메뉴 건너뛰기




Volumn 38, Issue 1, 2016, Pages

Mechanisms of interstrand DNA crosslink repair and human disorders

Author keywords

Fanconi anemia; Homologous recombination; Nucleotide excision repair; Translesion DNA synthesis

Indexed keywords

DNA HELICASE; DOUBLE STRANDED DNA;

EID: 84973568810     PISSN: 18807046     EISSN: 18807062     Source Type: Journal    
DOI: 10.1186/s41021-016-0037-9     Document Type: Review
Times cited : (93)

References (95)
  • 1
    • 0035807079 scopus 로고    scopus 로고
    • Repair of DNA interstrand cross-links
    • Dronkert ML, Kanaar R. Repair of DNA interstrand cross-links. Mutat Res. 2001;486(4):217-47.
    • (2001) Mutat Res. , vol.486 , Issue.4 , pp. 217-247
    • Dronkert, M.L.1    Kanaar, R.2
  • 2
    • 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 OD. Using synthetic DNA interstrand crosslinks to elucidate repair pathways and identify new therapeutic targets for cancer chemotherapy. Cell Mol Life Sci. 2010;67(21):3683-97. doi:10.1007/s00018-010-0492-6.
    • (2010) Cell Mol Life Sci. , vol.67 , Issue.21 , pp. 3683-3697
    • Guainazzi, A.1    Scharer, O.D.2
  • 3
    • 77955869859 scopus 로고    scopus 로고
    • Repair of DNA interstrand cross-links during S phase of the mammalian cell cycle
    • Legerski RJ Repair of DNA interstrand cross-links during S phase of the mammalian cell cycle. Environ Mol Mutagen. 2010;51(6):540-51. doi:10.1002/em.20566.
    • (2010) Environ Mol Mutagen , vol.51 , Issue.6 , pp. 540-551
    • Legerski, R.J.1
  • 4
    • 84885024085 scopus 로고    scopus 로고
    • Advances in understanding the complex mechanisms of DNA interstrand cross-link repair
    • Clauson C, Scharer OD, Niedernhofer L. Advances in understanding the complex mechanisms of DNA interstrand cross-link repair. Cold Spring Harb Perspect Biol. 2013;5(10):a012732. doi:10.1101/cshperspect.a012732.
    • (2013) Cold Spring Harb Perspect Biol. , vol.5 , Issue.10
    • Clauson, C.1    Scharer, O.D.2    Niedernhofer, L.3
  • 5
    • 33750309537 scopus 로고    scopus 로고
    • Replication-coupled repair of crotonaldehyde/acetaldehyde-induced guanine-guanine interstrand crosslinks and their mutagenicity
    • Liu X, Lao Y, Yang IY, Hecht SS, Moriya M. Replication-coupled repair of crotonaldehyde/acetaldehyde-induced guanine-guanine interstrand crosslinks and their mutagenicity. Biochemistry. 2006;45(42):12898-905. doi:10.1021/bi060792v.
    • (2006) Biochemistry , vol.45 , Issue.42 , pp. 12898-12905
    • Liu, X.1    Lao, Y.2    Yang, I.Y.3    Hecht, S.S.4    Moriya, M.5
  • 6
    • 84880866225 scopus 로고    scopus 로고
    • Visualizing inhibition of nucleosome mobility and transcription by cisplatin-DNA interstrand crosslinks in live mammalian cells
    • Zhu G, Song L, Lippard SJ. Visualizing inhibition of nucleosome mobility and transcription by cisplatin-DNA interstrand crosslinks in live mammalian cells. Cancer Res. 2013;73(1):4451-60. doi:10.1158/0008-5472.CAN-13-0198.
    • (2013) Cancer Res. , vol.73 , Issue.1 , pp. 4451-4460
    • Zhu, G.1    Song, L.2    Lippard, S.J.3
  • 7
    • 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, et al. The structure-specific endonuclease Mus81-Eme1 promotes conversion of interstrand DNA crosslinks into double-strands breaks. EMBO J. 2006;25(20):4921-32. doi:10.1038/sj.emboj.7601344.
    • (2006) EMBO J , vol.25 , Issue.20 , pp. 4921-4932
    • Hanada, K.1    Budzowska, M.2    Modesti, M.3    Maas, A.4    Wyman, C.5    Essers, J.6
  • 8
    • 34547942630 scopus 로고    scopus 로고
    • Psoralen and ultraviolet a light therapy for psoriasis
    • Stern RS Psoralen and ultraviolet a light therapy for psoriasis. N Engl J Med. 2007;357(7):682-90. doi:10.1056/NEJMct072317.
    • (2007) N Engl J Med. , vol.357 , Issue.7 , pp. 682-690
    • Stern, R.S.1
  • 9
    • 0029585833 scopus 로고
    • Solution structure of a cisplatin-induced DNA interstrand cross-link
    • Huang H, Zhu L, Reid BR, Drobny GP, Hopkins PB. Solution structure of a cisplatin-induced DNA interstrand cross-link. Science. 1995;270(5243):1842-5.
    • (1995) Science , vol.270 , Issue.5243 , pp. 1842-1845
    • Huang, H.1    Zhu, L.2    Reid, B.R.3    Drobny, G.P.4    Hopkins, P.B.5
  • 10
    • 0028949965 scopus 로고
    • A mechlorethamine-induced DNA interstrand crosslink bends duplex DNA
    • Rink SM, Hopkins PB. A mechlorethamine-induced DNA interstrand crosslink bends duplex DNA. Biochemistry. 1995;34(4):1439-45.
    • (1995) Biochemistry , vol.34 , Issue.4 , pp. 1439-1445
    • Rink, S.M.1    Hopkins, P.B.2
  • 11
    • 0000636701 scopus 로고
    • The initial clinical trial of nitrogen mustard
    • Gilman A. The initial clinical trial of nitrogen mustard. Am J Surg. 1963;105: 574-8.
    • (1963) Am J Surg. , vol.105 , pp. 574-578
    • Gilman, A.1
  • 12
    • 0034053776 scopus 로고    scopus 로고
    • Repair of intermediate structures produced at DNA interstrand cross-links in saccharomyces cerevisiae
    • McHugh PJ, Sones WR, Hartley JA. Repair of intermediate structures produced at DNA interstrand cross-links in Saccharomyces cerevisiae. Mol Cell Biol. 2000;20(10):3425-33.
    • (2000) Mol Cell Biol. , vol.20 , Issue.10 , pp. 3425-3433
    • McHugh, P.J.1    Sones, W.R.2    Hartley, J.A.3
  • 13
    • 0019370333 scopus 로고
    • A new apparatus with high radiation energy between 320-460 nm: Physical description and dermatological applications
    • Mutzhas MF, Holzle E, Hofmann C, Plewig G. A new apparatus with high radiation energy between 320-460 nm: physical description and dermatological applications. J Invest Dermatol. 1981;76(1):42-7.
    • (1981) J Invest Dermatol. , vol.76 , Issue.1 , pp. 42-47
    • Mutzhas, M.F.1    Holzle, E.2    Hofmann, C.3    Plewig, G.4
  • 14
    • 0023739833 scopus 로고
    • Phased psoralen cross-links do not bend the DNA double helix
    • Haran TE, Crothers DM. Phased psoralen cross-links do not bend the DNA double helix. Biochemistry. 1988;27(18):6967-71.
    • (1988) Biochemistry , vol.27 , Issue.18 , pp. 6967-6971
    • Haran, T.E.1    Crothers, D.M.2
  • 15
    • 0030030008 scopus 로고    scopus 로고
    • The solution structure of a psoralen cross-linked DNA duplex by NMR and relaxation matrix refinement
    • Hwang GS, Kim JK, Choi BS. The solution structure of a psoralen cross-linked DNA duplex by NMR and relaxation matrix refinement. Biochem Biophys Res Commun. 1996;219(1):191-7. doi:10.1006/bbrc.1996.0204.
    • (1996) Biochem Biophys Res Commun. , vol.219 , Issue.1 , pp. 191-197
    • Hwang, G.S.1    Kim, J.K.2    Choi, B.S.3
  • 16
    • 0025359651 scopus 로고
    • NMR and computational characterization of mitomycin cross-linked to adjacent deoxyguanosines in the minor groove of the d(T-A-C-G-T-A).d(T-A-C-G-T-A) duplex
    • Norman D, Live D, Sastry M, Lipman R, Hingerty BE, Tomasz M, et al. NMR and computational characterization of mitomycin cross-linked to adjacent deoxyguanosines in the minor groove of the d(T-A-C-G-T-A).d(T-A-C-G-T-A) duplex. Biochemistry. 1990;29(11):2861-75.
    • (1990) Biochemistry , vol.29 , Issue.11 , pp. 2861-2875
    • Norman, D.1    Live, D.2    Sastry, M.3    Lipman, R.4    Hingerty, B.E.5    Tomasz, M.6
  • 17
    • 0029877328 scopus 로고    scopus 로고
    • Bending of DNA by the mitomycin C-induced, GpG intrastrand cross-link
    • Rink SM, Lipman R, Alley SC, Hopkins PB, Tomasz M. Bending of DNA by the mitomycin C-induced, GpG intrastrand cross-link. Chem Res Toxicol. 1996; 9(2):382-9. doi:10.1021/tx950156q.
    • (1996) Chem Res Toxicol. , vol.9 , Issue.2 , pp. 382-389
    • Rink, S.M.1    Lipman, R.2    Alley, S.C.3    Hopkins, P.B.4    Tomasz, M.5
  • 18
    • 0035436539 scopus 로고    scopus 로고
    • Repair of DNA interstrand crosslinks: Molecular mechanisms and clinical relevance
    • McHugh PJ, Spanswick VJ, Hartley JA. Repair of DNA interstrand crosslinks: molecular mechanisms and clinical relevance. Lancet Oncol. 2001;2(8):483-90. doi:10.1016/S1470-2045(01)00454-5.
    • (2001) Lancet Oncol. , vol.2 , Issue.8 , pp. 483-490
    • McHugh, P.J.1    Spanswick, V.J.2    Hartley, J.A.3
  • 19
    • 33645312939 scopus 로고    scopus 로고
    • DNA interstrand crosslink repair during G1 involves nucleotide excision repair and DNA polymerase zeta
    • Sarkar S, Davies AA, Ulrich HD, McHugh PJ. DNA interstrand crosslink repair during G1 involves nucleotide excision repair and DNA polymerase zeta. EMBO J. 2006;25(6):1285-94. doi:10.1038/sj.emboj.7600993.
    • (2006) EMBO J , vol.25 , Issue.6 , pp. 1285-1294
    • Sarkar, S.1    Davies, A.A.2    Ulrich, H.D.3    McHugh, P.J.4
  • 20
    • 77955876503 scopus 로고    scopus 로고
    • Mammalian nucleotide excision repair proteins and interstrand crosslink repair
    • Wood RD Mammalian nucleotide excision repair proteins and interstrand crosslink repair. Environ Mol Mutagen. 2010;51(6):520-6. doi:10.1002/em.20569.
    • (2010) Environ Mol Mutagen , vol.51 , Issue.6 , pp. 520-526
    • Wood, R.D.1
  • 21
    • 33646815702 scopus 로고    scopus 로고
    • DNA interstrand cross-link repair in the cell cycle: A critical role for polymerase zeta in G1 phase
    • McHugh PJ, Sarkar S. DNA interstrand cross-link repair in the cell cycle: a critical role for polymerase zeta in G1 phase. Cell Cycle. 2006;5(10):1044-7.
    • (2006) Cell Cycle , vol.5 , Issue.10 , pp. 1044-1047
    • McHugh, P.J.1    Sarkar, S.2
  • 22
    • 84863840463 scopus 로고    scopus 로고
    • Replication-independent repair of DNA interstrand crosslinks
    • Williams HL, Gottesman ME, Gautier J. Replication-independent repair of DNA interstrand crosslinks. Mol Cell. 2012;47(1):140-7. doi:10.1016/j.molcel.2012.05.001.
    • (2012) Mol Cell , vol.47 , Issue.1 , pp. 140-147
    • Williams, H.L.1    Gottesman, M.E.2    Gautier, J.3
  • 23
    • 84858642631 scopus 로고    scopus 로고
    • Replication bypass of N2-N2 deoxyguanosine interstrand cross-links by human DNA polymerases eta and iota
    • Klug AR, Harbut MB, Lloyd RS, Minko IG. Replication bypass of N2-N2 deoxyguanosine interstrand cross-links by human DNA polymerases eta and iota. Chem Res Toxicol. 2012;25(3):755-62. doi:10.1021/tx300011w.
    • (2012) Chem Res Toxicol. , vol.25 , Issue.3 , pp. 755-762
    • Klug, A.R.1    Harbut, M.B.2    Lloyd, R.S.3    Minko, I.G.4
  • 24
    • 47749128072 scopus 로고    scopus 로고
    • Role for DNA polymerase kappa in the processing of N2-N2-guanine interstrand cross-links
    • Minko IG, Harbut MB, Kozekov ID, Kozekova A, Jakobs PM, Olson SB, et al. Role for DNA polymerase kappa in the processing of N2-N2-guanine interstrand cross-links. J Biol Chem. 2008;283(25):17075-82. doi:10.1074/jbc. M801238200.
    • (2008) J Biol Chem. , vol.283 , Issue.25 , pp. 17075-17082
    • Minko, I.G.1    Harbut, M.B.2    Kozekov, I.D.3    Kozekova, A.4    Jakobs, P.M.5    Olson, S.B.6
  • 25
    • 0033781210 scopus 로고    scopus 로고
    • Defining the roles of nucleotide excision repair and recombination in the repair of DNA interstrand cross-links in mammalian cells
    • De Silva IU, McHugh PJ, Clingen PH, Hartley JA. Defining the roles of nucleotide excision repair and recombination in the repair of DNA interstrand cross-links in mammalian cells. Mol Cell Biol. 2000;20(21): 7980-90.
    • (2000) Mol Cell Biol. , vol.20 , Issue.21 , pp. 7980-7990
    • De Silva, I.U.1    McHugh, P.J.2    Clingen, P.H.3    Hartley, J.A.4
  • 26
    • 2942709644 scopus 로고    scopus 로고
    • The structure-specific endonuclease ercc1-xpf is required to resolve DNA interstrand cross-link-induced double-strand breaks
    • Niedernhofer LJ, Odijk H, Budzowska M, van Drunen E, Maas A, Theil AF, et al. The structure-specific endonuclease Ercc1-Xpf is required to resolve DNA interstrand cross-link-induced double-strand breaks. Mol Cell Biol. 2004; 24(13):5776-87. doi:10.1128/MCB.24.13.5776-5787.2004.
    • (2004) Mol Cell Biol. , vol.24 , Issue.13 , pp. 5776-5787
    • Niedernhofer, L.J.1    Odijk, H.2    Budzowska, M.3    Van Drunen, E.4    Maas, A.5    Theil, A.F.6
  • 27
    • 0036712139 scopus 로고    scopus 로고
    • Defects in interstrand cross-link uncoupling do not account for the extreme sensitivity of ERCC1 and XPF cells to cisplatin
    • De Silva IU, McHugh PJ, Clingen PH, Hartley JA. Defects in interstrand cross-link uncoupling do not account for the extreme sensitivity of ERCC1 and XPF cells to cisplatin. Nucleic Acids Res. 2002;30(17):3848-56.
    • (2002) Nucleic Acids Res. , vol.30 , Issue.17 , pp. 3848-3856
    • De Silva, I.U.1    McHugh, P.J.2    Clingen, P.H.3    Hartley, J.A.4
  • 28
    • 0037090816 scopus 로고    scopus 로고
    • The active site of the DNA repair endonuclease XPF-ERCC1 forms a highly conserved nuclease motif
    • Enzlin JH, Scharer OD. The active site of the DNA repair endonuclease XPF-ERCC1 forms a highly conserved nuclease motif. EMBO J. 2002;21(8):2045-53. doi:10.1093/emboj/21.8.2045.
    • (2002) EMBO J. , vol.21 , Issue.8 , pp. 2045-2053
    • Enzlin, J.H.1    Scharer, O.D.2
  • 29
    • 10744231462 scopus 로고    scopus 로고
    • Eme1 is involved in DNA damage processing and maintenance of genomic stability in mammalian cells
    • Abraham J, Lemmers B, Hande MP, Moynahan ME, Chahwan C, Ciccia A, et al. Eme1 is involved in DNA damage processing and maintenance of genomic stability in mammalian cells. EMBO J. 2003;22(22):6137-47. doi:10. 1093/emboj/cdg580.
    • (2003) EMBO J. , vol.22 , Issue.22 , pp. 6137-6147
    • Abraham, J.1    Lemmers, B.2    Hande, M.P.3    Moynahan, M.E.4    Chahwan, C.5    Ciccia, A.6
  • 31
    • 0347624597 scopus 로고    scopus 로고
    • Repair kinetics of genomic interstrand DNA cross-links: Evidence for DNA double-strand break-dependent activation of the fanconi anemia/BRCA pathway
    • Rothfuss A, Grompe M. Repair kinetics of genomic interstrand DNA cross-links: evidence for DNA double-strand break-dependent activation of the Fanconi anemia/BRCA pathway. Mol Cell Biol. 2004;24(1):123-34.
    • (2004) Mol Cell Biol. , vol.24 , Issue.1 , pp. 123-134
    • Rothfuss, A.1    Grompe, M.2
  • 32
    • 0035083172 scopus 로고    scopus 로고
    • Chromosome instability and defective recombinational repair in knockout mutants of the five rad51 paralogs
    • Takata M, Sasaki MS, Tachiiri S, Fukushima T, Sonoda E, Schild D, et al. Chromosome instability and defective recombinational repair in knockout mutants of the five Rad51 paralogs. Mol Cell Biol. 2001;21(8):2858-66. doi:10. 1128/MCB.21.8.2858-2866.2001.
    • (2001) Mol Cell Biol , vol.21 , Issue.8 , pp. 2858-2866
    • Takata, M.1    Sasaki, M.S.2    Tachiiri, S.3    Fukushima, T.4    Sonoda, E.5    Schild, D.6
  • 34
    • 31344442810 scopus 로고    scopus 로고
    • Differential contributions of mammalian rad54 paralogs to recombination, DNA damage repair, and meiosis
    • Wesoly J, Agarwal S, Sigurdsson S, Bussen W, Van Komen S, Qin J, et al. Differential contributions of mammalian Rad54 paralogs to recombination, DNA damage repair, and meiosis. Mol Cell Biol. 2006;26(3):976-89. doi:10. 1128/MCB.26.3.976-989.2006.
    • (2006) Mol Cell Biol. , vol.26 , Issue.3 , pp. 976-989
    • Wesoly, J.1    Agarwal, S.2    Sigurdsson, S.3    Bussen, W.4    Van Komen, S.5    Qin, J.6
  • 35
    • 77957123627 scopus 로고    scopus 로고
    • Pathways of mammalian replication fork restart
    • Petermann E, Helleday T. Pathways of mammalian replication fork restart. Nat Rev Mol Cell Biol. 2010;11(10):683-7. doi:10.1038/nrm2974.
    • (2010) Nat Rev Mol Cell Biol. , vol.11 , Issue.10 , pp. 683-687
    • Petermann, E.1    Helleday, T.2
  • 36
    • 84872057291 scopus 로고    scopus 로고
    • Learning from a paradox: Recent insights into fanconi anaemia through studying mouse models
    • Bakker ST, de Winter JP, te Riele H. Learning from a paradox: recent insights into Fanconi anaemia through studying mouse models. Dis Model Mech. 2013;6(1):40-7. doi:10.1242/dmm.009795.
    • (2013) Dis Model Mech. , vol.6 , Issue.1 , pp. 40-47
    • Bakker, S.T.1    De Winter, J.P.2    Te Riele, H.3
  • 38
    • 33744481750 scopus 로고    scopus 로고
    • Molecular pathogenesis of fanconi anemia: Recent progress
    • Taniguchi T, D'Andrea AD. Molecular pathogenesis of Fanconi anemia: recent progress. Blood. 2006;107(11):4223-33. doi:10.1182/blood-2005-10-4240.
    • (2006) Blood , vol.107 , Issue.11 , pp. 4223-4233
    • Taniguchi, T.1    D'Andrea, A.D.2
  • 39
    • 84907061756 scopus 로고    scopus 로고
    • Inherited bone marrow failure syndromes in adolescents and young adults
    • Wilson DB, Link DC, Mason PJ, Bessler M. Inherited bone marrow failure syndromes in adolescents and young adults. Ann Med. 2014;46(6):353-63. doi:10.3109/07853890.2014.915579.
    • (2014) Ann Med. , vol.46 , Issue.6 , pp. 353-363
    • Wilson, D.B.1    Link, D.C.2    Mason, P.J.3    Bessler, M.4
  • 40
    • 84938667462 scopus 로고    scopus 로고
    • Mutations in the gene encoding the E2 conjugating enzyme UBE2T cause fanconi anemia
    • Hira A, Yoshida K, Sato K, Okuno Y, Shiraishi Y, Chiba K, et al. Mutations in the gene encoding the E2 conjugating enzyme UBE2T cause Fanconi anemia. Am J Hum Genet. 2015;96(6):1001-7. doi:10.1016/j.ajhg.2015.04.022.
    • (2015) Am J Hum Genet. , vol.96 , Issue.6 , pp. 1001-1007
    • Hira, A.1    Yoshida, K.2    Sato, K.3    Okuno, Y.4    Shiraishi, Y.5    Chiba, K.6
  • 41
    • 70349859881 scopus 로고    scopus 로고
    • DNA damage, aging, and cancer
    • Hoeijmakers JH DNA damage, aging, and cancer. N Engl J Med. 2009; 361(15):1475-85. doi:10.1056/NEJMra0804615.
    • (2009) N Engl J Med. , vol.361 , Issue.15 , pp. 1475-1485
    • Hoeijmakers, J.H.1
  • 42
    • 84878016439 scopus 로고    scopus 로고
    • Cockayne syndrome: The expanding clinical and mutational spectrum
    • Laugel V. Cockayne syndrome: the expanding clinical and mutational spectrum. Mech Ageing Dev. 2013;134(5-6):161-70. doi:10.1016/j.mad.2013.02.006.
    • (2013) Mech Ageing Dev. , vol.134 , Issue.5-6 , pp. 161-170
    • Laugel, V.1
  • 43
    • 77956985370 scopus 로고    scopus 로고
    • Trichothiodystrophy view from the molecular basis of DNA repair/transcription factor TFIIH
    • Hashimoto S, Egly JM. Trichothiodystrophy view from the molecular basis of DNA repair/transcription factor TFIIH. Hum Mol Genet. 2009;18(R2):R224-30. doi:10.1093/hmg/ddp390.
    • (2009) Hum Mol Genet. , vol.18 , Issue.R2 , pp. R224-R230
    • Hashimoto, S.1    Egly, J.M.2
  • 45
    • 84866952680 scopus 로고    scopus 로고
    • Genotoxic consequences of endogenous aldehydes on mouse haematopoietic stem cell function
    • Garaycoechea JI, Crossan GP, Langevin F, Daly M, Arends MJ, Patel KJ. Genotoxic consequences of endogenous aldehydes on mouse haematopoietic stem cell function. Nature. 2012;489(7417):571-5. doi:10.1038/nature11368.
    • (2012) Nature. , vol.489 , Issue.7417 , pp. 571-575
    • Garaycoechea, J.I.1    Crossan, G.P.2    Langevin, F.3    Daly, M.4    Arends, M.J.5    Patel, K.J.6
  • 46
    • 84902112143 scopus 로고    scopus 로고
    • Mechanism and regulation of incisions during DNA interstrand cross-link repair
    • Zhang J, Walter JC. Mechanism and regulation of incisions during DNA interstrand cross-link repair. DNA Repair (Amst). 2014;19:135-42. doi:10.1016/j.dnarep.2014.03.018.
    • (2014) DNA Repair (Amst) , vol.19 , pp. 135-142
    • Zhang, J.1    Walter, J.C.2
  • 47
    • 84865353862 scopus 로고    scopus 로고
    • Mcm8 and mcm9 form a complex that functions in homologous recombination repair induced by DNA interstrand crosslinks
    • Nishimura K, Ishiai M, Horikawa K, Fukagawa T, Takata M, Takisawa H, et al. Mcm8 and Mcm9 form a complex that functions in homologous recombination repair induced by DNA interstrand crosslinks. Mol Cell. 2012;47(4):511-22. doi:10.1016/j. molcel.2012.05.047.
    • (2012) Mol Cell , vol.47 , Issue.4 , pp. 511-522
    • Nishimura, K.1    Ishiai, M.2    Horikawa, K.3    Fukagawa, T.4    Takata, M.5    Takisawa, H.6
  • 48
    • 51549098159 scopus 로고    scopus 로고
    • Mechanism of replication-coupled DNA interstrand crosslink repair
    • Raschle M, Knipscheer P, Enoiu M, Angelov T, Sun J, Griffith JD, et al. Mechanism of replication-coupled DNA interstrand crosslink repair. Cell. 2008; 134(6):969-80. doi:10.1016/j.cell.2008.08.030.
    • (2008) Cell , vol.134 , Issue.6 , pp. 969-980
    • Raschle, M.1    Knipscheer, P.2    Enoiu, M.3    Angelov, T.4    Sun, J.5    Griffith, J.D.6
  • 49
    • 72949123930 scopus 로고    scopus 로고
    • The fanconi anemia pathway promotes replication-dependent DNA interstrand cross-link repair
    • Knipscheer P, Raschle M, Smogorzewska A, Enoiu M, Ho TV, Scharer OD, et al. The Fanconi anemia pathway promotes replication-dependent DNA interstrand cross-link repair. Science. 2009;326(5960):1698-701. doi:10.1126/science.1182372.
    • (2009) Science , vol.326 , Issue.5960 , pp. 1698-1701
    • Knipscheer, P.1    Raschle, M.2    Smogorzewska, A.3    Enoiu, M.4    Ho, T.V.5    Scharer, O.D.6
  • 50
    • 79959843168 scopus 로고    scopus 로고
    • Mechanism of RAD51-dependent DNA interstrand cross-link repair
    • Long DT, Raschle M, Joukov V, Walter JC. Mechanism of RAD51-dependent DNA interstrand cross-link repair. Science. 2011;333(6038):84-7. doi:10.1126/science.1204258.
    • (2011) Science , vol.333 , Issue.6038 , pp. 84-87
    • Long, D.T.1    Raschle, M.2    Joukov, V.3    Walter, J.C.4
  • 51
    • 84942039168 scopus 로고    scopus 로고
    • Regulation of the rev1-pol zeta complex during bypass of a DNA interstrand cross-link
    • Budzowska M, Graham TG, Sobeck A, Waga S, Walter JC. Regulation of the Rev1-pol zeta complex during bypass of a DNA interstrand cross-link. EMBO J. 2015;34(14):1971-85. doi:10.15252/embj.201490878.
    • (2015) EMBO J , vol.34 , Issue.14 , pp. 1971-1985
    • Budzowska, M.1    Graham, T.G.2    Sobeck, A.3    Waga, S.4    Walter, J.C.5
  • 52
    • 84925956835 scopus 로고    scopus 로고
    • UHRF1 contributes to DNA damage repair as a lesion recognition factor and nuclease scaffold
    • Tian Y, Paramasivam M, Ghosal G, Chen D, Shen X, Huang Y, et al. UHRF1 Contributes to DNA damage repair as a lesion recognition factor and nuclease scaffold. Cell Rep. 2015;10(12):1957-66. doi:10.1016/j.celrep.2015.03.038.
    • (2015) Cell Rep , vol.10 , Issue.12 , pp. 1957-1966
    • Tian, Y.1    Paramasivam, M.2    Ghosal, G.3    Chen, D.4    Shen, X.5    Huang, Y.6
  • 53
    • 84925938228 scopus 로고    scopus 로고
    • UHRF1 is a sensor for DNA interstrand crosslinks and recruits FANCD2 to initiate the fanconi anemia pathway
    • Liang CC, Zhan B, Yoshikawa Y, Haas W, Gygi SP, Cohn MA. UHRF1 Is a sensor for DNA interstrand crosslinks and recruits FANCD2 to initiate the Fanconi Anemia pathway. Cell Rep. 2015;10(12):1947-56. doi:10.1016/j.celrep.2015.02.053.
    • (2015) Cell Rep. , vol.10 , Issue.12 , pp. 1947-1956
    • Liang, C.C.1    Zhan, B.2    Yoshikawa, Y.3    Haas, W.4    Gygi, S.P.5    Cohn, M.A.6
  • 54
    • 84875883306 scopus 로고    scopus 로고
    • UHRF1 targets DNMT1 for DNA methylation through cooperative binding of hemi-methylated DNA and methylated H3K9
    • Liu X, Gao Q, Li P, Zhao Q, Zhang J, Li J, et al. UHRF1 targets DNMT1 for DNA methylation through cooperative binding of hemi-methylated DNA and methylated H3K9. Nat Commun. 2013;4:1563. doi:10.1038/ncomms2562.
    • (2013) Nat Commun. , vol.4 , pp. 1563
    • Liu, X.1    Gao, Q.2    Li, P.3    Zhao, Q.4    Zhang, J.5    Li, J.6
  • 55
    • 84885577142 scopus 로고    scopus 로고
    • Uhrf1-dependent H3K23 ubiquitylation couples maintenance DNA methylation and replication
    • Nishiyama A, Yamaguchi L, Sharif J, Johmura Y, Kawamura T, Nakanishi K, et al. Uhrf1-dependent H3K23 ubiquitylation couples maintenance DNA methylation and replication. Nature. 2013;502(7470):249-53. doi:10.1038/nature12488.
    • (2013) Nature , vol.502 , Issue.7470 , pp. 249-253
    • Nishiyama, A.1    Yamaguchi, L.2    Sharif, J.3    Johmura, Y.4    Kawamura, T.5    Nakanishi, K.6
  • 56
    • 0037072831 scopus 로고    scopus 로고
    • Targeted disruption of np95 gene renders murine embryonic stem cells hypersensitive to DNA damaging agents and DNA replication blocks
    • Muto M, Kanari Y, Kubo E, Takabe T, Kurihara T, Fujimori A, et al. Targeted disruption of Np95 gene renders murine embryonic stem cells hypersensitive to DNA damaging agents and DNA replication blocks. J Biol Chem. 2002;277(37):34549-55. doi:10.1074/jbc.M205189200.
    • (2002) J Biol Chem. , vol.277 , Issue.37 , pp. 34549-34555
    • Muto, M.1    Kanari, Y.2    Kubo, E.3    Takabe, T.4    Kurihara, T.5    Fujimori, A.6
  • 57
    • 0033025041 scopus 로고    scopus 로고
    • The FANCA gene in Japanese fanconi anemia: Reports of eight novel mutations and analysis of sequence variability
    • Tachibana A, Kato T, Ejima Y, Yamada T, Shimizu T, Yang L, et al. The FANCA gene in Japanese Fanconi anemia: reports of eight novel mutations and analysis of sequence variability. Hum Mutat. 1999;13(3):237-44. doi:10.1002/(SICI)1098-1004(1999)13:3<237::AID-HUMU8>3.0.CO;2-F.
    • (1999) Hum Mutat. , vol.13 , Issue.3 , pp. 237-244
    • Tachibana, A.1    Kato, T.2    Ejima, Y.3    Yamada, T.4    Shimizu, T.5    Yang, L.6
  • 59
    • 0026521238 scopus 로고
    • Cloning of cDNAs for fanconi's anaemia by functional complementation
    • Strathdee CA, Gavish H, Shannon WR, Buchwald M. Cloning of cDNAs for Fanconi's anaemia by functional complementation. Nature. 1992;356(6372):763-7. doi:10.1038/356763a0.
    • (1992) Nature , vol.356 , Issue.6372 , pp. 763-767
    • Strathdee, C.A.1    Gavish, H.2    Shannon, W.R.3    Buchwald, M.4
  • 66
    • 34247110291 scopus 로고    scopus 로고
    • Identification of the FANCI protein, a monoubiquitinated FANCD2 paralog required for DNA repair
    • Smogorzewska A, Matsuoka S, Vinciguerra P, McDonald 3rd ER, Hurov KE, Luo J, et al. Identification of the FANCI protein, a monoubiquitinated FANCD2 paralog required for DNA repair. Cell. 2007;129(2):289-301. doi:10.1016/j.cell.2007.03.009.
    • (2007) Cell , vol.129 , Issue.2 , pp. 289-301
    • Smogorzewska, A.1    Matsuoka, S.2    Vinciguerra, P.3    McDonald, E.R.4    Hurov, K.E.5    Luo, J.6
  • 68
  • 69
    • 24944575242 scopus 로고    scopus 로고
    • BACH1 is critical for homologous recombination and appears to be the fanconi anemia gene product FANCJ
    • Litman R, Peng M, Jin Z, Zhang F, Zhang J, Powell S, et al. BACH1 is critical for homologous recombination and appears to be the Fanconi anemia gene product FANCJ. Cancer Cell. 2005;8(3):255-65. doi:10.1016/j.ccr.2005.08.004.
    • (2005) Cancer Cell , vol.8 , Issue.3 , pp. 255-265
    • Litman, R.1    Peng, M.2    Jin, Z.3    Zhang, F.4    Zhang, J.5    Powell, S.6
  • 70
    • 2942664480 scopus 로고    scopus 로고
    • FANCL replaces BRCA1 as the likely ubiquitin ligase responsible for FANCD2 monoubiquitination
    • Meetei AR, Yan Z, Wang W. FANCL replaces BRCA1 as the likely ubiquitin ligase responsible for FANCD2 monoubiquitination. Cell Cycle. 2004;3(2):179-81.
    • (2004) Cell Cycle , vol.3 , Issue.2 , pp. 179-181
    • Meetei, A.R.1    Yan, Z.2    Wang, W.3
  • 71
    • 33846625493 scopus 로고    scopus 로고
    • PALB2, which encodes a BRCA2-interacting protein, is a breast cancer susceptibility gene
    • Rahman N, Seal S, Thompson D, Kelly P, Renwick A, Elliott A, et al. PALB2, which encodes a BRCA2-interacting protein, is a breast cancer susceptibility gene. Nat Genet. 2007;39(2):165-7. doi:10.1038/ng1959.
    • (2007) Nat Genet , vol.39 , Issue.2 , pp. 165-167
    • Rahman, N.1    Seal, S.2    Thompson, D.3    Kelly, P.4    Renwick, A.5    Elliott, A.6
  • 72
    • 33846569450 scopus 로고    scopus 로고
    • Biallelic mutations in PALB2 cause fanconi anemia subtype FA-N and predispose to childhood cancer
    • Reid S, Schindler D, Hanenberg H, Barker K, Hanks S, Kalb R, et al. Biallelic mutations in PALB2 cause Fanconi anemia subtype FA-N and predispose to childhood cancer. Nat Genet. 2007;39(2):162-4. doi:10.1038/ng1947.
    • (2007) Nat Genet , vol.39 , Issue.2 , pp. 162-164
    • Reid, S.1    Schindler, D.2    Hanenberg, H.3    Barker, K.4    Hanks, S.5    Kalb, R.6
  • 73
    • 77951747926 scopus 로고    scopus 로고
    • Mutation of the RAD51C gene in a fanconi anemia-like disorder
    • Vaz F, Hanenberg H, Schuster B, Barker K, Wiek C, Erven V, et al. Mutation of the RAD51C gene in a Fanconi anemia-like disorder. Nat Genet. 2010;42(5):406-9. doi:10.1038/ng.570.
    • (2010) Nat Genet , vol.42 , Issue.5 , pp. 406-409
    • Vaz, F.1    Hanenberg, H.2    Schuster, B.3    Barker, K.4    Wiek, C.5    Erven, V.6
  • 74
    • 77951720395 scopus 로고    scopus 로고
    • Germline mutations in breast and ovarian cancer pedigrees establish RAD51C as a human cancer susceptibility gene
    • Meindl A, Hellebrand H, Wiek C, Erven V, Wappenschmidt B, Niederacher D, et al. Germline mutations in breast and ovarian cancer pedigrees establish RAD51C as a human cancer susceptibility gene. Nat Genet. 2010;42(5):410-4. doi:10.1038/ng.569.
    • (2010) Nat Genet , vol.42 , Issue.5 , pp. 410-414
    • Meindl, A.1    Hellebrand, H.2    Wiek, C.3    Erven, V.4    Wappenschmidt, B.5    Niederacher, D.6
  • 77
    • 33845914051 scopus 로고    scopus 로고
    • A new progeroid syndrome reveals that genotoxic stress suppresses the somatotroph axis
    • Niedernhofer LJ, Garinis GA, Raams A, Lalai AS, Robinson AR, Appeldoorn E, et al. A new progeroid syndrome reveals that genotoxic stress suppresses the somatotroph axis. Nature. 2006;444(7122):1038-43. doi:10.1038/nature05456.
    • (2006) Nature , vol.444 , Issue.7122 , pp. 1038-1043
    • Niedernhofer, L.J.1    Garinis, G.A.2    Raams, A.3    Lalai, A.S.4    Robinson, A.R.5    Appeldoorn, E.6
  • 78
    • 84887610670 scopus 로고    scopus 로고
    • Evaluation of rare variants in the new fanconi anemia gene ERCC4 (FANCQ) as familial breast/ovarian cancer susceptibility alleles
    • Osorio A, Bogliolo M, Fernandez V, Barroso A, de la Hoya M, Caldes T, et al. Evaluation of rare variants in the new fanconi anemia gene ERCC4 (FANCQ) as familial breast/ovarian cancer susceptibility alleles. Hum Mutat. 2013; 34(12):1615-8. doi:10.1002/humu.22438.
    • (2013) Hum Mutat , vol.34 , Issue.12 , pp. 1615-1618
    • Osorio, A.1    Bogliolo, M.2    Fernandez, V.3    Barroso, A.4    De La Hoya, M.5    Caldes, T.6
  • 80
    • 84937525461 scopus 로고    scopus 로고
    • Deficiency of UBE2T, the E2 ubiquitin ligase necessary for FANCD2 and FANCI ubiquitination, causes FA-T subtype of fanconi anemia
    • Rickman KA, Lach FP, Abhyankar A, Donovan FX, Sanborn EM, Kennedy JA, et al. Deficiency of UBE2T, the E2 Ubiquitin Ligase necessary for FANCD2 and FANCI Ubiquitination, causes FA-T subtype of Fanconi anemia. Cell Rep. 2015;12(1):35-41. doi:10.1016/j.celrep.2015.06.014.
    • (2015) Cell Rep. , vol.12 , Issue.1 , pp. 35-41
    • Rickman, K.A.1    Lach, F.P.2    Abhyankar, A.3    Donovan, F.X.4    Sanborn, E.M.5    Kennedy, J.A.6
  • 81
    • 33847056347 scopus 로고    scopus 로고
    • First reported patient with human ERCC1 deficiency has cerebro-oculo-facio-skeletal syndrome with a mild defect in nucleotide excision repair and severe developmental failure
    • Jaspers NG, Raams A, Silengo MC, Wijgers N, Niedernhofer LJ, Robinson AR, et al. First reported patient with human ERCC1 deficiency has cerebro-oculo-facio-skeletal syndrome with a mild defect in nucleotide excision repair and severe developmental failure. Am J Hum Genet. 2007;80(3):457-66. doi:10.1086/512486.
    • (2007) Am J Hum Genet. , vol.80 , Issue.3 , pp. 457-466
    • Jaspers, N.G.1    Raams, A.2    Silengo, M.C.3    Wijgers, N.4    Niedernhofer, L.J.5    Robinson, A.R.6
  • 82
    • 0025168640 scopus 로고
    • Analysis of a human DNA excision repair gene involved in group A xeroderma pigmentosum and containing a zinc-finger domain
    • Tanaka K, Miura N, Satokata I, Miyamoto I, Yoshida MC, Satoh Y, et al. Analysis of a human DNA excision repair gene involved in group A xeroderma pigmentosum and containing a zinc-finger domain. Nature. 1990;348(6296):73-6. doi:10.1038/348073a0.
    • (1990) Nature , vol.348 , Issue.6296 , pp. 73-76
    • Tanaka, K.1    Miura, N.2    Satokata, I.3    Miyamoto, I.4    Yoshida, M.C.5    Satoh, Y.6
  • 83
    • 0026459944 scopus 로고
    • Cloning and characterization of the drosophila homolog of the xeroderma pigmentosum complementation-group B correcting gene, ERCC3
    • Koken MH, Vreeken C, Bol SA, Cheng NC, Jaspers-Dekker I, Hoeijmakers JH, et al. Cloning and characterization of the Drosophila homolog of the xeroderma pigmentosum complementation-group B correcting gene, ERCC3. Nucleic Acids Res. 1992;20(21):5541-8.
    • (1992) Nucleic Acids Res. , vol.20 , Issue.21 , pp. 5541-5548
    • Koken, M.H.1    Vreeken, C.2    Bol, S.A.3    Cheng, N.C.4    Jaspers-Dekker, I.5    Hoeijmakers, J.H.6
  • 84
    • 16944363270 scopus 로고    scopus 로고
    • A mutation in the XPB/ERCC3 DNA repair transcription gene, associated with trichothiodystrophy
    • Weeda G, Eveno E, Donker I, Vermeulen W, Chevallier-Lagente O, Taieb A, et al. A mutation in the XPB/ERCC3 DNA repair transcription gene, associated with trichothiodystrophy. Am J Hum Genet. 1997;60(2):320-9.
    • (1997) Am J Hum Genet. , vol.60 , Issue.2 , pp. 320-329
    • Weeda, G.1    Eveno, E.2    Donker, I.3    Vermeulen, W.4    Chevallier-Lagente, O.5    Taieb, A.6
  • 85
    • 33750922149 scopus 로고    scopus 로고
    • Phenotypic heterogeneity in the XPB DNA helicase gene (ERCC3): Xeroderma pigmentosum without and with cockayne syndrome
    • Oh KS, Khan SG, Jaspers NG, Raams A, Ueda T, Lehmann A, et al. Phenotypic heterogeneity in the XPB DNA helicase gene (ERCC3): xeroderma pigmentosum without and with Cockayne syndrome. Hum Mutat. 2006; 27(11):1092-103. doi:10.1002/humu.20392.
    • (2006) Hum Mutat. , vol.27 , Issue.11 , pp. 1092-1103
    • Oh, K.S.1    Khan, S.G.2    Jaspers, N.G.3    Raams, A.4    Ueda, T.5    Lehmann, A.6
  • 86
    • 0026697582 scopus 로고
    • Expression cloning of a human DNA repair gene involved in xeroderma pigmentosum group C
    • Legerski R, Peterson C. Expression cloning of a human DNA repair gene involved in xeroderma pigmentosum group C. Nature. 1992;359(6390):70-3. doi:10.1038/359070a0.
    • (1992) Nature , vol.359 , Issue.6390 , pp. 70-73
    • Legerski, R.1    Peterson, C.2
  • 87
    • 0024444425 scopus 로고
    • Molecular cloning and characterization of a mammalian excision repair gene that partially restores UV resistance to xeroderma pigmentosum complementation group D cells
    • Arrand JE, Bone NM, Johnson RT. Molecular cloning and characterization of a mammalian excision repair gene that partially restores UV resistance to xeroderma pigmentosum complementation group D cells. Proc Natl Acad Sci U S A. 1989;86(18):6997-7001.
    • (1989) Proc Natl Acad Sci U S A , vol.86 , Issue.18 , pp. 6997-7001
    • Arrand, J.E.1    Bone, N.M.2    Johnson, R.T.3
  • 88
    • 0028358988 scopus 로고
    • Mutations in the xeroderma pigmentosum group D DNA repair/transcription gene in patients with trichothiodystrophy
    • Broughton BC, Steingrimsdottir H, Weber CA, Lehmann AR. Mutations in the xeroderma pigmentosum group D DNA repair/transcription gene in patients with trichothiodystrophy. Nat Genet. 1994;7(2):189-94. doi:10.1038/ng0694-189.
    • (1994) Nat Genet. , vol.7 , Issue.2 , pp. 189-194
    • Broughton, B.C.1    Steingrimsdottir, H.2    Weber, C.A.3    Lehmann, A.R.4
  • 89
    • 0033565819 scopus 로고    scopus 로고
    • Cells from XP-D and XP-D-CS patients exhibit equally inefficient repair of UV-induced damage in transcribed genes but different capacity to recover UV-inhibited transcription
    • van Hoffen A, Kalle WH, de Jong-Versteeg. A, Lehmann AR, van Zeeland AA, Mullenders LH. Cells from XP-D and XP-D-CS patients exhibit equally inefficient repair of UV-induced damage in transcribed genes but different capacity to recover UV-inhibited transcription. Nucleic Acids Res. 1999; 27(14):2898-904.
    • (1999) Nucleic Acids Res. , vol.27 , Issue.14 , pp. 2898-2904
    • Van Hoffen, A.1    Kalle, W.H.2    De Jong-Versteeg, A.3    Lehmann, A.R.4    Van Zeeland, A.A.5    Mullenders, L.H.6
  • 90
    • 0023803543 scopus 로고
    • Xeroderma pigmentosum group E cells lack a nuclear factor that binds to damaged DNA
    • Chu G, Chang E. Xeroderma pigmentosum group E cells lack a nuclear factor that binds to damaged DNA. Science. 1988;242(4878):564-7.
    • (1988) Science , vol.242 , Issue.4878 , pp. 564-567
    • Chu, G.1    Chang, E.2
  • 92
    • 0028341685 scopus 로고
    • Mutations that disable the DNA repair gene XPG in a xeroderma pigmentosum group G patient
    • Nouspikel T, Clarkson SG. Mutations that disable the DNA repair gene XPG in a xeroderma pigmentosum group G patient. Hum Mol Genet. 1994;3(6):963-7.
    • (1994) Hum Mol Genet. , vol.3 , Issue.6 , pp. 963-967
    • Nouspikel, T.1    Clarkson, S.G.2
  • 93
    • 0029088143 scopus 로고
    • The cockayne syndrome group A gene encodes a WD repeat protein that interacts with CSB protein and a subunit of RNA polymerase II TFIIH
    • Henning KA, Li L, Iyer N, McDaniel LD, Reagan MS, Legerski R, et al. The Cockayne syndrome group A gene encodes a WD repeat protein that interacts with CSB protein and a subunit of RNA polymerase II TFIIH. Cell. 1995;82(4):555-64.
    • (1995) Cell , vol.82 , Issue.4 , pp. 555-564
    • Henning, K.A.1    Li, L.2    Iyer, N.3    McDaniel, L.D.4    Reagan, M.S.5    Legerski, R.6
  • 94
    • 0026465665 scopus 로고
    • ERCC6, a member of a subfamily of putative helicases, is involved in cockayne's syndrome and preferential repair of active genes
    • Troelstra C, van Gool A, de Wit J, Vermeulen W, Bootsma D, Hoeijmakers JH. ERCC6, a member of a subfamily of putative helicases, is involved in Cockayne's syndrome and preferential repair of active genes. Cell. 1992; 71(6):939-53.
    • (1992) Cell , vol.71 , Issue.6 , pp. 939-953
    • Troelstra, C.1    Van Gool, A.2    De Wit, J.3    Vermeulen, W.4    Bootsma, D.5    Hoeijmakers, J.H.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.