APOBEC3F Antibody

1. virus adaptation and computational studies to interrogate the APOBEC3F-Vif interface and build a robust structural model; taken together with mutagenesis results, propose a wobble model to explain how HIV-1 Vif has evolved to bind different APOBEC3 enzymes PMID: 26628363
2. Overexpression of APOBEC3F in tumor tissues is potentially predictive for poor recurrence-free survival from hepatitis b virus-hepatocellular carcinoma patients. PMID: 26760979
3. Our results provide genetic epidemiological evidence that A3F(APOBEC3F ) modulates HIV-1/AIDS disease progression PMID: 26942578
4. Six residues located within the conserved HIV-1 Vif F1-, F2-, and F3-box motifs are essential for both APOBEC3C and APOBEC3F degradation, and an additional four residues are uniquely required for APOBEC3F degradation. PMID: 26537685
5. This study showed for the first time a high level of APOBEC3F/3G editing in HIV-2 sequences from antiretroviral-naive patients. PMID: 25985400
6. The nucleocapsid domain of HIV-1 Gag and a linker sequence between the two cytidine deaminase domains are required for viral packaging of APOBEC3F. PMID: 25038404
7. Authors found that one pair of leucines in each of APOBEC3F's C-terminal and N-terminal cytidine deaminase domains jointly determined the degree of localization of APOBEC3F into HIV-1 virion cores. PMID: 25505075
8. This approach identified the alpha3 and alpha4 helices of human APOBEC3F as important determinants of the interaction with HIV-1 Vif. PMID: 25142588
9. Catalytic activity of APOBEC3F is required for efficient restriction of Vif-deficient human immunodeficiency virus 1. PMID: 24503066
10. Analysis of the A3F (W126A L306A) double mutant revealed that both residues are required for full anti-HIV function PMID: 22451677
11. the antiviral activity of endogenous A3F is negligible compared to that of A3G. PMID: 20702622
12. Long-term restriction by APOBEC3F selects human immunodeficiency virus type 1 variants with restored Vif function. PMID: 20686027
13. Alternative splicing of A3F mRNA generates truncated antiviral proteins that differ sharply in their sensitivity to Vif. PMID: 20624919
14. These results suggest that APOBEC3F neutralization is dispensable for HIV-1 replication in primary human T-lymphocytes. PMID: 20592068
15. The fact that several highly conserved tryphtophan residues in Vif are specifically required for the suppression of APOBEC3F (A3F) but not that of APOBEC3G (A3G) suggests a critical role for A3F in the restriction of HIV-1 in vivo. PMID: 16501124
16. APOBEC3B and APOBEC3F have roles in inhibiting L1 retrotransposition by a DNA deamination-independent mechanism PMID: 16648136
17. The Chinese population had a higher frequency of small alleles and showed a difference in allelic structure and frequency distribution in apolipoprotein B from European and American in this populations. PMID: 16767679
18. separation of function of the cytidine deaminase domains is maintained in hA3B and hA3F, but roles of the two domains are reversed in mouse A3 PMID: 17020885
19. Studies focused mainly on APOBEC3F imply that it occurs associated with mRNA-PABP1 in translationally active polysomes and to a lesser extent in mRNA processing bodies (P-bodies). PMID: 17977970
20. The APOBEC3F domain that interacts with the Vif DRMR region was located between amino acids 283 and 300 of A3F. PMID: 19036809

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HGNC: 17356

OMIM: 608993

KEGG: hsa:200316

STRING: 9606.ENSP00000309749

UniGene: Hs.659809