메뉴 건너뛰기




Volumn 85, Issue 11, 2011, Pages 5691-5695

Identification of a single amino acid required for APOBEC3 antiretroviral cytidine deaminase activity

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; APOLIPOPROTEIN B MESSENGER RNA EDITING ENZYME CATALYTIC POLYPEPTIDE 3; ASPARAGINE; CYSTEINE; CYTIDINE DEAMINASE; DNA; GLUTAMINE; HYDROLASE; LEUCINE; SERINE; THREONINE; TYROSINE; UNCLASSIFIED DRUG;

EID: 79956105749     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.00243-11     Document Type: Article
Times cited : (21)

References (15)
  • 2
    • 40449114441 scopus 로고    scopus 로고
    • Structure of the DNA deaminase domain of the HIV-1 restriction factor APOBEC3G
    • Chen, K. M., et al. 2008. Structure of the DNA deaminase domain of the HIV-1 restriction factor APOBEC3G. Nature 452:116-119.
    • (2008) Nature , vol.452 , pp. 116-119
    • Chen, K.M.1
  • 3
    • 34548697547 scopus 로고    scopus 로고
    • Extensive mutagenesis experiments corroborate a structural model for the DNA deaminase domain of APOBEC3G
    • Chen, K. M., et al. 2007. Extensive mutagenesis experiments corroborate a structural model for the DNA deaminase domain of APOBEC3G. FEBS Lett. 581:4761-4766.
    • (2007) FEBS Lett , vol.581 , pp. 4761-4766
    • Chen, K.M.1
  • 4
    • 33750344250 scopus 로고    scopus 로고
    • Identification of APOBEC3DE as another antiretroviral factor from the human APOBEC family
    • Dang, Y., X. Wang, W. J. Esselman, and Y. H. Zheng. 2006. Identification of APOBEC3DE as another antiretroviral factor from the human APOBEC family. J. Virol. 80:10522-10533.
    • (2006) J. Virol. , vol.80 , pp. 10522-10533
    • Dang, Y.1    Wang, X.2    Esselman, W.J.3    Zheng, Y.H.4
  • 5
    • 60549109045 scopus 로고    scopus 로고
    • Structure, interaction and real-time monitoring of the enzymatic reaction of wild-type APOBEC3G
    • Furukawa, A., et al. 2009. Structure, interaction and real-time monitoring of the enzymatic reaction of wild-type APOBEC3G. EMBO J. 28:440-451.
    • (2009) EMBO J , vol.28 , pp. 440-451
    • Furukawa, A.1
  • 6
    • 67349258491 scopus 로고    scopus 로고
    • An extended structure of the APOBEC3G catalytic domain suggests a unique holoenzyme model
    • Harjes, E., et al. 2009. An extended structure of the APOBEC3G catalytic domain suggests a unique holoenzyme model. J. Mol. Biol. 389:819-832.
    • (2009) J. Mol. Biol. , vol.389 , pp. 819-832
    • Harjes, E.1
  • 7
    • 55549098517 scopus 로고    scopus 로고
    • Crystal structure of the anti-viral APOBEC3G catalytic domain and functional implications
    • Holden, L. G., et al. 2008. Crystal structure of the anti-viral APOBEC3G catalytic domain and functional implications. Nature 456:121-124.
    • (2008) Nature , vol.456 , pp. 121-124
    • Holden, L.G.1
  • 8
    • 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 79:285-296.
    • (2002) Genomics , vol.79 , pp. 285-296
    • Jarmuz, A.1
  • 9
    • 69249137076 scopus 로고    scopus 로고
    • A portable hot spot recognition loop transfers sequence preferences from APOBEC family members to activation-induced cytidine deaminase
    • Kohli, R. M., et al. 2009. A portable hot spot recognition loop transfers sequence preferences from APOBEC family members to activation-induced cytidine deaminase. J. Biol. Chem. 284:22898-22904.
    • (2009) J. Biol. Chem. , vol.284 , pp. 22898-22904
    • Kohli, R.M.1
  • 10
    • 0037093644 scopus 로고    scopus 로고
    • Increasing the precision of comparative models with YASARA NOVA-a self-parameterizing force field
    • Krieger, E., G. Koraimann, and G. Vriend. 2002. Increasing the precision of comparative models with YASARA NOVA-a self-parameterizing force field. Proteins 47:393-402.
    • (2002) Proteins , vol.47 , pp. 393-402
    • Krieger, E.1    Koraimann, G.2    Vriend, G.3
  • 11
    • 65449141378 scopus 로고    scopus 로고
    • Dissecting APOBEC3G substrate specificity by nucleoside analog interference
    • Rausch, J. W., L. Chelico, M. F. Goodman, and S. F. Le Grice. 2009. Dissecting APOBEC3G substrate specificity by nucleoside analog interference. J. Biol. Chem. 284:7047-7058.
    • (2009) J. Biol. Chem. , vol.284 , pp. 7047-7058
    • Rausch, J.W.1    Chelico, L.2    Goodman, M.F.3    Le Grice, S.F.4
  • 12
    • 73449099592 scopus 로고    scopus 로고
    • Crystal structure of the APOBEC3G catalytic domain reveals potential oligomerization interfaces
    • Shandilya, S. M., et al. 2010. Crystal structure of the APOBEC3G catalytic domain reveals potential oligomerization interfaces. Structure 18:28-38.
    • (2010) Structure , vol.18 , pp. 28-38
    • Shandilya, S.M.1
  • 13
    • 33745184896 scopus 로고    scopus 로고
    • APOBEC3B and APOBEC3F inhibit L1 retrotransposition by a DNA deamination-independent mechanism
    • Stenglein, M. D., and R. S. Harris. 2006. APOBEC3B and APOBEC3F inhibit L1 retrotransposition by a DNA deamination-independent mechanism. J. Biol. Chem. 281:16837-16841.
    • (2006) J. Biol. Chem. , vol.281 , pp. 16837-16841
    • Stenglein, M.D.1    Harris, R.S.2
  • 14
    • 76149119416 scopus 로고    scopus 로고
    • Altering the spectrum of immunoglobulin V gene somatic hypermutation by modifying the active site of AID
    • Wang, M., C. Rada, and M. S. Neuberger. 2010. Altering the spectrum of immunoglobulin V gene somatic hypermutation by modifying the active site of AID. J. Exp. Med. 207:141-153.
    • (2010) J. Exp. Med. , vol.207 , pp. 141-153
    • Wang, M.1    Rada, C.2    Neuberger, M.S.3
  • 15
    • 77951984369 scopus 로고    scopus 로고
    • Moloney leukemia virus 10 (MOV10) protein inhibits retrovirus replication
    • Wang, X., et al. 2010. Moloney leukemia virus 10 (MOV10) protein inhibits retrovirus replication. J. Biol. Chem. 285:14346-14355.
    • (2010) J. Biol. Chem. , vol.285 , pp. 14346-14355
    • Wang, X.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.