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APOBEC3F is a member of the cytidine deaminase gene family. Additionally we are shipping APOBEC3F Proteins (4) and and many more products for this protein.
Showing 10 out of 45 products:
Human Polyclonal APOBEC3F Primary Antibody for ELISA, WB - ABIN566935
Han, Wang, Dang, Zheng: APOBEC3G and APOBEC3F require an endogenous cofactor to block HIV-1 replication. in PLoS pathogens 2008
Show all 2 references for ABIN566935
Human Polyclonal APOBEC3F Primary Antibody for EIA, FACS - ABIN950460
Khatua, Taylor, Hildreth, Popik: Inhibition of LINE-1 and Alu retrotransposition by exosomes encapsidating APOBEC3G and APOBEC3F. in Virology 2010
Show all 2 references for ABIN950460
Human Polyclonal APOBEC3F Primary Antibody for FACS, IHC (p) - ABIN653123
Koning, Newman, Kim, Kunstman, Wolinsky, Malim: Defining APOBEC3 expression patterns in human tissues and hematopoietic cell subsets. in Journal of virology 2009
Show all 2 references for ABIN653123
Human Polyclonal APOBEC3F Primary Antibody for WB - ABIN2776643
Gallois-Montbrun, Holmes, Swanson, Fernández-Ocaña, Byers, Ward, Malim: Comparison of cellular ribonucleoprotein complexes associated with the APOBEC3F and APOBEC3G antiviral proteins. in Journal of virology 2008
Findings support a role for APOBEC3G (show APOBEC3G Antibodies)/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 Antibodies) F1-, F2-, and F3-box motifs are essential for both APOBEC3C (show APOBEC3C Antibodies) 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 Antibodies)/F and APOBEC3G (show APOBEC3G Antibodies) fundamentally work as restriction factors against HIV-1 in vivo
APOBEC3G (show APOBEC3G Antibodies) is more efficient at mutating retroviral DNA than APOBEC3F.
The nucleocapsid domain of HIV-1 Gag and a linker sequence between the two cytidine deaminase (show CDA Antibodies) domains are required for viral packaging of APOBEC3F.
Authors found that one pair of leucines in each of APOBEC3F's C-terminal and N-terminal cytidine deaminase (show CDA Antibodies) domains jointly determined the degree of localization of APOBEC3F into HIV-1 virion cores.
This approach identified the alpha3 and alpha4 helices of human APOBEC3F as important determinants of the interaction with HIV-1 Vif (show BTG1 Antibodies).
APOBEC3F/G-specific responses in HIV-1-infected rhesus macaques are CD8 (show CD8A Antibodies)+ T cell mediated.
Increased APOBEC3G (show APOBEC3G Antibodies) 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