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Volumn 429, Issue 12, 2017, Pages 1787-1799

Family-Wide Comparative Analysis of Cytidine and Methylcytidine Deamination by Eleven Human APOBEC Proteins

Author keywords

APOBEC proteins; C and mC deamination; cytidine deaminase; mC selectivity factor

Indexed keywords

APOLIPOPROTEIN B MRNA EDITING ENZYME CATALYTIC POLYPEPTIDE LIKE; APOLIPOPROTEIN B MRNA EDITING ENZYME CATALYTIC POLYPEPTIDE LIKE 1; APOLIPOPROTEIN B MRNA EDITING ENZYME CATALYTIC POLYPEPTIDE LIKE 2; APOLIPOPROTEIN B MRNA EDITING ENZYME CATALYTIC POLYPEPTIDE LIKE 3A; APOLIPOPROTEIN B MRNA EDITING ENZYME CATALYTIC POLYPEPTIDE LIKE 3B; APOLIPOPROTEIN B MRNA EDITING ENZYME CATALYTIC POLYPEPTIDE LIKE 3C; APOLIPOPROTEIN B MRNA EDITING ENZYME CATALYTIC POLYPEPTIDE LIKE 3D; APOLIPOPROTEIN B MRNA EDITING ENZYME CATALYTIC POLYPEPTIDE LIKE 3F; APOLIPOPROTEIN B MRNA EDITING ENZYME CATALYTIC POLYPEPTIDE LIKE 3G; APOLIPOPROTEIN B MRNA EDITING ENZYME CATALYTIC POLYPEPTIDE LIKE 3H; APOLIPOPROTEIN B MRNA EDITING ENZYME CATALYTIC POLYPEPTIDE LIKE 4; APOLIPOPROTEIN B MRNA EDITING ENZYME CATALYTIC POLYPEPTIDE LIKE AID; CYTIDINE; DEAMINASE; DNA; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG; CYTOSINE;

EID: 85019359917     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2017.04.021     Document Type: Article
Times cited : (67)

References (75)
  • 1
    • 50349093233 scopus 로고    scopus 로고
    • The AID/APOBEC family of nucleic acid mutators
    • Conticello, S.G., The AID/APOBEC family of nucleic acid mutators. Genome Biol., 9, 2008, 229.
    • (2008) Genome Biol. , vol.9 , pp. 229
    • Conticello, S.G.1
  • 2
    • 33644992513 scopus 로고    scopus 로고
    • Directed DNA deamination by AID/APOBEC3 in immunity
    • Macduff, D.A., Harris, R.S., Directed DNA deamination by AID/APOBEC3 in immunity. Curr. Biol. 16 (2006), R186–R189.
    • (2006) Curr. Biol. , vol.16 , pp. R186-R189
    • Macduff, D.A.1    Harris, R.S.2
  • 3
    • 33846555779 scopus 로고    scopus 로고
    • The APOBEC-2 crystal structure and functional implications for the deaminase AID
    • Prochnow, C., Bransteitter, R., Klein, M.G., Goodman, M.F., Chen, X.S., The APOBEC-2 crystal structure and functional implications for the deaminase AID. Nature 445 (2007), 447–451.
    • (2007) Nature , vol.445 , pp. 447-451
    • Prochnow, C.1    Bransteitter, R.2    Klein, M.G.3    Goodman, M.F.4    Chen, X.S.5
  • 4
    • 55549098517 scopus 로고    scopus 로고
    • Crystal structure of the anti-viral APOBEC3G catalytic domain and functional implications
    • Holden, L.G., Prochnow, C., Chang, Y.P., Bransteitter, R., Chelico, L., Sen, U., et al. Crystal structure of the anti-viral APOBEC3G catalytic domain and functional implications. Nature 456 (2008), 121–124.
    • (2008) Nature , vol.456 , pp. 121-124
    • Holden, L.G.1    Prochnow, C.2    Chang, Y.P.3    Bransteitter, R.4    Chelico, L.5    Sen, U.6
  • 5
    • 70349335267 scopus 로고    scopus 로고
    • The current structural and functional understanding of APOBEC deaminases
    • Bransteitter, R., Prochnow, C., Chen, X.S., The current structural and functional understanding of APOBEC deaminases. Cell. Mol. Life Sci. 66 (2009), 3137–3147.
    • (2009) Cell. Mol. Life Sci. , vol.66 , pp. 3137-3147
    • Bransteitter, R.1    Prochnow, C.2    Chen, X.S.3
  • 6
    • 40449114441 scopus 로고    scopus 로고
    • Structure of the DNA deaminase domain of the HIV-1 restriction factor APOBEC3G
    • Chen, K.M., Harjes, E., Gross, P.J., Fahmy, A., Lu, Y., Shindo, K., et al. Structure of the DNA deaminase domain of the HIV-1 restriction factor APOBEC3G. Nature 452 (2008), 116–119.
    • (2008) Nature , vol.452 , pp. 116-119
    • Chen, K.M.1    Harjes, E.2    Gross, P.J.3    Fahmy, A.4    Lu, Y.5    Shindo, K.6
  • 7
    • 73449099592 scopus 로고    scopus 로고
    • Crystal structure of the APOBEC3G catalytic domain reveals potential oligomerization interfaces
    • Shandilya, S.M., Nalam, M.N., Nalivaika, E.A., Gross, P.J., Valesano, J.C., Shindo, K., et al. Crystal structure of the APOBEC3G catalytic domain reveals potential oligomerization interfaces. Structure 18 (2010), 28–38.
    • (2010) Structure , vol.18 , pp. 28-38
    • Shandilya, S.M.1    Nalam, M.N.2    Nalivaika, E.A.3    Gross, P.J.4    Valesano, J.C.5    Shindo, K.6
  • 9
    • 84878677763 scopus 로고    scopus 로고
    • NMR structure of human restriction factor APOBEC3A reveals substrate binding and enzyme specificity
    • Byeon, I.J., Ahn, J., Mitra, M., Byeon, C.H., Hercik, K., Hritz, J., et al. NMR structure of human restriction factor APOBEC3A reveals substrate binding and enzyme specificity. Nat. Commun., 4, 2013, 1890.
    • (2013) Nat. Commun. , vol.4 , pp. 1890
    • Byeon, I.J.1    Ahn, J.2    Mitra, M.3    Byeon, C.H.4    Hercik, K.5    Hritz, J.6
  • 10
    • 84878866554 scopus 로고    scopus 로고
    • Crystal structure of the DNA cytosine deaminase APOBEC3F: the catalytically active and HIV-1 Vif-binding domain
    • Bohn, M.F., Shandilya, S.M., Albin, J.S., Kouno, T., Anderson, B.D., McDougle, R.M., et al. Crystal structure of the DNA cytosine deaminase APOBEC3F: the catalytically active and HIV-1 Vif-binding domain. Structure 21 (2013), 1042–1050.
    • (2013) Structure , vol.21 , pp. 1042-1050
    • Bohn, M.F.1    Shandilya, S.M.2    Albin, J.S.3    Kouno, T.4    Anderson, B.D.5    McDougle, R.M.6
  • 11
    • 84887276822 scopus 로고    scopus 로고
    • Structural determinants of HIV-1 Vif susceptibility and DNA binding in APOBEC3F
    • Siu, K.K., Sultana, A., Azimi, F.C., Lee, J.E., Structural determinants of HIV-1 Vif susceptibility and DNA binding in APOBEC3F. Nat. Commun., 4, 2013, 2593.
    • (2013) Nat. Commun. , vol.4 , pp. 2593
    • Siu, K.K.1    Sultana, A.2    Azimi, F.C.3    Lee, J.E.4
  • 12
    • 84947771457 scopus 로고    scopus 로고
    • Crystal structure of the DNA deaminase APOBEC3B catalytic domain
    • Shi, K., Carpenter, M.A., Kurahashi, K., Harris, R.S., Aihara, H., Crystal structure of the DNA deaminase APOBEC3B catalytic domain. J. Biol. Chem. 290 (2015), 28,120–28,130.
    • (2015) J. Biol. Chem. , vol.290 , pp. 28120-28130
    • Shi, K.1    Carpenter, M.A.2    Kurahashi, K.3    Harris, R.S.4    Aihara, H.5
  • 13
    • 84987790072 scopus 로고    scopus 로고
    • AID and APOBECs span the gap between innate and adaptive immunity
    • Moris, A., Murray, S., Cardinaud, S., AID and APOBECs span the gap between innate and adaptive immunity. Front. Microbiol., 5, 2014, 534.
    • (2014) Front. Microbiol. , vol.5 , pp. 534
    • Moris, A.1    Murray, S.2    Cardinaud, S.3
  • 14
    • 84882417741 scopus 로고    scopus 로고
    • The APOBEC3 family of retroelement restriction factors
    • Refsland, E.W., Harris, R.S., The APOBEC3 family of retroelement restriction factors. Curr. Top. Microbiol. Immunol. 371 (2013), 1–27.
    • (2013) Curr. Top. Microbiol. Immunol. , vol.371 , pp. 1-27
    • Refsland, E.W.1    Harris, R.S.2
  • 17
    • 58249114897 scopus 로고    scopus 로고
    • Sole copy of Z2-type human cytidine deaminase APOBEC3H has inhibitory activity against retrotransposons and HIV-1
    • Tan, L., Sarkis, P.T., Wang, T., Tian, C., Yu, X.F., Sole copy of Z2-type human cytidine deaminase APOBEC3H has inhibitory activity against retrotransposons and HIV-1. FASEB J. 23 (2009), 279–287.
    • (2009) FASEB J. , vol.23 , pp. 279-287
    • Tan, L.1    Sarkis, P.T.2    Wang, T.3    Tian, C.4    Yu, X.F.5
  • 18
    • 50849100134 scopus 로고    scopus 로고
    • Antiretroelement activity of APOBEC3H was lost twice in recent human evolution
    • OhAinle, M., Kerns, J.A., Li, M.M., Malik, H.S., Emerman, M., Antiretroelement activity of APOBEC3H was lost twice in recent human evolution. Cell Host Microbe 4 (2008), 249–259.
    • (2008) Cell Host Microbe , vol.4 , pp. 249-259
    • OhAinle, M.1    Kerns, J.A.2    Li, M.M.3    Malik, H.S.4    Emerman, M.5
  • 19
    • 8544241736 scopus 로고    scopus 로고
    • Retroviral restriction by APOBEC proteins
    • Harris, R.S., Liddament, M.T., Retroviral restriction by APOBEC proteins. Nat. Rev. Immunol. 4 (2004), 868–877.
    • (2004) Nat. Rev. Immunol. , vol.4 , pp. 868-877
    • Harris, R.S.1    Liddament, M.T.2
  • 20
    • 77749335648 scopus 로고    scopus 로고
    • APOBEC deaminases-mutases with defensive roles for immunity
    • Prochnow, C., Bransteitter, R., Chen, X.S., APOBEC deaminases-mutases with defensive roles for immunity. Sci. China C Life Sci. 52 (2009), 893–902.
    • (2009) Sci. China C Life Sci. , vol.52 , pp. 893-902
    • Prochnow, C.1    Bransteitter, R.2    Chen, X.S.3
  • 21
    • 67149120661 scopus 로고    scopus 로고
    • The prospct of APOBEC3G for the future of HIV therapy
    • Prochnow, C., Goodman, M.F., Chen, X.S., The prospct of APOBEC3G for the future of HIV therapy. HIV Ther. 3 (2009), 7–10.
    • (2009) HIV Ther. , vol.3 , pp. 7-10
    • Prochnow, C.1    Goodman, M.F.2    Chen, X.S.3
  • 22
    • 10944223445 scopus 로고    scopus 로고
    • Biochemical analysis of hyper-mutational targeting by wild type and mutant AID
    • Bransteitter, R., Pham, P., Calabrese, P., Goodman, M.F., Biochemical analysis of hyper-mutational targeting by wild type and mutant AID. J. Biol. Chem. 279 (2004), 51,612–51,621.
    • (2004) J. Biol. Chem. , vol.279 , pp. 51612-51621
    • Bransteitter, R.1    Pham, P.2    Calabrese, P.3    Goodman, M.F.4
  • 23
    • 2942613670 scopus 로고    scopus 로고
    • AID: how does it aid antibody diversity?
    • Honjo, T., Muramatsu, M., Fagarasan, S., AID: how does it aid antibody diversity?. Immunity 20 (2004), 659–668.
    • (2004) Immunity , vol.20 , pp. 659-668
    • Honjo, T.1    Muramatsu, M.2    Fagarasan, S.3
  • 24
    • 0041381361 scopus 로고    scopus 로고
    • AID mutant analyses indicate requirement for class-switch-specific cofactors
    • (Epub 2003 Aug 10)
    • Ta, V.T., Nagaoka, H., Catalan, N., Durandy, A., Fischer, A., Imai, K., et al. AID mutant analyses indicate requirement for class-switch-specific cofactors. Nat. Immunol. 4 (2003), 843–848 (Epub 2003 Aug 10).
    • (2003) Nat. Immunol. , vol.4 , pp. 843-848
    • Ta, V.T.1    Nagaoka, H.2    Catalan, N.3    Durandy, A.4    Fischer, A.5    Imai, K.6
  • 25
    • 0037452080 scopus 로고    scopus 로고
    • Transcription-targeted DNA deamination by the AID antibody diversification enzyme
    • Chaudhuri, J., Tian, M., Khuong, C., Chua, K., Pinaud, E., Alt, F.W., 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    Tian, M.2    Khuong, C.3    Chua, K.4    Pinaud, E.5    Alt, F.W.6
  • 26
    • 3242795967 scopus 로고    scopus 로고
    • Separate domains of AID are required for somatic hypermutation and class-switch recombination
    • (Epub 2004 Jun 13)
    • Shinkura, R., Ito, S., Begum, N.A., Nagaoka, H., Muramatsu, M., Kinoshita, K., et al. Separate domains of AID are required for somatic hypermutation and class-switch recombination. Nat. Immunol. 5 (2004), 707–712 (Epub 2004 Jun 13).
    • (2004) Nat. Immunol. , vol.5 , pp. 707-712
    • Shinkura, R.1    Ito, S.2    Begum, N.A.3    Nagaoka, H.4    Muramatsu, M.5    Kinoshita, K.6
  • 27
    • 0034264851 scopus 로고    scopus 로고
    • Activation-induced cytidine deaminase (AID) deficiency causes the autosomal recessive form of the hyper-IgM syndrome (HIGM2)
    • Revy, P., Muto, T., Levy, Y., Geissmann, F., Plebani, A., Sanal, O., 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    Muto, T.2    Levy, Y.3    Geissmann, F.4    Plebani, A.5    Sanal, O.6
  • 28
    • 0027434027 scopus 로고
    • The p27 catalytic subunit of the apolipoprotein B mRNA editing enzyme is a cytidine deaminase
    • Navaratnam, N., Morrison, J.R., Bhattacharya, S., Patel, D., Funahashi, T., Giannoni, F., et al. The p27 catalytic subunit of the apolipoprotein B mRNA editing enzyme is a cytidine deaminase. J. Biol. Chem. 268 (1993), 20,709–20,712.
    • (1993) J. Biol. Chem. , vol.268 , pp. 20709-20712
    • Navaratnam, N.1    Morrison, J.R.2    Bhattacharya, S.3    Patel, D.4    Funahashi, T.5    Giannoni, F.6
  • 29
    • 84894582649 scopus 로고    scopus 로고
    • APOBEC3 multimerization correlates with HIV-1 packaging and restriction activity in living cells
    • Li, J., Chen, Y., Li, M., Carpenter, M.A., McDougle, R.M., Luengas, E.M., et al. APOBEC3 multimerization correlates with HIV-1 packaging and restriction activity in living cells. J. Mol. Biol. 426 (2014), 1296–1307.
    • (2014) J. Mol. Biol. , vol.426 , pp. 1296-1307
    • Li, J.1    Chen, Y.2    Li, M.3    Carpenter, M.A.4    McDougle, R.M.5    Luengas, E.M.6
  • 30
    • 80053493431 scopus 로고    scopus 로고
    • Core-APOBEC3C chimerical protein inhibits hepatitis B virus replication
    • Li, D., Liu, J., Kang, F., Guan, W., Gao, X., Wang, Y., et al. Core-APOBEC3C chimerical protein inhibits hepatitis B virus replication. J. Biochem. 150 (2011), 371–374.
    • (2011) J. Biochem. , vol.150 , pp. 371-374
    • Li, D.1    Liu, J.2    Kang, F.3    Guan, W.4    Gao, X.5    Wang, Y.6
  • 32
    • 42049096136 scopus 로고    scopus 로고
    • Evidence for editing of human papillomavirus DNA by APOBEC3 in benign and precancerous lesions
    • Vartanian, J.P., Guetard, D., Henry, M., Wain-Hobson, S., Evidence for editing of human papillomavirus DNA by APOBEC3 in benign and precancerous lesions. Science 320 (2008), 230–233.
    • (2008) Science , vol.320 , pp. 230-233
    • Vartanian, J.P.1    Guetard, D.2    Henry, M.3    Wain-Hobson, S.4
  • 33
    • 84891692481 scopus 로고    scopus 로고
    • APOBEC3 deaminases induce hypermutation in human papillomavirus 16 DNA upon beta interferon stimulation
    • Wang, Z., Wakae, K., Kitamura, K., Aoyama, S., Liu, G., Koura, M., et al. APOBEC3 deaminases induce hypermutation in human papillomavirus 16 DNA upon beta interferon stimulation. J. Virol. 88 (2014), 1308–1317.
    • (2014) J. Virol. , vol.88 , pp. 1308-1317
    • Wang, Z.1    Wakae, K.2    Kitamura, K.3    Aoyama, S.4    Liu, G.5    Koura, M.6
  • 34
    • 84919459598 scopus 로고    scopus 로고
    • APOBEC3A functions as a restriction factor of human papillomavirus
    • Warren, C.J., Xu, T., Guo, K., Griffin, L.M., Westrich, J.A., Lee, D., et al. APOBEC3A functions as a restriction factor of human papillomavirus. J. Virol. 89 (2015), 688–702.
    • (2015) J. Virol. , vol.89 , pp. 688-702
    • Warren, C.J.1    Xu, T.2    Guo, K.3    Griffin, L.M.4    Westrich, J.A.5    Lee, D.6
  • 35
  • 36
    • 34548779664 scopus 로고    scopus 로고
    • Hepatitis B virus DNA is subject to extensive editing by the human deaminase APOBEC3C
    • Baumert, T.F., Rosler, C., Malim, M.H., von Weizsacker, F., Hepatitis B virus DNA is subject to extensive editing by the human deaminase APOBEC3C. Hepatology 46 (2007), 682–689.
    • (2007) Hepatology , vol.46 , pp. 682-689
    • Baumert, T.F.1    Rosler, C.2    Malim, M.H.3    von Weizsacker, F.4
  • 38
    • 33747466389 scopus 로고    scopus 로고
    • Inhibition of hepatitis B virus replication by APOBEC3G in vitro and in vivo
    • Lei, Y.C., Hao, Y.H., Zhang, Z.M., Tian, Y.J., Wang, B.J., Yang, Y., et al. Inhibition of hepatitis B virus replication by APOBEC3G in vitro and in vivo. World J. Gastroenterol. 12 (2006), 4492–4497.
    • (2006) World J. Gastroenterol. , vol.12 , pp. 4492-4497
    • Lei, Y.C.1    Hao, Y.H.2    Zhang, Z.M.3    Tian, Y.J.4    Wang, B.J.5    Yang, Y.6
  • 39
    • 84982703210 scopus 로고    scopus 로고
    • Crystal structures of APOBEC3G N-domain alone and its complex with DNA
    • Xiao, X., Li, S.X., Yang, H., Chen, X.S., Crystal structures of APOBEC3G N-domain alone and its complex with DNA. Nat. Commun., 7, 2016, 12,193.
    • (2016) Nat. Commun. , vol.7 , pp. 12193
    • Xiao, X.1    Li, S.X.2    Yang, H.3    Chen, X.S.4
  • 40
    • 79952759408 scopus 로고    scopus 로고
    • Mutator effects and mutation signatures of editing deaminases produced in bacteria and yeast
    • Lada, A.G., Krick, C.F., Kozmin, S.G., Mayorov, V.I., Karpova, T.S., Rogozin, I.B., et al. Mutator effects and mutation signatures of editing deaminases produced in bacteria and yeast. Biochemistry (Mosc) 76 (2011), 131–146.
    • (2011) Biochemistry (Mosc) , vol.76 , pp. 131-146
    • Lada, A.G.1    Krick, C.F.2    Kozmin, S.G.3    Mayorov, V.I.4    Karpova, T.S.5    Rogozin, I.B.6
  • 41
    • 0036863733 scopus 로고    scopus 로고
    • RNA editing enzyme APOBEC1 and some of its homologs can act as DNA mutators
    • Harris, R.S., Petersen-Mahrt, S.K., Neuberger, M.S., 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    Petersen-Mahrt, S.K.2    Neuberger, M.S.3
  • 42
    • 0037388165 scopus 로고    scopus 로고
    • Activation-induced cytidine deaminase deaminates deoxycytidine on single-stranded DNA but requires the action of RNase
    • Bransteitter, R., Pham, P., Scharff, M.D., Goodman, M.F., Activation-induced cytidine deaminase deaminates deoxycytidine on single-stranded DNA but requires the action of RNase. Proc. Natl. Acad. Sci. U. S. A. 100 (2003), 4102–4107.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 4102-4107
    • Bransteitter, R.1    Pham, P.2    Scharff, M.D.3    Goodman, M.F.4
  • 43
    • 10644282845 scopus 로고    scopus 로고
    • Activation-induced cytidine deaminase deaminates 5-methylcytosine in DNA and is expressed in pluripotent tissues: implications for epigenetic reprogramming
    • (Epub 2004 Sep 24)
    • Morgan, H.D., Dean, W., Coker, H.A., Reik, W., Petersen-Mahrt, S.K., Activation-induced cytidine deaminase deaminates 5-methylcytosine in DNA and is expressed in pluripotent tissues: implications for epigenetic reprogramming. J. Biol. Chem. 279 (2004), 52,353–52,360 (Epub 2004 Sep 24).
    • (2004) J. Biol. Chem. , vol.279 , pp. 52353-52360
    • Morgan, H.D.1    Dean, W.2    Coker, H.A.3    Reik, W.4    Petersen-Mahrt, S.K.5
  • 45
    • 84865329141 scopus 로고    scopus 로고
    • AID/APOBEC deaminases disfavor modified cytosines implicated in DNA demethylation
    • Nabel, C.S., Jia, H., Ye, Y., Shen, L., Goldschmidt, H.L., Stivers, J.T., et al. AID/APOBEC deaminases disfavor modified cytosines implicated in DNA demethylation. Nat. Chem. Biol. 8 (2012), 751–758.
    • (2012) Nat. Chem. Biol. , vol.8 , pp. 751-758
    • Nabel, C.S.1    Jia, H.2    Ye, Y.3    Shen, L.4    Goldschmidt, H.L.5    Stivers, J.T.6
  • 46
    • 84867270112 scopus 로고    scopus 로고
    • Efficient deamination of 5-methylcytosines in DNA by human APOBEC3A, but not by AID or APOBEC3G
    • Wijesinghe, P., Bhagwat, A.S., Efficient deamination of 5-methylcytosines in DNA by human APOBEC3A, but not by AID or APOBEC3G. Nucleic Acids Res. 40 (2012), 9206–9217.
    • (2012) Nucleic Acids Res. , vol.40 , pp. 9206-9217
    • Wijesinghe, P.1    Bhagwat, A.S.2
  • 47
    • 84867266936 scopus 로고    scopus 로고
    • Methylcytosine and normal cytosine deamination by the foreign DNA restriction enzyme APOBEC3A
    • Carpenter, M.A., Li, M., Rathore, A., Lackey, L., Law, E.K., Land, A.M., et al. Methylcytosine and normal cytosine deamination by the foreign DNA restriction enzyme APOBEC3A. J. Biol. Chem. 287 (2012), 34,801–34,808.
    • (2012) J. Biol. Chem. , vol.287 , pp. 34801-34808
    • Carpenter, M.A.1    Li, M.2    Rathore, A.3    Lackey, L.4    Law, E.K.5    Land, A.M.6
  • 48
    • 84879255759 scopus 로고    scopus 로고
    • Efficient deamination of 5-methylcytidine and 5-substituted cytidine residues in DNA by human APOBEC3A cytidine deaminase
    • Suspene, R., Aynaud, M.M., Vartanian, J.P., Wain-Hobson, S., Efficient deamination of 5-methylcytidine and 5-substituted cytidine residues in DNA by human APOBEC3A cytidine deaminase. PLoS One, 8, 2013, e63461.
    • (2013) PLoS One , vol.8
    • Suspene, R.1    Aynaud, M.M.2    Vartanian, J.P.3    Wain-Hobson, S.4
  • 49
    • 84942327978 scopus 로고    scopus 로고
    • DNA cytosine and methylcytosine deamination by APOBEC3B: enhancing methylcytosine deamination by engineering APOBEC3B
    • Fu, Y., Ito, F., Zhang, G., Fernandez, B., Yang, H., Chen, X.S., DNA cytosine and methylcytosine deamination by APOBEC3B: enhancing methylcytosine deamination by engineering APOBEC3B. Biochem. J. 471 (2015), 25–35.
    • (2015) Biochem. J. , vol.471 , pp. 25-35
    • Fu, Y.1    Ito, F.2    Zhang, G.3    Fernandez, B.4    Yang, H.5    Chen, X.S.6
  • 50
    • 84994173179 scopus 로고    scopus 로고
    • Biochemical characterization of APOBEC3H variants: implications for their HIV-1 restriction activity and mC modification
    • Gu, J., Chen, Q., Xiao, X., Ito, F., Wolfe, A., Chen, X.S., Biochemical characterization of APOBEC3H variants: implications for their HIV-1 restriction activity and mC modification. J. Mol. Biol. 428 (2016), 4626–4638.
    • (2016) J. Mol. Biol. , vol.428 , pp. 4626-4638
    • Gu, J.1    Chen, Q.2    Xiao, X.3    Ito, F.4    Wolfe, A.5    Chen, X.S.6
  • 51
    • 84923309215 scopus 로고    scopus 로고
    • A prevalent cancer susceptibility APOBEC3A hybrid allele bearing APOBEC3B 3′UTR enhances chromosomal DNA damage
    • Caval, V., Suspene, R., Shapira, M., Vartanian, J.P., Wain-Hobson, S., A prevalent cancer susceptibility APOBEC3A hybrid allele bearing APOBEC3B 3′UTR enhances chromosomal DNA damage. Nat. Commun., 5, 2014, 5129.
    • (2014) Nat. Commun. , vol.5 , pp. 5129
    • Caval, V.1    Suspene, R.2    Shapira, M.3    Vartanian, J.P.4    Wain-Hobson, S.5
  • 52
    • 77249148019 scopus 로고    scopus 로고
    • Genome-wide erasure of DNA methylation in mouse primordial germ cells is affected by AID deficiency
    • Popp, C., Dean, W., Feng, S., Cokus, S.J., Andrews, S., Pellegrini, M., et al. Genome-wide erasure of DNA methylation in mouse primordial germ cells is affected by AID deficiency. Nature 463 (2010), 1101–1105.
    • (2010) Nature , vol.463 , pp. 1101-1105
    • Popp, C.1    Dean, W.2    Feng, S.3    Cokus, S.J.4    Andrews, S.5    Pellegrini, M.6
  • 53
    • 77649104794 scopus 로고    scopus 로고
    • Reprogramming towards pluripotency requires AID-dependent DNA demethylation
    • Bhutani, N., Brady, J.J., Damian, M., Sacco, A., Corbel, S.Y., Blau, H.M., Reprogramming towards pluripotency requires AID-dependent DNA demethylation. Nature 463 (2010), 1042–1047.
    • (2010) Nature , vol.463 , pp. 1042-1047
    • Bhutani, N.1    Brady, J.J.2    Damian, M.3    Sacco, A.4    Corbel, S.Y.5    Blau, H.M.6
  • 54
    • 84879415206 scopus 로고    scopus 로고
    • A comprehensive analysis of the effects of the deaminase AID on the transcriptome and methylome of activated B cells
    • Fritz, E.L., Rosenberg, B.R., Lay, K., Mihailovic, A., Tuschl, T., Papavasiliou, F.N., A comprehensive analysis of the effects of the deaminase AID on the transcriptome and methylome of activated B cells. Nat. Immunol. 14 (2013), 749–755.
    • (2013) Nat. Immunol. , vol.14 , pp. 749-755
    • Fritz, E.L.1    Rosenberg, B.R.2    Lay, K.3    Mihailovic, A.4    Tuschl, T.5    Papavasiliou, F.N.6
  • 55
    • 58149374613 scopus 로고    scopus 로고
    • Polymorphisms and splice variants influence the antiretroviral activity of human APOBEC3H
    • Harari, A., Ooms, M., Mulder, L.C., Simon, V., Polymorphisms and splice variants influence the antiretroviral activity of human APOBEC3H. J. Virol. 83 (2009), 295–303.
    • (2009) J. Virol. , vol.83 , pp. 295-303
    • Harari, A.1    Ooms, M.2    Mulder, L.C.3    Simon, V.4
  • 56
    • 79952611071 scopus 로고    scopus 로고
    • Analysis of human APOBEC3H haplotypes and anti-human immunodeficiency virus type 1 activity
    • Wang, X., Abudu, A., Son, S., Dang, Y., Venta, P.J., Zheng, Y.H., Analysis of human APOBEC3H haplotypes and anti-human immunodeficiency virus type 1 activity. J. Virol. 85 (2011), 3142–3152.
    • (2011) J. Virol. , vol.85 , pp. 3142-3152
    • Wang, X.1    Abudu, A.2    Son, S.3    Dang, Y.4    Venta, P.J.5    Zheng, Y.H.6
  • 57
    • 0037926476 scopus 로고    scopus 로고
    • Processive AID-catalysed cytosine deamination on single-stranded DNA simulates somatic hypermutation
    • Pham, P., Bransteitter, R., Petruska, J., Goodman, M.F., Processive AID-catalysed cytosine deamination on single-stranded DNA simulates somatic hypermutation. Nature 424 (2003), 103–107.
    • (2003) Nature , vol.424 , pp. 103-107
    • Pham, P.1    Bransteitter, R.2    Petruska, J.3    Goodman, M.F.4
  • 58
    • 0037019315 scopus 로고    scopus 로고
    • AID mutates E. coli suggesting a DNA deamination mechanism for antibody diversification
    • Petersen-Mahrt, S.K., Harris, R.S., Neuberger, M.S., AID mutates E. coli suggesting a DNA deamination mechanism for antibody diversification. Nature 418 (2002), 99–103.
    • (2002) Nature , vol.418 , pp. 99-103
    • Petersen-Mahrt, S.K.1    Harris, R.S.2    Neuberger, M.S.3
  • 60
    • 84924341659 scopus 로고    scopus 로고
    • The RNA editing enzyme APOBEC1 induces somatic mutations and a compatible mutational signature is present in esophageal adenocarcinomas
    • Saraconi, G., Severi, F., Sala, C., Mattiuz, G., Conticello, S.G., The RNA editing enzyme APOBEC1 induces somatic mutations and a compatible mutational signature is present in esophageal adenocarcinomas. Genome Biol., 15, 2014, 417.
    • (2014) Genome Biol. , vol.15 , pp. 417
    • Saraconi, G.1    Severi, F.2    Sala, C.3    Mattiuz, G.4    Conticello, S.G.5
  • 61
    • 33750344250 scopus 로고    scopus 로고
    • Identification of APOBEC3DE as another antiretroviral factor from the human APOBEC family
    • Dang, Y., Wang, X., Esselman, W.J., Zheng, Y.H., Identification of APOBEC3DE as another antiretroviral factor from the human APOBEC family. J. Virol. 80 (2006), 10,522–10,533.
    • (2006) J. Virol. , vol.80 , pp. 10522-10533
    • Dang, Y.1    Wang, X.2    Esselman, W.J.3    Zheng, Y.H.4
  • 62
    • 84971215822 scopus 로고    scopus 로고
    • The in vitro biochemical characterization of an HIV-1 restriction factor APOBEC3F: importance of loop 7 on both CD1 and CD2 for DNA binding and deamination
    • Chen, Q., Xiao, X., Wolfe, A., Chen, X.S., The in vitro biochemical characterization of an HIV-1 restriction factor APOBEC3F: importance of loop 7 on both CD1 and CD2 for DNA binding and deamination. J. Mol. Biol. 428 (2016), 2661–2670.
    • (2016) J. Mol. Biol. , vol.428 , pp. 2661-2670
    • Chen, Q.1    Xiao, X.2    Wolfe, A.3    Chen, X.S.4
  • 63
    • 84885641866 scopus 로고    scopus 로고
    • A biochemical analysis linking APOBEC3A to disparate HIV-1 restriction and skin cancer
    • Pham, P., Landolph, A., Mendez, C., Li, N., Goodman, M.F., A biochemical analysis linking APOBEC3A to disparate HIV-1 restriction and skin cancer. J. Biol. Chem. 288 (2013), 29,294–29,304.
    • (2013) J. Biol. Chem. , vol.288 , pp. 29294-29304
    • Pham, P.1    Landolph, A.2    Mendez, C.3    Li, N.4    Goodman, M.F.5
  • 64
    • 84874590585 scopus 로고    scopus 로고
    • A critical role for AID in the initiation of reprogramming to induced pluripotent stem cells
    • Bhutani, N., Decker, M.N., Brady, J.J., Bussat, R.T., Burns, D.M., Corbel, S.Y., et al. A critical role for AID in the initiation of reprogramming to induced pluripotent stem cells. FASEB J. 27 (2013), 1107–1113.
    • (2013) FASEB J. , vol.27 , pp. 1107-1113
    • Bhutani, N.1    Decker, M.N.2    Brady, J.J.3    Bussat, R.T.4    Burns, D.M.5    Corbel, S.Y.6
  • 65
    • 84881476513 scopus 로고    scopus 로고
    • AID stabilizes stem-cell phenotype by removing epigenetic memory of pluripotency genes
    • Kumar, R., DiMenna, L., Schrode, N., Liu, T.C., Franck, P., Munoz-Descalzo, S., et al. AID stabilizes stem-cell phenotype by removing epigenetic memory of pluripotency genes. Nature 500 (2013), 89–92.
    • (2013) Nature , vol.500 , pp. 89-92
    • Kumar, R.1    DiMenna, L.2    Schrode, N.3    Liu, T.C.4    Franck, P.5    Munoz-Descalzo, S.6
  • 69
    • 84884709231 scopus 로고    scopus 로고
    • Cancer mutation signatures, DNA damage mechanisms, and potential clinical implications
    • Harris, R.S., Cancer mutation signatures, DNA damage mechanisms, and potential clinical implications. Genome Med., 5, 2013, 87.
    • (2013) Genome Med. , vol.5 , pp. 87
    • Harris, R.S.1
  • 70
    • 84891276148 scopus 로고    scopus 로고
    • APOBEC3B upregulation and genomic mutation patterns in serous ovarian carcinoma
    • Leonard, B., Hart, S.N., Burns, M.B., Carpenter, M.A., Temiz, N.A., Rathore, A., et al. APOBEC3B upregulation and genomic mutation patterns in serous ovarian carcinoma. Cancer Res. 73 (2013), 7222–7231.
    • (2013) Cancer Res. , vol.73 , pp. 7222-7231
    • Leonard, B.1    Hart, S.N.2    Burns, M.B.3    Carpenter, M.A.4    Temiz, N.A.5    Rathore, A.6
  • 71
    • 84883356320 scopus 로고    scopus 로고
    • Evidence for APOBEC3B mutagenesis in multiple human cancers
    • Burns, M.B., Temiz, N.A., Harris, R.S., Evidence for APOBEC3B mutagenesis in multiple human cancers. Nat. Genet. 45 (2013), 977–983.
    • (2013) Nat. Genet. , vol.45 , pp. 977-983
    • Burns, M.B.1    Temiz, N.A.2    Harris, R.S.3
  • 72
    • 84883394595 scopus 로고    scopus 로고
    • APOBEC3B mutagenesis in cancer
    • Kuong, K.J., Loeb, L.A., APOBEC3B mutagenesis in cancer. Nat. Genet. 45 (2013), 964–965.
    • (2013) Nat. Genet. , vol.45 , pp. 964-965
    • Kuong, K.J.1    Loeb, L.A.2
  • 73
    • 84879061509 scopus 로고    scopus 로고
    • DNA deaminases induce break-associated mutation showers with implication of APOBEC3B and 3A in breast cancer kataegis
    • Taylor, B.J., Nik-Zainal, S., Wu, Y.L., Stebbings, L.A., Raine, K., Campbell, P.J., et al. DNA deaminases induce break-associated mutation showers with implication of APOBEC3B and 3A in breast cancer kataegis. elife, 2, 2013, e00534.
    • (2013) elife , vol.2 , pp. e00534
    • Taylor, B.J.1    Nik-Zainal, S.2    Wu, Y.L.3    Stebbings, L.A.4    Raine, K.5    Campbell, P.J.6
  • 74
    • 77952399342 scopus 로고    scopus 로고
    • Structural model for deoxycytidine deamination mechanisms of the HIV-1 inactivation enzyme APOBEC3G
    • Chelico, L., Prochnow, C., Erie, D.A., Chen, X.S., Goodman, M.F., Structural model for deoxycytidine deamination mechanisms of the HIV-1 inactivation enzyme APOBEC3G. J. Biol. Chem. 285 (2010), 16,195–16,205.
    • (2010) J. Biol. Chem. , vol.285 , pp. 16195-16205
    • Chelico, L.1    Prochnow, C.2    Erie, D.A.3    Chen, X.S.4    Goodman, M.F.5


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