chayot R, Danckaert A, Montagne B, and Ricchetti M. Lack of DNA polymerase mu affects the kinetics of DNA double-strand break repair and impacts on cellular senescence. DNA Repair (Amst) 9: 1187-1199, 2010.
    • (2010) DNA Repair (Amst) , vol.9 , pp. 1187-1199
    • Chayot, R.1    Danckaert, A.2    Montagne, B.3    Ricchetti, M.4
  • 55
    • 79955940616 scopus 로고    scopus 로고
    • Ubiquitination of PCNA and its essential role in eukaryotic translesion synthesis
    • Chen J, Bozza W, and Zhuang Z. Ubiquitination of PCNA and its essential role in eukaryotic translesion synthesis. Cell Biochem Biophys 60: 47-60, 2011.
    • (2011) Cell Biochem Biophys , vol.60 , pp. 47-60
    • Chen, J.1    Bozza, W.2    Zhuang, Z.3
  • 57
    • 33646158472 scopus 로고    scopus 로고
    • A novel role of DNA polymerase eta in modulating cellular sensitivity to chemotherapeutic agents
    • Chen YW, Cleaver JE, Hanaoka F, Chang CF, and Chou KM. A novel role of DNA polymerase eta in modulating cellular sensitivity to chemotherapeutic agents. Mol Cancer Res 4: 257-265, 2006.
    • (2006) Mol Cancer Res , vol.4 , pp. 257-265
    • Chen, Y.W.1    Cleaver, J.E.2    Hanaoka, F.3    Chang, C.F.4    Chou, K.M.5
  • 59
    • 65549112632 scopus 로고    scopus 로고
    • Kinetic analysis of base-pairing preference for nucleotide incorporation opposite template pyrimidines by human DNA polymerase iota
    • Choi JY, Lim S, Eoff RL, and Guengerich FP. Kinetic analysis of base-pairing preference for nucleotide incorporation opposite template pyrimidines by human DNA polymerase iota. J Mol Biol 389: 264-274, 2009.
    • (2009) J Mol Biol , vol.389 , pp. 264-274
    • Choi, J.Y.1    Lim, S.2    Eoff, R.L.3    Guengerich, F.P.4
  • 61
    • 0031979307 scopus 로고    scopus 로고
    • The Pol beta-14 dominant negative rat DNA polymerase beta mutator mutant commits errors during the gap-filling step of base excision repair in Saccharomyces cerevisiae
    • Clairmont CA and Sweasy JB. The Pol beta-14 dominant negative rat DNA polymerase beta mutator mutant commits errors during the gap-filling step of base excision repair in Saccharomyces cerevisiae. J Bacteriol 180: 2292-2297, 1998.
    • (1998) J Bacteriol , vol.180 , pp. 2292-2297
    • Clairmont, C.A.1    Sweasy, J.B.2
  • 62
    • 0347723976 scopus 로고    scopus 로고
    • Lesion bypass by human DNA polymerase mu reveals a template-dependent, sequence-independent nucleotidyl transferase activity
    • Covo S, Blanco L, and Livneh Z. Lesion bypass by human DNA polymerase mu reveals a template-dependent, sequence-independent nucleotidyl transferase activity. J Biol Chem 279: 859-865, 2004.
    • (2004) J Biol Chem , vol.279 , pp. 859-865
    • Covo, S.1    Blanco, L.2    Livneh, Z.3
  • 63
    • 0034681138 scopus 로고    scopus 로고
    • Translesion replication by DNA polymerase beta is modulated by sequence context and stimulated by fork-like flap structures in DNA
    • Daube SS, Arad G, and Livneh Z. Translesion replication by DNA polymerase beta is modulated by sequence context and stimulated by fork-like flap structures in DNA. Biochemistry 39: 397-405, 2000.
    • (2000) Biochemistry , vol.39 , pp. 397-405
    • Daube, S.S.1    Arad, G.2    Livneh, Z.3
  • 66
    • 33847630719 scopus 로고    scopus 로고
    • Co-ordination of DNA single strand break repair
    • Dianov GL and Parsons JL. Co-ordination of DNA single strand break repair. DNA Repair (Amst) 6: 454-460, 2007.
    • (2007) DNA Repair (Amst) , vol.6 , pp. 454-460
    • Dianov, G.L.1    Parsons, J.L.2
  • 68
    • 0141542616 scopus 로고    scopus 로고
    • Decreased frequency and highly aberrant spectrum of ultraviolet-induced mutations in the hprt gene of mouse fibroblasts expressing antisense RNA to DNA polymerase zeta
    • Diaz M, Watson NB, Turkington G, Verkoczy LK, Klinman NR, and McGregor WG. Decreased frequency and highly aberrant spectrum of ultraviolet-induced mutations in the hprt gene of mouse fibroblasts expressing antisense RNA to DNA polymerase zeta. Mol Cancer Res 1: 836-847, 2003.
    • (2003) Mol Cancer Res , vol.1 , pp. 836-847
    • Diaz, M.1    Watson, N.B.2    Turkington, G.3    Verkoczy, L.K.4    Klinman, N.R.5    McGregor, W.G.6
  • 69
    • 78650575542 scopus 로고    scopus 로고
    • Suppression of Rev3, the catalytic subunit of Pol{zeta}, sensitizes drug-resistant lung tumors to chemotherapy
    • Doles J, Oliver TG, Cameron ER, Hsu G, Jacks T, Walker GC, and Hemann MT. Suppression of Rev3, the catalytic subunit of Pol{zeta}, sensitizes drug-resistant lung tumors to chemotherapy. Proc Natl Acad Sci USA 107: 20786-20791, 2010.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 20786-20791
    • Doles, J.1    Oliver, T.G.2    Cameron, E.R.3    Hsu, G.4    Jacks, T.5    Walker, G.C.6    Hemann, M.T.7
  • 72
    • 33646080364 scopus 로고    scopus 로고
    • Efficiency of exonucleolytic action of apurinic/apyrimidinic endonuclease 1 towards matched and mismatched dNMP at the 3¢ terminus of different oligomeric DNA structures correlates with thermal stability of DNA duplexes
    • Dyrkheeva NS, Lomzov AA, Pyshnyi DV, Khodyreva SN, and Lavrik OI. Efficiency of exonucleolytic action of apurinic/apyrimidinic endonuclease 1 towards matched and mismatched dNMP at the 3¢ terminus of different oligomeric DNA structures correlates with thermal stability of DNA duplexes. Biochim Biophys Acta 1764: 699-706, 2006.
    • (2006) Biochim Biophys Acta , vol.1764 , pp. 699-706
    • Dyrkheeva, N.S.1    Lomzov, A.A.2    Pyshnyi, D.V.3    Khodyreva, S.N.4    Lavrik, O.I.5
  • 73
    • 0031038053 scopus 로고    scopus 로고
    • Abasic translesion synthesis by DNA polymerase beta violates the "a-rule" Novel types of nucleotide incorporation by human DNA polymerase beta at an abasic lesion in different sequence contexts
    • Efrati E, Tocco G, Eritja R, Wilson SH, and Goodman MF. Abasic translesion synthesis by DNA polymerase beta violates the "A-rule". Novel types of nucleotide incorporation by human DNA polymerase beta at an abasic lesion in different sequence contexts. J Biol Chem 272: 2559-2569, 1997.
    • (1997) J Biol Chem , vol.272 , pp. 2559-2569
    • Efrati, E.1    Tocco, G.2    Eritja, R.3    Wilson, S.H.4    Goodman, M.F.5
  • 75
    • 0034609725 scopus 로고    scopus 로고
    • Disruption of the Rev3l-encoded catalytic subunit of polymerase zeta in mice results in early embryonic lethality
    • Esposito G, Godindagger I, Klein U, Yaspo ML, Cumano A, and Rajewsky K. Disruption of the Rev3l-encoded catalytic subunit of polymerase zeta in mice results in early embryonic lethality. Curr Biol 10: 1221-1224, 2000.
    • (2000) Curr Biol , vol.10 , pp. 1221-1224
    • Esposito, G.1    Godindagger, I.2    Klein, U.3    Yaspo, M.L.4    Cumano, A.5    Rajewsky, K.6
  • 77
    • 34247897059 scopus 로고    scopus 로고
    • The human POLH gene is not mutated, and is expressed in a cohort of patients with basal or squamous cell carcinoma of the skin
    • Flanagan AM, Rafferty G, O'Neill A, Rynne L, Kelly J, McCann J, and Carty MP. The human POLH gene is not mutated, and is expressed in a cohort of patients with basal or squamous cell carcinoma of the skin. Int J Mol Med 19: 589-596, 2007.
    • (2007) Int J Mol Med , vol.19 , pp. 589-596
    • Flanagan, A.M.1    Rafferty, G.2    O'Neill, A.3    Rynne, L.4    Kelly, J.5    McCann, J.6    Carty, M.P.7
  • 78
    • 33847625356 scopus 로고    scopus 로고
    • Base damage and single-strand break repair: Mechanisms and functional significance of short-and long-patch repair subpathways
    • Fortini P and Dogliotti E. Base damage and single-strand break repair: mechanisms and functional significance of short-and long-patch repair subpathways. DNA Repair (Amst) 6: 398-409, 2007.
    • (2007) DNA Repair (Amst) , vol.6 , pp. 398-409
    • Fortini, P.1    Dogliotti, E.2
  • 79
    • 34548337284 scopus 로고    scopus 로고
    • Increased catalytic activity and altered fidelity of human DNA polymerase iota in the presence of manganese
    • Frank EG and Woodgate R. Increased catalytic activity and altered fidelity of human DNA polymerase iota in the presence of manganese. J Biol Chem 282: 24689-24696, 2007.
    • (2007) J Biol Chem , vol.282 , pp. 24689-24696
    • Frank, E.G.1    Woodgate, R.2
  • 80
    • 85047696768 scopus 로고    scopus 로고
    • Deregulated DNA polymerase beta strengthens ionizing radiation-induced nucleotidic and chromosomal instabilities
    • Frechet M, Canitrot Y, Bieth A, Dogliotti E, Cazaux C, and Hoffmann JS. Deregulated DNA polymerase beta strengthens ionizing radiation-induced nucleotidic and chromosomal instabilities. Oncogene 21: 2320-2327, 2002.
    • (2002) Oncogene , vol.21 , pp. 2320-2327
    • Frechet, M.1    Canitrot, Y.2    Bieth, A.3    Dogliotti, E.4    Cazaux, C.5    Hoffmann, J.S.6
  • 81
    • 28844506236 scopus 로고    scopus 로고
    • Suffering in silence: The tolerance of DNA damage
    • Friedberg EC. Suffering in silence: the tolerance of DNA damage. Nat Rev Mol Cell Biol 6: 943-953, 2005.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 943-953
    • Friedberg, E.C.1
  • 83
    • 43049160831 scopus 로고    scopus 로고
    • Rad6-Rad18 mediates a eukaryotic SOS response by ubi-quitinating the 9-1-1 checkpoint clamp
    • Fu Y, Zhu Y, Zhang K, Yeung M, Durocher D, and Xiao W. Rad6-Rad18 mediates a eukaryotic SOS response by ubi-quitinating the 9-1-1 checkpoint clamp. Cell 133: 601-611, 2008.
    • (2008) Cell , vol.133 , pp. 601-611
    • Fu, Y.1    Zhu, Y.2    Zhang, K.3    Yeung, M.4    Durocher, D.5    Xiao, W.6
  • 84
    • 42149157403 scopus 로고    scopus 로고
    • Inhibitors of DNA polymerase beta: Activity and mechanism
    • Gao Z, Maloney DJ, Dedkova LM, and Hecht SM. Inhibitors of DNA polymerase beta: activity and mechanism. Bioorg Med Chem 16: 4331-4340, 2008.
    • (2008) Bioorg Med Chem , vol.16 , pp. 4331-4340
    • Gao, Z.1    Maloney, D.J.2    Dedkova, L.M.3    Hecht, S.M.4
  • 87
    • 33748877779 scopus 로고    scopus 로고
    • Mutations in DNA polymerase eta are not detected in squamous cell carcinoma of the skin
    • Glick E, White LM, Elliott NA, Berg D, Kiviat NB, and Loeb LA. Mutations in DNA polymerase eta are not detected in squamous cell carcinoma of the skin. Int J Cancer 119: 2225-2227, 2006.
    • (2006) Int J Cancer , vol.119 , pp. 2225-2227
    • Glick, E.1    White, L.M.2    Elliott, N.A.3    Berg, D.4    Kiviat, N.B.5    Loeb, L.A.6
  • 90
    • 0027976408 scopus 로고
    • Initial events in the cellular effects of ionizing radiations: Clustered damage in DNA
    • Goodhead DT. Initial events in the cellular effects of ionizing radiations: clustered damage in DNA. Int J Radiat Biol 65: 7-17, 1994.
    • (1994) Int J Radiat Biol , vol.65 , pp. 7-17
    • Goodhead, D.T.1
  • 91
    • 0035997344 scopus 로고    scopus 로고
    • Error-prone repair DNA polymerases in prokaryotes and eukaryotes
    • Goodman MF. Error-prone repair DNA polymerases in prokaryotes and eukaryotes. Annu Rev Biochem 71: 17-50, 2002.
    • (2002) Annu Rev Biochem , vol.71 , pp. 17-50
    • Goodman, M.F.1
  • 93
    • 0028059099 scopus 로고
    • Deletion of a DNA polymerase beta gene segment in T cells using cell type-specific gene targeting
    • Gu H, Marth JD, Orban PC, Mossmann H, and Rajewsky K. Deletion of a DNA polymerase beta gene segment in T cells using cell type-specific gene targeting. Science 265: 103-106, 1994.
    • (1994) Science , vol.265 , pp. 103-106
    • Gu, H.1    Marth, J.D.2    Orban, P.C.3    Mossmann, H.4    Rajewsky, K.5
  • 94
    • 48149103684 scopus 로고    scopus 로고
    • Role of DNA polymerases eta, iota and zeta in UV resistance and UV-induced mutagen-esis in a human cell line
    • Gueranger Q, Stary A, Aoufouchi S, Faili A, Sarasin A, Reynaud CA, and Weill JC. Role of DNA polymerases eta, iota and zeta in UV resistance and UV-induced mutagen-esis in a human cell line. DNA Repair (Amst) 7: 1551-1562, 2008.
    • (2008) DNA Repair (Amst) , vol.7 , pp. 1551-1562
    • Gueranger, Q.1    Stary, A.2    Aoufouchi, S.3    Faili, A.4    Sarasin, A.5    Reynaud, C.A.6    Weill, J.C.7
  • 96
    • 35348827736 scopus 로고    scopus 로고
    • The role of cellular accumulation in determining sensitivity to platinum-based chemotherapy
    • Hall MD, Okabe M, Shen DW, Liang XJ, and Gottesman MM. The role of cellular accumulation in determining sensitivity to platinum-based chemotherapy. Annu Rev Pharmacol Toxicol 48: 495-535, 2008.
    • (2008) Annu Rev Pharmacol Toxicol , vol.48 , pp. 495-535
    • Hall, M.D.1    Okabe, M.2    Shen, D.W.3    Liang, X.J.4    Gottesman, M.M.5
  • 97
    • 77951218269 scopus 로고    scopus 로고
    • Crystal structure of human REV7 in complex with a human REV3 fragment and structural implication of the interaction between DNA polymerase zeta and REV1
    • Hara K, Hashimoto H, Murakumo Y, Kobayashi S, Kogame T, Unzai S, Akashi S, Takeda S, Shimizu T, and Sato M. Crystal structure of human REV7 in complex with a human REV3 fragment and structural implication of the interaction between DNA polymerase zeta and REV1. J Biol Chem 285: 12299-12307, 2010.
    • (2010) J Biol Chem , vol.285 , pp. 12299-12307
    • Hara, K.1    Hashimoto, H.2    Murakumo, Y.3    Kobayashi, S.4    Kogame, T.5    Unzai, S.6    Akashi, S.7    Takeda, S.8    Shimizu, T.9    Sato, M.10
  • 98
    • 12844271626 scopus 로고    scopus 로고
    • A single domain in human DNA polymerase iota mediates interaction with PCNA: Implications for translesion DNA synthesis
    • Haracska L, Acharya N, Unk I, Johnson RE, Hurwitz J, Prakash L, and Prakash S. A single domain in human DNA polymerase iota mediates interaction with PCNA: implications for translesion DNA synthesis. Mol Cell Biol 25: 1183-1190, 2005.
    • (2005) Mol Cell Biol , vol.25 , pp. 1183-1190
    • Haracska, L.1    Acharya, N.2    Unk, I.3    Johnson, R.E.4    Hurwitz, J.5    Prakash, L.6    Prakash, S.7
  • 99
    • 0037058976 scopus 로고    scopus 로고
    • Role of human DNA polymerase kappa as an extender in translesion synthesis
    • Haracska L, Prakash L, and Prakash S. Role of human DNA polymerase kappa as an extender in translesion synthesis. Proc Natl Acad Sci USA 99: 16000-16005, 2002.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 16000-16005
    • Haracska, L.1    Prakash, L.2    Prakash, S.3
  • 100
    • 2942529467 scopus 로고    scopus 로고
    • Opposing effects of ubiquitin conjugation and SUMO modification of PCNA on replicational bypass of DNA lesions in Saccharomyces cerevisiae
    • Haracska L, Torres-Ramos CA, Johnson RE, Prakash S, and Prakash L. Opposing effects of ubiquitin conjugation and SUMO modification of PCNA on replicational bypass of DNA lesions in Saccharomyces cerevisiae. Mol Cell Biol 24: 4267-4274, 2004.
    • (2004) Mol Cell Biol , vol.24 , pp. 4267-4274
    • Haracska, L.1    Torres-Ramos, C.A.2    Johnson, R.E.3    Prakash, S.4    Prakash, L.5
  • 103
    • 79955027304 scopus 로고    scopus 로고
    • E3 ligase Rad18 promotes monoubiquitination rather than ubiquitin chain formation byE2 enzyme Rad6
    • Hibbert RG, Huang A, Boelens R, and Sixma TK. E3 ligase Rad18 promotes monoubiquitination rather than ubiquitin chain formation byE2 enzyme Rad6. Proc Natl Acad Sci USA 108: 5590-5595, 2011.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 5590-5595
    • Hibbert, R.G.1    Huang, A.2    Boelens, R.3    Sixma, T.K.4
  • 106
    • 0024515691 scopus 로고
    • Difference in the expression level of DNA polymerase beta among mouse tissues: High expression in the pachytene spermatocyte
    • Hirose F, Hotta Y, Yamaguchi M, and Matsukage A. Difference in the expression level of DNA polymerase beta among mouse tissues: high expression in the pachytene spermatocyte. Exp Cell Res 181: 169-180, 1989.
    • (1989) Exp Cell Res , vol.181 , pp. 169-180
    • Hirose, F.1    Hotta, Y.2    Yamaguchi, M.3    Matsukage, A.4
  • 107
    • 78650855402 scopus 로고    scopus 로고
    • Lesion bypass activity of DNA polymerase theta (POLQ) is an intrinsic property of the pol domain and depends on unique sequence inserts
    • Hogg M, Seki M, Wood RD, Doublie S, and Wallace SS. Lesion bypass activity of DNA polymerase theta (POLQ) is an intrinsic property of the pol domain and depends on unique sequence inserts. J Mol Biol 405: 642-652, 2011.
    • (2011) J Mol Biol , vol.405 , pp. 642-652
    • Hogg, M.1    Seki, M.2    Wood, R.D.3    Doublie, S.4    Wallace, S.S.5
  • 108
    • 0037193540 scopus 로고    scopus 로고
    • Involvement of DNA polymerase beta in protection against the cytotoxicity of oxidative DNA damage
    • Horton JK, Baker A, Berg BJ, Sobol RW, and Wilson SH. Involvement of DNA polymerase beta in protection against the cytotoxicity of oxidative DNA damage. DNA Repair (Amst) 1: 317-333, 2002.
    • (2002) DNA Repair (Amst) , vol.1 , pp. 317-333
    • Horton, J.K.1    Baker, A.2    Berg, B.J.3    Sobol, R.W.4    Wilson, S.H.5
  • 112
    • 33750968508 scopus 로고    scopus 로고
    • Hypoxia-inducible factor-1 mediates the expression of DNA polymerase iota in human tumor cells
    • Ito A, Koshikawa N, Mochizuki S, Omura K, and Takenaga K. Hypoxia-inducible factor-1 mediates the expression of DNA polymerase iota in human tumor cells. Biochem Bio-phys Res Commun 351: 306-311, 2006.
    • (2006) Biochem Bio-phys Res Commun , vol.351 , pp. 306-311
    • Ito, A.1    Koshikawa, N.2    Mochizuki, S.3    Omura, K.4    Takenaga, K.5
  • 113
    • 79551652711 scopus 로고    scopus 로고
    • DNA polymerase beta as a novel target for chemotherapeutic intervention of colorectal cancer
    • Jaiswal AS, Banerjee S, Aneja R, Sarkar FH, Ostrov DA, and Narayan S. DNA polymerase beta as a novel target for chemotherapeutic intervention of colorectal cancer. PLoS One 6: e16691, 2011.
    • (2011) PLoS One , vol.6
    • Jaiswal, A.S.1    Banerjee, S.2    Aneja, R.3    Sarkar, F.H.4    Ostrov, D.A.5    Narayan, S.6
  • 114
    • 77954757691 scopus 로고    scopus 로고
    • The eukaryotic replicative DNA polymerases take shape
    • Johansson E and Macneill SA. The eukaryotic replicative DNA polymerases take shape. Trends Biochem Sci 35: 339-347, 2010.
    • (2010) Trends Biochem Sci , vol.35 , pp. 339-347
    • Johansson, E.1    MacNeill, S.A.2
  • 115
    • 77949570420 scopus 로고
    • The kinetic and chemical mechanism of high-fidelity DNA polymerases
    • Johnson KA. The kinetic and chemical mechanism of high-fidelity DNA polymerases. Biochim Biophys Acta 1804: 1041-1048, 2010.
    • (1804) Biochim Biophys Acta , pp. 1041-1048
    • Johnson, K.A.1
  • 116
    • 33747765185 scopus 로고    scopus 로고
    • Role of hoogsteen edge hydrogen bonding at template purines in nucleotide incorporation by human DNA polymerase iota
    • Johnson RE, Haracska L, Prakash L, and Prakash S. Role of hoogsteen edge hydrogen bonding at template purines in nucleotide incorporation by human DNA polymerase iota. Mol Cell Biol 26: 6435-6441, 2006.
    • (2006) Mol Cell Biol , vol.26 , pp. 6435-6441
    • Johnson, R.E.1    Haracska, L.2    Prakash, L.3    Prakash, S.4
  • 117
    • 0033538470 scopus 로고    scopus 로고
    • And Prakash L. hRAD30 mutations in the variant form of xeroderma pig-mentosum
    • Johnson RE, Kondratick CM, Prakash S, and Prakash L. hRAD30 mutations in the variant form of xeroderma pig-mentosum. Science 285: 263-265, 1999.
    • (1999) Science , vol.285 , pp. 263-265
    • Johnson, R.E.1    Kondratick, C.M.2    Prakash, S.3
  • 118
    • 0034738983 scopus 로고    scopus 로고
    • Eukaryotic polymerases iota and zeta act sequentially to bypass DNA lesions
    • Johnson RE, Washington MT, Haracska L, Prakash S, and Prakash L. Eukaryotic polymerases iota and zeta act sequentially to bypass DNA lesions. Nature 406: 1015-1019, 2000.
    • (2000) Nature , vol.406 , pp. 1015-1019
    • Johnson, R.E.1    Washington, M.T.2    Haracska, L.3    Prakash, S.4    Prakash, L.5
  • 119
    • 35148820034 scopus 로고    scopus 로고
    • A role for yeast and human translesion synthesis DNA polymerases in promoting replication through 3-methyl adenine
    • Johnson RE, Yu SL, Prakash S, and Prakash L. A role for yeast and human translesion synthesis DNA polymerases in promoting replication through 3-methyl adenine. Mol Cell Biol 27: 7198-7205, 2007.
    • (2007) Mol Cell Biol , vol.27 , pp. 7198-7205
    • Johnson, R.E.1    Yu, S.L.2    Prakash, S.3    Prakash, L.4
  • 120
    • 0344741364 scopus 로고    scopus 로고
    • Checkpoint responses to replication stalling: Inducing tolerance and preventing mutagenesis
    • Kai M and Wang TS. Checkpoint responses to replication stalling: inducing tolerance and preventing mutagenesis. Mutat Res 532: 59-73, 2003.
    • (2003) Mutat Res , vol.532 , pp. 59-73
    • Kai, M.1    Wang, T.S.2
  • 121
    • 84934434583 scopus 로고    scopus 로고
    • RAD18 signals DNA polymerase IOTA to stalled replication forks in cells entering S-phase with DNA damage
    • Kakar S, Watson NB, and McGregor WG. RAD18 signals DNA polymerase IOTA to stalled replication forks in cells entering S-phase with DNA damage. Adv Exp Med Biol 614: 137-143, 2008.
    • (2008) Adv Exp Med Biol , vol.614 , pp. 137-143
    • Kakar, S.1    Watson, N.B.2    McGregor, W.G.3
  • 122
    • 33947588087 scopus 로고    scopus 로고
    • Nodulisporol and Nodulisporone, novel specific inhibitors of human DNA polymerase lambda from a fungus, Nodulisporium sp
    • Kamisuki S, Ishimaru C, Onoda K, Kuriyama I, Ida N, Sugawara F, Yoshida H, and Mizushina Y. Nodulisporol and Nodulisporone, novel specific inhibitors of human DNA polymerase lambda from a fungus, Nodulisporium sp. Bioorg Med Chem 15: 3109-3114, 2007.
    • (2007) Bioorg Med Chem , vol.15 , pp. 3109-3114
    • Kamisuki, S.1    Ishimaru, C.2    Onoda, K.3    Kuriyama, I.4    Ida, N.5    Sugawara, F.6    Yoshida, H.7    Mizushina, Y.8
  • 123
    • 0035862988 scopus 로고    scopus 로고
    • Domain structure, localization, and function of DNA polymerase eta, defective in xeroderma pigmentosum variant cells
    • Kannouche P, Broughton BC, Volker M, Hanaoka F, Mul-lenders LH, and Lehmann AR. Domain structure, localization, and function of DNA polymerase eta, defective in xeroderma pigmentosum variant cells. Genes Dev 15: 158-172, 2001.
    • (2001) Genes Dev , vol.15 , pp. 158-172
    • Kannouche, P.1    Broughton, B.C.2    Volker, M.3    Hanaoka, F.4    Mul-Lenders, L.H.5    Lehmann, A.R.6
  • 125
    • 0942268173 scopus 로고    scopus 로고
    • Xeroderma pigmentosum variant and error-prone DNA polymerases
    • Kannouche P and Stary A. Xeroderma pigmentosum variant and error-prone DNA polymerases. Biochimie 85: 1123-1132, 2003.
    • (2003) Biochimie , vol.85 , pp. 1123-1132
    • Kannouche, P.1    Stary, A.2
  • 128
    • 42149089140 scopus 로고    scopus 로고
    • Novel azaphilones, kasanosins A and B, which are specific inhibitors of eukaryotic DNA poly-merases beta and lambda from Talaromyces sp
    • Kimura T, Nishida M, Kuramochi K, Sugawara F, Yoshida H, and Mizushina Y. Novel azaphilones, kasanosins A and B, which are specific inhibitors of eukaryotic DNA poly-merases beta and lambda from Talaromyces sp. Bioorg Med Chem 16: 4594-4599, 2008.
    • (2008) Bioorg Med Chem , vol.16 , pp. 4594-4599
    • Kimura, T.1    Nishida, M.2    Kuramochi, K.3    Sugawara, F.4    Yoshida, H.5    Mizushina, Y.6
  • 131
    • 0030957997 scopus 로고    scopus 로고
    • Second pathway for completion of human DNA base excision-repair: Reconstitution with purified proteins and requirement for DNase IV (FEN1)
    • Klungland A and Lindahl T. Second pathway for completion of human DNA base excision-repair: reconstitution with purified proteins and requirement for DNase IV (FEN1). EMBO J 16: 3341-3348, 1997.
    • (1997) EMBO J , vol.16 , pp. 3341-3348
    • Klungland, A.1    Lindahl, T.2
  • 132
    • 0037072865 scopus 로고    scopus 로고
    • Fidelity of Escherichia coli DNA polymerase IV. Preferential generation of small deletion mutations by dNTP-stabilized misalignment
    • Kobayashi S, Valentine MR, Pham P, O'Donnell M, and Goodman MF. Fidelity of Escherichia coli DNA polymerase IV. Preferential generation of small deletion mutations by dNTP-stabilized misalignment. J Biol Chem 277: 34198-34207, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 34198-34207
    • Kobayashi, S.1    Valentine, M.R.2    Pham, P.3    O'Donnell, M.4    Goodman, M.F.5
  • 134
    • 0142244122 scopus 로고    scopus 로고
    • Considering the cancer consequences of altered DNA polymerase function
    • Kunkel TA. Considering the cancer consequences of altered DNA polymerase function. Cancer Cell 3: 105-110, 2003.
    • (2003) Cancer Cell , vol.3 , pp. 105-110
    • Kunkel, T.A.1
  • 136
    • 54249092768 scopus 로고    scopus 로고
    • Dividing the workload at a eukaryotic replication fork
    • Kunkel TA and Burgers PM. Dividing the workload at a eukaryotic replication fork. Trends Cell Biol 18: 521-527, 2008.
    • (2008) Trends Cell Biol , vol.18 , pp. 521-527
    • Kunkel, T.A.1    Burgers, P.M.2
  • 137
    • 10244237651 scopus 로고    scopus 로고
    • DNA binding properties of human DNA poly-merase eta: Implications for fidelity and polymerase switching of translesion synthesis
    • Kusumoto R, Masutani C, Shimmyo S, Iwai S, and Ha-naoka F. DNA binding properties of human DNA poly-merase eta: implications for fidelity and polymerase switching of translesion synthesis. Genes Cells 9: 1139-1150, 2004.
    • (2004) Genes Cells , vol.9 , pp. 1139-1150
    • Kusumoto, R.1    Masutani, C.2    Shimmyo, S.3    Iwai, S.4    Ha-Naoka, F.5
  • 138
    • 34547195827 scopus 로고    scopus 로고
    • The E295K DNA polymerase beta gastric cancer-associated variant interferes with base excision repair and induces cellular transformation
    • Lang T, Dalal S, Chikova A, DiMaio D, and Sweasy JB. The E295K DNA polymerase beta gastric cancer-associated variant interferes with base excision repair and induces cellular transformation. Mol Cell Biol 27: 5587-5596, 2007.
    • (2007) Mol Cell Biol , vol.27 , pp. 5587-5596
    • Lang, T.1    Dalal, S.2    Chikova, A.3    Dimaio, D.4    Sweasy, J.B.5
  • 139
  • 142
    • 21244487080 scopus 로고    scopus 로고
    • Genetic linkage between Pol iota deficiency and increased susceptibility to lung tumors in mice
    • Lee GH and Matsushita H. Genetic linkage between Pol iota deficiency and increased susceptibility to lung tumors in mice. Cancer Sci 96: 256-259, 2005.
    • (2005) Cancer Sci , vol.96 , pp. 256-259
    • Lee, G.H.1    Matsushita, H.2
  • 143
    • 0347683431 scopus 로고    scopus 로고
    • Implication of DNA polymerase lambda in alignment-based gap filling for nonhomologous DNA end joining in human nuclear extracts
    • Lee JW, Blanco L, Zhou T, Garcia-Diaz M, Bebenek K, Kunkel TA, Wang Z, and Povirk LF. Implication of DNA polymerase lambda in alignment-based gap filling for nonhomologous DNA end joining in human nuclear extracts. J Biol Chem 279: 805-811, 2004.
    • (2004) J Biol Chem , vol.279 , pp. 805-811
    • Lee, J.W.1    Blanco, L.2    Zhou, T.3    Garcia-Diaz, M.4    Bebenek, K.5    Kunkel, T.A.6    Wang, Z.7    Povirk, L.F.8
  • 146
    • 3042716233 scopus 로고    scopus 로고
    • Plant sterols as selective DNA polymerase beta lyase inhibitors and potentiators of bleomycin cytotoxicity
    • Li SS, Gao Z, Feng X, Jones SH, and Hecht SM. Plant sterols as selective DNA polymerase beta lyase inhibitors and potentiators of bleomycin cytotoxicity. Bioorg Med Chem 12: 4253-4258, 2004.
    • (2004) Bioorg Med Chem , vol.12 , pp. 4253-4258
    • Li, S.S.1    Gao, Z.2    Feng, X.3    Jones, S.H.4    Hecht, S.M.5
  • 147
    • 34247219683 scopus 로고    scopus 로고
    • Xeroderma pigmentosum: beyond skin cancer
    • Lichon V and Khachemoune A. Xeroderma pigmentosum: beyond skin cancer. J Drugs Dermatol 6: 281-288, 2007.
    • (2007) J Drugs Dermatol , vol.6 , pp. 281-288
    • Lichon, V.1    Khachemoune, A.2
  • 148
    • 31544479310 scopus 로고    scopus 로고
    • DNA polymerase zeta accounts for the reduced cytotoxicity and enhanced mutagenicity of cisplatin in human colon carcinoma cells that have lost DNA mismatch repair
    • Lin X, Trang J, Okuda T, and Howell SB. DNA polymerase zeta accounts for the reduced cytotoxicity and enhanced mutagenicity of cisplatin in human colon carcinoma cells that have lost DNA mismatch repair. Clin Cancer Res 12: 563-568, 2006.
    • (2006) Clin Cancer Res , vol.12 , pp. 563-568
    • Lin, X.1    Trang, J.2    Okuda, T.3    Howell, S.B.4
  • 149
    • 0033520969 scopus 로고    scopus 로고
    • Quality control by DNA repair
    • Lindahl T and Wood RD. Quality control by DNA repair. Science 286: 1897-1905, 1999.
    • (1999) Science , vol.286 , pp. 1897-1905
    • Lindahl, T.1    Wood, R.D.2
  • 150
    • 0035812849 scopus 로고    scopus 로고
    • Crystal structure of a Y-family DNA polymerase in action: A mechanism for error-prone and lesion-bypass replication
    • Ling H, Boudsocq F, Woodgate R, and Yang W. Crystal structure of a Y-family DNA polymerase in action: a mechanism for error-prone and lesion-bypass replication. Cell 107: 91-102, 2001.
    • (2001) Cell , vol.107 , pp. 91-102
    • Ling, H.1    Boudsocq, F.2    Woodgate, R.3    Yang, W.4
  • 151
    • 0027087299 scopus 로고
    • Reduced drug accumulation as a major mechanism of acquired resistance to cisplatin in a human ovarian carcinoma cell line: Circumvention studies using novel platinum (II) and (IV) ammine/amine complexes
    • Loh SY, Mistry P, Kelland LR, Abel G, and Harrap KR. Reduced drug accumulation as a major mechanism of acquired resistance to cisplatin in a human ovarian carcinoma cell line: circumvention studies using novel platinum (II) and (IV) ammine/amine complexes. Br J Cancer 66: 1109-1115, 1992.
    • (1992) Br J Cancer , vol.66 , pp. 1109-1115
    • Loh, S.Y.1    Mistry, P.2    Kelland, L.R.3    Abel, G.4    Harrap, K.R.5
  • 155
    • 0028103889 scopus 로고
    • Fluorescence in situ hybridization analysis of 8p allelic loss and chromosome 8 instability in human prostate cancer
    • Macoska JA, Trybus TM, Sakr WA, Wolf MC, Benson PD, Powell IJ, and Pontes JE. Fluorescence in situ hybridization analysis of 8p allelic loss and chromosome 8 instability in human prostate cancer. Cancer Res 54: 3824-3830, 1994.
    • (1994) Cancer Res , vol.54 , pp. 3824-3830
    • MacOska, J.A.1    Trybus, T.M.2    Sakr, W.A.3    Wolf, M.C.4    Benson, P.D.5    Powell, I.J.6    Pontes, J.E.7
  • 156
  • 157
    • 0036293744 scopus 로고    scopus 로고
    • Association of DNA polymerase mu (pol mu) with Ku and ligase IV: Role for pol mu in end-joining double-strand break repair
    • Mahajan KN, Nick McElhinny SA, Mitchell BS, and Ramsden DA. Association of DNA polymerase mu (pol mu) with Ku and ligase IV: role for pol mu in end-joining double-strand break repair. Mol Cell Biol 22: 5194-5202, 2002.
    • (2002) Mol Cell Biol , vol.22 , pp. 5194-5202
    • Mahajan, K.N.1    Nick McElhinny, S.A.2    Mitchell, B.S.3    Ramsden, D.A.4
  • 158
    • 59849089955 scopus 로고    scopus 로고
    • Repair of ionizing radiation-induced DNA double-strand breaks by non-homologous end-joining
    • Mahaney BL, Meek K, and Lees-Miller SP. Repair of ionizing radiation-induced DNA double-strand breaks by non-homologous end-joining. Biochem J 417: 639-650, 2009.
    • (2009) Biochem J , vol.417 , pp. 639-650
    • Mahaney, B.L.1    Meek, K.2    Lees-Miller, S.P.3
  • 159
    • 0037144446 scopus 로고    scopus 로고
    • Threonine 79 is a hinge residue that governs the fidelity of DNA polymerase beta by helping to position the DNA within the active site
    • Maitra M, Gudzelak A, Jr., Li SX, Matsumoto Y, Eckert KA, Jager J, and Sweasy JB. Threonine 79 is a hinge residue that governs the fidelity of DNA polymerase beta by helping to position the DNA within the active site. J Biol Chem 277: 35550-35560, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 35550-35560
    • Maitra, M.1    Gudzelak Jr. A2    Li, S.X.3    Matsumoto, Y.4    Eckert, K.A.5    Jager, J.6    Sweasy, J.B.7
  • 160
    • 48149091758 scopus 로고    scopus 로고
    • Reevaluation of the role of DNA polymerase theta in somatic hypermutation of immunoglobulin genes
    • Martomo SA, Saribasak H, Yokoi M, Hanaoka F, and Gearhart PJ. Reevaluation of the role of DNA polymerase theta in somatic hypermutation of immunoglobulin genes. DNA Repair (Amst) 7: 1603-1608, 2008.
    • (2008) DNA Repair (Amst) , vol.7 , pp. 1603-1608
    • Martomo, S.A.1    Saribasak, H.2    Yokoi, M.3    Hanaoka, F.4    Gearhart, P.J.5
  • 161
    • 0034660259 scopus 로고    scopus 로고
    • Mechanisms of accurate translesion synthesis by human DNA polymerase eta
    • Masutani C, Kusumoto R, Iwai S, and Hanaoka F. Mechanisms of accurate translesion synthesis by human DNA polymerase eta. EMBO J 19: 3100-3109, 2000.
    • (2000) EMBO J , vol.19 , pp. 3100-3109
    • Masutani, C.1    Kusumoto, R.2    Iwai, S.3    Hanaoka, F.4
  • 164
    • 0029028964 scopus 로고
    • Excision of deoxyribose phosphate residues by DNA polymerase beta during DNA repair
    • Matsumoto Y and Kim K. Excision of deoxyribose phosphate residues by DNA polymerase beta during DNA repair. Science 269: 699-702, 1995.
    • (1995) Science , vol.269 , pp. 699-702
    • Matsumoto, Y.1    Kim, K.2
  • 166
    • 1542287220 scopus 로고    scopus 로고
    • Preferential cis-syn thymine dimer bypass by DNA polymerase eta occurs with biased fidelity
    • McCulloch SD, Kokoska RJ, Masutani C, Iwai S, Hanaoka F, and Kunkel TA. Preferential cis-syn thymine dimer bypass by DNA polymerase eta occurs with biased fidelity. Nature 428: 97-100, 2004.
    • (2004) Nature , vol.428 , pp. 97-100
    • McCulloch, S.D.1    Kokoska, R.J.2    Masutani, C.3    Iwai, S.4    Hanaoka, F.5    Kunkel, T.A.6
  • 167
    • 38049125552 scopus 로고    scopus 로고
    • The fidelity of DNA synthesis by eukaryotic replicative and translesion synthesis polymerases
    • McCulloch SD and Kunkel TA. The fidelity of DNA synthesis by eukaryotic replicative and translesion synthesis polymerases. Cell Res 18: 148-161, 2008.
    • (2008) Cell Res , vol.18 , pp. 148-161
    • McCulloch, S.D.1    Kunkel, T.A.2
  • 168
    • 0032836651 scopus 로고    scopus 로고
    • Initiation of base excision repair: Glycosylase mechanisms and structures
    • McCullough AK, Dodson ML, and Lloyd RS. Initiation of base excision repair: glycosylase mechanisms and structures. Annu Rev Biochem 68: 255-285, 1999.
    • (1999) Annu Rev Biochem , vol.68 , pp. 255-285
    • McCullough, A.K.1    Dodson, M.L.2    Lloyd, R.S.3
  • 170
    • 28444470501 scopus 로고    scopus 로고
    • Human DNA polymerase eta promotes DNA synthesis from strand invasion intermediates of homologous recombination
    • McIlwraith MJ, Vaisman A, Liu Y, Fanning E, Woodgate R, and West SC. Human DNA polymerase eta promotes DNA synthesis from strand invasion intermediates of homologous recombination. Mol Cell 20: 783-792, 2005.
    • (2005) Mol Cell , vol.20 , pp. 783-792
    • McIlwraith, M.J.1    Vaisman, A.2    Liu, Y.3    Fanning, E.4    Woodgate, R.5    West, S.C.6
  • 171
    • 0027053057 scopus 로고
    • Relationship of cellular glutathione to the cytotoxicity and resistance of seven platinum compounds
    • Meijer C, Mulder NH, Timmer-Bosscha H, Sluiter WJ, Meersma GJ, and de Vries EG. Relationship of cellular glutathione to the cytotoxicity and resistance of seven platinum compounds. Cancer Res 52: 6885-6889, 1992.
    • (1992) Cancer Res , vol.52 , pp. 6885-6889
    • Meijer, C.1    Mulder, N.H.2    Timmer-Bosscha, H.3    Sluiter, W.J.4    Meersma, G.J.5    De Vries, E.G.6
  • 172
    • 0027275229 scopus 로고
    • In vitro platinum drug chemosensitivity of human cervical squamous cell carcinoma cell lines with intrinsic and acquired resistance to cisplatin
    • Mellish KJ, Kelland LR, and Harrap KR. In vitro platinum drug chemosensitivity of human cervical squamous cell carcinoma cell lines with intrinsic and acquired resistance to cisplatin. Br J Cancer 68: 240-250, 1993.
    • (1993) Br J Cancer , vol.68 , pp. 240-250
    • Mellish, K.J.1    Kelland, L.R.2    Harrap, K.R.3
  • 175
    • 75149192733 scopus 로고    scopus 로고
    • 3-O-methylfuni-cone, a selective inhibitor of mammalian Y-family DNA polymerases from an Australian sea salt fungal strain
    • Mizushina Y, Motoshima H, Yamaguchi Y, Takeuchi T, Hirano K, Sugawara F, and Yoshida H. 3-O-methylfuni-cone, a selective inhibitor of mammalian Y-family DNA polymerases from an Australian sea salt fungal strain. Mar Drugs 7: 624-639, 2009.
    • (2009) Mar Drugs , vol.7 , pp. 624-639
    • Mizushina, Y.1    Motoshima, H.2    Yamaguchi, Y.3    Takeuchi, T.4    Hirano, K.5    Sugawara, F.6    Yoshida, H.7
  • 178
    • 46649092698 scopus 로고    scopus 로고
    • A comparison of BRCT domains involved in nonhomologous end-joining: Introducing the solution structure of the BRCT domain of polymerase lambda
    • Mueller GA, Moon AF, Derose EF, Havener JM, Ramsden DA, Pedersen LC, and London RE. A comparison of BRCT domains involved in nonhomologous end-joining: introducing the solution structure of the BRCT domain of polymerase lambda. DNA Repair (Amst) 7: 1340-1351, 2008.
    • (2008) DNA Repair (Amst) , vol.7 , pp. 1340-1351
    • Mueller, G.A.1    Moon, A.F.2    Derose, E.F.3    Havener, J.M.4    Ramsden, D.A.5    Pedersen, L.C.6    London, R.E.7
  • 179
    • 43849091136 scopus 로고    scopus 로고
    • Caenorhabditis elegans POLQ-1 and HEL-308 function in two distinct DNA interstrand cross-link repair pathways
    • Muzzini DM, Plevani P, Boulton SJ, Cassata G, and Marini F. Caenorhabditis elegans POLQ-1 and HEL-308 function in two distinct DNA interstrand cross-link repair pathways. DNA Repair (Amst) 7: 941-950, 2008.
    • (2008) DNA Repair (Amst) , vol.7 , pp. 941-950
    • Muzzini, D.M.1    Plevani, P.2    Boulton, S.J.3    Cassata, G.4    Marini, F.5
  • 180
    • 40949083456 scopus 로고    scopus 로고
    • 1-deoxyrubralactone, a novel specific inhibitor of families X and y of eukaryotic DNA polymerases from a fungal strain derived from sea algae
    • Naganuma M, Nishida M, Kuramochi K, Sugawara F, Yoshida H, and Mizushina Y. 1-deoxyrubralactone, a novel specific inhibitor of families X and Y of eukaryotic DNA polymerases from a fungal strain derived from sea algae. Bioorg Med Chem 16: 2939-2944, 2008.
    • (2008) Bioorg Med Chem , vol.16 , pp. 2939-2944
    • Naganuma, M.1    Nishida, M.2    Kuramochi, K.3    Sugawara, F.4    Yoshida, H.5    Mizushina, Y.6
  • 181
    • 3142674288 scopus 로고    scopus 로고
    • Replication by human DNA polymerase-iota occurs by Hoogsteen base-pairing
    • Nair DT, Johnson RE, Prakash S, Prakash L, and Aggarwal AK. Replication by human DNA polymerase-iota occurs by Hoogsteen base-pairing. Nature 430: 377-380, 2004.
    • (2004) Nature , vol.430 , pp. 377-380
    • Nair, D.T.1    Johnson, R.E.2    Prakash, S.3    Prakash, L.4    Aggarwal, A.K.5
  • 182
    • 28444442213 scopus 로고    scopus 로고
    • Radiosensitization by a dominant negative to DNA polymerase beta is DNA polymerase beta-independent and XRCC1-dependent
    • Neijenhuis S, Begg AC, and Vens C. Radiosensitization by a dominant negative to DNA polymerase beta is DNA polymerase beta-independent and XRCC1-dependent. Radiother Oncol 76: 123-128, 2005.
    • (2005) Radiother Oncol , vol.76 , pp. 123-128
    • Neijenhuis, S.1    Begg, A.C.2    Vens, C.3
  • 184
    • 0037379215 scopus 로고    scopus 로고
    • Polymerase mu is a DNA-directed DNA/RNA polymerase
    • Nick McElhinny SA and Ramsden DA. Polymerase mu is a DNA-directed DNA/RNA polymerase. Mol Cell Biol 23: 2309-2315, 2003.
    • (2003) Mol Cell Biol , vol.23 , pp. 2309-2315
    • Nick McElhinny, S.A.1    Ramsden, D.A.2
  • 185
    • 0035879009 scopus 로고    scopus 로고
    • DNA polymerase kappa, implicated in spontaneous and DNA damage-induced mutagenesis, is overexpressed in lung cancer
    • O-Wang J, Kawamura K, Tada Y, Ohmori H, Kimura H, Sakiyama S, and Tagawa M. DNA polymerase kappa, implicated in spontaneous and DNA damage-induced mutagenesis, is overexpressed in lung cancer. Cancer Res 61: 5366-5369, 2001.
    • (2001) Cancer Res , vol.61 , pp. 5366-5369
    • O-Wang, J.1    Kawamura, K.2    Tada, Y.3    Ohmori, H.4    Kimura, H.5    Sakiyama, S.6    Tagawa, M.7
  • 186
    • 0033118432 scopus 로고    scopus 로고
    • Cells deficient in DNA polymerase beta are hypersensitive to alkylating agent-induced apoptosis and chromosomal breakage
    • Ochs K, Sobol RW, Wilson SH, and Kaina B. Cells deficient in DNA polymerase beta are hypersensitive to alkylating agent-induced apoptosis and chromosomal breakage. Cancer Res 59: 1544-1551, 1999.
    • (1999) Cancer Res , vol.59 , pp. 1544-1551
    • Ochs, K.1    Sobol, R.W.2    Wilson, S.H.3    Kaina, B.4
  • 187
    • 14044272631 scopus 로고    scopus 로고
    • Localisation of human Y-family DNA polymerase kappa: Relationship to PCNA foci
    • Ogi T, Kannouche P, and Lehmann AR. Localisation of human Y-family DNA polymerase kappa: relationship to PCNA foci. J Cell Sci 118: 129-136, 2005.
    • (2005) J Cell Sci , vol.118 , pp. 129-136
    • Ogi, T.1    Kannouche, P.2    Lehmann, A.R.3
  • 188
    • 33744789415 scopus 로고    scopus 로고
    • The Y-family DNA polymerase kappa (pol kappa) functions in mammalian nucleotide-ex-cision repair
    • Ogi T and Lehmann AR. The Y-family DNA polymerase kappa (pol kappa) functions in mammalian nucleotide-ex-cision repair. Nat Cell Biol 8: 640-642, 2006.
    • (2006) Nat Cell Biol , vol.8 , pp. 640-642
    • Ogi, T.1    Lehmann, A.R.2
  • 192
    • 67650021428 scopus 로고    scopus 로고
    • Expression of an X-family DNA polymerase, pol lambda, in the respiratory epithelium of non-small cell lung cancer patients with habitual smoking
    • Ohba T, Kometani T, Shoji F, Yano T, Yoshino I, Taguchi K, Kuraoka I, Oda S, and Maehara Y. Expression of an X-family DNA polymerase, pol lambda, in the respiratory epithelium of non-small cell lung cancer patients with habitual smoking. Mutat Res 677: 66-71, 2009.
    • (2009) Mutat Res , vol.677 , pp. 66-71
    • Ohba, T.1    Kometani, T.2    Shoji, F.3    Yano, T.4    Yoshino, I.5    Taguchi, K.6    Kuraoka, I.7    Oda, S.8    Maehara, Y.9
  • 194
    • 11144344392 scopus 로고    scopus 로고
    • Down-regulation of DNA polymerases kappa, eta, iota, and zeta in human lung, stomach, and colorectal cancers
    • Pan Q, Fang Y, Xu Y, Zhang K, and Hu X. Down-regulation of DNA polymerases kappa, eta, iota, and zeta in human lung, stomach, and colorectal cancers. Cancer Lett 217: 139-147, 2005.
    • (2005) Cancer Lett , vol.217 , pp. 139-147
    • Pan, Q.1    Fang, Y.2    Xu, Y.3    Zhang, K.4    Hu, X.5
  • 195
    • 23244437030 scopus 로고    scopus 로고
    • DNA polymerase beta promotes recruitment of DNA ligase III alpha-XRCC1 to sites of base excision repair
    • Parsons JL, Dianova, II, Allinson SL, and Dianov GL. DNA polymerase beta promotes recruitment of DNA ligase III alpha-XRCC1 to sites of base excision repair. Biochemistry 44: 10613-10619, 2005.
    • (2005) Biochemistry , vol.44 , pp. 10613-10619
    • Parsons, J.L.1    Dianova, I.I.2    Allinson, S.L.3    Dianov, G.L.4
  • 196
    • 0033585087 scopus 로고    scopus 로고
    • Long patch base excision repair with purified human proteins. DNA ligase i as patch size mediator for DNA polymerases delta and epsilon
    • Pascucci B, Stucki M, Jonsson ZO, Dogliotti E, and Hub-scher U. Long patch base excision repair with purified human proteins. DNA ligase I as patch size mediator for DNA polymerases delta and epsilon. J Biol Chem 274: 33696-33702, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 33696-33702
    • Pascucci, B.1    Stucki, M.2    Jonsson, Z.O.3    Dogliotti, E.4    Hub-Scher, U.5
  • 197
    • 0028049441 scopus 로고
    • Structures of ternary complexes of rat DNA polymerase beta, a DNA template-primer, and ddCTP
    • Pelletier H, Sawaya MR, Kumar A, Wilson SH, and Kraut J. Structures of ternary complexes of rat DNA polymerase beta, a DNA template-primer, and ddCTP. Science 264: 1891-1903, 1994.
    • (1994) Science , vol.264 , pp. 1891-903
    • Pelletier, H.1    Sawaya, M.R.2    Kumar, A.3    Wilson, S.H.4    Kraut, J.5
  • 199
    • 33847775919 scopus 로고    scopus 로고
    • Upregulation of error-prone DNA polymerases beta and kappa slows down fork progression without activating the replication checkpoint
    • Pillaire MJ, Betous R, Conti C, Czaplicki J, Pasero P, Ben-simon A, Cazaux C, and Hoffmann JS. Upregulation of error-prone DNA polymerases beta and kappa slows down fork progression without activating the replication checkpoint. Cell Cycle 6: 471-477, 2007.
    • (2007) Cell Cycle , vol.6 , pp. 471-477
    • Pillaire, M.J.1    Betous, R.2    Conti, C.3    Czaplicki, J.4    Pasero, P.5    Ben-Simon, A.6    Cazaux, C.7    Hoffmann, J.S.8
  • 201
    • 43849089895 scopus 로고    scopus 로고
    • Negligible impact of pol iota expression on the alkylation sensitivity of pol beta-deficient mouse fibroblast cells
    • Poltoratsky V, Horton JK, Prasad R, Beard WA, Woodgate R, and Wilson SH. Negligible impact of pol iota expression on the alkylation sensitivity of pol beta-deficient mouse fibroblast cells. DNA Repair (Amst) 7: 830-833, 2008.
    • (2008) DNA Repair (Amst) , vol.7 , pp. 830-833
    • Poltoratsky, V.1    Horton, J.K.2    Prasad, R.3    Beard, W.A.4    Woodgate, R.5    Wilson, S.H.6
  • 202
    • 24944540730 scopus 로고    scopus 로고
    • REV1 mediated mutagenesis in base excision repair deficient mouse fibroblast
    • Poltoratsky V, Horton JK, Prasad R, and Wilson SH. REV1 mediated mutagenesis in base excision repair deficient mouse fibroblast. DNA Repair (Amst) 4: 1182-1188, 2005.
    • (2005) DNA Repair (Amst) , vol.4 , pp. 1182-1188
    • Poltoratsky, V.1    Horton, J.K.2    Prasad, R.3    Wilson, S.H.4
  • 203
    • 21244506437 scopus 로고    scopus 로고
    • Eukaryotic trans-lesion synthesis DNA polymerases: Specificity of structure and function
    • Prakash S, Johnson RE, and Prakash L. Eukaryotic trans-lesion synthesis DNA polymerases: specificity of structure and function. Annu Rev Biochem 74: 317-353, 2005.
    • (2005) Annu Rev Biochem , vol.74 , pp. 317-353
    • Prakash, S.1    Johnson, R.E.2    Prakash, L.3
  • 204
    • 77953257303 scopus 로고    scopus 로고
    • Incorporation of gemcitabine and cytarabine into DNA by DNA polymerase beta and ligase III/XRCC1
    • Prakasha Gowda AS, Polizzi JM, Eckert KA, and Spratt TE. Incorporation of gemcitabine and cytarabine into DNA by DNA polymerase beta and ligase III/XRCC1. Biochemistry 49: 4833-4840, 2010.
    • (2010) Biochemistry , vol.49 , pp. 4833-4840
    • Prakasha Gowda, A.S.1    Polizzi, J.M.2    Eckert, K.A.3    Spratt, T.E.4
  • 205
    • 0032510962 scopus 로고    scopus 로고
    • Human DNA polymerase beta deoxyribose phosphate lyase. Substrate specificity and catalytic mechanism
    • Prasad R, Beard WA, Strauss PR, and Wilson SH. Human DNA polymerase beta deoxyribose phosphate lyase. Substrate specificity and catalytic mechanism. J Biol Chem 273: 15263-15270, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 15263-15270
    • Prasad, R.1    Beard, W.A.2    Strauss, P.R.3    Wilson, S.H.4
  • 206
    • 64549092249 scopus 로고    scopus 로고
    • Human DNA polymerase theta possesses 5¢-dRP lyase activity and functions in single-nucleotide base excision repair in vitro
    • Prasad R, Longley MJ, Sharief FS, Hou EW, Copeland WC, and Wilson SH. Human DNA polymerase theta possesses 5¢-dRP lyase activity and functions in single-nucleotide base excision repair in vitro. Nucleic Acids Res 37: 1868-1877, 2009.
    • (2009) Nucleic Acids Res , vol.37 , pp. 1868-1877
    • Prasad, R.1    Longley, M.J.2    Sharief, F.S.3    Hou, E.W.4    Copeland, W.C.5    Wilson, S.H.6
  • 209
    • 0034676229 scopus 로고    scopus 로고
    • Alteration of ultraviolet-induced mutagenesis in yeast through molecular modulation of the REV3 and REV7 gene expression
    • Rajpal DK, Wu X, and Wang Z. Alteration of ultraviolet-induced mutagenesis in yeast through molecular modulation of the REV3 and REV7 gene expression. Mutat Res 461: 133-143, 2000.
    • (2000) Mutat Res , vol.461 , pp. 133-143
    • Rajpal, D.K.1    Wu, X.2    Wang, Z.3
  • 210
    • 0037163036 scopus 로고    scopus 로고
    • And Geacintov NE. trans-Lesion synthesis past bulky benzo[a]pyrene diol epoxide N2-dG and N6-dA lesions catalyzed by DNA bypass polymerases
    • Rechkoblit O, Zhang Y, Guo D, Wang Z, Amin S, Krze-minsky J, Louneva N, and Geacintov NE. trans-Lesion synthesis past bulky benzo[a]pyrene diol epoxide N2-dG and N6-dA lesions catalyzed by DNA bypass polymerases. J Biol Chem 277: 30488-30494, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 30488-30494
    • Rechkoblit, O.1    Zhang, Y.2    Guo, D.3    Wang, Z.4    Amin, S.5    Krze-Minsky, J.6    Louneva, N.7
  • 211
    • 7244255742 scopus 로고    scopus 로고
    • Pre-steady-state kinetic studies of the fidelity of human DNA polymerase mu
    • Roettger MP, Fiala KA, Sompalli S, Dong Y, and Suo Z. Pre-steady-state kinetic studies of the fidelity of human DNA polymerase mu. Biochemistry 43: 13827-13838, 2004.
    • (2004) Biochemistry , vol.43 , pp. 13827-13838
    • Roettger, M.P.1    Fiala, K.A.2    Sompalli, S.3    Dong, Y.4    Suo, Z.5
  • 214
    • 33644616440 scopus 로고    scopus 로고
    • The 9-1-1 checkpoint clamp physically interacts with polzeta and is partially required for spontaneous polzeta-dependent mu-tagenesis in Saccharomyces cerevisiae
    • Sabbioneda S, Minesinger BK, Giannattasio M, Plevani P, Muzi-Falconi M, and Jinks-Robertson S. The 9-1-1 checkpoint clamp physically interacts with polzeta and is partially required for spontaneous polzeta-dependent mu-tagenesis in Saccharomyces cerevisiae. J Biol Chem 280: 38657-38665, 2005.
    • (2005) J Biol Chem , vol.280 , pp. 38657-38665
    • Sabbioneda, S.1    Minesinger, B.K.2    Giannattasio, M.3    Plevani, P.4    Muzi-Falconi, M.5    Jinks-Robertson, S.6
  • 215
    • 0032544558 scopus 로고    scopus 로고
    • Fidelity and mutational specificity of uracil-initiated base excision DNA repair synthesis in human glioblastoma cell extracts
    • Sanderson RJ and Mosbaugh DW. Fidelity and mutational specificity of uracil-initiated base excision DNA repair synthesis in human glioblastoma cell extracts. J Biol Chem 273: 24822-24831, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 24822-24831
    • Sanderson, R.J.1    Mosbaugh, D.W.2
  • 216
    • 78049369869 scopus 로고    scopus 로고
    • Role of the ubiquitin-binding domain of Poleta in Rad18-independent transle-sion DNA synthesis in human cell extracts
    • Schmutz V, Janel-Bintz R, Wagner J, Biard D, Shiomi N, Fuchs RP, and Cordonnier AM. Role of the ubiquitin-binding domain of Poleta in Rad18-independent transle-sion DNA synthesis in human cell extracts. Nucleic Acids Res 38: 6456-6465, 2010.
    • (2010) Nucleic Acids Res , vol.38 , pp. 6456-6465
    • Schmutz, V.1    Janel-Bintz, R.2    Wagner, J.3    Biard, D.4    Shiomi, N.5    Fuchs, R.P.6    Cordonnier, A.M.7
  • 217
    • 0344011127 scopus 로고    scopus 로고
    • POLQ (Pol theta), a DNA polymerase and DNA-dependent ATPase in human cells
    • Seki M, Marini F, and Wood RD. POLQ (Pol theta), a DNA polymerase and DNA-dependent ATPase in human cells. Nucleic Acids Res 31: 6117-6126, 2003.
    • (2003) Nucleic Acids Res , vol.31 , pp. 6117-6126
    • Seki, M.1    Marini, F.2    Wood, R.D.3
  • 219
    • 36549043013 scopus 로고    scopus 로고
    • DNA polymerase theta (POLQ) can extend from mismatches and from bases opposite a (6-4) photoproduct
    • Seki M and Wood RD. DNA polymerase theta (POLQ) can extend from mismatches and from bases opposite a (6-4) photoproduct. DNA Repair (Amst) 7: 119-127, 2008.
    • (2008) DNA Repair (Amst) , vol.7 , pp. 119-127
    • Seki, M.1    Wood, R.D.2
  • 221
    • 34548241809 scopus 로고    scopus 로고
    • Targeting base excision repair to improve cancer therapies
    • Sharma RA and Dianov GL. Targeting base excision repair to improve cancer therapies. Mol Aspects Med 28: 345-374, 2007.
    • (2007) Mol Aspects Med , vol.28 , pp. 345-374
    • Sharma, R.A.1    Dianov, G.L.2
  • 223
    • 18044383922 scopus 로고    scopus 로고
    • Normal immunoglobulin gene somatic hy-permutation in Pol kappa-Pol iota double-deficient mice
    • Shimizu T, Azuma T, Ishiguro M, Kanjo N, Yamada S, and Ohmori H. Normal immunoglobulin gene somatic hy-permutation in Pol kappa-Pol iota double-deficient mice. Immunol Lett 98: 259-264, 2005.
    • (2005) Immunol Lett , vol.98 , pp. 259-264
    • Shimizu, T.1    Azuma, T.2    Ishiguro, M.3    Kanjo, N.4    Yamada, S.5    Ohmori, H.6
  • 225
    • 4944235161 scopus 로고    scopus 로고
    • Exchangeability of mammalian DNA ligases between base excision repair pathways
    • Sleeth KM, Robson RL, and Dianov GL. Exchangeability of mammalian DNA ligases between base excision repair pathways. Biochemistry 43: 12924-12930, 2004.
    • (2004) Biochemistry , vol.43 , pp. 12924-12930
    • Sleeth, K.M.1    Robson, R.L.2    Dianov, G.L.3
  • 228
    • 0032987099 scopus 로고    scopus 로고
    • DNA polymerase beta expression differences in selected human tumors and cell lines
    • Srivastava DK, Husain I, Arteaga CL, and Wilson SH. DNA polymerase beta expression differences in selected human tumors and cell lines. Carcinogenesis 20: 1049-1054, 1999.
    • (1999) Carcinogenesis , vol.20 , pp. 1049-1054
    • Srivastava, D.K.1    Husain, I.2    Arteaga, C.L.3    Wilson, S.H.4
  • 229
    • 75149154678 scopus 로고    scopus 로고
    • Potentiation of temozolomide cytotoxicity by inhibition of DNA polymerase beta is accentuated by BRCA2 mutation
    • Stachelek GC, Dalal S, Donigan KA, Campisi Hegan D, Sweasy JB, and Glazer PM. Potentiation of temozolomide cytotoxicity by inhibition of DNA polymerase beta is accentuated by BRCA2 mutation. Cancer Res 70: 409-417, 2010.
    • (2010) Cancer Res , vol.70 , pp. 409-417
    • Stachelek, G.C.1    Dalal, S.2    Donigan, K.A.3    Campisi Hegan, D.4    Sweasy, J.B.5    Glazer, P.M.6
  • 231
    • 13944279514 scopus 로고    scopus 로고
    • Is there a link between DNA polymerase beta and cancer?
    • Starcevic D, Dalal S, and Sweasy JB. Is there a link between DNA polymerase beta and cancer? Cell Cycle 3: 998-1001, 2004.
    • (2004) Cell Cycle , vol.3 , pp. 998-1001
    • Starcevic, D.1    Dalal, S.2    Sweasy, J.B.3
  • 232
    • 0033581011 scopus 로고    scopus 로고
    • DNA polymerases: Structural diversity and common mechanisms
    • Steitz TA. DNA polymerases: structural diversity and common mechanisms. J Biol Chem 274: 17395-17398, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 17395-17398
    • Steitz, T.A.1
  • 233
    • 14844338678 scopus 로고    scopus 로고
    • Human base excision repair enzymes apurinic/apyrimidinic endonuclease1 (APE1), DNA polymerase beta and poly(ADP-ribose) polymerase 1: Interplay between strand-displacement DNA synthesis and proofreading exonuclease activity
    • Sukhanova MV, Khodyreva SN, Lebedeva NA, Prasad R, Wilson SH, and Lavrik OI. Human base excision repair enzymes apurinic/apyrimidinic endonuclease1 (APE1), DNA polymerase beta and poly(ADP-ribose) polymerase 1: interplay between strand-displacement DNA synthesis and proofreading exonuclease activity. Nucleic Acids Res 33: 1222-1229, 2005.
    • (2005) Nucleic Acids Res , vol.33 , pp. 1222-1229
    • Sukhanova, M.V.1    Khodyreva, S.N.2    Lebedeva, N.A.3    Prasad, R.4    Wilson, S.H.5    Lavrik, O.I.6
  • 234
    • 26444605433 scopus 로고    scopus 로고
    • Expression of DNA polymerase {beta} cancer-associated variants in mouse cells results in cellular transformation
    • Sweasy JB, Lang T, Starcevic D, Sun KW, Lai CC, Dimaio D, and Dalal S. Expression of DNA polymerase {beta} cancer-associated variants in mouse cells results in cellular transformation. Proc Natl Acad Sci USA 102: 14350-14355, 2005.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 14350-14355
    • Sweasy, J.B.1    Lang, T.2    Starcevic, D.3    Sun, K.W.4    Lai, C.C.5    Dimaio, D.6    Dalal, S.7
  • 235
    • 33644867114 scopus 로고    scopus 로고
    • Involvement of vertebrate Polkappa in translesion DNA synthesis across DNA monoalkylation damage
    • Takenaka K, Ogi T, Okada T, Sonoda E, Guo C, Friedberg EC, and Takeda S. Involvement of vertebrate Polkappa in translesion DNA synthesis across DNA monoalkylation damage. J Biol Chem 281: 2000-2004, 2006.
    • (2006) J Biol Chem , vol.281 , pp. 2000-2004
    • Takenaka, K.1    Ogi, T.2    Okada, T.3    Sonoda, E.4    Guo, C.5    Friedberg, E.C.6    Takeda, S.7
  • 237
    • 78649334377 scopus 로고    scopus 로고
    • DNA polymer-ase eta protein expression predicts treatment response and survival of metastatic gastric adenocarcinoma patients treated with oxaliplatin-based chemotherapy
    • Teng KY, Qiu MZ, Li ZH, Luo HY, Zeng ZL, Luo RZ, Zhang HZ, Wang ZQ, Li YH, and Xu RH. DNA polymer-ase eta protein expression predicts treatment response and survival of metastatic gastric adenocarcinoma patients treated with oxaliplatin-based chemotherapy. J Transl Med 8: 126, 2010.
    • (2010) J Transl Med , vol.8 , pp. 126
    • Teng, K.Y.1    Qiu, M.Z.2    Zh, L.3    Luo, H.Y.4    Zeng, Z.L.5    Luo, R.Z.6    Zhang, H.Z.7    Wang, Z.Q.8    Li, Y.H.9    Xu, R.H.10
  • 239
    • 0034786832 scopus 로고    scopus 로고
    • DNA polymerase eta undergoes alternative splicing, protects against UV sensitivity and apoptosis, and suppresses Mre11-dependent recombination
    • Thakur M, Wernick M, Collins C, Limoli CL, Crowley E, and Cleaver JE. DNA polymerase eta undergoes alternative splicing, protects against UV sensitivity and apoptosis, and suppresses Mre11-dependent recombination. Genes Chromosomes Cancer 32: 222-235, 2001.
    • (2001) Genes Chromosomes Cancer , vol.32 , pp. 222-235
    • Thakur, M.1    Wernick, M.2    Collins, C.3    Limoli, C.L.4    Crowley, E.5    Cleaver, J.E.6
  • 240
    • 22244448679 scopus 로고    scopus 로고
    • The role of base excision repair in the sensitivity and resistance to temozolomide-mediated cell death
    • Trivedi RN, Almeida KH, Fornsaglio JL, Schamus S, and Sobol RW. The role of base excision repair in the sensitivity and resistance to temozolomide-mediated cell death. Cancer Res 65: 6394-6400, 2005.
    • (2005) Cancer Res , vol.65 , pp. 6394-6400
    • Trivedi, R.N.1    Almeida, K.H.2    Fornsaglio, J.L.3    Schamus, S.4    Sobol, R.W.5
  • 241
    • 47949120006 scopus 로고    scopus 로고
    • Human methyl purine DNA glycosylase and DNA polymerase beta expression collectively predict sensitivity to temozolomide
    • Trivedi RN, Wang XH, Jelezcova E, Goellner EM, Tang JB, and Sobol RW. Human methyl purine DNA glycosylase and DNA polymerase beta expression collectively predict sensitivity to temozolomide. Mol Pharmacol 74: 505-516, 2008.
    • (2008) Mol Pharmacol , vol.74 , pp. 505-516
    • Trivedi, R.N.1    Wang, X.H.2    Jelezcova, E.3    Goellner, E.M.4    Tang, J.B.5    Sobol, R.W.6
  • 242
    • 58549094699 scopus 로고    scopus 로고
    • Distribution and roles of X-family DNA polymerases in eukaryotes
    • Uchiyama Y, Takeuchi R, Kodera H, and Sakaguchi K. Distribution and roles of X-family DNA polymerases in eukaryotes. Biochimie 91: 165-170, 2009.
    • (2009) Biochimie , vol.91 , pp. 165-170
    • Uchiyama, Y.1    Takeuchi, R.2    Kodera, H.3    Sakaguchi, K.4
  • 243
    • 0034724922 scopus 로고    scopus 로고
    • The efficiency and fidelity of translesion synthesis past cisplatin and oxaliplatin GpG adducts by human DNA polymerase beta
    • Vaisman A and Chaney SG. The efficiency and fidelity of translesion synthesis past cisplatin and oxaliplatin GpG adducts by human DNA polymerase beta. J Biol Chem 275: 13017-13025, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 13017-13025
    • Vaisman, A.1    Chaney, S.G.2
  • 244
    • 0034712656 scopus 로고    scopus 로고
    • Efficient translesion replication past oxaliplatin and cisplatin GpG adducts by human DNA polymerase eta
    • Vaisman A, Masutani C, Hanaoka F, and Chaney SG. Efficient translesion replication past oxaliplatin and cisplatin GpG adducts by human DNA polymerase eta. Biochemistry 39: 4575-4580, 2000.
    • (2000) Biochemistry , vol.39 , pp. 4575-4580
    • Vaisman, A.1    Masutani, C.2    Hanaoka, F.3    Chaney, S.G.4
  • 245
    • 0035378482 scopus 로고    scopus 로고
    • The effect of DNA structure on the catalytic efficiency and fidelity of human DNA polymerase beta on templates with platinum-DNA adducts
    • Vaisman A, Warren MW, and Chaney SG. The effect of DNA structure on the catalytic efficiency and fidelity of human DNA polymerase beta on templates with platinum-DNA adducts. J Biol Chem 276: 18999-19005, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 18999-19005
    • Vaisman, A.1    Warren, M.W.2    Chaney, S.G.3
  • 246
    • 79952579536 scopus 로고    scopus 로고
    • Gene expression profiles of non-small cell lung cancer: Survival prediction and new biomarkers
    • Valk K, Vooder T, Kolde R, Reintam MA, Petzold C, Vilo J, and Metspalu A. Gene expression profiles of non-small cell lung cancer: survival prediction and new biomarkers. Oncology 79: 283-292, 2010.
    • (2010) Oncology , vol.79 , pp. 283-292
    • Valk, K.1    Vooder, T.2    Kolde, R.3    Reintam, M.A.4    Petzold, C.5    Vilo, J.6    Metspalu, A.7
  • 250
    • 38849173186 scopus 로고    scopus 로고
    • Ionizing radiation sensitivity of DNA polymerase lambda-deficient cells
    • Vermeulen C, Bertocci B, Begg AC, and Vens C. Ionizing radiation sensitivity of DNA polymerase lambda-deficient cells. Radiat Res 168: 683-688, 2007.
    • (2007) Radiat Res , vol.168 , pp. 683-688
    • Vermeulen, C.1    Bertocci, B.2    Begg, A.C.3    Vens, C.4
  • 251
    • 78650297834 scopus 로고    scopus 로고
    • Analysis of specialized DNA polymerases expression in human gliomas: Association with prognostic significance
    • Wang H, Wu W, Wang HW, Wang S, Chen Y, Zhang X, Yang J, Zhao S, Ding HF, and Lu D. Analysis of specialized DNA polymerases expression in human gliomas: association with prognostic significance. Neuro Oncol 12: 679-686, 2010.
    • (2010) Neuro Oncol , vol.12 , pp. 679-686
    • Wang, H.1    Wu, W.2    Wang, H.W.3    Wang, S.4    Chen, Y.5    Zhang, X.6    Yang, J.7    Zhao, S.8    Ding, H.F.9    Lu, D.10
  • 252
    • 34248195087 scopus 로고    scopus 로고
    • Evidence that in xeroderma pigmento-sum variant cells, which lack DNA polymerase eta, DNA polymerase iota causes the very high frequency and unique spectrum of UV-induced mutations
    • Wang Y, Woodgate R, McManus TP, Mead S, McCormick JJ, and Maher VM. Evidence that in xeroderma pigmento-sum variant cells, which lack DNA polymerase eta, DNA polymerase iota causes the very high frequency and unique spectrum of UV-induced mutations. Cancer Res 67: 3018-3026, 2007.
    • (2007) Cancer Res , vol.67 , pp. 3018-3026
    • Wang, Y.1    Woodgate, R.2    McManus, T.P.3    Mead, S.4    McCormick, J.J.5    Maher, V.M.6
  • 254
    • 0037133339 scopus 로고    scopus 로고
    • Human DINB1-encoded DNA polymerase kappa is a promiscuous extender of mispaired primer termini
    • Washington MT, Johnson RE, Prakash L, and Prakash S. Human DINB1-encoded DNA polymerase kappa is a promiscuous extender of mispaired primer termini. Proc Natl Acad Sci USA 99: 1910-1914, 2002.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 1910-1914
    • Washington, M.T.1    Johnson, R.E.2    Prakash, L.3    Prakash, S.4
  • 255
    • 6344288785 scopus 로고    scopus 로고
    • Rad18 guides poleta to replication stalling sites through physical interaction and PCNA monoubiquitination
    • Watanabe K, Tateishi S, Kawasuji M, Tsurimoto T, Inoue H, and Yamaizumi M. Rad18 guides poleta to replication stalling sites through physical interaction and PCNA monoubiquitination. EMBO J 23: 3886-3896, 2004.
    • (2004) EMBO J , vol.23 , pp. 3886-3896
    • Watanabe, K.1    Tateishi, S.2    Kawasuji, M.3    Tsurimoto, T.4    Inoue, H.5    Yamaizumi, M.6
  • 258
    • 0025314841 scopus 로고
    • Mismatch-specific thymine DNA glycosylase and DNA polymerase beta mediate the correction of G.T mispairs in nuclear extracts from human cells
    • Wiebauer K and Jiricny J. Mismatch-specific thymine DNA glycosylase and DNA polymerase beta mediate the correction of G.T mispairs in nuclear extracts from human cells. Proc Natl Acad Sci USA 87: 5842-5845, 1990.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 5842-5845
    • Wiebauer, K.1    Jiricny, J.2
  • 259
    • 53249097348 scopus 로고    scopus 로고
    • Control of DNA polymerase lambda stability by phosphoryla-tion and ubiquitination during the cell cycle
    • Wimmer U, Ferrari E, Hunziker P, and Hubscher U. Control of DNA polymerase lambda stability by phosphoryla-tion and ubiquitination during the cell cycle. EMBO Rep 9: 1027-1033, 2008.
    • (2008) EMBO Rep , vol.9 , pp. 1027-1033
    • Wimmer, U.1    Ferrari, E.2    Hunziker, P.3    Hubscher, U.4
  • 261
    • 31544434491 scopus 로고    scopus 로고
    • Loss of DNA polymerase zeta causes chromosomal instability in mammalian cells
    • Wittschieben JP, Reshmi SC, Gollin SM, and Wood RD. Loss of DNA polymerase zeta causes chromosomal instability in mammalian cells. Cancer Res 66: 134-142, 2006.
    • (2006) Cancer Res , vol.66 , pp. 134-142
    • Wittschieben, J.P.1    Reshmi, S.C.2    Gollin, S.M.3    Wood, R.D.4
  • 262
    • 27544479146 scopus 로고    scopus 로고
    • DNA polymerases eta and kappa are responsible for error-free translesion DNA synthesis activity over a cis-syn thymine dimer in Xenopus laevis oocyte extracts
    • Yagi Y, Ogawara D, Iwai S, Hanaoka F, Akiyama M, and Maki H. DNA polymerases eta and kappa are responsible for error-free translesion DNA synthesis activity over a cis-syn thymine dimer in Xenopus laevis oocyte extracts. DNA Repair (Amst) 4: 1252-1269, 2005.
    • (2005) DNA Repair (Amst) , vol.4 , pp. 1252-1269
    • Yagi, Y.1    Ogawara, D.2    Iwai, S.3    Hanaoka, F.4    Akiyama, M.5    Maki, H.6
  • 264
    • 77949571124 scopus 로고
    • DNA polymerase family X: Function, structure, and cellular roles
    • Yamtich J and Sweasy JB. DNA polymerase family X: function, structure, and cellular roles. Biochim Biophys Acta 1804: 1136-1150, 2010.
    • (1804) Biochim Biophys Acta , pp. 1136-1150
    • Yamtich, J.1    Sweasy, J.B.2
  • 265
    • 4143081674 scopus 로고    scopus 로고
    • Altered DNA polymerase iota expression in breast cancer cells leads to a reduction in DNA replication fidelity and a higher rate of mutagenesis
    • Yang J, Chen Z, Liu Y, Hickey RJ, and Malkas LH. Altered DNA polymerase iota expression in breast cancer cells leads to a reduction in DNA replication fidelity and a higher rate of mutagenesis. Cancer Res 64: 5597-5607, 2004.
    • (2004) Cancer Res , vol.64 , pp. 5597-5607
    • Yang, J.1    Chen, Z.2    Liu, Y.3    Hickey, R.J.4    Malkas, L.H.5
  • 267
    • 33749342111 scopus 로고    scopus 로고
    • Translesion synthesis past tamoxifen-derived DNA adducts by human DNA polymerases eta and kappa
    • Yasui M, Suzuki N, Laxmi YR, and Shibutani S. Translesion synthesis past tamoxifen-derived DNA adducts by human DNA polymerases eta and kappa. Biochemistry 45: 12167-12174, 2006.
    • (2006) Biochemistry , vol.45 , pp. 12167-12174
    • Yasui, M.1    Suzuki, N.2    Laxmi, Y.R.3    Shibutani, S.4
  • 269
    • 79958072354 scopus 로고    scopus 로고
    • DNA polymerases provide a canon of strategies for translesion synthesis past oxidatively generated lesions
    • Zahn KE, Wallace SS, and Doublie S. DNA polymerases provide a canon of strategies for translesion synthesis past oxidatively generated lesions. Curr Opin Struct Biol 21: 358-369, 2011.
    • (2011) Curr Opin Struct Biol , vol.21 , pp. 358-369
    • Zahn, K.E.1    Wallace, S.S.2    Doublie, S.3
  • 271
    • 0035158355 scopus 로고    scopus 로고
    • Highly frequent frameshift DNA synthesis by human DNA poly-merase mu
    • Zhang Y, Wu X, Yuan F, Xie Z, and Wang Z. Highly frequent frameshift DNA synthesis by human DNA poly-merase mu. Mol Cell Biol 21: 7995-8006, 2001.
    • (2001) Mol Cell Biol , vol.21 , pp. 7995-8006
    • Zhang, Y.1    Wu, X.2    Yuan, F.3    Xie, Z.4    Wang, Z.5
  • 274
    • 0023699975 scopus 로고
    • Characterization of DNA polymerase beta mRNA: Cell-cycle and growth response in cultured human cells
    • Zmudzka BZ, Fornace A, Collins J, and Wilson SH. Characterization of DNA polymerase beta mRNA: cell-cycle and growth response in cultured human cells. Nucleic Acids Res 16: 9587-9596, 1988.
    • (1988) Nucleic Acids Res , vol.16 , pp. 9587-9596
    • Zmudzka, B.Z.1    Fornace, A.2    Collins, J.3    Wilson, S.H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.