about
The biased nucleotide composition of HIV-1 triggers type I interferon response and correlates with subtype D increased pathogenicityAssociations between activation-induced cytidine deaminase/apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like cytidine deaminase expression, hepatitis B virus (HBV) replication and HBV-associated liver disease (Review)Functions and regulation of the APOBEC family of proteinsAPOBEC3B, a molecular driver of mutagenesis in human cancers.GANP interacts with APOBEC3G and facilitates its encapsidation into the virions to reduce HIV-1 infectivityThe virus-induced protein APOBEC3G inhibits anoikis by activation of Akt kinase in pancreatic cancer cells.APOBEC3G-Augmented Stem Cell Therapy to Modulate HIV Replication: A Computational Study.Lower HIV provirus levels are associated with more APOBEC3G protein in blood resting memory CD4+ T lymphocytes of controllers in vivo.Positioning of APOBEC3G/F mutational hotspots in the human immunodeficiency virus genome favors reduced recognition by CD8+ T cellsDeaminase activity on single-stranded DNA (ssDNA) occurs in vitro when APOBEC3G cytidine deaminase forms homotetramers and higher-order complexesDirect evidence that RNA inhibits APOBEC3G ssDNA cytidine deaminase activity.The HDAC6/APOBEC3G complex regulates HIV-1 infectiveness by inducing Vif autophagic degradation.APOBEC3G expression and hypermutation are inversely associated with human immunodeficiency virus type 1 (HIV-1) burden in vivo.Emerging complexities of APOBEC3G action on immunity and viral fitness during HIV infection and treatment.Host restriction factors in retroviral infection: promises in virus-host interaction.Host Factors and HIV-1 Replication: Clinical Evidence and Potential Therapeutic ApproachesBiological pathways to adaptability--interactions between genome, epigenome, nervous system and environment for adaptive behavior.Apolipoprotein B mRNA-editing, catalytic polypeptide cytidine deaminases and retroviral restriction.The multifaceted roles of RNA binding in APOBEC cytidine deaminase functions.DNA mutagenic activity and capacity for HIV-1 restriction of the cytidine deaminase APOBEC3G depend on whether DNA or RNA binds to tyrosine 315.Structural and functional assessment of APOBEC3G macromolecular complexes.The APOBEC Protein Family: United by Structure, Divergent in Function.RNA binding to APOBEC deaminases; Not simply a substrate for C to U editing.Synthesis and structure-activity relationship studies of HIV-1 virion infectivity factor (Vif) inhibitors that block viral replication.A putative antiviral role of plant cytidine deaminases.RNA binding to APOBEC3G induces the disassembly of functional deaminase complexes by displacing single-stranded DNA substrates.
P2860
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P2860
description
2011 nî lūn-bûn
@nan
2011 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
APOBEC3G: a double agent in defense
@ast
APOBEC3G: a double agent in defense
@en
APOBEC3G: a double agent in defense
@nl
type
label
APOBEC3G: a double agent in defense
@ast
APOBEC3G: a double agent in defense
@en
APOBEC3G: a double agent in defense
@nl
prefLabel
APOBEC3G: a double agent in defense
@ast
APOBEC3G: a double agent in defense
@en
APOBEC3G: a double agent in defense
@nl
P2860
P1476
APOBEC3G: a double agent in defense
@en
P2860
P304
P356
10.1016/J.TIBS.2010.12.003
P50
P577
2011-01-14T00:00:00Z