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Volumn 9, Issue 3, 2010, Pages 250-256

FANCJ: Solving problems in DNA replication

Author keywords

DNA repair; DNA replication; FANCJ; Fanconi anemia; Helicase

Indexed keywords

DNA; FANCJ HELICASE; HELICASE; UNCLASSIFIED DRUG;

EID: 76749116088     PISSN: 15687864     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.dnarep.2010.01.005     Document Type: Review
Times cited : (35)

References (67)
  • 3
    • 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
  • 7
    • 0142240342 scopus 로고    scopus 로고
    • BRCT repeats as phosphopeptide-binding modules involved in protein targeting
    • Manke I.A., Lowery D.M., Nguyen A., and Yaffe M.B. BRCT repeats as phosphopeptide-binding modules involved in protein targeting. Science 302 (2003) 636-639
    • (2003) Science , vol.302 , pp. 636-639
    • Manke, I.A.1    Lowery, D.M.2    Nguyen, A.3    Yaffe, M.B.4
  • 8
    • 34948855936 scopus 로고    scopus 로고
    • FANCJ (BACH1) helicase forms DNA damage inducible foci with replication protein A and interacts physically and functionally with the single-stranded DNA-binding protein
    • Gupta R., Sharma S., Sommers J.A., Kenny M.K., Cantor S.B., and Brosh Jr. R.M. FANCJ (BACH1) helicase forms DNA damage inducible foci with replication protein A and interacts physically and functionally with the single-stranded DNA-binding protein. Blood 110 (2007) 2390-2398
    • (2007) Blood , vol.110 , pp. 2390-2398
    • Gupta, R.1    Sharma, S.2    Sommers, J.A.3    Kenny, M.K.4    Cantor, S.B.5    Brosh Jr., R.M.6
  • 9
    • 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
  • 10
    • 34047260728 scopus 로고    scopus 로고
    • Characterization of the interactome of the human MutL homologues MLH1, PMS1, and PMS2
    • Cannavo E., Gerrits B., Marra G., Schlapbach R., and Jiricny J. Characterization of the interactome of the human MutL homologues MLH1, PMS1, and PMS2. J. Biol. Chem. 282 (2007) 2976-2986
    • (2007) J. Biol. Chem. , vol.282 , pp. 2976-2986
    • Cannavo, E.1    Gerrits, B.2    Marra, G.3    Schlapbach, R.4    Jiricny, J.5
  • 11
    • 25144503943 scopus 로고    scopus 로고
    • The 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 BRIP1 helicase functions independently of BRCA1 in the Fanconi anemia pathway for DNA crosslink repair. Nat. Genet. 37 (2005) 953-957
    • (2005) Nat. Genet. , vol.37 , pp. 953-957
    • Bridge, W.L.1    Vandenberg, C.J.2    Franklin, R.J.3    Hiom, K.4
  • 12
    • 40749095337 scopus 로고    scopus 로고
    • DOG-1 is the Caenorhabditis elegans BRIP1/FANCJ homologue and functions in interstrand cross-link repair
    • Youds J.L., Barber L.J., Ward J.D., Collis S.J., O'Neil N.J., Boulton S.J., and Rose A.M. DOG-1 is the Caenorhabditis elegans BRIP1/FANCJ homologue and functions in interstrand cross-link repair. Mol. Cell. Biol. 28 (2008) 1470-1479
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 1470-1479
    • Youds, J.L.1    Barber, L.J.2    Ward, J.D.3    Collis, S.J.4    O'Neil, N.J.5    Boulton, S.J.6    Rose, A.M.7
  • 13
    • 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
  • 14
    • 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
  • 15
    • 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
  • 16
    • 0028068579 scopus 로고
    • Hematologic abnormalities in Fanconi anemia: an International Fanconi Anemia Registry study
    • Butturini A., Gale R.P., Verlander P.C., Adler-Brecher B., Gillio A.P., and Auerbach A.D. Hematologic abnormalities in Fanconi anemia: an International Fanconi Anemia Registry study. Blood 84 (1994) 1650-1655
    • (1994) Blood , vol.84 , pp. 1650-1655
    • Butturini, A.1    Gale, R.P.2    Verlander, P.C.3    Adler-Brecher, B.4    Gillio, A.P.5    Auerbach, A.D.6
  • 17
    • 0025959243 scopus 로고
    • Leukemia and preleukemia in Fanconi anemia patients. A review of the literature and report of the International Fanconi Anemia Registry
    • Auerbach A.D., and Allen R.G. Leukemia and preleukemia in Fanconi anemia patients. A review of the literature and report of the International Fanconi Anemia Registry. Cancer Genet. Cytogenet. 51 (1991) 1-12
    • (1991) Cancer Genet. Cytogenet. , vol.51 , pp. 1-12
    • Auerbach, A.D.1    Allen, R.G.2
  • 18
    • 0019918242 scopus 로고
    • Cytogenetic toxicity of antitumor platinum compounds in Fanconi's anemia
    • Poll E.H., Arwert F., Joenje H., and Eriksson A.W. Cytogenetic toxicity of antitumor platinum compounds in Fanconi's anemia. Hum. Genet. 61 (1982) 228-230
    • (1982) Hum. Genet. , vol.61 , pp. 228-230
    • Poll, E.H.1    Arwert, F.2    Joenje, H.3    Eriksson, A.W.4
  • 19
    • 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
  • 20
    • 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
  • 29
    • 62549115236 scopus 로고    scopus 로고
    • PALB2 links BRCA1 and BRCA2 in the DNA-damage response
    • Zhang F., Ma J., Wu J., Ye L., Cai H., Xia B., and Yu X. PALB2 links BRCA1 and BRCA2 in the DNA-damage response. Curr. Biol. 19 (2009) 524-529
    • (2009) Curr. Biol. , vol.19 , pp. 524-529
    • Zhang, F.1    Ma, J.2    Wu, J.3    Ye, L.4    Cai, H.5    Xia, B.6    Yu, X.7
  • 30
    • 66349096607 scopus 로고    scopus 로고
    • PALB2 is an integral component of the BRCA complex required for homologous recombination repair
    • Sy S.M., Huen M.S., and Chen J. PALB2 is an integral component of the BRCA complex required for homologous recombination repair. Proc. Natl. Acad. Sci. U.S.A. 106 (2009) 7155-7160
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 7155-7160
    • Sy, S.M.1    Huen, M.S.2    Chen, J.3
  • 31
    • 70349667196 scopus 로고    scopus 로고
    • Xpf and not the Fanconi anaemia proteins or Rev3 accounts for the extreme resistance to cisplatin in Dictyostelium discoideum
    • Zhang X.Y., Langenick J., Traynor D., Babu M.M., Kay R.R., and Patel K.J. Xpf and not the Fanconi anaemia proteins or Rev3 accounts for the extreme resistance to cisplatin in Dictyostelium discoideum. PLoS Genet. 5 (2009) e1000645
    • (2009) PLoS Genet. , vol.5
    • Zhang, X.Y.1    Langenick, J.2    Traynor, D.3    Babu, M.M.4    Kay, R.R.5    Patel, K.J.6
  • 32
    • 1442281478 scopus 로고    scopus 로고
    • The BRCA1-associated protein BACH1 is a DNA helicase targeted by clinically relevant inactivating mutations
    • Cantor S., Drapkin R., Zhang F., Lin Y., Han J., Pamidi S., and Livingston D.M. The BRCA1-associated protein BACH1 is a DNA helicase targeted by clinically relevant inactivating mutations. Proc. Natl. Acad. Sci. U.S.A. 101 (2004) 2357-2362
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 2357-2362
    • Cantor, S.1    Drapkin, R.2    Zhang, F.3    Lin, Y.4    Han, J.5    Pamidi, S.6    Livingston, D.M.7
  • 34
    • 84870323168 scopus 로고    scopus 로고
    • Structure, function and evolution of the XPD family of iron-sulfur-containing 5′→3′ DNA helicases
    • White M.F. Structure, function and evolution of the XPD family of iron-sulfur-containing 5′→3′ DNA helicases. Biochem. Soc. Trans. 37 (2009) 547-551
    • (2009) Biochem. Soc. Trans. , vol.37 , pp. 547-551
    • White, M.F.1
  • 35
    • 0027243363 scopus 로고
    • Escherichia coli dinG gene encodes a putative DNA helicase related to a group of eukaryotic helicases including Rad3 protein
    • Koonin E.V. Escherichia coli dinG gene encodes a putative DNA helicase related to a group of eukaryotic helicases including Rad3 protein. Nucleic Acids Res. 21 (1993) 1497
    • (1993) Nucleic Acids Res. , vol.21 , pp. 1497
    • Koonin, E.V.1
  • 36
  • 39
    • 0034663639 scopus 로고    scopus 로고
    • CHL1 is a nuclear protein with an essential ATP binding site that exhibits a size-dependent effect on chromosome segregation
    • Holloway L. CHL1 is a nuclear protein with an essential ATP binding site that exhibits a size-dependent effect on chromosome segregation. Nucleic Acids Res. 28 (2000) 3056-3064
    • (2000) Nucleic Acids Res. , vol.28 , pp. 3056-3064
    • Holloway, L.1
  • 40
    • 1642360837 scopus 로고    scopus 로고
    • Chl1p, a DNA helicase-like protein in budding yeast, functions in sister-chromatid cohesion
    • Skibbens R.V. Chl1p, a DNA helicase-like protein in budding yeast, functions in sister-chromatid cohesion. Genetics 166 (2004) 33-42
    • (2004) Genetics , vol.166 , pp. 33-42
    • Skibbens, R.V.1
  • 41
    • 33748428875 scopus 로고    scopus 로고
    • The DNA repair helicases XPD and FancJ have essential iron-sulfur domains
    • Rudolf J., Makrantoni V., Ingledew W.J., Stark M.J., and White M.F. The DNA repair helicases XPD and FancJ have essential iron-sulfur domains. Mol. Cell 23 (2006) 801-808
    • (2006) Mol. Cell , vol.23 , pp. 801-808
    • Rudolf, J.1    Makrantoni, V.2    Ingledew, W.J.3    Stark, M.J.4    White, M.F.5
  • 44
    • 39149142997 scopus 로고    scopus 로고
    • The X-ray crystal structure of RNA polymerase from Archaea
    • Hirata A., Klein B.J., and Murakami K.S. The X-ray crystal structure of RNA polymerase from Archaea. Nature 451 (2008) 851-854
    • (2008) Nature , vol.451 , pp. 851-854
    • Hirata, A.1    Klein, B.J.2    Murakami, K.S.3
  • 45
    • 65549136266 scopus 로고    scopus 로고
    • An iron-sulfur cluster is essential for the binding of broken DNA by AddAB-type helicase-nucleases
    • Yeeles J.T., Cammack R., and Dillingham M.S. An iron-sulfur cluster is essential for the binding of broken DNA by AddAB-type helicase-nucleases. J. Biol. Chem. 284 (2009) 7746-7755
    • (2009) J. Biol. Chem. , vol.284 , pp. 7746-7755
    • Yeeles, J.T.1    Cammack, R.2    Dillingham, M.S.3
  • 46
  • 47
    • 38349091095 scopus 로고    scopus 로고
    • The iron-containing domain is essential in Rad3 helicases for coupling of ATP hydrolysis to DNA translocation and for targeting the helicase to the single-stranded DNA-double-stranded DNA junction
    • Pugh R.A., Honda M., Leesley H., Thomas A., Lin Y., Nilges M.J., Cann I.K., and Spies M. The iron-containing domain is essential in Rad3 helicases for coupling of ATP hydrolysis to DNA translocation and for targeting the helicase to the single-stranded DNA-double-stranded DNA junction. J. Biol. Chem. 283 (2008) 1732-1743
    • (2008) J. Biol. Chem. , vol.283 , pp. 1732-1743
    • Pugh, R.A.1    Honda, M.2    Leesley, H.3    Thomas, A.4    Lin, Y.5    Nilges, M.J.6    Cann, I.K.7    Spies, M.8
  • 50
    • 44149094083 scopus 로고    scopus 로고
    • XPD helicase structures and activities: insights into the cancer and aging phenotypes from XPD mutations
    • Fan L., Fuss J.O., Cheng Q.J., Arvai A.S., Hammel M., Roberts V.A., Cooper P.K., and Tainer J.A. XPD helicase structures and activities: insights into the cancer and aging phenotypes from XPD mutations. Cell 133 (2008) 789-800
    • (2008) Cell , vol.133 , pp. 789-800
    • Fan, L.1    Fuss, J.O.2    Cheng, Q.J.3    Arvai, A.S.4    Hammel, M.5    Roberts, V.A.6    Cooper, P.K.7    Tainer, J.A.8
  • 51
    • 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
  • 53
    • 65549113446 scopus 로고    scopus 로고
    • FANCJ uses its motor ATPase to destabilize protein-DNA complexes, unwind triplexes, and inhibit RAD51 strand exchange
    • Sommers J.A., Rawtani N., Gupta R., Bugreev D.V., Mazin A.V., Cantor S.B., and Brosh Jr. R.M. FANCJ uses its motor ATPase to destabilize protein-DNA complexes, unwind triplexes, and inhibit RAD51 strand exchange. J. Biol. Chem. 284 (2009) 7505-7517
    • (2009) J. Biol. Chem. , vol.284 , pp. 7505-7517
    • Sommers, J.A.1    Rawtani, N.2    Gupta, R.3    Bugreev, D.V.4    Mazin, A.V.5    Cantor, S.B.6    Brosh Jr., R.M.7
  • 54
    • 67650563908 scopus 로고    scopus 로고
    • FANCJ helicase uniquely senses oxidative base damage in either strand of duplex DNA and is stimulated by replication protein A to unwind the damaged DNA substrate in a strand-specific manner
    • Suhasini A.N., Sommers J.A., Mason A.C., Voloshin O.N., Camerini-Otero R.D., Wold M.S., and Brosh Jr. R.M. FANCJ helicase uniquely senses oxidative base damage in either strand of duplex DNA and is stimulated by replication protein A to unwind the damaged DNA substrate in a strand-specific manner. J. Biol. Chem. 284 (2009) 18458-18470
    • (2009) J. Biol. Chem. , vol.284 , pp. 18458-18470
    • Suhasini, A.N.1    Sommers, J.A.2    Mason, A.C.3    Voloshin, O.N.4    Camerini-Otero, R.D.5    Wold, M.S.6    Brosh Jr., R.M.7
  • 55
    • 69749106825 scopus 로고    scopus 로고
    • Recruitment of fanconi anemia and breast cancer proteins to DNA damage sites is differentially governed by replication
    • Shen X., Do H., Li Y., Chung W.H., Tomasz M., de Winter J.P., Xia B., Elledge S.J., Wang W., and Li L. Recruitment of fanconi anemia and breast cancer proteins to DNA damage sites is differentially governed by replication. Mol. Cell 35 (2009) 716-723
    • (2009) Mol. Cell , vol.35 , pp. 716-723
    • Shen, X.1    Do, H.2    Li, Y.3    Chung, W.H.4    Tomasz, M.5    de Winter, J.P.6    Xia, B.7    Elledge, S.J.8    Wang, W.9    Li, L.10
  • 56
    • 0036699095 scopus 로고    scopus 로고
    • Disruption of dog-1 in Caenorhabditis elegans triggers deletions upstream of guanine-rich DNA
    • Cheung I., Schertzer M., Rose A., and Lansdorp P.M. Disruption of dog-1 in Caenorhabditis elegans triggers deletions upstream of guanine-rich DNA. Nat. Genet. 31 (2002) 405-409
    • (2002) Nat. Genet. , vol.31 , pp. 405-409
    • Cheung, I.1    Schertzer, M.2    Rose, A.3    Lansdorp, P.M.4
  • 57
    • 33845352895 scopus 로고    scopus 로고
    • Dynamic roles for G4 DNA in the biology of eukaryotic cells
    • Maizels N. Dynamic roles for G4 DNA in the biology of eukaryotic cells. Nat. Struct. Mol. Biol. 13 (2006) 1055-1059
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 1055-1059
    • Maizels, N.1
  • 58
    • 34250878426 scopus 로고    scopus 로고
    • Expandable DNA repeats and human disease
    • Mirkin S.M. Expandable DNA repeats and human disease. Nature 447 (2007) 932-940
    • (2007) Nature , vol.447 , pp. 932-940
    • Mirkin, S.M.1
  • 59
    • 27144451010 scopus 로고    scopus 로고
    • Telomere end-binding proteins control the formation of G-quadruplex DNA structures in vivo
    • Paeschke K., Simonsson T., Postberg J., Rhodes D., and Lipps H.J. Telomere end-binding proteins control the formation of G-quadruplex DNA structures in vivo. Nat. Struct. Mol. Biol. 12 (2005) 847-854
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 847-854
    • Paeschke, K.1    Simonsson, T.2    Postberg, J.3    Rhodes, D.4    Lipps, H.J.5
  • 60
    • 20144364292 scopus 로고    scopus 로고
    • Prevalence of quadruplexes in the human genome
    • Huppert J.L., and Balasubramanian S. Prevalence of quadruplexes in the human genome. Nucleic Acids Res. 33 (2005) 2908-2916
    • (2005) Nucleic Acids Res. , vol.33 , pp. 2908-2916
    • Huppert, J.L.1    Balasubramanian, S.2
  • 61
    • 53149127633 scopus 로고    scopus 로고
    • Spectrum of mutational events in the absence of DOG-1/FANCJ in Caenorhabditis elegans
    • Zhao Y., Tarailo-Graovac M., O'Neil N.J., and Rose A.M. Spectrum of mutational events in the absence of DOG-1/FANCJ in Caenorhabditis elegans. DNA Rep. (Amst.) 7 (2008) 1846-1854
    • (2008) DNA Rep. (Amst.) , vol.7 , pp. 1846-1854
    • Zhao, Y.1    Tarailo-Graovac, M.2    O'Neil, N.J.3    Rose, A.M.4
  • 62
    • 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
  • 64
    • 0032538453 scopus 로고    scopus 로고
    • The Bloom's syndrome helicase unwinds G4 DNA
    • Sun H., Karow J.K., Hickson I.D., and Maizels N. The Bloom's syndrome helicase unwinds G4 DNA. J. Biol. Chem. 273 (1998) 27587-27592
    • (1998) J. Biol. Chem. , vol.273 , pp. 27587-27592
    • Sun, H.1    Karow, J.K.2    Hickson, I.D.3    Maizels, N.4
  • 65
    • 0037106470 scopus 로고    scopus 로고
    • G4 DNA unwinding by BLM and Sgs1p: substrate specificity and substrate-specific inhibition
    • Huber M.D., Lee D.C., and Maizels N. G4 DNA unwinding by BLM and Sgs1p: substrate specificity and substrate-specific inhibition. Nucleic Acids Res. 30 (2002) 3954-3961
    • (2002) Nucleic Acids Res. , vol.30 , pp. 3954-3961
    • Huber, M.D.1    Lee, D.C.2    Maizels, N.3
  • 66
    • 33745407668 scopus 로고    scopus 로고
    • Homologous recombination is required for genome stability in the absence of DOG-1 in Caenorhabditis elegans
    • Youds J.L., O'Neil N.J., and Rose A.M. Homologous recombination is required for genome stability in the absence of DOG-1 in Caenorhabditis elegans. Genetics 173 (2006) 697-708
    • (2006) Genetics , vol.173 , pp. 697-708
    • Youds, J.L.1    O'Neil, N.J.2    Rose, A.M.3
  • 67
    • 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


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