메뉴 건너뛰기




Volumn , Issue , 2007, Pages 369-419

Chemistry, Phylogeny, and Three-Dimensional Structure of the APOBEC Protein Family

Author keywords

Nucleophilic aromatic substitution; Phylogenetic; Sequence driven analysis; Single stranded (ss) DNA

Indexed keywords


EID: 84889317673     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9780470262269.ch16     Document Type: Chapter
Times cited : (4)

References (198)
  • 1
    • 33846804438 scopus 로고    scopus 로고
    • Activation-induced cytidine deaminase (AID) promotes B cell lymphomagenesis in Emu-cmyc transgenic mice
    • Kotani, A., et al. (2007) Activation-induced cytidine deaminase (AID) promotes B cell lymphomagenesis in Emu-cmyc transgenic mice. Proc Natl Acad Sci USA 104 (5), 1616-1620.
    • (2007) Proc Natl Acad Sci USA , vol.104 , Issue.5 , pp. 1616-1620
    • Kotani, A.1
  • 2
    • 15444366646 scopus 로고    scopus 로고
    • A target selection of somatic hypermutations is regulated similarly between T and B cells upon activation-induced cytidine deaminase expression
    • Kotani, A., et al. (2005) A target selection of somatic hypermutations is regulated similarly between T and B cells upon activation-induced cytidine deaminase expression. Proc Natl Acad Sci USA 102 (12), 4506-4511.
    • (2005) Proc Natl Acad Sci USA , vol.102 , Issue.12 , pp. 4506-4511
    • Kotani, A.1
  • 3
    • 0037881911 scopus 로고    scopus 로고
    • Constitutive expression of AID leads to tumorigenesis
    • Okazaki, I. M., et al. (2003) Constitutive expression of AID leads to tumorigenesis. J Exp Med 197 (9), 1173-1181.
    • (2003) J Exp Med , vol.197 , Issue.9 , pp. 1173-1181
    • Okazaki, I.M.1
  • 4
    • 4644257592 scopus 로고    scopus 로고
    • AIDis required for c-myc/IgH chromosometranslocations in vivo
    • Ramiro, A. R., et al. (2004) AIDis required for c-myc/IgH chromosometranslocations in vivo. Cell 118 (4), 431-438.
    • (2004) Cell , vol.118 , Issue.4 , pp. 431-438
    • Ramiro, A.R.1
  • 5
    • 0029159759 scopus 로고
    • Apolipoprotein B mRNA-editing protein induces hepatocellular carcinoma and dysplasia in transgenic animals
    • Yamanaka, S., et al. (1995) Apolipoprotein B mRNA-editing protein induces hepatocellular carcinoma and dysplasia in transgenic animals. Proc Natl Acad Sci USA 92 (18), 8483-8487.
    • (1995) Proc Natl Acad Sci USA , vol.92 , Issue.18 , pp. 8483-8487
    • Yamanaka, S.1
  • 6
    • 0031048641 scopus 로고    scopus 로고
    • A novel translational repressor mRNA is edited extensively in livers containing tumors caused by the transgene expression of the apoB mRNA-editing enzyme
    • Yamanaka, S., et al. (1997) A novel translational repressor mRNA is edited extensively in livers containing tumors caused by the transgene expression of the apoB mRNA-editing enzyme. Genes Dev 11 (3), 321-333.
    • (1997) Genes Dev , vol.11 , Issue.3 , pp. 321-333
    • Yamanaka, S.1
  • 7
    • 0029670088 scopus 로고    scopus 로고
    • The neurofibromatosis type I messengerRNAundergoes base-modification RNA editing
    • Skuse, G. R., et al. (1996) The neurofibromatosis type I messengerRNAundergoes base-modification RNA editing. Nucleic Acids Res 24 (3), 478-485.
    • (1996) Nucleic Acids Res , vol.24 , Issue.3 , pp. 478-485
    • Skuse, G.R.1
  • 8
    • 0035480006 scopus 로고    scopus 로고
    • Human genetic defects in class-switch recombination (hyper-IgM syndromes)
    • Durandy, A. and Honjo, T. (2001) Human genetic defects in class-switch recombination (hyper-IgM syndromes). Curr Opin Immunol 13 (5), 543-548.
    • (2001) Curr Opin Immunol , vol.13 , Issue.5 , pp. 543-548
    • Durandy, A.1    Honjo, T.2
  • 9
    • 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. (2000) Activation-induced cytidine deaminase (AID) deficiency causes the autosomal recessive form of the Hyper-IgM syndrome (HIGM2). Cell 102 (5), 565-575.
    • (2000) Cell , vol.102 , Issue.5 , pp. 565-575
    • Revy, P.1
  • 10
    • 0037872240 scopus 로고    scopus 로고
    • Type two hyper-IgM syndrome caused by mutation in activation-induced cytidine deaminase
    • Zhu,Y., et al. (2003) Type two hyper-IgM syndrome caused by mutation in activation-induced cytidine deaminase. J Med Dent Sci 50 (1), 41-46.
    • (2003) J Med Dent Sci , vol.50 , Issue.1 , pp. 41-46
    • Zhu, Y.1
  • 11
    • 0028246560 scopus 로고
    • Mutations affecting transition-state stabilization by residues coordinating zinc at the active site of cytidine deaminase
    • Smith, A. A., et al. (1994) Mutations affecting transition-state stabilization by residues coordinating zinc at the active site of cytidine deaminase. Biochemistry 33 (21), 6468-6474.
    • (1994) Biochemistry , vol.33 , Issue.21 , pp. 6468-6474
    • Smith, A.A.1
  • 12
    • 0024332902 scopus 로고
    • Binding of pyrimidin-2-one ribonucleoside by cytidine deaminase as the transition-state analogue 3, 4-dihydrouridine and the contribution of the 4-hydroxyl group to its binding affinity
    • Frick, L., et al. (1989) Binding of pyrimidin-2-one ribonucleoside by cytidine deaminase as the transition-state analogue 3, 4-dihydrouridine and the contribution of the 4-hydroxyl group to its binding affinity. Biochemistry 28 (24), 9423-9430.
    • (1989) Biochemistry , vol.28 , Issue.24 , pp. 9423-9430
    • Frick, L.1
  • 13
    • 0028958685 scopus 로고
    • Transition-state selectivity for a single hydroxyl group during catalysis by cytidine deaminase
    • Xiang, S., et al. (1995) Transition-state selectivity for a single hydroxyl group during catalysis by cytidine deaminase. Biochemistry 34 (14), 4516-4523.
    • (1995) Biochemistry , vol.34 , Issue.14 , pp. 4516-4523
    • Xiang, S.1
  • 14
    • 0028057520 scopus 로고
    • Cytidine deaminas. The 2. 3 Å crystal structure of an enzyme: Transition-state analog complex
    • Betts, L., et al. (1994) Cytidine deaminas. The 2. 3 Å crystal structure of an enzyme: Transition-state analog complex. J Mol Biol 235 (2), 635-656.
    • (1994) J Mol Biol , vol.235 , Issue.2 , pp. 635-656
    • Betts, L.1
  • 15
    • 0028930864 scopus 로고
    • Major contribution of a carboxymethyl group to transition-state stabilization by cytidine deaminase: Mutation and rescue
    • Carlow, D. C., et al. (1995) Major contribution of a carboxymethyl group to transition-state stabilization by cytidine deaminase: Mutation and rescue. Biochemistry 34 (13), 4220-4224.
    • (1995) Biochemistry , vol.34 , Issue.13 , pp. 4220-4224
    • Carlow, D.C.1
  • 16
    • 0031901544 scopus 로고    scopus 로고
    • Statistical modelling and phylogenetic analysis of a deaminase domain
    • Mian, I. S., et al. (1998) Statistical modelling and phylogenetic analysis of a deaminase domain. J Comput Biol 5 (1), 57-72.
    • (1998) J Comput Biol , vol.5 , Issue.1 , pp. 57-72
    • Mian, I.S.1
  • 17
    • 0345270035 scopus 로고    scopus 로고
    • Messenger RNA editing in mammals: New members of the APOBEC family seeking roles in the family business
    • Wedekind, J. E., et al. (2003) Messenger RNA editing in mammals: New members of the APOBEC family seeking roles in the family business. Trends Genet 19 (4), 207-216.
    • (2003) Trends Genet , vol.19 , Issue.4 , pp. 207-216
    • Wedekind, J.E.1
  • 18
    • 0030049613 scopus 로고    scopus 로고
    • Cytidine deaminase complexed to 3-deazacytidine: A "valence buffer" in zinc enzyme catalysis
    • Xiang, S., et al. (1996) Cytidine deaminase complexed to 3-deazacytidine: A "valence buffer" in zinc enzyme catalysis. Biochemistry 35 (5), 1335-1341.
    • (1996) Biochemistry , vol.35 , Issue.5 , pp. 1335-1341
    • Xiang, S.1
  • 19
    • 0003717374 scopus 로고    scopus 로고
    • Biochemistry
    • 5th ed.,W.H. Freeman and Company, New York
    • Berg, J. M.,Tymoczko, J. L., and Stryer, L. (2002) Biochemistry, 5th ed.,W.H. Freeman and Company, New York, p. 894.
    • (2002) , pp. 894
    • Berg, J.M.1    Tymoczko, J.L.2    Stryer, L.3
  • 20
    • 2542542827 scopus 로고    scopus 로고
    • The structure of a yeast RNA-editing deaminase provide insight into the fold and function of activation-induced deaminase and APOBEC-1
    • Xie, K., et al. (2004) The structure of a yeast RNA-editing deaminase provide insight into the fold and function of activation-induced deaminase and APOBEC-1. Proc Natl Acad Sci USA 101 (21), 8114-8119.
    • (2004) Proc Natl Acad Sci USA , vol.101 , Issue.21 , pp. 8114-8119
    • Xie, K.1
  • 21
    • 0022706389 scopus 로고
    • The relation between the divergence of sequence and structure in proteins
    • Chothia, C., and Lesk, A. M. (1986) The relation between the divergence of sequence and structure in proteins. EMBO J 5 (4), 823-826.
    • (1986) EMBO J , vol.5 , Issue.4 , pp. 823-826
    • Chothia, C.1    Lesk, A.M.2
  • 22
    • 0033873929 scopus 로고    scopus 로고
    • Comparative protein structure modeling of genes and genomes
    • Marti-Renom, M. A., et al. (2000) Comparative protein structure modeling of genes and genomes. Annu Rev Biophys Biomol Struct 29, 291-325.
    • (2000) Annu Rev Biophys Biomol Struct , vol.29 , pp. 291-325
    • Marti-Renom, M.A.1
  • 23
    • 0033954256 scopus 로고    scopus 로고
    • The Protein Data Bank
    • Berman, H. M., et al. (2000) The Protein Data Bank. Nucleic Acids Res 28 (1), 235-242.
    • (2000) Nucleic Acids Res , vol.28 , Issue.1 , pp. 235-242
    • Berman, H.M.1
  • 25
    • 0023176681 scopus 로고
    • Determinants of a protein fold: Unique features of the globin amino acid sequences
    • Bashford, D., Chothia, C., and Lesk, A. M. (1987) Determinants of a protein fold: Unique features of the globin amino acid sequences. J Mol Biol 196, 199-216.
    • (1987) J Mol Biol , vol.196 , pp. 199-216
    • Bashford, D.1    Chothia, C.2    Lesk, A.M.3
  • 26
    • 0025753142 scopus 로고
    • Similarity of the three-dimensional structures of actin and the ATPase fragment of a 70-kDa heat shock cognate protein
    • Flaherty, K. M., et al. (1991) Similarity of the three-dimensional structures of actin and the ATPase fragment of a 70-kDa heat shock cognate protein. Proc Natl Acad Sci USA 88, 5041-5045.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 5041-5045
    • Flaherty, K.M.1
  • 27
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • Holm, L. and Sander, C. (1993) Protein structure comparison by alignment of distance matrices. J Mol Biol 233 (1), 123-138.
    • (1993) J Mol Biol , vol.233 , Issue.1 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 28
    • 25444527785 scopus 로고    scopus 로고
    • APOBEC4, a newmember of the AID/APOBEC family of polynucleotide (deoxy)cytidine deaminases predicted by computational analysis
    • Rogozin, I. B., et al. (2005) APOBEC4, a newmember of the AID/APOBEC family of polynucleotide (deoxy)cytidine deaminases predicted by computational analysis. Cell Cycle 4 (9), 1281-1285.
    • (2005) Cell Cycle , vol.4 , Issue.9 , pp. 1281-1285
    • Rogozin, I.B.1
  • 29
    • 0031665423 scopus 로고    scopus 로고
    • Evolutionaryanalysis ofRNAediting enzymes
    • Chang, B. H.andChan, L. (1998)Evolutionaryanalysis ofRNAediting enzymes. Methods 15(1),41-50.
    • (1998) Methods , vol.15 , Issue.1 , pp. 41-50
    • Chang, B.H.1    Chan, L.2
  • 30
    • 27744488568 scopus 로고    scopus 로고
    • Heterotachy and long-branch attraction in phylogenetics
    • Philippe, H., et al. (2005)Heterotachy and long-branch attraction in phylogenetics. BMCEvol Biol 5, 50.
    • (2005) BMCEvol Biol , vol.5 , pp. 50
    • Philippe, H.1
  • 31
    • 11844269804 scopus 로고    scopus 로고
    • Evolution of the AID/APOBEC family of polynucleotide (deoxy) cytidine deaminases
    • Conticello, S. G., et al. (2005) Evolution of the AID/APOBEC family of polynucleotide (deoxy) cytidine deaminases. Mol Biol Evol 22 (2), 367-377.
    • (2005) Mol Biol Evol , vol.22 , Issue.2 , pp. 367-377
    • Conticello, S.G.1
  • 32
    • 0032499630 scopus 로고    scopus 로고
    • Complexes of adenosine deaminase with two potent inhibitors: X-ray structures in four independent molecules at pH of maximum activity
    • Wang, Z. and Quiocho, F. A. (1998) Complexes of adenosine deaminase with two potent inhibitors: X-ray structures in four independent molecules at pH of maximum activity. Biochemistry 37 (23), 8314-8324.
    • (1998) Biochemistry , vol.37 , Issue.23 , pp. 8314-8324
    • Wang, Z.1    Quiocho, F.A.2
  • 33
    • 0036304598 scopus 로고    scopus 로고
    • The structure of Escherichia coli cytosine deaminase
    • Ireton, G. C., et al. (2002) The structure of Escherichia coli cytosine deaminase. J Mol Biol 315 (4), 687-697.
    • (2002) J Mol Biol , vol.315 , Issue.4 , pp. 687-697
    • Ireton, G.C.1
  • 34
    • 0029874435 scopus 로고    scopus 로고
    • Aleft-hand beta-helix revealed by the crystal structure of a carbonic anhydrase from the archeon Methanosarcina thermophila
    • Kisker, C., et al. (1996) Aleft-hand beta-helix revealed by the crystal structure of a carbonic anhydrase from the archeon Methanosarcina thermophila. EMBO J 15, 2323-2330.
    • (1996) EMBO J , vol.15 , pp. 2323-2330
    • Kisker, C.1
  • 35
    • 0033162769 scopus 로고    scopus 로고
    • Molecular modelling of the biosynthesis of the RNAediting enzyme APOBEC-1, responsible for generating the alternative forms of apolipoprotein B
    • Scott, J., Navaratnam, N., and Carter, C. (1999) Molecular modelling of the biosynthesis of the RNAediting enzyme APOBEC-1, responsible for generating the alternative forms of apolipoprotein B. Exp Physiol 84 (4), 791-800.
    • (1999) Exp Physiol , vol.84 , Issue.4 , pp. 791-800
    • Scott, J.1    Navaratnam, N.2    Carter, C.3
  • 36
    • 0002756315 scopus 로고    scopus 로고
    • Nucleoside Deaminase for Cytidine and Adenosine: Comparison with Deaminases Acting on RNA
    • In: Grosjean, H. and Benne, R. (eds), In Modification and Editing of RNA, ASM Press,Washington, D.C
    • Carter, C. W. Jr. (1998) In: Grosjean, H. and Benne, R. (eds), Nucleoside Deaminase for Cytidine and Adenosine: Comparison with Deaminases Acting on RNA. In Modification and Editing of RNA, ASM Press,Washington, D.C., pp. 591-596.
    • (1998) , pp. 591-596
    • Carter Jr, C.W.1
  • 37
    • 0036200070 scopus 로고    scopus 로고
    • An anthropoid-specific locus of orphan C to U RNA-editing enzymes on chromosome 22
    • Jarmuz, A., et al. (2002) An anthropoid-specific locus of orphan C to U RNA-editing enzymes on chromosome 22. Genomics 79 (3), 285-296.
    • (2002) Genomics , vol.79 , Issue.3 , pp. 285-296
    • Jarmuz, A.1
  • 38
    • 15744390742 scopus 로고    scopus 로고
    • The retroviral hypermutation specificity of APOBEC3F and APOBEC3G is governed by the C-terminal DNA cytosine deaminase domain
    • Hache, G., Liddament, M. T., and Harris, R. S. (2005) The retroviral hypermutation specificity of APOBEC3F and APOBEC3G is governed by the C-terminal DNA cytosine deaminase domain. J Biol Chem 280 (12), 10920-10924.
    • (2005) J Biol Chem , vol.280 , Issue.12 , pp. 10920-10924
    • Hache, G.1    Liddament, M.T.2    Harris, R.S.3
  • 39
    • 12544256041 scopus 로고    scopus 로고
    • Antiviral function of APOBEC3G can be dissociated from cytidine deaminase activity
    • Newman, E. N., et al. (2005) Antiviral function of APOBEC3G can be dissociated from cytidine deaminase activity. Curr Biol 15 (2), 166-170.
    • (2005) Curr Biol , vol.15 , Issue.2 , pp. 166-170
    • Newman, E.N.1
  • 40
    • 13844270834 scopus 로고    scopus 로고
    • Complementary function of the two catalytic domains of APOBEC3G
    • Navarro, F., et al. (2005) Complementary function of the two catalytic domains of APOBEC3G. Virology 333 (2), 374-386.
    • (2005) Virology , vol.333 , Issue.2 , pp. 374-386
    • Navarro, F.1
  • 41
    • 0037176913 scopus 로고    scopus 로고
    • Crystal structure of the tetrameric cytidine deaminase from Bacillus subtilis at 2.0 Å resolution
    • Johansson, E., et al. (2002) Crystal structure of the tetrameric cytidine deaminase from Bacillus subtilis at 2.0 Å resolution. Biochemistry 41 (8), 2563-2570.
    • (2002) Biochemistry , vol.41 , Issue.8 , pp. 2563-2570
    • Johansson, E.1
  • 42
    • 13444265938 scopus 로고    scopus 로고
    • Structure of human cytidine deaminase bound to a potent inhibitor
    • Chung, S. J., Fromme, J. C., andVerdine, G. L. (2005) Structure of human cytidine deaminase bound to a potent inhibitor. J Med Chem 48 (3), 658-660.
    • (2005) J Med Chem , vol.48 , Issue.3 , pp. 658-660
    • Chung, S.J.1    Fromme, J.C.2    Verdine, G.L.3
  • 43
    • 33746917191 scopus 로고    scopus 로고
    • The 1.48 Å resolution crystal structure of the homotetrameric cytidine deaminase from mouse
    • Teh, A. H., et al. (2006) The 1.48 Å resolution crystal structure of the homotetrameric cytidine deaminase from mouse. Biochemistry 45 (25), 7825-7833.
    • (2006) Biochemistry , vol.45 , Issue.25 , pp. 7825-7833
    • Teh, A.H.1
  • 44
    • 0032822048 scopus 로고    scopus 로고
    • New insights into the pyrimidine salvage pathway of Saccharomyces cerevisiae: Requirement of six genes for cytidine metabolism
    • Kurtz, J. E., et al. (1999) New insights into the pyrimidine salvage pathway of Saccharomyces cerevisiae: Requirement of six genes for cytidine metabolism. Curr Genet 36 (3), 130-136.
    • (1999) Curr Genet , vol.36 , Issue.3 , pp. 130-136
    • Kurtz, J.E.1
  • 45
    • 0035870689 scopus 로고    scopus 로고
    • Identification of the yeast cytidine deaminase CDD1 as an orphan C!U RNA editase
    • Dance, G. S., et al. (2001) Identification of the yeast cytidine deaminase CDD1 as an orphan C!U RNA editase. Nucleic Acids Res 29 (8), 1772-1780.
    • (2001) Nucleic Acids Res , vol.29 , Issue.8 , pp. 1772-1780
    • Dance, G.S.1
  • 46
    • 0031019881 scopus 로고    scopus 로고
    • Tissue-specific inhibition of apolipoprotein B mRNA editing in the liver by adenovirus-mediated transfer of a dominant negative mutant APOBEC-1leads to increased lowdensity lipoprotein in mice
    • Oka, K., et al. (1997) Tissue-specific inhibition of apolipoprotein B mRNA editing in the liver by adenovirus-mediated transfer of a dominant negative mutant APOBEC-1leads to increased lowdensity lipoprotein in mice. J Biol Chem 272 (3), 1456-1460.
    • (1997) J Biol Chem , vol.272 , Issue.3 , pp. 1456-1460
    • Oka, K.1
  • 47
    • 0036863733 scopus 로고    scopus 로고
    • RNAediting enzymeAPOBEC1and some of its homologs can act as DNA mutators
    • Harris, R. S., Petersen-Mahrt, S. K., and Neuberger, M. S. (2002) RNAediting enzymeAPOBEC1and some of its homologs can act as DNA mutators. Mol Cell 10 (5), 1247-1253.
    • (2002) Mol Cell , vol.10 , Issue.5 , pp. 1247-1253
    • Harris, R.S.1    Petersen-Mahrt, S.K.2    Neuberger, M.S.3
  • 48
    • 0037019315 scopus 로고    scopus 로고
    • AIDmutates E. coli suggesting aDNA deamination mechanism for antibody diversification
    • Petersen-Mahrt, S. K., Harris, R. S., and Neuberger,M. S. (2002) AIDmutates E. coli suggesting aDNA deamination mechanism for antibody diversification. Nature 418 (6893), 99-103.
    • (2002) Nature , vol.418 , Issue.6893 , pp. 99-103
    • Petersen-Mahrt, S.K.1    Harris, R.S.2    Neuberger, M.S.3
  • 49
    • 84889431071 scopus 로고    scopus 로고
    • Fine-tuning of RNA functions by modification and editing in mammalian C to U editing
    • In: Grosjean H. (ed.), Topics in Current Genetics, Springer-Verlag, Berlin
    • Smith, H. C., Wedekind, J. E., Xie, K., and Sowden, M. P. (2005) Fine-tuning of RNA functions by modification and editing in mammalian C to U editing. In: Grosjean H. (ed.), Topics in Current Genetics, Springer-Verlag, Berlin, pp. 1610-2096.
    • (2005) , pp. 1610-2096
    • Smith, H.C.1    Wedekind, J.E.2    Xie, K.3    Sowden, M.P.4
  • 50
    • 0347382597 scopus 로고    scopus 로고
    • Domainorganization of activation-induced cytidine deaminase
    • author reply on
    • Zaim, J. and Kierzek, A. M.(2003)Domainorganization of activation-induced cytidine deaminase. Nat Immunol 4 (12), author reply on p. 1153-1154.
    • (2003) Nat Immunol , vol.4 , Issue.12 , pp. 1153-1154
    • Zaim, J.1    Kierzek, A.M.2
  • 51
    • 33646365634 scopus 로고    scopus 로고
    • Crystal structure of a bifunctional deaminase and reductase from Bacillus subtilis involved in riboflavin biosynthesis
    • Chen, S. C., et al. (2006) Crystal structure of a bifunctional deaminase and reductase from Bacillus subtilis involved in riboflavin biosynthesis. J Biol Chem 281 (11), 7605-7613.
    • (2006) J Biol Chem , vol.281 , Issue.11 , pp. 7605-7613
    • Chen, S.C.1
  • 52
    • 33846555779 scopus 로고    scopus 로고
    • The APOBEC-2 crystal structure and functional implications for the deaminase AID
    • Prochnow, C., et al. (2007) The APOBEC-2 crystal structure and functional implications for the deaminase AID. Nature 445 (7126), 447-451.
    • (2007) Nature , vol.445 , Issue.7126 , pp. 447-451
    • Prochnow, C.1
  • 53
    • 0028961335 scopus 로고
    • SCOP:Astructural classification of proteins database for the investigation of sequences and structures
    • Murzin, A. G., et al. (1995) SCOP:Astructural classification of proteins database for the investigation of sequences and structures. J Mol Biol 247 (4), 536-540.
    • (1995) J Mol Biol , vol.247 , Issue.4 , pp. 536-540
    • Murzin, A.G.1
  • 54
    • 24644519954 scopus 로고    scopus 로고
    • Inositol hexakisphosphate is bound in the ADAR2 core and required for RNA editing
    • Macbeth, M. R., et al. (2005) Inositol hexakisphosphate is bound in the ADAR2 core and required for RNA editing. Science 309 (5740), 1534-1539.
    • (2005) Science , vol.309 , Issue.5740 , pp. 1534-1539
    • Macbeth, M.R.1
  • 55
    • 33646888184 scopus 로고    scopus 로고
    • Structural and kinetic characterization of Escherichia coli TadA, the wobblespecific tRNA deaminase
    • Kim, J., et al. (2006) Structural and kinetic characterization of Escherichia coli TadA, the wobblespecific tRNA deaminase. Biochemistry 45 (20), 6407-6416.
    • (2006) Biochemistry , vol.45 , Issue.20 , pp. 6407-6416
    • Kim, J.1
  • 56
    • 34247111953 scopus 로고    scopus 로고
    • Identification of amino acid residues inAPOBEC3Grequired for regulation by human immunodeficiency virus type 1 Vif and Virion encapsidation
    • Huthoff, H., and Malim, M. H. (2007) Identification of amino acid residues inAPOBEC3Grequired for regulation by human immunodeficiency virus type 1 Vif and Virion encapsidation. J Virol 81 (8), 3807-3815.
    • (2007) J Virol , vol.81 , Issue.8 , pp. 3807-3815
    • Huthoff, H.1    Malim, M.H.2
  • 57
    • 0344413641 scopus 로고    scopus 로고
    • The antiretroviral enzyme APOBEC3G is degraded by the proteasome in response to HIV-1 Vif
    • Sheehy, A. M., Gaddis, N. C., and Malim, M. H. (2003) The antiretroviral enzyme APOBEC3G is degraded by the proteasome in response to HIV-1 Vif. Nat Med 9 (11), 1404-1407.
    • (2003) Nat Med , vol.9 , Issue.11 , pp. 1404-1407
    • Sheehy, A.M.1    Gaddis, N.C.2    Malim, M.H.3
  • 58
    • 22544465590 scopus 로고    scopus 로고
    • Regulation of Apobec3F and human immunodeficiency virus type 1 Vif by Vif-Cul5-ElonB/C E3 ubiquitin ligase
    • Liu, B., et al. (2005) Regulation of Apobec3F and human immunodeficiency virus type 1 Vif by Vif-Cul5-ElonB/C E3 ubiquitin ligase. J Virol 79 (15), p. 9579-9587.
    • (2005) J Virol , vol.79 , Issue.15 , pp. 9579-9587
    • Liu, B.1
  • 59
    • 7244249940 scopus 로고    scopus 로고
    • Three-dimensional structure of the R115E mutant of T4-bacteriophage 20-deoxycytidylate deaminase
    • Almog, R., et al. (2004) Three-dimensional structure of the R115E mutant of T4-bacteriophage 20-deoxycytidylate deaminase. Biochemistry 43 (43), 13715-13723.
    • (2004) Biochemistry , vol.43 , Issue.43 , pp. 13715-13723
    • Almog, R.1
  • 60
    • 0031658826 scopus 로고    scopus 로고
    • Drug resistance to 5-aza-20-deoxycytidine, 20,20-difluorodeoxycytidine, and cytosine arabinoside conferred by retroviral-mediated transfer of human cytidine deaminase cDNA into murine cells
    • Eliopoulos, N., Cournoyer, D., and Momparler, R. L. (1998) Drug resistance to 5-aza-20-deoxycytidine, 20,20-difluorodeoxycytidine, and cytosine arabinoside conferred by retroviral-mediated transfer of human cytidine deaminase cDNA into murine cells. Cancer Chemother Pharmacol 42 (5), 373-378.
    • (1998) Cancer Chemother Pharmacol , vol.42 , Issue.5 , pp. 373-378
    • Eliopoulos, N.1    Cournoyer, D.2    Momparler, R.L.3
  • 61
    • 0035123128 scopus 로고    scopus 로고
    • Gene directed enzyme/prodrug therapy of cancer: Historical appraisal and future prospectives
    • Greco, O. and Dachs, G. U. (2001) Gene directed enzyme/prodrug therapy of cancer: Historical appraisal and future prospectives. J Cell Physiol 187 (1), 22-36.
    • (2001) J Cell Physiol , vol.187 , Issue.1 , pp. 22-36
    • Greco, O.1    Dachs, G.U.2
  • 62
    • 0037220313 scopus 로고    scopus 로고
    • Assessment of the effect of phosphorylated metabolites of anti-human immunodeficiency virus and anti-hepatitis B virus pyrimidine analogs on the behavior of human deoxycytidylate deaminase
    • Liou, J. Y., et al. (2003) Assessment of the effect of phosphorylated metabolites of anti-human immunodeficiency virus and anti-hepatitis B virus pyrimidine analogs on the behavior of human deoxycytidylate deaminase. Mol Pharmacol 63 (1), 105-110.
    • (2003) Mol Pharmacol , vol.63 , Issue.1 , pp. 105-110
    • Liou, J.Y.1
  • 63
    • 0029987826 scopus 로고    scopus 로고
    • Arterial therapy of hepatic colorectal metastases
    • Vauthey, J. N., et al. (1996) Arterial therapy of hepatic colorectal metastases. Br J Surg 83 (4), 447-455.
    • (1996) Br J Surg , vol.83 , Issue.4 , pp. 447-455
    • Vauthey, J.N.1
  • 64
    • 0038482076 scopus 로고    scopus 로고
    • Crystal structure of yeast cytosine deaminase. Insights into enzyme mechanism and evolution
    • Ko, T. P., et al. (2003) Crystal structure of yeast cytosine deaminase. Insights into enzyme mechanism and evolution. J Biol Chem 278 (21), 19111-19117.
    • (2003) J Biol Chem , vol.278 , Issue.21 , pp. 19111-19117
    • Ko, T.P.1
  • 65
    • 4143081742 scopus 로고    scopus 로고
    • Crystal structure of Bacillus subtilis guanine deaminase: The first domainswapped structure in the cytidine deaminase superfamily
    • Liaw, S. H., et al. (2004) Crystal structure of Bacillus subtilis guanine deaminase: The first domainswapped structure in the cytidine deaminase superfamily. J Biol Chem 279 (34), 35479-35485.
    • (2004) J Biol Chem , vol.279 , Issue.34 , pp. 35479-35485
    • Liaw, S.H.1
  • 66
    • 18144392611 scopus 로고    scopus 로고
    • Crystal structure of tRNA adenosine deaminase (TadA) from Aquifex aeolicus
    • Kuratani, M., et al. (2005) Crystal structure of tRNA adenosine deaminase (TadA) from Aquifex aeolicus. J Biol Chem 280 (16), 16002-16008.
    • (2005) J Biol Chem , vol.280 , Issue.16 , pp. 16002-16008
    • Kuratani, M.1
  • 67
    • 0028077637 scopus 로고
    • Refined structure of dimeric diphtheria toxin at 2
    • Bennett, M. J., Choe, S., and Eisenberg, D. (1994) Refined structure of dimeric diphtheria toxin at 2. 0 A resolution. Protein Sci 3 (9), 1444-1463.
    • (1994) 0 A resolution. Protein Sci , vol.3 , Issue.9 , pp. 1444-1463
    • Bennett, M.J.1    Choe, S.2    Eisenberg, D.3
  • 68
    • 0036108484 scopus 로고    scopus 로고
    • 3Ddomain swapping: Asdomains continue to swap
    • Liu,Y. and Eisenberg, D. (2002) 3Ddomain swapping: Asdomains continue to swap. Protein Sci 11 (6), 1285-1299.
    • (2002) Protein Sci , vol.11 , Issue.6 , pp. 1285-1299
    • Liu, Y.1    Eisenberg, D.2
  • 69
    • 0028222099 scopus 로고
    • Identification of a site necessary for allosteric regulation in T4-phage deoxycytidylate deaminase
    • Moore, J. T., et al. (1994) Identification of a site necessary for allosteric regulation in T4-phage deoxycytidylate deaminase. Biochemistry 33 (8), 2104-2112.
    • (1994) Biochemistry , vol.33 , Issue.8 , pp. 2104-2112
    • Moore, J.T.1
  • 70
    • 0034724722 scopus 로고    scopus 로고
    • A T4-phage deoxycytidylate deaminase mutant that no longer requires deoxycytidine 50-triphosphate for activation
    • Keefe, R. G., et al. (2000) A T4-phage deoxycytidylate deaminase mutant that no longer requires deoxycytidine 50-triphosphate for activation. J Biol Chem 275 (17), 12598-12602.
    • (2000) J Biol Chem , vol.275 , Issue.17 , pp. 12598-12602
    • Keefe, R.G.1
  • 71
    • 0037196419 scopus 로고    scopus 로고
    • Mechanismof oligomerization of Escherichia coli carbamoyl phosphate synthetase and modulation by the allosteric effectors. A site-directed mutagenesis study
    • Mora,P., Rubio,V., and Cervera, J. (2002)Mechanismof oligomerization of Escherichia coli carbamoyl phosphate synthetase and modulation by the allosteric effectors. A site-directed mutagenesis study. FEBS Lett 511 (1-3), 6-10.
    • (2002) FEBS Lett , vol.511 , Issue.1-3 , pp. 6-10
    • Mora, P.1    Rubio, V.2    Cervera, J.3
  • 72
    • 0037080335 scopus 로고    scopus 로고
    • A comprehensive model for the allosteric regulation of mammalian ribonucleotide reductase. Functional consequences of ATP-and dATP-induced oligomerization of the large subunit
    • Kashlan, O. B., et al. (2002) A comprehensive model for the allosteric regulation of mammalian ribonucleotide reductase. Functional consequences of ATP-and dATP-induced oligomerization of the large subunit. Biochemistry 41 (2), 462-474.
    • (2002) Biochemistry , vol.41 , Issue.2 , pp. 462-474
    • Kashlan, O.B.1
  • 73
    • 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. (2003) Activation-induced cytidine deaminase deaminates deoxycytidine on single-stranded DNA but requires the action of RNase. Proc Natl Acad Sci USA 100 (7), 4102-4107.
    • (2003) Proc Natl Acad Sci USA , vol.100 , Issue.7 , pp. 4102-4107
    • Bransteitter, R.1
  • 74
    • 33847246310 scopus 로고    scopus 로고
    • Newly synthesizedAPOBEC3Gis incorporated into HIV virions, inhibited by HIV RNA, and subsequently activated by RNase H
    • Soros,V. B.,Yonemoto,W., and Greene,W. C., (2007)Newly synthesizedAPOBEC3Gis incorporated into HIV virions, inhibited by HIV RNA, and subsequently activated by RNase H. PLoS Pathog 3 (2), e15.
    • (2007) PLoS Pathog , vol.3 , Issue.2
    • Soros, V.B.1    Yonemoto, W.2    Greene, W.C.3
  • 75
    • 0003187567 scopus 로고    scopus 로고
    • The atomic structure of protein-protein recognition sites
    • Lo Conte, L., Chothia, C., and Janin, J. (1999) The atomic structure of protein-protein recognition sites. J Mol Biol 285 (5), 2177-2198.
    • (1999) J Mol Biol , vol.285 , Issue.5 , pp. 2177-2198
    • Lo Conte, L.1    Chothia, C.2    Janin, J.3
  • 76
    • 2342441325 scopus 로고    scopus 로고
    • Crystal structures of human bifunctional enzyme aminoimidazole-4-carboxamide ribonucleotide transformylase/IMP cyclohydrolase in complex with potent sulfonylcontaining antifolates
    • Cheong, C. G., et al. (2004) Crystal structures of human bifunctional enzyme aminoimidazole-4-carboxamide ribonucleotide transformylase/IMP cyclohydrolase in complex with potent sulfonylcontaining antifolates. J Biol Chem 279 (17), 18034-18045.
    • (2004) J Biol Chem , vol.279 , Issue.17 , pp. 18034-18045
    • Cheong, C.G.1
  • 77
    • 10744223020 scopus 로고    scopus 로고
    • Adenosine deaminases acting on RNA (ADARs): RNA-editing enzymes
    • Keegan, L. P., et al. (2004) Adenosine deaminases acting on RNA (ADARs): RNA-editing enzymes. Genome Biol 5 (2), 209.
    • (2004) Genome Biol , vol.5 , Issue.2 , pp. 209
    • Keegan, L.P.1
  • 78
    • 0014942572 scopus 로고
    • Structure of lactate dehydrogenase at 2-8Åresolution
    • Adams, M. J., et al. (1970) Structure of lactate dehydrogenase at 2-8Åresolution. Nature 227 (5263), 1098-1103.
    • (1970) Nature , vol.227 , Issue.5263 , pp. 1098-1103
    • Adams, M.J.1
  • 79
    • 0014945069 scopus 로고
    • The structure of the nicotinamide-adenine dinucleotide coenzyme when bound to lactate dehydrogenase
    • Adams, M. J., et al. (1970) The structure of the nicotinamide-adenine dinucleotide coenzyme when bound to lactate dehydrogenase. J Mol Biol 51 (1), 31-38.
    • (1970) J Mol Biol , vol.51 , Issue.1 , pp. 31-38
    • Adams, M.J.1
  • 80
    • 31344462177 scopus 로고    scopus 로고
    • Conformational diversity of ligands bound to proteins
    • Stockwell, G. R. and Thornton, J. M. (2006) Conformational diversity of ligands bound to proteins. J Mol Biol 356 (4), 928-944.
    • (2006) J Mol Biol , vol.356 , Issue.4 , pp. 928-944
    • Stockwell, G.R.1    Thornton, J.M.2
  • 81
    • 0030946770 scopus 로고    scopus 로고
    • Biosynthesis of riboflavin: Characterization of the bifunctional deaminasereductase of Escherichia coli and Bacillus subtilis
    • Richter, G., et al. (1997) Biosynthesis of riboflavin: Characterization of the bifunctional deaminasereductase of Escherichia coli and Bacillus subtilis. J Bacteriol 179 (6), 2022-2028.
    • (1997) J Bacteriol , vol.179 , Issue.6 , pp. 2022-2028
    • Richter, G.1
  • 82
    • 0037592977 scopus 로고    scopus 로고
    • Requirement of dimerization forRNAediting activity of adenosine deaminases acting on RNA
    • Cho, D. S., et al. (2003) Requirement of dimerization forRNAediting activity of adenosine deaminases acting on RNA. J Biol Chem 278 (19), 17093-17102.
    • (2003) J Biol Chem , vol.278 , Issue.19 , pp. 17093-17102
    • Cho, D.S.1
  • 83
    • 0037587631 scopus 로고    scopus 로고
    • An ADAR that edits transcripts encoding ion channel subunits functions as a dimer
    • Gallo, A., et al. (2003) An ADAR that edits transcripts encoding ion channel subunits functions as a dimer. EMBO J 22 (13), 3421-3430.
    • (2003) EMBO J , vol.22 , Issue.13 , pp. 3421-3430
    • Gallo, A.1
  • 84
    • 33745202288 scopus 로고    scopus 로고
    • FRET analysis of in vivo dimerization by RNA-editing enzymes
    • Chilibeck, K. A., et al. (2006) FRET analysis of in vivo dimerization by RNA-editing enzymes. J Biol Chem 281 (24), 16530-16535.
    • (2006) J Biol Chem , vol.281 , Issue.24 , pp. 16530-16535
    • Chilibeck, K.A.1
  • 85
    • 34447542355 scopus 로고    scopus 로고
    • RNA-Binding independent dimerization of ADAR and dominant negative effects of nonfunctional subunits on dimer functions
    • Valente, L. and Nishikura, K. (2007) RNA-Binding independent dimerization of ADAR and dominant negative effects of nonfunctional subunits on dimer functions. J Biol Chem 282 (22), 16054-16061.
    • (2007) J Biol Chem , vol.282 , Issue.22 , pp. 16054-16061
    • Valente, L.1    Nishikura, K.2
  • 86
    • 12644303230 scopus 로고    scopus 로고
    • The enolase superfamily: A general strategy for enzyme-catalyzed abstraction of the alpha-protons of carboxylic acids
    • Babbitt, P. C., et al. (1996) The enolase superfamily: A general strategy for enzyme-catalyzed abstraction of the alpha-protons of carboxylic acids. Biochemistry 35 (51), 16489-16501.
    • (1996) Biochemistry , vol.35 , Issue.51 , pp. 16489-16501
    • Babbitt, P.C.1
  • 87
    • 0025284257 scopus 로고
    • The evolution of alpha/beta barrel enzymes
    • Farber, G. K. and Petsko, G. A. (1990) The evolution of alpha/beta barrel enzymes. Trends Biochem Sci 15 (6), 228-234.
    • (1990) Trends Biochem Sci , vol.15 , Issue.6 , pp. 228-234
    • Farber, G.K.1    Petsko, G.A.2
  • 88
    • 84889411590 scopus 로고    scopus 로고
    • Measuring editing activity and identifyingCtoUmRNAediting factors in cells and biochemical isolates
    • In: Gott J. M. (ed.), In: Methods in Enzymology, RNA Editing & Modification, Academic Press, New York
    • Smith, H. C. (2007) Measuring editing activity and identifyingCtoUmRNAediting factors in cells and biochemical isolates. In: Gott J. M. (ed.), In: Methods in Enzymology, RNA Editing & Modification, Academic Press, New York, pp. 390-419.
    • (2007) , pp. 390-419
    • Smith, H.C.1
  • 89
    • 0034650495 scopus 로고    scopus 로고
    • APOBEC-1dependent cytidine to uridine editing of apolipoproteinBRNAin yeast
    • Dance, G. S., et al. (2000) APOBEC-1dependent cytidine to uridine editing of apolipoproteinBRNAin yeast. Nucleic Acids Res 28 (2), 424-429.
    • (2000) Nucleic Acids Res , vol.28 , Issue.2 , pp. 424-429
    • Dance, G.S.1
  • 90
    • 15844373417 scopus 로고    scopus 로고
    • Hyperediting of multiple cytidines of apolipoprotein B mRNA by APOBEC-1 requires auxiliary protein(s) but not a mooring sequence motif
    • Yamanaka, S., et al. (1996) Hyperediting of multiple cytidines of apolipoprotein B mRNA by APOBEC-1 requires auxiliary protein(s) but not a mooring sequence motif. J Biol Chem 271 (19), 11506-11510.
    • (1996) J Biol Chem , vol.271 , Issue.19 , pp. 11506-11510
    • Yamanaka, S.1
  • 91
    • 0033544013 scopus 로고    scopus 로고
    • Disproportionate relationship between APOBEC-1 expression and apolipoprotein B mRNA editing activity
    • Siddiqui, J. F., et al. (1999) Disproportionate relationship between APOBEC-1 expression and apolipoprotein B mRNA editing activity. Exp Cell Res 252 (1), 154-164.
    • (1999) Exp Cell Res , vol.252 , Issue.1 , pp. 154-164
    • Siddiqui, J.F.1
  • 92
    • 0030020790 scopus 로고    scopus 로고
    • Overexpression of APOBEC-1 results in mooring sequence-dependent promiscuous RNA editing
    • Sowden, M., Hamm, J. K., and Smith, H. C. (1996) Overexpression of APOBEC-1 results in mooring sequence-dependent promiscuous RNA editing. J Biol Chem 271 (6), 3011-3017.
    • (1996) J Biol Chem , vol.271 , Issue.6 , pp. 3011-3017
    • Sowden, M.1    Hamm, J.K.2    Smith, H.C.3
  • 93
    • 0032052265 scopus 로고    scopus 로고
    • Apolipoprotein B RNA sequence 30 of the mooring sequence and cellular sources of auxiliary factors determine the location and extent of promiscuous editing
    • Sowden, M. P., Eagleton, M. J., and Smith, H. C. (1998) Apolipoprotein B RNA sequence 30 of the mooring sequence and cellular sources of auxiliary factors determine the location and extent of promiscuous editing. Nucleic Acids Res 26 (7), 1644-1652.
    • (1998) Nucleic Acids Res , vol.26 , Issue.7 , pp. 1644-1652
    • Sowden, M.P.1    Eagleton, M.J.2    Smith, H.C.3
  • 94
    • 32244445417 scopus 로고    scopus 로고
    • Crystal structure of Staphylococcus aureus tRNA adenosine deaminase TadA in complex with RNA
    • Losey, H. C., Ruthenburg, A. J., and Verdine, G. L. (2006) Crystal structure of Staphylococcus aureus tRNA adenosine deaminase TadA in complex with RNA. Nat Struct Mol Biol 13 (2), 153-159.
    • (2006) Nat Struct Mol Biol , vol.13 , Issue.2 , pp. 153-159
    • Losey, H.C.1    Ruthenburg, A.J.2    Verdine, G.L.3
  • 95
    • 0034633941 scopus 로고    scopus 로고
    • Analysis of the RNA-editing reaction of ADAR2with structural and fluorescent analogues of the GluR-BR/Gediting site
    • Stephens, O. M., Yi-Brunozzi, H. Y., and Beal, P. A. (2000) Analysis of the RNA-editing reaction of ADAR2with structural and fluorescent analogues of the GluR-BR/Gediting site. Biochemistry 39 (40), 12243-12251.
    • (2000) Biochemistry , vol.39 , Issue.40 , pp. 12243-12251
    • Stephens, O.M.1    Yi-Brunozzi, H.Y.2    Beal, P.A.3
  • 96
    • 0021715830 scopus 로고
    • The molecular clock may be an episodic clock
    • Gillespie, J. H. (1984) The molecular clock may be an episodic clock. Proc Natl Acad Sci USA 81 (24), 8009-8013.
    • (1984) Proc Natl Acad Sci USA , vol.81 , Issue.24 , pp. 8009-8013
    • Gillespie, J.H.1
  • 97
    • 0022641120 scopus 로고
    • Natural selection and the molecular clock
    • Gillespie, J. H. (1986) Natural selection and the molecular clock. Mol Biol Evol 3 (2), 138-155.
    • (1986) Mol Biol Evol , vol.3 , Issue.2 , pp. 138-155
    • Gillespie, J.H.1
  • 98
    • 0036720020 scopus 로고    scopus 로고
    • The Ka/Ks ratio: Diagnosing the form of sequence evolution
    • Hurst, L. D. (2002) The Ka/Ks ratio: Diagnosing the form of sequence evolution. Trends Genet 18 (9), 486.
    • (2002) Trends Genet , vol.18 , Issue.9 , pp. 486
    • Hurst, L.D.1
  • 99
    • 0002027029 scopus 로고
    • A new evolutionary law
    • Van Valen, L. (1973) A new evolutionary law. Evol Theory 1, 1-30.
    • (1973) Evol Theory , vol.1 , pp. 1-30
    • Van Valen, L.1
  • 100
    • 0038375028 scopus 로고    scopus 로고
    • In vitro deamination of cytosine to uracil in singlestrandedDNAby apolipoproteinBediting complex catalytic subunit 1 (APOBEC1)
    • Petersen-Mahrt, S. K. and Neuberger, M. S. (2003) In vitro deamination of cytosine to uracil in singlestrandedDNAby apolipoproteinBediting complex catalytic subunit 1 (APOBEC1). J Biol Chem 278 (22), 19583-19586.
    • (2003) J Biol Chem , vol.278 , Issue.22 , pp. 19583-19586
    • Petersen-Mahrt, S.K.1    Neuberger, M.S.2
  • 101
    • 1542328859 scopus 로고    scopus 로고
    • Comparison of the differential context-dependence ofDNAdeamination by APOBEC enzymes: Correlation with mutation spectra in vivo
    • Beale, R. C., et al. (2004) Comparison of the differential context-dependence ofDNAdeamination by APOBEC enzymes: Correlation with mutation spectra in vivo. J Mol Biol 337 (3), 585-596.
    • (2004) J Mol Biol , vol.337 , Issue.3 , pp. 585-596
    • Beale, R.C.1
  • 102
    • 11144244647 scopus 로고    scopus 로고
    • APOBEC3B and APOBEC3C are potent inhibitors of simian immunodeficiency virus replication
    • Yu, Q., et al. (2004) APOBEC3B and APOBEC3C are potent inhibitors of simian immunodeficiency virus replication. J Biol Chem 279 (51), 53379-53386.
    • (2004) J Biol Chem , vol.279 , Issue.51 , pp. 53379-53386
    • Yu, Q.1
  • 103
    • 0033603340 scopus 로고    scopus 로고
    • Specific expression of activation-induced cytidine deaminase (AID), a novel member of theRNA-editing deaminase family in germinal centerBcells
    • Muramatsu, M., et al. (1999) Specific expression of activation-induced cytidine deaminase (AID), a novel member of theRNA-editing deaminase family in germinal centerBcells. J Biol Chem 274 (26), 18470-18476.
    • (1999) J Biol Chem , vol.274 , Issue.26 , pp. 18470-18476
    • Muramatsu, M.1
  • 104
    • 0034662773 scopus 로고    scopus 로고
    • Isolation, tissue distribution, and chromosomal localization of the human activation-induced cytidine deaminase (AID) gene
    • Muto, T., et al. (2000) Isolation, tissue distribution, and chromosomal localization of the human activation-induced cytidine deaminase (AID) gene. Genomics 68 (1), 85-88.
    • (2000) Genomics , vol.68 , Issue.1 , pp. 85-88
    • Muto, T.1
  • 105
    • 0034268780 scopus 로고    scopus 로고
    • Class switch recombination and hypermutation require activationinduced cytidine deaminase (AID), a potential RNA editing enzyme
    • Muramatsu, M., et al. (2000) Class switch recombination and hypermutation require activationinduced cytidine deaminase (AID), a potential RNA editing enzyme. Cell 102 (5), 553-563.
    • (2000) Cell , vol.102 , Issue.5 , pp. 553-563
    • Muramatsu, M.1
  • 106
    • 0036718611 scopus 로고    scopus 로고
    • Comparative analyses ofimmunoglobulin genes: Surprises and portents
    • Flajnik,M. F. (2002) Comparative analyses ofimmunoglobulin genes: Surprises and portents. Nat Rev Immunol 2 (9), 688-698.
    • (2002) Nat Rev Immunol , vol.2 , Issue.9 , pp. 688-698
    • Flajnik, M.F.1
  • 107
    • 1642334586 scopus 로고    scopus 로고
    • Cloning expression of the AID gene in the channel catfish
    • Saunders, H. L. and Magor, B. G. (2004) Cloning expression of the AID gene in the channel catfish. Dev Comp Immunol 28 (7-8), 657-663.
    • (2004) Dev Comp Immunol , vol.28 , Issue.7-8 , pp. 657-663
    • Saunders, H.L.1    Magor, B.G.2
  • 108
    • 4344654828 scopus 로고    scopus 로고
    • Identification of the activation-induced cytidine deaminase gene from zebrafish: An evolutionary analysis
    • Zhao,Y., et al. (2005) Identification of the activation-induced cytidine deaminase gene from zebrafish: An evolutionary analysis. Dev Comp Immunol 29 (1), 61-71.
    • (2005) Dev Comp Immunol , vol.29 , Issue.1 , pp. 61-71
    • Zhao, Y.1
  • 109
    • 19344362934 scopus 로고    scopus 로고
    • Ancient adaptive evolution of the primate antiviral DNA-editing enzyme APOBEC3G
    • Sawyer, S. L., Emerman, M., and Malik, H. S. (2004) Ancient adaptive evolution of the primate antiviral DNA-editing enzyme APOBEC3G. PLoS Biol 2 (9), E275.
    • (2004) PLoS Biol , vol.2 , Issue.9
    • Sawyer, S.L.1    Emerman, M.2    Malik, H.S.3
  • 110
    • 34249065874 scopus 로고    scopus 로고
    • Evolution and diversification of lamprey antigen receptors: evidence for involvement of an AID-APOBEC family cytosine deaminase
    • Rogozin, I. B., et al. (2007) Evolution and diversification of lamprey antigen receptors: evidence for involvement of an AID-APOBEC family cytosine deaminase. Nat Immunol. 8 (6), 647-656.
    • (2007) Nat Immunol. , vol.8 , Issue.6 , pp. 647-656
    • Rogozin, I.B.1
  • 111
    • 0002936990 scopus 로고    scopus 로고
    • Major Events in Early Vertebrate Evolution
    • In: Ahlberg, P. E. (ed.), Taylor & Francis, London
    • Hedges, S. B. (2001) In: Ahlberg, P. E. (ed.), Major Events in Early Vertebrate Evolution, Taylor & Francis, London, pp. 119-134.
    • (2001) , pp. 119-134
    • Hedges, S.B.1
  • 112
    • 0025196283 scopus 로고
    • The A. T-DNA-binding domain of mammalian high mobility group I chromosomal proteins. Anovel peptide motif for recognizingDNAstructure
    • Reeves, R. and Nissen, M. S. (1990) The A. T-DNA-binding domain of mammalian high mobility group I chromosomal proteins.Anovel peptide motif for recognizingDNAstructure. J Biol Chem 265 (15), 8573-8582.
    • (1990) J Biol Chem , vol.265 , Issue.15 , pp. 8573-8582
    • Reeves, R.1    Nissen, M.S.2
  • 113
    • 0032190230 scopus 로고    scopus 로고
    • AT-hook motifs identified in a wide variety of DNA-binding proteins
    • Aravind, L. and Landsman, D. (1998) AT-hook motifs identified in a wide variety of DNA-binding proteins. Nucleic Acids Res 26 (19), 4413-4421.
    • (1998) Nucleic Acids Res , vol.26 , Issue.19 , pp. 4413-4421
    • Aravind, L.1    Landsman, D.2
  • 114
    • 0242476502 scopus 로고    scopus 로고
    • Genomic analysis of immunity in a Urochordate and the emergence of the vertebrate immune system: "Waiting for Godot
    • Azumi, K., et al. (2003) Genomic analysis of immunity in a Urochordate and the emergence of the vertebrate immune system: "Waiting for Godot." Immunogenetics 55 (8), 570-581.
    • (2003) Immunogenetics , vol.55 , Issue.8 , pp. 570-581
    • Azumi, K.1
  • 115
    • 33745853463 scopus 로고    scopus 로고
    • Identification of a specific domain required for dimerization of activationinduced cytidine deaminase
    • Wang, J., et al. (2006) Identification of a specific domain required for dimerization of activationinduced cytidine deaminase. J Biol Chem 281 (28), 19115-19123.
    • (2006) J Biol Chem , vol.281 , Issue.28 , pp. 19115-19123
    • Wang, J.1
  • 116
    • 0033526865 scopus 로고    scopus 로고
    • APOBEC-2, a cardiac-and skeletal muscle-specific member of the cytidine deaminase supergene family
    • Liao, W., et al. (1999) APOBEC-2, a cardiac-and skeletal muscle-specific member of the cytidine deaminase supergene family. Biochem Biophys Res Commun 260 (2), 398-404.
    • (1999) Biochem Biophys Res Commun , vol.260 , Issue.2 , pp. 398-404
    • Liao, W.1
  • 117
    • 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. (2001) 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 (6), C1904-C1916.
    • (2001) Am J Physiol Cell Physiol , vol.281 , Issue.6
    • Anant, S.1
  • 118
    • 0037351989 scopus 로고    scopus 로고
    • Genome duplication, a trait shared by 22000 species of ray-finned fish
    • Taylor, J. S., et al. (2003) Genome duplication, a trait shared by 22000 species of ray-finned fish. Genome Res 13 (3), 382-390.
    • (2003) Genome Res , vol.13 , Issue.3 , pp. 382-390
    • Taylor, J.S.1
  • 119
    • 2442707716 scopus 로고    scopus 로고
    • Fugu genome analysis provides evidence for a wholegenome duplication early during the evolution of ray-finned fishes
    • Christoffels, A., et al. (2004) Fugu genome analysis provides evidence for a wholegenome duplication early during the evolution of ray-finned fishes. Mol Biol Evol 21 (6), 1146-1151.
    • (2004) Mol Biol Evol , vol.21 , Issue.6 , pp. 1146-1151
    • Christoffels, A.1
  • 120
    • 31444441811 scopus 로고    scopus 로고
    • Expression of APOBEC2 is transcriptionally regulated by NF-kappaB in human hepatocytes
    • Matsumoto, T., et al. (2006) Expression of APOBEC2 is transcriptionally regulated by NF-kappaB in human hepatocytes. FEBS Lett 580 (3), 731-735.
    • (2006) FEBS Lett , vol.580 , Issue.3 , pp. 731-735
    • Matsumoto, T.1
  • 121
    • 23344440307 scopus 로고    scopus 로고
    • Mice deficient in APOBEC2 and APOBEC3
    • Mikl, M. C., et al. (2005) Mice deficient in APOBEC2 and APOBEC3. Mol Cell Biol 25 (16), 7270-7277.
    • (2005) Mol Cell Biol , vol.25 , Issue.16 , pp. 7270-7277
    • Mikl, M.C.1
  • 122
    • 0027200620 scopus 로고
    • Molecular cloning of an apolipoprotein B messenger RNA editing protein
    • Teng, B., Burant, C. F., and Davidson, N. O. (1993) Molecular cloning of an apolipoprotein B messenger RNA editing protein. Science 260 (5115), 1816-1819.
    • (1993) Science , vol.260 , Issue.5115 , pp. 1816-1819
    • Teng, B.1    Burant, C.F.2    Davidson, N.O.3
  • 123
    • 0027434027 scopus 로고
    • The p27 catalytic subunit of the apolipoproteinBmRNAediting enzyme is a cytidine deaminase
    • Navaratnam, N., et al. (1993) The p27 catalytic subunit of the apolipoproteinBmRNAediting enzyme is a cytidine deaminase. J Biol Chem 268 (28), 20709-20712.
    • (1993) J Biol Chem , vol.268 , Issue.28 , pp. 20709-20712
    • Navaratnam, N.1
  • 124
    • 0023617743 scopus 로고
    • Apolipoprotein B-48 is the product of a messenger RNA with an organ-specific in-frame stop codon
    • Chen, S. H., et al. (1987) Apolipoprotein B-48 is the product of a messenger RNA with an organ-specific in-frame stop codon. Science 238 (4825), 363-366.
    • (1987) Science , vol.238 , Issue.4825 , pp. 363-366
    • Chen, S.H.1
  • 125
    • 0023651359 scopus 로고
    • Anovel form of tissue-specificRNAprocessing produces apolipoprotein-B48 in intestine
    • Powell, L. M., et al. (1987) Anovel form of tissue-specificRNAprocessing produces apolipoprotein-B48 in intestine. Cell 50 (6), 831-840.
    • (1987) Cell , vol.50 , Issue.6 , pp. 831-840
    • Powell, L.M.1
  • 126
    • 0036500884 scopus 로고    scopus 로고
    • The editosome for cytidine to uridine mRNA editing has a native complexity of 27S:identification of intracellular domains containing active and inactive editing factors
    • Sowden, M. P., et al. (2002) The editosome for cytidine to uridine mRNA editing has a native complexity of 27S:identification of intracellular domains containing active and inactive editing factors. J Cell Sci 115 (Pt 5), 1027-1039.
    • (2002) J Cell Sci , vol.115 , Issue.PT. 5 , pp. 1027-1039
    • Sowden, M.P.1
  • 127
    • 0031829287 scopus 로고    scopus 로고
    • Asequence-specificRNA-binding proteincomplements apobec-1 To edit apolipoprotein B mRNA
    • Mehta, A. and Driscoll, D. M.(1998)Asequence-specificRNA-binding proteincomplements apobec-1 To edit apolipoprotein B mRNA. Mol Cell Biol 18 (8), 4426-4432.
    • (1998) Mol Cell Biol , vol.18 , Issue.8 , pp. 4426-4432
    • Mehta, A.1    Driscoll, D.M.2
  • 128
    • 0033520929 scopus 로고    scopus 로고
    • Phylogenentic Analysis of the Apolipoprotein B mRNA-editing Region
    • Hersberger, M., Patarroyo-White, S., Arnold, K. S. and., and Innerarity, T. L. (1999) Phylogenentic Analysis of the Apolipoprotein B mRNA-editing Region. J Biol Chem 274 (49), 34590-34597.
    • (1999) J Biol Chem , vol.274 , Issue.49 , pp. 34590-34597
    • Hersberger, M.1    Patarroyo-White, S.2    Arnold, K.S.3    Innerarity, T.L.4
  • 129
    • 12844281639 scopus 로고    scopus 로고
    • NMRstructure of the apoBmRNAstem-loop and its interaction with theCtoU editing APOBEC1 complementary factor
    • Maris, C., et al. (2005) NMRstructure of the apoBmRNAstem-loop and its interaction with theCtoU editing APOBEC1 complementary factor. RNA 11 (2), 173-186.
    • (2005) RNA , vol.11 , Issue.2 , pp. 173-186
    • Maris, C.1
  • 130
    • 0027172292 scopus 로고
    • Apolipoprotein B mRNA editing in 12 different mammalian species: Hepatic expression is reflected in low concentrations of apoB-containing plasma lipoproteins
    • Greeve, J., et al. (1993) Apolipoprotein B mRNA editing in 12 different mammalian species: Hepatic expression is reflected in low concentrations of apoB-containing plasma lipoproteins. J Lipid Res 34 (8), 1367-1383.
    • (1993) J Lipid Res , vol.34 , Issue.8 , pp. 1367-1383
    • Greeve, J.1
  • 131
    • 0029036964 scopus 로고
    • Alternative mRNA splicing and differential promoter utilization determine tissue-specific expression of the apolipoprotein B mRNA-editing protein (Apobec1) gene in mice. Structure and evolution of Apobec1 and related nucleoside/nucleotide deaminases
    • Nakamuta, M., et al. (1995) Alternative mRNA splicing and differential promoter utilization determine tissue-specific expression of the apolipoprotein B mRNA-editing protein (Apobec1) gene in mice. Structure and evolution of Apobec1 and related nucleoside/nucleotide deaminases. J Biol Chem 270 (22), 13042-13056.
    • (1995) J Biol Chem , vol.270 , Issue.22 , pp. 13042-13056
    • Nakamuta, M.1
  • 132
    • 0028559994 scopus 로고
    • Assignment of the gene encoding the human apolipoprotein BmRNA editing enzyme (APOBEC1) to chromosome 12p13.1
    • Espinosa, R. 3rd., et al. (1994) Assignment of the gene encoding the human apolipoprotein BmRNA editing enzyme (APOBEC1) to chromosome 12p13.1. Genomics 24 (2), 414-415.
    • (1994) Genomics , vol.24 , Issue.2 , pp. 414-415
    • Espinosa III, R.1
  • 133
    • 0028085932 scopus 로고
    • Dimeric structure of a human apolipoprotein B mRNA editing protein and cloning and chromosomal localization of its gene
    • Lau, P. P., et al. (1994) Dimeric structure of a human apolipoprotein B mRNA editing protein and cloning and chromosomal localization of its gene. Proc Natl Acad Sci USA 91 (18), 8522-8526.
    • (1994) Proc Natl Acad Sci USA , vol.91 , Issue.18 , pp. 8522-8526
    • Lau, P.P.1
  • 134
    • 0033153769 scopus 로고    scopus 로고
    • C!U editing of apolipoprotein B mRNA in marsupials: identification and characterisation of APOBEC-1 from the American opossum Monodelphus domestica
    • Fujino, T., et al. (1999) C!U editing of apolipoprotein B mRNA in marsupials: identification and characterisation of APOBEC-1 from the American opossum Monodelphus domestica. Nucleic Acids Res 27 (13), 2662-2671.
    • (1999) Nucleic Acids Res , vol.27 , Issue.13 , pp. 2662-2671
    • Fujino, T.1
  • 135
    • 0032580152 scopus 로고    scopus 로고
    • A molecular timescale for vertebrate evolution
    • Kumar, S. and Hedges, S. B. (1998) A molecular timescale for vertebrate evolution. Nature 392 (6679), 917-920.
    • (1998) Nature , vol.392 , Issue.6679 , pp. 917-920
    • Kumar, S.1    Hedges, S.B.2
  • 136
    • 0035879114 scopus 로고    scopus 로고
    • Intracellular trafficking determinants inAPOBEC-1, the catalytic subunit for cytidine to uridine editing of apolipoprotein B mRNA
    • Yang,Y., Sowden,M. P., and Smith, H. C. (2001) Intracellular trafficking determinants inAPOBEC-1, the catalytic subunit for cytidine to uridine editing of apolipoprotein B mRNA. Exp Cell Res 267 (2), 153-164.
    • (2001) Exp Cell Res , vol.267 , Issue.2 , pp. 153-164
    • Yang, Y.1    Sowden, M.P.2    Smith, H.C.3
  • 137
    • 0032958220 scopus 로고    scopus 로고
    • Mutational analysis of apolipoprotein B mRNA editing enzyme (APOBEC1). structure-function relationships of RNA editing and dimerization
    • Teng, B. B., et al. (1999) Mutational analysis of apolipoprotein B mRNA editing enzyme (APOBEC1). structure-function relationships of RNA editing and dimerization. J Lipid Res 40 (4), 623-635.
    • (1999) J Lipid Res , vol.40 , Issue.4 , pp. 623-635
    • Teng, B.B.1
  • 138
    • 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. (1998) Escherichia coli cytidine deaminase provides a molecular model for ApoB RNA editing and a mechanism for RNA substrate recognition. J Mol Biol 275 (4), 695-714.
    • (1998) J Mol Biol , vol.275 , Issue.4 , pp. 695-714
    • Navaratnam, N.1
  • 139
    • 0029056474 scopus 로고
    • Evolutionary origins of apoB mRNA editing: Catalysis by a cytidine deaminase that has acquired a novel RNA-binding motif at its active site
    • Navaratnam, N., et al. (1995) Evolutionary origins of apoB mRNA editing: Catalysis by a cytidine deaminase that has acquired a novel RNA-binding motif at its active site. Cell 81 (2), 187-195.
    • (1995) Cell , vol.81 , Issue.2 , pp. 187-195
    • Navaratnam, N.1
  • 140
    • 1642308939 scopus 로고    scopus 로고
    • Inhibition of hepatitisBvirus replication byAPOBEC3G
    • Turelli, P., et al. (2004) Inhibition of hepatitisBvirus replication byAPOBEC3G. Science 303 (5665), 1829.
    • (2004) Science , vol.303 , Issue.5665 , pp. 1829
    • Turelli, P.1
  • 141
    • 20444416733 scopus 로고    scopus 로고
    • Extensive editing of both hepatitis B virus DNA strands by APOBEC3 cytidine deaminases in vitro and in vivo
    • Suspene, R., et al. (2005) Extensive editing of both hepatitis B virus DNA strands by APOBEC3 cytidine deaminases in vitro and in vivo. Proc Natl Acad Sci USA 102 (23), 8321-8326.
    • (2005) Proc Natl Acad Sci USA , vol.102 , Issue.23 , pp. 8321-8326
    • Suspene, R.1
  • 142
    • 0038681023 scopus 로고    scopus 로고
    • Broad antiretroviral defence by human APOBEC3G through lethal editing of nascent reverse transcripts
    • Mangeat, B., et al. (2003) Broad antiretroviral defence by human APOBEC3G through lethal editing of nascent reverse transcripts. Nature 424 (6944), 99-103.
    • (2003) Nature , vol.424 , Issue.6944 , pp. 99-103
    • Mangeat, B.1
  • 143
    • 33846895873 scopus 로고    scopus 로고
    • Selective inhibition of Alu retrotransposition by APOBEC3G
    • Hulme, A. E., et al. (2007) Selective inhibition of Alu retrotransposition by APOBEC3G. Gene 390 (1-2), 199-205.
    • (2007) Gene , vol.390 , Issue.1-2 , pp. 199-205
    • Hulme, A.E.1
  • 144
    • 34247635482 scopus 로고    scopus 로고
    • Deamination-independent inhibition of hepatitis B virus reverse transcription by APOBEC3G
    • Nguyen, D. H., Gummuluru, S., and Hu, J. (2007) Deamination-independent inhibition of hepatitis B virus reverse transcription by APOBEC3G. J Virol 81 (9), 4465-4472.
    • (2007) J Virol , vol.81 , Issue.9 , pp. 4465-4472
    • Nguyen, D.H.1    Gummuluru, S.2    Hu, J.3
  • 145
    • 34249892197 scopus 로고    scopus 로고
    • The intrinsic antiretroviral factorAPOBEC3Bcontains two enzymatically active cytidine deaminase domains
    • Bogerd, H. P., et al. (2007) The intrinsic antiretroviral factorAPOBEC3Bcontains two enzymatically active cytidine deaminase domains. Virology 364 (2), 486-493.
    • (2007) Virology , vol.364 , Issue.2 , pp. 486-493
    • Bogerd, H.P.1
  • 146
    • 33745044396 scopus 로고    scopus 로고
    • Cellular inhibitors of long interspersed element 1 and Alu retrotransposition
    • Bogerd, H. P., et al. (2006) Cellular inhibitors of long interspersed element 1 and Alu retrotransposition. Proc Natl Acad Sci USA 103 (23), 8780-8785.
    • (2006) Proc Natl Acad Sci USA , vol.103 , Issue.23 , pp. 8780-8785
    • Bogerd, H.P.1
  • 147
    • 33750344250 scopus 로고    scopus 로고
    • Identification of APOBEC3DE as another antiretroviral factor from the human APOBEC family
    • Dang,Y., et al. (2006) Identification of APOBEC3DE as another antiretroviral factor from the human APOBEC family. J Virol 80 (21), 10522-10533.
    • (2006) J Virol , vol.80 , Issue.21 , pp. 10522-10533
    • Dang, Y.1
  • 148
    • 4143071549 scopus 로고    scopus 로고
    • APOBEC3F properties and hypermutation preferences indicate activity against HIV-1 in vivo
    • Liddament, M. T., et al. (2004) APOBEC3F properties and hypermutation preferences indicate activity against HIV-1 in vivo. Curr Biol 14 (15), 1385-1391.
    • (2004) Curr Biol , vol.14 , Issue.15 , pp. 1385-1391
    • Liddament, M.T.1
  • 149
    • 33645760962 scopus 로고    scopus 로고
    • Adaptive evolution and antiviral activity of the conserved mammalian cytidine deaminase APOBEC3H
    • OhAinle, M., et al. (2006) Adaptive evolution and antiviral activity of the conserved mammalian cytidine deaminase APOBEC3H. J Virol 80 (8), 3853-3862.
    • (2006) J Virol , vol.80 , Issue.8 , pp. 3853-3862
    • OhAinle, M.1
  • 150
    • 33644769083 scopus 로고    scopus 로고
    • APOBEC3A is a potent inhibitor of adeno-associated virus and retrotransposons
    • Chen, H., et al. (2006) APOBEC3A is a potent inhibitor of adeno-associated virus and retrotransposons. Curr Biol 16 (5), 480-485.
    • (2006) Curr Biol , vol.16 , Issue.5 , pp. 480-485
    • Chen, H.1
  • 151
    • 19344372749 scopus 로고    scopus 로고
    • Gene duplication: The genomic trade in spare parts
    • Hurles, M. (2004) Gene duplication: The genomic trade in spare parts. PLoS Biol 2 (7), E206.
    • (2004) PLoS Biol , vol.2 , Issue.7
    • Hurles, M.1
  • 152
    • 7444233609 scopus 로고    scopus 로고
    • Mammalian phylogenomics comes of age
    • Murphy,W. J., Pevzner, P. A., and O'Brien, S. J. (2004) Mammalian phylogenomics comes of age. Trends Genet 20 (12), 631-639.
    • (2004) Trends Genet , vol.20 , Issue.12 , pp. 631-639
    • Murphy, W.J.1    Pevzner, P.A.2    O'Brien, S.J.3
  • 153
    • 0035895841 scopus 로고    scopus 로고
    • Comparative study and prediction of DNA fragments associated with various elements of the nuclear matrix
    • Glazko, G. V., Rogozin, I. B., and Glazkov, M. V. (2001) Comparative study and prediction of DNA fragments associated with various elements of the nuclear matrix. Biochim Biophys Acta 1517 (3), 351-364.
    • (2001) Biochim Biophys Acta , vol.1517 , Issue.3 , pp. 351-364
    • Glazko, G.V.1    Rogozin, I.B.2    Glazkov, M.V.3
  • 154
    • 7244259101 scopus 로고    scopus 로고
    • Genome duplication in the teleost fish Tetraodon nigroviridis reveals the early vertebrate proto-karyotype
    • Jaillon, O., et al. (2004) Genome duplication in the teleost fish Tetraodon nigroviridis reveals the early vertebrate proto-karyotype. Nature 431 (7011), 946-957.
    • (2004) Nature , vol.431 , Issue.7011 , pp. 946-957
    • Jaillon, O.1
  • 155
    • 84889285811 scopus 로고    scopus 로고
    • OhAinle, M., Emerman, M., and Malik, H.
    • In: Conference on Retroviruses and Opportunistic Infections, Los Angeles, CA
    • OhAinle, M., Emerman, M., and Malik, H. (2007) Evolution of antiretroviral Activity of APOBEC genes in primates. In: Conference on Retroviruses and Opportunistic Infections, Los Angeles, CA.
    • (2007)
  • 156
    • 0021274960 scopus 로고
    • The phylogeny of the hominoid primates, as indicated by DNA-DNA hybridization
    • Sibley, C. G. and Ahlquist, J. E. (1984) The phylogeny of the hominoid primates, as indicated by DNA-DNA hybridization. J Mol Evol 20 (1), 2-15.
    • (1984) J Mol Evol , vol.20 , Issue.1 , pp. 2-15
    • Sibley, C.G.1    Ahlquist, J.E.2
  • 157
    • 0038107587 scopus 로고    scopus 로고
    • Species-specific exclusion of APOBEC3G from HIV-1 virions by Vif
    • Mariani, R., et al. (2003) Species-specific exclusion of APOBEC3G from HIV-1 virions by Vif. Cell 114 (1), 21-31.
    • (2003) Cell , vol.114 , Issue.1 , pp. 21-31
    • Mariani, R.1
  • 158
    • 33751014554 scopus 로고    scopus 로고
    • Evolutionarily conserved and non-conserved retrovirus restriction activities of artiodactyl APOBEC3F proteins
    • Jonsson, S. R., et al. (2006) Evolutionarily conserved and non-conserved retrovirus restriction activities of artiodactyl APOBEC3F proteins. Nucleic Acids Res 34 (19), 5683-5694.
    • (2006) Nucleic Acids Res , vol.34 , Issue.19 , pp. 5683-5694
    • Jonsson, S.R.1
  • 159
    • 20344379929 scopus 로고    scopus 로고
    • The antiretroviral activity of APOBEC3 is inhibited by the foamy virus accessory Bet protein
    • Lochelt, M., et al. (2005) The antiretroviral activity of APOBEC3 is inhibited by the foamy virus accessory Bet protein. Proc Natl Acad Sci USA 102 (22), 7982-7987.
    • (2005) Proc Natl Acad Sci USA , vol.102 , Issue.22 , pp. 7982-7987
    • Lochelt, M.1
  • 160
    • 33846031136 scopus 로고    scopus 로고
    • Reversed functional organization of mouse and human APOBEC3 cytidine deaminase domains
    • Hakata, Y. and Landau, N. R. (2006) Reversed functional organization of mouse and human APOBEC3 cytidine deaminase domains. J Biol Chem 281 (48), 36624-36631.
    • (2006) J Biol Chem , vol.281 , Issue.48 , pp. 36624-36631
    • Hakata, Y.1    Landau, N.R.2
  • 161
    • 33745541663 scopus 로고    scopus 로고
    • Interferon-inducible expression of APOBEC3 editing enzymes in human hepatocytes and inhibition of hepatitis B virus replication
    • Bonvin, M., et al. (2006) Interferon-inducible expression of APOBEC3 editing enzymes in human hepatocytes and inhibition of hepatitis B virus replication. Hepatology 43 (6), 1364-1374.
    • (2006) Hepatology , vol.43 , Issue.6 , pp. 1364-1374
    • Bonvin, M.1
  • 162
    • 34250688401 scopus 로고    scopus 로고
    • All APOBEC3 family proteins differentially inhibit LINE-1 retrotransposition
    • Kinomoto, M., et al. (2007) All APOBEC3 family proteins differentially inhibit LINE-1 retrotransposition. Nucleic Acids Res 35 (9), 2955-2964.
    • (2007) Nucleic Acids Res , vol.35 , Issue.9 , pp. 2955-2964
    • Kinomoto, M.1
  • 163
    • 33846847836 scopus 로고    scopus 로고
    • Dual effect of APOBEC3G on hepatitis B virus
    • Noguchi, C., et al. Dual effect of APOBEC3G on hepatitis B virus. J Gen Virol (2007) 88 (Pt 2), 432-432.
    • (2007) J Gen Virol , vol.88 , Issue.PT. 2 , pp. 432-432
    • Noguchi, C.1
  • 164
    • 0036138187 scopus 로고    scopus 로고
    • Human-specific duplication and mosaic transcripts: The recent paralogous structure of chromosome 22
    • Bailey, J. A., et al. (2002) Human-specific duplication and mosaic transcripts: The recent paralogous structure of chromosome 22. Am J Hum Genet 70 (1), 83-100.
    • (2002) Am J Hum Genet , vol.70 , Issue.1 , pp. 83-100
    • Bailey, J.A.1
  • 165
    • 34247623286 scopus 로고    scopus 로고
    • Population Stratification of a Common APOBEC Gene Deletion Polymorphism
    • Kidd, J. M., et al. (2007) Population Stratification of a Common APOBEC Gene Deletion Polymorphism. PLoS Genet 3 (4), e63.
    • (2007) PLoS Genet , vol.3 , Issue.4
    • Kidd, J.M.1
  • 166
    • 0142059650 scopus 로고    scopus 로고
    • AnAlu transpositionmodel for the origin and expansion of human segmental duplications
    • Bailey, J. A., Liu, G., and Eichler, E. E. (2003) AnAlu transpositionmodel for the origin and expansion of human segmental duplications. Am J Hum Genet 73 (4), 823-834.
    • (2003) Am J Hum Genet , vol.73 , Issue.4 , pp. 823-834
    • Bailey, J.A.1    Liu, G.2    Eichler, E.E.3
  • 167
    • 0035500899 scopus 로고    scopus 로고
    • Recent duplication, domain accretion and the dynamic mutation of the human genome
    • Eichler, E. E. (2001) Recent duplication, domain accretion and the dynamic mutation of the human genome. Trends Genet 17 (11), 661-669.
    • (2001) Trends Genet , vol.17 , Issue.11 , pp. 661-669
    • Eichler, E.E.1
  • 168
    • 0036468807 scopus 로고    scopus 로고
    • Genomearchitecture, rearrangements and genomic disorders
    • Stankiewicz,P. and Lupski, J. R. (2002) Genomearchitecture, rearrangements and genomic disorders. Trends Genet 18 (2), 74-82.
    • (2002) Trends Genet , vol.18 , Issue.2 , pp. 74-82
    • Stankiewicz, P.1    Lupski, J.R.2
  • 169
    • 4444290423 scopus 로고    scopus 로고
    • Rapid evolution of primate antiviral enzyme APOBEC3G
    • Zhang, J. andWebb, D. M. (2004) Rapid evolution of primate antiviral enzyme APOBEC3G. Hum Mol Genet 13 (16), 1785-1791.
    • (2004) Hum Mol Genet , vol.13 , Issue.16 , pp. 1785-1791
    • Zhang, J.1    Webb, D.M.2
  • 170
    • 2042437650 scopus 로고    scopus 로고
    • Initial sequencing and analysis of the human genome
    • Lander, E. S., et al. (2001) Initial sequencing and analysis of the human genome. Nature 409 (6822), 860-921.
    • (2001) Nature , vol.409 , Issue.6822 , pp. 860-921
    • Lander, E.S.1
  • 171
    • 33745373606 scopus 로고    scopus 로고
    • Primate segmental duplications: Crucibles of evolution, diversity and disease
    • Bailey, J. A. and Eichler, E. E. (2006) Primate segmental duplications: Crucibles of evolution, diversity and disease. Nat Rev Genet 7 (7), 552-564.
    • (2006) Nat Rev Genet , vol.7 , Issue.7 , pp. 552-564
    • Bailey, J.A.1    Eichler, E.E.2
  • 172
    • 2342437120 scopus 로고    scopus 로고
    • Alu repeat analysis in the completehumangenome:Trends and variations with respect to genomic composition
    • Grover, D., et al. (2004) Alu repeat analysis in the completehumangenome:Trends and variations with respect to genomic composition. Bioinformatics 20 (6), 813-817.
    • (2004) Bioinformatics , vol.20 , Issue.6 , pp. 813-817
    • Grover, D.1
  • 173
    • 33645038598 scopus 로고    scopus 로고
    • The finishedDNAsequence ofhumanchromosome12
    • Scherer, S. E., et al. (2006) The finishedDNAsequence ofhumanchromosome12. Nature 440 (7082), 346-351.
    • (2006) Nature , vol.440 , Issue.7082 , pp. 346-351
    • Scherer, S.E.1
  • 174
    • 9244255880 scopus 로고    scopus 로고
    • Fluorescence in situ hybridization to chromosomes as a tool to understand human and primate genome evolution
    • Wienberg, J. (2005) Fluorescence in situ hybridization to chromosomes as a tool to understand human and primate genome evolution. Cytogenet Genome Res 108 (1-3), 139-160.
    • (2005) Cytogenet Genome Res , vol.108 , Issue.1-3 , pp. 139-160
    • Wienberg, J.1
  • 175
    • 33845972280 scopus 로고    scopus 로고
    • Nanostructures ofAPOBEC3Gsupport a hierarchical assembly modelof high molecular mass ribonucleoprotein particles from dimeric subunits
    • Wedekind, J. E., et al. (2006) Nanostructures ofAPOBEC3Gsupport a hierarchical assembly modelof high molecular mass ribonucleoprotein particles from dimeric subunits. J Biol Chem 281 (50), 38122-38126.
    • (2006) J Biol Chem , vol.281 , Issue.50 , pp. 38122-38126
    • Wedekind, J.E.1
  • 176
    • 18344372631 scopus 로고    scopus 로고
    • Cellular APOBEC3G restricts HIV-1 infection in resting CD4+ T cells
    • Chiu, Y. L., et al. (2005) Cellular APOBEC3G restricts HIV-1 infection in resting CD4+ T cells. Nature 435 (7038), 108-114.
    • (2005) Nature , vol.435 , Issue.7038 , pp. 108-114
    • Chiu, Y.L.1
  • 177
    • 33750379905 scopus 로고    scopus 로고
    • High-molecular-mass APOBEC3G complexes restrict Alu retrotransposition
    • Chiu, Y. L., et al. (2006) High-molecular-mass APOBEC3G complexes restrict Alu retrotransposition. Proc Natl Acad Sci USA 103 (42), 15588-15593.
    • (2006) Proc Natl Acad Sci USA , vol.103 , Issue.42 , pp. 15588-15593
    • Chiu, Y.L.1
  • 178
    • 33645862586 scopus 로고    scopus 로고
    • Endogenous factors enhance HIVinfection of tissue naiveCD4Tcells by stimulating high molecular massAPOBEC3Gcomplex formation
    • Kreisberg, J. F.,Yonemoto,W., and Greene,W. C. (2006) Endogenous factors enhance HIVinfection of tissue naiveCD4Tcells by stimulating high molecular massAPOBEC3Gcomplex formation. JExp Med 203 (4), 865-870.
    • (2006) JExp Med , vol.203 , Issue.4 , pp. 865-870
    • Kreisberg, J.F.1    Yonemoto, W.2    Greene, W.C.3
  • 179
    • 31144469701 scopus 로고    scopus 로고
    • Role mechanism of action of the APOBEC3 family of antiretroviral resistance factors
    • Cullen, B. R. (2006) Role mechanism of action of the APOBEC3 family of antiretroviral resistance factors. J Virol 80 (3), 1067-1076.
    • (2006) J Virol , vol.80 , Issue.3 , pp. 1067-1076
    • Cullen, B.R.1
  • 180
    • 13444282074 scopus 로고    scopus 로고
    • APOBEC3G cytidine deaminase inhibits retrotransposition of endogenous retroviruses
    • Esnault, C., et al. (2005) APOBEC3G cytidine deaminase inhibits retrotransposition of endogenous retroviruses. Nature 433 (7024), 430-433.
    • (2005) Nature , vol.433 , Issue.7024 , pp. 430-433
    • Esnault, C.1
  • 181
    • 33749384520 scopus 로고    scopus 로고
    • The anti-HIV-1 editing enzyme APOBEC3G binds HIV-1 RNA and messenger RNAs that shuttle between polysomes and stress granules
    • Kozak, S. L., et al. (2006) The anti-HIV-1 editing enzyme APOBEC3G binds HIV-1 RNA and messenger RNAs that shuttle between polysomes and stress granules. J Biol Chem 281 (39), 29105-29115.
    • (2006) J Biol Chem , vol.281 , Issue.39 , pp. 29105-29115
    • Kozak, S.L.1
  • 182
    • 33745067722 scopus 로고    scopus 로고
    • APOBEC3G DNA deaminase acts processively 30!50 on single-stranded DNA
    • Chelico, L., et al. (2006) APOBEC3G DNA deaminase acts processively 30!50 on single-stranded DNA. Nat Struct Mol Biol 13 (5), 392-399.
    • (2006) Nat Struct Mol Biol , vol.13 , Issue.5 , pp. 392-399
    • Chelico, L.1
  • 183
    • 33646443637 scopus 로고    scopus 로고
    • Monomeric APOBEC3G is catalytically active and has antiviral activity
    • Opi, S., et al. (2006) Monomeric APOBEC3G is catalytically active and has antiviral activity. J Virol 80 (10), 4673-4682.
    • (2006) J Virol , vol.80 , Issue.10 , pp. 4673-4682
    • Opi, S.1
  • 184
    • 33748640960 scopus 로고    scopus 로고
    • Antiviral potency of APOBEC proteins does not correlate with cytidine deamination
    • Bishop, K. N., Holmes, R. K., and Malim, M. H. (2006) Antiviral potency of APOBEC proteins does not correlate with cytidine deamination. J Virol 80 (17), 8450-8458.
    • (2006) J Virol , vol.80 , Issue.17 , pp. 8450-8458
    • Bishop, K.N.1    Holmes, R.K.2    Malim, M.H.3
  • 185
    • 33751206549 scopus 로고    scopus 로고
    • Inhibition of formula-primedreverse transcription by humanAPOBEC3Gduring human immunodeficiency virus type 1 replication
    • Guo,F., et al. (2006) Inhibition of formula-primedreverse transcription by humanAPOBEC3Gduring human immunodeficiency virus type 1 replication. J Virol 80 (23), 11710-11722.
    • (2006) J Virol , vol.80 , Issue.23 , pp. 11710-11722
    • Guo, F.1
  • 186
    • 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. (2002) Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein. Nature 418 (6898), 646-650.
    • (2002) Nature , vol.418 , Issue.6898 , pp. 646-650
    • Sheehy, A.M.1
  • 187
    • 14744275703 scopus 로고    scopus 로고
    • The power of phylogenetic comparison in revealing protein function
    • Yang, Z. (2005) The power of phylogenetic comparison in revealing protein function. Proc Natl Acad Sci USA 102 (9), 3179-3180.
    • (2005) Proc Natl Acad Sci USA , vol.102 , Issue.9 , pp. 3179-3180
    • Yang, Z.1
  • 188
    • 33645141552 scopus 로고    scopus 로고
    • Patterns of evolution of host proteins involved in retroviral pathogenesis
    • Ortiz, M., et al. (2006) Patterns of evolution of host proteins involved in retroviral pathogenesis. Retrovirology 3, 11.
    • (2006) Retrovirology , vol.3 , pp. 11
    • Ortiz, M.1
  • 189
    • 1642367210 scopus 로고    scopus 로고
    • Asingle amino acid difference in the hostAPOBEC3Gprotein controls the primate species specificity of HIV type 1 virion infectivity factor
    • Bogerd, H. P., et al. (2004) Asingle amino acid difference in the hostAPOBEC3Gprotein controls the primate species specificity of HIV type 1 virion infectivity factor. Proc Natl Acad Sci USA 101 (11), 3770-3774.
    • (2004) Proc Natl Acad Sci USA , vol.101 , Issue.11 , pp. 3770-3774
    • Bogerd, H.P.1
  • 190
    • 2442511993 scopus 로고    scopus 로고
    • A single amino acid determinant governs the species-specific sensitivity of APOBEC3G to Vif action
    • Mangeat, B., et al. (2004) A single amino acid determinant governs the species-specific sensitivity of APOBEC3G to Vif action. J Biol Chem 279 (15), 14481-14483.
    • (2004) J Biol Chem , vol.279 , Issue.15 , pp. 14481-14483
    • Mangeat, B.1
  • 191
    • 0344845196 scopus 로고    scopus 로고
    • HIV-1 Vif protein binds the editing enzyme APOBEC3G and induces its degradation
    • Marin, M., et al. (2003) HIV-1 Vif protein binds the editing enzyme APOBEC3G and induces its degradation. Nat Med 9 (11), 1398-1403.
    • (2003) Nat Med , vol.9 , Issue.11 , pp. 1398-1403
    • Marin, M.1
  • 192
    • 1642380210 scopus 로고    scopus 로고
    • Asingle amino acid ofAPOBEC3Gcontrols its species-specific interaction with virion infectivity factor (Vif)
    • Schrofelbauer, B., Chen, D., and Landau, N. R. (2004) Asingle amino acid ofAPOBEC3Gcontrols its species-specific interaction with virion infectivity factor (Vif). Proc Natl Acad Sci USA 101 (11), 3927-3932.
    • (2004) Proc Natl Acad Sci USA , vol.101 , Issue.11 , pp. 3927-3932
    • Schrofelbauer, B.1    Chen, D.2    Landau, N.R.3
  • 193
    • 1842732157 scopus 로고    scopus 로고
    • A single amino acid substitution in human APOBEC3G antiretroviral enzyme confers resistance to HIV-1 virion infectivity factor-induced depletion
    • Xu, H., et al. (2004) A single amino acid substitution in human APOBEC3G antiretroviral enzyme confers resistance to HIV-1 virion infectivity factor-induced depletion. Proc Natl Acad Sci USA 101 (15), 5652-5657.
    • (2004) Proc Natl Acad Sci USA , vol.101 , Issue.15 , pp. 5652-5657
    • Xu, H.1
  • 194
    • 33744939997 scopus 로고    scopus 로고
    • Mutational alteration of human immunodeficiency virus type 1 Vif allows for functional interaction with nonhuman primate APOBEC3G
    • Schrofelbauer, B., et al. (2006) Mutational alteration of human immunodeficiency virus type 1 Vif allows for functional interaction with nonhuman primate APOBEC3G. J Virol 80 (12), 5984-5991.
    • (2006) J Virol , vol.80 , Issue.12 , pp. 5984-5991
    • Schrofelbauer, B.1
  • 195
    • 34447340466 scopus 로고    scopus 로고
    • Fromthe cover: discovery and analysis of the first endogenous lentivirus
    • Katzourakis, A., et al. (2007) Fromthe cover: discovery and analysis of the first endogenous lentivirus. Proc Natl Acad Sci USA 104 (15), 6261-6265.
    • (2007) Proc Natl Acad Sci USA , vol.104 , Issue.15 , pp. 6261-6265
    • Katzourakis, A.1
  • 196
    • 3242712200 scopus 로고    scopus 로고
    • Asecond human antiretroviral factor, APOBEC3F, is suppressed by the HIV-1 and HIV-2 Vif proteins
    • Wiegand, H. L., et al. (2004) Asecond human antiretroviral factor, APOBEC3F, is suppressed by the HIV-1 and HIV-2 Vif proteins. EMBO J 23 (12), 2451-2558.
    • (2004) EMBO J , vol.23 , Issue.12 , pp. 2451-2558
    • Wiegand, H.L.1
  • 197
    • 22244448696 scopus 로고    scopus 로고
    • APOBEC3Ghypermutates genomicDNA and inhibits Ty1 retrotransposition in yeast
    • Schumacher, A. J., Nissley, D. V., and Harris, R. S. (2005) APOBEC3Ghypermutates genomicDNA and inhibits Ty1 retrotransposition in yeast. Proc Natl Acad Sci USA 102 (28), 9854-9859.
    • (2005) Proc Natl Acad Sci USA , vol.102 , Issue.28 , pp. 9854-9859
    • Schumacher, A.J.1    Nissley, D.V.2    Harris, R.S.3
  • 198
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • Guex, N. and Peitsch, M. C. (1997) SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling. Electrophoresis 18 (15), 2714-2723.
    • (1997) Electrophoresis , vol.18 , Issue.15 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.