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Volumn 28, Issue 6, 2003, Pages 305-312

Immunity through DNA deamination

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBODY; DEAMINASE; DNA; IMMUNOGLOBULIN; NUCLEIC ACID;

EID: 0038713344     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0968-0004(03)00111-7     Document Type: Review
Times cited : (206)

References (62)
  • 1
    • 0000476915 scopus 로고
    • An N-glycosidase from Escherichia coli that releases free uracil from DNA containing deaminated cytosine residues
    • Lindahl T. An N-glycosidase from Escherichia coli that releases free uracil from DNA containing deaminated cytosine residues. Proc. Natl. Acad. Sci. U. S. A. 71:1974;3649-3653.
    • (1974) Proc. Natl. Acad. Sci. U. S. A. , vol.71 , pp. 3649-3653
    • Lindahl, T.1
  • 2
    • 0034930217 scopus 로고    scopus 로고
    • Base excision repair in a network of defence and tolerance
    • Nilsen H., Krokan H.E. Base excision repair in a network of defence and tolerance. Carcinogenesis. 22:2001;987-998.
    • (2001) Carcinogenesis , vol.22 , pp. 987-998
    • Nilsen, H.1    Krokan, H.E.2
  • 3
    • 0033603340 scopus 로고    scopus 로고
    • Specific expression of activation-induced cytidine deaminase (AID), a novel member of the RNA-editing deaminase family in germinal center B cells
    • Muramatsu M., et al. Specific expression of activation-induced cytidine deaminase (AID), a novel member of the RNA-editing deaminase family in germinal center B cells. J. Biol. Chem. 274:1999;18470-18476.
    • (1999) J. Biol. Chem. , vol.274 , pp. 18470-18476
    • Muramatsu, M.1
  • 4
    • 0037019315 scopus 로고    scopus 로고
    • AID mutates E. coli suggesting a DNA deamination mechanism for antibody diversification
    • Petersen-Mahrt S.K., et al. AID mutates E. coli suggesting a DNA deamination mechanism for antibody diversification. Nature. 418:2002;99-104.
    • (2002) Nature , vol.418 , pp. 99-104
    • Petersen-Mahrt, S.K.1
  • 5
    • 0037026482 scopus 로고    scopus 로고
    • Altering the pathway of Ig V gene hypermutation by inhibiting uracil DNA glycosylase
    • Di Noia J., Neuberger M.S. Altering the pathway of Ig V gene hypermutation by inhibiting uracil DNA glycosylase. Nature. 419:2002;43-48.
    • (2002) Nature , vol.419 , pp. 43-48
    • Di Noia, J.1    Neuberger, M.S.2
  • 6
    • 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. 12:2002;1748-1755.
    • (2002) Curr. Biol. , vol.12 , pp. 1748-1755
    • Rada, C.1
  • 7
    • 0020534965 scopus 로고
    • Somatic generation of antibody diversity
    • Tonegawa S. Somatic generation of antibody diversity. Nature. 302:1983;575-581.
    • (1983) Nature , vol.302 , pp. 575-581
    • Tonegawa, S.1
  • 8
    • 0024846088 scopus 로고
    • The V(D)J recombination activating gene, RAG-1
    • Schatz D.G., et al. The V(D)J recombination activating gene, RAG-1. Cell. 59:1989;1035-1048.
    • (1989) Cell , vol.59 , pp. 1035-1048
    • Schatz, D.G.1
  • 9
    • 0035997348 scopus 로고    scopus 로고
    • V(D)J recombination: RAG proteins, repair factors, and regulation
    • Gellert M. V(D)J recombination: RAG proteins, repair factors, and regulation. Annu. Rev. Biochem. 71:2002;101-132.
    • (2002) Annu. Rev. Biochem. , vol.71 , pp. 101-132
    • Gellert, M.1
  • 10
    • 0028673962 scopus 로고
    • Formation of the chicken B-cell repertoire: Ontogenesis, regulation of Ig gene rearrangement, and diversification by gene conversion
    • Reynaud C.A., et al. Formation of the chicken B-cell repertoire: ontogenesis, regulation of Ig gene rearrangement, and diversification by gene conversion. Adv. Immunol. 57:1994;353-378.
    • (1994) Adv. Immunol. , vol.57 , pp. 353-378
    • Reynaud, C.A.1
  • 11
    • 0030006070 scopus 로고    scopus 로고
    • Clonal selection and learning in the antibody system
    • Rajewsky K. Clonal selection and learning in the antibody system. Nature. 381:1996;751-758.
    • (1996) Nature , vol.381 , pp. 751-758
    • Rajewsky, K.1
  • 12
    • 0036152242 scopus 로고    scopus 로고
    • Mechanism and control of class-switch recombination
    • Manis J.P., et al. Mechanism and control of class-switch recombination. Trends Immunol. 23:2002;31-39.
    • (2002) Trends Immunol. , vol.23 , pp. 31-39
    • Manis, J.P.1
  • 13
    • 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. 102:2000;553-563.
    • (2000) Cell , vol.102 , pp. 553-563
    • Muramatsu, M.1
  • 14
    • 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. 102:2000;565-575.
    • (2000) Cell , vol.102 , pp. 565-575
    • Revy, P.1
  • 15
    • 0037083364 scopus 로고    scopus 로고
    • Requirement of the activation-induced deaminase (AID) gene for immunoglobulin gene conversion
    • Arakawa H., et al. Requirement of the activation-induced deaminase (AID) gene for immunoglobulin gene conversion. Science. 295:2002;1301-1306.
    • (2002) Science , vol.295 , pp. 1301-1306
    • Arakawa, H.1
  • 16
    • 0037022540 scopus 로고    scopus 로고
    • AID is essential for immunoglobulin V gene conversion in a cultured B cell line
    • Harris R.S., et al. AID is essential for immunoglobulin V gene conversion in a cultured B cell line. Curr. Biol. 12:2002;435-438.
    • (2002) Curr. Biol. , vol.12 , pp. 435-438
    • Harris, R.S.1
  • 17
    • 0035974862 scopus 로고    scopus 로고
    • Ablation of XRCC2/3 transforms immunoglobulin V gene conversion into somatic hypermutation
    • Sale J.E., et al. Ablation of XRCC2/3 transforms immunoglobulin V gene conversion into somatic hypermutation. Nature. 412:2001;921-926.
    • (2001) Nature , vol.412 , pp. 921-926
    • Sale, J.E.1
  • 18
    • 0028818503 scopus 로고
    • Somatic hypermutation: How many mechanisms diversify V region sequences?
    • Maizels N. Somatic hypermutation: how many mechanisms diversify V region sequences? Cell. 83:1995;9-12.
    • (1995) Cell , vol.83 , pp. 9-12
    • Maizels, N.1
  • 19
    • 0030052281 scopus 로고    scopus 로고
    • Rearrangement-hypermutation-gene conversion: When, where and why?
    • Weill J.C., Reynaud C.A. Rearrangement-hypermutation-gene conversion: when, where and why? Immunol. Today. 17:1996;92-97.
    • (1996) Immunol. Today , vol.17 , pp. 92-97
    • Weill, J.C.1    Reynaud, C.A.2
  • 20
    • 0033564878 scopus 로고    scopus 로고
    • Deficiency in Msh2 affects the efficiency and local sequence specificity of immunoglobulin class-switch recombination: Parallels with somatic hypermutation
    • Ehrenstein M.R., Neuberger M.S. Deficiency in Msh2 affects the efficiency and local sequence specificity of immunoglobulin class-switch recombination: parallels with somatic hypermutation. EMBO J. 18:1999;3484-3490.
    • (1999) EMBO J. , vol.18 , pp. 3484-3490
    • Ehrenstein, M.R.1    Neuberger, M.S.2
  • 21
    • 0033497745 scopus 로고    scopus 로고
    • Antibody diversification and selection in the mature B-cell compartment
    • Neuberger M.S., et al. Antibody diversification and selection in the mature B-cell compartment. Cold Spring Harb. Symp. Quant. Biol. 64:1999;211-216.
    • (1999) Cold Spring Harb. Symp. Quant. Biol. , vol.64 , pp. 211-216
    • Neuberger, M.S.1
  • 22
    • 0034728685 scopus 로고    scopus 로고
    • Memory in the B-cell compartment: Antibody affinity maturation
    • Neuberger M.S., et al. Memory in the B-cell compartment: antibody affinity maturation. Philos. Trans. R. Soc. Lond. B Biol. Sci. 355:2000;357-360.
    • (2000) Philos. Trans. R. Soc. Lond. B Biol. Sci. , vol.355 , pp. 357-360
    • Neuberger, M.S.1
  • 23
    • 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. 415:2002;802-806.
    • (2002) Nature , vol.415 , pp. 802-806
    • Martin, A.1
  • 24
    • 0037149473 scopus 로고    scopus 로고
    • The AID enzyme induces class switch recombination in fibroblasts
    • Okazaki I., et al. The AID enzyme induces class switch recombination in fibroblasts. Nature. 416:2002;340-345.
    • (2002) Nature , vol.416 , pp. 340-345
    • Okazaki, I.1
  • 25
    • 0023651359 scopus 로고
    • A novel form of tissue-specific RNA processing produces apolipoprotein-B48 in intestine
    • Powell L.M., et al. A novel form of tissue-specific RNA processing produces apolipoprotein-B48 in intestine. Cell. 50:1987;831-840.
    • (1987) Cell , vol.50 , pp. 831-840
    • Powell, L.M.1
  • 26
    • 0027200620 scopus 로고
    • Molecular cloning of an apolipoprotein B messenger RNA editing protein
    • Teng B., et al. Molecular cloning of an apolipoprotein B messenger RNA editing protein. Science. 260:1993;1816-1819.
    • (1993) Science , vol.260 , pp. 1816-1819
    • Teng, B.1
  • 27
    • 0032127804 scopus 로고    scopus 로고
    • Hot spot focusing of somatic hypermutation in MSH2-deficient mice suggests two stages of mutational targeting
    • Rada C., et al. Hot spot focusing of somatic hypermutation in MSH2-deficient mice suggests two stages of mutational targeting. Immunity. 9:1998;135-141.
    • (1998) Immunity , vol.9 , pp. 135-141
    • Rada, C.1
  • 28
    • 0034614916 scopus 로고    scopus 로고
    • Somatic hypermutation in MutS homologue (MSH)3-, MSH6-, and MSH3/MSH6-deficient mice reveals a role for the MSH2-MSH6 heterodimer in modulating the base substitution pattern
    • Wiesendanger M., et al. Somatic hypermutation in MutS homologue (MSH)3-, MSH6-, and MSH3/MSH6-deficient mice reveals a role for the MSH2-MSH6 heterodimer in modulating the base substitution pattern. J. Exp. Med. 191:2000;579-584.
    • (2000) J. Exp. Med. , vol.191 , pp. 579-584
    • Wiesendanger, M.1
  • 29
    • 0035377269 scopus 로고    scopus 로고
    • DNA polymerase eta is an A-T mutator in somatic hypermutation of immunoglobulin variable genes
    • Zeng X., et al. DNA polymerase eta is an A-T mutator in somatic hypermutation of immunoglobulin variable genes. Nat. Immun. 2:2001;537-541.
    • (2001) Nat. Immun. , vol.2 , pp. 537-541
    • Zeng, X.1
  • 30
    • 0036863733 scopus 로고    scopus 로고
    • RNA editing enzyme APOBEC1 and some of its homologs can act as DNA mutators
    • Harris R.S., et al. RNA editing enzyme APOBEC1 and some of its homologs can act as DNA mutators. Mol. Cell. 10:2002;1247-1253.
    • (2002) Mol. Cell , vol.10 , pp. 1247-1253
    • Harris, R.S.1
  • 31
    • 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. 5:2000;1059-1065.
    • (2000) Mol. Cell , vol.5 , pp. 1059-1065
    • Nilsen, H.1
  • 32
    • 0033511807 scopus 로고    scopus 로고
    • Psoriasis upregulated phorbolin-1 shares structural but not functional similarity to the mRNA-editing protein apobec-1
    • Madsen P. Psoriasis upregulated phorbolin-1 shares structural but not functional similarity to the mRNA-editing protein apobec-1. J. Invest. Dermatol. 113:1999;162-169.
    • (1999) J. Invest. Dermatol. , vol.113 , pp. 162-169
    • Madsen, P.1
  • 33
    • 0035658430 scopus 로고    scopus 로고
    • ARCD-1, an apobec-1-related cytidine deaminase, exerts a dominant negative effect on C to U RNA editing
    • Anant S., et al. ARCD-1, an apobec-1-related cytidine deaminase, exerts a dominant negative effect on C to U RNA editing. Am. J. Physiol. Cell Physiol. 281:2001;C1904-C1916.
    • (2001) Am. J. Physiol. Cell Physiol. , vol.281
    • Anant, S.1
  • 34
    • 0036200070 scopus 로고    scopus 로고
    • An anthropoid-specific locus of orphan C to U RNA-editing enzymes on chromosome 22
    • Jarmuz A., et al. An anthropoid-specific locus of orphan C to U RNA-editing enzymes on chromosome 22. Genomics. 79:2002;285-296.
    • (2002) Genomics , vol.79 , pp. 285-296
    • Jarmuz, A.1
  • 35
    • 13144259628 scopus 로고    scopus 로고
    • Escherichia coli cytidine deaminase provides a molecular model for ApoB RNA editing and a mechanism for RNA substrate recognition
    • Navaratnam N., et al. Escherichia coli cytidine deaminase provides a molecular model for ApoB RNA editing and a mechanism for RNA substrate recognition. J. Mol. Biol. 275:1998;695-714.
    • (1998) J. Mol. Biol. , vol.275 , pp. 695-714
    • Navaratnam, N.1
  • 36
    • 0037449753 scopus 로고    scopus 로고
    • C-to-U RNA editing: Mechanisms leading to genetic diversity
    • Blanc V., Davidson N.O. C-to-U RNA editing: mechanisms leading to genetic diversity. J. Biol. Chem. 278:2003;1395-1398.
    • (2003) J. Biol. Chem. , vol.278 , pp. 1395-1398
    • Blanc, V.1    Davidson, N.O.2
  • 37
    • 0034733528 scopus 로고    scopus 로고
    • Purification and molecular cloning of a novel essential component of the apolipoprotein B mRNA editing enzyme-complex
    • Lellek H., et al. Purification and molecular cloning of a novel essential component of the apolipoprotein B mRNA editing enzyme-complex. J. Biol. Chem. 275:2000;19848-19856.
    • (2000) J. Biol. Chem. , vol.275 , pp. 19848-19856
    • Lellek, H.1
  • 38
    • 0033970066 scopus 로고    scopus 로고
    • Molecular cloning of apobec-1 complementation factor, a novel RNA-binding protein involved in the editing of apolipoprotein B mRNA
    • Mehta A., et al. Molecular cloning of apobec-1 complementation factor, a novel RNA-binding protein involved in the editing of apolipoprotein B mRNA. Mol. Cell. Biol. 20:2000;1846-1854.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 1846-1854
    • Mehta, A.1
  • 39
    • 0029614378 scopus 로고
    • Frequent somatic hypermutation of the 5′ noncoding region of the BCL6 gene in B-cell lymphoma
    • Migliazza A., et al. Frequent somatic hypermutation of the 5′ noncoding region of the BCL6 gene in B-cell lymphoma. Proc. Natl. Acad. Sci. U. S. A. 92:1995;12520-12524.
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 12520-12524
    • Migliazza, A.1
  • 40
    • 13144259651 scopus 로고    scopus 로고
    • R. BCL-6 mutations in normal germinal center B cells: Evidence of somatic hypermutation acting outside Ig loci
    • Pasqualucci L., et al. R. BCL-6 mutations in normal germinal center B cells: evidence of somatic hypermutation acting outside Ig loci. Proc. Natl. Acad. Sci. U. S. A. 95:1998;11816-11821.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 11816-11821
    • Pasqualucci, L.1
  • 41
    • 2642623612 scopus 로고    scopus 로고
    • Mutation of BCL-6 gene in normal B cells by the process of somatic hypermutation of Ig genes
    • Shen H.M., et al. Mutation of BCL-6 gene in normal B cells by the process of somatic hypermutation of Ig genes. Science. 280:1998;1750-1752.
    • (1998) Science , vol.280 , pp. 1750-1752
    • Shen, H.M.1
  • 42
    • 0035913362 scopus 로고    scopus 로고
    • Hypermutation of multiple proto-oncogenes in B-cell diffuse large-cell lymphomas
    • Pasqualucci L., et al. Hypermutation of multiple proto-oncogenes in B-cell diffuse large-cell lymphomas. Nature. 412:2001;341-346.
    • (2001) Nature , vol.412 , pp. 341-346
    • Pasqualucci, L.1
  • 43
    • 0037043699 scopus 로고    scopus 로고
    • Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein
    • Sheehy A.M., et al. Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein. Nature. 418:2002;646-650.
    • (2002) Nature , vol.418 , pp. 646-650
    • Sheehy, A.M.1
  • 44
    • 0035997389 scopus 로고    scopus 로고
    • RNA editing by adenosine deaminases that act on RNA
    • Bass B.L. RNA editing by adenosine deaminases that act on RNA. Annu. Rev. Biochem. 71:2002;817-846.
    • (2002) Annu. Rev. Biochem. , vol.71 , pp. 817-846
    • Bass, B.L.1
  • 45
    • 0025641736 scopus 로고
    • Premeiotic instability of repeated sequences in Neurospora crassa
    • Selker E.U. Premeiotic instability of repeated sequences in Neurospora crassa. Annu. Rev. Genet. 24:1990;579-613.
    • (1990) Annu. Rev. Genet. , vol.24 , pp. 579-613
    • Selker, E.U.1
  • 46
    • 0037172977 scopus 로고    scopus 로고
    • A cytosine methyltransferase homologue is essential for repeat-induced point mutation in Neurospora crassa
    • Freitag M., et al. A cytosine methyltransferase homologue is essential for repeat-induced point mutation in Neurospora crassa. Proc. Natl. Acad. Sci. U. S. A. 99:2002;8802-8807.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 8802-8807
    • Freitag, M.1
  • 47
    • 0027093283 scopus 로고
    • High frequency mutagenesis by a DNA methyltransferase
    • Shen J.-C., et al. High frequency mutagenesis by a DNA methyltransferase. Cell. 71:1992;1073-1080.
    • (1992) Cell , vol.71 , pp. 1073-1080
    • Shen, J.-C.1
  • 48
    • 0028794055 scopus 로고
    • A cytosine methyltransferase converts 5-methylcytosine in DNA to thymine
    • Yebra M.J., Bhagwat A.S. A cytosine methyltransferase converts 5-methylcytosine in DNA to thymine. Biochemistry. 34:1995;14752-14757.
    • (1995) Biochemistry , vol.34 , pp. 14752-14757
    • Yebra, M.J.1    Bhagwat, A.S.2
  • 49
    • 0035148664 scopus 로고    scopus 로고
    • Lowering S-adenosylmethionine levels in Escherichia coli modulates C-to-T transition mutations
    • Macintyre G., et al. Lowering S-adenosylmethionine levels in Escherichia coli modulates C-to-T transition mutations. J. Bacteriol. 183:2001;921-927.
    • (2001) J. Bacteriol. , vol.183 , pp. 921-927
    • Macintyre, G.1
  • 50
    • 0027278557 scopus 로고
    • Instability and decay of the primary structure of DNA
    • Lindahl T. Instability and decay of the primary structure of DNA. Nature. 362:1993;709-715.
    • (1993) Nature , vol.362 , pp. 709-715
    • Lindahl, T.1
  • 51
    • 0027970838 scopus 로고
    • Chromosomal translocations in human cancer
    • Rabbitts T.H. Chromosomal translocations in human cancer. Nature. 372:1994;143-149.
    • (1994) Nature , vol.372 , pp. 143-149
    • Rabbitts, T.H.1
  • 52
    • 0035839959 scopus 로고    scopus 로고
    • Mechanisms of chromosomal translocations in B cell lymphomas
    • Kuppers R., Dalla-Favera R. Mechanisms of chromosomal translocations in B cell lymphomas. Oncogene. 20:2001;5580-5594.
    • (2001) Oncogene , vol.20 , pp. 5580-5594
    • Kuppers, R.1    Dalla-Favera, R.2
  • 53
    • 0029159759 scopus 로고
    • Apolipoprotein B mRNA-editing protein induces hepatocellular carcinoma and dysplasia in transgenic animals
    • Yamanaka S., et al. Apolipoprotein B mRNA-editing protein induces hepatocellular carcinoma and dysplasia in transgenic animals. Proc. Natl. Acad. Sci. U. S. A. 92:1995;8483-8487.
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 8483-8487
    • Yamanaka, S.1
  • 54
    • 0000933459 scopus 로고
    • Replacement of thymidylic acid by deoxyuridylic acid in the deoxyribonucleic acid of a transducing phage for Bacillus subtilis
    • Takahashi L., Marmur J. Replacement of thymidylic acid by deoxyuridylic acid in the deoxyribonucleic acid of a transducing phage for Bacillus subtilis. Nature. 197:1963;794-795.
    • (1963) Nature , vol.197 , pp. 794-795
    • Takahashi, L.1    Marmur, J.2
  • 55
    • 0032522564 scopus 로고    scopus 로고
    • Ku80 is required for immunoglobulin isotype switching
    • Casellas R., et al. Ku80 is required for immunoglobulin isotype switching. EMBO J. 17:1998;2404-2411.
    • (1998) EMBO J. , vol.17 , pp. 2404-2411
    • Casellas, R.1
  • 56
    • 0032526290 scopus 로고    scopus 로고
    • Ku70 is required for late B cell development and immunoglobulin heavy chain class switching
    • Manis J.P., et al. Ku70 is required for late B cell development and immunoglobulin heavy chain class switching. J. Exp. Med. 187:1998;2081-2089.
    • (1998) J. Exp. Med. , vol.187 , pp. 2081-2089
    • Manis, J.P.1
  • 57
    • 0035369742 scopus 로고    scopus 로고
    • RNA editing by base deamination: More enzymes, more targets, new mysteries
    • Gerber A.P., Keller W. RNA editing by base deamination: more enzymes, more targets, new mysteries. Trends Biochem. Sci. 26:2001;376-384.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 376-384
    • Gerber, A.P.1    Keller, W.2
  • 58
    • 0028057520 scopus 로고
    • Cytidine deaminase. The 2.3 Å crystal structure of an enzyme:transition state analog complex
    • Betts L., et al. Cytidine deaminase. The 2.3 Å crystal structure of an enzyme:transition state analog complex. J. Mol. Biol. 235:1994;635-656.
    • (1994) J. Mol. Biol. , vol.235 , pp. 635-656
    • Betts, L.1
  • 59
    • 0037388165 scopus 로고    scopus 로고
    • Activation-induced cytidine deaminase deaminates deoxycytidine on single-stranded DNA but requires the action of RNase
    • Bransteitter R., et al. Activation-induced cytidine deaminase deaminates deoxycytidine on single-stranded DNA but requires the action of RNase. Proc. Natl. Acad. Sci. U. S. A. 100:2003;4102-4107.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 4102-4107
    • Bransteitter, R.1
  • 60
    • 0037452080 scopus 로고    scopus 로고
    • Transcription-targeted DNA deamination by the AID antibody diversification enzyme
    • Chaudhuri J., et al. Transcription-targeted DNA deamination by the AID antibody diversification enzyme. Nature. 422:2003;726-730.
    • (2003) Nature , vol.422 , pp. 726-730
    • Chaudhuri, J.1
  • 61
    • 0038293484 scopus 로고    scopus 로고
    • Transcription enhances AID-mediated cytidine deamination by exposing single-stranded DNA on the nontemplate strand
    • Ramiro A.R., et al. Transcription enhances AID-mediated cytidine deamination by exposing single-stranded DNA on the nontemplate strand. Nat. Immunol. 4:2003;452-456.
    • (2003) Nat. Immunol. , vol.4 , pp. 452-456
    • Ramiro, A.R.1
  • 62
    • 0038375028 scopus 로고    scopus 로고
    • In vitro deamination of cytosine to uracil in single-stranded DNA by APOBEC1
    • Petersen-Mahrt S.K., Neuberger M.S. In vitro deamination of cytosine to uracil in single-stranded DNA by APOBEC1. J. Biol. Chem. 278:2003;19583-19586.
    • (2003) J. Biol. Chem. , vol.278 , pp. 19583-19586
    • Petersen-Mahrt, S.K.1    Neuberger, M.S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.