Source:http://linkedlifedata.com/resource/entrezgene/interaction/60489-155030
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entrezgene:pubmed |
pubmed-article:15159405,
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pubmed-article:21239176,
pubmed-article:21752914,
pubmed-article:21972557
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entrezgene:interactant | |
entrezgene:geneRifText |
APOBEC3G in exosomes reduces accumulation of HIV-1 reverse transcription products and steady-state levels of HIV-1 Gag and Vif proteins,
Approximately 7 (+/-4) molecules of A3G are incorporated into Delta-vif virions produced from human PBMCs; this incorporation is mediated by the nucleocapsid domain of HIV-1 Gag,
Approximately 7 (+/-4) molecules of APOBEC3G are incorporated into HIV-1 Vif-negative virions produced from human PBMCs; this incorporation is mediated by HIV-1 nucleocapsid,
Efficient incorporation of 7SL RNA and A3G into virions is mediated by the RNA-binding nucleocapsid domain of HIV-1 Gag,
Formation of the NC and A3G complex in vitro is promoted by single-stranded RNAs (ssRNAs) containing G residues, human Y RNAs and 7SL RNA, but not promoted by highly structured tRNAs and rRNAs,
Gag interacts with APOBEC3G.,
HIV-1 Gag chimeras formed by replacing HIV-1 nucleocapsid (NC) domain with SARS-CoV nucleocapsid (N) residues 2-213, 215-421, or 234-421 are capable of incorporating large amounts of human APOBEC3G (hA3G) into virus-like particles (VLPs),
HIV-1 Gag co-localizes with A3G complex in cells. C97A A3G mutant is delayed in A3G complex formation compared to the wild type,
In vitro biochemical assays show A3G significantly inhibits all HIV-1 RT-catalyzed DNA elongation reactions with or without HIV-1 NC. In the case of (-) strong-stop DNA synthesis, the inhibition is independent of A3G's catalytic activity,
Inhibition of tRNA3-Lys priming by A3G is associated with an inhibition of tRNA3-Lys annealing to viral RNA. The A3G-induced inhibition of tRNA-Lys priming occurs in a dose-dependent manner and can be rescued with increasing amounts of NC,
Interaction of APOBEC3G with HIV-1 nucleocapsid requires RNA, which may form a bridge between these two proteins,
Interaction of APOBEC3G with the carboxy-terminal nucleocapsid/p6 domain of the Gag polyprotein precursor is observed by Western analysis,
Newly synthesized A3G is incorporated into virion cores and assembles into a large RNA containing intravirion complex composed of IN, NC, and genomic RNA. Enzymatic activity of A3G is negatively regulated by RNA binding in the complex,
Overexpression of A3G and Mov10 decreases the efficiency of HIV-1 Gag processing in virus-producing cells,
Overexpression of SRP19 reduces the incorporation of 7SL RNA and A3G into virions in a dose-dependent manner,
Producer cell A3G complexes decrease HIV-1 pseudovirus production and intracellular HIV-1 Gag half-life,
Protein-RNA,
The N-terminus (residues 1-11) of HIV-1 nucleocapsid is critical for HIV-1 Gag and APOBEC3G interaction and virion packaging; the linker region (residues 121-161) of APOBEC3G is also important for efficient packaging into HIV-1 Gag virus like particles,
The amino-terminal half of A3G, which contains only a single cytidine deaminase domain (CDA), is able to bind to HIV-1 Gag and package into HIV-1 virions,
The basic linker region (Gag405-411) of NC is essential for the membrane association of APOBEC3G in a Gag-APOBEC3G complex. APOBEC3G is packaged as a multimer that is bound to packaged RNA,
Transient exposure of Pr(-) viral RNA to NCp7 in vitro returns the quality and quantity of tRNA(3)(Lys) annealing to Pr(+) levels. The presence of A3G prevents this rescue and creates a further reduction in tRNA(3)(Lys) annealing
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entrezgene:interactionSourc... |
BIND,
BioGRID
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entrezgene:keyphrase |
interacts with,
inhibited by,
co-localizes with,
binds,
associates with,
complexes with,
incorporates
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