Source:http://linkedlifedata.com/resource/entrezgene/hivinteraction/155871-5970
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entrezgene:pubmed |
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entrezgene:interactant | |
entrezgene:geneRifText |
A compound in curry known as Curcumin inhibits HIV-1 Tat-mediated long terminal repeat transactivation by reversing Tat-induced dissociation of HDAC1 from LTR and by reducing the binding of p65/NFKappaB to LTR promoted by Tat,
Activation of NFkappaB by HIV-1 Tat is inhibited by Nitric Oxide,
Activation of NFkappaB by HIV-1 Tat leads to a reduction in adenylyl cyclase activity and an inhibition of cAMP synthesis,
Curcumin attenuates HIV-1 Tat-induced p65/NFKappaB phosphorylation and IKK phosphorylation,
HIV-1 Tat activates NFkappaB through the cellular interferon-inducible, double-stranded RNA dependent protein kinase, PKR,
HIV-1 Tat activates NFkappaB, causing the induction of CD95 ligand, CD69, iNOS, MCP-1, IL-2, IL-6, IL-8, IL-10, TNF-alpha, VCAM-1, ICAM-1, E-selectin, and MMP-9, as well as monocyte adhesion, cellular activation and angiogenesis,
HIV-1 Tat and morphine treatment significantly increase the levels of phosphorylated p65 NF-kappaB in human hepatocellular carcinoma cells,
HIV-1 Tat enhances the NFkappaB activity and promotes the transcriptional activation of MIP-1alpha by interacting with IkappaB-alpha and p65 RelA,
HIV-1 Tat enhances the NFkappaB activity by inhibiting IkappaB-alpha binding to p65 RelA,
HIV-1 Tat enhances tumor necrosis factor-induced activation of NFkappaB by downregulating manganese-dependent superoxide dismutase (MnSOD),
HIV-1 Tat has been shown to bind NFkappaB in vitro in gel shift, GST-pull down and affinity matrix assays,
HIV-1 Tat increases the p65 RelA affinity binding to DNA through association with p65 RelA,
HIV-1 Tat induces the acetylation of the NFkappaB p50 subunit as well as the p50/p65 complex by p300, causing an increase in NFkappaB DNA binding activity and in the rate of transcription,
HIV-1 Tat inhibits the LPS-induced activation of NFkappaB p65 via its induction of IkappaBalpha expression, which results in retention of NFkappaB p65 in the cytosol,
HIV-1 Tat recruits P/CAF to the integrated HIV-1 LTR promoter causing the acetylation of histones, which in turn leads to the recruitment the p65 subunit of NFkappaB to the promoter,
HIV-1 Tat upregulates c-rel and RelA transcription factor binding to the CD28-responsive element in the IL-8 promoter, leading to super-induction of IL-8,
HIV-1 Tat-mediated transcriptional activation of the HIV-1 LTR promoter requires NFkappaB binding sites in the promoter and involves the activation of NFkappaB by Tat,
Inhibition of HIV-1 Tat-mediated transactivation of the HIV-1 LTR promoter by NFkappaB/Rel inhibitors correlates with their inhibitory activities on the RelA subunit of the NFkappaB complex, indicating an interaction of Tat with RelA,
NFAT-1 negatively regulates HIV-1 Tat-mediated transactivation of the HIV-1 LTR by competing with NFkappaB for its binding to the LTR, thereby blocking the interaction of NFkappaB with Tat,
NFkappaB tethers the p160 nuclear receptor co-activator GRIP1 to the HIV-1 LTR promoter, thereby regulating the full activation of this promoter by HIV-1 Tat,
p56-lck plays a critical role in the activation of NFkappaB by HIV-1 Tat
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entrezgene:keyphrase |
inhibits,
interacts with,
induces phosphorylation of,
regulated by,
upregulates,
binds,
activates,
recruits,
enhances,
acetylates
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