The DOI matches its Crossref record; 47 of the 47 references it cites were found in a registry or an index.
Complementary function of the two catalytic domains of APOBEC3G
Open accessAbstract
The HIV-1 viral accessory protein Vif prevents the encapsidation of the antiviral cellular cytidine deaminases APOBEC3F and APOBEC3G by inducing their proteasomal degradation. In the absence of Vif, APOBEC3G is encapsidated and blocks virus replication by deaminating cytosines of the viral cDNA. APOBEC3G encapsidation has been recently shown to depend on the viral nucleocapsid protein; however, the role of RNA remains unclear. Using APOBEC3G deletion and point mutants, we mapped the encapsidation determinant to the Zn(2+) coordination residues of the N-terminal catalytic domain (CD1). Notably, these residues were also required for RNA binding. Mutations in the two aromatic residues of CD1 but not CD2, which are conserved in cytidine deaminase core domains and are required for RNA binding, prevented encapsidation into HIV-1, HTLV-I and MLV. The Zn(2+) coordination residues of the C-terminal catalytic domain (CD2) were not required for encapsidation but were essential for cytidine deaminase activity and the antiviral effect. These findings suggest a model in which CD1 mediates encapsidation and RNA binding while CD2 mediates cytidine deaminase activity. Interestingly, HTLV-I was relatively resistant to the antiviral effects of encapsidated APOBEC3G.
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Self-citationInduction of APOBEC3G Ubiquitination and Degradation by an HIV-1 Vif-Cul5-SCF Complex
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Cited by
Harris, R. S., & Dudley, J. P. (2015) · Virology · doi:10.1016/j.virol.2015.03.012 · Cited by 551
The APOBEC Protein Family: United by Structure, Divergent in Function
Salter, J. D., Bennett, R. P., & Smith, H. C. (2016) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2016.05.001 · Cited by 408
APOBEC3G Generates Nonsense Mutations in Human T-Cell Leukemia Virus Type 1 Proviral Genomes In Vivo
Fan, J., Ma, G., Nosaka, K., Tanabe, J., Satou, Y., Koito, A., Wain-Hobson, S., Vartanian, J.-P., & Matsuoka, M. (2010) · Journal of Virology · doi:10.1128/jvi.02239-09 · Cited by 130
The double-domain cytidine deaminase APOBEC3G is a cellular site-specific RNA editing enzyme
Sharma, S., Patnaik, S. K., Taggart, R. T., & Baysal, B. E. (2016) · Scientific Reports · doi:10.1038/srep39100 · Cited by 97
Multifaceted antiviral actions of APOBEC3 cytidine deaminases
Chiu, Y.-L., & Greene, W. C. (2006) · Trends in Immunology · doi:10.1016/j.it.2006.04.003 · Cited by 72
Metadata
- Authors
- Navarro, F., Bollman, B., Chen, H., König, R., Yu, Q., Chiles, K., & Landau, N. R.
- Venue
- Virology
- Publisher
- Elsevier BV
- Published
- 2005-03
- Volume
- 333
- Issue
- 2
- Pages
- 374-386
- ISSN
- 0042-6822 (ISSN-L)
- OpenAlex
- W2070677647
- Cited by
- 305
- References
- 47
- FWCI
- 10.56
- Type
- journal article
- Language
- en
- Open access
- bronze
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