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Volumn 5, Issue 2, 2005, Pages 171-178

Somatic hypermutation at A•T pairs: Polymerase error versus dUTP incorporation

Author keywords

[No Author keywords available]

Indexed keywords

DEOXYURIDINE TRIPHOSPHATE PYROPHOSPHATASE; DNA DIRECTED DNA POLYMERASE ALPHA; URACIL; ADENINE; DEOXYURIDINE PHOSPHATE; DEOXYURIDINE TRIPHOSPHATE; DNA DIRECTED DNA POLYMERASE; THYMINE;

EID: 13444259474     PISSN: 14741733     EISSN: None     Source Type: Journal    
DOI: 10.1038/nri1553     Document Type: Review
Times cited : (126)

References (75)
  • 1
    • 0002225186 scopus 로고
    • A modification of Jerne's theory of antibody formation using the concept of clonal selection
    • Burnet, F. M. A modification of Jerne's theory of antibody formation using the concept of clonal selection. Aust. J. Sci. 20, 67-69 (1957).
    • (1957) Aust. J. Sci. , vol.20 , pp. 67-69
    • Burnet, F.M.1
  • 2
    • 0000590741 scopus 로고
    • Genes and antibodies. Do antigens bear instructions for antibody specificity or do they select cell lines that arise by mutation?
    • Lederberg, J. Genes and antibodies. Do antigens bear instructions for antibody specificity or do they select cell lines that arise by mutation? Science 129, 1649-1653 (1959).
    • (1959) Science , vol.129 , pp. 1649-1653
    • Lederberg, J.1
  • 3
    • 0013783533 scopus 로고
    • Amino acid sequence studies with Bence-Jones proteins
    • Hilschmann, N. & Craig, L. C. Amino acid sequence studies with Bence-Jones proteins. Proc. Natl Acad. Sci. USA 53, 1403-1409 (1965).
    • (1965) Proc. Natl. Acad. Sci. USA , vol.53 , pp. 1403-1409
    • Hilschmann, N.1    Craig, L.C.2
  • 4
    • 0014010657 scopus 로고
    • Immunoglobulin structure: Partial amino acid sequence of a Bence Jones protein
    • Titani, K., Whitley, E., Avogardo, L. & Putnam, F. W. Immunoglobulin structure: partial amino acid sequence of a Bence Jones protein. Science 152, 1513-1516 (1966).
    • (1966) Science , vol.152 , pp. 1513-1516
    • Titani, K.1    Whitley, E.2    Avogardo, L.3    Putnam, F.W.4
  • 5
    • 0014024565 scopus 로고
    • Variations in amino acid sequence near the disulphide bridges of Bence-Jones proteins
    • Milstein, C. Variations in amino acid sequence near the disulphide bridges of Bence-Jones proteins. Nature 209, 370-373 (1966).
    • (1966) Nature , vol.209 , pp. 370-373
    • Milstein, C.1
  • 6
    • 0014019617 scopus 로고
    • Origin of antibody variation
    • Brenner, S. & Milstein, C. Origin of antibody variation. Nature 211, 242-243 (1966).
    • (1966) Nature , vol.211 , pp. 242-243
    • Brenner, S.1    Milstein, C.2
  • 8
    • 0013882288 scopus 로고
    • The unusual mutagenic specificity of an E. coli mutator gene
    • Yanotsky, C., Cox, E. C. & Horn, V. The unusual mutagenic specificity of an E. coli mutator gene. Proc. Natl Acad. Sci. USA 55, 274-281 (1966).
    • (1966) Proc. Natl. Acad. Sci. USA , vol.55 , pp. 274-281
    • Yanotsky, C.1    Cox, E.C.2    Horn, V.3
  • 9
    • 0020534965 scopus 로고
    • Somatic generation of antibody diversity
    • Tonegawa, S. Somatic generation of antibody diversity. Nature 302, 575-561 (1983).
    • (1983) Nature , vol.302 , pp. 575-1561
    • Tonegawa, S.1
  • 10
    • 0030006070 scopus 로고    scopus 로고
    • Clonal selection and learning in the antibody system
    • Rajewsky, K. Clonal selection and learning in the antibody system. Nature 381, 751-758 (1996).
    • (1996) Nature , vol.381 , pp. 751-758
    • Rajewsky, K.1
  • 11
    • 0000296526 scopus 로고    scopus 로고
    • Somatic hypermutation of immunoglobulin genes
    • Parham, P. (ed.) Somatic hypermutation of immunoglobulin genes. Immunol. Rev. 162, 1-298 (1998).
    • (1998) Immunol. Rev. , vol.162 , pp. 1-298
    • Parham, P.1
  • 12
    • 17944380943 scopus 로고    scopus 로고
    • The Y-family of DNA polymerases
    • Ohmori, H. et al. The Y-family of DNA polymerases. Mol. Cell 8, 7-8 (2001).
    • (2001) Mol. Cell , vol.8 , pp. 7-8
    • Ohmori, H.1
  • 14
    • 0035377269 scopus 로고    scopus 로고
    • DNA polymerase η is an A-T mutator in somatic hypermutation of immunoglobulin variable genes
    • Zeng, X. et al. DNA polymerase η is an A-T mutator in somatic hypermutation of immunoglobulin variable genes. Nature Immunol. 2, 537-5411 (2001).
    • (2001) Nature Immunol. , vol.2 , pp. 537-5411
    • Zeng, X.1
  • 15
    • 1642499721 scopus 로고    scopus 로고
    • DNA polymerase η is involved in hypermutation occurring during immunoglobulin class switch recombination
    • Faili, A. et al. DNA polymerase η is involved in hypermutation occurring during immunoglobulin class switch recombination. J. Exp. Med. 199, 265-270 (2004).
    • (2004) J. Exp. Med. , vol.199 , pp. 265-270
    • Faili, A.1
  • 16
    • 1842732235 scopus 로고    scopus 로고
    • Absence of DNA polymerase η reveals targeting of C mutations on the nontranscribed strand in immunoglobulin switch regions
    • Zeng, X., Negrete, G. A., Kasmer, C., Yang, W. W. & Gearhart, P. J. Absence of DNA polymerase η reveals targeting of C mutations on the nontranscribed strand in immunoglobulin switch regions. J. Exp. Med. 199, 917-924 (2004).
    • (2004) J. Exp. Med. , vol.199 , pp. 917-924
    • Zeng, X.1    Negrete, G.A.2    Kasmer, C.3    Yang, W.W.4    Gearhart, P.J.5
  • 17
    • 0037206851 scopus 로고    scopus 로고
    • Induction ot somatic hypermutation in immunoglobulin genes is dependent on DNA polymerase ι
    • Faili, A. et al. Induction ot somatic hypermutation in immunoglobulin genes is dependent on DNA polymerase ι. Nature 419, 944-947 (2002).
    • (2002) Nature , vol.419 , pp. 944-947
    • Faili, A.1
  • 18
    • 0035399804 scopus 로고    scopus 로고
    • Decreased frequency of somatic hypermutation and impaired affinity maturation but intact germinal center formation in mice expressing antisense RNA to DNA polymerase ζ
    • Dlaz, M., Verkoczy, L. K., Flajnik, M. F. & Klinman, N. R. Decreased frequency of somatic hypermutation and impaired affinity maturation but intact germinal center formation in mice expressing antisense RNA to DNA polymerase ζ. J. Immunol. 167, 327-335 (2001).
    • (2001) J. Immunol. , vol.167 , pp. 327-335
    • Dlaz, M.1    Verkoczy, L.K.2    Flajnik, M.F.3    Klinman, N.R.4
  • 19
    • 0035005241 scopus 로고    scopus 로고
    • The translesion DNA polymerase ζ plays a major role in Ig and BCL-6 somatic hypermutation
    • Zan, H. et al. The translesion DNA polymerase ζ plays a major role in Ig and BCL-6 somatic hypermutation. Immunity 14, 643-653 (2001).
    • (2001) Immunity , vol.14 , pp. 643-653
    • Zan, H.1
  • 20
    • 0037388452 scopus 로고    scopus 로고
    • Rev1 is essential for DNA damage tolerance and non-templated immunoglobulin gene mutation in a vertebrate cell line
    • Simpson, L. J. & Sale, J. E. Rev1 is essential for DNA damage tolerance and non-templated immunoglobulin gene mutation in a vertebrate cell line. EMBO J. 22, 1654-1664 (2003).
    • (2003) EMBO J. , vol.22 , pp. 1654-1664
    • Simpson, L.J.1    Sale, J.E.2
  • 21
    • 0037019315 scopus 로고    scopus 로고
    • AID mutates E. coli suggesting a DNA deamination mechanism tor antibody diversification
    • Petersen-Mahrt, S. K., Harris, R. S. & Neuberger, M. S. AID mutates E. coli suggesting a DNA deamination mechanism tor antibody diversification. Nature 418, 99-104 (2002).
    • (2002) Nature , vol.418 , pp. 99-104
    • Petersen-Mahrt, S.K.1    Harris, R.S.2    Neuberger, M.S.3
  • 22
    • 0037926476 scopus 로고    scopus 로고
    • Processive AID-catalysed cytosine deamination on single-stranded DNA simulates somatic hypermutation
    • Pham, P., Bransteltter, R., Petruska, J. & Goodman, M. F. Processive AID-catalysed cytosine deamination on single-stranded DNA simulates somatic hypermutation. Nature 424, 103-107 (2003).
    • (2003) Nature , vol.424 , pp. 103-107
    • Pham, P.1    Bransteltter, R.2    Petruska, J.3    Goodman, M.F.4
  • 23
    • 0037452080 scopus 로고    scopus 로고
    • Transcriplion-targeted DNA deamination by the AID antibody diversification enzyme
    • Chaudhuri, J. et al. Transcriplion-targeted DNA deamination by the AID antibody diversification enzyme. Nature 422, 726-730 (2003).
    • (2003) Nature , vol.422 , pp. 726-730
    • Chaudhuri, J.1
  • 24
    • 0037388165 scopus 로고    scopus 로고
    • Activation-induced cytidine deaminase deaminates deoxycytidine on single-stranded DNA but requires the action of RNase
    • Bransteitter, R., Pham P., Scharff M. D. & Goodman, M. F. Activation-induced cytidine deaminase deaminates deoxycytidine on single-stranded DNA but requires the action of RNase. Proc. Natl Acad. Sci. USA 100, 4102-4107 (2003).
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 4102-4107
    • Bransteitter, R.1    Pham, P.2    Scharff, M.D.3    Goodman, M.F.4
  • 25
    • 0038293484 scopus 로고    scopus 로고
    • Transcription enhances AID-mediated cytidine deamination by exposing single-stranded DNA on the nontemplale strand
    • Ramiro, A. R., Stavropoulos, P., Jankovic, M. & Nussenzweig, M. C. Transcription enhances AID-mediated cytidine deamination by exposing single-stranded DNA on the nontemplale strand. Nature Immunol. 4, 452-456 (2003).
    • (2003) Nature Immunol. , vol.4 , pp. 452-456
    • Ramiro, A.R.1    Stavropoulos, P.2    Jankovic, M.3    Nussenzweig, M.C.4
  • 26
    • 0037901850 scopus 로고    scopus 로고
    • Human activation-induced cytidine deaminase causes transcription- dependent, strand-biased C to U deaminations
    • Sohail, A., Klapacz, J., Samaranayake, M., Ullah, A. & Bhagwat, A. S. Human activation-induced cytidine deaminase causes transcription-dependent, strand-biased C to U deaminations. Nucleic Acids Res. 31, 2990-2994 (2003).
    • (2003) Nucleic Acids Res. , vol.31 , pp. 2990-2994
    • Sohail, A.1    Klapacz, J.2    Samaranayake, M.3    Ullah, A.4    Bhagwat, A.S.5
  • 27
    • 1542328859 scopus 로고    scopus 로고
    • Comparison of the differential context-dependence of DNA deamination by APOBEC enzymes: Correlation with mutation spectra in vivo
    • Beale, R. C. et al. Comparison of the differential context-dependence of DNA deamination by APOBEC enzymes: correlation with mutation spectra in vivo. J. Mol. Biol. 337, 585-596 (2004).
    • (2004) J. Mol. Biol. , vol.337 , pp. 585-596
    • Beale, R.C.1
  • 28
    • 1342282983 scopus 로고    scopus 로고
    • DNA substrate length and surrounding sequence affect the activation-induced deaminase activity at cytidine
    • Yu, K., Huang, F. T. & Lieber, M. R. DNA substrate length and surrounding sequence affect the activation-induced deaminase activity at cytidine. J. Biol. Chem. 279, 6496-6500 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 6496-6500
    • Yu, K.1    Huang, F.T.2    Lieber, M.R.3
  • 29
    • 0037074975 scopus 로고    scopus 로고
    • Activation-induced cytidine deaminase turns on somatic hypermutation in hybridomas
    • Martin, A. et al. Activation-induced cytidine deaminase turns on somatic hypermutation in hybridomas. Nature 415, 802-806 (2002).
    • (2002) Nature , vol.415 , pp. 802-806
    • Martin, A.1
  • 30
    • 0037076967 scopus 로고    scopus 로고
    • AID enzyme-induced hypermutation in an actively transcribed gene in fibroblasts
    • Yoshikawa, K. et al. AID enzyme-induced hypermutation in an actively transcribed gene in fibroblasts. Science 296, 2033-2036 (2002).
    • (2002) Science , vol.296 , pp. 2033-2036
    • Yoshikawa, K.1
  • 31
    • 0037026482 scopus 로고    scopus 로고
    • Altering the pathway of IgV gene hypermutation by inhibiting uracil DNA glycosylase
    • Di Nola, J. & Neuberger, M. S. Altering the pathway of IgV gene hypermutation by inhibiting uracil DNA glycosylase. Nature 419, 43-48 (2002).
    • (2002) Nature , vol.419 , pp. 43-48
    • Di Nola, J.1    Neuberger, M.S.2
  • 32
    • 0037108463 scopus 로고    scopus 로고
    • Immunoglobulin isotype switching is inhibited and somatic hypermutation perturbed in UNG-deficient mice
    • Rada, C. et al. Immunoglobulin isotype switching is inhibited and somatic hypermutation perturbed in UNG-deficient mice. Curr. Biol. 12, 1748-1755 (2002).
    • (2002) Curr. Biol. , vol.12 , pp. 1748-1755
    • Rada, C.1
  • 33
    • 0142092610 scopus 로고    scopus 로고
    • Human uracil-DNA glycosylase deficiency associated with profoundly impaired immunoglobulin class-switch recombination
    • Imai, K. et al. Human uracil-DNA glycosylase deficiency associated with profoundly impaired immunoglobulin class-switch recombination. Nature Immunol. 4, 1023-1028 (2003).
    • (2003) Nature Immunol. , vol.4 , pp. 1023-1028
    • Imai, K.1
  • 34
    • 0032127804 scopus 로고    scopus 로고
    • Hotspot focusing of somatic hypermutation in MSH2-deficient mice suggests two stages of mutational targeting
    • Rada, C., Ehrenstein, M. R., Neuberger, M. S. & Milstein, C. Hotspot focusing of somatic hypermutation in MSH2-deficient mice suggests two stages of mutational targeting. Immunity 9, 135-141 (1998).
    • (1998) Immunity , vol.9 , pp. 135-141
    • Rada, C.1    Ehrenstein, M.R.2    Neuberger, M.S.3    Milstein, C.4
  • 35
    • 0032101611 scopus 로고    scopus 로고
    • Increased hypermutation at G and C nucleotides in immunoglobulin variable genes from mice deficient in the MSH2 mismatch repair protein
    • Phung, Q. H. et al. Increased hypermutation at G and C nucleotides in immunoglobulin variable genes from mice deficient in the MSH2 mismatch repair protein. J. Exp. Med. 187, 1745-1751 (1998)
    • (1998) J. Exp. Med. , vol.187 , pp. 1745-1751
    • Phung, Q.H.1
  • 36
    • 0032127811 scopus 로고    scopus 로고
    • Mismatch repair deficiency interferes with the accumulation of mutations in chronically stimulated B cells and not with the hypermutation process
    • Frey, S. et al. Mismatch repair deficiency interferes with the accumulation of mutations in chronically stimulated B cells and not with the hypermutation process. Immunity 9, 127-134 (1998).
    • (1998) Immunity , vol.9 , pp. 127-134
    • Frey, S.1
  • 37
    • 0034268780 scopus 로고    scopus 로고
    • Class switch recombination and hypermutation require activation-induced cytidine deaminase (AID), a potential RNA editing enzyme
    • Muramatsu, M. et al. Class switch recombination and hypermutation require activation-induced cytidine deaminase (AID), a potential RNA editing enzyme. Cell 102, 553-563 (2000).
    • (2000) Cell , vol.102 , pp. 553-563
    • Muramatsu, M.1
  • 38
    • 0034264851 scopus 로고    scopus 로고
    • Activation-induced cytidine deaminase (AID) deficiency causes the autosomal recessive form of the hyper-IgM syndrome (HIGM2)
    • Revy, P. et al. Activation-induced cytidine deaminase (AID) deficiency causes the autosomal recessive form of the hyper-IgM syndrome (HIGM2). Cell 102, 565-575 (2000).
    • (2000) Cell , vol.102 , pp. 565-575
    • Revy, P.1
  • 39
    • 0034614916 scopus 로고    scopus 로고
    • Somatic hypermutation in MutS homologue (MSH)3-, MSH6-, and MSH3/MSH6-deficient mice reveals a role tor the MSH2-MSH6 heterodimer in modulating the base substitution pattern
    • Wlesendanger, M., Kneitz, B., Edelmann, W. & Scharff, M. D. Somatic hypermutation in MutS homologue (MSH)3-, MSH6-, and MSH3/MSH6-deficient mice reveals a role tor the MSH2-MSH6 heterodimer in modulating the base substitution pattern. J. Exp. Med. 191, 579-584 (2000).
    • (2000) J. Exp. Med. , vol.191 , pp. 579-584
    • Wlesendanger, M.1    Kneitz, B.2    Edelmann, W.3    Scharff, M.D.4
  • 40
    • 3142674907 scopus 로고    scopus 로고
    • Examination of Msh6- and Msh3-deficient mice in class switching reveals overlapping and distinct roles ot MutS homologues in antibody diversification
    • Li, Z. B. et al. Examination of Msh6- and Msh3-deficient mice in class switching reveals overlapping and distinct roles ot MutS homologues in antibody diversification. J. Exp. Med. 200, 47-59 (2004).
    • (2004) J. Exp. Med. , vol.200 , pp. 47-59
    • Li, Z.B.1
  • 41
    • 3142663166 scopus 로고    scopus 로고
    • A role for Msh6 but not Msh3 in somatic hypermutation and class switch recombination
    • Martomo, S. A., Yang, W. W. & Gaarhart, P. J. A role for Msh6 but not Msh3 in somatic hypermutation and class switch recombination. J. Exp. Med. 200, 61-68 (2004).
    • (2004) J. Exp. Med. , vol.200 , pp. 61-68
    • Martomo, S.A.1    Yang, W.W.2    Gaarhart, P.J.3
  • 42
    • 1142299546 scopus 로고    scopus 로고
    • Altered somatic hypermutation and reduced class-switch recombination in exonuctease 1 - Mutant mice
    • Bardwell, P. D. et al. Altered somatic hypermutation and reduced class-switch recombination in exonuctease 1 - mutant mice. Nature Immunol. 5, 224-229 (2004).
    • (2004) Nature Immunol. , vol.5 , pp. 224-229
    • Bardwell, P.D.1
  • 43
    • 6344256944 scopus 로고    scopus 로고
    • Mismatch recognition and uracil-excision provide complementary paths to both Ig switching and the A•T-focused phase of somalic mutation
    • Rada, C., Di Noia, J. M. & Neuberger, M. S. Mismatch recognition and uracil-excision provide complementary paths to both Ig switching and the A•T-focused phase of somalic mutation. Mol. Cell 16, 163-171 (2004).
    • (2004) Mol. Cell , vol.16 , pp. 163-171
    • Rada, C.1    Di Noia, J.M.2    Neuberger, M.S.3
  • 44
    • 2342570833 scopus 로고    scopus 로고
    • Genesis of the strand-biased signature in somatic hypermutation of rearranged immunoglobulin variable genes
    • Steele, E. J., Franklin, A. & Blanden, R. V. Genesis of the strand-biased signature in somatic hypermutation of rearranged immunoglobulin variable genes. Immunol. Cell Biol. 82, 209-218 (2004).
    • (2004) Immunol. Cell Biol. , vol.82 , pp. 209-218
    • Steele, E.J.1    Franklin, A.2    Blanden, R.V.3
  • 46
    • 0034720285 scopus 로고    scopus 로고
    • Low fidelity DNA synthesis by human DNA polymerase-η
    • Matsuda, T., Bebenek, K., Masutani, C., Hanaoka, F. & Kunkel, T. A. Low fidelity DNA synthesis by human DNA polymerase-η. Nature 404, 1011-1013 (2000).
    • (2000) Nature , vol.404 , pp. 1011-1013
    • Matsuda, T.1    Bebenek, K.2    Masutani, C.3    Hanaoka, F.4    Kunkel, T.A.5
  • 47
    • 0035860310 scopus 로고    scopus 로고
    • Error rate and specificity of human and murine DNA polymerase η
    • Matsuda, T. et al. Error rate and specificity of human and murine DNA polymerase η. J. Mol. Biol. 312, 335-346 (2001).
    • (2001) J. Mol. Biol. , vol.312 , pp. 335-346
    • Matsuda, T.1
  • 48
    • 0035379581 scopus 로고    scopus 로고
    • Somatic mutation hotspots correlate with DNA polymerase η error spectrum
    • Rogozin, I. B., Pavlov, Y. I., Bebenek, K., Matsuda, T. & Kunkel, T. A. Somatic mutation hotspots correlate with DNA polymerase η error spectrum. Nature Immunol. 2, 530-536 (2001).
    • (2001) Nature Immunol. , vol.2 , pp. 530-536
    • Rogozin, I.B.1    Pavlov, Y.I.2    Bebenek, K.3    Matsuda, T.4    Kunkel, T.A.5
  • 49
    • 0037162552 scopus 로고    scopus 로고
    • Correlation of somatic hyperrnutation specificity and A-T base pair substitution errors by DNA polymerase η during copying ot a mouse immunoglobulin κ light chain transgene
    • Pavtov, Y. I. et al. Correlation of somatic hyperrnutation specificity and A-T base pair substitution errors by DNA polymerase η during copying ot a mouse immunoglobulin κ light chain transgene. Proc. Natl Acad. Sci USA 99, 9954-9959 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 9954-9959
    • Pavtov, Y.I.1
  • 50
    • 0042422042 scopus 로고    scopus 로고
    • 129-Derived strains ot mice are deficient in DNA polymerase ι and have normal immunoglobulin hypermutation
    • McDonald, J. P. et al. 129-derived strains ot mice are deficient in DNA polymerase ι and have normal immunoglobulin hypermutation. J. Exp. Med. 198, 635-643 (2003).
    • (2003) J. Exp. Med. , vol.198 , pp. 635-643
    • McDonald, J.P.1
  • 51
    • 0034738983 scopus 로고    scopus 로고
    • Eukaryotic polymerases ι and ζ act sequentially to bypass DNA lesions
    • Johnson, R. E., Washington, M. T., Haracska, L., Prakash, S. & Prakash, L. Eukaryotic polymerases ι and ζ act sequentially to bypass DNA lesions. Nature 406, 1015-1019 (2000).
    • (2000) Nature , vol.406 , pp. 1015-1019
    • Johnson, R.E.1    Washington, M.T.2    Haracska, L.3    Prakash, S.4    Prakash, L.5
  • 52
    • 0017886373 scopus 로고
    • Escherichia coli mutants deficient in deoxyuridine triphosphatase
    • Hochhauser, S. J. & Wiess, B. Escherichia coli mutants deficient in deoxyuridine triphosphatase. J. Bacteriol. 134, 157-166 (1978).
    • (1978) J. Bacteriol. , vol.134 , pp. 157-166
    • Hochhauser, S.J.1    Wiess, B.2
  • 53
    • 0242412184 scopus 로고    scopus 로고
    • Origin of endogenous DNA abasic sites in Saccharomyces cerevisiae
    • Guillet, M. & Boiteux, S. Origin of endogenous DNA abasic sites in Saccharomyces cerevisiae. Mol. Cell. Biol. 23, 8386-8394 (2003).
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 8386-8394
    • Guillet, M.1    Boiteux, S.2
  • 54
    • 0013608322 scopus 로고
    • Transient accumulation of Okazaki fragments as a result of uracil incorporation into nascent DNA
    • Tye, B. K., Nyman, P. O., Lehman, I. R., Hochhauser, S. & Weiss, B. Transient accumulation of Okazaki fragments as a result of uracil incorporation into nascent DNA. Proc. Natl Acad. Sci. USA 74, 154-157 (1977).
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 154-157
    • Tye, B.K.1    Nyman, P.O.2    Lehman, I.R.3    Hochhauser, S.4    Weiss, B.5
  • 55
    • 0027426749 scopus 로고
    • dUTP pyrophosphatase is an essential enzyme in Saccharomyces cerevisiae
    • Gadsden, M. H., McIntosh, E. M., Game, J. C., Wilson, P. J. & Haynes, R. H. dUTP pyrophosphatase is an essential enzyme in Saccharomyces cerevisiae. EMBO J. 12, 4425-4431 (1993).
    • (1993) EMBO J. , vol.12 , pp. 4425-4431
    • Gadsden, M.H.1    McIntosh, E.M.2    Game, J.C.3    Wilson, P.J.4    Haynes, R.H.5
  • 56
    • 0022778805 scopus 로고
    • Transcription ot genes encoding enzymes involved in DNA synthesis during the cell cycle of Saccharomyces cerevisiae
    • McIntosh, E. M., Gadsden, M. H. & Haynes, R. H. Transcription ot genes encoding enzymes involved in DNA synthesis during the cell cycle of Saccharomyces cerevisiae. Mol. Gen. Genet. 204, 363-366 (1986).
    • (1986) Mol. Gen. Genet. , vol.204 , pp. 363-366
    • McIntosh, E.M.1    Gadsden, M.H.2    Haynes, R.H.3
  • 57
    • 0027254420 scopus 로고
    • Maturation stage and proliferation-dependent expression of dUTPase in human T cells
    • Strahler, J. R. et al. Maturation stage and proliferation-dependent expression of dUTPase in human T cells. Proc. Natl Acad. Sci. USA 90, 4991-4995 (1993).
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 4991-4995
    • Strahler, J.R.1
  • 58
    • 0030791450 scopus 로고    scopus 로고
    • The human dUTPase gene encodes both nuclear and mitochondria/isoforms. Differential expression of the isoforms and characterization ot a cDNA encoding the mitochondrial species
    • Ladner, R. D. & Caradonna, S. J. The human dUTPase gene encodes both nuclear and mitochondria/isoforms. Differential expression of the isoforms and characterization ot a cDNA encoding the mitochondrial species. J. Biol. Chem. 272, 19072-19080 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 19072-19080
    • Ladner, R.D.1    Caradonna, S.J.2
  • 59
    • 0032143823 scopus 로고    scopus 로고
    • Probing immunoglcbulin gene hypermutation with microsatellites suggests a nonreplicative shori patch DNA synthesis process
    • Bertocci, B. et al. Probing immunoglcbulin gene hypermutation with microsatellites suggests a nonreplicative shori patch DNA synthesis process. Immunity 9, 257-265 (1998).
    • (1998) Immunity , vol.9 , pp. 257-265
    • Bertocci, B.1
  • 60
    • 0036732772 scopus 로고    scopus 로고
    • AID-dependent somatic hypermutation occurs as a DNA single-strand event in the BL2 cell line
    • Faili, A. et al. AID-dependent somatic hypermutation occurs as a DNA single-strand event in the BL2 cell line. Nature Immunol. 3, 815-821 (2002).
    • (2002) Nature Immunol. , vol.3 , pp. 815-821
    • Faili, A.1
  • 61
    • 6044230603 scopus 로고    scopus 로고
    • Repair of U-G and U-A in DNA by UNG2-associated repair complexes takes place predominantly by short-patch repairboth in proliferating and growth-arrested cells
    • Akbari, M. et al. Repair of U-G and U-A in DNA by UNG2-associated repair complexes takes place predominantly by short-patch repairboth in proliferating and growth-arrested cells. Nucleic Acids Res. 32, 5486-5498 (2004).
    • (2004) Nucleic Acids Res. , vol.32 , pp. 5486-5498
    • Akbari, M.1
  • 62
    • 0037115911 scopus 로고    scopus 로고
    • Uracil in DNA - Occurrence, consequences and repair
    • Krokan, H. E., Drablos, F. & Slupphaug G. Uracil in DNA - occurrence, consequences and repair. Oncogene 21, 8935-8948 (2002).
    • (2002) Oncogene , vol.21 , pp. 8935-8948
    • Krokan, H.E.1    Drablos, F.2    Slupphaug, G.3
  • 63
    • 0034734383 scopus 로고    scopus 로고
    • Structure and function in the uracil-DNA glycosylase superfamily
    • Pearl, L. H. Structure and function in the uracil-DNA glycosylase superfamily. Mutat Res. 460, 165-181 (2000).
    • (2000) Mutat Res. , vol.460 , pp. 165-181
    • Pearl, L.H.1
  • 64
    • 0033636312 scopus 로고    scopus 로고
    • Uracil-DNA glycosylase (UNG)-deficient mice reveal a primary role of the enzyme during DNA replication
    • Nilsen, H. et al. Uracil-DNA glycosylase (UNG)-deficient mice reveal a primary role of the enzyme during DNA replication. Mol. Cell 5, 1059-1065 (2000).
    • (2000) Mol. Cell , vol.5 , pp. 1059-1065
    • Nilsen, H.1
  • 65
    • 0025630537 scopus 로고
    • Boundaries of somatic mutation in rearranged immunogtobulin genes: 5′ boundary is near the promoter, and 3′ boundary is approximately 1 kb from V(D)J gene
    • Lebecque, S. G. & Gearhart, P. J. Boundaries of somatic mutation in rearranged immunogtobulin genes: 5′ boundary is near the promoter, and 3′ boundary is approximately 1 kb from V(D)J gene. J. Exp. Med. 172, 1717-1727 (1990).
    • (1990) J. Exp. Med. , vol.172 , pp. 1717-1727
    • Lebecque, S.G.1    Gearhart, P.J.2
  • 66
    • 0032555232 scopus 로고    scopus 로고
    • Both DNA strands of antibody genes are hypermutation targets
    • Milstein, C., Neuberger, M. S. & Staden, R. Both DNA strands of antibody genes are hypermutation targets. Proc. Natl Acad. Sci. USA 95, 8791-3794 (1998).
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 8791-13794
    • Milstein, C.1    Neuberger, M.S.2    Staden, R.3
  • 67
    • 8544241736 scopus 로고    scopus 로고
    • Retroviral restriction by APOBEC proteins
    • Harris, R. S. & Liddament, M. T. Retroviral restriction by APOBEC proteins. Nature Rev. Immunol. 4, 868-877 (2004).
    • (2004) Nature Rev. Immunol. , vol.4 , pp. 868-877
    • Harris, R.S.1    Liddament, M.T.2
  • 68
    • 0036788148 scopus 로고    scopus 로고
    • Roles of uracil-DNA glycosylase and dUTPase in virus replication
    • Chen, R., Wang, H. & Mansky, L. M. Roles of uracil-DNA glycosylase and dUTPase in virus replication. J. Gen. Virol. 83, 2339-2345 (2002).
    • (2002) J. Gen. Virol. , vol.83 , pp. 2339-2345
    • Chen, R.1    Wang, H.2    Mansky, L.M.3
  • 69
    • 0031010763 scopus 로고    scopus 로고
    • dUTPase-minus caprine arthritis-encephalitis virus is attenuated for pathogenesis and accumulates G-to-A substitutions
    • Turelli, P., Guiguen, F., Momex, J. F., Vigne, R. & Querat, G. dUTPase-minus caprine arthritis-encephalitis virus is attenuated for pathogenesis and accumulates G-to-A substitutions. J. Virol. 71, 4522-1530 (1997).
    • (1997) J. Virol. , vol.71 , pp. 4522-11530
    • Turelli, P.1    Guiguen, F.2    Momex, J.F.3    Vigne, R.4    Querat, G.5
  • 70
    • 0029153930 scopus 로고
    • Increased mutation frequency of feline immunodeficiency virus lacking functional deoxyuridine-triphosphatase
    • Lerner, D. L. et al. Increased mutation frequency of feline immunodeficiency virus lacking functional deoxyuridine-triphosphatase. Proc. Natl Acad. Sci. USA 92, 7480-7484 (1995).
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 7480-7484
    • Lerner, D.L.1
  • 71
    • 0037085991 scopus 로고    scopus 로고
    • Reverse transcriptase-mediated tropism switching in Boruetella bacteriophaga
    • Liu, M. et al. Reverse transcriptase-mediated tropism switching in Boruetella bacteriophaga. Science 295, 2091-2094 (2002).
    • (2002) Science , vol.295 , pp. 2091-2094
    • Liu, M.1
  • 72
    • 4644278381 scopus 로고    scopus 로고
    • Evolution: A is for adaptation
    • Boeke, J. D. Evolution: A is for adaptation. Nature 431, 408-409 (2004).
    • (2004) Nature , vol.431 , pp. 408-409
    • Boeke, J.D.1
  • 75
    • 0031720426 scopus 로고    scopus 로고
    • A murine AP-endonuclease gene-targeted deficiency with post-implantation embryonic progression and ionizing radiation sensitivity
    • Ludwig, D. L. et al. A murine AP-endonuclease gene-targeted deficiency with post-implantation embryonic progression and ionizing radiation sensitivity. Mutat. Res. 409, 17-29 (1998).
    • (1998) Mutat. Res. , vol.409 , pp. 17-29
    • Ludwig, D.L.1


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