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Volumn 226, Issue 2, 2012, Pages 326-337

The Fanconi anaemia pathway orchestrates incisions at sites of crosslinked DNA

Author keywords

Btbd12; crosslink; DNA repair; Fanconi anaemia; genome instability; Slx4

Indexed keywords

CISPLATIN; DNA; ENDONUCLEASE; FANCONI ANEMIA GROUP D2 PROTEIN; FANCONI ANEMIA PROTEIN; FANCONI ASSOCIATED NUCLEASE 1; GENE PRODUCT; MITOMYCIN C; MUTAGENIC AGENT; TRANSCRIPTION FACTOR RUNX1; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG;

EID: 82755184119     PISSN: 00223417     EISSN: 10969896     Source Type: Journal    
DOI: 10.1002/path.3002     Document Type: Review
Times cited : (97)

References (151)
  • 1
    • 33750315873 scopus 로고    scopus 로고
    • Guido Fanconi (1892-1979): A jack of all trades
    • DOI 10.1038/nrc2009, PII NRC2009
    • Lobitz S, Velleuer E,. Guido Fanconi (1892-1979): a jack of all trades. Nat Rev Cancer 2006; 6: 893-898. (Pubitemid 44629901)
    • (2006) Nature Reviews Cancer , vol.6 , Issue.11 , pp. 893-898
    • Lobitz, S.1    Velleuer, E.2
  • 2
    • 0035379611 scopus 로고    scopus 로고
    • The emerging genetic and molecular basis of Fanconi anaemia
    • DOI 10.1038/35076590
    • Joenje H, Patel KJ,. The emerging genetic and molecular basis of Fanconi anaemia. Nat Rev Genet 2001; 2: 446-457. (Pubitemid 33673411)
    • (2001) Nature Reviews Genetics , vol.2 , Issue.6 , pp. 446-457
    • Joenje, H.1    Patel, K.J.2
  • 3
    • 67650451108 scopus 로고    scopus 로고
    • Fanconi anemia and its diagnosis
    • Auerbach AD,. Fanconi anemia and its diagnosis. Mutat Res 2009; 668: 4-10.
    • (2009) Mutat Res , vol.668 , pp. 4-10
    • Auerbach, A.D.1
  • 4
    • 0031012093 scopus 로고    scopus 로고
    • VACTERL with hydrocephalus in twins due to Fanconi anemia (FA): Mutation in the FAC gene
    • DOI 10.1002/(SICI)1096-8628(19970110)68:1<86::AID-AJMG17>3.0.CO;2-K
    • Cox PM, Gibson RA, Morgan N, et al., VACTERL with hydrocephalus in twins due to Fanconi anemia (FA): mutation in the FAC gene. Am J Med Genet 1997; 68: 86-90. (Pubitemid 27023848)
    • (1997) American Journal of Medical Genetics , vol.68 , Issue.1 , pp. 86-90
    • Cox, P.M.1    Gibson, R.A.2    Morgan, N.3    Brueton, L.A.4
  • 5
    • 33749252180 scopus 로고    scopus 로고
    • Fanconi anaemia complementation group B presenting as X linked VACTERL with hydrocephalus syndrome
    • DOI 10.1136/jmg.2006.041673
    • Holden ST, Cox JJ, Kesterton I, et al., Fanconi anaemia complementation group B presenting as X-linked VACTERL with hydrocephalus syndrome. J Med Genet 2006; 43: 750-754. (Pubitemid 44483919)
    • (2006) Journal of Medical Genetics , vol.43 , Issue.9 , pp. 750-754
    • Holden, S.T.1    Cox, J.J.2    Kesterton, I.3    Thomas, N.S.4    Carr, C.5    Woods, C.G.6
  • 6
    • 0242583890 scopus 로고    scopus 로고
    • Fanconi's Anemia and Clinical Radiosensitivity: Report on Two Adult Patients with Locally Advanced Solid Tumors Treated by Radiotherapy
    • DOI 10.1007/s00066-003-1099-8
    • Bremer M, Schindler D, Gross M, et al., Fanconi's anemia and clinical radiosensitivity report on two adult patients with locally advanced solid tumors treated by radiotherapy. Strahlenther Onkol 2003; 179: 748-753. (Pubitemid 37376989)
    • (2003) Strahlentherapie und Onkologie , vol.179 , Issue.11 , pp. 748-753
    • Bremer, M.1    Schindler, D.2    Gross, M.3    Dork, T.4    Morlot, S.5    Karstens, J.H.6
  • 8
    • 0026742503 scopus 로고
    • VACTERL with hydrocephalus: One end of the Fanconi anemia spectrum of anomalies?
    • Porteous ME, Cross I, Burn J,. VACTERL with hydrocephalus: one end of the Fanconi anemia spectrum of anomalies? Am J Med Genet 1992; 43: 1032-1034.
    • (1992) Am J Med Genet , vol.43 , pp. 1032-1034
    • Porteous, M.E.1    Cross, I.2    Burn, J.3
  • 9
    • 0027450296 scopus 로고
    • Hydrocephalus in Fanconi anemia
    • Alter BP,. Hydrocephalus in Fanconi anemia. Am J Med Genet 1993; 45: 785.
    • (1993) Am J Med Genet , vol.45 , pp. 785
    • Alter, B.P.1
  • 12
    • 3142631738 scopus 로고    scopus 로고
    • Individualized risks of first adverse events in patients with Fanconi anemia
    • DOI 10.1182/blood-2004-01-0083
    • Rosenberg PS, Huang Y, Alter BP,. Individualized risks of first adverse events in patients with Fanconi anemia. Blood 2004; 104: 350-355. (Pubitemid 38900014)
    • (2004) Blood , vol.104 , Issue.2 , pp. 350-355
    • Rosenberg, P.S.1    Huang, Y.2    Alter, B.P.3
  • 13
    • 77951740623 scopus 로고    scopus 로고
    • Knockdown of Fanconi anemia genes in human embryonic stem cells reveals early developmental defects in the hematopoietic lineage
    • Tulpule A, Lensch MW, Miller JD, et al., Knockdown of Fanconi anemia genes in human embryonic stem cells reveals early developmental defects in the hematopoietic lineage. Blood 2010; 115: 3453-3462.
    • (2010) Blood , vol.115 , pp. 3453-3462
    • Tulpule, A.1    Lensch, M.W.2    Miller, J.D.3
  • 14
    • 77957771805 scopus 로고    scopus 로고
    • Fertility recovery and pregnancy after allogeneic hematopoietic stem cell transplantation in Fanconi anemia patients
    • Nabhan SK, Bitencourt MA, Duval M, et al., Fertility recovery and pregnancy after allogeneic hematopoietic stem cell transplantation in Fanconi anemia patients. Haematologica 2010; 95: 1783-1787.
    • (2010) Haematologica , vol.95 , pp. 1783-1787
    • Nabhan, S.K.1    Bitencourt, M.A.2    Duval, M.3
  • 15
    • 0031012179 scopus 로고    scopus 로고
    • Diagnosis of Fanconi anemia in patients without congenital malformations: An International Fanconi Anemia Registry study
    • DOI 10.1002/(SICI)1096-8628(19970110)68:1<58::AID-AJMG11>3.0.CO;2-N
    • Giampietro PF, Verlander PC, Davis JG, et al., Diagnosis of Fanconi anemia in patients without congenital malformations: an international Fanconi Anemia Registry Study. Am J Med Genet 1997; 68: 58-61. (Pubitemid 27023842)
    • (1997) American Journal of Medical Genetics , vol.68 , Issue.1 , pp. 58-61
    • Giampietro, P.F.1    Verlander, P.C.2    Davis, J.G.3    Auerbach, A.D.4
  • 18
    • 79251624412 scopus 로고    scopus 로고
    • Disruption of mouse Slx4, a regulator of structure-specific nucleases, phenocopies Fanconi anemia
    • Crossan GP, van der Weyden L, Rosado IV, et al., Disruption of mouse Slx4, a regulator of structure-specific nucleases, phenocopies Fanconi anemia. Nat Genet 2011; 43: 147-152.
    • (2011) Nat Genet , vol.43 , pp. 147-152
    • Crossan, G.P.1    Van Der Weyden, L.2    Rosado, I.V.3
  • 20
    • 0037112817 scopus 로고    scopus 로고
    • A novel gene, Pog, is necessary for primordial germ cell proliferation in the mouse and underlies the germ cell deficient mutation, gcd
    • Agoulnik AI, Lu B, Zhu Q, et al., A novel gene, Pog, is necessary for primordial germ cell proliferation in the mouse and underlies the germ cell deficient mutation, gcd. Hum Mol Genet 2002; 11: 3047-3053. (Pubitemid 35414818)
    • (2002) Human Molecular Genetics , vol.11 , Issue.24 , pp. 3047-3053
    • Agoulnik, A.I.1    Lu, B.2    Zhu, Q.3    Truong, C.4    Ty, M.T.5    Arango, N.6    Chada, K.K.7    Bishop, C.E.8
  • 25
    • 59649114341 scopus 로고    scopus 로고
    • Inactivation of murine Usp1 results in genomic instability and a Fanconi anemia phenotype
    • Kim JM, Parmar K, Huang M, et al., Inactivation of murine Usp1 results in genomic instability and a Fanconi anemia phenotype. Dev Cell 2009; 16: 314-320.
    • (2009) Dev Cell , vol.16 , pp. 314-320
    • Kim, J.M.1    Parmar, K.2    Huang, M.3
  • 26
    • 69449102249 scopus 로고    scopus 로고
    • Fancm-deficient mice reveal unique features of Fanconi anemia complementation group M
    • Bakker ST, van de Vrugt HJ, Rooimans MA, et al., Fancm-deficient mice reveal unique features of Fanconi anemia complementation group M. Hum Mol Genet 2009; 18: 3484-3495.
    • (2009) Hum Mol Genet , vol.18 , pp. 3484-3495
    • Bakker, S.T.1    Van De Vrugt, H.J.2    Rooimans, M.A.3
  • 27
    • 79959821094 scopus 로고    scopus 로고
    • Mammalian BTBD12 (SLX4) protects against genomic instability during mammalian spermatogenesis
    • Holloway JK, Mohan S, Balmus G, et al., Mammalian BTBD12 (SLX4) protects against genomic instability during mammalian spermatogenesis. PLoS Genet 2011; 7: e1002094.
    • (2011) PLoS Genet , vol.7
    • Holloway, J.K.1    Mohan, S.2    Balmus, G.3
  • 28
    • 0033851758 scopus 로고    scopus 로고
    • Fanconi anemia complementation group C is required for proliferation of murine primordial germ cells
    • Nadler JJ, Braun RE,. Fanconi anemia complementation group C is required for proliferation of murine primordial germ cells. Genesis 2000; 27: 117-123.
    • (2000) Genesis , vol.27 , pp. 117-123
    • Nadler, J.J.1    Braun, R.E.2
  • 33
    • 0037306904 scopus 로고    scopus 로고
    • Cancer incidence in persons with Fanconi anemia
    • DOI 10.1182/blood-2002-05-1498
    • Rosenberg PS, Greene MH, Alter BP,. Cancer incidence in persons with Fanconi anemia. Blood 2003; 101: 822-826. (Pubitemid 36139345)
    • (2003) Blood , vol.101 , Issue.3 , pp. 822-826
    • Rosenberg, P.S.1    Greene, M.H.2    Alter, B.P.3
  • 36
    • 79954595653 scopus 로고    scopus 로고
    • Myelodysplasia and leukemia of Fanconi anemia are associated with a specific pattern of genomic abnormalities that includes cryptic RUNX1/AML1 lesions
    • Quentin S, Cuccuini W, Ceccaldi R, et al., Myelodysplasia and leukemia of Fanconi anemia are associated with a specific pattern of genomic abnormalities that includes cryptic RUNX1/AML1 lesions. Blood 2011; 117: e161-170.
    • (2011) Blood , vol.117
    • Quentin, S.1    Cuccuini, W.2    Ceccaldi, R.3
  • 37
    • 56749181183 scopus 로고    scopus 로고
    • Clinical and molecular characteristics of squamous cell carcinomas from Fanconi anemia patients
    • van Zeeburg HJ, Snijders PJ, Wu T, et al., Clinical and molecular characteristics of squamous cell carcinomas from Fanconi anemia patients. J Natl Cancer Inst 2008; 100: 1649-1653.
    • (2008) J Natl Cancer Inst , vol.100 , pp. 1649-1653
    • Van Zeeburg, H.J.1    Snijders, P.J.2    Wu, T.3
  • 38
    • 42149116279 scopus 로고    scopus 로고
    • Cancer risks in Fanconi anemia: Findings from the German Fanconi Anemia Registry
    • DOI 10.3324/haematol.12234
    • Rosenberg PS, Alter BP, Ebell W,. Cancer risks in Fanconi anemia: findings from the German Fanconi Anemia Registry. Haematologica 2008; 93: 511-517. (Pubitemid 351536378)
    • (2008) Haematologica , vol.93 , Issue.4 , pp. 511-517
    • Rosenberg, P.S.1    Alter, B.P.2    Ebell, W.3
  • 42
    • 13544274012 scopus 로고    scopus 로고
    • In utero origins of childhood leukaemia
    • DOI 10.1016/j.earlhumdev.2004.10.004
    • Greaves M,. In utero origins of childhood leukaemia. Early Hum Dev 2005; 81: 123-129. (Pubitemid 40221990)
    • (2005) Early Human Development , vol.81 , Issue.1 SPEC. ISS. , pp. 123-129
    • Greaves, M.1
  • 43
    • 0000023706 scopus 로고
    • Prenatal origin of childhood leukemia. Evidence from twins
    • Macmahon B, Levy MA,. Prenatal origin of childhood leukemia. Evidence from twins. N Engl J Med 1964; 270: 1082-1085.
    • (1964) N Engl J Med , vol.270 , pp. 1082-1085
    • MacMahon, B.1    Levy, M.A.2
  • 44
    • 0014985528 scopus 로고
    • Deaths from childhood leukemia and solid tumors among twins and other sibs in the United States, 1960-67
    • Miller RW,. Deaths from childhood leukemia and solid tumors among twins and other sibs in the United States, 1960-67. J Natl Cancer Inst 1971; 46: 203-209.
    • (1971) J Natl Cancer Inst , vol.46 , pp. 203-209
    • Miller, R.W.1
  • 45
    • 0036166879 scopus 로고    scopus 로고
    • Risks among siblings and twins for childhood acute lymphoid leukemia: Results from the Swedish Family-Cancer Database [2]
    • DOI 10.1038/sj/leu/2402351
    • Hemminki K, Jiang Y,. Risks among siblings and twins for childhood acute lymphoid leukaemia: results from the Swedish Family Cancer Database. Leukemia 2002; 16: 297-298. (Pubitemid 34145149)
    • (2002) Leukemia , vol.16 , Issue.2 , pp. 297-298
    • Hemminki, K.1    Jiang, Y.2
  • 46
    • 0141482011 scopus 로고    scopus 로고
    • Leukemia in twins: Lessons in natural history
    • DOI 10.1182/blood-2002-12-3817
    • Greaves MF, Maia AT, Wiemels JL, et al., Leukemia in twins: lessons in natural history. Blood 2003; 102: 2321-2333. (Pubitemid 37193565)
    • (2003) Blood , vol.102 , Issue.7 , pp. 2321-2333
    • Greaves, M.F.1    Maia, A.T.2    Wiemels, J.L.3    Ford, A.M.4
  • 47
    • 0015208906 scopus 로고
    • Possible explanation of the high concordance for acute leukaemia in monozygotic twins
    • Clarkson BD, Boyse EA,. Possible explanation of the high concordance for acute leukaemia in monozygotic twins. Lancet 1971; 1: 699-701.
    • (1971) Lancet , vol.1 , pp. 699-701
    • Clarkson, B.D.1    Boyse, E.A.2
  • 48
    • 0141634051 scopus 로고    scopus 로고
    • Origins of chromosome translocations in childhood leukaemia
    • Greaves MF, Wiemels J,. Origins of chromosome translocations in childhood leukaemia. Nat Rev Cancer 2003; 3: 639-649. (Pubitemid 37328819)
    • (2003) Nature Reviews Cancer , vol.3 , Issue.9 , pp. 639-649
    • Greaves, M.F.1    Wiemels, J.2
  • 49
    • 0030023611 scopus 로고    scopus 로고
    • Blood group chimerism in human multiple births is not rare
    • van Dijk BA, Boomsma DI, de Man AJ,. Blood group chimerism in human multiple births is not rare. Am J Med Genet 1996; 61: 264-268.
    • (1996) Am J Med Genet , vol.61 , pp. 264-268
    • Van Dijk, B.A.1    Boomsma, D.I.2    De Man, A.J.3
  • 50
    • 67349107395 scopus 로고    scopus 로고
    • Cellular and molecular consequences of defective Fanconi anemia proteins in replication-coupled DNA repair: Mechanistic insights
    • Thompson LH, Hinz JM,. Cellular and molecular consequences of defective Fanconi anemia proteins in replication-coupled DNA repair: mechanistic insights. Mutat Res 2009; 668: 54-72.
    • (2009) Mutat Res , vol.668 , pp. 54-72
    • Thompson, L.H.1    Hinz, J.M.2
  • 51
    • 34249931173 scopus 로고    scopus 로고
    • Fanconi anemia and DNA replication repair
    • DOI 10.1016/j.dnarep.2007.02.002, PII S1568786407000523, Replication Fork Repair Processes
    • Patel KJ, Joenje H,. Fanconi anemia and DNA replication repair. DNA Repair (Amst) 2007; 6: 885-890. (Pubitemid 46880469)
    • (2007) DNA Repair , vol.6 , Issue.7 , pp. 885-890
    • Patel, K.J.1    Joenje, H.2
  • 52
    • 0030464203 scopus 로고    scopus 로고
    • In vitro formation of DNA adducts by cisplatin, lobaplatin and oxaliplatin in calf thymus DNA in solution and in cultured human cells
    • DOI 10.1093/carcin/17.12.2763
    • Saris CP, van de Vaart PJ, Rietbroek RC, et al., In vitro formation of DNA adducts by cisplatin, lobaplatin and oxaliplatin in calf thymus DNA in solution and in cultured human cells. Carcinogenesis 1996; 17: 2763-2769. (Pubitemid 27037637)
    • (1996) Carcinogenesis , vol.17 , Issue.12 , pp. 2763-2769
    • Saris, C.P.1    Van De Vaart, P.J.M.2    Rietbroek, R.C.3    Blommaert, F.A.4
  • 53
    • 77955692257 scopus 로고    scopus 로고
    • Determination of cisplatin 1,2-intrastrand guanine-guanine DNA adducts in human leukocytes by high-performance liquid chromatography coupled to inductively coupled plasma mass spectrometry
    • Harrington CF, Le Pla RC, Jones GD, et al., Determination of cisplatin 1,2-intrastrand guanine-guanine DNA adducts in human leukocytes by high-performance liquid chromatography coupled to inductively coupled plasma mass spectrometry. Chem Res Toxicol 2010; 23: 1313-1321.
    • (2010) Chem Res Toxicol , vol.23 , pp. 1313-1321
    • Harrington, C.F.1    Le Pla, R.C.2    Jones, G.D.3
  • 54
    • 0017118656 scopus 로고
    • Susceptibility of Fanconi's anaemia fibroblasts to chromosome damage by carcinogens
    • Auerbach AD, Wolman SR,. Susceptibility of Fanconi's anaemia fibroblasts to chromosome damage by carcinogens. Nature 1976; 261: 494-496.
    • (1976) Nature , vol.261 , pp. 494-496
    • Auerbach, A.D.1    Wolman, S.R.2
  • 55
    • 67650500593 scopus 로고    scopus 로고
    • The genetic and molecular basis of Fanconi anemia
    • de Winter JP, Joenje H,. The genetic and molecular basis of Fanconi anemia. Mutat Res 2009; 668: 11-19.
    • (2009) Mutat Res , vol.668 , pp. 11-19
    • De Winter, J.P.1    Joenje, H.2
  • 56
    • 79251632658 scopus 로고    scopus 로고
    • SLX4, a coordinator of structure-specific endonucleases, is mutated in a new Fanconi anemia subtype
    • Stoepker C, Hain K, Schuster B, et al., SLX4, a coordinator of structure-specific endonucleases, is mutated in a new Fanconi anemia subtype. Nat Genet 2011; 43: 138-141.
    • (2011) Nat Genet , vol.43 , pp. 138-141
    • Stoepker, C.1    Hain, K.2    Schuster, B.3
  • 57
    • 79251611165 scopus 로고    scopus 로고
    • Mutations of the SLX4 gene in Fanconi anemia
    • Kim Y, Lach FP, Desetty R, et al., Mutations of the SLX4 gene in Fanconi anemia. Nat Genet 2011; 43: 142-146.
    • (2011) Nat Genet , vol.43 , pp. 142-146
    • Kim, Y.1    Lach, F.P.2    Desetty, R.3
  • 58
    • 77951747926 scopus 로고    scopus 로고
    • Mutation of the RAD51C gene in a Fanconi anemia-like disorder
    • Vaz F, Hanenberg H, Schuster B, et al., Mutation of the RAD51C gene in a Fanconi anemia-like disorder. Nat Genet 2010; 42: 406-409.
    • (2010) Nat Genet , vol.42 , pp. 406-409
    • Vaz, F.1    Hanenberg, H.2    Schuster, B.3
  • 59
    • 0026735882 scopus 로고
    • Cloning of cDNAs for Fanconi's anaemia by functional complementation
    • Strathdee CA, Gavish H, Shannon WR, et al., Cloning of cDNAs for Fanconi's anaemia by functional complementation. Nature 1992; 358: 434.
    • (1992) Nature , vol.358 , pp. 434
    • Strathdee, C.A.1    Gavish, H.2    Shannon, W.R.3
  • 60
    • 0034672154 scopus 로고    scopus 로고
    • Association of complementation group and mutation type with clinical outcome in fanconi anemia. European Fanconi Anemia Research Group
    • Faivre L, Guardiola P, Lewis C, et al., Association of complementation group and mutation type with clinical outcome in fanconi anemia. European Fanconi Anemia Research Group. Blood 2000; 96: 4064-4070.
    • (2000) Blood , vol.96 , pp. 4064-4070
    • Faivre, L.1    Guardiola, P.2    Lewis, C.3
  • 62
    • 0033710326 scopus 로고    scopus 로고
    • Spectrum of mutations in the Fanconi anaemia group G gene, FANCG/XRCC9
    • Demuth I, Wlodarski M, Tipping AJ, et al., Spectrum of mutations in the Fanconi anaemia group G gene, FANCG/XRCC9. Eur J Hum Genet 2000; 8: 861-868.
    • (2000) Eur J Hum Genet , vol.8 , pp. 861-868
    • Demuth, I.1    Wlodarski, M.2    Tipping, A.J.3
  • 64
    • 0032956991 scopus 로고    scopus 로고
    • Variable pathogenicity of exon 43del (FAA) in four Fanconi anaemia patients within a consanguineous family
    • DOI 10.1046/j.1365-2141.1999.01156.x
    • Koc A, Pronk JC, Alikasifoglu M, et al., Variable pathogenicity of exon 43del (FAA) in four Fanconi anaemia patients within a consanguineous family. Br J Haematol 1999; 104: 127-130. (Pubitemid 29037030)
    • (1999) British Journal of Haematology , vol.104 , Issue.1 , pp. 127-130
    • Koc, A.1    Pronk, J.C.2    Alikasifoglu, M.3    Joenje, H.4    Altay, C.5
  • 65
    • 33645741745 scopus 로고    scopus 로고
    • Natural gene therapy in monozygotic twins with Fanconi anemia
    • Mankad A, Taniguchi T, Cox B, et al., Natural gene therapy in monozygotic twins with Fanconi anemia. Blood 2006; 107: 3084-3090.
    • (2006) Blood , vol.107 , pp. 3084-3090
    • Mankad, A.1    Taniguchi, T.2    Cox, B.3
  • 68
    • 70349667196 scopus 로고    scopus 로고
    • Xpf and not the Fanconi anaemia proteins or Rev3 accounts for the extreme resistance to cisplatin in Dictyostelium discoideum
    • Zhang XY, Langenick J, Traynor D, et al., Xpf and not the Fanconi anaemia proteins or Rev3 accounts for the extreme resistance to cisplatin in Dictyostelium discoideum. PLoS Genet 2009; 5: e1000645.
    • (2009) PLoS Genet , vol.5
    • Zhang, X.Y.1    Langenick, J.2    Traynor, D.3
  • 70
    • 2942705849 scopus 로고    scopus 로고
    • Functional interaction of monoubiquitinated FANCD2 and BRCA2/FANCD1 in chromatin
    • DOI 10.1128/MCB.24.13.5850-5862.2004
    • Wang X, Andreassen PR, D'Andrea AD,. Functional interaction of monoubiquitinated FANCD2 and BRCA2/FANCD1 in chromatin. Mol Cell Biol 2004; 24: 5850-5862. (Pubitemid 38787970)
    • (2004) Molecular and Cellular Biology , vol.24 , Issue.13 , pp. 5850-5862
    • Wang, X.1    Andreassen, P.R.2    D'Andrea, A.D.3
  • 74
    • 63049094474 scopus 로고    scopus 로고
    • Monoubiquitylation in the Fanconi anemia DNA damage response pathway
    • Alpi AF, Patel KJ,. Monoubiquitylation in the Fanconi anemia DNA damage response pathway. DNA Repair (Amst) 2009; 8: 430-435.
    • (2009) DNA Repair (Amst) , vol.8 , pp. 430-435
    • Alpi, A.F.1    Patel, K.J.2
  • 79
    • 33744958660 scopus 로고    scopus 로고
    • The WD40 repeats of FANCL are required for Fanconi anemia core complex assembly
    • DOI 10.1074/jbc.M511411200
    • Gurtan AM, Stuckert P, D'Andrea AD,. The WD40 repeats of FANCL are required for Fanconi anemia core complex assembly. J Biol Chem 2006; 281: 10896-10905. (Pubitemid 43855513)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.16 , pp. 10896-10905
    • Gurtan, A.M.1    Stuckert, P.2    D'Andrea, A.D.3
  • 81
    • 79960539404 scopus 로고    scopus 로고
    • Structure of the FANCI-FANCD2 complex: Insights into the Fanconi anemia DNA repair pathway
    • Joo W, Xu G, Persky NS, et al., Structure of the FANCI-FANCD2 complex: insights into the Fanconi anemia DNA repair pathway. Science 2011; 333: 312-316.
    • (2011) Science , vol.333 , pp. 312-316
    • Joo, W.1    Xu, G.2    Persky, N.S.3
  • 82
    • 55549137026 scopus 로고    scopus 로고
    • FANCI phosphorylation functions as a molecular switch to turn on the Fanconi anemia pathway
    • Ishiai M, Kitao H, Smogorzewska A, et al., FANCI phosphorylation functions as a molecular switch to turn on the Fanconi anemia pathway. Nat Struct Mol Biol 2008; 15: 1138-1146.
    • (2008) Nat Struct Mol Biol , vol.15 , pp. 1138-1146
    • Ishiai, M.1    Kitao, H.2    Smogorzewska, A.3
  • 83
    • 4344597147 scopus 로고    scopus 로고
    • The Fanconi anaemia gene FANCC promotes homologous recombination and error-prone DNA repair
    • DOI 10.1016/j.molcel.2004.08.009, PII S1097276504004502
    • Niedzwiedz W, Mosedale G, Johnson M, et al., The Fanconi anaemia gene FANCC promotes homologous recombination and error-prone DNA repair. Mol Cell 2004; 15: 607-620. (Pubitemid 39141787)
    • (2004) Molecular Cell , vol.15 , Issue.4 , pp. 607-620
    • Niedzwiedz, W.1    Mosedale, G.2    Johnson, M.3    Ong, C.Y.4    Pace, P.5    Patel, K.J.6
  • 85
    • 67949085157 scopus 로고    scopus 로고
    • The Walker B motif in avian FANCM is required to limit sister chromatid exchanges but is dispensable for DNA crosslink repair
    • Rosado IV, Niedzwiedz W, Alpi AF, et al., The Walker B motif in avian FANCM is required to limit sister chromatid exchanges but is dispensable for DNA crosslink repair. Nucleic Acids Res 2009; 37: 4360-4370.
    • (2009) Nucleic Acids Res , vol.37 , pp. 4360-4370
    • Rosado, I.V.1    Niedzwiedz, W.2    Alpi, A.F.3
  • 86
    • 25144503943 scopus 로고    scopus 로고
    • The BRIP1 helicase functions independently of BRCA1 in the Fanconi anemia pathway for DNA crosslink repair
    • DOI 10.1038/ng1627, PII NG1627
    • Bridge WL, Vandenberg CJ, Franklin RJ, et al., The BRIP1 helicase functions independently of BRCA1 in the Fanconi anemia pathway for DNA crosslink repair. Nat Genet 2005; 37: 953-957. (Pubitemid 43086151)
    • (2005) Nature Genetics , vol.37 , Issue.9 , pp. 953-957
    • Bridge, W.L.1    Vandenberg, C.J.2    Franklin, R.J.3    Hiom, K.4
  • 89
    • 0037388452 scopus 로고    scopus 로고
    • Rev1 is essential for DNA damage tolerance and non-templated immunoglobulin gene mutation in a vertebrate cell line
    • DOI 10.1093/emboj/cdg161
    • Simpson LJ, Sale JE,. Rev1 is essential for DNA damage tolerance and non-templated immunoglobulin gene mutation in a vertebrate cell line. EMBO J 2003; 22: 1654-1664. (Pubitemid 36417413)
    • (2003) EMBO Journal , vol.22 , Issue.7 , pp. 1654-1664
    • Simpson, L.J.1    Sale, J.E.2
  • 90
    • 33751050806 scopus 로고    scopus 로고
    • A role for PCNA ubiquitination in immunoglobulin hypermutation
    • Arakawa H, Moldovan GL, Saribasak H, et al., A role for PCNA ubiquitination in immunoglobulin hypermutation. PLoS Biol 2006; 4: e366.
    • (2006) PLoS Biol , vol.4
    • Arakawa, H.1    Moldovan, G.L.2    Saribasak, H.3
  • 91
    • 0029787108 scopus 로고    scopus 로고
    • Deoxycytidyl transferase activity of yeast REV1 protein
    • DOI 10.1038/382729a0
    • Nelson JR, Lawrence CW, Hinkle DC,. Deoxycytidyl transferase activity of yeast REV1 protein. Nature 1996; 382: 729-731. (Pubitemid 26282181)
    • (1996) Nature , vol.382 , Issue.6593 , pp. 729-731
    • Nelson, J.R.1    Lawrence, C.W.2    Hinkle, D.C.3
  • 92
    • 14844362615 scopus 로고    scopus 로고
    • Vertebrate DNA damage tolerance requires the C-terminus but not BRCT or transferase domains of REV1
    • DOI 10.1093/nar/gki279
    • Ross AL, Simpson LJ, Sale JE,. Vertebrate DNA damage tolerance requires the C-terminus but not BRCT or transferase domains of REV1. Nucleic Acids Res 2005; 33: 1280-1289. (Pubitemid 41439921)
    • (2005) Nucleic Acids Research , vol.33 , Issue.4 , pp. 1280-1289
    • Ross, A.-L.1    Simpson, L.J.2    Sale, J.E.3
  • 94
    • 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, et al., 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: 7980-7990.
    • (2000) Mol Cell Biol , vol.20 , pp. 7980-7990
    • De Silva, I.U.1    McHugh, P.J.2    Clingen, P.H.3
  • 95
    • 51549098159 scopus 로고    scopus 로고
    • Mechanism of replication-coupled DNA interstrand crosslink repair
    • Raschle M, Knipscheer P, Enoiu M, et al., Mechanism of replication-coupled DNA interstrand crosslink repair. Cell 2008; 134: 969-980.
    • (2008) Cell , vol.134 , pp. 969-980
    • Raschle, M.1    Knipscheer, P.2    Enoiu, M.3
  • 96
    • 72949123930 scopus 로고    scopus 로고
    • The Fanconi anemia pathway promotes replication-dependent DNA interstrand cross-link repair
    • Knipscheer P, Raschle M, Smogorzewska A, et al., The Fanconi anemia pathway promotes replication-dependent DNA interstrand cross-link repair. Science 2009; 326: 1698-1701.
    • (2009) Science , vol.326 , pp. 1698-1701
    • Knipscheer, P.1    Raschle, M.2    Smogorzewska, A.3
  • 97
    • 79959843168 scopus 로고    scopus 로고
    • Mechanism of RAD51-dependent DNA interstrand cross-link repair
    • Long DT, Raschle M, Joukov V, et al., Mechanism of RAD51-dependent DNA interstrand cross-link repair. Science 2011; 333: 84-87.
    • (2011) Science , vol.333 , pp. 84-87
    • Long, D.T.1    Raschle, M.2    Joukov, V.3
  • 98
    • 69749095427 scopus 로고    scopus 로고
    • Checkpoint signaling from a single DNA interstrand crosslink
    • Ben-Yehoyada M, Wang LC, Kozekov ID, et al., Checkpoint signaling from a single DNA interstrand crosslink. Mol Cell 2009; 35: 704-715.
    • (2009) Mol Cell , vol.35 , pp. 704-715
    • Ben-Yehoyada, M.1    Wang, L.C.2    Kozekov, I.D.3
  • 99
    • 77954279611 scopus 로고    scopus 로고
    • Deficiency of FANCD2-associated nuclease KIAA1018/FAN1 sensitizes cells to interstrand crosslinking agents
    • Kratz K, Schopf B, Kaden S, et al., Deficiency of FANCD2-associated nuclease KIAA1018/FAN1 sensitizes cells to interstrand crosslinking agents. Cell 2010; 142: 77-88.
    • (2010) Cell , vol.142 , pp. 77-88
    • Kratz, K.1    Schopf, B.2    Kaden, S.3
  • 100
    • 77955290719 scopus 로고    scopus 로고
    • FAN1 acts with FANCI-FANCD2 to promote DNA interstrand cross-link repair
    • Liu T, Ghosal G, Yuan J, et al., FAN1 acts with FANCI-FANCD2 to promote DNA interstrand cross-link repair. Science 2010; 329: 693-696.
    • (2010) Science , vol.329 , pp. 693-696
    • Liu, T.1    Ghosal, G.2    Yuan, J.3
  • 101
    • 77954274685 scopus 로고    scopus 로고
    • Identification of KIAA1018/FAN1, a DNA repair nuclease recruited to DNA damage by monoubiquitinated FANCD2
    • MacKay C, Declais AC, Lundin C, et al., Identification of KIAA1018/FAN1, a DNA repair nuclease recruited to DNA damage by monoubiquitinated FANCD2. Cell 2010; 142: 65-76.
    • (2010) Cell , vol.142 , pp. 65-76
    • MacKay, C.1    Declais, A.C.2    Lundin, C.3
  • 102
    • 77954286076 scopus 로고    scopus 로고
    • A genetic screen identifies FAN1, a Fanconi anemia-associated nuclease necessary for DNA interstrand crosslink repair
    • Smogorzewska A, Desetty R, Saito TT, et al., A genetic screen identifies FAN1, a Fanconi anemia-associated nuclease necessary for DNA interstrand crosslink repair. Mol Cell 2010; 39: 36-47.
    • (2010) Mol Cell , vol.39 , pp. 36-47
    • Smogorzewska, A.1    Desetty, R.2    Saito, T.T.3
  • 103
    • 78650734182 scopus 로고    scopus 로고
    • KIAA1018/FAN1 nuclease protects cells against genomic instability induced by interstrand cross-linking agents
    • Yoshikiyo K, Kratz K, Hirota K, et al., KIAA1018/FAN1 nuclease protects cells against genomic instability induced by interstrand cross-linking agents. Proc Natl Acad Sci USA 2010; 107: 21553-21557.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 21553-21557
    • Yoshikiyo, K.1    Kratz, K.2    Hirota, K.3
  • 104
    • 34848861407 scopus 로고    scopus 로고
    • Human Mus81 and FANCB independently contribute to repair of DNA damage during replication
    • DOI 10.1111/j.1365-2443.2007.01124.x
    • Nomura Y, Adachi N, Koyama H,. Human Mus81 and FANCB independently contribute to repair of DNA damage during replication. Genes Cells 2007; 12: 1111-1122. (Pubitemid 47500525)
    • (2007) Genes to Cells , vol.12 , Issue.10 , pp. 1111-1122
    • Nomura, Y.1    Adachi, N.2    Koyama, H.3
  • 105
    • 33750206776 scopus 로고    scopus 로고
    • The structure-specific endonuclease Mus81-Eme1 promotes conversion of interstrand DNA crosslinks into double-strands breaks
    • DOI 10.1038/sj.emboj.7601344, PII 7601344
    • Hanada K, Budzowska M, Modesti M, et al., The structure-specific endonuclease Mus81-Eme1 promotes conversion of interstrand DNA crosslinks into double-strands breaks. EMBO J 2006; 25: 4921-4932. (Pubitemid 44607036)
    • (2006) EMBO Journal , 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    Kanaar, R.7
  • 106
    • 23844468833 scopus 로고    scopus 로고
    • Disruption of murine Mus81 increases genomic instability and DNA damage sensitivity but does not promote tumorigenesis
    • DOI 10.1128/MCB.25.17.7569-7579.2005
    • Dendouga N, Gao H, Moechars D, et al., Disruption of murine Mus81 increases genomic instability and DNA damage sensitivity but does not promote tumorigenesis. Mol Cell Biol 2005; 25: 7569-7579. (Pubitemid 41170119)
    • (2005) Molecular and Cellular Biology , vol.25 , Issue.17 , pp. 7569-7579
    • Dendouga, N.1    Gao, H.2    Moechars, D.3    Janicot, M.4    Vialard, J.5    McGowan, C.H.6
  • 110
    • 38349098477 scopus 로고    scopus 로고
    • The ERCC1/XPF endonuclease is required for efficient single-strand annealing and gene conversion in mammalian cells
    • Al-Minawi AZ, Saleh-Gohari N, Helleday T,. The ERCC1/XPF endonuclease is required for efficient single-strand annealing and gene conversion in mammalian cells. Nucleic Acids Res 2008; 36: 1-9.
    • (2008) Nucleic Acids Res , vol.36 , pp. 1-9
    • Al-Minawi, A.Z.1    Saleh-Gohari, N.2    Helleday, T.3
  • 111
    • 0027225340 scopus 로고
    • Yeast DNA repair and recombination proteins Rad1 and Rad10 constitute a single-strand-DNA endonuclease
    • DOI 10.1038/362860a0
    • Tomkinson AE, Bardwell AJ, Bardwell L, et al., Yeast DNA repair and recombination proteins Rad1 and Rad10 constitute a single-stranded-DNA endonuclease. Nature 1993; 362: 860-862. (Pubitemid 23132166)
    • (1993) Nature , vol.362 , Issue.6423 , pp. 860-862
    • Tomkinson, A.E.1    Bardwell, A.J.2    Bardwell, L.3    Tappe, N.J.4    Friedberg, E.C.5
  • 112
    • 0027943565 scopus 로고
    • Specific cleavage of model recombination and repair intermediates by the yeast Rad1-Rad10 DNA endonuclease
    • Bardwell AJ, Bardwell L, Tomkinson AE, et al., Specific cleavage of model recombination and repair intermediates by the yeast Rad1-Rad10 DNA endonuclease. Science 1994; 265: 2082-2085. (Pubitemid 24325688)
    • (1994) Science , vol.265 , Issue.5181 , pp. 2082-2085
    • Bardwell, A.J.1    Bardwell, L.2    Tomkinson, A.E.3    Friedberg, E.C.4
  • 113
    • 0027378895 scopus 로고
    • Mice with DNA repair gene (ERCC-1) deficiency have elevated levels of p53, liver nuclear abnormalities and die before weaning
    • DOI 10.1038/ng1193-217
    • McWhir J, Selfridge J, Harrison DJ, et al., Mice with DNA repair gene (ERCC-1) deficiency have elevated levels of p53, liver nuclear abnormalities and die before weaning. Nat Genet 1993; 5: 217-224. (Pubitemid 23330382)
    • (1993) Nature Genetics , vol.5 , Issue.3 , pp. 217-224
    • McWhir, J.1    Selfridge, J.2    Harrison, D.J.3    Squires, S.4    Melton, D.W.5
  • 114
    • 1542309071 scopus 로고    scopus 로고
    • Growth Retardation, Early Death, and DNA Repair Defects in Mice Deficient for the Nucleotide Excision Repair Enzyme XPF
    • DOI 10.1128/MCB.24.3.1200-1205.2004
    • Tian M, Shinkura R, Shinkura N, et al., Growth retardation, early death, and DNA repair defects in mice deficient for the nucleotide excision repair enzyme XPF. Mol Cell Biol 2004; 24: 1200-1205. (Pubitemid 38112182)
    • (2004) Molecular and Cellular Biology , vol.24 , Issue.3 , pp. 1200-1205
    • Tian, M.1    Shinkura, R.2    Shinkura, N.3    Alt, F.W.4
  • 116
    • 71949083551 scopus 로고    scopus 로고
    • XPF-ERCC1 participates in the Fanconi anemia pathway of cross-link repair
    • Bhagwat N, Olsen AL, Wang AT, et al., XPF-ERCC1 participates in the Fanconi anemia pathway of cross-link repair. Mol Cell Biol 2009; 29: 6427-6437.
    • (2009) Mol Cell Biol , vol.29 , pp. 6427-6437
    • Bhagwat, N.1    Olsen, A.L.2    Wang, A.T.3
  • 118
    • 0037266378 scopus 로고    scopus 로고
    • DNA repair gene Ercc1 is essential for normal spermatogenesis and oogenesis and for functional integrity of germ cell DNA in the mouse
    • DOI 10.1242/dev.00221
    • Hsia KT, Millar MR, King S, et al., DNA repair gene Ercc1 is essential for normal spermatogenesis and oogenesis and for functional integrity of germ cell DNA in the mouse. Development 2003; 130: 369-378. (Pubitemid 36181491)
    • (2003) Development , vol.130 , Issue.2 , pp. 369-378
    • Hsia, K.-T.1    Millar, M.R.2    King, S.3    Selfridge, J.4    Redhead, N.J.5    Melton, D.W.6    Saunders, P.T.K.7
  • 119
    • 50649091874 scopus 로고    scopus 로고
    • Structural and functional relationships of the XPF/MUS81 family of proteins
    • Ciccia A, McDonald N, West SC,. Structural and functional relationships of the XPF/MUS81 family of proteins. Annu Rev Biochem 2008; 77: 259-287.
    • (2008) Annu Rev Biochem , vol.77 , pp. 259-287
    • Ciccia, A.1    McDonald, N.2    West, S.C.3
  • 121
    • 38349150057 scopus 로고    scopus 로고
    • Processing of a psoralen DNA interstrand cross-link by XPF-ERCC1 complex in vitro
    • Fisher LA, Bessho M, Bessho T,. Processing of a psoralen DNA interstrand cross-link by XPF-ERCC1 complex in vitro. J Biol Chem 2008; 283: 1275-1281.
    • (2008) J Biol Chem , vol.283 , pp. 1275-1281
    • Fisher, L.A.1    Bessho, M.2    Bessho, T.3
  • 122
    • 67649655402 scopus 로고    scopus 로고
    • Human SLX4 is a Holliday junction resolvase subunit that binds multiple DNA repair/recombination endonucleases
    • Fekairi S, Scaglione S, Chahwan C, et al., Human SLX4 is a Holliday junction resolvase subunit that binds multiple DNA repair/recombination endonucleases. Cell 2009; 138: 78-89.
    • (2009) Cell , vol.138 , pp. 78-89
    • Fekairi, S.1    Scaglione, S.2    Chahwan, C.3
  • 123
    • 67649662604 scopus 로고    scopus 로고
    • Mammalian BTBD12/SLX4 assembles a Holliday junction resolvase and is required for DNA repair
    • Svendsen JM, Smogorzewska A, Sowa ME, et al., Mammalian BTBD12/SLX4 assembles a Holliday junction resolvase and is required for DNA repair. Cell 2009; 138: 63-77.
    • (2009) Cell , vol.138 , pp. 63-77
    • Svendsen, J.M.1    Smogorzewska, A.2    Sowa, M.E.3
  • 124
    • 67649641641 scopus 로고    scopus 로고
    • Coordination of structure-specific nucleases by human SLX4/BTBD12 is required for DNA repair
    • Munoz IM, Hain K, Declais AC, et al., Coordination of structure-specific nucleases by human SLX4/BTBD12 is required for DNA repair. Mol Cell 2009; 35: 116-127.
    • (2009) Mol Cell , vol.35 , pp. 116-127
    • Munoz, I.M.1    Hain, K.2    Declais, A.C.3
  • 125
    • 67649655954 scopus 로고    scopus 로고
    • Drosophila MUS312 and the vertebrate ortholog BTBD12 interact with DNA structure-specific endonucleases in DNA repair and recombination
    • Andersen SL, Bergstralh DT, Kohl KP, et al., Drosophila MUS312 and the vertebrate ortholog BTBD12 interact with DNA structure-specific endonucleases in DNA repair and recombination. Mol Cell 2009; 35: 128-135.
    • (2009) Mol Cell , vol.35 , pp. 128-135
    • Andersen, S.L.1    Bergstralh, D.T.2    Kohl, K.P.3
  • 126
    • 0035148955 scopus 로고    scopus 로고
    • Requirement for three novel protein complexes in the absence of the Sgs1 DNA helicase in Saccharomyces cerevisiae
    • Mullen JR, Kaliraman V, Ibrahim SS, et al., Requirement for three novel protein complexes in the absence of the Sgs1 DNA helicase in Saccharomyces cerevisiae. Genetics 2001; 157: 103-118.
    • (2001) Genetics , vol.157 , pp. 103-118
    • Mullen, J.R.1    Kaliraman, V.2    Ibrahim, S.S.3
  • 127
    • 33846443975 scopus 로고    scopus 로고
    • + ATPase and cytosolic acidification in sensitivity to DNA-damaging agents such as cisplatin
    • DOI 10.1124/mol.106.030494
    • + ATPase and cytosolic acidification in sensitivity to DNA-damaging agents such as cisplatin. Mol Pharmacol 2007; 71: 416-425. (Pubitemid 46147908)
    • (2007) Molecular Pharmacology , vol.71 , Issue.2 , pp. 416-425
    • Liao, C.1    Hu, B.2    Arno, M.J.3    Panaretou, B.4
  • 128
    • 79955580794 scopus 로고    scopus 로고
    • Involvement of SLX4 in interstrand cross-link repair is regulated by the Fanconi anemia pathway
    • Yamamoto KN, Kobayashi S, Tsuda M, et al., Involvement of SLX4 in interstrand cross-link repair is regulated by the Fanconi anemia pathway. Proc Natl Acad Sci USA 2011; 108: 6492-6496.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 6492-6496
    • Yamamoto, K.N.1    Kobayashi, S.2    Tsuda, M.3
  • 129
    • 27444444448 scopus 로고    scopus 로고
    • Slx4 becomes phosphorylated after DNA damage in a Mec1/Tel1-dependent manner and is required for repair of DNA alkylation damage
    • DOI 10.1042/BJ20050768
    • Flott S, Rouse J,. Slx4 becomes phosphorylated after DNA damage in a Mec1/Tel1-dependent manner and is required for repair of DNA alkylation damage. Biochem J 2005; 391: 325-333. (Pubitemid 41532430)
    • (2005) Biochemical Journal , vol.391 , Issue.2 , pp. 325-333
    • Flott, S.1    Rouse, J.2
  • 130
    • 0031832670 scopus 로고    scopus 로고
    • Characterization of molecular defects in xeroderma pigmentosum group F in relation to its clinically mild symptoms
    • DOI 10.1093/hmg/7.6.969
    • Matsumura Y, Nishigori C, Yagi T, et al., Characterization of molecular defects in xeroderma pigmentosum group F in relation to its clinically mild symptoms. Hum Mol Genet 1998; 7: 969-974. (Pubitemid 28256589)
    • (1998) Human Molecular Genetics , vol.7 , Issue.6 , pp. 969-974
    • Matsumura, Y.1    Nishigori, C.2    Yagi, T.3    Imamura, S.4    Takebe, H.5
  • 133
    • 77950487121 scopus 로고    scopus 로고
    • The XPA-binding domain of ERCC1 is required for nucleotide excision repair but not other DNA repair pathways
    • Orelli B, McClendon TB, Tsodikov OV, et al., The XPA-binding domain of ERCC1 is required for nucleotide excision repair but not other DNA repair pathways. J Biol Chem 2010; 285: 3705-3712.
    • (2010) J Biol Chem , vol.285 , pp. 3705-3712
    • Orelli, B.1    McClendon, T.B.2    Tsodikov, O.V.3
  • 135
    • 79960037006 scopus 로고    scopus 로고
    • Fancd2 counteracts the toxic effects of naturally produced aldehydes in mice
    • Langevin F, Crossan GP, Rosado IV, et al., Fancd2 counteracts the toxic effects of naturally produced aldehydes in mice. Nature 2011; 475: 53-58.
    • (2011) Nature , vol.475 , pp. 53-58
    • Langevin, F.1    Crossan, G.P.2    Rosado, I.V.3
  • 136
    • 82955235602 scopus 로고    scopus 로고
    • Essential requirement for formaldehyde catabolism in Fanconi anaemia DNA repair pathway deficient cells
    • (in press)
    • Rosado IV, Langevin F, Crossan GP, et al., Essential requirement for formaldehyde catabolism in Fanconi anaemia DNA repair pathway deficient cells. Nat Struct Mol Biol 2011; (in press).
    • (2011) Nat Struct Mol Biol
    • Rosado, I.V.1    Langevin, F.2    Crossan, G.P.3
  • 137
    • 28144464890 scopus 로고    scopus 로고
    • Aldehyde sources, metabolism, molecular toxicity mechanisms, and possible effects on human health
    • DOI 10.1080/10408440591002183, PII J308373361196
    • O'Brien PJ, Siraki AG, Shangari N,. Aldehyde sources, metabolism, molecular toxicity mechanisms, and possible effects on human health. Crit Rev Toxicol 2005; 35: 609-662. (Pubitemid 41693601)
    • (2005) Critical Reviews in Toxicology , vol.35 , Issue.7 , pp. 609-662
    • O'Brien, P.1    Siraki, A.2    Shangari, N.3
  • 138
    • 0033725545 scopus 로고    scopus 로고
    • Identification of DNA adducts of acetaldehyde
    • Wang M, McIntee EJ, Cheng G, et al., Identification of DNA adducts of acetaldehyde. Chem Res Toxicol 2000; 13: 1149-1157.
    • (2000) Chem Res Toxicol , vol.13 , pp. 1149-1157
    • Wang, M.1    McIntee, E.J.2    Cheng, G.3
  • 140
    • 79959203849 scopus 로고    scopus 로고
    • [13C2]-acetaldehyde promotes unequivocal formation of 1,N2 - Propano - 2′-deoxyguanosine in human cells
    • Garcia CC, Angeli JP, Freitas FP, et al., [13C2]-acetaldehyde promotes unequivocal formation of 1,N2-propano-2′-deoxyguanosine in human cells. J Am Chem Soc 2011; 133: 9140-9143.
    • (2011) J Am Chem Soc , vol.133 , pp. 9140-9143
    • Garcia, C.C.1    Angeli, J.P.2    Freitas, F.P.3
  • 141
    • 0037330015 scopus 로고    scopus 로고
    • Reactions of formaldehyde plus acetaldehyde with deoxyguanosine and DNA: Formation of cyclic deoxyguanosine adducts and formaldehyde cross-links
    • DOI 10.1021/tx025614r
    • Cheng G, Shi Y, Sturla SJ, et al., Reactions of formaldehyde plus acetaldehyde with deoxyguanosine and DNA: formation of cyclic deoxyguanosine adducts and formaldehyde cross-links. Chem Res Toxicol 2003; 16: 145-152. (Pubitemid 36245864)
    • (2003) Chemical Research in Toxicology , vol.16 , Issue.2 , pp. 145-152
    • Cheng, G.1    Shi, Y.2    Sturla, S.J.3    Jalas, J.R.4    McIntee, E.J.5    Villalta, P.W.6    Wang, M.7    Hecht, S.S.8
  • 142
    • 1842337370 scopus 로고    scopus 로고
    • Expression cloning of a cDNA for the major Fanconi anaemia gene, FAA
    • Lo Ten Foe JR, Rooimans MA, Bosnoyan-Collins L, et al., Expression cloning of a cDNA for the major Fanconi anaemia gene, FAA. Nat Genet 1996; 14: 320-323.
    • (1996) Nat Genet , vol.14 , pp. 320-323
    • Lo Ten Foe, J.R.1    Rooimans, M.A.2    Bosnoyan-Collins, L.3
  • 143
    • 10944239213 scopus 로고    scopus 로고
    • X-linked inheritance of Fanconi anemia complementation group B
    • Meetei AR, Levitus M, Xue Y, et al., X-linked inheritance of Fanconi anemia complementation group B. Nat Genet 2004; 36: 1219-1224.
    • (2004) Nat Genet , vol.36 , pp. 1219-1224
    • Meetei, A.R.1    Levitus, M.2    Xue, Y.3
  • 144
    • 0026521238 scopus 로고
    • Cloning of cDNAs for Fanconi's anaemia by functional complementation
    • Strathdee CA, Gavish H, Shannon WR, et al., Cloning of cDNAs for Fanconi's anaemia by functional complementation. Nature 1992; 356: 763-767.
    • (1992) Nature , vol.356 , pp. 763-767
    • Strathdee, C.A.1    Gavish, H.2    Shannon, W.R.3
  • 147
    • 77953879925 scopus 로고    scopus 로고
    • Ku70 corrupts DNA repair in the absence of the Fanconi anemia pathway
    • Pace P, Mosedale G, Hodskinson MR, et al., Ku70 corrupts DNA repair in the absence of the Fanconi anemia pathway. Science 2010; 329: 219-223.
    • (2010) Science , vol.329 , pp. 219-223
    • Pace, P.1    Mosedale, G.2    Hodskinson, M.R.3
  • 149
  • 151
    • 33745200945 scopus 로고    scopus 로고
    • Control of BRCA2 cellular and clinical functions by a nuclear partner, PALB2
    • Xia B, Sheng Q, Nakanishi K, et al., Control of BRCA2 cellular and clinical functions by a nuclear partner, PALB2. Mol Cell 2006; 22: 719-729.
    • (2006) Mol Cell , vol.22 , pp. 719-729
    • Xia, B.1    Sheng, Q.2    Nakanishi, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.