메뉴 건너뛰기




Volumn 743-744, Issue , 2013, Pages 44-52

Evidence for base excision repair processing of DNA interstrand crosslinks

Author keywords

AP endonuclease; Base excision repair; BCNU; Cisplatin; DNA glycosylase; DNA Polymerase beta; Interstrand crosslinks; Mitomycin C; Nitrogen mustard; Oxaliplatin; Psoralen

Indexed keywords

3 ALKYLADENINE DNA GLYCOSYLASE; APHIDICOLIN; CARMUSTINE; CISPLATIN; DNA (APURINIC OR APYRIMIDINIC SITE) LYASE; DNA (APURINIC OR APYRIMIDINIC SITE) LYASE 1; DNA DIRECTED DNA POLYMERASE BETA; DNA DIRECTED DNA POLYMERASE EPSILON; DNA DIRECTED DNA POLYMERASE GAMMA; DNA GLYCOSYLTRANSFERASE; DNA POLYMERASE; ENDONUCLEASE; MITOMYCIN; NEIL1 PROTEIN; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; OXALIPLATIN; PROTEIN FEN1; REACTIVE OXYGEN METABOLITE; UNCLASSIFIED DRUG; XRCC1 PROTEIN;

EID: 84877923913     PISSN: 00275107     EISSN: 09218262     Source Type: Journal    
DOI: 10.1016/j.mrfmmm.2012.11.007     Document Type: Review
Times cited : (19)

References (157)
  • 2
    • 25444501238 scopus 로고    scopus 로고
    • Repair of genome destabilizing lesions
    • Reddy M.C., Vasquez K.M. Repair of genome destabilizing lesions. Radiat. Res. 2005, 164:345-356.
    • (2005) Radiat. Res. , vol.164 , pp. 345-356
    • Reddy, M.C.1    Vasquez, K.M.2
  • 3
    • 11144357255 scopus 로고    scopus 로고
    • Cellular machineries for chromosomal DNA repair
    • Peterson C.L., Cote J. Cellular machineries for chromosomal DNA repair. Genes Dev. 2004, 18:602-616.
    • (2004) Genes Dev. , vol.18 , pp. 602-616
    • Peterson, C.L.1    Cote, J.2
  • 4
    • 44449112688 scopus 로고    scopus 로고
    • Base excision DNA repair
    • Zharkov D.O. Base excision DNA repair. Cell. Mol. Life Sci. 2008, 65:1544-1565.
    • (2008) Cell. Mol. Life Sci. , vol.65 , pp. 1544-1565
    • Zharkov, D.O.1
  • 6
    • 50649108365 scopus 로고    scopus 로고
    • Base excision repair and its role in maintaining genome stability
    • Baute J., Depicker A. Base excision repair and its role in maintaining genome stability. Crit. Rev. Biochem. Mol. Biol. 2008, 43:239-276.
    • (2008) Crit. Rev. Biochem. Mol. Biol. , vol.43 , pp. 239-276
    • Baute, J.1    Depicker, A.2
  • 7
    • 34250900982 scopus 로고    scopus 로고
    • Base-excision repair of oxidative DNA damage
    • David S.S., O'Shea V.L., Kundu S. Base-excision repair of oxidative DNA damage. Nature 2007, 447:941-950.
    • (2007) Nature , vol.447 , pp. 941-950
    • David, S.S.1    O'Shea, V.L.2    Kundu, S.3
  • 9
    • 38049112778 scopus 로고    scopus 로고
    • Early steps in the DNA base excision/single-strand interruption repair pathway in mammalian cells
    • Hegde M.L., Hazra T.K., Mitra S. Early steps in the DNA base excision/single-strand interruption repair pathway in mammalian cells. Cell Res. 2008, 18:27-47.
    • (2008) Cell Res. , vol.18 , pp. 27-47
    • Hegde, M.L.1    Hazra, T.K.2    Mitra, S.3
  • 11
    • 0035869014 scopus 로고    scopus 로고
    • Human DNA polymerase beta initiates DNA synthesis during long-patch repair of reduced AP sites in DNA
    • Podlutsky A.J., Dianova I.I., Podust V.N., Bohr V.A., Dianov G.L. Human DNA polymerase beta initiates DNA synthesis during long-patch repair of reduced AP sites in DNA. EMBO J. 2001, 20:1477-1482.
    • (2001) EMBO J. , vol.20 , pp. 1477-1482
    • Podlutsky, A.J.1    Dianova, I.I.2    Podust, V.N.3    Bohr, V.A.4    Dianov, G.L.5
  • 12
    • 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., Dogliotti E. Base damage and single-strand break repair: mechanisms and functional significance of short- and long-patch repair subpathways. DNA Repair 2007, 6:398-409.
    • (2007) DNA Repair , vol.6 , pp. 398-409
    • Fortini, P.1    Dogliotti, E.2
  • 15
    • 0030740948 scopus 로고    scopus 로고
    • Interaction of human apurinic endonuclease and DNA polymerase beta in the base excision repair pathway
    • Bennett R.A.O., Wilson D.M., Wong D., Demple B. Interaction of human apurinic endonuclease and DNA polymerase beta in the base excision repair pathway. Proc. Natl. Acad. Sci. U.S.A. 1997, 94:7166-7169.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 7166-7169
    • Bennett, R.A.O.1    Wilson, D.M.2    Wong, D.3    Demple, B.4
  • 16
    • 33847293432 scopus 로고    scopus 로고
    • Mechanism of interaction between human B-oxoguanine-DNA glycosylase and AP endonuclease
    • Sidorenko V.S., Nevinsky G.A., Zharkov D.O. Mechanism of interaction between human B-oxoguanine-DNA glycosylase and AP endonuclease. DNA Repair 2007, 6:317-328.
    • (2007) DNA Repair , vol.6 , pp. 317-328
    • Sidorenko, V.S.1    Nevinsky, G.A.2    Zharkov, D.O.3
  • 17
    • 0036324222 scopus 로고    scopus 로고
    • DNA repair in resistance to alkylating anticancer drugs
    • Kaina B., Christmann M. DNA repair in resistance to alkylating anticancer drugs. Int. J. Clin. Pharmacol. Ther. 2002, 40:354-367.
    • (2002) Int. J. Clin. Pharmacol. Ther. , vol.40 , pp. 354-367
    • Kaina, B.1    Christmann, M.2
  • 18
    • 0032412943 scopus 로고    scopus 로고
    • Mechanisms of resistance to alkylating agents
    • Damia G., D'Incalci M. Mechanisms of resistance to alkylating agents. Cytotechnology 1998, 27:165-173.
    • (1998) Cytotechnology , vol.27 , pp. 165-173
    • Damia, G.1    D'Incalci, M.2
  • 20
    • 22244448679 scopus 로고    scopus 로고
    • The role of base excision repair in the sensitivity and resistance to temozolomide-mediated cell death
    • Trivedi R.N., Almeida K.H., Fornsaglio J.L., Schamus S., Sobol R.W. The role of base excision repair in the sensitivity and resistance to temozolomide-mediated cell death. Cancer Res. 2005, 65:6394-6400.
    • (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
  • 22
    • 34548241809 scopus 로고    scopus 로고
    • Targeting base excision repair to improve cancer therapies
    • Sharma R.A., Dianov G.L. Targeting base excision repair to improve cancer therapies. Mol. Aspects Med. 2007, 28:345-374.
    • (2007) Mol. Aspects Med. , vol.28 , pp. 345-374
    • Sharma, R.A.1    Dianov, G.L.2
  • 23
    • 78149466586 scopus 로고    scopus 로고
    • Small molecule inhibitors of DNA repair nuclease activities of APE1
    • Wilson D.M., Simeonov A. Small molecule inhibitors of DNA repair nuclease activities of APE1. Cell. Mol. Life Sci. 2010, 67:3621-3631.
    • (2010) Cell. Mol. Life Sci. , vol.67 , pp. 3621-3631
    • Wilson, D.M.1    Simeonov, A.2
  • 24
    • 69849113681 scopus 로고    scopus 로고
    • Small-molecule inhibitors of proteins involved in base excision repair potentiate the anti-tumorigenic effect of existing chemotherapeutics and irradiation
    • Reed A.M., Fishel M.L., Kelley M.R. Small-molecule inhibitors of proteins involved in base excision repair potentiate the anti-tumorigenic effect of existing chemotherapeutics and irradiation. Future Oncol. 2009, 5:713-726.
    • (2009) Future Oncol. , vol.5 , pp. 713-726
    • Reed, A.M.1    Fishel, M.L.2    Kelley, M.R.3
  • 28
  • 29
    • 33847673066 scopus 로고    scopus 로고
    • Crosstalk of DNA glycosylases with pathways other than base excision repair
    • Kovtun I.V., McMurray C.T. Crosstalk of DNA glycosylases with pathways other than base excision repair. DNA Repair 2007, 6:517-529.
    • (2007) DNA Repair , vol.6 , pp. 517-529
    • Kovtun, I.V.1    McMurray, C.T.2
  • 31
    • 78149468904 scopus 로고    scopus 로고
    • Using synthetic DNA interstrand crosslinks to elucidate repair pathways and identify new therapeutic targets for cancer chemotherapy
    • Guainazzi A., Scharer O.D. Using synthetic DNA interstrand crosslinks to elucidate repair pathways and identify new therapeutic targets for cancer chemotherapy. Cell. Mol. Life Sci. 2010, 67:3683-3697.
    • (2010) Cell. Mol. Life Sci. , vol.67 , pp. 3683-3697
    • Guainazzi, A.1    Scharer, O.D.2
  • 33
    • 0242589403 scopus 로고
    • The fate of 8-methoxypsoralen photoinduced crosslinks in nuclear and mitochondrial yeast DNA - comparison of wild-type and repair-deficient strains
    • Maganaschwencke N., Henriques J.A.P., Chanet R., Moustacchi E. The fate of 8-methoxypsoralen photoinduced crosslinks in nuclear and mitochondrial yeast DNA - comparison of wild-type and repair-deficient strains. Proc. Nat. Acad. Sci. U.S.A. Biol. Sci. 1982, 79:1722-1726.
    • (1982) Proc. Nat. Acad. Sci. U.S.A. Biol. Sci. , vol.79 , pp. 1722-1726
    • Maganaschwencke, N.1    Henriques, J.A.P.2    Chanet, R.3    Moustacchi, E.4
  • 35
    • 77955860817 scopus 로고    scopus 로고
    • Strategies for DNA interstrand crosslink repair: insights from worms, flies, frogs, and slime molds
    • Mcvey M. Strategies for DNA interstrand crosslink repair: insights from worms, flies, frogs, and slime molds. Environ. Mol. Mutagen. 2010, 51:646-658.
    • (2010) Environ. Mol. Mutagen. , vol.51 , pp. 646-658
    • Mcvey, M.1
  • 36
    • 77955894128 scopus 로고    scopus 로고
    • Mutagenic repair of DNA interstrand crosslinks
    • Shen X., Li L. Mutagenic repair of DNA interstrand crosslinks. Environ. Mol. Mutagen. 2010, 51:493-499.
    • (2010) Environ. Mol. Mutagen. , vol.51 , pp. 493-499
    • Shen, X.1    Li, L.2
  • 37
    • 15744364715 scopus 로고    scopus 로고
    • Interstrand crosslink-induced homologous recombination carries an increased risk of deletions and insertions
    • Jonnalagadda V.S., Matsuguchi T., Engelward B.P. Interstrand crosslink-induced homologous recombination carries an increased risk of deletions and insertions. DNA Repair 2005, 4:594-605.
    • (2005) DNA Repair , vol.4 , pp. 594-605
    • Jonnalagadda, V.S.1    Matsuguchi, T.2    Engelward, B.P.3
  • 38
    • 12344282013 scopus 로고    scopus 로고
    • DNA interstrand crosslinks: natural and drug-induced DNA adducts that induce unique cellular responses
    • Scharer O.D. DNA interstrand crosslinks: natural and drug-induced DNA adducts that induce unique cellular responses. Chembiochem 2005, 6:27-32.
    • (2005) Chembiochem , vol.6 , pp. 27-32
    • Scharer, O.D.1
  • 39
    • 77955855049 scopus 로고    scopus 로고
    • Targeting and processing of site-specific DNA interstrand crosslinks
    • Vasquez K.M. Targeting and processing of site-specific DNA interstrand crosslinks. Environ. Mol. Mutagen. 2010, 51:527-539.
    • (2010) Environ. Mol. Mutagen. , vol.51 , pp. 527-539
    • Vasquez, K.M.1
  • 40
    • 0036255553 scopus 로고    scopus 로고
    • The role of DNA repair in nitrogen mustard drug resistance
    • Panasci L., Xu Z.Y., Bello V., Aloyz R. The role of DNA repair in nitrogen mustard drug resistance. Anticancer Drugs 2002, 13:211-220.
    • (2002) Anticancer Drugs , vol.13 , pp. 211-220
    • Panasci, L.1    Xu, Z.Y.2    Bello, V.3    Aloyz, R.4
  • 41
    • 34948880694 scopus 로고    scopus 로고
    • Enhanced repair of DNA interstrand crosslinking in ovarian cancer cells from patients following treatment with platinum-based chemotherapy
    • Wynne P., Newton C., Ledermann J., Olaitan A., Mould T.A., Hartley J.A. Enhanced repair of DNA interstrand crosslinking in ovarian cancer cells from patients following treatment with platinum-based chemotherapy. Br. J. Cancer 2007, 97:927-933.
    • (2007) Br. J. Cancer , vol.97 , pp. 927-933
    • Wynne, P.1    Newton, C.2    Ledermann, J.3    Olaitan, A.4    Mould, T.A.5    Hartley, J.A.6
  • 44
    • 77955876503 scopus 로고    scopus 로고
    • Mammalian nucleotide excision repair proteins and interstrand crosslink repair
    • Wood R.D. Mammalian nucleotide excision repair proteins and interstrand crosslink repair. Environ. Mol. Mutagen. 2010, 51:520-526.
    • (2010) Environ. Mol. Mutagen. , vol.51 , pp. 520-526
    • Wood, R.D.1
  • 45
    • 77955910902 scopus 로고    scopus 로고
    • Role of homologous recombination in DNA interstrand crosslink repair
    • Hinz J.M. Role of homologous recombination in DNA interstrand crosslink repair. Environ. Mol. Mutagen. 2010, 51:582-603.
    • (2010) Environ. Mol. Mutagen. , vol.51 , pp. 582-603
    • Hinz, J.M.1
  • 46
    • 77951889437 scopus 로고    scopus 로고
    • Initiation of DNA interstrand cross-link repair in mammalian cells
    • Hlavin E.M., Smeaton M.B., Miller P.S. Initiation of DNA interstrand cross-link repair in mammalian cells. Environ. Mol. Mutagen. 2010, 51:604-624.
    • (2010) Environ. Mol. Mutagen. , vol.51 , pp. 604-624
    • Hlavin, E.M.1    Smeaton, M.B.2    Miller, P.S.3
  • 48
    • 77955868586 scopus 로고    scopus 로고
    • Translesion DNA synthesis polymerases in DNA interstrand crosslink repair
    • Ho V., Scharer O.D. Translesion DNA synthesis polymerases in DNA interstrand crosslink repair. Environ. Mol. Mutagen. 2010, 51:552-566.
    • (2010) Environ. Mol. Mutagen. , vol.51 , pp. 552-566
    • Ho, V.1    Scharer, O.D.2
  • 50
    • 77951905220 scopus 로고    scopus 로고
    • Cross-link structure affects replication-independent DNA interstrand cross-link repair in mammalian cells
    • Hlavin E.M., Smeaton M.B., Noronha A.M., Wilds C.J., Miller P.S. Cross-link structure affects replication-independent DNA interstrand cross-link repair in mammalian cells. Biochemistry 2010, 49:3977-3988.
    • (2010) Biochemistry , vol.49 , pp. 3977-3988
    • Hlavin, E.M.1    Smeaton, M.B.2    Noronha, A.M.3    Wilds, C.J.4    Miller, P.S.5
  • 51
    • 77955869859 scopus 로고    scopus 로고
    • Repair of DNA interstrand cross-links during S phase of the mammalian cell cycle
    • Legerski R.J. Repair of DNA interstrand cross-links during S phase of the mammalian cell cycle. Environ. Mol. Mutagen. 2010, 51:540-551.
    • (2010) Environ. Mol. Mutagen. , vol.51 , pp. 540-551
    • Legerski, R.J.1
  • 52
    • 33344469882 scopus 로고    scopus 로고
    • Enhanced repair of DNA interstrand crosslinks in S phase
    • Mladenova V., Russev G. Enhanced repair of DNA interstrand crosslinks in S phase. FEBS Lett. 2006, 580:1631-1634.
    • (2006) FEBS Lett. , vol.580 , pp. 1631-1634
    • Mladenova, V.1    Russev, G.2
  • 54
    • 77955869918 scopus 로고    scopus 로고
    • DNA interstrand crosslinks: repair, cell signaling, and therapeutic implications
    • Vasquez K.M., Legerski R.J. DNA interstrand crosslinks: repair, cell signaling, and therapeutic implications. Environ. Mol. Mutagen. 2010, 51:491-492.
    • (2010) Environ. Mol. Mutagen. , vol.51 , pp. 491-492
    • Vasquez, K.M.1    Legerski, R.J.2
  • 55
    • 33645312939 scopus 로고    scopus 로고
    • DNA interstrand crosslink repair during G1 involves nucleotide excision repair and DNA polymerase zeta
    • Sarkar S., Davies A.A., Ulrich H.D., Mchugh P.J. DNA interstrand crosslink repair during G1 involves nucleotide excision repair and DNA polymerase zeta. EMBO J. 2006, 25:1285-1294.
    • (2006) EMBO J. , vol.25 , pp. 1285-1294
    • Sarkar, S.1    Davies, A.A.2    Ulrich, H.D.3    Mchugh, P.J.4
  • 56
    • 70350761663 scopus 로고    scopus 로고
    • Repair of laser-localized DNA interstrand cross-links in G(1) phase mammalian cells
    • Muniandy P.A., Thapa D., Thazhathveetil A.K., Liu S.T., Seidman M.M. Repair of laser-localized DNA interstrand cross-links in G(1) phase mammalian cells. J. Biol. Chem. 2009, 284:27908-27917.
    • (2009) J. Biol. Chem. , vol.284 , pp. 27908-27917
    • Muniandy, P.A.1    Thapa, D.2    Thazhathveetil, A.K.3    Liu, S.T.4    Seidman, M.M.5
  • 57
    • 33846696024 scopus 로고    scopus 로고
    • Chemosensitivity of primary human fibroblasts with defective unhooking of DNA interstrand cross-links
    • Clingen P.H., Arlett C.F., Hartley J.A., Parris C.N. Chemosensitivity of primary human fibroblasts with defective unhooking of DNA interstrand cross-links. Exp. Cell Res. 2007, 313:753-760.
    • (2007) Exp. Cell Res. , vol.313 , pp. 753-760
    • Clingen, P.H.1    Arlett, C.F.2    Hartley, J.A.3    Parris, C.N.4
  • 58
    • 62549114478 scopus 로고    scopus 로고
    • Fanconi anemia proteins, DNA interstrand crosslink repair pathways, and cancer therapy
    • Andreassen P.R., Ren K.Q. Fanconi anemia proteins, DNA interstrand crosslink repair pathways, and cancer therapy. Curr. Cancer Drug Targets 2009, 9:101-117.
    • (2009) Curr. Cancer Drug Targets , vol.9 , pp. 101-117
    • Andreassen, P.R.1    Ren, K.Q.2
  • 60
    • 33750206776 scopus 로고    scopus 로고
    • The structure-specific endonuclease Mus81-Eme1 promotes conversion of interstrand DNA crosslinks into double-strands breaks
    • Hanada K., Budzowska M., Modesti M., Maas A., Wyman C., Essers J., Kanaar R. The structure-specific endonuclease Mus81-Eme1 promotes conversion of interstrand DNA crosslinks into double-strands breaks. EMBO J. 2006, 25:4921-4932.
    • (2006) EMBO J. , vol.25 , pp. 4921-4932
    • Hanada, K.1    Budzowska, M.2    Modesti, M.3    Maas, A.4    Wyman, C.5    Essers, J.6    Kanaar, R.7
  • 61
    • 0034714401 scopus 로고    scopus 로고
    • Repair of an interstrand DNA cross-link initiated by ERCC1-XPF repair/recombination nuclease
    • Kuraoka I., Kobertz W.R., Ariza R.R., Biggerstaff M., Essigmann J.M., Wood R.D. Repair of an interstrand DNA cross-link initiated by ERCC1-XPF repair/recombination nuclease. J. Biol. Chem. 2000, 275:26632-26636.
    • (2000) J. Biol. Chem. , vol.275 , pp. 26632-26636
    • Kuraoka, I.1    Kobertz, W.R.2    Ariza, R.R.3    Biggerstaff, M.4    Essigmann, J.M.5    Wood, R.D.6
  • 62
    • 2642516304 scopus 로고    scopus 로고
    • Recombination repair pathway in the maintenance of chromosomal integrity against DNA interstrand crosslinks
    • Sasaki M.S., Takata M., Sonoda E., Tachibana A., Takeda S. Recombination repair pathway in the maintenance of chromosomal integrity against DNA interstrand crosslinks. Cytogenet. Genome Res. 2004, 104:28-34.
    • (2004) Cytogenet. Genome Res. , vol.104 , pp. 28-34
    • Sasaki, M.S.1    Takata, M.2    Sonoda, E.3    Tachibana, A.4    Takeda, S.5
  • 63
    • 33744927954 scopus 로고    scopus 로고
    • REV3 and REV1 play major roles in recombination-independent repair of DNA interstrand cross-links mediated by monoubiquitinated proliferating cell nuclear antigen (PCNA)
    • Shen X., Jun S., O'Neal L.E., Sonoda E., Bemark M., Sale J.E., Li L. REV3 and REV1 play major roles in recombination-independent repair of DNA interstrand cross-links mediated by monoubiquitinated proliferating cell nuclear antigen (PCNA). J. Biol. Chem. 2006, 281:13869-13872.
    • (2006) J. Biol. Chem. , vol.281 , pp. 13869-13872
    • Shen, X.1    Jun, S.2    O'Neal, L.E.3    Sonoda, E.4    Bemark, M.5    Sale, J.E.6    Li, L.7
  • 64
    • 0035132725 scopus 로고    scopus 로고
    • Involvement of nucleotide excision repair in a recombination-independent and error-prone pathway of DNA interstrand cross-link repair
    • Wang X., Peterson C.A., Zheng H.Y., Nairn R.S., Legerski R.J., Li L. Involvement of nucleotide excision repair in a recombination-independent and error-prone pathway of DNA interstrand cross-link repair. Mol. Cell. Biol. 2001, 21:713-720.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 713-720
    • Wang, X.1    Peterson, C.A.2    Zheng, H.Y.3    Nairn, R.S.4    Legerski, R.J.5    Li, L.6
  • 65
    • 0037223410 scopus 로고    scopus 로고
    • Nucleotide excision repair- and polymerase eta-mediated error-prone removal of mitomycin C interstrand cross-links
    • Zheng H.Y., Wang X., Warren A.J., Legerski R.J., Nairn R.S., Hamilton J.W., Li L. Nucleotide excision repair- and polymerase eta-mediated error-prone removal of mitomycin C interstrand cross-links. Mol. Cell. Biol. 2003, 23:754-761.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 754-761
    • Zheng, H.Y.1    Wang, X.2    Warren, A.J.3    Legerski, R.J.4    Nairn, R.S.5    Hamilton, J.W.6    Li, L.7
  • 66
    • 0027159566 scopus 로고
    • Covalent structure of A nitrogen mustard-induced DNA interstrand cross-link - An N7-to-N7 linkage of deoxyguanosine residues at the duplex sequence 5'-D(Gnc)
    • Rink S.M., Solomon M.S., Taylor M.J., Rajur S.B., Mclaughlin L.W., Hopkins P.B. Covalent structure of A nitrogen mustard-induced DNA interstrand cross-link - An N7-to-N7 linkage of deoxyguanosine residues at the duplex sequence 5'-D(Gnc). J. Am. Chem. Soc. 1993, 115:2551-2557.
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 2551-2557
    • Rink, S.M.1    Solomon, M.S.2    Taylor, M.J.3    Rajur, S.B.4    Mclaughlin, L.W.5    Hopkins, P.B.6
  • 67
    • 0026735585 scopus 로고
    • Structure of the DNA interstrand cross-link of 4,5',8-trimethylpsoralen
    • Kumaresan K.R., Ramaswamy M., Yeung A.T. Structure of the DNA interstrand cross-link of 4,5',8-trimethylpsoralen. Biochemistry 1992, 31:6774-6783.
    • (1992) Biochemistry , vol.31 , pp. 6774-6783
    • Kumaresan, K.R.1    Ramaswamy, M.2    Yeung, A.T.3
  • 68
    • 0029921138 scopus 로고    scopus 로고
    • An NMR study of [d(CGCGAATTCGCG)](2) containing an interstrand cross-link derived from a distamycin-pyrrole conjugate
    • Fagan P.A., Spielmann H.P., Sigurdsson S.T., Rink S.M., Hopkins P.B., Wemmer D.E. An NMR study of [d(CGCGAATTCGCG)](2) containing an interstrand cross-link derived from a distamycin-pyrrole conjugate. Nucleic Acids Res. 1996, 24:1566-1573.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 1566-1573
    • Fagan, P.A.1    Spielmann, H.P.2    Sigurdsson, S.T.3    Rink, S.M.4    Hopkins, P.B.5    Wemmer, D.E.6
  • 69
    • 0033560940 scopus 로고    scopus 로고
    • Crystal structure of a double-stranded DNA containing a cisplatin interstrand cross-link at 1.63angstrom resolution: hydration at the platinated site
    • Coste F., Malinge J.M., Serre L., Shepard W., Roth M., Leng M., Zelwer C. Crystal structure of a double-stranded DNA containing a cisplatin interstrand cross-link at 1.63angstrom resolution: hydration at the platinated site. Nucleic Acids Res. 1999, 27:1837-1846.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 1837-1846
    • Coste, F.1    Malinge, J.M.2    Serre, L.3    Shepard, W.4    Roth, M.5    Leng, M.6    Zelwer, C.7
  • 70
    • 0029585833 scopus 로고
    • Solution structure of A cisplatin-induced DNA interstrand cross-link
    • Huang H.F., Zhu L.M., Reid B.R., Drobny G.P., Hopkins P.B. Solution structure of A cisplatin-induced DNA interstrand cross-link. Science 1995, 270:1842-1845.
    • (1995) Science , vol.270 , pp. 1842-1845
    • Huang, H.F.1    Zhu, L.M.2    Reid, B.R.3    Drobny, G.P.4    Hopkins, P.B.5
  • 71
    • 33644626078 scopus 로고    scopus 로고
    • NMR structures of damaged DNA
    • Lukin M., de los Santos C. NMR structures of damaged DNA. Chem. Rev. 2006, 106:607-686.
    • (2006) Chem. Rev. , vol.106 , pp. 607-686
    • Lukin, M.1    de los Santos, C.2
  • 72
    • 38849181093 scopus 로고    scopus 로고
    • Unique properties of DNA interstrand cross-links of antitumor oxaliplatin and the effect of chirality of the carrier ligand
    • Kasparkova J., Vojtiskova M., Natile G., Brabec V. Unique properties of DNA interstrand cross-links of antitumor oxaliplatin and the effect of chirality of the carrier ligand. Chem. Eur. J. 2008, 14:1330-1341.
    • (2008) Chem. Eur. J. , vol.14 , pp. 1330-1341
    • Kasparkova, J.1    Vojtiskova, M.2    Natile, G.3    Brabec, V.4
  • 73
    • 0027485725 scopus 로고
    • DNA conformational change produced by the site-specific interstrand cross-link of trans-diamminedichloroplatinum(Ii)
    • Brabec V., Sip M., Leng M. DNA conformational change produced by the site-specific interstrand cross-link of trans-diamminedichloroplatinum(Ii). Biochemistry 1993, 32:11676-11681.
    • (1993) Biochemistry , vol.32 , pp. 11676-11681
    • Brabec, V.1    Sip, M.2    Leng, M.3
  • 75
    • 77952584412 scopus 로고    scopus 로고
    • A novel link to base excision repair?
    • Wilson D.M., Seidman M.M. A novel link to base excision repair?. Trends Biochem. Sci. 2010, 35:247-252.
    • (2010) Trends Biochem. Sci. , vol.35 , pp. 247-252
    • Wilson, D.M.1    Seidman, M.M.2
  • 76
    • 34948904826 scopus 로고    scopus 로고
    • Psoralen-induced DNA adducts are substrates for the base excision repair pathway in human cells
    • Couve-Privat S., Mace G., Rosselli F., Saparbaev M.K. Psoralen-induced DNA adducts are substrates for the base excision repair pathway in human cells. Nucleic Acids Res. 2007, 35:5672-5682.
    • (2007) Nucleic Acids Res. , vol.35 , pp. 5672-5682
    • Couve-Privat, S.1    Mace, G.2    Rosselli, F.3    Saparbaev, M.K.4
  • 78
    • 0032836651 scopus 로고    scopus 로고
    • Initiation of base excision repair: glycosylase mechanisms and structures
    • McCullough A.K., Dodson M.L., Lloyd R.S. Initiation of base excision repair: glycosylase mechanisms and structures. Annu. Rev. Biochem. 1999, 68:255-285.
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 255-285
    • McCullough, A.K.1    Dodson, M.L.2    Lloyd, R.S.3
  • 79
    • 0030041960 scopus 로고    scopus 로고
    • Repair-deficient 3-methyladenine DNA glycosylase homozygous mutant mouse cells have increased sensitivity to alkylation-induced chromosome damage and cell killing
    • Engelward B.P., Dreslin A., Christensen J., Huszar D., Kurahara C., Samson L. Repair-deficient 3-methyladenine DNA glycosylase homozygous mutant mouse cells have increased sensitivity to alkylation-induced chromosome damage and cell killing. EMBO J. 1996, 15:945-952.
    • (1996) EMBO J. , vol.15 , pp. 945-952
    • Engelward, B.P.1    Dreslin, A.2    Christensen, J.3    Huszar, D.4    Kurahara, C.5    Samson, L.6
  • 80
    • 0032170023 scopus 로고    scopus 로고
    • Mammalian 3-methyladenine DNA glycosylase protects against the toxicity and clastogenicity of certain chemotherapeutic DNA cross-linking agents
    • Allan J.M., Engelward B.P., Dreslin A.J., Wyatt M.D., Tomasz M., Samson L.D. Mammalian 3-methyladenine DNA glycosylase protects against the toxicity and clastogenicity of certain chemotherapeutic DNA cross-linking agents. Cancer Res. 1998, 58:3965-3973.
    • (1998) Cancer Res. , vol.58 , pp. 3965-3973
    • Allan, J.M.1    Engelward, B.P.2    Dreslin, A.J.3    Wyatt, M.D.4    Tomasz, M.5    Samson, L.D.6
  • 81
    • 46649113931 scopus 로고    scopus 로고
    • 3-methyladenine DNA glycosylase ill important for cellular resistance to psoralen interstrand cross-links
    • Maor-Shoshani A., Meira L.B., Yang X.M., Samson L.D. 3-methyladenine DNA glycosylase ill important for cellular resistance to psoralen interstrand cross-links. DNA Repair 2008, 7:1399-1406.
    • (2008) DNA Repair , vol.7 , pp. 1399-1406
    • Maor-Shoshani, A.1    Meira, L.B.2    Yang, X.M.3    Samson, L.D.4
  • 82
    • 0029936462 scopus 로고    scopus 로고
    • Excision of DNA adducts of nitrogen mustards by bacterial and mammalian 3-methyladenine-DNA glycosylases
    • Mattes W.B., Lee C.S., Laval J., OConnor T.R. Excision of DNA adducts of nitrogen mustards by bacterial and mammalian 3-methyladenine-DNA glycosylases. Carcinogenesis 1996, 17:643-648.
    • (1996) Carcinogenesis , vol.17 , pp. 643-648
    • Mattes, W.B.1    Lee, C.S.2    Laval, J.3    OConnor, T.R.4
  • 83
    • 0036468545 scopus 로고    scopus 로고
    • 3-methyladenine DNA glycosylase-deficient Aag null mice display unexpected bone marrow alkylation resistance
    • Roth R.B., Samson L.D. 3-methyladenine DNA glycosylase-deficient Aag null mice display unexpected bone marrow alkylation resistance. Cancer Res. 2002, 62:656-660.
    • (2002) Cancer Res. , vol.62 , pp. 656-660
    • Roth, R.B.1    Samson, L.D.2
  • 85
    • 28544446417 scopus 로고    scopus 로고
    • Sensitization of human carcinoma cells to alkylating agents by small interfering RNA suppression of 3-alkyladenine-DNA glycosylase
    • Paik J., Duncan T., Lindahl T., Sedgwick B. Sensitization of human carcinoma cells to alkylating agents by small interfering RNA suppression of 3-alkyladenine-DNA glycosylase. Cancer Res. 2005, 65:10472-10477.
    • (2005) Cancer Res. , vol.65 , pp. 10472-10477
    • Paik, J.1    Duncan, T.2    Lindahl, T.3    Sedgwick, B.4
  • 86
    • 77955901457 scopus 로고    scopus 로고
    • The Fanconi anemia pathway promotes DNA glycosylase-dependent excision of interstrand DNA crosslinks
    • Mace-Aime G., Couve S., Khassenov B., Rosselli F., Saparbaev M.K. The Fanconi anemia pathway promotes DNA glycosylase-dependent excision of interstrand DNA crosslinks. Environ. Mol. Mutagen. 2010, 51:508-519.
    • (2010) Environ. Mol. Mutagen. , vol.51 , pp. 508-519
    • Mace-Aime, G.1    Couve, S.2    Khassenov, B.3    Rosselli, F.4    Saparbaev, M.K.5
  • 87
    • 34250338508 scopus 로고    scopus 로고
    • Real-time monitoring of uracil removal by uracil-DNA glycosylase using fluorescent resonance energy transfer probes
    • Liu B., Yang X.H., Wang K.M., Tan W.H., Li H.M., Tang H.X. Real-time monitoring of uracil removal by uracil-DNA glycosylase using fluorescent resonance energy transfer probes. Anal. Biochem. 2007, 366:237-243.
    • (2007) Anal. Biochem. , vol.366 , pp. 237-243
    • Liu, B.1    Yang, X.H.2    Wang, K.M.3    Tan, W.H.4    Li, H.M.5    Tang, H.X.6
  • 88
    • 41349108483 scopus 로고    scopus 로고
    • The human endonuclease III enzyme is a relevant target to potentiate cisplatin cytotoxicity in Y-box-binding protein-1 overexpressing tumor cells
    • Guay D., Garand C., Reddy S., Schmutte C., Lebel M. The human endonuclease III enzyme is a relevant target to potentiate cisplatin cytotoxicity in Y-box-binding protein-1 overexpressing tumor cells. Cancer Sci. 2008, 99:762-769.
    • (2008) Cancer Sci. , vol.99 , pp. 762-769
    • Guay, D.1    Garand, C.2    Reddy, S.3    Schmutte, C.4    Lebel, M.5
  • 90
    • 0032782907 scopus 로고    scopus 로고
    • Overexpression of cDNA encoding FANCC, SPHAR, MPG, SNM1 or HA 3611 does not render CHO cells more resistant to DNA crosslinking agents
    • Grombacher T., Tomicic M., Digweed M., Kaina B. Overexpression of cDNA encoding FANCC, SPHAR, MPG, SNM1 or HA 3611 does not render CHO cells more resistant to DNA crosslinking agents. Anticancer Res. 1999, 19:1729-1735.
    • (1999) Anticancer Res. , vol.19 , pp. 1729-1735
    • Grombacher, T.1    Tomicic, M.2    Digweed, M.3    Kaina, B.4
  • 91
    • 20144386176 scopus 로고    scopus 로고
    • N-methylpurine DNA glycosylase overexpression increases alkylation sensitivity by rapidly removing non-toxic 7-methylguanine adducts
    • Rinne M.L., He Y., Pachkowski B.F., Nakamura J., Kelley M.R. N-methylpurine DNA glycosylase overexpression increases alkylation sensitivity by rapidly removing non-toxic 7-methylguanine adducts. Nucleic Acids Res. 2005, 33:2859-2867.
    • (2005) Nucleic Acids Res. , vol.33 , pp. 2859-2867
    • Rinne, M.L.1    He, Y.2    Pachkowski, B.F.3    Nakamura, J.4    Kelley, M.R.5
  • 92
    • 77955095659 scopus 로고    scopus 로고
    • Human AP endonuclease 1 (APE1): from mechanistic insights to druggable target in cancer
    • Abbotts R., Madhusudan S. Human AP endonuclease 1 (APE1): from mechanistic insights to druggable target in cancer. Cancer Treat. Rev. 2010, 36:425-435.
    • (2010) Cancer Treat. Rev. , vol.36 , pp. 425-435
    • Abbotts, R.1    Madhusudan, S.2
  • 94
    • 0035176178 scopus 로고    scopus 로고
    • Apurinic/apyrimidinic endonuclease activity is elevated in human adult gliomas
    • Bobola M.S., Blank A., Berger M.S., Stevens B.A., Silber J.R. Apurinic/apyrimidinic endonuclease activity is elevated in human adult gliomas. Clin. Cancer Res. 2001, 7:3510-3518.
    • (2001) Clin. Cancer Res. , vol.7 , pp. 3510-3518
    • Bobola, M.S.1    Blank, A.2    Berger, M.S.3    Stevens, B.A.4    Silber, J.R.5
  • 95
    • 0036718792 scopus 로고    scopus 로고
    • The apurinic/apyrimidinic endonuclease activity of Apel/Ref-1 contributes to human glioma cell resistance to alkylating agents and is elevated by oxidative stress
    • Silber J.R., Bobola M.S., Blank A., Schoeler K.D., Haroldson P.D., Huynh M.B., Kolstoe D.D. The apurinic/apyrimidinic endonuclease activity of Apel/Ref-1 contributes to human glioma cell resistance to alkylating agents and is elevated by oxidative stress. Clin. Cancer Res. 2002, 8:3008-3018.
    • (2002) Clin. Cancer Res. , vol.8 , pp. 3008-3018
    • Silber, J.R.1    Bobola, M.S.2    Blank, A.3    Schoeler, K.D.4    Haroldson, P.D.5    Huynh, M.B.6    Kolstoe, D.D.7
  • 96
    • 85013697088 scopus 로고    scopus 로고
    • The apurinic/apyrimidinic endonuclease activity of Apel/Ref-1 contributes to human glioma cell resistance to alkylating agents and is elevated by oxidative stress
    • Silber J.R., Bobola M.S., Blank A., Schoeler K.D., Haroldson P.D., Huynh M.B., Kolstoe D.D. The apurinic/apyrimidinic endonuclease activity of Apel/Ref-1 contributes to human glioma cell resistance to alkylating agents and is elevated by oxidative stress. Clin. Cancer Res. 2003, 9:2877.
    • (2003) Clin. Cancer Res. , vol.9 , pp. 2877
    • Silber, J.R.1    Bobola, M.S.2    Blank, A.3    Schoeler, K.D.4    Haroldson, P.D.5    Huynh, M.B.6    Kolstoe, D.D.7
  • 97
    • 0034905642 scopus 로고    scopus 로고
    • Elevated and altered expression of the multifunctional DNA base excision repair and redox enzyme Ape1/ref-1 in prostate cancer
    • Kelley M.R., Cheng L., Foster R., Tritt R., Jiang J.Z., Broshears J., Koch M. Elevated and altered expression of the multifunctional DNA base excision repair and redox enzyme Ape1/ref-1 in prostate cancer. Clin. Cancer Res. 2001, 7:824-830.
    • (2001) Clin. Cancer Res. , vol.7 , pp. 824-830
    • Kelley, M.R.1    Cheng, L.2    Foster, R.3    Tritt, R.4    Jiang, J.Z.5    Broshears, J.6    Koch, M.7
  • 101
    • 70350622182 scopus 로고    scopus 로고
    • APE1 overexpression is associated with cisplatin resistance in non-small cell lung cancer and targeted inhibition of APE1 enhances the activity of cisplatin in A549 cells
    • Wang D., Xiang D.B., Yang X.Q., Chen L.S., Li M.X., Zhong Z.Y., Zhang Y.S. APE1 overexpression is associated with cisplatin resistance in non-small cell lung cancer and targeted inhibition of APE1 enhances the activity of cisplatin in A549 cells. Lung Cancer 2009, 66:298-304.
    • (2009) Lung Cancer , vol.66 , pp. 298-304
    • Wang, D.1    Xiang, D.B.2    Yang, X.Q.3    Chen, L.S.4    Li, M.X.5    Zhong, Z.Y.6    Zhang, Y.S.7
  • 102
    • 0142219356 scopus 로고    scopus 로고
    • Studies of apurinic/apyrimidinic endonuclease/ref-1 expression in epithelial ovarian cancer: correlations with tumor progression and platinum resistance
    • Freitas S., Moore D.H., Michael H., Kelley M.R. Studies of apurinic/apyrimidinic endonuclease/ref-1 expression in epithelial ovarian cancer: correlations with tumor progression and platinum resistance. Clin. Cancer Res. 2003, 9:4689-4694.
    • (2003) Clin. Cancer Res. , vol.9 , pp. 4689-4694
    • Freitas, S.1    Moore, D.H.2    Michael, H.3    Kelley, M.R.4
  • 103
    • 30344434348 scopus 로고    scopus 로고
    • Alterations in the expression of the apurinic/apyrimidinic endonuclease-1/redox factor-1 (APE/Ref-1) in human melanoma and identification of the therapeutic potential of resveratrol as an APE/Ref-1 inhibitor
    • Yang S., Irani K., Heffron S.E., Jurnak F., Meyskens F.L. Alterations in the expression of the apurinic/apyrimidinic endonuclease-1/redox factor-1 (APE/Ref-1) in human melanoma and identification of the therapeutic potential of resveratrol as an APE/Ref-1 inhibitor. Mol. Cancer Ther. 2005, 4:1923-1935.
    • (2005) Mol. Cancer Ther. , vol.4 , pp. 1923-1935
    • Yang, S.1    Irani, K.2    Heffron, S.E.3    Jurnak, F.4    Meyskens, F.L.5
  • 104
    • 0028596574 scopus 로고
    • A role for the human DNA-repair enzyme Hap1 in cellular-protection against DNA-damaging agents and hypoxic stress
    • Walker L.J., Craig R.B., Harris A.L., Hickson I.D. A role for the human DNA-repair enzyme Hap1 in cellular-protection against DNA-damaging agents and hypoxic stress. Nucleic Acids Res. 1994, 22:4884-4889.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4884-4889
    • Walker, L.J.1    Craig, R.B.2    Harris, A.L.3    Hickson, I.D.4
  • 105
    • 67649580307 scopus 로고    scopus 로고
    • Impairment of APE1 function enhances cellular sensitivity to clinically relevant alkylators and antimetabolites
    • McNeill D.R., Lam W., DeWeese T.L., Cheng Y.C., Wilson D.M. Impairment of APE1 function enhances cellular sensitivity to clinically relevant alkylators and antimetabolites. Mol. Cancer Res. 2009, 7:897-906.
    • (2009) Mol. Cancer Res. , vol.7 , pp. 897-906
    • McNeill, D.R.1    Lam, W.2    DeWeese, T.L.3    Cheng, Y.C.4    Wilson, D.M.5
  • 106
    • 33846976720 scopus 로고    scopus 로고
    • A dominant-negative form of the major human abasic endonuclease enhances cellular sensitivity to laboratory and clinical DNA-damaging agents
    • McNeill D.R., Wilson D.M. A dominant-negative form of the major human abasic endonuclease enhances cellular sensitivity to laboratory and clinical DNA-damaging agents. Mol. Cancer Res. 2007, 5:61-70.
    • (2007) Mol. Cancer Res. , vol.5 , pp. 61-70
    • McNeill, D.R.1    Wilson, D.M.2
  • 107
    • 2442684173 scopus 로고    scopus 로고
    • Blockage of abasic site repair enhances antitumor efficacy of 1,3-bis-(2-chloroethyl)-1-nitrosourea in colon tumor xenografts
    • Liu L.L., Yan L., Donze J.R., Gerson S.L. Blockage of abasic site repair enhances antitumor efficacy of 1,3-bis-(2-chloroethyl)-1-nitrosourea in colon tumor xenografts. Mol. Cancer Ther. 2003, 2:1061-1066.
    • (2003) Mol. Cancer Ther. , vol.2 , pp. 1061-1066
    • Liu, L.L.1    Yan, L.2    Donze, J.R.3    Gerson, S.L.4
  • 108
    • 0033961301 scopus 로고    scopus 로고
    • Alterations in the expression of the DNA repair/redox enzyme APE/ref-1 in epithelial ovarian cancers
    • Moore D.H., Michael H., Tritt R., Parsons S.H., Kelley M.R. Alterations in the expression of the DNA repair/redox enzyme APE/ref-1 in epithelial ovarian cancers. Clin. Cancer Res. 2000, 6:602-609.
    • (2000) Clin. Cancer Res. , vol.6 , pp. 602-609
    • Moore, D.H.1    Michael, H.2    Tritt, R.3    Parsons, S.H.4    Kelley, M.R.5
  • 109
    • 0031439376 scopus 로고    scopus 로고
    • The apurinic/apyrimidinic endonuclease (APE/ref-1) DNA repair enzyme is elevated in premalignant and malignant cervical cancer
    • Xu Y., Moore D.H., Broshears J., Liu L.F., Wilson T.M., Kelley M.R. The apurinic/apyrimidinic endonuclease (APE/ref-1) DNA repair enzyme is elevated in premalignant and malignant cervical cancer. Anticancer Res. 1997, 17:3713-3719.
    • (1997) Anticancer Res. , vol.17 , pp. 3713-3719
    • Xu, Y.1    Moore, D.H.2    Broshears, J.3    Liu, L.F.4    Wilson, T.M.5    Kelley, M.R.6
  • 110
    • 4444327784 scopus 로고    scopus 로고
    • Human apurinic endonuclease 1 (APE1) expression and prognostic significance in osteosarcoma: enhanced sensitivity of osteosarcoma to DNA damaging agents using silencing RNA APE1 expression inhibition
    • Wang D., Luo M.H., Kelley M.R. Human apurinic endonuclease 1 (APE1) expression and prognostic significance in osteosarcoma: enhanced sensitivity of osteosarcoma to DNA damaging agents using silencing RNA APE1 expression inhibition. Mol. Cancer Ther. 2004, 3:679-686.
    • (2004) Mol. Cancer Ther. , vol.3 , pp. 679-686
    • Wang, D.1    Luo, M.H.2    Kelley, M.R.3
  • 111
    • 0037049975 scopus 로고    scopus 로고
    • Alternative nucleotide incision repair pathway for oxidative DNA damage
    • Ischenko A.A., Saparbaev M.K. Alternative nucleotide incision repair pathway for oxidative DNA damage. Nature 2002, 415:183-187.
    • (2002) Nature , vol.415 , pp. 183-187
    • Ischenko, A.A.1    Saparbaev, M.K.2
  • 112
    • 66449134321 scopus 로고    scopus 로고
    • The human oxidative DNA glycosylase NEIL1 excises psoralen-induced interstrand DNA cross-links in a three-stranded DNA structure
    • Couve S., Mace-Aime G., Rosselli F., Saparbaev M.K. The human oxidative DNA glycosylase NEIL1 excises psoralen-induced interstrand DNA cross-links in a three-stranded DNA structure. J. Biol. Chem. 2009, 284:11963-11970.
    • (2009) J. Biol. Chem. , vol.284 , pp. 11963-11970
    • Couve, S.1    Mace-Aime, G.2    Rosselli, F.3    Saparbaev, M.K.4
  • 114
    • 69249161787 scopus 로고    scopus 로고
    • FEN1 is overexpressed in testis, lung and brain tumors
    • Nikolova T., Christmann M., Kaina B. FEN1 is overexpressed in testis, lung and brain tumors. Anticancer Res. 2009, 29:2453-2459.
    • (2009) Anticancer Res. , vol.29 , pp. 2453-2459
    • Nikolova, T.1    Christmann, M.2    Kaina, B.3
  • 116
    • 0034053776 scopus 로고    scopus 로고
    • Repair of intermediate structures produced at DNA interstrand cross-links in Saccharomyces cerevisiae
    • Mchugh P.J., Sones W.R., Hartley J.A. Repair of intermediate structures produced at DNA interstrand cross-links in Saccharomyces cerevisiae. Mol. Cell. Biol. 2000, 20:3425-3433.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 3425-3433
    • Mchugh, P.J.1    Sones, W.R.2    Hartley, J.A.3
  • 117
    • 0242551649 scopus 로고    scopus 로고
    • Increased expression and no mutation of the Flap endonuclease (FEN1) gene in human lung cancer
    • Sato M., Girard L., Sekine I., Sunaga N., Ramirez R.D., Kamibayashi C., Minna J.D. Increased expression and no mutation of the Flap endonuclease (FEN1) gene in human lung cancer. Oncogene 2003, 22:7243-7246.
    • (2003) Oncogene , vol.22 , pp. 7243-7246
    • Sato, M.1    Girard, L.2    Sekine, I.3    Sunaga, N.4    Ramirez, R.D.5    Kamibayashi, C.6    Minna, J.D.7
  • 121
    • 0042470700 scopus 로고    scopus 로고
    • Nuclease-deficient FEN-1 blocks rad51/BRCA1-mediated repair and causes trinucleotide repeat instability
    • Spiro C., McMurray C.T. Nuclease-deficient FEN-1 blocks rad51/BRCA1-mediated repair and causes trinucleotide repeat instability. Mol. Cell. Biol. 2003, 23:6063-6074.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 6063-6074
    • Spiro, C.1    McMurray, C.T.2
  • 123
    • 0742288051 scopus 로고    scopus 로고
    • WRN helicase and FEN-1 form a complex upon replication arrest and together process branch-migrating DNA structures associated with the replication fork
    • Sharma S., Otterlei M., Sommers J.A., Driscoll H.C., Dianov G.L., Kao H.I., Bambara R.A., Brosh R.M. WRN helicase and FEN-1 form a complex upon replication arrest and together process branch-migrating DNA structures associated with the replication fork. Mol. Biol. Cell 2004, 15:734-750.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 734-750
    • Sharma, S.1    Otterlei, M.2    Sommers, J.A.3    Driscoll, H.C.4    Dianov, G.L.5    Kao, H.I.6    Bambara, R.A.7    Brosh, R.M.8
  • 125
    • 0029909482 scopus 로고    scopus 로고
    • Mechanism of tracking and cleavage of adduct-damaged DNA substrates by the mammalian 5'- to 3'-exonuclease endonuclease RAD2 homologue 1 or flap endonuclease 1
    • Barnes C.J., Wahl A.F., Shen B.H., Park M.S., Bambara R.A. Mechanism of tracking and cleavage of adduct-damaged DNA substrates by the mammalian 5'- to 3'-exonuclease endonuclease RAD2 homologue 1 or flap endonuclease 1. J. Biol. Chem. 1996, 271:29624-29631.
    • (1996) J. Biol. Chem. , vol.271 , pp. 29624-29631
    • Barnes, C.J.1    Wahl, A.F.2    Shen, B.H.3    Park, M.S.4    Bambara, R.A.5
  • 126
    • 77949571124 scopus 로고    scopus 로고
    • DNA polymerase family X: function, structure, and cellular roles
    • Yamtich J., Sweasy J.B. DNA polymerase family X: function, structure, and cellular roles. Biochim. Biophys. Acta Proteins Proteomics 2010, 1804:1136-1150.
    • (2010) Biochim. Biophys. Acta Proteins Proteomics , vol.1804 , pp. 1136-1150
    • Yamtich, J.1    Sweasy, J.B.2
  • 128
    • 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 S.L., Dianova I.I., Dianov G.L. DNA polymerase beta is the major dRP lyase involved in repair of oxidative base lesions in DNA by mammalian cell extracts. EMBO J. 2001, 20:6919-6926.
    • (2001) EMBO J. , vol.20 , pp. 6919-6926
    • Allinson, S.L.1    Dianova, I.I.2    Dianov, G.L.3
  • 129
    • 0345620782 scopus 로고    scopus 로고
    • Overexpression of DNA polymerase beta: a genomic instability enhancer process
    • Canitrot Y., Frechet M., Servant L., Cazaux C., Hoffmann J.B. Overexpression of DNA polymerase beta: a genomic instability enhancer process. FASEB J. 1999, 13:1107-1111.
    • (1999) FASEB J. , vol.13 , pp. 1107-1111
    • Canitrot, Y.1    Frechet, M.2    Servant, L.3    Cazaux, C.4    Hoffmann, J.B.5
  • 130
    • 0032987099 scopus 로고    scopus 로고
    • DNA polymerase beta expression differences in selected human tumors and cell lines
    • Srivastava D.K., Husain I., Arteaga C.L., Wilson S.H. DNA polymerase beta expression differences in selected human tumors and cell lines. Carcinogenesis 1999, 20:1049-1054.
    • (1999) Carcinogenesis , vol.20 , pp. 1049-1054
    • Srivastava, D.K.1    Husain, I.2    Arteaga, C.L.3    Wilson, S.H.4
  • 131
    • 16244375578 scopus 로고    scopus 로고
    • The overexpression of specialized DNA polymerases in cancer
    • Albertella M.R., Lau A., O'Connor M.J. The overexpression of specialized DNA polymerases in cancer. DNA Repair 2005, 4:583-593.
    • (2005) DNA Repair , vol.4 , pp. 583-593
    • Albertella, M.R.1    Lau, A.2    O'Connor, M.J.3
  • 133
    • 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.M., Dalal S., Chikova A., DiMaio D., Sweasy J.B. The E295K DNA polymerase beta gastric cancer-associated variant interferes with base excision repair and induces cellular transformation. Mol. Cell. Biol. 2007, 27:5587-5596.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 5587-5596
    • Lang, T.M.1    Dalal, S.2    Chikova, A.3    DiMaio, D.4    Sweasy, J.B.5
  • 134
    • 84877928103 scopus 로고    scopus 로고
    • A gastric cancer variant of DNA polymerase beta induces cellular transformation by a mutational mechanism
    • Sweasy J.B., Dalal S., Lang T. A gastric cancer variant of DNA polymerase beta induces cellular transformation by a mutational mechanism. Environ. Mol. Mutagen. 2006, 47:415.
    • (2006) Environ. Mol. Mutagen. , vol.47 , pp. 415
    • Sweasy, J.B.1    Dalal, S.2    Lang, T.3
  • 135
    • 26444605433 scopus 로고    scopus 로고
    • Expression of DNA polymerase beta cancer-associated variants in mouse cells results in cellular transformation
    • Sweasy J.B., Lang T., Starcevic D., Sunt K.W., Lai C.C., DiMaio D., Dalal S. Expression of DNA polymerase beta cancer-associated variants in mouse cells results in cellular transformation. Proc. Natl. Acad. Sci. U.S.A. 2005, 102:14350-14355.
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 14350-14355
    • Sweasy, J.B.1    Lang, T.2    Starcevic, D.3    Sunt, K.W.4    Lai, C.C.5    DiMaio, D.6    Dalal, S.7
  • 136
    • 0034903413 scopus 로고    scopus 로고
    • The response of human breast tumour cell lines with altered polymerase beta levels to cisplatin and radiation
    • Raaphorst G.P., Cybulski S.E., Sobol R., Ng C.E. The response of human breast tumour cell lines with altered polymerase beta levels to cisplatin and radiation. Anticancer Res. 2001, 21:2079-2083.
    • (2001) Anticancer Res. , vol.21 , pp. 2079-2083
    • Raaphorst, G.P.1    Cybulski, S.E.2    Sobol, R.3    Ng, C.E.4
  • 138
    • 0033118432 scopus 로고    scopus 로고
    • Cells deficient in DNA polymerase beta are hypersensitive to alkylating agent-induced apoptosis and chromosomal breakage
    • Ochs K., Sobol R.W., Wilson S.H., Kaina B. Cells deficient in DNA polymerase beta are hypersensitive to alkylating agent-induced apoptosis and chromosomal breakage. Cancer Res. 1999, 59:1544-1551.
    • (1999) Cancer Res. , vol.59 , pp. 1544-1551
    • Ochs, K.1    Sobol, R.W.2    Wilson, S.H.3    Kaina, B.4
  • 140
    • 0036150143 scopus 로고    scopus 로고
    • Comparison of response to radiation, hyperthermia and cisplatin in parental and polymerase beta knockout cells
    • Raaphorst G.P., Ng C.E., Yang D.P. Comparison of response to radiation, hyperthermia and cisplatin in parental and polymerase beta knockout cells. Int. J. Hyperthermia 2002, 18:33-39.
    • (2002) Int. J. Hyperthermia , vol.18 , pp. 33-39
    • Raaphorst, G.P.1    Ng, C.E.2    Yang, D.P.3
  • 141
    • 0037193540 scopus 로고    scopus 로고
    • Involvement of DNA polymerase beta in protection against the cytotoxicity of oxidative DNA damage
    • Horton J.K., Baker A., Vande Berg B.J., Sobol R.W., Wilson S.H. Involvement of DNA polymerase beta in protection against the cytotoxicity of oxidative DNA damage. DNA Repair 2002, 1:317-333.
    • (2002) DNA Repair , vol.1 , pp. 317-333
    • Horton, J.K.1    Baker, A.2    Vande Berg, B.J.3    Sobol, R.W.4    Wilson, S.H.5
  • 142
    • 0028819767 scopus 로고
    • Strategic down-regulation of DNA Polymerase beta by antisense RNA sensitizes mammalian cells to specific DNA damaging agents
    • Horton J.K., Srivastava D.K., Zmudzka B.Z., Wilson S.H. Strategic down-regulation of DNA Polymerase beta by antisense RNA sensitizes mammalian cells to specific DNA damaging agents. Nucleic Acids Res. 1995, 23:3810-3815.
    • (1995) Nucleic Acids Res. , vol.23 , pp. 3810-3815
    • Horton, J.K.1    Srivastava, D.K.2    Zmudzka, B.Z.3    Wilson, S.H.4
  • 144
    • 0034681190 scopus 로고    scopus 로고
    • Translesion replication by DNA polymerase delta depends on processivity accessory proteins and differs in specificity from DNA polymerase beta
    • Daube S.S., Tomer G., Livneh Z. Translesion replication by DNA polymerase delta depends on processivity accessory proteins and differs in specificity from DNA polymerase beta. Biochemistry 2000, 39:348-355.
    • (2000) Biochemistry , vol.39 , pp. 348-355
    • Daube, S.S.1    Tomer, G.2    Livneh, Z.3
  • 145
    • 0036682979 scopus 로고    scopus 로고
    • Translesion DNA synthesis in eukaryotes: a one- or two-polymerase affair
    • Prakash S., Prakash L. Translesion DNA synthesis in eukaryotes: a one- or two-polymerase affair. Genes Dev. 2002, 16:1872-1883.
    • (2002) Genes Dev. , vol.16 , pp. 1872-1883
    • Prakash, S.1    Prakash, L.2
  • 146
    • 0029851151 scopus 로고    scopus 로고
    • Aphidicolin markedly increases the platinum sensitivity of cells from primary ovarian tumours
    • Sargent J.M., Elgie A.W., Williamson C.J., Taylor C.G. Aphidicolin markedly increases the platinum sensitivity of cells from primary ovarian tumours. Br. J. Cancer 1996, 74:1730-1733.
    • (1996) Br. J. Cancer , vol.74 , pp. 1730-1733
    • Sargent, J.M.1    Elgie, A.W.2    Williamson, C.J.3    Taylor, C.G.4
  • 147
    • 0027958095 scopus 로고
    • Antitumor-activity and biochemical effects of aphidicolin glycinate (Nsc-303812) alone and in combination with cisplatin in-vivo
    • Odwyer P.J., Moyer J.D., Suffness M., Harrison S.D., Cysyk R., Hamilton T.C., Plowman J. Antitumor-activity and biochemical effects of aphidicolin glycinate (Nsc-303812) alone and in combination with cisplatin in-vivo. Cancer Res. 1994, 54:724-729.
    • (1994) Cancer Res. , vol.54 , pp. 724-729
    • Odwyer, P.J.1    Moyer, J.D.2    Suffness, M.3    Harrison, S.D.4    Cysyk, R.5    Hamilton, T.C.6    Plowman, J.7
  • 148
    • 0026722362 scopus 로고
    • Activity of aphidicolin glycinate alone or in combination with cisplatin in A murine ovarian tumor resistant to cisplatin
    • Damia G., Tagliabue G., Zucchetti M., Davoli E., Sessa C., Cavalli F., Dincalci M. Activity of aphidicolin glycinate alone or in combination with cisplatin in A murine ovarian tumor resistant to cisplatin. Cancer Chemother. Pharmacol. 1992, 30:459-464.
    • (1992) Cancer Chemother. Pharmacol. , vol.30 , pp. 459-464
    • Damia, G.1    Tagliabue, G.2    Zucchetti, M.3    Davoli, E.4    Sessa, C.5    Cavalli, F.6    Dincalci, M.7
  • 149
    • 0028939389 scopus 로고
    • Modulation of resistance to cisplatin by amphotericin-B and aphidicolin in human larynx-carcinoma cells
    • Beketicoreskovic L., Osmak M. Modulation of resistance to cisplatin by amphotericin-B and aphidicolin in human larynx-carcinoma cells. Cancer Chemother. Pharmacol. 1995, 35:327-333.
    • (1995) Cancer Chemother. Pharmacol. , vol.35 , pp. 327-333
    • Beketicoreskovic, L.1    Osmak, M.2
  • 150
    • 5344270493 scopus 로고    scopus 로고
    • Enhancement of genotoxic effects in the comet assay with human blood samples by aphidicolin
    • Speit G., Schutz P., Hoffmann H. Enhancement of genotoxic effects in the comet assay with human blood samples by aphidicolin. Toxicol. Lett. 2004, 153:303-310.
    • (2004) Toxicol. Lett. , vol.153 , pp. 303-310
    • Speit, G.1    Schutz, P.2    Hoffmann, H.3
  • 151
    • 0042235200 scopus 로고    scopus 로고
    • Partial reconstitution of human interstrand cross-link repair in vitro: characterization of the roles of RPA and PCNA
    • Zhang N.X., Lu X.Y., Legerski R.J. Partial reconstitution of human interstrand cross-link repair in vitro: characterization of the roles of RPA and PCNA. Biochem. Biophys. Res. Commun. 2003, 309:71-78.
    • (2003) Biochem. Biophys. Res. Commun. , vol.309 , pp. 71-78
    • Zhang, N.X.1    Lu, X.Y.2    Legerski, R.J.3
  • 152
    • 4344567395 scopus 로고    scopus 로고
    • XPD and XRCC1 genetic polymorphisms are prognostic factors in advanced non-small-cell lung cancer patients treated with platinum chemotherapy
    • Gurubhagavatula S., Liu G., Park S., Zhou W., Su L., Wain J.C., Lynch T.J., Neuberg D.S., Christiani D.C. XPD and XRCC1 genetic polymorphisms are prognostic factors in advanced non-small-cell lung cancer patients treated with platinum chemotherapy. J. Clin. Oncol. 2004, 22:2594-2601.
    • (2004) J. Clin. Oncol. , vol.22 , pp. 2594-2601
    • Gurubhagavatula, S.1    Liu, G.2    Park, S.3    Zhou, W.4    Su, L.5    Wain, J.C.6    Lynch, T.J.7    Neuberg, D.S.8    Christiani, D.C.9
  • 154
    • 26844514889 scopus 로고    scopus 로고
    • ABCC5, ERCC2, XPA and XRCC1 transcript abundance levels correlate with cisplatin chemoresistance in non-small cell lung cancer cell lines
    • Weaver D.A., Crawford E.L., Warner K.A., Elkhairi F., Khuder S.A., Willey J.C. ABCC5, ERCC2, XPA and XRCC1 transcript abundance levels correlate with cisplatin chemoresistance in non-small cell lung cancer cell lines. Mol. Cancer 2005, 4.
    • (2005) Mol. Cancer , vol.4
    • Weaver, D.A.1    Crawford, E.L.2    Warner, K.A.3    Elkhairi, F.4    Khuder, S.A.5    Willey, J.C.6
  • 155
    • 73749084430 scopus 로고    scopus 로고
    • Increase the cisplatin cytotoxicity and cisplatin-induced DNA damage in HepG2 cells by XRCC1 abrogation related mechanisms
    • Zhang R., Niu Y.J., Zhou Y.K. Increase the cisplatin cytotoxicity and cisplatin-induced DNA damage in HepG2 cells by XRCC1 abrogation related mechanisms. Toxicol. Lett. 2010, 192:108-114.
    • (2010) Toxicol. Lett. , vol.192 , pp. 108-114
    • Zhang, R.1    Niu, Y.J.2    Zhou, Y.K.3
  • 157
    • 66649137114 scopus 로고    scopus 로고
    • Photoaffinity Labeling Reveals Nuclear Proteins That Uniquely Recognize Cisplatin-DNA Interstrand Cross-Links
    • Zhu G.Y., Lippard S.J. Photoaffinity Labeling Reveals Nuclear Proteins That Uniquely Recognize Cisplatin-DNA Interstrand Cross-Links. Biochemistry 2009, 48:4916-4925.
    • (2009) Biochemistry , vol.48 , pp. 4916-4925
    • Zhu, G.Y.1    Lippard, S.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.