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Volumn 9, Issue 3, 2010, Pages 224-236

The FANCM family of DNA helicases/translocases

Author keywords

FANCM; Fanconi Anemia; Fml1; Hef; Homologous recombination; Mph1

Indexed keywords

ADENOSINE TRIPHOSPHATASE; CARRIER PROTEIN; DOUBLE STRANDED DNA; HELICASE; NUCLEASE;

EID: 76749123854     PISSN: 15687864     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.dnarep.2009.12.012     Document Type: Review
Times cited : (90)

References (92)
  • 1
    • 17344391705 scopus 로고    scopus 로고
    • MPH1, a yeast gene encoding a DEAH protein, plays a role in protection of the genome from spontaneous and chemically induced damage
    • Scheller J., Schurer A., Rudolph C., Hettwer S., and Kramer W. MPH1, a yeast gene encoding a DEAH protein, plays a role in protection of the genome from spontaneous and chemically induced damage. Genetics 155 (2000) 1069-1081
    • (2000) Genetics , vol.155 , pp. 1069-1081
    • Scheller, J.1    Schurer, A.2    Rudolph, C.3    Hettwer, S.4    Kramer, W.5
  • 2
    • 0036698611 scopus 로고    scopus 로고
    • Novel endonuclease in Archaea cleaving DNA with various branched structure
    • Komori K., Fujikane R., Shinagawa H., and Ishino Y. Novel endonuclease in Archaea cleaving DNA with various branched structure. Genes Genet. Syst. 77 (2002) 227-241
    • (2002) Genes Genet. Syst. , vol.77 , pp. 227-241
    • Komori, K.1    Fujikane, R.2    Shinagawa, H.3    Ishino, Y.4
  • 5
    • 53149087431 scopus 로고    scopus 로고
    • The fission yeast FANCM ortholog Fml1 promotes recombination at stalled replication forks and limits crossing over during double-strand break repair
    • Sun W., Nandi S., Osman F., Ahn J.S., Jakovleska J., Lorenz A., and Whitby M.C. The fission yeast FANCM ortholog Fml1 promotes recombination at stalled replication forks and limits crossing over during double-strand break repair. Mol. Cell 32 (2008) 118-128
    • (2008) Mol. Cell , vol.32 , pp. 118-128
    • Sun, W.1    Nandi, S.2    Osman, F.3    Ahn, J.S.4    Jakovleska, J.5    Lorenz, A.6    Whitby, M.C.7
  • 6
    • 34548638261 scopus 로고    scopus 로고
    • Structure and mechanism of helicases and nucleic acid translocases
    • Singleton M.R., Dillingham M.S., and Wigley D.B. Structure and mechanism of helicases and nucleic acid translocases. Annu. Rev. Biochem. 76 (2007) 23-50
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 23-50
    • Singleton, M.R.1    Dillingham, M.S.2    Wigley, D.B.3
  • 7
    • 11844252069 scopus 로고    scopus 로고
    • Crystal structure and functional implications of Pyrococcus furiosus Hef helicase domain involved in branched DNA processing
    • Nishino T., Komori K., Tsuchiya D., Ishino Y., and Morikawa K. Crystal structure and functional implications of Pyrococcus furiosus Hef helicase domain involved in branched DNA processing. Structure 13 (2005) 143-153
    • (2005) Structure , vol.13 , pp. 143-153
    • Nishino, T.1    Komori, K.2    Tsuchiya, D.3    Ishino, Y.4    Morikawa, K.5
  • 8
    • 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
  • 9
    • 23444443484 scopus 로고    scopus 로고
    • Structural and functional analyses of an archaeal XPF/Rad1/Mus81 nuclease: asymmetric DNA binding and cleavage mechanisms
    • Nishino T., Komori K., Ishino Y., and Morikawa K. Structural and functional analyses of an archaeal XPF/Rad1/Mus81 nuclease: asymmetric DNA binding and cleavage mechanisms. Structure (Camb.) 13 (2005) 1183-1192
    • (2005) Structure (Camb.) , vol.13 , pp. 1183-1192
    • Nishino, T.1    Komori, K.2    Ishino, Y.3    Morikawa, K.4
  • 11
    • 14844296413 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae MPH1 gene, required for homologous recombination-mediated mutation avoidance, encodes a 3′ to 5′ DNA helicase
    • Prakash R., Krejci L., Van Komen S., Anke Schurer K., Kramer W., and Sung P. Saccharomyces cerevisiae MPH1 gene, required for homologous recombination-mediated mutation avoidance, encodes a 3′ to 5′ DNA helicase. J. Biol. Chem. 280 (2005) 7854-7860
    • (2005) J. Biol. Chem. , vol.280 , pp. 7854-7860
    • Prakash, R.1    Krejci, L.2    Van Komen, S.3    Anke Schurer, K.4    Kramer, W.5    Sung, P.6
  • 12
    • 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., Hidaka M., Horiuchi T., Fujikane R., Shinagawa H., and Ishino Y. Cooperation of the N-terminal helicase and C-terminal endonuclease activities of Archaeal Hef protein in processing stalled replication forks. J. Biol. Chem. 279 (2004) 53175-53185
    • (2004) J. Biol. Chem. , vol.279 , pp. 53175-53185
    • Komori, K.1    Hidaka, M.2    Horiuchi, T.3    Fujikane, R.4    Shinagawa, H.5    Ishino, Y.6
  • 13
    • 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
  • 15
    • 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
  • 17
    • 12444336898 scopus 로고    scopus 로고
    • X-ray and biochemical anatomy of an archaeal XPF/Rad1/Mus81 family nuclease: similarity between its endonuclease domain and restriction enzymes
    • Nishino T., Komori K., Ishino Y., and Morikawa K. X-ray and biochemical anatomy of an archaeal XPF/Rad1/Mus81 family nuclease: similarity between its endonuclease domain and restriction enzymes. Structure 11 (2003) 445-457
    • (2003) Structure , vol.11 , pp. 445-457
    • Nishino, T.1    Komori, K.2    Ishino, Y.3    Morikawa, K.4
  • 18
    • 67649862225 scopus 로고    scopus 로고
    • Replication fork reversal and the maintenance of genome stability
    • Atkinson J., and McGlynn P. Replication fork reversal and the maintenance of genome stability. Nucleic Acids Res. 37 (2009) 3475-3492
    • (2009) Nucleic Acids Res. , vol.37 , pp. 3475-3492
    • Atkinson, J.1    McGlynn, P.2
  • 19
    • 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
  • 20
    • 0036844340 scopus 로고    scopus 로고
    • Recombinational repair and restart of damaged replication forks
    • McGlynn P., and Lloyd R.G. Recombinational repair and restart of damaged replication forks. Nat. Rev. Mol. Cell. Biol. 3 (2002) 859-870
    • (2002) Nat. Rev. Mol. Cell. Biol. , vol.3 , pp. 859-870
    • McGlynn, P.1    Lloyd, R.G.2
  • 21
    • 76749114560 scopus 로고    scopus 로고
    • Mechanism of eukaryotic homologous recombination
    • San Filippo J., Sung P., and Klein H. Mechanism of eukaryotic homologous recombination. Annu. Rev. Biochem. 14 (2008) 14
    • (2008) Annu. Rev. Biochem. , vol.14 , pp. 14
    • San Filippo, J.1    Sung, P.2    Klein, H.3
  • 22
    • 0038799991 scopus 로고    scopus 로고
    • Multiple pathways of recombination induced by double-strand breaks in Saccharomyces cerevisiae
    • Paques F., and Haber J.E. Multiple pathways of recombination induced by double-strand breaks in Saccharomyces cerevisiae. Microbiol. Mol. Biol. Rev. 63 (1999) 349-404
    • (1999) Microbiol. Mol. Biol. Rev. , vol.63 , pp. 349-404
    • Paques, F.1    Haber, J.E.2
  • 23
    • 34249942213 scopus 로고    scopus 로고
    • Exploring the roles of Mus81-Eme1/Mms4 at perturbed replication forks
    • Osman F., and Whitby M.C. Exploring the roles of Mus81-Eme1/Mms4 at perturbed replication forks. DNA Repair 6 (2007) 1004-1017
    • (2007) DNA Repair , vol.6 , pp. 1004-1017
    • Osman, F.1    Whitby, M.C.2
  • 24
    • 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
  • 25
    • 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
  • 26
    • 72149119542 scopus 로고    scopus 로고
    • How the Fanconi Anemia pathway guards the genome
    • Moldovan G.L., and D'Andrea A.D. How the Fanconi Anemia pathway guards the genome. Annu. Rev. Genet. 17 (2009) 223-249
    • (2009) Annu. Rev. Genet. , vol.17 , pp. 223-249
    • Moldovan, G.L.1    D'Andrea, A.D.2
  • 32
    • 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
  • 36
    • 76749109191 scopus 로고    scopus 로고
    • The fanconi anemia protein FANCM is controlled by FANCD2 and the ATR/ATM pathways
    • Sobeck A., Stone S., Landais I., de Graaf B., and Hoatlin M.E. The fanconi anemia protein FANCM is controlled by FANCD2 and the ATR/ATM pathways. J. Biol. Chem. 24 (2009) 24
    • (2009) J. Biol. Chem. , vol.24 , pp. 24
    • Sobeck, A.1    Stone, S.2    Landais, I.3    de Graaf, B.4    Hoatlin, M.E.5
  • 38
    • 67949085157 scopus 로고    scopus 로고
    • The Walker B motif in avian FANCM is required to limit sister chromatid exchanges but is dispensable for DNA crosslink repair
    • Rosado I.V., Niedzwiedz W., Alpi A.F., and Patel K.J. The Walker B motif in avian FANCM is required to limit sister chromatid exchanges but is dispensable for DNA crosslink repair. Nucleic Acids Res. 37 (2009) 4360-4370
    • (2009) Nucleic Acids Res. , vol.37 , pp. 4360-4370
    • Rosado, I.V.1    Niedzwiedz, W.2    Alpi, A.F.3    Patel, K.J.4
  • 39
    • 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., Kuang Y., Denham J., and D'Andrea A.D. The Fanconi anemia proteins FANCA and FANCG stabilize each other and promote the nuclear accumulation of the Fanconi anemia complex. Blood 96 (2000) 3224-3230
    • (2000) Blood , vol.96 , pp. 3224-3230
    • Garcia-Higuera, I.1    Kuang, Y.2    Denham, J.3    D'Andrea, A.D.4
  • 40
    • 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
  • 41
    • 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 (2001) 23391-23396
    • (2001) J. Biol. Chem. , vol.276 , pp. 23391-23396
    • Qiao, F.1    Moss, A.2    Kupfer, G.M.3
  • 42
    • 61849128915 scopus 로고    scopus 로고
    • Regulated degradation of FANCM in the Fanconi anemia pathway during mitosis
    • Kee Y., Kim J.M., and D'Andrea A.D. Regulated degradation of FANCM in the Fanconi anemia pathway during mitosis. Genes Dev. 23 (2009) 555-560
    • (2009) Genes Dev. , vol.23 , pp. 555-560
    • Kee, Y.1    Kim, J.M.2    D'Andrea, A.D.3
  • 44
    • 0024095589 scopus 로고
    • Mutation of lysine-48 to arginine in the yeast RAD3 protein abolishes its ATPase and DNA helicase activities but not the ability to bind ATP
    • Sung P., Higgins D., Prakash L., and Prakash S. Mutation of lysine-48 to arginine in the yeast RAD3 protein abolishes its ATPase and DNA helicase activities but not the ability to bind ATP. EMBO J. 7 (1988) 3263-3269
    • (1988) EMBO J. , vol.7 , pp. 3263-3269
    • Sung, P.1    Higgins, D.2    Prakash, L.3    Prakash, S.4
  • 45
    • 34249937178 scopus 로고    scopus 로고
    • The ATR pathway: fine-tuning the fork
    • Paulsen R.D., and Cimprich K.A. The ATR pathway: fine-tuning the fork. DNA Repair (Amst.) 6 (2007) 953-966
    • (2007) DNA Repair (Amst.) , vol.6 , pp. 953-966
    • Paulsen, R.D.1    Cimprich, K.A.2
  • 46
    • 0037567268 scopus 로고    scopus 로고
    • Sensing DNA damage through ATRIP recognition of RPA-ssDNA complexes
    • Zou L., and Elledge S.J. Sensing DNA damage through ATRIP recognition of RPA-ssDNA complexes. Science 300 (2003) 1542-1548
    • (2003) Science , vol.300 , pp. 1542-1548
    • Zou, L.1    Elledge, S.J.2
  • 47
    • 0035941021 scopus 로고    scopus 로고
    • ATR and ATRIP: partners in checkpoint signaling
    • Cortez D., Guntuku S., Qin J., and Elledge S.J. ATR and ATRIP: partners in checkpoint signaling. Science 294 (2001) 1713-1716
    • (2001) Science , vol.294 , pp. 1713-1716
    • Cortez, D.1    Guntuku, S.2    Qin, J.3    Elledge, S.J.4
  • 49
    • 37349014081 scopus 로고    scopus 로고
    • Lange Tel2 regulates the stability of PI3K-related protein kinases
    • Takai H., Wang R.C., Takai K.K., Yang H., and de T. Lange Tel2 regulates the stability of PI3K-related protein kinases. Cell 131 (2007) 1248-1259
    • (2007) Cell , vol.131 , pp. 1248-1259
    • Takai, H.1    Wang, R.C.2    Takai, K.K.3    Yang, H.4    de, T.5
  • 50
    • 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
  • 51
    • 33747188057 scopus 로고    scopus 로고
    • Crossover promotion and prevention
    • Lorenz A., and Whitby M.C. Crossover promotion and prevention. Biochem. Soc. Trans. 34 (2006) 537-541
    • (2006) Biochem. Soc. Trans. , vol.34 , pp. 537-541
    • Lorenz, A.1    Whitby, M.C.2
  • 52
    • 0345447604 scopus 로고    scopus 로고
    • Srs2 and Sgs1-Top3 suppress crossovers during double-strand break repair in yeast
    • Ira G., Malkova A., Liberi G., Foiani M., and Haber J.E. Srs2 and Sgs1-Top3 suppress crossovers during double-strand break repair in yeast. Cell 115 (2003) 401-411
    • (2003) Cell , vol.115 , pp. 401-411
    • Ira, G.1    Malkova, A.2    Liberi, G.3    Foiani, M.4    Haber, J.E.5
  • 53
    • 38649130654 scopus 로고    scopus 로고
    • The Srs2 helicase activity is stimulated by Rad51 filaments on dsDNA: implications for crossover incidence during mitotic recombination
    • Dupaigne P., Le Breton C., Fabre F., Gangloff S., Le Cam E., and Veaute X. The Srs2 helicase activity is stimulated by Rad51 filaments on dsDNA: implications for crossover incidence during mitotic recombination. Mol. Cell 29 (2008) 243-254
    • (2008) Mol. Cell , vol.29 , pp. 243-254
    • Dupaigne, P.1    Le Breton, C.2    Fabre, F.3    Gangloff, S.4    Le Cam, E.5    Veaute, X.6
  • 55
    • 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
  • 57
    • 33744927719 scopus 로고    scopus 로고
    • A double Holliday junction dissolvasome comprising BLM, topoisomerase IIIalpha, and BLAP75
    • Raynard S., Bussen W., and Sung P. A double Holliday junction dissolvasome comprising BLM, topoisomerase IIIalpha, and BLAP75. J. Biol. Chem. 281 (2006) 13861-13864
    • (2006) J. Biol. Chem. , vol.281 , pp. 13861-13864
    • Raynard, S.1    Bussen, W.2    Sung, P.3
  • 58
    • 64249120749 scopus 로고    scopus 로고
    • Replicon dynamics, dormant origin firing, and terminal fork integrity after double-strand break formation
    • Doksani Y., Bermejo R., Fiorani S., Haber J.E., and Foiani M. Replicon dynamics, dormant origin firing, and terminal fork integrity after double-strand break formation. Cell 137 (2009) 247-258
    • (2009) Cell , vol.137 , pp. 247-258
    • Doksani, Y.1    Bermejo, R.2    Fiorani, S.3    Haber, J.E.4    Foiani, M.5
  • 59
    • 0022363977 scopus 로고
    • Methylation-induced blocks to in vitro DNA replication
    • Larson K., Sahm J., Shenkar R., and Strauss B. Methylation-induced blocks to in vitro DNA replication. Mutat. Res. 150 (1985) 77-84
    • (1985) Mutat. Res. , vol.150 , pp. 77-84
    • Larson, K.1    Sahm, J.2    Shenkar, R.3    Strauss, B.4
  • 60
    • 0030971099 scopus 로고    scopus 로고
    • Translesional synthesis on DNA templates containing a single abasic site. A mechanistic study of the "A rule"
    • Shibutani S., Takeshita M., and Grollman A.P. Translesional synthesis on DNA templates containing a single abasic site. A mechanistic study of the "A rule". J. Biol. Chem. 272 (1997) 13916-13922
    • (1997) J. Biol. Chem. , vol.272 , pp. 13916-13922
    • Shibutani, S.1    Takeshita, M.2    Grollman, A.P.3
  • 61
    • 0038365180 scopus 로고    scopus 로고
    • Fate of DNA replication fork encountering a single DNA lesion during oriC plasmid DNA replication in vitro
    • Higuchi K., Katayama T., Iwai S., Hidaka M., Horiuchi T., and Maki H. Fate of DNA replication fork encountering a single DNA lesion during oriC plasmid DNA replication in vitro. Genes Cells 8 (2003) 437-449
    • (2003) Genes Cells , vol.8 , pp. 437-449
    • Higuchi, K.1    Katayama, T.2    Iwai, S.3    Hidaka, M.4    Horiuchi, T.5    Maki, H.6
  • 62
    • 0016605312 scopus 로고
    • Postreplication repair in human cells: on the presence of gaps opposite dimers and recombination
    • Meneghini R., and Hanawalt P.C. Postreplication repair in human cells: on the presence of gaps opposite dimers and recombination. Basic Life Sci. 5B (1975) 639-642
    • (1975) Basic Life Sci. , vol.5 B , pp. 639-642
    • Meneghini, R.1    Hanawalt, P.C.2
  • 63
    • 2442686846 scopus 로고    scopus 로고
    • Functional uncoupling of twin polymerases: mechanism of polymerase dissociation from a lagging-strand block
    • McInerney P., and O'Donnell M. Functional uncoupling of twin polymerases: mechanism of polymerase dissociation from a lagging-strand block. J. Biol. Chem. 279 (2004) 21543-21551
    • (2004) J. Biol. Chem. , vol.279 , pp. 21543-21551
    • McInerney, P.1    O'Donnell, M.2
  • 64
    • 0037799191 scopus 로고    scopus 로고
    • Uncoupling of leading- and lagging-strand DNA replication during lesion bypass in vivo
    • Pages V., and Fuchs R.P. Uncoupling of leading- and lagging-strand DNA replication during lesion bypass in vivo. Science 300 (2003) 1300-1303
    • (2003) Science , vol.300 , pp. 1300-1303
    • Pages, V.1    Fuchs, R.P.2
  • 65
    • 29544437558 scopus 로고    scopus 로고
    • Multiple mechanisms control chromosome integrity after replication fork uncoupling and restart at irreparable UV lesions
    • Lopes M., Foiani M., and Sogo J.M. Multiple mechanisms control chromosome integrity after replication fork uncoupling and restart at irreparable UV lesions. Mol. Cell 21 (2006) 15-27
    • (2006) Mol. Cell , vol.21 , pp. 15-27
    • Lopes, M.1    Foiani, M.2    Sogo, J.M.3
  • 66
    • 33750935287 scopus 로고    scopus 로고
    • Gaps and forks in DNA replication: rediscovering old models
    • Lehmann A.R., and Fuchs R.P. Gaps and forks in DNA replication: rediscovering old models. DNA Repair (Amst.) 5 (2006) 1495-1498
    • (2006) DNA Repair (Amst.) , vol.5 , pp. 1495-1498
    • Lehmann, A.R.1    Fuchs, R.P.2
  • 67
    • 31844456472 scopus 로고    scopus 로고
    • Replication fork reactivation downstream of a blocked nascent leading strand
    • Heller R.C., and Marians K.J. Replication fork reactivation downstream of a blocked nascent leading strand. Nature 439 (2006) 557-562
    • (2006) Nature , vol.439 , pp. 557-562
    • Heller, R.C.1    Marians, K.J.2
  • 68
    • 33947327048 scopus 로고    scopus 로고
    • Replication fork stalling and cell cycle arrest in UV-irradiated Escherichia coli
    • Rudolph C.J., Upton A.L., and Lloyd R.G. Replication fork stalling and cell cycle arrest in UV-irradiated Escherichia coli. Genes Dev. 21 (2007) 668-681
    • (2007) Genes Dev. , vol.21 , pp. 668-681
    • Rudolph, C.J.1    Upton, A.L.2    Lloyd, R.G.3
  • 69
    • 53449085954 scopus 로고    scopus 로고
    • PCNA modifications for regulation of post-replication repair pathways
    • Lee K.Y., and Myung K. PCNA modifications for regulation of post-replication repair pathways. Mol. Cell 26 (2008) 5-11
    • (2008) Mol. Cell , vol.26 , pp. 5-11
    • Lee, K.Y.1    Myung, K.2
  • 71
    • 35648951199 scopus 로고    scopus 로고
    • What a difference a decade makes: insights into translesion DNA synthesis
    • Yang W., and Woodgate R. What a difference a decade makes: insights into translesion DNA synthesis. Proc. Natl. Acad. Sci. U.S.A. 104 (2007) 15591-15598
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 15591-15598
    • Yang, W.1    Woodgate, R.2
  • 72
    • 27644590452 scopus 로고    scopus 로고
    • The error-free component of the RAD6/RAD18 DNA damage tolerance pathway of budding yeast employs sister-strand recombination
    • Zhang H., and Lawrence C.W. The error-free component of the RAD6/RAD18 DNA damage tolerance pathway of budding yeast employs sister-strand recombination. Proc. Natl. Acad. Sci. U.S.A. 102 (2005) 15954-15959
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 15954-15959
    • Zhang, H.1    Lawrence, C.W.2
  • 73
    • 0037705461 scopus 로고    scopus 로고
    • Multiple recombination pathways for sister chromatid exchange in Saccharomyces cerevisiae: role of RAD1 and the RAD52 epistasis group genes
    • Dong Z., and Fasullo M. Multiple recombination pathways for sister chromatid exchange in Saccharomyces cerevisiae: role of RAD1 and the RAD52 epistasis group genes. Nucleic Acids Res. 31 (2003) 2576-2585
    • (2003) Nucleic Acids Res. , vol.31 , pp. 2576-2585
    • Dong, Z.1    Fasullo, M.2
  • 74
    • 33746816108 scopus 로고    scopus 로고
    • The Rad53 signal transduction pathway: replication fork stabilization, DNA repair, and adaptation
    • Branzei D., and Foiani M. The Rad53 signal transduction pathway: replication fork stabilization, DNA repair, and adaptation. Exp. Cell Res. 312 (2006) 2654-2659
    • (2006) Exp. Cell Res. , vol.312 , pp. 2654-2659
    • Branzei, D.1    Foiani, M.2
  • 75
  • 76
    • 14644436335 scopus 로고    scopus 로고
    • In vivo evidence for a recA-independent recombination process in Escherichia coli that permits completion of replication of DNA containing UV damage in both strands
    • Ozgenc A.I., Szekeres E.S., and Lawrence C.W. In vivo evidence for a recA-independent recombination process in Escherichia coli that permits completion of replication of DNA containing UV damage in both strands. J. Bacteriol. 187 (2005) 1974-1984
    • (2005) J. Bacteriol. , vol.187 , pp. 1974-1984
    • Ozgenc, A.I.1    Szekeres, E.S.2    Lawrence, C.W.3
  • 77
    • 2442572065 scopus 로고    scopus 로고
    • Yeast MPH1 gene functions in an error-free DNA damage bypass pathway that requires genes from homologous recombination, but not from postreplicative repair
    • Schurer K.A., Rudolph C., Ulrich H.D., and Kramer W. Yeast MPH1 gene functions in an error-free DNA damage bypass pathway that requires genes from homologous recombination, but not from postreplicative repair. Genetics 166 (2004) 1673-1686
    • (2004) Genetics , vol.166 , pp. 1673-1686
    • Schurer, K.A.1    Rudolph, C.2    Ulrich, H.D.3    Kramer, W.4
  • 79
    • 33750437743 scopus 로고    scopus 로고
    • Ubc9- and Mms21-mediated sumoylation counteracts recombinogenic events at damaged replication forks
    • Branzei D., Sollier J., Liberi G., Zhao X., Maeda D., Seki M., Enomoto T., Ohta K., and Foiani M. Ubc9- and Mms21-mediated sumoylation counteracts recombinogenic events at damaged replication forks. Cell 127 (2006) 509-522
    • (2006) Cell , vol.127 , pp. 509-522
    • Branzei, D.1    Sollier, J.2    Liberi, G.3    Zhao, X.4    Maeda, D.5    Seki, M.6    Enomoto, T.7    Ohta, K.8    Foiani, M.9
  • 80
    • 65249090885 scopus 로고    scopus 로고
    • Esc2 and Sgs1 act in functionally distinct branches of the homologous recombination repair pathway in Saccharomyces cerevisiae
    • Mankouri H.W., Ngo H.P., and Hickson I.D. Esc2 and Sgs1 act in functionally distinct branches of the homologous recombination repair pathway in Saccharomyces cerevisiae. Mol. Biol. Cell 20 (2009) 1683-1694
    • (2009) Mol. Biol. Cell , vol.20 , pp. 1683-1694
    • Mankouri, H.W.1    Ngo, H.P.2    Hickson, I.D.3
  • 81
    • 65249118311 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae Esc2 and Smc5-6 proteins promote sister chromatid junction-mediated intra-S repair
    • Sollier J., Driscoll R., Castellucci F., Foiani M., Jackson S.P., and Branzei D. The Saccharomyces cerevisiae Esc2 and Smc5-6 proteins promote sister chromatid junction-mediated intra-S repair. Mol. Biol. Cell 20 (2009) 1671-1682
    • (2009) Mol. Biol. Cell , vol.20 , pp. 1671-1682
    • Sollier, J.1    Driscoll, R.2    Castellucci, F.3    Foiani, M.4    Jackson, S.P.5    Branzei, D.6
  • 82
    • 25444484394 scopus 로고    scopus 로고
    • Proteins with two SUMO-like domains in chromatin-associated complexes: the RENi (Rad60-Esc2-NIP45) family
    • Novatchkova M., Bachmair A., Eisenhaber B., and Eisenhaber F. Proteins with two SUMO-like domains in chromatin-associated complexes: the RENi (Rad60-Esc2-NIP45) family. BMC Bioinform. 6 (2005) 22
    • (2005) BMC Bioinform. , vol.6 , pp. 22
    • Novatchkova, M.1    Bachmair, A.2    Eisenhaber, B.3    Eisenhaber, F.4
  • 84
    • 21244449061 scopus 로고    scopus 로고
    • Crosstalk between SUMO and ubiquitin on PCNA is mediated by recruitment of the helicase Srs2p
    • Papouli E., Chen S., Davies A.A., Huttner D., Krejci L., Sung P., and Ulrich H.D. Crosstalk between SUMO and ubiquitin on PCNA is mediated by recruitment of the helicase Srs2p. Mol. Cell 19 (2005) 123-133
    • (2005) Mol. Cell , vol.19 , pp. 123-133
    • Papouli, E.1    Chen, S.2    Davies, A.A.3    Huttner, D.4    Krejci, L.5    Sung, P.6    Ulrich, H.D.7
  • 85
    • 0037068455 scopus 로고    scopus 로고
    • RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO
    • Hoege C., Pfander B., Moldovan G.L., Pyrowolakis G., and Jentsch S. RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO. Nature 419 (2002) 135-141
    • (2002) Nature , vol.419 , pp. 135-141
    • Hoege, C.1    Pfander, B.2    Moldovan, G.L.3    Pyrowolakis, G.4    Jentsch, S.5
  • 86
    • 21244440716 scopus 로고    scopus 로고
    • Replication fork blockage by RTS1 at an ectopic site promotes recombination in fission yeast
    • Ahn J.S., Osman F., and Whitby M.C. Replication fork blockage by RTS1 at an ectopic site promotes recombination in fission yeast. EMBO J. 24 (2005) 2011-2023
    • (2005) EMBO J. , vol.24 , pp. 2011-2023
    • Ahn, J.S.1    Osman, F.2    Whitby, M.C.3
  • 87
    • 3943086339 scopus 로고    scopus 로고
    • Flap endonuclease 1: a central component of DNA metabolism
    • Liu Y., Kao H.I., and Bambara R.A. Flap endonuclease 1: a central component of DNA metabolism. Annu. Rev. Biochem. 73 (2004) 589-615
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 589-615
    • Liu, Y.1    Kao, H.I.2    Bambara, R.A.3
  • 88
    • 0034528196 scopus 로고    scopus 로고
    • Characterization of the enzymatic properties of the yeast dna2 helicase/endonuclease suggests a new model for Okazaki fragment processing
    • Bae S.H., and Seo Y.S. Characterization of the enzymatic properties of the yeast dna2 helicase/endonuclease suggests a new model for Okazaki fragment processing. J. Biol. Chem. 275 (2000) 38022-38031
    • (2000) J. Biol. Chem. , vol.275 , pp. 38022-38031
    • Bae, S.H.1    Seo, Y.S.2
  • 89
    • 0035954737 scopus 로고    scopus 로고
    • RPA governs endonuclease switching during processing of Okazaki fragments in eukaryotes
    • Bae S.H., Bae K.H., Kim J.A., and Seo Y.S. RPA governs endonuclease switching during processing of Okazaki fragments in eukaryotes. Nature 412 (2001) 456-461
    • (2001) Nature , vol.412 , pp. 456-461
    • Bae, S.H.1    Bae, K.H.2    Kim, J.A.3    Seo, Y.S.4
  • 90
    • 10944271787 scopus 로고    scopus 로고
    • Dna2p helicase/nuclease is a tracking protein, like FEN1, for flap cleavage during Okazaki fragment maturation
    • Kao H.I., Campbell J.L., and Bambara R.A. Dna2p helicase/nuclease is a tracking protein, like FEN1, for flap cleavage during Okazaki fragment maturation. J. Biol. Chem. 279 (2004) 50840-50849
    • (2004) J. Biol. Chem. , vol.279 , pp. 50840-50849
    • Kao, H.I.1    Campbell, J.L.2    Bambara, R.A.3
  • 91
    • 67449091971 scopus 로고    scopus 로고
    • The MPH1 gene of Saccharomyces cerevisiae functions in Okazaki fragment processing
    • Kang Y.H., Kang M.J., Kim J.H., Lee C.H., Cho I.T., Hurwitz J., and Seo Y.S. The MPH1 gene of Saccharomyces cerevisiae functions in Okazaki fragment processing. J. Biol. Chem. 284 (2009) 10376-10386
    • (2009) J. Biol. Chem. , vol.284 , pp. 10376-10386
    • Kang, Y.H.1    Kang, M.J.2    Kim, J.H.3    Lee, C.H.4    Cho, I.T.5    Hurwitz, J.6    Seo, Y.S.7
  • 92
    • 43249128930 scopus 로고    scopus 로고
    • Mus81 is essential for sister chromatid recombination at broken replication forks
    • Roseaulin L., Yamada Y., Tsutsui Y., Russell P., Iwasaki H., and Arcangioli B. Mus81 is essential for sister chromatid recombination at broken replication forks. EMBO J. 27 (2008) 1378-1387
    • (2008) EMBO J. , vol.27 , pp. 1378-1387
    • Roseaulin, L.1    Yamada, Y.2    Tsutsui, Y.3    Russell, P.4    Iwasaki, H.5    Arcangioli, B.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.