메뉴 건너뛰기




Volumn , Issue , 2009, Pages 349-366

Single-stranded DNA Binding proteins involved in genome maintenance

Author keywords

ATM; DNA; Repair; Replication; RPA; SSB

Indexed keywords


EID: 84874433075     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1007/978-90-481-2561-6_16     Document Type: Chapter
Times cited : (3)

References (126)
  • 1
    • 51349140504 scopus 로고    scopus 로고
    • RPA phosphorylation facilitates mitotic exit in response to mitotic DNA damage
    • Anantha, R. W., E. Sokolova, and J. A. Borowiec. 2008. RPA phosphorylation facilitates mitotic exit in response to mitotic DNA damage. Proc Natl Acad Sci USA. 105:12903-8.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 12903-12908
    • Anantha, R.W.1    Sokolova, E.2    Borowiec, J.A.3
  • 2
    • 0030969429 scopus 로고    scopus 로고
    • The recombination hot spot chi is a regulatory element that switches the polarity of DNA degradation by the RecBCD enzyme
    • Anderson, D. G., and S. C. Kowalczykowski. 1997. The recombination hot spot chi is a regulatory element that switches the polarity of DNA degradation by the RecBCD enzyme. Genes Dev. 11:571-81.
    • (1997) Genes Dev. , vol.11 , pp. 571-581
    • Anderson, D.G.1    Kowalczykowski, S.C.2
  • 3
    • 4444372436 scopus 로고    scopus 로고
    • Development of a high-throughput screen for inhibitors of replication protein A and its role in nucleotide excision repair
    • Andrews, B. J., and J. J. Turchi. 2004. Development of a high-throughput screen for inhibitors of replication protein A and its role in nucleotide excision repair. Mol Cancer Ther. 3:385-91.
    • (2004) Mol Cancer Ther. , vol.3 , pp. 385-391
    • Andrews, B.J.1    Turchi, J.J.2
  • 4
    • 43749084397 scopus 로고    scopus 로고
    • Single-stranded DNAbinding protein recruits DNA polymerase v to primer termini on RecA-coated DNA
    • Arad, G., A. Hendel, C. Urbanke, U. Curth, and Z. Livneh. 2008. Single-stranded DNAbinding protein recruits DNA polymerase V to primer termini on RecA-coated DNA. J Biol Chem. 283:8274-82.
    • (2008) J Biol Chem. , vol.283 , pp. 8274-8282
    • Arad, G.1    Hendel, A.2    Urbanke, C.3    Curth, U.4    Livneh, Z.5
  • 5
    • 0029866780 scopus 로고    scopus 로고
    • Reversible protein phosphorylationmodulates nucleotide excision repair of damaged DNA by human cell extracts
    • Ariza, R. R., S. M. Keyse, J. G. Moggs, and R. D. Wood. 1996. Reversible protein phosphorylationmodulates nucleotide excision repair of damaged DNA by human cell extracts. Nucleic Acids Res. 24:433-40.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 433-440
    • Ariza, R.R.1    Keyse, S.M.2    Moggs, J.G.3    Wood, R.D.4
  • 6
    • 0142135087 scopus 로고    scopus 로고
    • Independent and coordinated functions of replication protein A tandem high affinity single-stranded DNA binding domains
    • Arunkumar, A. I., M. E. Stauffer, E. Bochkareva, A. Bochkarev, and W. J. Chazin. 2003. Independent and coordinated functions of replication protein A tandem high affinity single-stranded DNA binding domains. J Biol Chem. 278:41077-82.
    • (2003) J Biol Chem. , vol.278 , pp. 41077-41082
    • Arunkumar, A.I.1    Stauffer, M.E.2    Bochkareva, E.3    Bochkarev, A.4    Chazin, W.J.5
  • 8
    • 18244385718 scopus 로고    scopus 로고
    • ATRIP binding to replication protein Asingle- stranded DNA promotes ATR-ATRIP localization but is dispensable for Chk1 phosphorylation
    • Ball, H. L., J. S. Myers, and D. Cortez. 2005. ATRIP binding to replication protein Asingle- stranded DNA promotes ATR-ATRIP localization but is dispensable for Chk1 phosphorylation. Mol Biol Cell. 16:2372-81.
    • (2005) Mol Biol Cell. , vol.16 , pp. 2372-2381
    • Ball, H.L.1    Myers, J.S.2    Cortez, D.3
  • 9
    • 3442896884 scopus 로고    scopus 로고
    • Replication protein A phosphorylation and the cellular response to DNA damage
    • Binz, S. K., A. M. Sheehan, and M. S. Wold. 2004. Replication protein A phosphorylation and the cellular response to DNA damage. DNA Repair (Amst). 3:1015-24.
    • (2004) DNA Repair (Amst) , vol.3 , pp. 1015-1024
    • Binz, S.K.1    Sheehan, A.M.2    Wold, M.S.3
  • 11
    • 0029759341 scopus 로고    scopus 로고
    • Single-stranded-DNA binding alters human replication protein A structure and facilitates interaction with DNA-dependent protein kinase
    • Blackwell, L. J., J. A. Borowiec, and I. A. Masrangelo. 1996. Single-stranded-DNA binding alters human replication protein A structure and facilitates interaction with DNA-dependent protein kinase. Mol Cell Biol. 16:4798-807.
    • (1996) Mol Cell Biol. , vol.16 , pp. 4798-4807
    • Blackwell, L.J.1    Borowiec, J.A.2    Masrangelo, I.A.3
  • 12
    • 2342618116 scopus 로고    scopus 로고
    • Phosphatidyl inositol 3-kinase-like serine/ threonine protein kinases (PIKKs) are required for DNA damage-induced phosphorylation of the 32 kDa subunit of replication protein A at threonine 21
    • Block, W. D., Y. Yu, and S. P. Lees-Miller. 2004. Phosphatidyl inositol 3-kinase-like serine/ threonine protein kinases (PIKKs) are required for DNA damage-induced phosphorylation of the 32 kDa subunit of replication protein A at threonine 21. Nucleic Acids Res. 32:997-1005.
    • (2004) Nucleic Acids Res. , vol.32 , pp. 997-1005
    • Block, W.D.1    Yu, Y.2    Lees-Miller, S.P.3
  • 13
    • 1342302794 scopus 로고    scopus 로고
    • From RPA to BRCA2: Lessons from singlestranded DNA binding by the OB-fold
    • Bochkarev, A., and E. Bochkareva. 2004. From RPA to BRCA2: lessons from singlestranded DNA binding by the OB-fold. Curr Opin Struct Biol. 14:36-42.
    • (2004) Curr Opin Struct Biol. , vol.14 , pp. 36-42
    • Bochkarev, A.1    Bochkareva, E.2
  • 15
    • 0037007223 scopus 로고    scopus 로고
    • Structure of the RPA trimerization core and its role in the multistep DNA-binding mechanism of RPA
    • Bochkareva, E., S. Korolev, S. P. Lees-Miller, and A. Bochkarev. 2002. Structure of the RPA trimerization core and its role in the multistep DNA-binding mechanism of RPA. Embo J. 21:1855-63.
    • (2002) Embo J. , vol.21 , pp. 1855-1863
    • Bochkareva, E.1    Korolev, S.2    Lees-Miller, S.P.3    Bochkarev, A.4
  • 16
    • 0030140414 scopus 로고    scopus 로고
    • Internal repeats in the BRCA2 protein sequence
    • Bork, P., N. Blomberg, and M. Nilges. 1996. Internal repeats in the BRCA2 protein sequence. Nat Genet. 13:22-3.
    • (1996) Nat Genet. , vol.13 , pp. 22-23
    • Bork, P.1    Blomberg, N.2    Nilges, M.3
  • 18
    • 32844458451 scopus 로고    scopus 로고
    • Mechanisms of eukaryotic DNA double strand break repair
    • Cahill, D., B. Connor, and J. P. Carney. 2006. Mechanisms of eukaryotic DNA double strand break repair. Front Biosci. 11:1958-76.
    • (2006) Front Biosci. , vol.11 , pp. 1958-1976
    • Cahill, D.1    Connor, B.2    Carney, J.P.3
  • 19
    • 0028355488 scopus 로고
    • UV light-induced DNA synthesis arrest in HeLa cells is associated with changes in phosphorylation of human singlestranded DNA-binding protein
    • Carty, M. P., M. Zernik-Kobak, S. McGrath, and K. Dixon. 1994. UV light-induced DNA synthesis arrest in HeLa cells is associated with changes in phosphorylation of human singlestranded DNA-binding protein. Embo J. 13:2114-23.
    • (1994) Embo J. , vol.13 , pp. 2114-2123
    • Carty, M.P.1    Zernik-Kobak, M.2    McGrath, S.3    Dixon, K.4
  • 20
    • 0037093318 scopus 로고    scopus 로고
    • Cdc2-cyclin B kinase activity links Crb2 and Rqh1-topoisomerase III
    • Caspari, T., J. M. Murray, and A. M. Carr. 2002. Cdc2-cyclin B kinase activity links Crb2 and Rqh1-topoisomerase III. Genes Dev. 16:1195-208.
    • (2002) Genes Dev. , vol.16 , pp. 1195-1208
    • Caspari, T.1    Murray, J.M.2    Carr, A.M.3
  • 21
    • 0032109778 scopus 로고    scopus 로고
    • Chromosomal rearrangements occur in s. cerevisiae rfa1 mutator mutants due to mutagenic lesions processed by double-strand-break repair
    • Chen, C., K. Umezu, and R. D. Kolodner. 1998. Chromosomal rearrangements occur in S. cerevisiae rfa1 mutator mutants due to mutagenic lesions processed by double-strand-break repair. Mol Cell. 2:9-22.
    • (1998) Mol Cell. , vol.2 , pp. 9-22
    • Chen, C.1    Umezu, K.2    Kolodner, R.D.3
  • 22
    • 0032860479 scopus 로고    scopus 로고
    • Gross chromosomal rearrangements in Saccharomyces cerevisiae replication and recombination defective mutants
    • Chen, C., and R. D. Kolodner. 1999. Gross chromosomal rearrangements in Saccharomyces cerevisiae replication and recombination defective mutants. Nat Genet. 23:81-5.
    • (1999) Nat Genet. , vol.23 , pp. 81-85
    • Chen, C.1    Kolodner, R.D.2
  • 23
    • 43149118369 scopus 로고    scopus 로고
    • Cell cycle-dependent complex formation of BRCA1. CtIP MRN is important for DNA double-strand break repair
    • Chen, L., C. J. Nievera, A. Y. Lee, and X. Wu. 2008. Cell cycle-dependent complex formation of BRCA1. CtIP. MRN is important for DNA double-strand break repair. J Biol Chem. 283:7713-20.
    • (2008) J Biol Chem. , vol.283 , pp. 7713-7720
    • Chen, L.1    Nievera, C.J.2    Lee, A.Y.3    Wu, X.4
  • 24
    • 0032574733 scopus 로고    scopus 로고
    • The BRC repeats in BRCA2 are critical for RAD51 binding and resistance to methyl methanesulfonate treatment
    • Chen, P. L., C. F. Chen, Y. Chen, J. Xiao, Z. D. Sharp, and W. H. Lee. 1998b. The BRC repeats in BRCA2 are critical for RAD51 binding and resistance to methyl methanesulfonate treatment. Proc Natl Acad Sci USA. 95:5287-92.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 5287-5292
    • Chen, P.L.1    Chen, C.F.2    Chen, Y.3    Xiao, J.4    Sharp, Z.D.5    Lee, W.H.6
  • 25
    • 0028366253 scopus 로고
    • Loss of S-phase-dependent radioresistance in irs-1 cells exposed to X-rays
    • Cheong, N., X. Wang, Y. Wang, and G. Iliakis. 1994. Loss of S-phase-dependent radioresistance in irs-1 cells exposed to X-rays. Mutat Res. 314:77-85.
    • (1994) Mutat Res. , vol.314 , pp. 77-85
    • Cheong, N.1    Wang, X.2    Wang, Y.3    Iliakis, G.4
  • 26
    • 0036154228 scopus 로고    scopus 로고
    • BRCA1 modulates ionizing radiation-induced nuclear focus formation by the replication protein A p34 subunit
    • Choudhary, S. K., and R. Li. 2002. BRCA1 modulates ionizing radiation-induced nuclear focus formation by the replication protein A p34 subunit. J Cell Biochem. 84:666-74.
    • (2002) J Cell Biochem. , vol.84 , pp. 666-674
    • Choudhary, S.K.1    Li, R.2
  • 27
    • 2542422284 scopus 로고    scopus 로고
    • The Rad52-Rad59 complex interacts with Rad51 and replication protein A
    • Davis, A. P., and L. S. Symington. 2003. The Rad52-Rad59 complex interacts with Rad51 and replication protein A. DNA Repair (Amst). 2:1127-34.
    • (2003) DNA Repair (Amst) , vol.2 , pp. 1127-1134
    • Davis, A.P.1    Symington, L.S.2
  • 29
    • 0032529167 scopus 로고    scopus 로고
    • DNA-binding polarity of human replication protein A positions nucleases in nucleotide excision repair
    • de Laat, W. L., E. Appeldoorn, K. Sugasawa, E. Weterings, N. G. Jaspers, and J. H. Hoeijmakers. 1998. DNA-binding polarity of human replication protein A positions nucleases in nucleotide excision repair. Genes Dev. 12:2598-609.
    • (1998) Genes Dev. , vol.12 , pp. 2598-2609
    • De Laat, W.L.1    Appeldoorn, E.2    Sugasawa, K.3    Weterings, E.4    Jaspers, N.G.5    Hoeijmakers, J.H.6
  • 30
    • 0009607249 scopus 로고
    • Simian virus 40 (SV40) DNA replication: SV40 large T antigen unwinds DNA containing the SV40 origin of replication
    • Dean, F. B., P. Bullock, Y. Murakami, C. R. Wobbe, L. Weissbach, and J. Hurwitz. 1987. Simian virus 40 (SV40) DNA replication: SV40 large T antigen unwinds DNA containing the SV40 origin of replication. Proc Natl Acad Sci USA. 84:16-20.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 16-20
    • Dean, F.B.1    Bullock, P.2    Murakami, Y.3    Wobbe, C.R.4    Weissbach, L.5    Hurwitz, J.6
  • 31
    • 0025365192 scopus 로고
    • Cell-cycle-regulated phosphorylation of DNA replication factor A from human and yeast cells
    • Din, S., S. J. Brill, M. P. Fairman, and B. Stillman. 1990. Cell-cycle-regulated phosphorylation of DNA replication factor A from human and yeast cells. Genes Dev. 4:968-77.
    • (1990) Genes Dev. , vol.4 , pp. 968-977
    • Din, S.1    Brill, S.J.2    Fairman, M.P.3    Stillman, B.4
  • 32
    • 0027358857 scopus 로고
    • Inhibition of DNA replication factor RPA by p 53
    • Dutta, A., J. M. Ruppert, J. C. Aster, and E. Winchester. 1993. Inhibition of DNA replication factor RPA by p 53. Nature. 365:79-82.
    • (1993) Nature. , vol.365 , pp. 79-82
    • Dutta, A.1    Ruppert, J.M.2    Aster, J.C.3    Winchester, E.4
  • 33
    • 0026539144 scopus 로고
    • Cdc2 family kinases phosphorylate a human cell DNA replication factor, RPA, and activate DNA replication
    • Dutta, A., and B. Stillman. 1992. cdc2 family kinases phosphorylate a human cell DNA replication factor, RPA, and activate DNA replication. Embo J. 11:2189-99.
    • (1992) Embo J. , vol.11 , pp. 2189-2199
    • Dutta, A.1    Stillman, B.2
  • 34
    • 1842311742 scopus 로고
    • Cellular factors required for multiple stages of SV40 DNA replication in vitro
    • Fairman, M. P., and B. Stillman. 1988. Cellular factors required for multiple stages of SV40 DNA replication in vitro. Embo J. 7:1211-8.
    • (1988) Embo J. , vol.7 , pp. 1211-1218
    • Fairman, M.P.1    Stillman, B.2
  • 35
    • 0027517871 scopus 로고
    • Distinct roles of cdk2 and cdc2 in RP-A phosphorylation during the cell cycle
    • Fang, F., and J. W. Newport. 1993. Distinct roles of cdk2 and cdc2 in RP-A phosphorylation during the cell cycle. J Cell Sci. 106 (Pt 3):983-94.
    • (1993) J Cell Sci , vol.106 , Issue.PART 3 , pp. 983-994
    • Fang, F.1    Newport, J.W.2
  • 36
    • 0035106262 scopus 로고    scopus 로고
    • The fission yeast Taz1 protein protects chromosomes from Ku-dependent end-to-end fusions
    • Ferreira, M. G., and J. P. Cooper. 2001. The fission yeast Taz1 protein protects chromosomes from Ku-dependent end-to-end fusions. Mol Cell. 7:55-63.
    • (2001) Mol Cell. , vol.7 , pp. 55-63
    • Ferreira, M.G.1    Cooper, J.P.2
  • 37
    • 0037173719 scopus 로고    scopus 로고
    • Impaired DNA damageinduced nuclear Rad51 foci formation uniquely characterizes Fanconi anemia group D 1
    • Godthelp, B. C., F. Artwert, H. Joenje, and M. Z. Zdzienicka. 2002. Impaired DNA damageinduced nuclear Rad51 foci formation uniquely characterizes Fanconi anemia group D 1. Oncogene. 21:5002-5.
    • (2002) Oncogene. , vol.21 , pp. 5002-5005
    • Godthelp, B.C.1    Artwert, F.2    Joenje, H.3    Zdzienicka, M.Z.4
  • 38
    • 0029868656 scopus 로고    scopus 로고
    • Proteolytic mapping of human replication protein A: Evidence for multiple structural domains and a conformational change upon interaction with single-stranded DNA
    • Gomes, X. V., L. A. Henricksen, and M. S. Wold. 1996. Proteolytic mapping of human replication protein A: evidence for multiple structural domains and a conformational change upon interaction with single-stranded DNA. Biochemistry. 35:5586-95.
    • (1996) Biochemistry , vol.35 , pp. 5586-5595
    • Gomes, X.V.1    Henricksen, L.A.2    Wold, M.S.3
  • 40
    • 0035907374 scopus 로고    scopus 로고
    • Chimeras between single-stranded DNAbinding proteins from Escherichia coli and Mycobacterium tuberculosis reveal that their C-terminal domains interact with uracil DNA glycosylases
    • Handa, P., N. Acharya, and U. Varshney. 2001. Chimeras between single-stranded DNAbinding proteins from Escherichia coli and Mycobacterium tuberculosis reveal that their C-terminal domains interact with uracil DNA glycosylases. J Biol Chem. 276: 16992-7.
    • (2001) J Biol Chem. , vol.276 , pp. 16992-16997
    • Handa, P.1    Acharya, N.2    Varshney, U.3
  • 41
    • 0027299244 scopus 로고
    • The transactivator proteins VP16 and GAL4 bind replication factor A
    • He, Z., B. T. Brinton, J. Greenblatt, J. A. Hassell, and C. J. Ingles. 1993. The transactivator proteins VP16 and GAL4 bind replication factor A. Cell. 73:1223-32.
    • (1993) Cell. , vol.73 , pp. 1223-1232
    • He, Z.1    Brinton, B.T.2    Greenblatt, J.3    Hassell, J.A.4    Ingles, C.J.5
  • 42
    • 0034601672 scopus 로고    scopus 로고
    • 5 -3 -molecular polarity of human replication protein A (hRPA) binding to pseudo-origin DNA substrates
    • Iftode, C., and J. A. Borowiec. 2000. 5 -3 -molecular polarity of human replication protein A (hRPA) binding to pseudo-origin DNA substrates. Biochemistry. 39:11970-81.
    • (2000) Biochemistry , vol.39 , pp. 11970-11981
    • Iftode, C.1    Borowiec, J.A.2
  • 45
    • 0036349930 scopus 로고    scopus 로고
    • Analysis of the human replication protein A:Rad52 complex: Evidence for crosstalk between RPA32, RPA70, Rad52 and DNA
    • Jackson, D., K. Dhar, J. K. Wahl, M. S. Wold, and G. E. Borgstahl. 2002. Analysis of the human replication protein A:Rad52 complex: evidence for crosstalk between RPA32, RPA70, Rad52 and DNA. J Mol Biol. 321:133-48.
    • (2002) J Mol Biol. , vol.321 , pp. 133-148
    • Jackson, D.1    Dhar, K.2    Wahl, J.K.3    Wold, M.S.4    Borgstahl, G.E.5
  • 47
    • 0032522760 scopus 로고    scopus 로고
    • Devoted to the lagging strand-The subunit of DNA polymerase III holoenzyme contacts SSB to promote processive elongation and sliding clamp assembly
    • Kelman, Z., A. Yuzhakov, J. Andjelkovic, and M. O'Donnell. 1998. Devoted to the lagging strand-the subunit of DNA polymerase III holoenzyme contacts SSB to promote processive elongation and sliding clamp assembly. Embo J. 17:2436-49.
    • (1998) Embo J. , vol.17 , pp. 2436-2449
    • Kelman, Z.1    Yuzhakov, A.2    Andjelkovic, J.3    O'Donnell, M.4
  • 48
    • 0027939024 scopus 로고
    • Interactions of human replication protein A with oligonucleotides
    • Kim, C., B. F. Paulus, andM. S. Wold. 1994. Interactions of human replication protein A with oligonucleotides. Biochemistry. 33:14197-206.
    • (1994) Biochemistry. , vol.33 , pp. 14197-14206
    • Kim, C.1    Paulus, B.F.2    Wold, M.S.3
  • 49
    • 0026772415 scopus 로고
    • Binding properties of replication protein A from human and yeast cells
    • Kim, C., R. O. Snyder, and M. S. Wold. 1992. Binding properties of replication protein A from human and yeast cells. Mol Cell Biol. 12:3050-9.
    • (1992) Mol Cell Biol. , vol.12 , pp. 3050-3059
    • Kim, C.1    Snyder, R.O.2    Wold, M.S.3
  • 50
    • 0028957756 scopus 로고
    • Recombinant human replication protein A binds to polynucleotides with low cooperativity
    • Kim, C., and M. S. Wold. 1995. Recombinant human replication protein A binds to polynucleotides with low cooperativity. Biochemistry. 34:2058-64.
    • (1995) Biochemistry. , vol.34 , pp. 2058-2064
    • Kim, C.1    Wold, M.S.2
  • 51
    • 0029892484 scopus 로고    scopus 로고
    • Role of the 70-kDa subunit of human replication protein A (I). Single-stranded dna binding activity, but not polymerase stimulatory activity, is required for DNA replication
    • Kim, D. K., E. Stigger, and S. H. Lee. 1996. Role of the 70-kDa subunit of human replication protein A (I). Single-stranded dna binding activity, but not polymerase stimulatory activity, is required for DNA replication. J Biol Chem. 271:15124-9.
    • (1996) J Biol Chem. , vol.271 , pp. 15124-15129
    • Kim, D.K.1    Stigger, E.2    Lee, S.H.3
  • 52
    • 23744447715 scopus 로고    scopus 로고
    • Independent and sequential recruitment of NHEJ and HR factors to DNA damage sites in mammalian cells
    • Kim, J. S., T. B. Krasieva, H. Kurumizaka, D. J. Chen, A. M. Taylor, and K. Yokomori. 2005. Independent and sequential recruitment of NHEJ and HR factors to DNA damage sites in mammalian cells. J Cell Biol. 170:341-7.
    • (2005) J Cell Biol. , vol.170 , pp. 341-347
    • Kim, J.S.1    Krasieva, T.B.2    Kurumizaka, H.3    Chen, D.J.4    Taylor, A.M.5    Yokomori, K.6
  • 55
    • 10344263324 scopus 로고    scopus 로고
    • Recombination proteins in yeast
    • Krogh, B. O., and L. S. Symington. 2004. Recombination proteins in yeast. Annu Rev Genet. 38:233-71.
    • (2004) Annu Rev Genet. , vol.38 , pp. 233-271
    • Krogh, B.O.1    Symington, L.S.2
  • 56
    • 9644275421 scopus 로고    scopus 로고
    • Claspin and the activated form of ATRATRIP collaborate in the activation of Chk1
    • Kumagai, A., S. M. Kim, and W. G. Dunphy. 2004. Claspin and the activated form of ATRATRIP collaborate in the activation of Chk1. J Biol Chem. 279:49599-608.
    • (2004) J Biol Chem. , vol.279 , pp. 49599-49608
    • Kumagai, A.1    Kim, S.M.2    Dunphy, W.G.3
  • 58
    • 0037291130 scopus 로고    scopus 로고
    • Claspin, a Chk1-regulatory protein, monitors DNA replication on chromatin independently of RPA, ATR, and Rad17
    • Lee, J., A. Kumagai, and W. G. Dunphy. 2003. Claspin, a Chk1-regulatory protein, monitors DNA replication on chromatin independently of RPA, ATR, and Rad17. Mol Cell. 11:329-40.
    • (2003) Mol Cell. , vol.11 , pp. 329-340
    • Lee, J.1    Kumagai, A.2    Dunphy, W.G.3
  • 59
    • 0027195936 scopus 로고
    • The acidic transcriptional activation domains of VP16 and p53 bind the cellular replication protein A and stimulate in vitro BPV-1 DNA replication
    • Li, R., and M. R. Botchan. 1993. The acidic transcriptional activation domains of VP16 and p53 bind the cellular replication protein A and stimulate in vitro BPV-1 DNA replication. Cell. 73:1207-21.
    • (1993) Cell. , vol.73 , pp. 1207-1221
    • Li, R.1    Botchan, M.R.2
  • 60
    • 2342628449 scopus 로고    scopus 로고
    • Human Claspin works with BRCA1 to both positively and negatively regulate cell proliferation
    • Lin, S. Y., K. Li, G. S. Stewart, and S. J. Elledge. 2004. Human Claspin works with BRCA1 to both positively and negatively regulate cell proliferation. Proc Natl Acad Sci USA. 101:6484-9.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 6484-6489
    • Lin, S.Y.1    Li, K.2    Stewart, G.S.3    Elledge, S.J.4
  • 61
    • 4544281398 scopus 로고    scopus 로고
    • Choreography of the DNA damage response: Spatiotemporal relationships among checkpoint and repair proteins
    • Lisby, M., J. H. Barlow, R. C. Burgess, and R. Rothstein. 2004. Choreography of the DNA damage response: spatiotemporal relationships among checkpoint and repair proteins. Cell. 118:699-713.
    • (2004) Cell. , vol.118 , pp. 699-713
    • Lisby, M.1    Barlow, J.H.2    Burgess, R.C.3    Rothstein, R.4
  • 62
    • 0023114469 scopus 로고
    • Homology requirement for efficient gene conversion between duplicated chromosomal sequences in mammalian cells
    • Liskay, R. M., A. Letsou, and J. L. Stachelek. 1987. Homology requirement for efficient gene conversion between duplicated chromosomal sequences in mammalian cells. Genetics. 115:161-7.
    • (1987) Genetics. , vol.115 , pp. 161-167
    • Liskay, R.M.1    Letsou, A.2    Stachelek, J.L.3
  • 63
    • 0033954476 scopus 로고    scopus 로고
    • Adozelesin triggers DNA damage response pathways and arrests SV40 DNA replication through replication protein A inactivation
    • Liu, J. S., S. R. Kuo, M. M. McHugh, T. A. Beerman, and T. Melendy. 2000. Adozelesin triggers DNA damage response pathways and arrests SV40 DNA replication through replication protein A inactivation. J Biol Chem. 275:1391-7.
    • (2000) J Biol Chem. , vol.275 , pp. 1391-1397
    • Liu, J.S.1    Kuo, S.R.2    McHugh, M.M.3    Beerman, T.A.4    Melendy, T.5
  • 64
    • 0027428513 scopus 로고
    • The ionizing radiation-induced replication protein A phosphorylation response differs between ataxia telangiectasia and normal human cells
    • Liu, V. F., and D. T. Weaver. 1993. The ionizing radiation-induced replication protein A phosphorylation response differs between ataxia telangiectasia and normal human cells. Mol Cell Biol. 13:7222-31.
    • (1993) Mol Cell Biol. , vol.13 , pp. 7222-7231
    • Liu, V.F.1    Weaver, D.T.2
  • 65
    • 12844281114 scopus 로고    scopus 로고
    • Interactions of human replication protein A with single-stranded DNA adducts
    • Liu, Y., Z. Yang, C. D. Utzat, Y. Liu, N. E. Geacintov, A. K. Basu, and Y. Zou. 2005. Interactions of human replication protein A with single-stranded DNA adducts. Biochem J. 385:519-26.
    • (2005) Biochem J. , vol.385 , pp. 519-526
    • Liu, Y.1    Yang, Z.2    Utzat, C.D.3    Liu, Y.4    Geacintov, N.E.5    Basu, A.K.6    Zou, Y.7
  • 66
    • 0028246888 scopus 로고
    • Escherichia coli single-stranded DNA-binding protein: Multiple DNA-binding modes and cooperativities
    • Lohman, T. M., and M. E. Ferrari. 1994. Escherichia coli single-stranded DNA-binding protein: multiple DNA-binding modes and cooperativities. Annu Rev Biochem. 63:527-70.
    • (1994) Annu Rev Biochem. , vol.63 , pp. 527-570
    • Lohman, T.M.1    Ferrari, M.E.2
  • 67
    • 0034711381 scopus 로고    scopus 로고
    • Reconstitution of the strand invasion step of double-strand break repair using human Rad51 Rad52 and RPA proteins
    • McIlwraith, M. J., E. Van Dyck, J. Y. Masson, A. Z. Stasiak, A. Stasiak, and S. C. West. 2000. Reconstitution of the strand invasion step of double-strand break repair using human Rad51 Rad52 and RPA proteins. J Mol Biol. 304:151-64.
    • (2000) J Mol Biol. , vol.304 , pp. 151-164
    • McIlwraith, M.J.1    Van Dyck, E.2    Masson, J.Y.3    Stasiak, A.Z.4    Stasiak, A.5    West, S.C.6
  • 68
    • 0034721654 scopus 로고    scopus 로고
    • Structural basis for the recognition of DNA repair proteins UNG2, XPA, and RAD52 by replication factor RPA
    • Mer, G., A. Bochkarev, R. Gupta, E. Bochkareva, L. Frappier, C. J. Ingles, A. M. Edwards, and W. J. Chazin. 2000. Structural basis for the recognition of DNA repair proteins UNG2, XPA, and RAD52 by replication factor RPA. Cell. 103:449-56.
    • (2000) Cell. , vol.103 , pp. 449-456
    • Mer, G.1    Bochkarev, A.2    Gupta, R.3    Bochkareva, E.4    Frappier, L.5    Ingles, C.J.6    Edwards, A.M.7    Chazin, W.J.8
  • 69
    • 34147224324 scopus 로고
    • The single-stranded DNA-binding protein of Escherichia coli
    • Meyer, R. R., and P. S. Laine. 1990. The single-stranded DNA-binding protein of Escherichia coli. Microbiol Rev. 54:342-80.
    • (1990) Microbiol Rev. , vol.54 , pp. 342-380
    • Meyer, R.R.1    Laine, P.S.2
  • 72
    • 0027227980 scopus 로고
    • Dominant negative alleles of RAD52 reveal a DNA repair/recombination complex including Rad51 and Rad52
    • Milne, G. T., and D. T. Weaver. 1993. Dominant negative alleles of RAD52 reveal a DNA repair/recombination complex including Rad51 and Rad52. Genes Dev. 7:1755-65.
    • (1993) Genes Dev. , vol.7 , pp. 1755-1765
    • Milne, G.T.1    Weaver, D.T.2
  • 73
    • 0016296093 scopus 로고
    • Properties of the Escherichia coli in DNA binding (unwinding) protein: Interaction with DNA polymerase and DNA
    • Molineux, I. J., and M. L. Gefter. 1974. Properties of the Escherichia coli in DNA binding (unwinding) protein: interaction with DNA polymerase and DNA. Proc Natl Acad Sci USA. 71:3858-62.
    • (1974) Proc Natl Acad Sci USA , vol.71 , pp. 3858-3862
    • Molineux, I.J.1    Gefter, M.L.2
  • 74
    • 33646777679 scopus 로고    scopus 로고
    • Rapid activation of ATR by ionizing radiation requires ATM and Mre11
    • Myers, J. S., and D. Cortez. 2006. Rapid activation of ATR by ionizing radiation requires ATM and Mre11. J Biol Chem. 281:9346-50.
    • (2006) J Biol Chem. , vol.281 , pp. 9346-9350
    • Myers, J.S.1    Cortez, D.2
  • 75
    • 31444452984 scopus 로고    scopus 로고
    • ATRIP associates with replication protein A-coated ssDNA through multiple interactions
    • Namiki, Y., and L. Zou. 2006. ATRIP associates with replication protein A-coated ssDNA through multiple interactions. Proc Natl Acad Sci USA. 103:580-5.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 580-585
    • Namiki, Y.1    Zou, L.2
  • 76
    • 0030924695 scopus 로고    scopus 로고
    • Mapping of amino acid residues in the p34 subunit of human single-stranded DNA-binding protein phosphorylated by DNA-dependent protein kinase and Cdc2 kinase in vitro
    • Niu, H., H. Erdjument-Bromage, Z. Q. Pan, S. H. Lee, P. Tempst, and J. Hurwitz. 1997. Mapping of amino acid residues in the p34 subunit of human single-stranded DNA-binding protein phosphorylated by DNA-dependent protein kinase and Cdc2 kinase in vitro. J Biol Chem. 272:12634-41.
    • (1997) J Biol Chem. , vol.272 , pp. 12634-12641
    • Niu, H.1    Erdjument-Bromage, H.2    Pan, Z.Q.3    Lee, S.H.4    Tempst, P.5    Hurwitz, J.6
  • 77
    • 20444375871 scopus 로고    scopus 로고
    • DNA damage induced hyperphosphorylation of replication protein A 1. Identification of novel sites of phosphorylation in response to DNA damage
    • Nuss, J. E., S. M. Patrick, G. G. Oakley, G. M. Alter, J. G. Robison, K. Dixon, and J. J. Turchi. 2005. DNA damage induced hyperphosphorylation of replication protein A. 1. Identification of novel sites of phosphorylation in response to DNA damage. Biochemistry. 44:8428-37.
    • (2005) Biochemistry. , vol.44 , pp. 8428-8437
    • Nuss, J.E.1    Patrick, S.M.2    Oakley, G.G.3    Alter, G.M.4    Robison, J.G.5    Dixon, K.6    Turchi, J.J.7
  • 78
    • 0242417571 scopus 로고    scopus 로고
    • RPA phosphorylation in mitosis alters DNA binding and protein-protein interactions
    • Oakley, G. G., S. M. Patrick, J. Yao, M. P. Carty, J. J. Turchi, and K. Dixon. 2003. RPA phosphorylation in mitosis alters DNA binding and protein-protein interactions. Biochemistry. 42:3255-64.
    • (2003) Biochemistry. , vol.42 , pp. 3255-3264
    • Oakley, G.G.1    Patrick, S.M.2    Yao, J.3    Carty, M.P.4    Turchi, J.J.5    Dixon, K.6
  • 79
    • 0028016304 scopus 로고
    • Phosphorylation of the p34 subunit of human single-stranded-DNA-binding protein in cyclin A-activated G1 extracts is catalyzed by cdk-cyclin A complex and DNA-dependent protein kinase
    • Pan, Z. Q., A. A. Amin, E. Gibbs, H. Niu, and J. Hurwitz. 1994. Phosphorylation of the p34 subunit of human single-stranded-DNA-binding protein in cyclin A-activated G1 extracts is catalyzed by cdk-cyclin A complex and DNA-dependent protein kinase. Proc Natl Acad Sci USA. 91:8343-7.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 8343-8347
    • Pan, Z.Q.1    Amin, A.A.2    Gibbs, E.3    Niu, H.4    Hurwitz, J.5
  • 80
    • 0029074504 scopus 로고
    • Phosphorylated and unphosphorylated forms of human single-stranded DNA-binding protein are equally active in simian virus 40 DNA replication and in nucleotide excision repair
    • Pan, Z. Q., C. H. Park, A. A. Amin, J. Hurwitz, and A. Sancar. 1995. Phosphorylated and unphosphorylated forms of human single-stranded DNA-binding protein are equally active in simian virus 40 DNA replication and in nucleotide excision repair. Proc Natl Acad Sci USA. 92:4636-40.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 4636-4640
    • Pan, Z.Q.1    Park, C.H.2    Amin, A.A.3    Hurwitz, J.4    Sancar, A.5
  • 81
    • 0038799991 scopus 로고    scopus 로고
    • Multiple pathways of recombination induced by doublestrand breaks in Saccharomyces cerevisiae
    • Paques, F., and J. E. Haber. 1999. Multiple pathways of recombination induced by doublestrand breaks in Saccharomyces cerevisiae. Microbiol Mol Biol Rev. 63:349-404.
    • (1999) Microbiol Mol Biol Rev. , vol.63 , pp. 349-404
    • Paques, F.1    Haber, J.E.2
  • 82
    • 0032870929 scopus 로고    scopus 로고
    • Zinc finger of replication protein A, a non-DNA binding element, regulates its DNA binding activity through redox
    • Park, J. S., M. Wang, S. J. Park, and S. H. Lee. 1999. Zinc finger of replication protein A, a non-DNA binding element, regulates its DNA binding activity through redox. J Biol Chem. 274:29075-80.
    • (1999) J Biol Chem. , vol.274 , pp. 29075-29080
    • Park, J.S.1    Wang, M.2    Park, S.J.3    Lee, S.H.4
  • 83
    • 0242413125 scopus 로고    scopus 로고
    • Cut5 is required for the binding of Atr and DNA polymerase alpha to genotoxin-damaged chromatin
    • Parrilla-Castellar, E. R., and L. M. Karnitz. 2003. Cut5 is required for the binding of Atr and DNA polymerase alpha to genotoxin-damaged chromatin. J Biol Chem. 278:45507-11.
    • (2003) J Biol Chem. , vol.278 , pp. 45507-45511
    • Parrilla-Castellar, E.R.1    Karnitz, L.M.2
  • 84
    • 20444392406 scopus 로고    scopus 로고
    • DNA damage induced hyperphosphorylation of replication protein A. 2. Characterization of DNA binding activity, protein interactions, and activity in DNA replication and repair
    • Patrick, S. M., G. G. Oakley, K. Dixon, and J. J. Turchi. 2005. DNA damage induced hyperphosphorylation of replication protein A. 2. Characterization of DNA binding activity, protein interactions, and activity in DNA replication and repair. Biochemistry. 44: 8438-48.
    • (2005) Biochemistry. , vol.44 , pp. 8438-8448
    • Patrick, S.M.1    Oakley, G.G.2    Dixon, K.3    Turchi, J.J.4
  • 85
    • 3042829478 scopus 로고    scopus 로고
    • Human replication protein A (RPA) binds a primer-template junction in the absence of its major ssDNA-binding domains
    • Pestryakov, P. E., D. Y. Khlimankov, E. Bochkareva, A. Bochkarev, and O. I. Lavrik. 2004. Human replication protein A (RPA) binds a primer-template junction in the absence of its major ssDNA-binding domains. Nucleic Acids Res. 32:1894-903.
    • (2004) Nucleic Acids Res. , vol.32 , pp. 1894-1903
    • Pestryakov, P.E.1    Khlimankov, D.Y.2    Bochkareva, E.3    Bochkarev, A.4    Lavrik, O.I.5
  • 86
    • 0033887437 scopus 로고    scopus 로고
    • Structure of the DNA binding domain of E. coli SSB bound to ssDNA
    • Raghunathan, S., A. G. Kozlov, T. M. Lohman, and G. Waksman. 2000. Structure of the DNA binding domain of E. coli SSB bound to ssDNA. Nat Struct Biol. 7:648-52.
    • (2000) Nat Struct Biol. , vol.7 , pp. 648-652
    • Raghunathan, S.1    Kozlov, A.G.2    Lohman, T.M.3    Waksman, G.4
  • 87
    • 0031009811 scopus 로고    scopus 로고
    • Crystal structure of the homo-tetrameric DNA binding domain of Escherichia coli single-stranded DNA-binding protein determined by multiwavelength x-ray diffraction on the selenomethionyl protein at 2. 9-A resolution
    • Raghunathan, S., C. S. Ricard, T. M. Lohman, and G. Waksman. 1997. Crystal structure of the homo-tetrameric DNA binding domain of Escherichia coli single-stranded DNA-binding protein determined by multiwavelength x-ray diffraction on the selenomethionyl protein at 2. 9-A resolution. Proc Natl Acad Sci USA. 94:6652-7.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 6652-6657
    • Raghunathan, S.1    Ricard, C.S.2    Lohman, T.M.3    Waksman, G.4
  • 89
    • 4544339736 scopus 로고    scopus 로고
    • Replication protein A and the Mre11. Rad50. Nbs1 complex co-localize and interact at sites of stalled replication forks
    • Robison, J. G., J. Elliott, K. Dixon, and G. G. Oakley. 2004. Replication protein A and the Mre11. Rad50. Nbs1 complex co-localize and interact at sites of stalled replication forks. J Biol Chem. 279:34802-10.
    • (2004) J Biol Chem. , vol.279 , pp. 34802-34810
    • Robison, J.G.1    Elliott, J.2    Dixon, K.3    Oakley, G.G.4
  • 90
    • 0042632901 scopus 로고    scopus 로고
    • Pathways of DNA doublestrand break repair during the mammalian cell cycle
    • Rothkamm, K., I. Kruger, L. H. Thompson, andM. Lobrich. 2003. Pathways of DNA doublestrand break repair during the mammalian cell cycle. Mol Cell Biol. 23:5706-15.
    • (2003) Mol Cell Biol. , vol.23 , pp. 5706-5715
    • Rothkamm, K.1    Kruger, I.2    Thompson, L.H.3    Lobrich, M.4
  • 91
    • 0021742268 scopus 로고
    • The minimum amount of homology required for homologous recombination in mammalian cells
    • Rubnitz, J., and S. Subramani. 1984. The minimum amount of homology required for homologous recombination in mammalian cells. Mol Cell Biol. 4:2253-8.
    • (1984) Mol Cell Biol. , vol.4 , pp. 2253-2258
    • Rubnitz, J.1    Subramani, S.2
  • 92
    • 33645789832 scopus 로고    scopus 로고
    • Differential involvement of phosphatidylinositol 3-kinase-related protein kinases in hyperphosphorylation of replication protein A2 in response to replication-mediated DNA double-strand breaks
    • Sakasai, R., K. Shinohe, Y. Ichijima, N. Okita, A. Shibata, K. Asahina, and H. Teraoka. 2006. Differential involvement of phosphatidylinositol 3-kinase-related protein kinases in hyperphosphorylation of replication protein A2 in response to replication-mediated DNA double-strand breaks. Genes Cells. 11:237-46.
    • (2006) Genes Cells , vol.11 , pp. 237-246
    • Sakasai, R.1    Shinohe, K.2    Ichijima, Y.3    Okita, N.4    Shibata, A.5    Asahina, K.6    Teraoka, H.7
  • 94
    • 0030047343 scopus 로고    scopus 로고
    • Specific interactions between the human RAD51 and RAD52 proteins
    • Shen, Z., K. G. Cloud, D. J. Chen, and M. S. Park. 1996. Specific interactions between the human RAD51 and RAD52 proteins. J Biol Chem. 271:148-52.
    • (1996) J Biol Chem. , vol.271 , pp. 148-152
    • Shen, Z.1    Cloud, K.G.2    Chen, D.J.3    Park, M.S.4
  • 95
    • 34547121734 scopus 로고    scopus 로고
    • A central role for SSB in Escherichia coli RecQ DNA helicase function
    • Shereda, R. D., D. A. Bernstein, and J. L. Keck. 2007. A central role for SSB in Escherichia coli RecQ DNA helicase function. J Biol Chem. 282:19247-58.
    • (2007) J Biol Chem. , vol.282 , pp. 19247-19258
    • Shereda, R.D.1    Bernstein, D.A.2    Keck, J.L.3
  • 97
    • 0035893241 scopus 로고    scopus 로고
    • Mediator function of the human Rad51B-Rad51C complex in Rad51/RPA-catalyzed DNA strand exchange
    • Sigurdsson, S., S. Van Komen, W. Bussen, D. Schild, J. S. Albala, and P. Sung. 2001. Mediator function of the human Rad51B-Rad51C complex in Rad51/RPA-catalyzed DNA strand exchange. Genes Dev. 15:3308-18.
    • (2001) Genes Dev. , vol.15 , pp. 3308-3318
    • Sigurdsson, S.1    Van Komen, S.2    Bussen, W.3    Schild, D.4    Albala, J.S.5    Sung, P.6
  • 98
    • 33847306350 scopus 로고    scopus 로고
    • Characterization of the ATPase activity of the Escherichia coli RecG protein reveals that the preferred cofactor is negatively supercoiled DNA
    • Slocum, S. L., J. A. Buss, Y. Kimura, and P. R. Bianco. 2007. Characterization of the ATPase activity of the Escherichia coli RecG protein reveals that the preferred cofactor is negatively supercoiled DNA. J Mol Biol. 367:647-64.
    • (2007) J Mol Biol. , vol.367 , pp. 647-664
    • Slocum, S.L.1    Buss, J.A.2    Kimura, Y.3    Bianco, P.R.4
  • 99
    • 0034717199 scopus 로고    scopus 로고
    • Functional interactions among yeast Rad51 recombinase, Rad52 mediator, and replication protein A in DNA strand exchange
    • Song, B., and P. Sung. 2000. Functional interactions among yeast Rad51 recombinase, Rad52 mediator, and replication protein A in DNA strand exchange. J Biol Chem. 275:15895-904.
    • (2000) J Biol Chem. , vol.275 , pp. 15895-15904
    • Song, B.1    Sung, P.2
  • 100
    • 33747889217 scopus 로고    scopus 로고
    • Differential usage of non-homologous end-joining and homologous recombination in double strand break repair
    • Sonoda, E., H. Hochegger, A. Saberi, Y. Taniguchi, and S. Takeda. 2006. Differential usage of non-homologous end-joining and homologous recombination in double strand break repair. DNA Repair (Amst). 5:1021-9.
    • (2006) DNA Repair (Amst) , vol.5 , pp. 1021-1029
    • Sonoda, E.1    Hochegger, H.2    Saberi, A.3    Taniguchi, Y.4    Takeda, S.5
  • 101
    • 2942532181 scopus 로고    scopus 로고
    • Physical interaction between replication protein A and Rad51 promotes exchange on single-stranded DNA
    • Stauffer, M. E., and W. J. Chazin. 2004. Physical interaction between replication protein A and Rad51 promotes exchange on single-stranded DNA. J Biol Chem. 279:25638-45.
    • (2004) J Biol Chem. , vol.279 , pp. 25638-25645
    • Stauffer, M.E.1    Chazin, W.J.2
  • 102
    • 3242891189 scopus 로고    scopus 로고
    • The Mre11 complex and the metabolism of chromosome breaks: The importance of communicating and holding things together
    • Stracker, T. H., J. W. Theunissen, M. Morales, and J. H. Petrini. 2004. The Mre11 complex and the metabolism of chromosome breaks: the importance of communicating and holding things together. DNA Repair (Amst). 3:845-54.
    • (2004) DNA Repair (Amst) , vol.3 , pp. 845-854
    • Stracker, T.H.1    Theunissen, J.W.2    Morales, M.3    Petrini, J.H.4
  • 103
    • 0037199924 scopus 로고    scopus 로고
    • Rad52 protein associates with replication protein A (RPA)-single-stranded DNA to accelerate Rad51-mediated displacement of RPA and presynaptic complex formation
    • Sugiyama, T., and S. C. Kowalczykowski. 2002. Rad52 protein associates with replication protein A (RPA)-single-stranded DNA to accelerate Rad51-mediated displacement of RPA and presynaptic complex formation. J Biol Chem. 277:31663-72.
    • (2002) J Biol Chem. , vol.277 , pp. 31663-31672
    • Sugiyama, T.1    Kowalczykowski, S.C.2
  • 104
    • 0031004885 scopus 로고    scopus 로고
    • A single-stranded DNAbinding protein is needed for efficient presynaptic complex formation by the Saccharomyces cerevisiae Rad51 protein
    • Sugiyama, T., E. M. Zaitseva, and S. C. Kowalczykowski. 1997. A single-stranded DNAbinding protein is needed for efficient presynaptic complex formation by the Saccharomyces cerevisiae Rad51 protein. J Biol Chem. 272:7940-5.
    • (1997) J Biol Chem. , vol.272 , pp. 7940-7945
    • Sugiyama, T.1    Zaitseva, E.M.2    Kowalczykowski, S.C.3
  • 105
    • 0030666945 scopus 로고    scopus 로고
    • Function of yeast Rad52 protein as a mediator between replication protein A and the Rad51 recombinase
    • Sung, P. 1997. Function of yeast Rad52 protein as a mediator between replication protein A and the Rad51 recombinase. J Biol Chem. 272:28194-7.
    • (1997) J Biol Chem. , vol.272 , pp. 28194-28197
    • Sung, P.1
  • 106
    • 0030995362 scopus 로고    scopus 로고
    • Yeast Rad55 and Rad57 proteins form a heterodimer that functions with replication protein A to promote DNA strand exchange by Rad51 recombinase
    • Sung, P. 1997. Yeast Rad55 and Rad57 proteins form a heterodimer that functions with replication protein A to promote DNA strand exchange by Rad51 recombinase. Genes Dev. 11:1111-21.
    • (1997) Genes Dev. , vol.11 , pp. 1111-1121
    • Sung, P.1
  • 107
    • 0036900120 scopus 로고    scopus 로고
    • Role of RAD52 epistasis group genes in homologous recombination and double-strand break repair
    • table of contents
    • Symington, L. S. 2002. Role of RAD52 epistasis group genes in homologous recombination and double-strand break repair. Microbiol Mol Biol Rev. 66:630-70, table of contents.
    • (2002) Microbiol Mol Biol Rev , vol.66 , pp. 630-670
    • Symington, L.S.1
  • 108
    • 0032530658 scopus 로고    scopus 로고
    • Homologous recombination and non-homologous end-joining pathways of DNA double-strand break repair have overlapping roles in the maintenance of chromosomal integrity in vertebrate cells
    • Takata, M., M. S. Sasaki, E. Sonoda, C. Morrison, M. Hashimoto, H. Utsumi, Y. Yamaguchi- Iwai, A. Shinohara, and S. Takeda. 1998. Homologous recombination and non-homologous end-joining pathways of DNA double-strand break repair have overlapping roles in the maintenance of chromosomal integrity in vertebrate cells. Embo J. 17:5497-508.
    • (1998) Embo J. , vol.17 , pp. 5497-5508
    • Takata, M.1    Sasaki, M.S.2    Sonoda, E.3    Morrison, C.4    Hashimoto, M.5    Utsumi, H.6    Yamaguchi-Iwai, Y.7    Shinohara, A.8    Takeda, S.9
  • 109
    • 0027238208 scopus 로고
    • Biochemical interaction of the Escherichia coli RecF, RecO, and RecR proteins with RecA protein and single-stranded DNA binding protein
    • Umezu, K., N. W. Chi, and R. D. Kolodner. 1993. Biochemical interaction of the Escherichia coli RecF, RecO, and RecR proteins with RecA protein and single-stranded DNA binding protein. Proc Natl Acad Sci USA. 90:3875-9.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 3875-3879
    • Umezu, K.1    Chi, N.W.2    Kolodner, R.D.3
  • 110
    • 1342325347 scopus 로고    scopus 로고
    • Replication protein A (RPA) phosphorylation prevents RPA association with replication centers
    • Vassin, V. M., M. S. Wold, and J. A. Borowiec. 2004. Replication protein A (RPA) phosphorylation prevents RPA association with replication centers. Mol Cell Biol. 24:1930-43.
    • (2004) Mol Cell Biol. , vol.24 , pp. 1930-1943
    • Vassin, V.M.1    Wold, M.S.2    Borowiec, J.A.3
  • 112
    • 0033618278 scopus 로고    scopus 로고
    • Roles of replication protein A and DNA-dependent protein kinase in the regulation of DNA replication following DNA damage
    • Wang, Y., X. Y. Zhou, H. Wang, M. S. Huq, and G. Iliakis. 1999. Roles of replication protein A and DNA-dependent protein kinase in the regulation of DNA replication following DNA damage. J Biol Chem. 274:22060-4.
    • (1999) J Biol Chem. , vol.274 , pp. 22060-22064
    • Wang, Y.1    Zhou, X.Y.2    Wang, H.3    Huq, M.S.4    Iliakis, G.5
  • 113
    • 0043163774 scopus 로고    scopus 로고
    • DNA polymerase III chi subunit ties singlestranded DNA binding protein to the bacterial replication machinery
    • Witte, G., C. Urbanke, and U. Curth. 2003. DNA polymerase III chi subunit ties singlestranded DNA binding protein to the bacterial replication machinery. Nucleic Acids Res. 31:4434-40.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 4434-4440
    • Witte, G.1    Urbanke, C.2    Curth, U.3
  • 115
    • 0024537212 scopus 로고
    • Identification of cellular proteins required for simian virus 40 DNA replication
    • Wold, M. S., D. H. Weinberg, D. M. Virshup, J. J. Li, and T. J. Kelly. 1989. Identification of cellular proteins required for simian virus 40 DNA replication. J Biol Chem. 264:2801-9.
    • (1989) J Biol Chem. , vol.264 , pp. 2801-2809
    • Wold, M.S.1    Weinberg, D.H.2    Virshup, D.M.3    Li, J.J.4    Kelly, T.J.5
  • 116
    • 0023992803 scopus 로고
    • Purification and characterization of replication protein A, a cellular protein required for in vitro replication of simian virus 40 DNA
    • Wold, M. S., and T. Kelly. 1988. Purification and characterization of replication protein A, a cellular protein required for in vitro replication of simian virus 40 DNA. Proc Natl Acad Sci USA. 85:2523-7.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 2523-2527
    • Wold, M.S.1    Kelly, T.2
  • 117
    • 0031466027 scopus 로고    scopus 로고
    • RAD51 interacts with the evolutionarily conserved BRC motifs in the human breast cancer susceptibility gene brca2
    • Wong, A. K., R. Pero, P. A. Ormonde, S. V. Tavtigian, and P. L. Bartel. 1997. RAD51 interacts with the evolutionarily conserved BRC motifs in the human breast cancer susceptibility gene brca2. J Biol Chem. 272:31941-4.
    • (1997) J Biol Chem. , vol.272 , pp. 31941-31944
    • Wong, A.K.1    Pero, R.2    Ormonde, P.A.3    Tavtigian, S.V.4    Bartel, P.L.5
  • 118
    • 0037427075 scopus 로고    scopus 로고
    • Interaction between BRCA2 and replication protein A is compromised by a cancer-predisposing mutation in BRCA2
    • Wong, J. M., D. Ionescu, and C. J. Ingles. 2003. Interaction between BRCA2 and replication protein A is compromised by a cancer-predisposing mutation in BRCA2. Oncogene. 22: 28-33.
    • (2003) Oncogene. , vol.22 , pp. 28-33
    • Wong, J.M.1    Ionescu, D.2    Ingles, C.J.3
  • 119
    • 27744588177 scopus 로고    scopus 로고
    • Preferential localization of hyperphosphorylated replication protein A to double-strand break repair and checkpoint complexes upon DNA damage
    • Wu, X., Z. Yang, Y. Liu, and Y. Zou. 2005. Preferential localization of hyperphosphorylated replication protein A to double-strand break repair and checkpoint complexes upon DNA damage. Biochem J. 391:473-80.
    • (2005) Biochem J. , vol.391 , pp. 473-480
    • Wu, X.1    Yang, Z.2    Liu, Y.3    Zou, Y.4
  • 120
    • 0242507460 scopus 로고    scopus 로고
    • Replication protein A interactions with DNA: Differential binding of the core domains and analysis of the DNA interaction surface
    • Wyka, I. M., K. Dhar, S. K. Binz, and M. S. Wold. 2003. Replication protein A interactions with DNA: differential binding of the core domains and analysis of the DNA interaction surface. Biochemistry. 42:12909-18.
    • (2003) Biochemistry. , vol.42 , pp. 12909-12918
    • Wyka, I.M.1    Dhar, K.2    Binz, S.K.3    Wold, M.S.4
  • 122
    • 24644507171 scopus 로고    scopus 로고
    • 53BP1 is associated with replication protein A and is required for RPA2 hyperphosphorylation following DNA damage
    • Yoo, E., B. U. Kim, S. Y. Lee, C. H. Cho, J. H. Chung, and C. H. Lee. 2005. 53BP1 is associated with replication protein A and is required for RPA2 hyperphosphorylation following DNA damage. Oncogene. 24:5423-30.
    • (2005) Oncogene. , vol.24 , pp. 5423-5430
    • Yoo, E.1    Kim, B.U.2    Lee, S.Y.3    Cho, C.H.4    Chung, J.H.5    Lee, C.H.6
  • 123
    • 0033179235 scopus 로고    scopus 로고
    • BRCA2 is required for ionizing radiation-induced assembly of Rad51 complex in vivo
    • Yuan, S. S., S. Y. Lee, G. Chen, M. Song, G. E. Tomlinson, and E. Y. Lee. 1999. BRCA2 is required for ionizing radiation-induced assembly of Rad51 complex in vivo. Cancer Res. 59:3547-51.
    • (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
  • 124
    • 0033534380 scopus 로고    scopus 로고
    • Trading places on DNA - A threepoint switch underlies primer handoff from primase to the replicative DNA polymerase
    • Yuzhakov, A., Z. Kelman, and M. O'Donnell. 1999. Trading places on DNA - a threepoint switch underlies primer handoff from primase to the replicative DNA polymerase. Cell. 96:153-63.
    • (1999) Cell. , vol.96 , pp. 153-163
    • Yuzhakov, A.1    Kelman, Z.2    O'donnell, M.3
  • 125
    • 0030810633 scopus 로고    scopus 로고
    • Sites of UV-induced phosphorylation of the p34 subunit of replication protein A from HeLa cells
    • Zernik-Kobak, M., K. Vasunia, M. Connelly, C. W. Anderson, and K. Dixon. 1997. Sites of UV-induced phosphorylation of the p34 subunit of replication protein A from HeLa cells. J Biol Chem. 272:23896-904.
    • (1997) J Biol Chem. , vol.272 , pp. 23896-23904
    • Zernik-Kobak, M.1    Vasunia, K.2    Connelly, M.3    Anderson, C.W.4    Dixon, K.5
  • 126
    • 0037567268 scopus 로고    scopus 로고
    • Sensing DNA damage through ATRIP recognition of RPAssDNA complexes
    • Zou, L., and S. J. Elledge. 2003. Sensing DNA damage through ATRIP recognition of RPAssDNA complexes. Science. 300:1542-8.
    • (2003) Science. , vol.300 , pp. 1542-1548
    • Zou, L.1    Elledge, S.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.