메뉴 건너뛰기




Volumn 29, Issue , 2015, Pages 74-82

Redundancy in ribonucleotide excision repair: Competition, compensation, and cooperation

Author keywords

DNA polymerase I; Flap endonuclease; Mismatch repair; Nucleotide excision repair; Ribonuclease H; Ribonucleotide excision repair

Indexed keywords

ESCHERICHIA COLI PROTEIN; FUNGAL DNA; RIBONUCLEASE H; RIBONUCLEOTIDE; SACCHAROMYCES CEREVISIAE PROTEIN;

EID: 84939993041     PISSN: 15687864     EISSN: 15687856     Source Type: Journal    
DOI: 10.1016/j.dnarep.2015.02.008     Document Type: Article
Times cited : (23)

References (63)
  • 2
    • 79951620951 scopus 로고    scopus 로고
    • Unlocking the sugar steric gate of DNA polymerases
    • Brown J.A., Suo Z. Unlocking the sugar steric gate of DNA polymerases. Biochemistry 2011, 50:1135-1142.
    • (2011) Biochemistry , vol.50 , pp. 1135-1142
    • Brown, J.A.1    Suo, Z.2
  • 3
    • 84939952005 scopus 로고    scopus 로고
    • Ribonucleotide selectivity of translesion synthesis DNA polymerases
    • Research Signpost, Kerala, India
    • Vaisman A., Woodgate R. Ribonucleotide selectivity of translesion synthesis DNA polymerases. Function of Translesion DNA polymerases in Genome Stability 2015, 1-23. Research Signpost, Kerala, India, ISBN: 978-81-308-0538-2.
    • (2015) Function of Translesion DNA polymerases in Genome Stability , pp. 1-23
    • Vaisman, A.1    Woodgate, R.2
  • 4
    • 84902074659 scopus 로고    scopus 로고
    • Ribonucleotides in DNA: origins, repair and consequences
    • Williams J.S., Kunkel T.A. Ribonucleotides in DNA: origins, repair and consequences. DNA Repair 2014, 19:27-37.
    • (2014) DNA Repair , vol.19 , pp. 27-37
    • Williams, J.S.1    Kunkel, T.A.2
  • 5
    • 84872485372 scopus 로고    scopus 로고
    • Ribonucleotide incorporation, proofreading and bypass by human DNA polymerase δ
    • Clausen A.R., Zhang S., Burgers P.M., Lee M.Y., Kunkel T.A. Ribonucleotide incorporation, proofreading and bypass by human DNA polymerase δ. DNA Repair 2013, 12:121-127.
    • (2013) DNA Repair , vol.12 , pp. 121-127
    • Clausen, A.R.1    Zhang, S.2    Burgers, P.M.3    Lee, M.Y.4    Kunkel, T.A.5
  • 6
    • 84871125561 scopus 로고    scopus 로고
    • Human DNA polymerase e{open} is able to efficiently extend from multiple consecutive ribonucleotides
    • Goksenin A.Y., Zahurancik W., LeCompte K.G., Taggart D.J., Suo Z., Pursell Z.F. Human DNA polymerase e{open} is able to efficiently extend from multiple consecutive ribonucleotides. J. Biol. Chem. 2012, 287:42675-42684.
    • (2012) J. Biol. Chem. , vol.287 , pp. 42675-42684
    • Goksenin, A.Y.1    Zahurancik, W.2    LeCompte, K.G.3    Taggart, D.J.4    Suo, Z.5    Pursell, Z.F.6
  • 7
    • 0031042722 scopus 로고    scopus 로고
    • Choosing the right sugar: how polymerases select a nucleotide substrate
    • Joyce C.M. Choosing the right sugar: how polymerases select a nucleotide substrate. Proc. Natl. Acad. Sci. U. S. A. 1997, 94:1619-1622.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 1619-1622
    • Joyce, C.M.1
  • 9
    • 0037379215 scopus 로고    scopus 로고
    • Polymerase μ is a DNA-directed DNA/RNA polymerase
    • Nick McElhinny S.A., Ramsden D.A. Polymerase μ is a DNA-directed DNA/RNA polymerase. Mol. Cell. Biol. 2003, 23:2309-2315.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 2309-2315
    • Nick McElhinny, S.A.1    Ramsden, D.A.2
  • 12
    • 84887156806 scopus 로고    scopus 로고
    • Ribonucleotides are signals for mismatch repair of leading-strand replication errors
    • Lujan S.A., Williams J.S., Clausen A.R., Clark A.B., Kunkel T.A. Ribonucleotides are signals for mismatch repair of leading-strand replication errors. Mol. Cell 2013, 50:437-443.
    • (2013) Mol. Cell , vol.50 , pp. 437-443
    • Lujan, S.A.1    Williams, J.S.2    Clausen, A.R.3    Clark, A.B.4    Kunkel, T.A.5
  • 13
    • 77955297664 scopus 로고    scopus 로고
    • DNA polymerase β ribonucleotide discrimination: insertion, misinsertion, extension, and coding
    • Cavanaugh N.A., Beard W.A., Wilson S.H. DNA polymerase β ribonucleotide discrimination: insertion, misinsertion, extension, and coding. J. Biol. Chem. 2010, 285:24457-24465.
    • (2010) J. Biol. Chem. , vol.285 , pp. 24457-24465
    • Cavanaugh, N.A.1    Beard, W.A.2    Wilson, S.H.3
  • 15
    • 84869080625 scopus 로고    scopus 로고
    • Causes and consequences of ribonucleotide incorporation into nuclear DNA
    • Dalgaard J.Z. Causes and consequences of ribonucleotide incorporation into nuclear DNA. Trends Genet. 2012, 28:592-597.
    • (2012) Trends Genet. , vol.28 , pp. 592-597
    • Dalgaard, J.Z.1
  • 16
    • 84921329939 scopus 로고    scopus 로고
    • How the misincorporation of ribonucleotides into genomic DNA can be both harmful and helpful to cells
    • Potenski C.J., Klein H.L. How the misincorporation of ribonucleotides into genomic DNA can be both harmful and helpful to cells. Nucleic Acids Res. 2014, 42:10226-10234.
    • (2014) Nucleic Acids Res. , vol.42 , pp. 10226-10234
    • Potenski, C.J.1    Klein, H.L.2
  • 18
    • 79953743966 scopus 로고    scopus 로고
    • Identification of a novel type of spacer element required for imprinting in fission yeast
    • Sayrac S., Vengrova S., Godfrey E.L., Dalgaard J.Z. Identification of a novel type of spacer element required for imprinting in fission yeast. PLoS Genet. 2011, 7:e1001328.
    • (2011) PLoS Genet. , vol.7 , pp. e1001328
    • Sayrac, S.1    Vengrova, S.2    Godfrey, E.L.3    Dalgaard, J.Z.4
  • 19
    • 0027278557 scopus 로고
    • Instability and decay of the primary structure of DNA
    • Lindahl T. Instability and decay of the primary structure of DNA. Nature 1993, 362:709-715.
    • (1993) Nature , vol.362 , pp. 709-715
    • Lindahl, T.1
  • 20
    • 0034326316 scopus 로고    scopus 로고
    • B-form to A-form conversion by a 3'-terminal ribose: crystal structure of the chimera d(CCACTAGTG)r(G)
    • Wahl M.C., Sundaralingam M. B-form to A-form conversion by a 3'-terminal ribose: crystal structure of the chimera d(CCACTAGTG)r(G). Nucleic Acids Res. 2000, 28:4356-4363.
    • (2000) Nucleic Acids Res. , vol.28 , pp. 4356-4363
    • Wahl, M.C.1    Sundaralingam, M.2
  • 21
    • 84859201354 scopus 로고    scopus 로고
    • Solution structure of the Dickerson DNA dodecamer containing a single ribonucleotide
    • DeRose E.F., Perera L., Murray M.S., Kunkel T.A., London R.E. Solution structure of the Dickerson DNA dodecamer containing a single ribonucleotide. Biochemistry 2012, 51:2407-2416.
    • (2012) Biochemistry , vol.51 , pp. 2407-2416
    • DeRose, E.F.1    Perera, L.2    Murray, M.S.3    Kunkel, T.A.4    London, R.E.5
  • 23
    • 79955097646 scopus 로고    scopus 로고
    • Mismatch repair-independent tandem repeat sequence instability resulting from ribonucleotide incorporation by DNA polymerase e{open}
    • Clark A.B., Lujan S.A., Kissling G.E., Kunkel T.A. Mismatch repair-independent tandem repeat sequence instability resulting from ribonucleotide incorporation by DNA polymerase e{open}. DNA Repair 2011, 10:476-482.
    • (2011) DNA Repair , vol.10 , pp. 476-482
    • Clark, A.B.1    Lujan, S.A.2    Kissling, G.E.3    Kunkel, T.A.4
  • 24
    • 84864479581 scopus 로고    scopus 로고
    • Critical amino acids in Escherichia coli responsible for sugar discrimination and base-substitution fidelity
    • Vaisman A., Kuban W., McDonald J.P., Karata K., Yang W., Goodman M.F., Woodgate R. Critical amino acids in Escherichia coli responsible for sugar discrimination and base-substitution fidelity. Nucleic Acids Res. 2012, 40:6144-6157.
    • (2012) Nucleic Acids Res. , vol.40 , pp. 6144-6157
    • Vaisman, A.1    Kuban, W.2    McDonald, J.P.3    Karata, K.4    Yang, W.5    Goodman, M.F.6    Woodgate, R.7
  • 25
    • 84865090917 scopus 로고    scopus 로고
    • Escherichia coli UmuC active site mutants: effects on translesion DNA synthesis, mutagenesis and cell survival
    • Kuban W., Vaisman A., McDonald J.P., Karata K., Yang W., Goodman M.F., Woodgate R. Escherichia coli UmuC active site mutants: effects on translesion DNA synthesis, mutagenesis and cell survival. DNA Repair 2012, 11:726-732.
    • (2012) DNA Repair , vol.11 , pp. 726-732
    • Kuban, W.1    Vaisman, A.2    McDonald, J.P.3    Karata, K.4    Yang, W.5    Goodman, M.F.6    Woodgate, R.7
  • 26
    • 84870714773 scopus 로고    scopus 로고
    • Mechanisms employed by Escherichia coli to prevent ribonucleotide incorporation into genomic DNA by pol V
    • McDonald J.P., Vaisman A., Kuban W., Goodman M.F., Woodgate R. Mechanisms employed by Escherichia coli to prevent ribonucleotide incorporation into genomic DNA by pol V. PLoS Genet. 2012, 8:e1003030.
    • (2012) PLoS Genet. , vol.8 , pp. e1003030
    • McDonald, J.P.1    Vaisman, A.2    Kuban, W.3    Goodman, M.F.4    Woodgate, R.5
  • 28
    • 34250900335 scopus 로고    scopus 로고
    • Lessons from 50 years of SOS DNA-damage-induced mutagenesis
    • Schlacher K., Goodman M.F. Lessons from 50 years of SOS DNA-damage-induced mutagenesis. Nat. Rev. Mol. Cell Biol. 2007, 8:587-594.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 587-594
    • Schlacher, K.1    Goodman, M.F.2
  • 29
    • 84887143167 scopus 로고    scopus 로고
    • Translesion DNA synthesis and mutagenesis in prokaryotes
    • Fuchs R.P., Fujii S. Translesion DNA synthesis and mutagenesis in prokaryotes. Cold Spring Harb. Perspect. Biol. 2013, 5:a012682.
    • (2013) Cold Spring Harb. Perspect. Biol. , vol.5 , pp. a012682
    • Fuchs, R.P.1    Fujii, S.2
  • 32
    • 0037032428 scopus 로고    scopus 로고
    • Cleavage of a DNA-RNA-DNA/DNA chimeric substrate containing a single ribonucleotide at the DNA-RNA junction with prokaryotic RNases HII
    • Haruki M., Tsunaka Y., Morikawa M., Kanaya S. Cleavage of a DNA-RNA-DNA/DNA chimeric substrate containing a single ribonucleotide at the DNA-RNA junction with prokaryotic RNases HII. FEBS Lett. 2002, 531:204-208.
    • (2002) FEBS Lett. , vol.531 , pp. 204-208
    • Haruki, M.1    Tsunaka, Y.2    Morikawa, M.3    Kanaya, S.4
  • 33
    • 78649267074 scopus 로고    scopus 로고
    • Crystal structures of RNase H2 in complex with nucleic acid reveal the mechanism of RNA-DNA junction recognition and cleavage
    • Rychlik M.P., Chon H., Cerritelli S.M., Klimek P., Crouch R.J., Nowotny M. Crystal structures of RNase H2 in complex with nucleic acid reveal the mechanism of RNA-DNA junction recognition and cleavage. Mol. Cell 2010, 40:658-670.
    • (2010) Mol. Cell , vol.40 , pp. 658-670
    • Rychlik, M.P.1    Chon, H.2    Cerritelli, S.M.3    Klimek, P.4    Crouch, R.J.5    Nowotny, M.6
  • 34
    • 79953170528 scopus 로고    scopus 로고
    • The structural and biochemical characterization of human RNase H2 complex reveals the molecular basis for substrate recognition and Aicardi-Goutieres syndrome defects
    • Figiel M., Chon H., Cerritelli S.M., Cybulska M., Crouch R.J., Nowotny M. The structural and biochemical characterization of human RNase H2 complex reveals the molecular basis for substrate recognition and Aicardi-Goutieres syndrome defects. J. Biol. Chem. 2011, 286:10540-10550.
    • (2011) J. Biol. Chem. , vol.286 , pp. 10540-10550
    • Figiel, M.1    Chon, H.2    Cerritelli, S.M.3    Cybulska, M.4    Crouch, R.J.5    Nowotny, M.6
  • 35
    • 61349102407 scopus 로고    scopus 로고
    • Ribonuclease H: the enzymes in eukaryotes
    • Cerritelli S.M., Crouch R.J. Ribonuclease H: the enzymes in eukaryotes. FEBS J. 2009, 276:1494-1505.
    • (2009) FEBS J. , vol.276 , pp. 1494-1505
    • Cerritelli, S.M.1    Crouch, R.J.2
  • 36
    • 0037168516 scopus 로고    scopus 로고
    • Excision of misincorporated ribonucleotides in DNA by RNase H (type 2) and FEN-1 in cell-free extracts
    • Rydberg B., Game J. Excision of misincorporated ribonucleotides in DNA by RNase H (type 2) and FEN-1 in cell-free extracts. Proc. Natl. Acad. Sci. U. S. A. 2002, 99:16654-16659.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 16654-16659
    • Rydberg, B.1    Game, J.2
  • 37
    • 61349178533 scopus 로고    scopus 로고
    • Ribonuclease H: molecular diversities, substrate binding domains, and catalytic mechanism of the prokaryotic enzymes
    • Tadokoro T., Kanaya S. Ribonuclease H: molecular diversities, substrate binding domains, and catalytic mechanism of the prokaryotic enzymes. FEBS J. 2009, 276:1482-1493.
    • (2009) FEBS J. , vol.276 , pp. 1482-1493
    • Tadokoro, T.1    Kanaya, S.2
  • 38
    • 84876829295 scopus 로고    scopus 로고
    • Topoisomerase 1-mediated removal of ribonucleotides from nascent leading-strand DNA
    • Williams J.S., Smith D.J., Marjavaara L., Lujan S.A., Chabes A., Kunkel T.A. Topoisomerase 1-mediated removal of ribonucleotides from nascent leading-strand DNA. Mol. Cell 2013, 49:1010-1015.
    • (2013) Mol. Cell , vol.49 , pp. 1010-1015
    • Williams, J.S.1    Smith, D.J.2    Marjavaara, L.3    Lujan, S.A.4    Chabes, A.5    Kunkel, T.A.6
  • 41
    • 84888247843 scopus 로고    scopus 로고
    • Removal of misincorporated ribonucleotides from prokaryotic genomes: an unexpected role for nucleotide excision repair
    • Vaisman A., McDonald J.P., Huston D., Kuban W., Liu L., Van Houten B., Woodgate R. Removal of misincorporated ribonucleotides from prokaryotic genomes: an unexpected role for nucleotide excision repair. PLoS Genet. 2013, e1003878.
    • (2013) PLoS Genet. , pp. e1003878
    • Vaisman, A.1    McDonald, J.P.2    Huston, D.3    Kuban, W.4    Liu, L.5    Van Houten, B.6    Woodgate, R.7
  • 42
    • 79951500316 scopus 로고    scopus 로고
    • Okazaki fragment maturation: nucleases take centre stage
    • Zheng L., Shen B. Okazaki fragment maturation: nucleases take centre stage. J. Mol. Cell Biol. 2011, 3:23-30.
    • (2011) J. Mol. Cell Biol. , vol.3 , pp. 23-30
    • Zheng, L.1    Shen, B.2
  • 43
    • 8644285427 scopus 로고    scopus 로고
    • Idling by DNA polymerase delta maintains a ligatable nick during lagging-strand DNA replication
    • Garg P., Stith C.M., Sabouri N., Johansson E., Burgers P.M. Idling by DNA polymerase delta maintains a ligatable nick during lagging-strand DNA replication. Genes Dev. 2004, 18:2764-2773.
    • (2004) Genes Dev. , vol.18 , pp. 2764-2773
    • Garg, P.1    Stith, C.M.2    Sabouri, N.3    Johansson, E.4    Burgers, P.M.5
  • 44
    • 57749100294 scopus 로고    scopus 로고
    • Flexibility of eukaryotic Okazaki fragment maturation through regulated strand displacement synthesis
    • Stith C.M., Sterling J., Resnick M.A., Gordenin D.A., Burgers P.M. Flexibility of eukaryotic Okazaki fragment maturation through regulated strand displacement synthesis. J. Biol. Chem. 2008, 283:34129-34140.
    • (2008) J. Biol. Chem. , vol.283 , pp. 34129-34140
    • Stith, C.M.1    Sterling, J.2    Resnick, M.A.3    Gordenin, D.A.4    Burgers, P.M.5
  • 45
    • 0034617275 scopus 로고    scopus 로고
    • Coordination between the polymerase and 5'-nuclease components of DNA polymerase I of Escherichia coli
    • Xu Y., Grindley N.D., Joyce C.M. Coordination between the polymerase and 5'-nuclease components of DNA polymerase I of Escherichia coli. J. Biol. Chem. 2000, 275:20949-20955.
    • (2000) J. Biol. Chem. , vol.275 , pp. 20949-20955
    • Xu, Y.1    Grindley, N.D.2    Joyce, C.M.3
  • 46
    • 0018265532 scopus 로고
    • On the processive mechanism of Escherichia coli DNA polymerase I. The polA5 mutation
    • Matson S.W., Capaldo-Kimball F.N., Bambara R.A. On the processive mechanism of Escherichia coli DNA polymerase I. The polA5 mutation. J. Biol. Chem. 1978, 253:7851-7856.
    • (1978) J. Biol. Chem. , vol.253 , pp. 7851-7856
    • Matson, S.W.1    Capaldo-Kimball, F.N.2    Bambara, R.A.3
  • 47
    • 3843114709 scopus 로고    scopus 로고
    • When pol I goes into high gear: processive DNA synthesis by pol I in the cell
    • Camps M., Loeb L.A. When pol I goes into high gear: processive DNA synthesis by pol I in the cell. Cell Cycle 2004, 3:116-118.
    • (2004) Cell Cycle , vol.3 , pp. 116-118
    • Camps, M.1    Loeb, L.A.2
  • 48
    • 0037472087 scopus 로고    scopus 로고
    • Escherichia coli uracil- and ethenocytosine-initiated base excision DNA repair: rate-limiting step and patch size distribution
    • Sung J.S., Mosbaugh D.W. Escherichia coli uracil- and ethenocytosine-initiated base excision DNA repair: rate-limiting step and patch size distribution. Biochemistry 2003, 42:4613-4625.
    • (2003) Biochemistry , vol.42 , pp. 4613-4625
    • Sung, J.S.1    Mosbaugh, D.W.2
  • 49
    • 84866562631 scopus 로고    scopus 로고
    • Reconstitution of the very short patch repair pathway from Escherichia coli
    • Robertson A.B., Matson S.W. Reconstitution of the very short patch repair pathway from Escherichia coli. J. Biol. Chem. 2012, 287:32953-32966.
    • (2012) J. Biol. Chem. , vol.287 , pp. 32953-32966
    • Robertson, A.B.1    Matson, S.W.2
  • 50
    • 84924087089 scopus 로고    scopus 로고
    • Eukaryotic replicative DNA polymerases
    • Springer-Verlag, Heidelberg, K.S. Murakami, M.A. Trakselis (Eds.)
    • Walsh E., Eckert K.A. Eukaryotic replicative DNA polymerases. Nucleic Acid Polymerases, Nucleic Acids and Molecular Biology 2014, 17-41. Springer-Verlag, Heidelberg. K.S. Murakami, M.A. Trakselis (Eds.).
    • (2014) Nucleic Acid Polymerases, Nucleic Acids and Molecular Biology , pp. 17-41
    • Walsh, E.1    Eckert, K.A.2
  • 51
    • 84855469296 scopus 로고    scopus 로고
    • Mispaired rNMPs in DNA are mutagenic and are targets of mismatch repair and RNases H
    • Shen Y., Koh K.D., Weiss B., Storici F. Mispaired rNMPs in DNA are mutagenic and are targets of mismatch repair and RNases H. Nat. Struct. Mol. Biol. 2012, 19:98-104.
    • (2012) Nat. Struct. Mol. Biol. , vol.19 , pp. 98-104
    • Shen, Y.1    Koh, K.D.2    Weiss, B.3    Storici, F.4
  • 52
    • 84891159240 scopus 로고    scopus 로고
    • Ribonucleotides as nucleotide excision repair substrates
    • Cai Y., Geacintov N.E., Broyde S. Ribonucleotides as nucleotide excision repair substrates. DNA Repair 2014, 13:55-60.
    • (2014) DNA Repair , vol.13 , pp. 55-60
    • Cai, Y.1    Geacintov, N.E.2    Broyde, S.3
  • 54
    • 84888259361 scopus 로고    scopus 로고
    • RNA:DNA hybrids initiate quasi-palindrome-associated mutations in highly transcribed yeast DNA
    • Kim N., Cho J.E., Li Y.C., Jinks-Robertson S. RNA:DNA hybrids initiate quasi-palindrome-associated mutations in highly transcribed yeast DNA. PLoS Genet. 2013, 9:e1003924.
    • (2013) PLoS Genet. , vol.9 , pp. e1003924
    • Kim, N.1    Cho, J.E.2    Li, Y.C.3    Jinks-Robertson, S.4
  • 55
    • 79959493444 scopus 로고    scopus 로고
    • Molecular biology. A new twist for topoisomerase
    • Cerritelli S.M., Chon H., Crouch R.J. Molecular biology. A new twist for topoisomerase. Science 2011, 332:1510-1511.
    • (2011) Science , vol.332 , pp. 1510-1511
    • Cerritelli, S.M.1    Chon, H.2    Crouch, R.J.3
  • 56
    • 77954841539 scopus 로고    scopus 로고
    • Loss of topoisomerase I leads to R-loop-mediated transcriptional blocks during ribosomal RNA synthesis
    • El Hage A., French S.L., Beyer A.L., Tollervey D. Loss of topoisomerase I leads to R-loop-mediated transcriptional blocks during ribosomal RNA synthesis. Genes Dev. 2010, 24:1546-1558.
    • (2010) Genes Dev. , vol.24 , pp. 1546-1558
    • El Hage, A.1    French, S.L.2    Beyer, A.L.3    Tollervey, D.4
  • 58
    • 84866462296 scopus 로고    scopus 로고
    • Mammalian RNase H2 removes ribonucleotides from DNA to maintain genome integrity
    • Hiller B., Achleitner M., Glage S., Naumann R., Behrendt R., Roers A. Mammalian RNase H2 removes ribonucleotides from DNA to maintain genome integrity. J. Exp. Med. 2012, 209:1419-1426.
    • (2012) J. Exp. Med. , vol.209 , pp. 1419-1426
    • Hiller, B.1    Achleitner, M.2    Glage, S.3    Naumann, R.4    Behrendt, R.5    Roers, A.6
  • 59
    • 0041620605 scopus 로고    scopus 로고
    • DNA polymerase β can incorporate ribonucleotides during DNA synthesis of undamaged and CPD-damaged DNA
    • Bergoglio V., Ferrari E., Hubscher U., Cazaux C., Hoffmann J.S. DNA polymerase β can incorporate ribonucleotides during DNA synthesis of undamaged and CPD-damaged DNA. J. Mol. Biol. 2003, 331:1017-1023.
    • (2003) J. Mol. Biol. , vol.331 , pp. 1017-1023
    • Bergoglio, V.1    Ferrari, E.2    Hubscher, U.3    Cazaux, C.4    Hoffmann, J.S.5
  • 60
    • 0032514636 scopus 로고    scopus 로고
    • Overexpression of DNA polymerase β in cell results in a mutator phenotype and a decreased sensitivity to anticancer drugs
    • Canitrot Y., Cazaux C., Frechet M., Bouayadi K., Lesca C., Salles B., Hoffmann J.S. Overexpression of DNA polymerase β in cell results in a mutator phenotype and a decreased sensitivity to anticancer drugs. Proc. Natl. Acad. Sci. U. S. A. 1998, 95:12586-12590.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 12586-12590
    • Canitrot, Y.1    Cazaux, C.2    Frechet, M.3    Bouayadi, K.4    Lesca, C.5    Salles, B.6    Hoffmann, J.S.7
  • 62
    • 0031028380 scopus 로고    scopus 로고
    • Conferring RNA polymerase activity to a DNA polymerase: a single residue in reverse transcriptase controls substrate selection
    • Gao G., Orlova M., Georgiadis M.M., Hendrickson W.A., Goff S.P. Conferring RNA polymerase activity to a DNA polymerase: a single residue in reverse transcriptase controls substrate selection. Proc. Natl. Acad. Sci. U. S. A. 1997, 94:407-411.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 407-411
    • Gao, G.1    Orlova, M.2    Georgiadis, M.M.3    Hendrickson, W.A.4    Goff, S.P.5
  • 63
    • 78650463005 scopus 로고    scopus 로고
    • Differential correction of lagging-strand replication errors made by DNA polymerases α and δ
    • Nick McElhinny S.A., Kissling G.E., Kunkel T.A. Differential correction of lagging-strand replication errors made by DNA polymerases α and δ. Proc. Natl. Acad. Sci. U. S. A. 2010, 107:21070-21075.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 21070-21075
    • Nick McElhinny, S.A.1    Kissling, G.E.2    Kunkel, T.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.