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Volumn 668, Issue 1-2, 2009, Pages 54-72

Cellular and molecular consequences of defective Fanconi anemia proteins in replication-coupled DNA repair: Mechanistic insights

Author keywords

Chromosomal instability; Crosslink repair; DNA crosslinking; DNA replication forks; Homologous recombination repair; Mutagenesis; Translesion synthesis

Indexed keywords

ATR PROTEIN; BRCA1 PROTEIN; DIHYDROFOLATE REDUCTASE; DNA; EXCISION REPAIR CROSS COMPLEMENTING PROTEIN 1; FANCONI ANEMIA A ASSOCIATED PROTEIN 100; FANCONI ANEMIA A ASSOCIATED PROTEIN 24; FANCONI ANEMIA GROUP A PROTEIN; FANCONI ANEMIA GROUP B PROTEIN; FANCONI ANEMIA GROUP C PROTEIN; FANCONI ANEMIA GROUP D2 PROTEIN; FANCONI ANEMIA GROUP E PROTEIN; FANCONI ANEMIA GROUP F PROTEIN; FANCONI ANEMIA GROUP G PROTEIN; FANCONI ANEMIA GROUP I PROTEIN; FANCONI ANEMIA GROUP J PROTEIN; FANCONI ANEMIA GROUP L PROTEIN; FANCONI ANEMIA GROUP M PROTEIN; FANCONI ANEMIA GROUP N PROTEIN; FANCONI ANEMIA PROTEIN; HYPOXANTHINE PHOSPHORIBOSYLTRANSFERASE; NIBRIN; RAD51 PROTEIN; UNCLASSIFIED DRUG;

EID: 67349107395     PISSN: 00275107     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mrfmmm.2009.02.003     Document Type: Review
Times cited : (129)

References (283)
  • 1
    • 33750342243 scopus 로고
    • Hypothesis of chromosomal translocation as a genetic interpretation of Fanconi's familial constitutional panmyelopathy
    • Fanconi G. Hypothesis of chromosomal translocation as a genetic interpretation of Fanconi's familial constitutional panmyelopathy. Helv. Paediatr. Acta 19 (1964) 29-33
    • (1964) Helv. Paediatr. Acta , vol.19 , pp. 29-33
    • Fanconi, G.1
  • 2
    • 0037439356 scopus 로고    scopus 로고
    • Cancer in Fanconi anemia, 1927-2001
    • Alter B.P. Cancer in Fanconi anemia, 1927-2001. Cancer 97 (2003) 425-440
    • (2003) Cancer , vol.97 , pp. 425-440
    • Alter, B.P.1
  • 4
    • 33749023325 scopus 로고    scopus 로고
    • Fanconi anaemia genes and susceptibility to cancer
    • Mathew C.G. Fanconi anaemia genes and susceptibility to cancer. Oncogene 25 (2006) 5875-5884
    • (2006) Oncogene , vol.25 , pp. 5875-5884
    • Mathew, C.G.1
  • 5
    • 34548759123 scopus 로고    scopus 로고
    • Emergence of a DNA-damage response network consisting of Fanconi anaemia and BRCA proteins
    • Wang W. Emergence of a DNA-damage response network consisting of Fanconi anaemia and BRCA proteins. Nat. Rev. Genet. 8 (2007) 735-748
    • (2007) Nat. Rev. Genet. , vol.8 , pp. 735-748
    • Wang, W.1
  • 6
    • 34249931173 scopus 로고    scopus 로고
    • Fanconi anemia and DNA replication repair
    • Patel K.J., and Joenje H. Fanconi anemia and DNA replication repair. DNA Repair (Amst.) 6 (2007) 885-890
    • (2007) DNA Repair (Amst.) , vol.6 , pp. 885-890
    • Patel, K.J.1    Joenje, H.2
  • 7
    • 33747883762 scopus 로고    scopus 로고
    • Dedicated to the core: understanding the Fanconi anemia complex
    • Gurtan A.M., and D'Andrea A.D. Dedicated to the core: understanding the Fanconi anemia complex. DNA Repair 5 (2006) 1119-1125
    • (2006) DNA Repair , vol.5 , pp. 1119-1125
    • Gurtan, A.M.1    D'Andrea, A.D.2
  • 8
    • 33744481750 scopus 로고    scopus 로고
    • The molecular pathogenesis of Fanconi anemia: recent progress
    • Taniguchi T., and D'Andrea A.D. The molecular pathogenesis of Fanconi anemia: recent progress. Blood 107 (2006) 4223-4233
    • (2006) Blood , vol.107 , pp. 4223-4233
    • Taniguchi, T.1    D'Andrea, A.D.2
  • 9
    • 0031927305 scopus 로고    scopus 로고
    • Is Fanconi anemia caused by a defect in the processing of DNA damage?
    • Buchwald M., and Moustacchi E. Is Fanconi anemia caused by a defect in the processing of DNA damage?. Mutat. Res. 408 (1998) 75-90
    • (1998) Mutat. Res. , vol.408 , pp. 75-90
    • Buchwald, M.1    Moustacchi, E.2
  • 10
    • 33646366385 scopus 로고    scopus 로고
    • The Fanconi anemia pathway of genomic maintenance
    • Levitus M., Joenje H., and de Winter J.P. The Fanconi anemia pathway of genomic maintenance. Cell. Oncol. 28 (2006) 3-29
    • (2006) Cell. Oncol. , vol.28 , pp. 3-29
    • Levitus, M.1    Joenje, H.2    de Winter, J.P.3
  • 12
    • 38349050087 scopus 로고    scopus 로고
    • The Fanconi anemia protein FANCM can promote branch migration of Holliday junctions and replication forks
    • Gari K., Decaillet C., Stasiak A.Z., Stasiak A., and Constantinou A. The Fanconi anemia protein FANCM can promote branch migration of Holliday junctions and replication forks. Mol. Cell 29 (2008) 141-148
    • (2008) Mol. Cell , vol.29 , pp. 141-148
    • Gari, K.1    Decaillet, C.2    Stasiak, A.Z.3    Stasiak, A.4    Constantinou, A.5
  • 13
    • 44349174992 scopus 로고    scopus 로고
    • FANCM of the Fanconi anemia core complex is required for both monoubiquitination and DNA repair
    • Xue Y., Li Y., Guo R., Ling C., and Wang W. FANCM of the Fanconi anemia core complex is required for both monoubiquitination and DNA repair. Hum. Mol. Genet. 17 (2008) 1641-1652
    • (2008) Hum. Mol. Genet. , vol.17 , pp. 1641-1652
    • Xue, Y.1    Li, Y.2    Guo, R.3    Ling, C.4    Wang, W.5
  • 14
    • 46749106037 scopus 로고    scopus 로고
    • Cell cycle-dependent chromatin loading of the Fanconi anemia core complex by FANCM/FAAP24
    • Kim J.M., Kee Y., Gurtan A., and D'Andrea A.D. Cell cycle-dependent chromatin loading of the Fanconi anemia core complex by FANCM/FAAP24. Blood 111 (2008) 5215-5222
    • (2008) Blood , vol.111 , pp. 5215-5222
    • Kim, J.M.1    Kee, Y.2    Gurtan, A.3    D'Andrea, A.D.4
  • 16
    • 2942664480 scopus 로고    scopus 로고
    • FANCL replaces BRCA1 as the likely ubiquitin ligase responsible for FANCD2 monoubiquitination
    • Meetei A.R., Yan Z., and Wang W. FANCL replaces BRCA1 as the likely ubiquitin ligase responsible for FANCD2 monoubiquitination. Cell Cycle 3 (2004) 179-181
    • (2004) Cell Cycle , vol.3 , pp. 179-181
    • Meetei, A.R.1    Yan, Z.2    Wang, W.3
  • 25
    • 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., Andreassen P.R., and Cantor S.B. BACH1 is critical for homologous recombination and appears to be the Fanconi anemia gene product FANCJ. Cancer Cell 8 (2005) 255-265
    • (2005) Cancer Cell , vol.8 , pp. 255-265
    • Litman, R.1    Peng, M.2    Jin, Z.3    Zhang, F.4    Zhang, J.5    Powell, S.6    Andreassen, P.R.7    Cantor, S.B.8
  • 32
    • 0015891353 scopus 로고
    • A high susceptibility of Fanconi's anemia to chromosome breakage by DNA cross-linking agents
    • Sasaki M.S., and Tonomura A. A high susceptibility of Fanconi's anemia to chromosome breakage by DNA cross-linking agents. Cancer Res. 33 (1973) 1829-1836
    • (1973) Cancer Res. , vol.33 , pp. 1829-1836
    • Sasaki, M.S.1    Tonomura, A.2
  • 33
    • 0020357892 scopus 로고
    • Susceptibility of Fanconi's anemia lymphoblasts to DNA-cross-linking and alkylating agents
    • Ishida R., and Buchwald M. Susceptibility of Fanconi's anemia lymphoblasts to DNA-cross-linking and alkylating agents. Cancer Res. 42 (1982) 4000-4006
    • (1982) Cancer Res. , vol.42 , pp. 4000-4006
    • Ishida, R.1    Buchwald, M.2
  • 34
    • 0016825649 scopus 로고
    • Is Fanconi's anaemia defective in a process essential to the repair of DNA cross links?
    • Sasaki M.S. Is Fanconi's anaemia defective in a process essential to the repair of DNA cross links?. Nature 257 (1975) 501-503
    • (1975) Nature , vol.257 , pp. 501-503
    • Sasaki, M.S.1
  • 35
    • 0017652299 scopus 로고
    • Cross-link repair in human cells and its possible defect in Fanconi's anemia cells
    • Fujiwara Y., and Tatsumi M. Cross-link repair in human cells and its possible defect in Fanconi's anemia cells. J. Mol. Biol. 113 (1977) 635-649
    • (1977) J. Mol. Biol. , vol.113 , pp. 635-649
    • Fujiwara, Y.1    Tatsumi, M.2
  • 36
    • 0020395134 scopus 로고
    • Defective repair of mitomycin C crosslinks in Fanconi's anemia and loss in confluent normal human and xeroderma pigmentosum cells
    • Fujiwara Y. Defective repair of mitomycin C crosslinks in Fanconi's anemia and loss in confluent normal human and xeroderma pigmentosum cells. Biochim. Biophys. Acta 699 (1982) 217-225
    • (1982) Biochim. Biophys. Acta , vol.699 , pp. 217-225
    • Fujiwara, Y.1
  • 37
    • 0023926585 scopus 로고
    • Repair of 4,5′,8-trimethylpsoralen plus light-induced DNA damage in normal and Fanconi's anemia cell lines
    • Averbeck D., Papadopoulo D., and Moustacchi E. Repair of 4,5′,8-trimethylpsoralen plus light-induced DNA damage in normal and Fanconi's anemia cell lines. Cancer Res. 48 (1988) 2015-2020
    • (1988) Cancer Res. , vol.48 , pp. 2015-2020
    • Averbeck, D.1    Papadopoulo, D.2    Moustacchi, E.3
  • 38
    • 0024566852 scopus 로고
    • Repair analysis of mitomycin C-induced DNA crosslinking in ribosomal RNA genes in lymphoblastoid cells from Fanconi's anemia patients
    • Matsumoto A., Vos J.M., and Hanawalt P.C. Repair analysis of mitomycin C-induced DNA crosslinking in ribosomal RNA genes in lymphoblastoid cells from Fanconi's anemia patients. Mutat. Res. 217 (1989) 185-192
    • (1989) Mutat. Res. , vol.217 , pp. 185-192
    • Matsumoto, A.1    Vos, J.M.2    Hanawalt, P.C.3
  • 39
    • 0018844455 scopus 로고
    • DNA repair in human cells containing photoadducts of 8-methoxypsoralen or angelicin
    • Kaye J., Smith C.A., and Hanawalt P.C. DNA repair in human cells containing photoadducts of 8-methoxypsoralen or angelicin. Cancer Res. 40 (1980) 696-702
    • (1980) Cancer Res. , vol.40 , pp. 696-702
    • Kaye, J.1    Smith, C.A.2    Hanawalt, P.C.3
  • 40
    • 0021751852 scopus 로고
    • Fanconi anaemia cells are not uniformly deficient in unhooking of DNA interstrand crosslinks, induced by mitomycin C or 8-methoxypsoralen plus UVA
    • Poll E.H., Arwert F., Kortbeek H.T., and Eriksson A.W. Fanconi anaemia cells are not uniformly deficient in unhooking of DNA interstrand crosslinks, induced by mitomycin C or 8-methoxypsoralen plus UVA. Hum. Genet. 68 (1984) 228-234
    • (1984) Hum. Genet. , vol.68 , pp. 228-234
    • Poll, E.H.1    Arwert, F.2    Kortbeek, H.T.3    Eriksson, A.W.4
  • 42
    • 34547131860 scopus 로고    scopus 로고
    • Disparate contributions of the Fanconi anemia pathway and homologous recombination in preventing spontaneous mutagenesis
    • Hinz J.M., Nham P.B., Urbin S.S., Jones I.M., and Thompson L.H. Disparate contributions of the Fanconi anemia pathway and homologous recombination in preventing spontaneous mutagenesis. Nucleic Acids Res. 35 (2007) 3733-3740
    • (2007) Nucleic Acids Res. , vol.35 , pp. 3733-3740
    • Hinz, J.M.1    Nham, P.B.2    Urbin, S.S.3    Jones, I.M.4    Thompson, L.H.5
  • 43
    • 0035379611 scopus 로고    scopus 로고
    • The emerging genetic and molecular basis of Fanconi anaemia
    • Joenje H., and Patel K.J. The emerging genetic and molecular basis of Fanconi anaemia. Nat. Rev. Genet. 2 (2001) 446-457
    • (2001) Nat. Rev. Genet. , vol.2 , pp. 446-457
    • Joenje, H.1    Patel, K.J.2
  • 45
    • 38049115657 scopus 로고    scopus 로고
    • The mechanism of human nonhomologous DNA end joining
    • Lieber M.R. The mechanism of human nonhomologous DNA end joining. J. Biol. Chem. 283 (2008) 1-5
    • (2008) J. Biol. Chem. , vol.283 , pp. 1-5
    • Lieber, M.R.1
  • 46
    • 38049125555 scopus 로고    scopus 로고
    • The endless tale of non-homologous end-joining
    • Weterings E., and Chen D.J. The endless tale of non-homologous end-joining. Cell Res. 18 (2008) 114-124
    • (2008) Cell Res. , vol.18 , pp. 114-124
    • Weterings, E.1    Chen, D.J.2
  • 47
    • 0026521238 scopus 로고
    • Cloning of cDNAs for Fanconi's anaemia by functional complementation
    • Strathdee C.A., Gavish H., Shannon W.R., and Buchwald M. Cloning of cDNAs for Fanconi's anaemia by functional complementation. Nature 356 (1992) 763-767
    • (1992) Nature , vol.356 , pp. 763-767
    • Strathdee, C.A.1    Gavish, H.2    Shannon, W.R.3    Buchwald, M.4
  • 49
    • 38049125552 scopus 로고    scopus 로고
    • The fidelity of DNA synthesis by eukaryotic replicative and translesion synthesis polymerases
    • McCulloch S.D., and Kunkel T.A. The fidelity of DNA synthesis by eukaryotic replicative and translesion synthesis polymerases. Cell Res. 18 (2008) 148-161
    • (2008) Cell Res. , vol.18 , pp. 148-161
    • McCulloch, S.D.1    Kunkel, T.A.2
  • 50
    • 47649100711 scopus 로고    scopus 로고
    • DNA polymerases and human disease
    • Loeb L.A., and Monnat Jr. R.J. DNA polymerases and human disease. Nat. Rev. Genet. 9 (2008) 594-604
    • (2008) Nat. Rev. Genet. , vol.9 , pp. 594-604
    • Loeb, L.A.1    Monnat Jr., R.J.2
  • 51
    • 43849098620 scopus 로고    scopus 로고
    • The Fanconi anemia core complex is required for efficient point mutagenesis and Rev1 foci assembly
    • Mirchandani K.D., McCaffrey R.M., and D'Andrea A.D. The Fanconi anemia core complex is required for efficient point mutagenesis and Rev1 foci assembly. DNA Repair 7 (2008) 902-911
    • (2008) DNA Repair , vol.7 , pp. 902-911
    • Mirchandani, K.D.1    McCaffrey, R.M.2    D'Andrea, A.D.3
  • 53
    • 12444257433 scopus 로고    scopus 로고
    • Fanconi anaemia proteins: major roles in cell protection against oxidative damage
    • Pagano G., and Youssoufian H. Fanconi anaemia proteins: major roles in cell protection against oxidative damage. Bioessays 25 (2003) 589-595
    • (2003) Bioessays , vol.25 , pp. 589-595
    • Pagano, G.1    Youssoufian, H.2
  • 56
    • 0032213353 scopus 로고    scopus 로고
    • Abnormal microsomal detoxification implicated in Fanconi anemia group C by interaction of the FAC protein with NADPH cytochrome P450 reductase
    • Kruyt F.A., Hoshino T., Liu J.M., Joseph P., Jaiswal A.K., and Youssoufian H. Abnormal microsomal detoxification implicated in Fanconi anemia group C by interaction of the FAC protein with NADPH cytochrome P450 reductase. Blood 92 (1998) 3050-3056
    • (1998) Blood , vol.92 , pp. 3050-3056
    • Kruyt, F.A.1    Hoshino, T.2    Liu, J.M.3    Joseph, P.4    Jaiswal, A.K.5    Youssoufian, H.6
  • 57
    • 0034927378 scopus 로고    scopus 로고
    • Fanconi anemia group C protein prevents apoptosis in hematopoietic cells through redox regulation of GSTP1
    • Cumming R.C., Lightfoot J., Beard K., Youssoufian H., O'Brien P.J., and Buchwald M. Fanconi anemia group C protein prevents apoptosis in hematopoietic cells through redox regulation of GSTP1. Nat. Med. 7 (2001) 814-820
    • (2001) Nat. Med. , vol.7 , pp. 814-820
    • Cumming, R.C.1    Lightfoot, J.2    Beard, K.3    Youssoufian, H.4    O'Brien, P.J.5    Buchwald, M.6
  • 58
    • 0036195950 scopus 로고    scopus 로고
    • The FANCG Fanconi anemia protein interacts with CYP2E1: possible role in protection against oxidative DNA damage
    • Futaki M., Igarashi T., Watanabe S., Kajigaya S., Tatsuguchi A., Wang J., and Liu J.M. The FANCG Fanconi anemia protein interacts with CYP2E1: possible role in protection against oxidative DNA damage. Carcinogenesis 23 (2002) 67-72
    • (2002) Carcinogenesis , vol.23 , pp. 67-72
    • Futaki, M.1    Igarashi, T.2    Watanabe, S.3    Kajigaya, S.4    Tatsuguchi, A.5    Wang, J.6    Liu, J.M.7
  • 59
    • 3142666893 scopus 로고    scopus 로고
    • Oxidative stress/damage induces multimerization and interaction of Fanconi anemia proteins
    • Park S.J., Ciccone S.L., Beck B.D., Hwang B., Freie B., Clapp D.W., and Lee S.H. Oxidative stress/damage induces multimerization and interaction of Fanconi anemia proteins. J. Biol. Chem. 279 (2004) 30053-30059
    • (2004) J. Biol. Chem. , vol.279 , pp. 30053-30059
    • Park, S.J.1    Ciccone, S.L.2    Beck, B.D.3    Hwang, B.4    Freie, B.5    Clapp, D.W.6    Lee, S.H.7
  • 60
    • 0019444973 scopus 로고
    • Oxygen-dependence of chromosomal aberrations in Fanconi's anaemia
    • Joenje H., Arwert F., Eriksson A.W., de Koning H., and Oostra A.B. Oxygen-dependence of chromosomal aberrations in Fanconi's anaemia. Nature 290 (1981) 142-143
    • (1981) Nature , vol.290 , pp. 142-143
    • Joenje, H.1    Arwert, F.2    Eriksson, A.W.3    de Koning, H.4    Oostra, A.B.5
  • 64
    • 0022502910 scopus 로고
    • Re-evaluation of in vitro radiosensitivity of human fibroblasts of different genetic origins
    • [published erratum appears in Int. J. Radiat. Biol. 50(6, Dec.) (1986) 1129]
    • Deschavanne P.J., Debieu D., Fertil B., and Malaise E.P. Re-evaluation of in vitro radiosensitivity of human fibroblasts of different genetic origins. Int. J. Radiat. Biol. 50 (1986) 279-293 [published erratum appears in Int. J. Radiat. Biol. 50(6, Dec.) (1986) 1129]
    • (1986) Int. J. Radiat. Biol. , vol.50 , pp. 279-293
    • Deschavanne, P.J.1    Debieu, D.2    Fertil, B.3    Malaise, E.P.4
  • 65
    • 0032882001 scopus 로고    scopus 로고
    • Drug sensitivity spectra in Fanconi anemia lymphoblastoid cell lines of defined complementation groups
    • Carreau M., Alon N., Bosnoyan-Collins L., Joenje H., and Buchwald M. Drug sensitivity spectra in Fanconi anemia lymphoblastoid cell lines of defined complementation groups. Mutat. Res. 435 (1999) 103-109
    • (1999) Mutat. Res. , vol.435 , pp. 103-109
    • Carreau, M.1    Alon, N.2    Bosnoyan-Collins, L.3    Joenje, H.4    Buchwald, M.5
  • 69
    • 34848861407 scopus 로고    scopus 로고
    • FANCB independently contribute to repair of DNA damage during replication
    • Nomura Y., Adachi N., Koyama H., and Human Mus81. FANCB independently contribute to repair of DNA damage during replication. Genes Cells 12 (2007) 1111-1122
    • (2007) Genes Cells , vol.12 , pp. 1111-1122
    • Nomura, Y.1    Adachi, N.2    Koyama, H.3    Human Mus814
  • 72
    • 4344597147 scopus 로고    scopus 로고
    • The Fanconi anaemia gene FANCC promotes homologous recombination and error-prone DNA repair
    • Niedzwiedz W., Mosedale G., Johnson M., Ong C.Y., Pace P., and Patel K.J. The Fanconi anaemia gene FANCC promotes homologous recombination and error-prone DNA repair. Mol. Cell 15 (2004) 607-620
    • (2004) Mol. Cell , vol.15 , pp. 607-620
    • Niedzwiedz, W.1    Mosedale, G.2    Johnson, M.3    Ong, C.Y.4    Pace, P.5    Patel, K.J.6
  • 77
    • 45949121186 scopus 로고
    • Isolation and cross-sensitivity of X-ray-sensitive mutants of V79-4 hamster cells
    • Jones N.J., Cox R., and Thacker J. Isolation and cross-sensitivity of X-ray-sensitive mutants of V79-4 hamster cells. Mutat. Res. 183 (1987) 279-286
    • (1987) Mutat. Res. , vol.183 , pp. 279-286
    • Jones, N.J.1    Cox, R.2    Thacker, J.3
  • 80
    • 33645728557 scopus 로고    scopus 로고
    • BACH1 is a DNA repair protein supporting BRCA1 damage response
    • Peng M., Litman R., Jin Z., Fong G., and Cantor S.B. BACH1 is a DNA repair protein supporting BRCA1 damage response. Oncogene 25 (2006) 2245-2253
    • (2006) Oncogene , vol.25 , pp. 2245-2253
    • Peng, M.1    Litman, R.2    Jin, Z.3    Fong, G.4    Cantor, S.B.5
  • 83
    • 19944434079 scopus 로고    scopus 로고
    • Similar effects of Brca2 truncation and Rad51 paralog deficiency on immunoglobulin V gene diversification in DT40 cells support an early role for Rad51 paralogs in homologous recombination
    • Hatanaka A., Yamazoe M., Sale J.E., Takata M., Yamamoto K., Kitao H., Sonoda E., Kikuchi K., Yonetani Y., and Takeda S. Similar effects of Brca2 truncation and Rad51 paralog deficiency on immunoglobulin V gene diversification in DT40 cells support an early role for Rad51 paralogs in homologous recombination. Mol. Cell. Biol. 25 (2005) 1124-1134
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 1124-1134
    • Hatanaka, A.1    Yamazoe, M.2    Sale, J.E.3    Takata, M.4    Yamamoto, K.5    Kitao, H.6    Sonoda, E.7    Kikuchi, K.8    Yonetani, Y.9    Takeda, S.10
  • 84
    • 0025299270 scopus 로고
    • The chromosome-breakage syndromes: rare disorders that provide models for studying somatic mutation
    • Spatz L., Bloom A.D., and Paul N.W. (Eds), March of Dimes Birth Defects Foundation, White Plains, NY
    • German J. The chromosome-breakage syndromes: rare disorders that provide models for studying somatic mutation. In: Spatz L., Bloom A.D., and Paul N.W. (Eds). Detection of Cancer Predisposition: Laboratory Approaches (1990), March of Dimes Birth Defects Foundation, White Plains, NY 85-111
    • (1990) Detection of Cancer Predisposition: Laboratory Approaches , pp. 85-111
    • German, J.1
  • 85
    • 0017877785 scopus 로고
    • Repair deficient human disorders and cancer
    • Setlow R.B. Repair deficient human disorders and cancer. Nature 271 (1978) 713-717
    • (1978) Nature , vol.271 , pp. 713-717
    • Setlow, R.B.1
  • 86
    • 0017118656 scopus 로고
    • Susceptibility of Fanconi's anaemia fibroblasts to chromosome damage by carcinogens
    • Auerbach A.D., and Wolman S.R. Susceptibility of Fanconi's anaemia fibroblasts to chromosome damage by carcinogens. Nature 261 (1976) 494-496
    • (1976) Nature , vol.261 , pp. 494-496
    • Auerbach, A.D.1    Wolman, S.R.2
  • 87
    • 0015882277 scopus 로고
    • In vitro chromosomal radiosensitivity in "chromosomal breakage syndromes"
    • Higurashi M., and Conen P.E. In vitro chromosomal radiosensitivity in "chromosomal breakage syndromes". Cancer 32 (1973) 380-383
    • (1973) Cancer , vol.32 , pp. 380-383
    • Higurashi, M.1    Conen, P.E.2
  • 88
    • 0346351375 scopus 로고
    • A manyfold increase in sister chromatid exchanges in Bloom's syndrome lymphocytes
    • Chaganti R.S.K., Schonberg S., and German J. A manyfold increase in sister chromatid exchanges in Bloom's syndrome lymphocytes. Proc. Natl. Acad. Sci. USA 71 (1974) 4508-4512
    • (1974) Proc. Natl. Acad. Sci. USA , vol.71 , pp. 4508-4512
    • Chaganti, R.S.K.1    Schonberg, S.2    German, J.3
  • 89
    • 0027861014 scopus 로고
    • Fanconi anemia diagnosis and the diepoxybutane (DEB) test
    • Auerbach A.D. Fanconi anemia diagnosis and the diepoxybutane (DEB) test. Exp. Hematol. 21 (1993) 731-733
    • (1993) Exp. Hematol. , vol.21 , pp. 731-733
    • Auerbach, A.D.1
  • 90
  • 91
    • 33746503650 scopus 로고    scopus 로고
    • The Fanconi anemia pathway limits the severity of mutagenesis
    • Hinz J.M., Nham P.B., Salazar E.P., and Thompson L.H. The Fanconi anemia pathway limits the severity of mutagenesis. DNA Repair 5 (2006) 875-884
    • (2006) DNA Repair , vol.5 , pp. 875-884
    • Hinz, J.M.1    Nham, P.B.2    Salazar, E.P.3    Thompson, L.H.4
  • 93
    • 0034871198 scopus 로고    scopus 로고
    • Telomere shortening in Fanconi anaemia demonstrated by a direct FISH approach
    • Hanson H., Mathew C.G., Docherty Z., and Mackie Ogilvie C. Telomere shortening in Fanconi anaemia demonstrated by a direct FISH approach. Cytogenet. Cell Genet. 93 (2001) 203-206
    • (2001) Cytogenet. Cell Genet. , vol.93 , pp. 203-206
    • Hanson, H.1    Mathew, C.G.2    Docherty, Z.3    Mackie Ogilvie, C.4
  • 96
    • 44949114282 scopus 로고    scopus 로고
    • FANCJ helicase defective in Fanconia anemia and breast cancer unwinds G-quadruplex DNA to defend genomic stability
    • Wu Y., Shin-ya K., and Brosh Jr. R.M. FANCJ helicase defective in Fanconia anemia and breast cancer unwinds G-quadruplex DNA to defend genomic stability. Mol. Cell. Biol. 28 (2008) 4116-4128
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 4116-4128
    • Wu, Y.1    Shin-ya, K.2    Brosh Jr., R.M.3
  • 97
    • 0035018021 scopus 로고    scopus 로고
    • G-quadruplex DNA structures-variations on a theme
    • Simonsson T. G-quadruplex DNA structures-variations on a theme. Biol. Chem. 382 (2001) 621-628
    • (2001) Biol. Chem. , vol.382 , pp. 621-628
    • Simonsson, T.1
  • 98
    • 34547117416 scopus 로고    scopus 로고
    • G-quadruplex formation in human telomeric (TTAGGG)4 sequence with complementary strand in close vicinity under molecularly crowded condition
    • Kan Z.Y., Lin Y., Wang F., Zhuang X.Y., Zhao Y., Pang D.W., Hao Y.H., and Tan Z. G-quadruplex formation in human telomeric (TTAGGG)4 sequence with complementary strand in close vicinity under molecularly crowded condition. Nucleic Acids Res. 35 (2007) 3646-3653
    • (2007) Nucleic Acids Res. , vol.35 , pp. 3646-3653
    • Kan, Z.Y.1    Lin, Y.2    Wang, F.3    Zhuang, X.Y.4    Zhao, Y.5    Pang, D.W.6    Hao, Y.H.7    Tan, Z.8
  • 99
    • 47049092433 scopus 로고    scopus 로고
    • Genomic stability: FANCJ-dependent G4 DNA repair
    • Maizels N. Genomic stability: FANCJ-dependent G4 DNA repair. Curr. Biol. 18 (2008) R613-614
    • (2008) Curr. Biol. , vol.18
    • Maizels, N.1
  • 100
    • 0033780760 scopus 로고    scopus 로고
    • DNA replication is required to elicit cellular responses to psoralen-induced DNA interstrand cross-links
    • Akkari Y.M., Bateman R.L., Reifsteck C.A., Olson S.B., and Grompe M. DNA replication is required to elicit cellular responses to psoralen-induced DNA interstrand cross-links. Mol. Cell. Biol. 20 (2000) 8283-8289
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 8283-8289
    • Akkari, Y.M.1    Bateman, R.L.2    Reifsteck, C.A.3    Olson, S.B.4    Grompe, M.5
  • 101
    • 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., Nairn R.S., Legerski R.J., and Li L. Involvement of nucleotide excision repair in a recombination-independent and error-prone pathway of DNA interstrand cross-link repair. Mol. Cell. Biol. 21 (2001) 713-720
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 713-720
    • Wang, X.1    Peterson, C.A.2    Zheng, H.3    Nairn, R.S.4    Legerski, R.J.5    Li, L.6
  • 102
    • 0034549346 scopus 로고    scopus 로고
    • Differential processing of UV mimetic and interstrand crosslink damage by XPF cell extracts
    • Zhang N., Zhang X., Peterson C., Li L., and Legerski R. Differential processing of UV mimetic and interstrand crosslink damage by XPF cell extracts. Nucleic Acids Res. 28 (2000) 4800-4804
    • (2000) Nucleic Acids Res. , vol.28 , pp. 4800-4804
    • Zhang, N.1    Zhang, X.2    Peterson, C.3    Li, L.4    Legerski, R.5
  • 103
    • 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., and 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. 24 (2004) 123-134
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 123-134
    • Rothfuss, A.1    Grompe, M.2
  • 104
    • 0037223410 scopus 로고    scopus 로고
    • Nucleotide excision repair- and polymerase eta-mediated error-prone removal of mitomycin C interstrand cross-links
    • Zheng H., Wang X., Warren A.J., Legerski R.J., Nairn R.S., Hamilton J.W., and Li L. Nucleotide excision repair- and polymerase eta-mediated error-prone removal of mitomycin C interstrand cross-links. Mol. Cell. Biol. 23 (2003) 754-761
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 754-761
    • Zheng, H.1    Wang, X.2    Warren, A.J.3    Legerski, R.J.4    Nairn, R.S.5    Hamilton, J.W.6    Li, L.7
  • 106
    • 0032814145 scopus 로고    scopus 로고
    • Interstrand cross-links induce DNA synthesis in damaged and undamaged plasmids in mammalian cell extracts
    • Li L., Peterson C.A., Lu X., Wei P., and Legerski R.J. Interstrand cross-links induce DNA synthesis in damaged and undamaged plasmids in mammalian cell extracts. Mol. Cell. Biol. 19 (1999) 5619-5630
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 5619-5630
    • Li, L.1    Peterson, C.A.2    Lu, X.3    Wei, P.4    Legerski, R.J.5
  • 107
    • 0036005855 scopus 로고    scopus 로고
    • hMutSbeta is required for the recognition and uncoupling of psoralen interstrand cross-links in vitro
    • Zhang N., Lu X., Zhang X., Peterson C.A., and Legerski R.J. hMutSbeta is required for the recognition and uncoupling of psoralen interstrand cross-links in vitro. Mol. Cell. Biol. 22 (2002) 2388-2397
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 2388-2397
    • Zhang, N.1    Lu, X.2    Zhang, X.3    Peterson, C.A.4    Legerski, R.J.5
  • 108
    • 35348946359 scopus 로고    scopus 로고
    • Double-strand breaks induce homologous recombinational repair of interstrand cross-links via cooperation of MSH2, ERCC1-XPF, REV3, and the Fanconi anemia pathway
    • Zhang N., Liu X., Li L., and Legerski R. Double-strand breaks induce homologous recombinational repair of interstrand cross-links via cooperation of MSH2, ERCC1-XPF, REV3, and the Fanconi anemia pathway. DNA Repair 6 (2007) 1670-1678
    • (2007) DNA Repair , vol.6 , pp. 1670-1678
    • Zhang, N.1    Liu, X.2    Li, L.3    Legerski, R.4
  • 109
    • 0034008802 scopus 로고    scopus 로고
    • Fanconi anemia, complementation group A, cells are defective in ability to produce incisions at sites of psoralen interstrand cross-links
    • Kumaresan K.R., and Lambert M.W. Fanconi anemia, complementation group A, cells are defective in ability to produce incisions at sites of psoralen interstrand cross-links. Carcinogenesis 21 (2000) 741-751
    • (2000) Carcinogenesis , vol.21 , pp. 741-751
    • Kumaresan, K.R.1    Lambert, M.W.2
  • 110
    • 37349014537 scopus 로고    scopus 로고
    • Deficiency in incisions produced by XPF at the site of a DNA interstrand cross-link in Fanconi anemia cells
    • Kumaresan K.R., Sridharan D.M., McMahon L.W., and Lambert M.W. Deficiency in incisions produced by XPF at the site of a DNA interstrand cross-link in Fanconi anemia cells. Biochemistry 46 (2007) 14359-14368
    • (2007) Biochemistry , vol.46 , pp. 14359-14368
    • Kumaresan, K.R.1    Sridharan, D.M.2    McMahon, L.W.3    Lambert, M.W.4
  • 111
    • 0037154127 scopus 로고    scopus 로고
    • Contribution of XPF functional domains to the 5′ and 3′ incisions produced at the site of a psoralen interstrand cross-link
    • Kumaresan K.R., Hwang M., Thelen M.P., and Lambert M.W. Contribution of XPF functional domains to the 5′ and 3′ incisions produced at the site of a psoralen interstrand cross-link. Biochemistry 41 (2002) 890-896
    • (2002) Biochemistry , vol.41 , pp. 890-896
    • Kumaresan, K.R.1    Hwang, M.2    Thelen, M.P.3    Lambert, M.W.4
  • 112
    • 33750326176 scopus 로고    scopus 로고
    • alphaII-Spectrin interacts with five groups of functionally important proteins in the nucleus
    • Sridharan D.M., McMahon L.W., and Lambert M.W. alphaII-Spectrin interacts with five groups of functionally important proteins in the nucleus. Cell Biol. Int. 30 (2006) 866-878
    • (2006) Cell Biol. Int. , vol.30 , pp. 866-878
    • Sridharan, D.M.1    McMahon, L.W.2    Lambert, M.W.3
  • 113
    • 0035912843 scopus 로고    scopus 로고
    • Human alpha spectrin II and the FANCA, FANCC, and FANCG proteins bind to DNA containing psoralen interstrand cross-links
    • McMahon L.W., Sangerman J., Goodman S.R., Kumaresan K., and Lambert M.W. Human alpha spectrin II and the FANCA, FANCC, and FANCG proteins bind to DNA containing psoralen interstrand cross-links. Biochemistry 40 (2001) 7025-7034
    • (2001) Biochemistry , vol.40 , pp. 7025-7034
    • McMahon, L.W.1    Sangerman, J.2    Goodman, S.R.3    Kumaresan, K.4    Lambert, M.W.5
  • 114
    • 0037350437 scopus 로고    scopus 로고
    • Nonerythroid alphaII spectrin is required for recruitment of FANCA and XPF to nuclear foci induced by DNA interstrand cross-links
    • Sridharan D., Brown M., Lambert W.C., McMahon L.W., and Lambert M.W. Nonerythroid alphaII spectrin is required for recruitment of FANCA and XPF to nuclear foci induced by DNA interstrand cross-links. J. Cell Sci. 116 (2003) 823-835
    • (2003) J. Cell Sci. , vol.116 , pp. 823-835
    • Sridharan, D.1    Brown, M.2    Lambert, W.C.3    McMahon, L.W.4    Lambert, M.W.5
  • 115
    • 59849090474 scopus 로고    scopus 로고
    • The SH3 domain of alphaII spectrin is a target for the fanconi anemia protein, FANCG
    • Lefferts J.A., Wang C., Sridharan D., Baralt M., and Lambert M.W. The SH3 domain of alphaII spectrin is a target for the fanconi anemia protein, FANCG. Biochemistry 48 (2009) 254-263
    • (2009) Biochemistry , vol.48 , pp. 254-263
    • Lefferts, J.A.1    Wang, C.2    Sridharan, D.3    Baralt, M.4    Lambert, M.W.5
  • 116
    • 0035937735 scopus 로고    scopus 로고
    • Deficient DNA end joining activity in extracts from Fanconi anemia fibroblasts
    • Lundberg R., Mavinakere M., and Campbell C. Deficient DNA end joining activity in extracts from Fanconi anemia fibroblasts. J. Biol. Chem. 276 (2001) 9543-9549
    • (2001) J. Biol. Chem. , vol.276 , pp. 9543-9549
    • Lundberg, R.1    Mavinakere, M.2    Campbell, C.3
  • 117
    • 0031835895 scopus 로고    scopus 로고
    • The fidelity of double strand breaks processing is impaired in complementation groups B and D of Fanconi anemia
    • Escarceller M., Rousset E., Moustacchi E., and Papadopoulo D. The fidelity of double strand breaks processing is impaired in complementation groups B and D of Fanconi anemia. Somat. Cell Mol. Genet. 23 (1997) 401-411
    • (1997) Somat. Cell Mol. Genet. , vol.23 , pp. 401-411
    • Escarceller, M.1    Rousset, E.2    Moustacchi, E.3    Papadopoulo, D.4
  • 119
    • 0037195937 scopus 로고    scopus 로고
    • A DNA double strand break repair defect in Fanconi anemia fibroblasts
    • Donahue S.L., and Campbell C. A DNA double strand break repair defect in Fanconi anemia fibroblasts. J. Biol. Chem. 277 (2002) 46243-46247
    • (2002) J. Biol. Chem. , vol.277 , pp. 46243-46247
    • Donahue, S.L.1    Campbell, C.2
  • 120
    • 27544514954 scopus 로고    scopus 로고
    • Fancd2 functions in a double strand break repair pathway that is distinct from non-homologous end joining
    • Houghtaling S., Newell A., Akkari Y., Taniguchi T., Olson S., and Grompe M. Fancd2 functions in a double strand break repair pathway that is distinct from non-homologous end joining. Hum. Mol. Genet. 14 (2005) 3027-3033
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 3027-3033
    • Houghtaling, S.1    Newell, A.2    Akkari, Y.3    Taniguchi, T.4    Olson, S.5    Grompe, M.6
  • 121
    • 0042531939 scopus 로고    scopus 로고
    • Deficient regulation of DNA double-strand break repair in Fanconi anemia fibroblasts
    • Donahue S.L., Lundberg R., Saplis R., and Campbell C. Deficient regulation of DNA double-strand break repair in Fanconi anemia fibroblasts. J. Biol. Chem. 278 (2003) 29487-29495
    • (2003) J. Biol. Chem. , vol.278 , pp. 29487-29495
    • Donahue, S.L.1    Lundberg, R.2    Saplis, R.3    Campbell, C.4
  • 122
    • 0030854142 scopus 로고    scopus 로고
    • Elevated homologous recombination activity in fanconi anemia fibroblasts
    • Thyagarajan B., and Campbell C. Elevated homologous recombination activity in fanconi anemia fibroblasts. J. Biol. Chem. 272 (1997) 23328-23333
    • (1997) J. Biol. Chem. , vol.272 , pp. 23328-23333
    • Thyagarajan, B.1    Campbell, C.2
  • 125
    • 25144503943 scopus 로고    scopus 로고
    • The BACH1/BRIP1 helicase functions independently of BRCA1 in the Fanconi anemia pathway for DNA crosslink repair
    • Bridge W.L., Vandenberg C.J., Franklin R.J., and Hiom K. The BACH1/BRIP1 helicase functions independently of BRCA1 in the Fanconi anemia pathway for DNA crosslink repair. Nat. Genet. 37 (2005) 934-935
    • (2005) Nat. Genet. , vol.37 , pp. 934-935
    • Bridge, W.L.1    Vandenberg, C.J.2    Franklin, R.J.3    Hiom, K.4
  • 126
    • 17644369692 scopus 로고    scopus 로고
    • FANCD2 functions independently of BRCA2 and RAD51 associated homologous recombination in response to DNA damage
    • Ohashi A., Zdzienicka M.Z., Chen J., and Couch F.J. FANCD2 functions independently of BRCA2 and RAD51 associated homologous recombination in response to DNA damage. J. Biol. Chem. 280 (2005) 14877-14883
    • (2005) J. Biol. Chem. , vol.280 , pp. 14877-14883
    • Ohashi, A.1    Zdzienicka, M.Z.2    Chen, J.3    Couch, F.J.4
  • 128
    • 0036796260 scopus 로고    scopus 로고
    • DNA cross-link-dependent RAD50/MRE11/NBS1 subnuclear assembly requires the Fanconi anemia C protein
    • Pichierri P., Averbeck D., and Rosselli F. DNA cross-link-dependent RAD50/MRE11/NBS1 subnuclear assembly requires the Fanconi anemia C protein. Hum. Mol. Genet. 11 (2002) 2531-2546
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 2531-2546
    • Pichierri, P.1    Averbeck, D.2    Rosselli, F.3
  • 129
    • 2942674745 scopus 로고    scopus 로고
    • A Rad50-dependent pathway of DNA repair is deficient in Fanconi anemia fibroblasts
    • Donahue S.L., and Campbell C. A Rad50-dependent pathway of DNA repair is deficient in Fanconi anemia fibroblasts. Nucleic Acids Res. 32 (2004) 3248-3257
    • (2004) Nucleic Acids Res. , vol.32 , pp. 3248-3257
    • Donahue, S.L.1    Campbell, C.2
  • 130
    • 27444436092 scopus 로고    scopus 로고
    • Non-homologous end-joining defect in Fanconi anemia hematopoietic cells exposed to ionizing radiation
    • Casado J.A., Nunez M.I., Segovia J.C., Ruiz de Almodovar J.M., and Bueren J.A. Non-homologous end-joining defect in Fanconi anemia hematopoietic cells exposed to ionizing radiation. Radiat. Res. 164 (2005) 635-641
    • (2005) Radiat. Res. , vol.164 , pp. 635-641
    • Casado, J.A.1    Nunez, M.I.2    Segovia, J.C.3    Ruiz de Almodovar, J.M.4    Bueren, J.A.5
  • 132
    • 34250200743 scopus 로고    scopus 로고
    • Defective signal joint recombination in fanconi anemia fibroblasts reveals a role for Rad50 in V(D)J recombination
    • Donahue S.L., Tabah A.A., Schmitz K., Aaron A., and Campbell C. Defective signal joint recombination in fanconi anemia fibroblasts reveals a role for Rad50 in V(D)J recombination. J. Mol. Biol. 370 (2007) 449-458
    • (2007) J. Mol. Biol. , vol.370 , pp. 449-458
    • Donahue, S.L.1    Tabah, A.A.2    Schmitz, K.3    Aaron, A.4    Campbell, C.5
  • 133
    • 0003802597 scopus 로고
    • Wolff S. (Ed), John Wiley & Sons, New York
    • In: Wolff S. (Ed). Sister Chromatid Exchange (1982), John Wiley & Sons, New York
    • (1982) Sister Chromatid Exchange
  • 134
    • 33846684170 scopus 로고    scopus 로고
    • Molecular mechanisms of sister-chromatid exchange
    • Wilson III D.M., and Thompson L.H. Molecular mechanisms of sister-chromatid exchange. Mutat. Res. 616 (2007) 11-23
    • (2007) Mutat. Res. , vol.616 , pp. 11-23
    • Wilson III, D.M.1    Thompson, L.H.2
  • 135
    • 0347987856 scopus 로고    scopus 로고
    • The Bloom's syndrome helicase suppresses crossing over during homologous recombination
    • Wu L., and Hickson I.D. The Bloom's syndrome helicase suppresses crossing over during homologous recombination. Nature 426 (2003) 870-874
    • (2003) Nature , vol.426 , pp. 870-874
    • Wu, L.1    Hickson, I.D.2
  • 136
    • 0342349439 scopus 로고
    • Sister chromatid exchanges and disease states in man
    • Wolff S. (Ed), John Wiley & Sons, New York
    • Evans H.J. Sister chromatid exchanges and disease states in man. In: Wolff S. (Ed). Sister Chromatid Exchange (1982), John Wiley & Sons, New York 183-228
    • (1982) Sister Chromatid Exchange , pp. 183-228
    • Evans, H.J.1
  • 137
    • 0021923167 scopus 로고
    • Cytogenetic analyses utilizing various clastogens in two sibs with Fanconi anemia, their relatives, and control individuals
    • Gebhart E., Kysela D., Matthee H., and Nikol M. Cytogenetic analyses utilizing various clastogens in two sibs with Fanconi anemia, their relatives, and control individuals. Hum. Genet. 69 (1985) 309-315
    • (1985) Hum. Genet. , vol.69 , pp. 309-315
    • Gebhart, E.1    Kysela, D.2    Matthee, H.3    Nikol, M.4
  • 138
    • 0020571775 scopus 로고
    • Proliferative kinetics and mitomycin C-induced chromosome damage in Fanconi's anemia lymphocytes
    • Miura K., Morimoto K., and Koizumi A. Proliferative kinetics and mitomycin C-induced chromosome damage in Fanconi's anemia lymphocytes. Hum. Genet. 63 (1983) 19-23
    • (1983) Hum. Genet. , vol.63 , pp. 19-23
    • Miura, K.1    Morimoto, K.2    Koizumi, A.3
  • 139
    • 0020535875 scopus 로고
    • Failure of diepoxybutane to enhance sister chromatid exchange levels in Fanconi's anemia patients and heterozygotes
    • Porfirio B., Dallapiccola B., Mokini V., Alimena G., and Gandini E. Failure of diepoxybutane to enhance sister chromatid exchange levels in Fanconi's anemia patients and heterozygotes. Hum. Genet. 63 (1983) 117-120
    • (1983) Hum. Genet. , vol.63 , pp. 117-120
    • Porfirio, B.1    Dallapiccola, B.2    Mokini, V.3    Alimena, G.4    Gandini, E.5
  • 140
    • 0035688468 scopus 로고    scopus 로고
    • The Chinese hamster FANCG/XRCC9 mutant NM3 fails to express the monoubiquitinated form of the FANCD2 protein, is hypersensitive to a range of DNA damaging agents and exhibits a normal level of spontaneous sister chromatid exchange
    • Wilson J.B., Johnson M.A., Stuckert A.P., Trueman K.L., May S., Bryant P.E., Meyn R.E., D'Andrea A.D., and Jones N.J. The Chinese hamster FANCG/XRCC9 mutant NM3 fails to express the monoubiquitinated form of the FANCD2 protein, is hypersensitive to a range of DNA damaging agents and exhibits a normal level of spontaneous sister chromatid exchange. Carcinogenesis 22 (2001) 1939-1946
    • (2001) Carcinogenesis , vol.22 , pp. 1939-1946
    • Wilson, J.B.1    Johnson, M.A.2    Stuckert, A.P.3    Trueman, K.L.4    May, S.5    Bryant, P.E.6    Meyn, R.E.7    D'Andrea, A.D.8    Jones, N.J.9
  • 142
    • 0016720309 scopus 로고
    • Induction by alkylating agents of sister chromatid exchanges and chromatid breaks in Fanconi's anemia
    • Latt S.A., Stetten G., Juergens L.A., Buchanan G.R., and Gerald P.S. Induction by alkylating agents of sister chromatid exchanges and chromatid breaks in Fanconi's anemia. Proc. Natl. Acad. Sci. USA 72 (1975) 4066-4070
    • (1975) Proc. Natl. Acad. Sci. USA , vol.72 , pp. 4066-4070
    • Latt, S.A.1    Stetten, G.2    Juergens, L.A.3    Buchanan, G.R.4    Gerald, P.S.5
  • 143
    • 0022501312 scopus 로고
    • Comparison of the sensitivity of Fanconi's anemia and normal fibroblasts to the induction of sister-chromatid exchanges by photoaddition of mono- and bi-functional psoralens
    • Billardon B., and Moustacchi E. Comparison of the sensitivity of Fanconi's anemia and normal fibroblasts to the induction of sister-chromatid exchanges by photoaddition of mono- and bi-functional psoralens. Mutat. Res. 174 (1986) 241-246
    • (1986) Mutat. Res. , vol.174 , pp. 241-246
    • Billardon, B.1    Moustacchi, E.2
  • 144
    • 0022403083 scopus 로고
    • The effect of aphidicolin on Fanconi's anemia lymphocyte chromosomes
    • Porfirio B., Dallapiccola B., and Gandini E. The effect of aphidicolin on Fanconi's anemia lymphocyte chromosomes. Mutat. Res. 144 (1985) 257-263
    • (1985) Mutat. Res. , vol.144 , pp. 257-263
    • Porfirio, B.1    Dallapiccola, B.2    Gandini, E.3
  • 145
    • 34547634597 scopus 로고    scopus 로고
    • Fanconi anemia: genetic analysis of a human disease using chicken system
    • Takata M., Kitao H., and Ishiai M. Fanconi anemia: genetic analysis of a human disease using chicken system. Cytogenet. Genome Res. 117 (2007) 346-351
    • (2007) Cytogenet. Genome Res. , vol.117 , pp. 346-351
    • Takata, M.1    Kitao, H.2    Ishiai, M.3
  • 146
    • 34547486820 scopus 로고    scopus 로고
    • The Fanconi anemia pathway promotes homologous recombination repair in DT40 cell line
    • Takata M., Yamamoto K., Matsushita N., Kitao H., Hirano S., and Ishiai M. The Fanconi anemia pathway promotes homologous recombination repair in DT40 cell line. Subcell. Biochem. 40 (2006) 295-311
    • (2006) Subcell. Biochem. , vol.40 , pp. 295-311
    • Takata, M.1    Yamamoto, K.2    Matsushita, N.3    Kitao, H.4    Hirano, S.5    Ishiai, M.6
  • 147
    • 16844383231 scopus 로고    scopus 로고
    • Extensive chromosomal instability in Rad51d-deficient mouse cells
    • Smiraldo P.G., Gruver A.M., Osborn J.C., and Pittman D.L. Extensive chromosomal instability in Rad51d-deficient mouse cells. Cancer Res. 65 (2005) 2089-2096
    • (2005) Cancer Res. , vol.65 , pp. 2089-2096
    • Smiraldo, P.G.1    Gruver, A.M.2    Osborn, J.C.3    Pittman, D.L.4
  • 149
    • 13444250245 scopus 로고    scopus 로고
    • How Fanconi anemia proteins promote the four Rs: Replication, recombination, repair, and recovery
    • Thompson L.H., Hinz J.M., Yamada N.A., and Jones N.J. How Fanconi anemia proteins promote the four Rs: Replication, recombination, repair, and recovery. Environ. Mol. Mutagen. 45 (2005) 128-142
    • (2005) Environ. Mol. Mutagen. , vol.45 , pp. 128-142
    • Thompson, L.H.1    Hinz, J.M.2    Yamada, N.A.3    Jones, N.J.4
  • 150
    • 67650584680 scopus 로고
    • Decreased mutagenesis in cells from patients with Fanconi's anemia
    • Finkelberg R., Buchwald M., and Siminovitch L. Decreased mutagenesis in cells from patients with Fanconi's anemia. Am. J. Hum. Genet. 29 (1977) 42A
    • (1977) Am. J. Hum. Genet. , vol.29
    • Finkelberg, R.1    Buchwald, M.2    Siminovitch, L.3
  • 151
    • 0025346318 scopus 로고
    • Mutagenic response of Fanconi's anemia cells from a defined complementation group after treatment with photoactivated bifunctional psoralens
    • Papadopoulo D., Porfirio B., and Moustacchi E. Mutagenic response of Fanconi's anemia cells from a defined complementation group after treatment with photoactivated bifunctional psoralens. Cancer Res. 50 (1990) 3289-3294
    • (1990) Cancer Res. , vol.50 , pp. 3289-3294
    • Papadopoulo, D.1    Porfirio, B.2    Moustacchi, E.3
  • 152
    • 0025059685 scopus 로고
    • Hypomutability in Fanconi anemia cells is associated with increased deletion frequency at the HPRT locus
    • Papadopoulo D., Guillouf C., Mohrenweiser H., and Moustacchi E. Hypomutability in Fanconi anemia cells is associated with increased deletion frequency at the HPRT locus. Proc. Natl. Acad. Sci. USA 87 (1990) 8383-8387
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 8383-8387
    • Papadopoulo, D.1    Guillouf, C.2    Mohrenweiser, H.3    Moustacchi, E.4
  • 153
    • 0027212633 scopus 로고
    • Molecular spectrum of mutations induced at the HPRT locus by a cross-linking agent in human cell lines with different repair capacities
    • Papadopoulo D., Laquerbe A., Guillouf C., and Moustacchi E. Molecular spectrum of mutations induced at the HPRT locus by a cross-linking agent in human cell lines with different repair capacities. Mutat. Res. 294 (1993) 167-177
    • (1993) Mutat. Res. , vol.294 , pp. 167-177
    • Papadopoulo, D.1    Laquerbe, A.2    Guillouf, C.3    Moustacchi, E.4
  • 154
    • 0027197518 scopus 로고
    • Mutagenic processing of psoralen monoadducts differ in normal and Fanconi anemia cells
    • Guillouf C., Laquerbe A., Moustacchi E., and Papadopoulo D. Mutagenic processing of psoralen monoadducts differ in normal and Fanconi anemia cells. Mutagenesis 8 (1993) 355-361
    • (1993) Mutagenesis , vol.8 , pp. 355-361
    • Guillouf, C.1    Laquerbe, A.2    Moustacchi, E.3    Papadopoulo, D.4
  • 155
    • 0028821379 scopus 로고
    • The molecular mechanism underlying formation of deletions in Fanconi
    • Laquerbe A., Moustacchi E., Fuscoe J.C., and Papadopoulo D. The molecular mechanism underlying formation of deletions in Fanconi anemia cells may involve a site-specific recombination. Proc. Natl. Acad. Sci. USA 92 (1995) 831-835
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 831-835
    • Laquerbe, A.1    Moustacchi, E.2    Fuscoe, J.C.3    Papadopoulo, D.4
  • 158
    • 0028956569 scopus 로고
    • Mutational response of Fanconi anaemia cells to shuttle vector site-specific psoralen cross-links
    • Bredberg A., Sandor Z., and Brant M. Mutational response of Fanconi anaemia cells to shuttle vector site-specific psoralen cross-links. Carcinogen. 16 (1995) 555-562
    • (1995) Carcinogen. , vol.16 , pp. 555-562
    • Bredberg, A.1    Sandor, Z.2    Brant, M.3
  • 159
    • 0027249768 scopus 로고
    • Frequencies of HPRT-lymphocytes and glycophorin A variants erythrocytes in Fanconi anemia patients, their parents and control donors
    • Sala-Trepat M., Boyse J., Richard P., Papadopoulo D., and Moustacchi E. Frequencies of HPRT-lymphocytes and glycophorin A variants erythrocytes in Fanconi anemia patients, their parents and control donors. Mutat. Res. 289 (1993) 115-126
    • (1993) Mutat. Res. , vol.289 , pp. 115-126
    • Sala-Trepat, M.1    Boyse, J.2    Richard, P.3    Papadopoulo, D.4    Moustacchi, E.5
  • 160
    • 18244371436 scopus 로고    scopus 로고
    • Use of the glycophorin A somatic mutation assay for rapid, unambiguous identification of Fanconi anemia homozygotes regardless of GPA genotype
    • Evdokimova V.N., McLoughlin R.K., Wenger S.L., and Grant S.G. Use of the glycophorin A somatic mutation assay for rapid, unambiguous identification of Fanconi anemia homozygotes regardless of GPA genotype. Am. J. Med. Genet. A 135 (2005) 59-65
    • (2005) Am. J. Med. Genet. A , vol.135 , pp. 59-65
    • Evdokimova, V.N.1    McLoughlin, R.K.2    Wenger, S.L.3    Grant, S.G.4
  • 161
    • 0033385037 scopus 로고    scopus 로고
    • Molecular spectra of HPRT deletion mutations in circulating T-lymphocytes in Fanconi anemia patients
    • Laquerbe A., Sala-Trepat M., Vives C., Escarceller M., and Papadopoulo D. Molecular spectra of HPRT deletion mutations in circulating T-lymphocytes in Fanconi anemia patients. Mutat. Res. 431 (1999) 341-350
    • (1999) Mutat. Res. , vol.431 , pp. 341-350
    • Laquerbe, A.1    Sala-Trepat, M.2    Vives, C.3    Escarceller, M.4    Papadopoulo, D.5
  • 162
    • 0014873211 scopus 로고
    • Evidence for transfer of enzyme product as the basis of metabolic cooperation between tissue culture fibroblasts of Lesch-Nyhan disease and normal cells
    • Cox R.P., Krauss M.R., Balis M.E., and Dancis J. Evidence for transfer of enzyme product as the basis of metabolic cooperation between tissue culture fibroblasts of Lesch-Nyhan disease and normal cells. Proc. Natl. Acad. Sci. USA 67 (1970) 1573-1579
    • (1970) Proc. Natl. Acad. Sci. USA , vol.67 , pp. 1573-1579
    • Cox, R.P.1    Krauss, M.R.2    Balis, M.E.3    Dancis, J.4
  • 163
    • 0001641514 scopus 로고
    • Mutations of bacteria from virus sensitivity to virus resistance
    • Luria S.E., and Delbrück M. Mutations of bacteria from virus sensitivity to virus resistance. Genetics 28 (1943) 491-511
    • (1943) Genetics , vol.28 , pp. 491-511
    • Luria, S.E.1    Delbrück, M.2
  • 164
    • 0028790076 scopus 로고
    • Molecular nature of spontaneous mutations at the hypoxanthine-guanine phosphoribosyltransferase (hprt) locus in Chinese hamster ovary cells
    • Xu Z., Yu Y., Schwartz J.L., Meltz M.L., and Hsie A.W. Molecular nature of spontaneous mutations at the hypoxanthine-guanine phosphoribosyltransferase (hprt) locus in Chinese hamster ovary cells. Environ. Mol. Mutagen. 26 (1995) 127-138
    • (1995) Environ. Mol. Mutagen. , vol.26 , pp. 127-138
    • Xu, Z.1    Yu, Y.2    Schwartz, J.L.3    Meltz, M.L.4    Hsie, A.W.5
  • 165
    • 0031021813 scopus 로고    scopus 로고
    • Cloning and characterization of Chinese hamster p53 cDNA
    • Lee H., Larner J.M., and Hamlin J.L. Cloning and characterization of Chinese hamster p53 cDNA. Gene 184 (1997) 177-183
    • (1997) Gene , vol.184 , pp. 177-183
    • Lee, H.1    Larner, J.M.2    Hamlin, J.L.3
  • 166
    • 0032965702 scopus 로고    scopus 로고
    • Characterization of p53 in Chinese hamster cell lines CHO-K1, CHO-WBL, and CHL: implications for genotoxicity testing
    • Hu T., Miller C.M., Ridder G.M., and Aardema M.J. Characterization of p53 in Chinese hamster cell lines CHO-K1, CHO-WBL, and CHL: implications for genotoxicity testing. Mutat. Res. 426 (1999) 51-62
    • (1999) Mutat. Res. , vol.426 , pp. 51-62
    • Hu, T.1    Miller, C.M.2    Ridder, G.M.3    Aardema, M.J.4
  • 167
    • 0024357990 scopus 로고
    • Differences in the rates of gene amplification in nontumorigenic and tumorigenic cell lines as measured by Luria-Delbruck fluctuation analysis
    • Tlsty T.D., Margolin B.H., and Lum K. Differences in the rates of gene amplification in nontumorigenic and tumorigenic cell lines as measured by Luria-Delbruck fluctuation analysis. Proc. Natl. Acad. Sci. USA 86 (1989) 9441-9445
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 9441-9445
    • Tlsty, T.D.1    Margolin, B.H.2    Lum, K.3
  • 168
    • 33746255899 scopus 로고    scopus 로고
    • Gene amplification in cancer
    • Albertson D.G. Gene amplification in cancer. Trends Genet 22 (2006) 447-455
    • (2006) Trends Genet , vol.22 , pp. 447-455
    • Albertson, D.G.1
  • 169
    • 0026801062 scopus 로고
    • Altered cell cycle arrest and gene amplification potential accompany loss of wild-type p53
    • Livingstone L.R., White A., Sprouse J., Livanos E., Jacks T., and Tlsty T.D. Altered cell cycle arrest and gene amplification potential accompany loss of wild-type p53. Cell 70 (1992) 923-935
    • (1992) Cell , vol.70 , pp. 923-935
    • Livingstone, L.R.1    White, A.2    Sprouse, J.3    Livanos, E.4    Jacks, T.5    Tlsty, T.D.6
  • 170
    • 0023620862 scopus 로고
    • Hamster cells with increased rates of DNA amplification, a new phenotype
    • Giulotto E., Knights C., and Stark G.R. Hamster cells with increased rates of DNA amplification, a new phenotype. Cell 48 (1987) 837-845
    • (1987) Cell , vol.48 , pp. 837-845
    • Giulotto, E.1    Knights, C.2    Stark, G.R.3
  • 172
    • 0035361714 scopus 로고    scopus 로고
    • Increased gene amplification in immortal rodent cells deficient for the DNA-dependent protein kinase catalytic subunit
    • Mondello C., Rebuzzini P., Dolzan M., Edmonson S., Taccioli G.E., and Giulotto E. Increased gene amplification in immortal rodent cells deficient for the DNA-dependent protein kinase catalytic subunit. Cancer Res. 61 (2001) 4520-4525
    • (2001) Cancer Res. , vol.61 , pp. 4520-4525
    • Mondello, C.1    Rebuzzini, P.2    Dolzan, M.3    Edmonson, S.4    Taccioli, G.E.5    Giulotto, E.6
  • 174
    • 0027994653 scopus 로고
    • Modulation of the spontaneous G2 phase blockage in Fanconi anemia cells by caffeine: differences from cells arrested by X-irradiation
    • Seyschab H., Bretzel G., Friedl R., Schindler D., Sun Y., and Hoehn H. Modulation of the spontaneous G2 phase blockage in Fanconi anemia cells by caffeine: differences from cells arrested by X-irradiation. Mutat. Res. 308 (1994) 149-157
    • (1994) Mutat. Res. , vol.308 , pp. 149-157
    • Seyschab, H.1    Bretzel, G.2    Friedl, R.3    Schindler, D.4    Sun, Y.5    Hoehn, H.6
  • 176
    • 0029744915 scopus 로고    scopus 로고
    • The effect of the Fanconi anemia polypeptide, FAC, upon p53 induction and G2 checkpoint regulation
    • Kupfer G.M., and D'Andrea A.D. The effect of the Fanconi anemia polypeptide, FAC, upon p53 induction and G2 checkpoint regulation. Blood 88 (1996) 1019-1025
    • (1996) Blood , vol.88 , pp. 1019-1025
    • Kupfer, G.M.1    D'Andrea, A.D.2
  • 177
    • 0027282135 scopus 로고
    • Fanconi anemia. Chromosome breakage and cell cycle studies
    • Berger R., Le Coniat M., and Gendron M.C. Fanconi anemia. Chromosome breakage and cell cycle studies. Cancer Genet. Cytogenet 69 (1993) 13-16
    • (1993) Cancer Genet. Cytogenet , vol.69 , pp. 13-16
    • Berger, R.1    Le Coniat, M.2    Gendron, M.C.3
  • 178
    • 0028950319 scopus 로고
    • Comparative evaluation of diepoxybutane sensitivity and cell cycle blockage in the diagnosis of Fanconi anemia
    • Seyschab H., Friedl R., Sun Y., Schindler D., Hoehn H., Hentze S., and Schroeder-Kurth T. Comparative evaluation of diepoxybutane sensitivity and cell cycle blockage in the diagnosis of Fanconi anemia. Blood 85 (1995) 2233-2237
    • (1995) Blood , vol.85 , pp. 2233-2237
    • Seyschab, H.1    Friedl, R.2    Sun, Y.3    Schindler, D.4    Hoehn, H.5    Hentze, S.6    Schroeder-Kurth, T.7
  • 180
    • 0034332550 scopus 로고    scopus 로고
    • Damage-resistant DNA synthesis in Fanconi anemia cells treated with a DNA cross-linking agent
    • Centurion S.A., Kuo H.R., and Lambert W.C. Damage-resistant DNA synthesis in Fanconi anemia cells treated with a DNA cross-linking agent. Exp. Cell Res. 260 (2000) 216-221
    • (2000) Exp. Cell Res. , vol.260 , pp. 216-221
    • Centurion, S.A.1    Kuo, H.R.2    Lambert, W.C.3
  • 182
    • 34249995761 scopus 로고    scopus 로고
    • Loss of FANCC function is associated with failure to inhibit late firing replication origins after DNA cross-linking
    • Phelps R.A., Gingras H., and Hockenbery D.M. Loss of FANCC function is associated with failure to inhibit late firing replication origins after DNA cross-linking. Exp. Cell Res. 313 (2007) 2283-2292
    • (2007) Exp. Cell Res. , vol.313 , pp. 2283-2292
    • Phelps, R.A.1    Gingras, H.2    Hockenbery, D.M.3
  • 183
    • 1842576658 scopus 로고    scopus 로고
    • The DNA crosslink-induced S-phase checkpoint depends on ATR-CHK1 and ATR-NBS1-FANCD2 pathways
    • Pichierri P., and Rosselli F. The DNA crosslink-induced S-phase checkpoint depends on ATR-CHK1 and ATR-NBS1-FANCD2 pathways. EMBO J. 23 (2004) 1178-1187
    • (2004) EMBO J. , vol.23 , pp. 1178-1187
    • Pichierri, P.1    Rosselli, F.2
  • 185
    • 13244298119 scopus 로고    scopus 로고
    • Fanconi anemia proteins and the S phase checkpoint
    • Pichierri P., and Rosselli F. Fanconi anemia proteins and the S phase checkpoint. Cell Cycle 3 (2004) 698-700
    • (2004) Cell Cycle , vol.3 , pp. 698-700
    • Pichierri, P.1    Rosselli, F.2
  • 186
    • 9644301156 scopus 로고    scopus 로고
    • Human SNM1B is required for normal cellular response to both DNA interstrand crosslink-inducing agents and ionizing radiation
    • Demuth I., Digweed M., and Concannon P. Human SNM1B is required for normal cellular response to both DNA interstrand crosslink-inducing agents and ionizing radiation. Oncogene 23 (2004) 8611-8618
    • (2004) Oncogene , vol.23 , pp. 8611-8618
    • Demuth, I.1    Digweed, M.2    Concannon, P.3
  • 187
    • 50649091340 scopus 로고    scopus 로고
    • Snm1B/Apollo mediates replication fork collapse and S Phase checkpoint activation in response to DNA interstrand cross-links
    • Bae J.B., Mukhopadhyay S.S., Liu L., Zhang N., Tan J., Akhter S., Liu X., Shen X., Li L., and Legerski R.J. Snm1B/Apollo mediates replication fork collapse and S Phase checkpoint activation in response to DNA interstrand cross-links. Oncogene 27 (2008) 5045-5056
    • (2008) Oncogene , vol.27 , pp. 5045-5056
    • Bae, J.B.1    Mukhopadhyay, S.S.2    Liu, L.3    Zhang, N.4    Tan, J.5    Akhter, S.6    Liu, X.7    Shen, X.8    Li, L.9    Legerski, R.J.10
  • 188
  • 191
    • 11244337035 scopus 로고    scopus 로고
    • The Fanconi anemia core complex associates with chromatin during S phase
    • Mi J., and Kupfer G.M. The Fanconi anemia core complex associates with chromatin during S phase. Blood 105 (2005) 759-766
    • (2005) Blood , vol.105 , pp. 759-766
    • Mi, J.1    Kupfer, G.M.2
  • 193
    • 33748656748 scopus 로고    scopus 로고
    • Phosphorylation of FANCD2 on two novel sites is required for mitomycin C resistance
    • Ho G.P., Margossian S., Taniguchi T., and D'Andrea A.D. Phosphorylation of FANCD2 on two novel sites is required for mitomycin C resistance. Mol. Cell. Biol. 26 (2006) 7005-7015
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 7005-7015
    • Ho, G.P.1    Margossian, S.2    Taniguchi, T.3    D'Andrea, A.D.4
  • 194
    • 14844288960 scopus 로고    scopus 로고
    • Post-irradiation phosphorylation of structural maintenance chromosome 1 (SMC1) is independent of the Fanconi protein pathway
    • Nahas S.A., Lai C.H., and Gatti R.A. Post-irradiation phosphorylation of structural maintenance chromosome 1 (SMC1) is independent of the Fanconi protein pathway. Int. J. Radiat. Oncol. Biol. Phys. 61 (2005) 1167-1172
    • (2005) Int. J. Radiat. Oncol. Biol. Phys. , vol.61 , pp. 1167-1172
    • Nahas, S.A.1    Lai, C.H.2    Gatti, R.A.3
  • 196
    • 33749989371 scopus 로고    scopus 로고
    • Drosophila homologs of FANCD2 and FANCL function in DNA repair
    • Marek L.R., and Bale A.E. Drosophila homologs of FANCD2 and FANCL function in DNA repair. DNA Repair (Amst) 5 (2006) 1317-1326
    • (2006) DNA Repair (Amst) , vol.5 , pp. 1317-1326
    • Marek, L.R.1    Bale, A.E.2
  • 197
    • 33750020933 scopus 로고    scopus 로고
    • C. elegans FANCD2 responds to replication stress and functions in interstrand cross-link repair
    • Collis S.J., Barber L.J., Ward J.D., Martin J.S., and Boulton S.J. C. elegans FANCD2 responds to replication stress and functions in interstrand cross-link repair. DNA Repair (Amst) 5 (2006) 1398-1406
    • (2006) DNA Repair (Amst) , vol.5 , pp. 1398-1406
    • Collis, S.J.1    Barber, L.J.2    Ward, J.D.3    Martin, J.S.4    Boulton, S.J.5
  • 201
    • 0030831350 scopus 로고    scopus 로고
    • The Fanconi anemia polypeptide, FAC, binds to the cyclin-dependent kinase, cdc2
    • Kupfer G.M., Yamashita T., Naf D., Suliman A., Asano S., and D'Andrea A.D. The Fanconi anemia polypeptide, FAC, binds to the cyclin-dependent kinase, cdc2. Blood 90 (1997) 1047-1054
    • (1997) Blood , vol.90 , pp. 1047-1054
    • Kupfer, G.M.1    Yamashita, T.2    Naf, D.3    Suliman, A.4    Asano, S.5    D'Andrea, A.D.6
  • 203
    • 0035032649 scopus 로고    scopus 로고
    • Involvement of Brca1 in S-phase and G(2)-phase checkpoints after ionizing irradiation
    • Xu B., Kim S.T., and Kastan M.B. Involvement of Brca1 in S-phase and G(2)-phase checkpoints after ionizing irradiation. Mol. Cell. Biol. 21 (2001) 3445-3450
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 3445-3450
    • Xu, B.1    Kim, S.T.2    Kastan, M.B.3
  • 204
    • 0036510163 scopus 로고    scopus 로고
    • BRCA1 regulates the G2/M checkpoint by activating Chk1 kinase upon DNA damage
    • Yarden R.I., Pardo-Reoyo S., Sgagias M., Cowan K.H., and Brody L.C. BRCA1 regulates the G2/M checkpoint by activating Chk1 kinase upon DNA damage. Nat. Genet. 30 (2002) 285-289
    • (2002) Nat. Genet. , vol.30 , pp. 285-289
    • Yarden, R.I.1    Pardo-Reoyo, S.2    Sgagias, M.3    Cowan, K.H.4    Brody, L.C.5
  • 205
    • 0142147272 scopus 로고    scopus 로고
    • The BRCT domain is a phospho-protein binding domain
    • Yu X., Chini C.C., He M., Mer G., and Chen J. The BRCT domain is a phospho-protein binding domain. Science 302 (2003) 639-642
    • (2003) Science , vol.302 , pp. 639-642
    • Yu, X.1    Chini, C.C.2    He, M.3    Mer, G.4    Chen, J.5
  • 206
    • 0028957889 scopus 로고
    • Nuclear foci of mammalian Rad51 recombination protein in somatic cells after DNA damage and its localization in synaptonemal complexes
    • Haaf T., Golub E.I., Reddy G., Radding C.M., and Ward D.C. Nuclear foci of mammalian Rad51 recombination protein in somatic cells after DNA damage and its localization in synaptonemal complexes. Proc. Natl. Acad. Sci. USA 92 (1995) 2298-2302
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 2298-2302
    • Haaf, T.1    Golub, E.I.2    Reddy, G.3    Radding, C.M.4    Ward, D.C.5
  • 207
    • 0030764691 scopus 로고    scopus 로고
    • hMre11 and hRad50 nuclear foci are induced during the normal cellular response to DNA double-strand breaks
    • Maser R.S., Monsen K.J., Nelms B.E., and Petrini J.H.J. hMre11 and hRad50 nuclear foci are induced during the normal cellular response to DNA double-strand breaks. Mol. Cell. Biol. 17 (1997) 6097-6104
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 6097-6104
    • Maser, R.S.1    Monsen, K.J.2    Nelms, B.E.3    Petrini, J.H.J.4
  • 208
    • 0033179235 scopus 로고    scopus 로고
    • BRCA2 is required for ionizing radiation-induced assembly of Rad51 complex in vivo
    • Yuan S.S., Lee S.Y., Chen G., Song M., Tomlinson G.E., and Lee E.Y. BRCA2 is required for ionizing radiation-induced assembly of Rad51 complex in vivo. Cancer Res. 59 (1999) 3547-3551
    • (1999) Cancer Res. , vol.59 , pp. 3547-3551
    • Yuan, S.S.1    Lee, S.Y.2    Chen, G.3    Song, M.4    Tomlinson, G.E.5    Lee, E.Y.6
  • 210
    • 53549087771 scopus 로고    scopus 로고
    • Cell-cycle coordination between DNA replication and recombination revealed by a vertebrate N-end rule degron-Rad51
    • Su X., Bernal J.A., and Venkitaraman A.R. Cell-cycle coordination between DNA replication and recombination revealed by a vertebrate N-end rule degron-Rad51. Nat. Struct. Mol. Biol. 15 (2008) 1049-1058
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 1049-1058
    • Su, X.1    Bernal, J.A.2    Venkitaraman, A.R.3
  • 211
    • 0037173719 scopus 로고    scopus 로고
    • Impaired DNA damage-induced nuclear Rad51 foci formation uniquely characterizes Fanconi anemia group D1
    • Godthelp B.C., Artwert F., Joenje H., and Zdzienicka M.Z. Impaired DNA damage-induced nuclear Rad51 foci formation uniquely characterizes Fanconi anemia group D1. Oncogene 21 (2002) 5002-5005
    • (2002) Oncogene , vol.21 , pp. 5002-5005
    • Godthelp, B.C.1    Artwert, F.2    Joenje, H.3    Zdzienicka, M.Z.4
  • 212
    • 31644434780 scopus 로고    scopus 로고
    • Inducibility of nuclear Rad51 foci after DNA damage distinguishes all Fanconi anemia complementation groups from D1/BRCA2
    • Godthelp B.C., Wiegant W.W., Waisfisz Q., Medhurst A.L., Arwert F., Joenje H., and Zdzienicka M.Z. Inducibility of nuclear Rad51 foci after DNA damage distinguishes all Fanconi anemia complementation groups from D1/BRCA2. Mutat. Res. 594 (2006) 39-48
    • (2006) Mutat. Res. , vol.594 , pp. 39-48
    • Godthelp, B.C.1    Wiegant, W.W.2    Waisfisz, Q.3    Medhurst, A.L.4    Arwert, F.5    Joenje, H.6    Zdzienicka, M.Z.7
  • 213
    • 2942705849 scopus 로고    scopus 로고
    • Functional interaction of monoubiquitinated FANCD2 and BRCA2/FANCD1 in chromatin
    • Wang X., Andreassen P.R., and D'Andrea A.D. Functional interaction of monoubiquitinated FANCD2 and BRCA2/FANCD1 in chromatin. Mol. Cell. Biol. 24 (2004) 5850-5862
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 5850-5862
    • Wang, X.1    Andreassen, P.R.2    D'Andrea, A.D.3
  • 215
    • 34247497770 scopus 로고    scopus 로고
    • XRCC4 in G1 suppresses homologous recombination in S/G2, in G1 checkpoint-defective cells
    • Saintigny Y., Delacote F., Boucher D., Averbeck D., and Lopez B.S. XRCC4 in G1 suppresses homologous recombination in S/G2, in G1 checkpoint-defective cells. Oncogene 26 (2007) 2769-2780
    • (2007) Oncogene , vol.26 , pp. 2769-2780
    • Saintigny, Y.1    Delacote, F.2    Boucher, D.3    Averbeck, D.4    Lopez, B.S.5
  • 218
    • 0035655724 scopus 로고    scopus 로고
    • Function of the Fanconi anemia pathway in Fanconi anemia complementation group F and D1 cells
    • Siddique M.A., Nakanishi K., Taniguchi T., Grompe M., and D'Andrea A.D. Function of the Fanconi anemia pathway in Fanconi anemia complementation group F and D1 cells. Exp. Hematol. 29 (2001) 1448-1455
    • (2001) Exp. Hematol. , vol.29 , pp. 1448-1455
    • Siddique, M.A.1    Nakanishi, K.2    Taniguchi, T.3    Grompe, M.4    D'Andrea, A.D.5
  • 220
    • 4043133287 scopus 로고    scopus 로고
    • ATR couples FANCD2 monoubiquitination to the DNA-damage response
    • Andreassen P.R., D'Andrea A.D., and Taniguchi T. ATR couples FANCD2 monoubiquitination to the DNA-damage response. Genes Dev. 18 (2004) 1958-1963
    • (2004) Genes Dev. , vol.18 , pp. 1958-1963
    • Andreassen, P.R.1    D'Andrea, A.D.2    Taniguchi, T.3
  • 222
    • 34547628200 scopus 로고    scopus 로고
    • Proteasome function is required for DNA damage response and fanconi anemia pathway activation
    • Jacquemont C., and Taniguchi T. Proteasome function is required for DNA damage response and fanconi anemia pathway activation. Cancer Res. 67 (2007) 7395-7405
    • (2007) Cancer Res. , vol.67 , pp. 7395-7405
    • Jacquemont, C.1    Taniguchi, T.2
  • 225
    • 25144492769 scopus 로고    scopus 로고
    • Unraveling the Fanconi anemia-DNA repair connection
    • Thompson L.H. Unraveling the Fanconi anemia-DNA repair connection. Nat. Genet. 37 (2005) 921-922
    • (2005) Nat. Genet. , vol.37 , pp. 921-922
    • Thompson, L.H.1
  • 226
    • 33847059931 scopus 로고    scopus 로고
    • The Fanconi anemia signalosome anchor
    • Niedernhofer L.J. The Fanconi anemia signalosome anchor. Mol. Cell 25 (2007) 487-490
    • (2007) Mol. Cell , vol.25 , pp. 487-490
    • Niedernhofer, L.J.1
  • 227
    • 29244489543 scopus 로고    scopus 로고
    • Fanconi anemia (cross)linked to DNA Repair
    • Niedernhofer L.J., Lalai A.S., and Hoeijmakers J.H. Fanconi anemia (cross)linked to DNA Repair. Cell 123 (2005) 1191-1198
    • (2005) Cell , vol.123 , pp. 1191-1198
    • Niedernhofer, L.J.1    Lalai, A.S.2    Hoeijmakers, J.H.3
  • 228
    • 50649091874 scopus 로고    scopus 로고
    • Structural and functional relationships of the XPF/MUS81 family of proteins
    • Ciccia A., McDonald N., and West S.C. Structural and functional relationships of the XPF/MUS81 family of proteins. Annu. Rev. Biochem. 77 (2008) 259-287
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 259-287
    • Ciccia, A.1    McDonald, N.2    West, S.C.3
  • 229
  • 230
    • 0017298802 scopus 로고
    • A model for replication repair in mammalian cells
    • Higgins N.P., Kato K., and Strauss B. A model for replication repair in mammalian cells. J. Mol. Biol. 101 (1976) 417-425
    • (1976) J. Mol. Biol. , vol.101 , pp. 417-425
    • Higgins, N.P.1    Kato, K.2    Strauss, B.3
  • 232
    • 33747352774 scopus 로고    scopus 로고
    • The Bloom's syndrome helicase can promote the regression of a model replication fork
    • Ralf C., Hickson I.D., and Wu L. The Bloom's syndrome helicase can promote the regression of a model replication fork. J. Biol. Chem. 281 (2006) 22839-22846
    • (2006) J. Biol. Chem. , vol.281 , pp. 22839-22846
    • Ralf, C.1    Hickson, I.D.2    Wu, L.3
  • 233
    • 0034665121 scopus 로고    scopus 로고
    • Ataxia telangiectasia-related protein is involved in the phosphorylation of BRCA1 following deoxyribonucleic acid damage
    • Chen J. Ataxia telangiectasia-related protein is involved in the phosphorylation of BRCA1 following deoxyribonucleic acid damage. Cancer Res. 60 (2000) 5037-5039
    • (2000) Cancer Res. , vol.60 , pp. 5037-5039
    • Chen, J.1
  • 234
    • 55549103709 scopus 로고    scopus 로고
    • A major switch for the Fanconi anemia DNA damage-response pathway
    • Wang W. A major switch for the Fanconi anemia DNA damage-response pathway. Nat. Struct. Mol. Biol. 15 (2008) 1128-1130
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 1128-1130
    • Wang, W.1
  • 235
    • 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., and Kanaar R. The structure-specific endonuclease Mus81-Eme1 promotes conversion of interstrand DNA crosslinks into double-strands breaks. EMBO J. 25 (2006) 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
  • 236
    • 23844468833 scopus 로고    scopus 로고
    • Disruption of murine Mus81 increases genomic instability and DNA damage sensitivity but does not promote tumorigenesis
    • Dendouga N., Gao H., Moechars D., Janicot M., Vialard J., and McGowan C.H. Disruption of murine Mus81 increases genomic instability and DNA damage sensitivity but does not promote tumorigenesis. Mol. Cell. Biol. 25 (2005) 7569-7679
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 7569-7679
    • Dendouga, N.1    Gao, H.2    Moechars, D.3    Janicot, M.4    Vialard, J.5    McGowan, C.H.6
  • 239
    • 0021824209 scopus 로고
    • Defective DNA cross-link removal in Chinese hamster cell mutants hypersensitive to bifunctional alkylating agents
    • Hoy C.A., Thompson L.H., Mooney C.L., and Salazar E.P. Defective DNA cross-link removal in Chinese hamster cell mutants hypersensitive to bifunctional alkylating agents. Cancer Res. 45 (1985) 1737-1743
    • (1985) Cancer Res. , vol.45 , pp. 1737-1743
    • Hoy, C.A.1    Thompson, L.H.2    Mooney, C.L.3    Salazar, E.P.4
  • 240
    • 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 I.U., McHugh P.J., Clingen P.H., and Hartley J.A. Defects in interstrand cross-link uncoupling do not account for the extreme sensitivity of ERCC1 and XPF cells to cisplatin. Nucleic Acids Res. 30 (2002) 3848-3856
    • (2002) Nucleic Acids Res. , vol.30 , pp. 3848-3856
    • De Silva, I.U.1    McHugh, P.J.2    Clingen, P.H.3    Hartley, J.A.4
  • 241
    • 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., and Wood R.D. Repair of an interstrand DNA cross-link initiated by ERCC1-XPF repair/recombination nuclease. J. Biol. Chem. 275 (2000) 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
  • 242
    • 38549146496 scopus 로고    scopus 로고
    • Interstrand crosslink repair: can XPF-ERCC1 be let off the hook?
    • Bergstralh D.T., and Sekelsky J. Interstrand crosslink repair: can XPF-ERCC1 be let off the hook?. Trends Genet. 24 (2008) 70-76
    • (2008) Trends Genet. , vol.24 , pp. 70-76
    • Bergstralh, D.T.1    Sekelsky, J.2
  • 244
    • 21844445309 scopus 로고    scopus 로고
    • Analysis of the DNA substrate specificity of the human BACH1 helicase associated with breast cancer
    • Gupta R., Sharma S., Sommers J.A., Jin Z., Cantor S.B., and Brosh Jr. R.M. Analysis of the DNA substrate specificity of the human BACH1 helicase associated with breast cancer. J. Biol. Chem. 280 (2005) 25450-25460
    • (2005) J. Biol. Chem. , vol.280 , pp. 25450-25460
    • Gupta, R.1    Sharma, S.2    Sommers, J.A.3    Jin, Z.4    Cantor, S.B.5    Brosh Jr., R.M.6
  • 246
    • 34447318130 scopus 로고    scopus 로고
    • The FANCJ/MutLalpha interaction is required for correction of the cross-link response in FA-J cells
    • Peng M., Litman R., Xie J., Sharma S., Brosh Jr. R.M., and Cantor S.B. The FANCJ/MutLalpha interaction is required for correction of the cross-link response in FA-J cells. EMBO J. 26 (2007) 3238-3249
    • (2007) EMBO J. , vol.26 , pp. 3238-3249
    • Peng, M.1    Litman, R.2    Xie, J.3    Sharma, S.4    Brosh Jr., R.M.5    Cantor, S.B.6
  • 247
    • 0034717283 scopus 로고    scopus 로고
    • Identification of a second MutL DNA mismatch repair complex (hPMS1 and hMLH1) in human epithelial cells
    • Leung W.K., Kim J.J., Wu L., Sepulveda J.L., and Sepulveda A.R. Identification of a second MutL DNA mismatch repair complex (hPMS1 and hMLH1) in human epithelial cells. J. Biol. Chem. 275 (2000) 15728-15732
    • (2000) J. Biol. Chem. , vol.275 , pp. 15728-15732
    • Leung, W.K.1    Kim, J.J.2    Wu, L.3    Sepulveda, J.L.4    Sepulveda, A.R.5
  • 249
    • 0038823615 scopus 로고    scopus 로고
    • Structure and enzymatic properties of a stable complex of the human REV1 and REV7 proteins
    • Masuda Y., Ohmae M., Masuda K., and Kamiya K. Structure and enzymatic properties of a stable complex of the human REV1 and REV7 proteins. J. Biol. Chem. 278 (2003) 12356-12360
    • (2003) J. Biol. Chem. , vol.278 , pp. 12356-12360
    • Masuda, Y.1    Ohmae, M.2    Masuda, K.3    Kamiya, K.4
  • 253
    • 33646183367 scopus 로고    scopus 로고
    • DNA damage responses and their many interactions with the replication fork
    • Andreassen P.R., Ho G.P., and D'Andrea A.D. DNA damage responses and their many interactions with the replication fork. Carcinogenesis 27 (2006) 883-892
    • (2006) Carcinogenesis , vol.27 , pp. 883-892
    • Andreassen, P.R.1    Ho, G.P.2    D'Andrea, A.D.3
  • 254
    • 34748890424 scopus 로고    scopus 로고
    • Activation of BRCA1/BRCA2-associated helicase BACH1 is required for timely progression through S phase
    • Kumaraswamy E., and Shiekhattar R. Activation of BRCA1/BRCA2-associated helicase BACH1 is required for timely progression through S phase. Mol. Cell. Biol. 27 (2007) 6733-6741
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 6733-6741
    • Kumaraswamy, E.1    Shiekhattar, R.2
  • 255
    • 0035501412 scopus 로고    scopus 로고
    • SUVi and BACH1: a new subfamily of mammalian helicases?
    • Menichini P., and Linial M. SUVi and BACH1: a new subfamily of mammalian helicases?. Mutat. Res. 487 (2001) 67-71
    • (2001) Mutat. Res. , vol.487 , pp. 67-71
    • Menichini, P.1    Linial, M.2
  • 257
    • 45449102827 scopus 로고    scopus 로고
    • Mutagenic capacity of endogenous G4 DNA underlies genome instability in FANCJ-defective C. elegans
    • Kruisselbrink E., Guryev V., Brouwer K., Pontier D.B., Cuppen E., and Tijsterman M. Mutagenic capacity of endogenous G4 DNA underlies genome instability in FANCJ-defective C. elegans. Curr. Biol. 18 (2008) 900-905
    • (2008) Curr. Biol. , vol.18 , pp. 900-905
    • Kruisselbrink, E.1    Guryev, V.2    Brouwer, K.3    Pontier, D.B.4    Cuppen, E.5    Tijsterman, M.6
  • 259
    • 14644391577 scopus 로고    scopus 로고
    • The Fanconi anemia pathway is required for the DNA replication stress response and for the regulation of common fragile site stability
    • Howlett N.G., Taniguchi T., Durkin S.G., D'Andrea A.D., and Glover T.W. The Fanconi anemia pathway is required for the DNA replication stress response and for the regulation of common fragile site stability. Hum. Mol. Genet. 14 (2005) 693-701
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 693-701
    • Howlett, N.G.1    Taniguchi, T.2    Durkin, S.G.3    D'Andrea, A.D.4    Glover, T.W.5
  • 262
    • 0000102949 scopus 로고
    • Poly(ADP-ribose) polymerase: a molecular nick-sensor
    • de Murcia G., de J.M., and Murcia. Poly(ADP-ribose) polymerase: a molecular nick-sensor. Trends Biochem. Sci. 19 (1994) 172-176
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 172-176
    • de Murcia, G.1    de, J.M.2    Murcia3
  • 263
    • 0142009654 scopus 로고    scopus 로고
    • A requirement for PARP-1 for the assembly or stability of XRCC1 nuclear foci at sites of oxidative DNA damage
    • El-Khamisy S.F., Masutani M., Suzuki H., and Caldecott K.W. A requirement for PARP-1 for the assembly or stability of XRCC1 nuclear foci at sites of oxidative DNA damage. Nucleic Acids Res. 31 (2003) 5526-5533
    • (2003) Nucleic Acids Res. , vol.31 , pp. 5526-5533
    • El-Khamisy, S.F.1    Masutani, M.2    Suzuki, H.3    Caldecott, K.W.4
  • 266
    • 57349106091 scopus 로고    scopus 로고
    • Chromosomal instability syndromes are sensitive to poly ADP ribose polymerase inhibitors
    • Gaymes T.J., Shall S., Farzaneh F., and Mufti G.J. Chromosomal instability syndromes are sensitive to poly ADP ribose polymerase inhibitors. Haematologica 93 (2008) 1886-1889
    • (2008) Haematologica , vol.93 , pp. 1886-1889
    • Gaymes, T.J.1    Shall, S.2    Farzaneh, F.3    Mufti, G.J.4
  • 268
    • 0034102337 scopus 로고    scopus 로고
    • ATR disruption leads to chromosomal fragmentation and early embryonic lethality
    • Brown E.J., and Baltimore D. ATR disruption leads to chromosomal fragmentation and early embryonic lethality. Genes Dev. 14 (2000) 397-402
    • (2000) Genes Dev. , vol.14 , pp. 397-402
    • Brown, E.J.1    Baltimore, D.2
  • 269
    • 28244497051 scopus 로고    scopus 로고
    • Depletion of Chk1 leads to premature activation of Cdc2-cyclin B and mitotic catastrophe
    • Niida H., Tsuge S., Katsuno Y., Konishi A., Takeda N., and Nakanishi M. Depletion of Chk1 leads to premature activation of Cdc2-cyclin B and mitotic catastrophe. J. Biol. Chem. 280 (2005) 39246-39252
    • (2005) J. Biol. Chem. , vol.280 , pp. 39246-39252
    • Niida, H.1    Tsuge, S.2    Katsuno, Y.3    Konishi, A.4    Takeda, N.5    Nakanishi, M.6
  • 271
    • 0033594904 scopus 로고    scopus 로고
    • Disruption of mRad50 causes embryonic stem cell lethality, abnormal embryonic development, and sensitivity to ionising radiation
    • Luo G., Yao M.S., Bender C.F., Mills M., Bladl A.R., Bradley A., and Petrini J.H. Disruption of mRad50 causes embryonic stem cell lethality, abnormal embryonic development, and sensitivity to ionising radiation. Proc. Natl. Acad. Sci. USA 96 (1999) 7376-7381
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 7376-7381
    • Luo, G.1    Yao, M.S.2    Bender, C.F.3    Mills, M.4    Bladl, A.R.5    Bradley, A.6    Petrini, J.H.7
  • 272
    • 0032542216 scopus 로고    scopus 로고
    • A targeted disruption of the murine Brca1 gene causes gamma-irradiation hypersensitivity and genetic instability
    • Shen S.X., Weaver Z., Xu X., Li C., Weinstein M., Chen L., Guan X.Y., Ried T., and Deng C.X. A targeted disruption of the murine Brca1 gene causes gamma-irradiation hypersensitivity and genetic instability. Oncogene 17 (1998) 3115-3124
    • (1998) Oncogene , vol.17 , pp. 3115-3124
    • Shen, S.X.1    Weaver, Z.2    Xu, X.3    Li, C.4    Weinstein, M.5    Chen, L.6    Guan, X.Y.7    Ried, T.8    Deng, C.X.9
  • 273
    • 49649113678 scopus 로고    scopus 로고
    • Cellular functions of human RPA1. Multiple roles of domains in replication, repair, and checkpoints
    • Haring S.J., Mason A.C., Binz S.K., and Wold M.S. Cellular functions of human RPA1. Multiple roles of domains in replication, repair, and checkpoints. J. Biol. Chem. 283 (2008) 19095-19111
    • (2008) J. Biol. Chem. , vol.283 , pp. 19095-19111
    • Haring, S.J.1    Mason, A.C.2    Binz, S.K.3    Wold, M.S.4
  • 277
    • 0035936554 scopus 로고    scopus 로고
    • Targeted disruption of the Nijmegen breakage syndrome gene NBS1 leads to early embryonic lethality in mice
    • Zhu J., Petersen S., Tessarollo L., and Nussenzweig A. Targeted disruption of the Nijmegen breakage syndrome gene NBS1 leads to early embryonic lethality in mice. Curr. Biol. 11 (2001) 105-109
    • (2001) Curr. Biol. , vol.11 , pp. 105-109
    • Zhu, J.1    Petersen, S.2    Tessarollo, L.3    Nussenzweig, A.4
  • 278
    • 33750309537 scopus 로고    scopus 로고
    • Replication-coupled repair of crotonaldehyde/acetaldehyde-induced guanine-guanine interstrand cross-links and their mutagenicity
    • Liu X., Lao Y., Yang I.Y., Hecht S.S., and Moriya M. Replication-coupled repair of crotonaldehyde/acetaldehyde-induced guanine-guanine interstrand cross-links and their mutagenicity. Biochemistry 45 (2006) 12898-12905
    • (2006) Biochemistry , vol.45 , pp. 12898-12905
    • Liu, X.1    Lao, Y.2    Yang, I.Y.3    Hecht, S.S.4    Moriya, M.5
  • 281
    • 33646048054 scopus 로고    scopus 로고
    • DNA repair: DNA polymerase zeta and Rev1 break in
    • Kolas N.K., and Durocher D. DNA repair: DNA polymerase zeta and Rev1 break in. Curr. Biol. 16 (2006) R296-R299
    • (2006) Curr. Biol. , vol.16
    • Kolas, N.K.1    Durocher, D.2


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