메뉴 건너뛰기




Volumn 5, Issue 9-10, 2006, Pages 1119-1125

Dedicated to the core: Understanding the Fanconi anemia complex

Author keywords

DNA repair; E3 ligase; Fanconi anemia; Mono ubiquitination

Indexed keywords

FANCONI ANEMIA COMPLEMENTATION GROUP M PROTEIN; FANCONI ANEMIA GROUP D2 PROTEIN; FANCONI ANEMIA GROUP L PROTEIN; PROTEIN; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG;

EID: 33747883762     PISSN: 15687864     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.dnarep.2006.05.009     Document Type: Article
Times cited : (52)

References (64)
  • 1
    • 0037268338 scopus 로고    scopus 로고
    • The Fanconi anaemia/BRCA pathway
    • D'Andrea A.D., and Grompe M. The Fanconi anaemia/BRCA pathway. Nat. Rev. Cancer 3 1 (2003) 23-34
    • (2003) Nat. Rev. Cancer , vol.3 , Issue.1 , pp. 23-34
    • D'Andrea, A.D.1    Grompe, M.2
  • 3
    • 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 7 (2005) 1191-1198
    • (2005) Cell , vol.123 , Issue.7 , pp. 1191-1198
    • Niedernhofer, L.J.1    Lalai, A.S.2    Hoeijmakers, J.H.3
  • 4
    • 17744394476 scopus 로고    scopus 로고
    • Positional cloning of a novel Fanconi anemia gene, FANCD2
    • Timmers C., et al. Positional cloning of a novel Fanconi anemia gene, FANCD2. Mol. Cell. 7 2 (2001) 241-248
    • (2001) Mol. Cell. , vol.7 , Issue.2 , pp. 241-248
    • Timmers, C.1
  • 5
    • 25144457604 scopus 로고    scopus 로고
    • The DNA helicase BRIP1 is defective in Fanconi anemia complementation group
    • Levitus M., et al. The DNA helicase BRIP1 is defective in Fanconi anemia complementation group. J. Nat. Genet 37 9 (2005) 934-935
    • (2005) J. Nat. Genet , vol.37 , Issue.9 , pp. 934-935
    • Levitus, M.1
  • 6
    • 25144497571 scopus 로고    scopus 로고
    • The BRCA1-interacting helicase BRIP1 is deficient in Fanconi anemia
    • Levran O., et al. The BRCA1-interacting helicase BRIP1 is deficient in Fanconi anemia. Nat. Genet 37 9 (2005) 931-933
    • (2005) Nat. Genet , vol.37 , Issue.9 , pp. 931-933
    • Levran, O.1
  • 7
    • 1842337370 scopus 로고    scopus 로고
    • Expression cloning of a cDNA for the major Fanconi anaemia gene
    • Lo Ten Foe J.R., et al. Expression cloning of a cDNA for the major Fanconi anaemia gene. FAA. Nat. Genet 14 3 (1996) 320-323
    • (1996) FAA. Nat. Genet , vol.14 , Issue.3 , pp. 320-323
    • Lo Ten Foe, J.R.1
  • 8
    • 0026735882 scopus 로고
    • Cloning of cDNAs for Fanconi's anaemia by functional complementation
    • Strathdee C.A., et al. Cloning of cDNAs for Fanconi's anaemia by functional complementation. Nature 358 6385 (1992) 434
    • (1992) Nature , vol.358 , Issue.6385 , pp. 434
    • Strathdee, C.A.1
  • 9
    • 0033759693 scopus 로고    scopus 로고
    • Isolation of a cDNA representing the Fanconi anemia complementation group E gene
    • de Winter J.P., et al. Isolation of a cDNA representing the Fanconi anemia complementation group E gene. Am. J. Hum. Genet 67 5 (2000) 1306-1308
    • (2000) Am. J. Hum. Genet , vol.67 , Issue.5 , pp. 1306-1308
    • de Winter, J.P.1
  • 10
    • 0033989248 scopus 로고    scopus 로고
    • The Fanconi anaemia gene FANCF encodes a novel protein with homology to ROM
    • de Winter J.P., et al. The Fanconi anaemia gene FANCF encodes a novel protein with homology to ROM. Nat. Genet 24 1 (2000) 15-16
    • (2000) Nat. Genet , vol.24 , Issue.1 , pp. 15-16
    • de Winter, J.P.1
  • 11
    • 17344363009 scopus 로고    scopus 로고
    • The Fanconi anaemia group G gene FANCG is identical with XRCC9
    • de Winter J.P., et al. The Fanconi anaemia group G gene FANCG is identical with XRCC9. Nat. Genet 20 3 (1998) 281-283
    • (1998) Nat. Genet , vol.20 , Issue.3 , pp. 281-283
    • de Winter, J.P.1
  • 12
    • 10944239213 scopus 로고    scopus 로고
    • X-linked inheritance of Fanconi anemia complementation group B
    • Meetei A.R., et al. X-linked inheritance of Fanconi anemia complementation group B. Nat. Genet 36 11 (2004) 1219-1224
    • (2004) Nat. Genet , vol.36 , Issue.11 , pp. 1219-1224
    • Meetei, A.R.1
  • 13
    • 0141484612 scopus 로고    scopus 로고
    • A novel ubiquitin ligase is deficient in Fanconi anemia
    • Meetei A.R., et al. A novel ubiquitin ligase is deficient in Fanconi anemia. Nat. Genet 35 2 (2003) 165-170
    • (2003) Nat. Genet , vol.35 , Issue.2 , pp. 165-170
    • Meetei, A.R.1
  • 14
    • 25144449181 scopus 로고    scopus 로고
    • A human ortholog of archaeal DNA repair protein Hef is defective in Fanconi anemia complementation group M
    • Meetei A.R., et al. A human ortholog of archaeal DNA repair protein Hef is defective in Fanconi anemia complementation group M. Nat. Genet 37 9 (2005) 958-963
    • (2005) Nat. Genet , vol.37 , Issue.9 , pp. 958-963
    • Meetei, A.R.1
  • 15
    • 18444362122 scopus 로고    scopus 로고
    • Biallelic inactivation of BRCA2 in Fanconi anemia
    • Howlett N.G., et al. Biallelic inactivation of BRCA2 in Fanconi anemia. Science 297 5581 (2002) 606-609
    • (2002) Science , vol.297 , Issue.5581 , pp. 606-609
    • Howlett, N.G.1
  • 16
    • 24944575242 scopus 로고    scopus 로고
    • BACH1 is critical for homologous recombination and appears to be the Fanconi anemia gene product FANCJ
    • Litman R., et al. BACH1 is critical for homologous recombination and appears to be the Fanconi anemia gene product FANCJ. Cancer Cell. 8 3 (2005) 255-265
    • (2005) Cancer Cell. , vol.8 , Issue.3 , pp. 255-265
    • Litman, R.1
  • 17
    • 26944499485 scopus 로고    scopus 로고
    • The vertebrate Hef ortholog is a component of the Fanconi anemia tumor-suppressor pathway
    • Mosedale G., et al. The vertebrate Hef ortholog is a component of the Fanconi anemia tumor-suppressor pathway. Nat. Struct. Mol. Biol. 12 9 (2005) 763-771
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , Issue.9 , pp. 763-771
    • Mosedale, G.1
  • 18
    • 0035105291 scopus 로고    scopus 로고
    • Interaction of the Fanconi anemia proteins and BRCA1 in a common pathway
    • Garcia-Higuera I., et al. Interaction of the Fanconi anemia proteins and BRCA1 in a common pathway. Mol. Cell. 7 2 (2001) 249-262
    • (2001) Mol. Cell. , vol.7 , Issue.2 , pp. 249-262
    • Garcia-Higuera, I.1
  • 19
    • 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 13 (2004) 5850-5862
    • (2004) Mol. Cell. Biol. , vol.24 , Issue.13 , pp. 5850-5862
    • Wang, X.1    Andreassen, P.R.2    D'Andrea, A.D.3
  • 20
    • 4544280871 scopus 로고    scopus 로고
    • Interaction of FANCD2 and NBS1 in the DNA damage response
    • Nakanishi K., et al. Interaction of FANCD2 and NBS1 in the DNA damage response. Nat. Cell. Biol. 4 12 (2002) 913-920
    • (2002) Nat. Cell. Biol. , vol.4 , Issue.12 , pp. 913-920
    • Nakanishi, K.1
  • 21
    • 29144506137 scopus 로고    scopus 로고
    • The Fanconi Anemia/BRCA pathway: new faces in the crowd
    • Kennedy R.D., and D'Andrea A.D. The Fanconi Anemia/BRCA pathway: new faces in the crowd. Genes Dev. 19 24 (2005) 2925-2940
    • (2005) Genes Dev. , vol.19 , Issue.24 , pp. 2925-2940
    • Kennedy, R.D.1    D'Andrea, A.D.2
  • 22
    • 0038075462 scopus 로고    scopus 로고
    • Disruption of the Fanconi anemia-BRCA pathway in cisplatin-sensitive ovarian tumors
    • Taniguchi T., et al. Disruption of the Fanconi anemia-BRCA pathway in cisplatin-sensitive ovarian tumors. Nat. Med. 9 5 (2003) 568-574
    • (2003) Nat. Med. , vol.9 , Issue.5 , pp. 568-574
    • Taniguchi, T.1
  • 23
    • 13244283007 scopus 로고    scopus 로고
    • The anaphase-promoting complex: a key factor in the regulation of cell cycle
    • Castro A., et al. The anaphase-promoting complex: a key factor in the regulation of cell cycle. Oncogene 24 3 (2005) 314-325
    • (2005) Oncogene , vol.24 , Issue.3 , pp. 314-325
    • Castro, A.1
  • 24
    • 0346880059 scopus 로고    scopus 로고
    • Multiple TPR motifs characterize the Fanconi anemia FANCG protein
    • Blom E., et al. Multiple TPR motifs characterize the Fanconi anemia FANCG protein. DNA Repair (Amst) 3 1 (2004) 77-84
    • (2004) DNA Repair (Amst) , vol.3 , Issue.1 , pp. 77-84
    • Blom, E.1
  • 25
    • 4544355937 scopus 로고    scopus 로고
    • The Fanconi anemia gene product FANCF is a flexible adaptor protein
    • Leveille F., et al. The Fanconi anemia gene product FANCF is a flexible adaptor protein. J. Biol. Chem. 279 38 (2004) 39421-39430
    • (2004) J. Biol. Chem. , vol.279 , Issue.38 , pp. 39421-39430
    • Leveille, F.1
  • 26
    • 0034329325 scopus 로고    scopus 로고
    • The fanconi anemia proteins FANCA and FANCG stabilize each other and promote the nuclear accumulation of the Fanconi anemia complex
    • Garcia-Higuera I., et al. The fanconi anemia proteins FANCA and FANCG stabilize each other and promote the nuclear accumulation of the Fanconi anemia complex. Blood 96 9 (2000) 3224-3230
    • (2000) Blood , vol.96 , Issue.9 , pp. 3224-3230
    • Garcia-Higuera, I.1
  • 27
    • 0036786873 scopus 로고    scopus 로고
    • The Fanconi anemia protein, FANCE, promotes the nuclear accumulation of FANCC
    • Taniguchi T., and D'Andrea A.D. The Fanconi anemia protein, FANCE, promotes the nuclear accumulation of FANCC. Blood 100 7 (2002) 2457-2462
    • (2002) Blood , vol.100 , Issue.7 , pp. 2457-2462
    • Taniguchi, T.1    D'Andrea, A.D.2
  • 28
    • 18444384217 scopus 로고    scopus 로고
    • FANCE: the link between Fanconi anaemia complex assembly and activity
    • Pace P., et al. FANCE: the link between Fanconi anaemia complex assembly and activity. Embo J. 21 13 (2002) 3414-3423
    • (2002) Embo J. , vol.21 , Issue.13 , pp. 3414-3423
    • Pace, P.1
  • 29
    • 0038644654 scopus 로고    scopus 로고
    • Fanconi anemia protein complex: mapping protein interactions in the yeast 2-and 3-hybrid systems
    • Gordon S.M., and Buchwald M. Fanconi anemia protein complex: mapping protein interactions in the yeast 2-and 3-hybrid systems. Blood 102 1 (2003) 136-141
    • (2003) Blood , vol.102 , Issue.1 , pp. 136-141
    • Gordon, S.M.1    Buchwald, M.2
  • 30
    • 27744591558 scopus 로고    scopus 로고
    • FANCC, FANCE and FANCD2 form a ternary complex essential to the integrity of the Fanconi anemia DNA damage response pathway
    • Gordon S.M., Alon N., and Buchwald M. FANCC, FANCE and FANCD2 form a ternary complex essential to the integrity of the Fanconi anemia DNA damage response pathway. J. Biol. Chem. (2005)
    • (2005) J. Biol. Chem.
    • Gordon, S.M.1    Alon, N.2    Buchwald, M.3
  • 31
    • 0038642027 scopus 로고    scopus 로고
    • A multiprotein nuclear complex connects Fanconi anemia and Bloom syndrome
    • Meetei A.R., et al. A multiprotein nuclear complex connects Fanconi anemia and Bloom syndrome. Mol. Cell. Biol. 23 10 (2003) 3417-3426
    • (2003) Mol. Cell. Biol. , vol.23 , Issue.10 , pp. 3417-3426
    • Meetei, A.R.1
  • 32
    • 0037364415 scopus 로고    scopus 로고
    • RecQ helicases: caretakers of the genome
    • Hickson I.D. RecQ helicases: caretakers of the genome. Nat. Rev. Cancer 3 3 (2003) 169-178
    • (2003) Nat. Rev. Cancer , vol.3 , Issue.3 , pp. 169-178
    • Hickson, I.D.1
  • 33
    • 0034612333 scopus 로고    scopus 로고
    • The Bloom's syndrome gene product promotes branch migration of holliday junctions
    • Karow J.K., et al. The Bloom's syndrome gene product promotes branch migration of holliday junctions. Proc. Natl. Acad. Sci. USA 97 12 (2000) 6504-6508
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , Issue.12 , pp. 6504-6508
    • Karow, J.K.1
  • 34
    • 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 6968 (2003) 870-874
    • (2003) Nature , vol.426 , Issue.6968 , pp. 870-874
    • Wu, L.1    Hickson, I.D.2
  • 35
    • 0034604545 scopus 로고    scopus 로고
    • Replication protein A physically interacts with the Bloom's syndrome protein and stimulates its helicase activity
    • Brosh Jr. R.M., et al. Replication protein A physically interacts with the Bloom's syndrome protein and stimulates its helicase activity. J. Biol. Chem. 275 31 (2000) 23500-23508
    • (2000) J. Biol. Chem. , vol.275 , Issue.31 , pp. 23500-23508
    • Brosh Jr., R.M.1
  • 36
    • 0037112611 scopus 로고    scopus 로고
    • The Bloom's syndrome helicase stimulates the activity of human topoisomerase IIIalpha
    • Wu L., and Hickson I.D. The Bloom's syndrome helicase stimulates the activity of human topoisomerase IIIalpha. Nucleic Acids Res. 30 22 (2002) 4823-4829
    • (2002) Nucleic Acids Res. , vol.30 , Issue.22 , pp. 4823-4829
    • Wu, L.1    Hickson, I.D.2
  • 37
    • 10944257674 scopus 로고    scopus 로고
    • Crosslinks and crosstalk: human cancer syndromes and DNA repair defects
    • Risinger M.A., and Groden J. Crosslinks and crosstalk: human cancer syndromes and DNA repair defects. Cancer Cell 6 6 (2004) 539-545
    • (2004) Cancer Cell , vol.6 , Issue.6 , pp. 539-545
    • Risinger, M.A.1    Groden, J.2
  • 38
    • 2942735213 scopus 로고    scopus 로고
    • The Fanconi anemia core complex forms four complexes of different sizes in different subcellular compartments
    • Thomashevski A., et al. The Fanconi anemia core complex forms four complexes of different sizes in different subcellular compartments. J. Biol. Chem. 279 25 (2004) 26201-26209
    • (2004) J. Biol. Chem. , vol.279 , Issue.25 , pp. 26201-26209
    • Thomashevski, A.1
  • 39
    • 29144527503 scopus 로고    scopus 로고
    • Localization of the coactivator Cdh1 and the cullin subunit Apc2 in a cryo-electron microscopy model of vertebrate APC/C
    • Dube P., et al. Localization of the coactivator Cdh1 and the cullin subunit Apc2 in a cryo-electron microscopy model of vertebrate APC/C. Mol. Cell. 20 6 (2005) 867-879
    • (2005) Mol. Cell. , vol.20 , Issue.6 , pp. 867-879
    • Dube, P.1
  • 40
    • 29144484041 scopus 로고    scopus 로고
    • Structural analysis of the anaphase-promoting complex reveals multiple active sites and insights into polyubiquitylation
    • Passmore L.A., et al. Structural analysis of the anaphase-promoting complex reveals multiple active sites and insights into polyubiquitylation. Mol. Cell. 20 6 (2005) 855-866
    • (2005) Mol. Cell. , vol.20 , Issue.6 , pp. 855-866
    • Passmore, L.A.1
  • 41
    • 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 6 (2003) 589-595
    • (2003) Bioessays , vol.25 , Issue.6 , pp. 589-595
    • Pagano, G.1    Youssoufian, H.2
  • 42
    • 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 16 (2004) 1958-1963
    • (2004) Genes Dev. , vol.18 , Issue.16 , pp. 1958-1963
    • Andreassen, P.R.1    D'Andrea, A.D.2    Taniguchi, T.3
  • 43
    • 30644459206 scopus 로고    scopus 로고
    • Fanconi anemia proteins are required to prevent accumulation of replication-associated DNA double-strand breaks
    • Sobeck A., et al. Fanconi anemia proteins are required to prevent accumulation of replication-associated DNA double-strand breaks. Mol. Cell. Biol. 26 2 (2006) 425-437
    • (2006) Mol. Cell. Biol. , vol.26 , Issue.2 , pp. 425-437
    • Sobeck, A.1
  • 44
    • 0032573229 scopus 로고    scopus 로고
    • The fanconi anemia pathway requires FAA phosphorylation and FAA/FAC nuclear accumulation
    • Yamashita T., et al. The fanconi anemia pathway requires FAA phosphorylation and FAA/FAC nuclear accumulation. Proc. Natl. Acad. Sci. USA 95 22 (1998) 13085-13090
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , Issue.22 , pp. 13085-13090
    • Yamashita, T.1
  • 45
    • 8544268704 scopus 로고    scopus 로고
    • Phosphorylation of fanconi anemia (FA) complementation group G protein, FANCG, at serine 7 is important for function of the FA pathway
    • Qiao F., et al. Phosphorylation of fanconi anemia (FA) complementation group G protein, FANCG, at serine 7 is important for function of the FA pathway. J. Biol. Chem. 279 44 (2004) 46035-46045
    • (2004) J. Biol. Chem. , vol.279 , Issue.44 , pp. 46035-46045
    • Qiao, F.1
  • 46
    • 0030974684 scopus 로고    scopus 로고
    • Involvement of the Fanconi's anemia protein FAC in a pathway that signals to the cyclin B/cdc2 kinase
    • Kruyt F.A., et al. Involvement of the Fanconi's anemia protein FAC in a pathway that signals to the cyclin B/cdc2 kinase. Cancer Res. 57 11 (1997) 2244-2251
    • (1997) Cancer Res. , vol.57 , Issue.11 , pp. 2244-2251
    • Kruyt, F.A.1
  • 47
    • 4544253225 scopus 로고    scopus 로고
    • FANCG is phosphorylated at serines 383 and 387 during mitosis
    • Mi J., et al. FANCG is phosphorylated at serines 383 and 387 during mitosis. Mol. Cell. Biol. 24 19 (2004) 8576-8585
    • (2004) Mol. Cell. Biol. , vol.24 , Issue.19 , pp. 8576-8585
    • Mi, J.1
  • 48
    • 0030831350 scopus 로고    scopus 로고
    • The Fanconi anemia polypeptide, FAC, binds to the cyclin-dependent kinase, cdc2
    • Kupfer G.M., et al. The Fanconi anemia polypeptide, FAC, binds to the cyclin-dependent kinase, cdc2. Blood 90 3 (1997) 1047-1054
    • (1997) Blood , vol.90 , Issue.3 , pp. 1047-1054
    • Kupfer, G.M.1
  • 49
    • 0035293622 scopus 로고    scopus 로고
    • Protein regulation by monoubiquitin
    • Hicke L. Protein regulation by monoubiquitin. Nat. Rev. Mol. Cell. Biol. 2 3 (2001) 195-201
    • (2001) Nat. Rev. Mol. Cell. Biol. , vol.2 , Issue.3 , pp. 195-201
    • Hicke, L.1
  • 50
    • 0034682718 scopus 로고    scopus 로고
    • Structure of a c-Cbl-UbcH7 complex: RING domain function in ubiquitin-protein ligases
    • Zheng N., et al. Structure of a c-Cbl-UbcH7 complex: RING domain function in ubiquitin-protein ligases. Cell 102 4 (2000) 533-539
    • (2000) Cell , vol.102 , Issue.4 , pp. 533-539
    • Zheng, N.1
  • 51
    • 0033930277 scopus 로고    scopus 로고
    • The APC11 RING-H2 finger mediates E2-dependent ubiquitination
    • Leverson J.D., et al. The APC11 RING-H2 finger mediates E2-dependent ubiquitination. Mol. Biol. Cell. 11 7 (2000) 2315-2325
    • (2000) Mol. Biol. Cell. , vol.11 , Issue.7 , pp. 2315-2325
    • Leverson, J.D.1
  • 52
    • 33744958660 scopus 로고    scopus 로고
    • The WD40 repeats of FANCL are required for Fanconi anemia core complex assembly
    • Gurtan A.M., Stuckert P., and D'Andrea A.D. The WD40 repeats of FANCL are required for Fanconi anemia core complex assembly. J. Biol. Chem. 281 16 (2006) 10896-10905
    • (2006) J. Biol. Chem. , vol.281 , Issue.16 , pp. 10896-10905
    • Gurtan, A.M.1    Stuckert, P.2    D'Andrea, A.D.3
  • 53
    • 9644273891 scopus 로고    scopus 로고
    • A hitchhiker's guide to the cullin ubiquitin ligases: SCF and its kin
    • Willems A.R., Schwab M., and Tyers M. A hitchhiker's guide to the cullin ubiquitin ligases: SCF and its kin. Biochim. Biophys. Acta 1695 1-3 (2004) 133-170
    • (2004) Biochim. Biophys. Acta , vol.1695 , Issue.1-3 , pp. 133-170
    • Willems, A.R.1    Schwab, M.2    Tyers, M.3
  • 54
    • 11144225798 scopus 로고    scopus 로고
    • Cooperation of the N-terminal Helicase and C-terminal endonuclease activities of Archaeal Hef protein in processing stalled replication forks
    • Komori K., et al. Cooperation of the N-terminal Helicase and C-terminal endonuclease activities of Archaeal Hef protein in processing stalled replication forks. J. Biol. Chem. 279 51 (2004) 53175-53185
    • (2004) J. Biol. Chem. , vol.279 , Issue.51 , pp. 53175-53185
    • Komori, K.1
  • 55
    • 0035968325 scopus 로고    scopus 로고
    • Fanconi anemia proteins localize to chromatin and the nuclear matrix in a DNA damage-and cell cycle-regulated manner
    • Qiao F., Moss A., and Kupfer G.M. Fanconi anemia proteins localize to chromatin and the nuclear matrix in a DNA damage-and cell cycle-regulated manner. J. Biol. Chem. 276 26 (2001) 23391-23396
    • (2001) J. Biol. Chem. , vol.276 , Issue.26 , pp. 23391-23396
    • Qiao, F.1    Moss, A.2    Kupfer, G.M.3
  • 56
    • 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 2 (2005) 759-766
    • (2005) Blood , vol.105 , Issue.2 , pp. 759-766
    • Mi, J.1    Kupfer, G.M.2
  • 57
    • 21244451611 scopus 로고    scopus 로고
    • Direct DNA binding activity of the Fanconi anemia D2 protein
    • Park W.H., et al. Direct DNA binding activity of the Fanconi anemia D2 protein. J. Biol. Chem. 280 25 (2005) 23593-23598
    • (2005) J. Biol. Chem. , vol.280 , Issue.25 , pp. 23593-23598
    • Park, W.H.1
  • 58
    • 24944461145 scopus 로고    scopus 로고
    • A FancD2-monoubiquitin fusion reveals hidden functions of Fanconi anemia core complex in DNA repair
    • Matsushita N., et al. A FancD2-monoubiquitin fusion reveals hidden functions of Fanconi anemia core complex in DNA repair. Mol. Cell. 19 6 (2005) 841-847
    • (2005) Mol. Cell. , vol.19 , Issue.6 , pp. 841-847
    • Matsushita, N.1
  • 59
    • 0038339144 scopus 로고    scopus 로고
    • A novel regulation mechanism of DNA repair by damage-induced and RAD23-dependent stabilization of xeroderma pigmentosum group C protein
    • Ng J.M., et al. A novel regulation mechanism of DNA repair by damage-induced and RAD23-dependent stabilization of xeroderma pigmentosum group C protein. Genes Dev. 17 13 (2003) 1630-1645
    • (2003) Genes Dev. , vol.17 , Issue.13 , pp. 1630-1645
    • Ng, J.M.1
  • 60
    • 29144499065 scopus 로고    scopus 로고
    • Ubiquitin-binding domains in Y-family polymerases regulate translesion synthesis
    • Bienko M., et al. Ubiquitin-binding domains in Y-family polymerases regulate translesion synthesis. Science 310 5755 (2005) 1821-1824
    • (2005) Science , vol.310 , Issue.5755 , pp. 1821-1824
    • Bienko, M.1
  • 61
    • 4344597147 scopus 로고    scopus 로고
    • The Fanconi anaemia gene FANCC promotes homologous recombination and error-prone DNA repair
    • Niedzwiedz W., et al. The Fanconi anaemia gene FANCC promotes homologous recombination and error-prone DNA repair. Mol. Cell. 15 4 (2004) 607-620
    • (2004) Mol. Cell. , vol.15 , Issue.4 , pp. 607-620
    • Niedzwiedz, W.1
  • 62
    • 0036785375 scopus 로고    scopus 로고
    • S-phase-specific interaction of the Fanconi anemia protein, FANCD2, with BRCA1 and RAD51
    • Taniguchi T., et al. S-phase-specific interaction of the Fanconi anemia protein, FANCD2, with BRCA1 and RAD51. Blood 100 7 (2002) 2414-2420
    • (2002) Blood , vol.100 , Issue.7 , pp. 2414-2420
    • Taniguchi, T.1
  • 63
    • 0033780760 scopus 로고    scopus 로고
    • DNA replication is required to elicit cellular responses to psoralen-induced DNA interstrand cross-links
    • Akkari Y.M., et al. DNA replication is required to elicit cellular responses to psoralen-induced DNA interstrand cross-links. Mol. Cell. Biol. 20 21 (2000) 8283-8289
    • (2000) Mol. Cell. Biol. , vol.20 , Issue.21 , pp. 8283-8289
    • Akkari, Y.M.1
  • 64
    • 12144288675 scopus 로고    scopus 로고
    • Heterogeneity in Fanconi anemia: evidence for 2 new genetic subtypes
    • Levitus M., et al. Heterogeneity in Fanconi anemia: evidence for 2 new genetic subtypes. Blood 103 7 (2004) 2498-2503
    • (2004) Blood , vol.103 , Issue.7 , pp. 2498-2503
    • Levitus, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.