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APOBEC3F is a member of the cytidine deaminase gene family. Additionally we are shipping APOBEC3F Antibodies (42) and and many more products for this protein.
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APOBEC3DE (show APOBEC3D Proteins) binds to itself, APOBEC3F, and APOBEC3G (show APOBEC3G Proteins) and antagonizes APOBEC3F and, to a lesser extent, APOBEC3G (show APOBEC3G Proteins) restriction of hepatitis B virus replication.
These results indicate that APOBEC3 proteins can be copackaged and can comutate the same genomes, and can cooperate to inhibit HIV replication.
an APOBEC3F/APOBEC3G (show APOBEC3G Proteins) hetero-oligomer can form that has unique properties compared to each APOBEC3 alone. This hetero-oligomer has increased efficiency of virus hypermutation, raising the idea that we still may not fully realize the antiviral mechanisms of endogenous APOBEC3 enzymes. Hetero-oligomerization may be a mechanism to increase their antiviral activity in the presence of Vif (show BTG1 Proteins).
virus adaptation and computational studies to interrogate the APOBEC3F-Vif (show BTG1 Proteins) interface and build a robust structural model; taken together with mutagenesis results, propose a wobble model to explain how HIV-1 Vif (show BTG1 Proteins) has evolved to bind different APOBEC3 enzymes
Findings support a role for APOBEC3G (show APOBEC3G Proteins)/F proteins in the generation of plasma drug-resistant minority human immunodeficiency virus type 1 variants (DRMVs). However, this role seems to be limited to a small subset of mutations and does not explain most of the DRMVs evaluated.
Overexpression of APOBEC3F in tumor tissues is potentially predictive for poor recurrence-free survival from hepatitis b virus-hepatocellular carcinoma patients.
Our results provide genetic epidemiological evidence that A3F(APOBEC3F ) modulates HIV-1/AIDS disease progression
Six residues located within the conserved HIV-1 Vif (show BTG1 Proteins) F1-, F2-, and F3-box motifs are essential for both APOBEC3C (show APOBEC3C Proteins) and APOBEC3F degradation, and an additional four residues are uniquely required for APOBEC3F degradation.
This study showed for the first time a high level of APOBEC3F/3G editing in HIV-2 sequences from antiretroviral-naive patients.
APOBEC3D (show APOBEC3D Proteins)/F and APOBEC3G (show APOBEC3G Proteins) fundamentally work as restriction factors against HIV-1 in vivo
APOBEC3F/G-specific responses in HIV-1-infected rhesus macaques are CD8 (show CD8A Proteins)+ T cell mediated.
Increased APOBEC3G (show APOBEC3G Proteins) and APOBEC3F expression is associated with low viral load and prolonged survival in simian immunodeficiency virus infected rhesus monkeys.
APOBEC3 proteins restrict xenotropic murine leukemia virus-related virus infections in a Macaca mulatta model.
These results strongly imply that human and porcine APOBEC3 could inhibit porcine endogenous retroviruses replication in vivo, thereby reducing the risk of infection of human cells in the context of pig-to-human xenotransplantation.
This gene is a member of the cytidine deaminase gene family. It is one of seven related genes or pseudogenes found in a cluster, thought to result from gene duplication, on chromosome 22. Members of the cluster encode proteins that are structurally and functionally related to the C to U RNA-editing cytidine deaminase APOBEC1. It is thought that the proteins may be RNA editing enzymes and have roles in growth or cell cycle control. Alternatively spliced transcript variants encoding different isoforms have been identified.
DNA dC->dU-editing enzyme APOBEC-3F
, apolipoprotein B mRNA editing enzyme cytidine deaminase
, apolipoprotein B mRNA-editing enzyme catalytic polypeptide-like 3F
, induced upon T-cell activation
, apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 3F
, apolipoprotein B mRNA editing enzyme catalytic polypeptide-like 3F