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Bishop et al., 2006 - Google Patents

Antiviral potency of APOBEC proteins does not correlate with cytidine deamination

Bishop et al., 2006

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Document ID
3382786160491020141
Author
Bishop K
Holmes R
Malim M
Publication year
Publication venue
Journal of virology

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The human cytidine deaminases APOBEC3G (hA3G) and APOBEC3F (hA3F) are intracellular antiretroviral factors that can hypermutate nascent reverse transcripts and inhibit the replication of human immunodeficiency virus type 1 (HIV-1). Both enzymes have two …
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    • C12N2740/00—Reverse Transcribing RNA Viruses
    • C12N2740/00011—Reverse Transcribing RNA Viruses
    • C12N2740/10011—Retroviridae
    • C12N2740/16011—Human Immunodeficiency Virus, HIV
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    • C12N9/14—Hydrolases (3)
    • C12N9/24—Hydrolases (3) acting on glycosyl compounds (3.2)
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Similar Documents

Publication Publication Date Title
Bishop et al. Antiviral potency of APOBEC proteins does not correlate with cytidine deamination
Mbisa et al. Human immunodeficiency virus type 1 cDNAs produced in the presence of APOBEC3G exhibit defects in plus-strand DNA transfer and integration
Russell et al. Identification of two distinct human immunodeficiency virus type 1 Vif determinants critical for interactions with human APOBEC3G and APOBEC3F
Chaipan et al. APOBEC3G restricts HIV-1 to a greater extent than APOBEC3F and APOBEC3DE in human primary CD4+ T cells and macrophages
Lee et al. Hypermutation of an ancient human retrovirus by APOBEC3G
Gillick et al. Suppression of HIV-1 infection by APOBEC3 proteins in primary human CD4+ T cells is associated with inhibition of processive reverse transcription as well as excessive cytidine deamination
Cullen Role and mechanism of action of the APOBEC3 family of antiretroviral resistance factors
Luo et al. Cytidine deaminases APOBEC3G and APOBEC3F interact with human immunodeficiency virus type 1 integrase and inhibit proviral DNA formation
Mbisa et al. APOBEC3F and APOBEC3G inhibit HIV-1 DNA integration by different mechanisms
Opi et al. Monomeric APOBEC3G is catalytically active and has antiviral activity
Zheng et al. Human APOBEC3F is another host factor that blocks human immunodeficiency virus type 1 replication
Navarro et al. Complementary function of the two catalytic domains of APOBEC3G
Tanchou et al. Role of the N-terminal zinc finger of human immunodeficiency virus type 1 nucleocapsid protein in virus structure and replication
Iwatani et al. Biochemical activities of highly purified, catalytically active human APOBEC3G: correlation with antiviral effect
Wu et al. Human immunodeficiency virus type 1 integrase protein promotes reverse transcription through specific interactions with the nucleoprotein reverse transcription complex
Svarovskaia et al. Azido-containing diketo acid derivatives inhibit human immunodeficiency virus type 1 integrase in vivo and influence the frequency of deletions at two-long-terminal-repeat-circle junctions
Liddament et al. APOBEC3F properties and hypermutation preferences indicate activity against HIV-1 in vivo
Harari et al. Polymorphisms and splice variants influence the antiretroviral activity of human APOBEC3H
Delebecque et al. Restriction of foamy viruses by APOBEC cytidine deaminases
Huthoff et al. Identification of amino acid residues in APOBEC3G required for regulation by human immunodeficiency virus type 1 Vif and Virion encapsidation
Russell et al. Distinct domains within APOBEC3G and APOBEC3F interact with separate regions of human immunodeficiency virus type 1 Vif
King et al. Resistance to the anti-human immunodeficiency virus type 1 compound L-chicoric acid results from a single mutation at amino acid 140 of integrase
Duggal et al. The breadth of antiviral activity of Apobec3DE in chimpanzees has been driven by positive selection
Contreras-Galindo et al. Human endogenous retrovirus Type K (HERV-K) particles package and transmit HERV-K–related sequences
Mansky In vivo analysis of human T-cell leukemia virus type 1 reverse transcription accuracy