메뉴 건너뛰기




Volumn 82, Issue 3, 2008, Pages 1305-1313

Species-specific restriction of Apobec3-mediated hypermutation

Author keywords

[No Author keywords available]

Indexed keywords

APOBEC3 PROTEIN; APOLIPOPROTEIN B MESSENGER RNA EDITING ENZYME CATALYTIC POLYPEPTIDE 1; COMPLEMENTARY DNA; CYTIDINE DEAMINASE; UNCLASSIFIED DRUG; VIRUS DNA;

EID: 38349096771     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.01371-07     Document Type: Article
Times cited : (66)

References (34)
  • 2
    • 33748640960 scopus 로고    scopus 로고
    • Antiviral potency of APOBEC proteins does not correlate with cytidine deamination
    • Bishop, K. N., R. K. Holmes, and M. H. Malim. 2006. Antiviral potency of APOBEC proteins does not correlate with cytidine deamination. J. Virol. 80:8450-8458.
    • (2006) J. Virol , vol.80 , pp. 8450-8458
    • Bishop, K.N.1    Holmes, R.K.2    Malim, M.H.3
  • 5
    • 33744931693 scopus 로고    scopus 로고
    • Multifaceted antiviral actions of APOBEC3 cytidine deaminases
    • Chiu, Y. L., and W. C. Greene. 2006. Multifaceted antiviral actions of APOBEC3 cytidine deaminases. Trends Immunol. 27:291-297.
    • (2006) Trends Immunol , vol.27 , pp. 291-297
    • Chiu, Y.L.1    Greene, W.C.2
  • 7
    • 20744439203 scopus 로고    scopus 로고
    • Differential sensitivity of murine leukemia virus to APOBEC3-mediated inhibition is governed by virion exclusion
    • Doehle, B. P., A. Schafer, H. L. Wiegand, H. P. Bogerd, and B. R. Cullen. 2005. Differential sensitivity of murine leukemia virus to APOBEC3-mediated inhibition is governed by virion exclusion. J. Virol. 79:8201-8207.
    • (2005) J. Virol , vol.79 , pp. 8201-8207
    • Doehle, B.P.1    Schafer, A.2    Wiegand, H.L.3    Bogerd, H.P.4    Cullen, B.R.5
  • 10
    • 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., M. T. Liddament, and R. S. Harris. 2005. The retroviral hypermutation specificity of APOBEC3F and APOBEC3G is governed by the C-terminal DNA cytosine deaminase domain. J. Biol. Chem. 280:10920-10924.
    • (2005) J. Biol. Chem , vol.280 , pp. 10920-10924
    • Hache, G.1    Liddament, M.T.2    Harris, R.S.3
  • 11
    • 33846031136 scopus 로고    scopus 로고
    • Reversed functional organization of mouse and human APOBEC3 cytidine deaminase domains
    • Hakata, Y., and N. R. Landau. 2006. Reversed functional organization of mouse and human APOBEC3 cytidine deaminase domains. J. Biol. Chem. 281:36624-36631.
    • (2006) J. Biol. Chem , vol.281 , pp. 36624-36631
    • Hakata, Y.1    Landau, N.R.2
  • 12
    • 33847625391 scopus 로고    scopus 로고
    • APOBEC3F can inhibit the accumulation of HIV-1 reverse transcription products in the absence of hypermutation: Comparisons with APOBEC3G
    • Holmes, R. K., F. A. Koning, K. N. Bishop, and M. H. Malim. 2006. APOBEC3F can inhibit the accumulation of HIV-1 reverse transcription products in the absence of hypermutation: comparisons with APOBEC3G. J. Biol. Chem. 282:2587-2595.
    • (2006) J. Biol. Chem , vol.282 , pp. 2587-2595
    • Holmes, R.K.1    Koning, F.A.2    Bishop, K.N.3    Malim, M.H.4
  • 14
    • 36148995875 scopus 로고    scopus 로고
    • APOBEC3G inhibits DNA strand transfer during HIV-1 reverse transcription
    • Li, X. Y., F. Guo, L. Zhang, L. Kleiman, and S. Cen. 2007. APOBEC3G inhibits DNA strand transfer during HIV-1 reverse transcription. J. Biol. Chem. 282:32065-32074.
    • (2007) J. Biol. Chem , vol.282 , pp. 32065-32074
    • Li, X.Y.1    Guo, F.2    Zhang, L.3    Kleiman, L.4    Cen, S.5
  • 15
    • 34250857925 scopus 로고    scopus 로고
    • Cytidine deaminases APOBEC3G and APOBEC3F interact with HIV-1 integrase and inhibit proviral DNA formation
    • Luo, K., T. Wang, B. Liu, C. Tian, Z. Xiao, J. Kappes, and X. F. Yu. 2007. Cytidine deaminases APOBEC3G and APOBEC3F interact with HIV-1 integrase and inhibit proviral DNA formation. J. Virol. 81:7238-7248.
    • (2007) J. Virol , vol.81 , pp. 7238-7248
    • Luo, K.1    Wang, T.2    Liu, B.3    Tian, C.4    Xiao, Z.5    Kappes, J.6    Yu, X.F.7
  • 16
    • 0038107587 scopus 로고    scopus 로고
    • Mariani, R., D. Chen, B. Schrofelbauer, F. Navarro, R. Konig, B. Bollman, C. Munk, H. Nymark-McMahon, and N. R. Landau. 2003. Species-specific exclusion of APOBEC3G from HIV-1 virions by Vif. Cell 114:21-31.
    • Mariani, R., D. Chen, B. Schrofelbauer, F. Navarro, R. Konig, B. Bollman, C. Munk, H. Nymark-McMahon, and N. R. Landau. 2003. Species-specific exclusion of APOBEC3G from HIV-1 virions by Vif. Cell 114:21-31.
  • 17
    • 0344845196 scopus 로고    scopus 로고
    • HIV-1 Vif protein binds the editing enzyme APOBEC3G and induces its degradation
    • Marin, M., K. M. Rose, S. L. Kozak, and D. Kabat. 2003. HIV-1 Vif protein binds the editing enzyme APOBEC3G and induces its degradation. Nat. Med. 9:1398-1403.
    • (2003) Nat. Med , vol.9 , pp. 1398-1403
    • Marin, M.1    Rose, K.M.2    Kozak, S.L.3    Kabat, D.4
  • 21
    • 0029955714 scopus 로고    scopus 로고
    • The pCL vector system: Rapid production of helper-free, high-titer, recombinant retroviruses
    • Naviaux, R. K., E. Costanzi, M. Haas, and I. M. Verma. 1996. The pCL vector system: rapid production of helper-free, high-titer, recombinant retroviruses. J. Virol. 70:5701-5705.
    • (1996) J. Virol , vol.70 , pp. 5701-5705
    • Naviaux, R.K.1    Costanzi, E.2    Haas, M.3    Verma, I.M.4
  • 23
    • 33847200788 scopus 로고    scopus 로고
    • APOBEC3 inhibits mouse mammary tumour virus replication in vivo
    • Okeoma, C. M., N. Lovsin, B. M. Peterlin, and S. R. Ross. 2007. APOBEC3 inhibits mouse mammary tumour virus replication in vivo. Nature 445:927-930.
    • (2007) Nature , vol.445 , pp. 927-930
    • Okeoma, C.M.1    Lovsin, N.2    Peterlin, B.M.3    Ross, S.R.4
  • 24
  • 25
    • 25444527785 scopus 로고    scopus 로고
    • APOBEC4, a new member of the AID/APOBEC family of polynucleotide (deoxy)cytidine deaminases predicted by computational analysis
    • Rogozin, I. B., M. K. Basu, I. K. Jordan, Y. I. Pavlov, and E. V. Koonin. 2005. APOBEC4, a new member of the AID/APOBEC family of polynucleotide (deoxy)cytidine deaminases predicted by computational analysis. Cell Cycle 4:1281-1285.
    • (2005) Cell Cycle , vol.4 , pp. 1281-1285
    • Rogozin, I.B.1    Basu, M.K.2    Jordan, I.K.3    Pavlov, Y.I.4    Koonin, E.V.5
  • 26
    • 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., N. C. Gaddis, J. D. Choi, and M. H. Malim. 2002. Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein. Nature 418:646-650.
    • (2002) Nature , vol.418 , pp. 646-650
    • Sheehy, A.M.1    Gaddis, N.C.2    Choi, J.D.3    Malim, M.H.4
  • 27
    • 0344413641 scopus 로고    scopus 로고
    • The antiretroviral enzyme APOBEC3G is degraded by the proteasome in response to HIV-1 Vif
    • Sheehy, A. M., N. C. Gaddis, and M. H. Malim. 2003. The antiretroviral enzyme APOBEC3G is degraded by the proteasome in response to HIV-1 Vif. Nat. Med. 9:1404-1407.
    • (2003) Nat. Med , vol.9 , pp. 1404-1407
    • Sheehy, A.M.1    Gaddis, N.C.2    Malim, M.H.3
  • 28
    • 0141638436 scopus 로고    scopus 로고
    • HIV-1 Vif blocks the antiviral activity of APOBEC3G by impairing both its translation and intracellular stability
    • Stopak, K., C. de Noronha, W. Yonemoto, and W. C. Greene. 2003. HIV-1 Vif blocks the antiviral activity of APOBEC3G by impairing both its translation and intracellular stability. Mol. Cell 12:591-601.
    • (2003) Mol. Cell , vol.12 , pp. 591-601
    • Stopak, K.1    de Noronha, C.2    Yonemoto, W.3    Greene, W.C.4
  • 30
    • 34250186071 scopus 로고    scopus 로고
    • Inhibition of initiation of reverse transcription in HIV-1 by human APOBEC3F
    • Yang, Y., F. Guo, S. Cen, and L. Kleiman. 2007. Inhibition of initiation of reverse transcription in HIV-1 by human APOBEC3F. Virology 365:92-100.
    • (2007) Virology , vol.365 , pp. 92-100
    • Yang, Y.1    Guo, F.2    Cen, S.3    Kleiman, L.4
  • 31
    • 11144244647 scopus 로고    scopus 로고
    • APOBEC3B and APOBEC3C are potent inhibitors of simian immunodeficiency virus replication
    • Yu, Q., D. Chen, R. Konig, R. Mariani, D. Unutmaz, and N. R. Landau. 2004. APOBEC3B and APOBEC3C are potent inhibitors of simian immunodeficiency virus replication. J. Biol. Chem. 279:53379-53386.
    • (2004) J. Biol. Chem , vol.279 , pp. 53379-53386
    • Yu, Q.1    Chen, D.2    Konig, R.3    Mariani, R.4    Unutmaz, D.5    Landau, N.R.6
  • 32
    • 0242578406 scopus 로고    scopus 로고
    • Induction of APOBEC3G ubiquitination and degradation by an HIV-1 Vif-Cul5-SCF complex
    • Yu, X., Y. Yu, B. Liu, K. Luo, W. Kong, P. Mao, and X. F. Yu. 2003. Induction of APOBEC3G ubiquitination and degradation by an HIV-1 Vif-Cul5-SCF complex. Science 302:1056-1060.
    • (2003) Science , vol.302 , pp. 1056-1060
    • Yu, X.1    Yu, Y.2    Liu, B.3    Luo, K.4    Kong, W.5    Mao, P.6    Yu, X.F.7
  • 33
    • 6344294871 scopus 로고    scopus 로고
    • APOBEC3G incorporation into human immunodeficiency virus type 1 particles
    • Zennou, V., D. Perez-Caballero, H. Gottlinger, and P. D. Bieniasz. 2004. APOBEC3G incorporation into human immunodeficiency virus type 1 particles. J. Virol. 78:12058-12061.
    • (2004) J. Virol , vol.78 , pp. 12058-12061
    • Zennou, V.1    Perez-Caballero, D.2    Gottlinger, H.3    Bieniasz, P.D.4
  • 34
    • 2442692812 scopus 로고    scopus 로고
    • Human APOBEC3F is another host factor that blocks human immunodeficiency virus type 1 replication
    • Zheng, Y. H., D. Irwin, T. Kurosu, K. Tokunaga, T. Sata, and B. M. Peterlin. 2004. Human APOBEC3F is another host factor that blocks human immunodeficiency virus type 1 replication. J. Virol. 78:6073-6076.
    • (2004) J. Virol , vol.78 , pp. 6073-6076
    • Zheng, Y.H.1    Irwin, D.2    Kurosu, T.3    Tokunaga, K.4    Sata, T.5    Peterlin, B.M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.