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• W2137156912 endingPage "9126" @default.
• W2137156912 startingPage "9114" @default.
• W2137156912 abstract "The human immunodeficiency virus type 1 (HIV-1)-encoded RNA-binding protein Tat is known to play an essential role in viral gene expression. In the search for novel compounds to inhibit Tat transactivity, one coumarin derivative, BPRHIV001, was identified, with a 50% effective concentration (EC(50)) against HIV-1 at 1.3 nM. BPRHIV001 is likely to exert its effects at the stage after initiation of RNAPII elongation since Tat protein expression and the assembly of the Tat/P-TEFb complex remained unchanged. Next, a reduction of the p300 protein level, known to modulate Tat function through acetylation, was observed upon BPRHIV001 treatment, while the p300 mRNA level was unaffected. A concordant reduction of phosphorylated Akt, which was shown to be closely related to p300 stability, was observed in the presence of BPRHIV001 and was accompanied by a decrease of phosphorylated PDPK1, a well-known Akt activator. Furthermore, the docking analysis revealed that the reduced PDPK1 phosphorylation likely resulted from the allosteric effect of interaction between BPRHIV001 and PDPK1. With strong synergistic effects with current reverse transcriptase inhibitors, BPRHIV001 has the potential to become a promising lead compound for the development of a novel therapeutic agent against HIV-1 infection." @default.
• W2137156912 created "2016-06-24" @default.
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• W2137156912 date "2011-09-01" @default.
• W2137156912 modified "2023-10-16" @default.
• W2137156912 title "Inhibition of HIV-1 Tat-Mediated Transcription by a Coumarin Derivative, BPRHIV001, through the Akt Pathway" @default.
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• W2137156912 doi "https://doi.org/10.1128/jvi.00175-11" @default.
• W2137156912 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3165834" @default.
• W2137156912 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/21697490" @default.
• W2137156912 hasPublicationYear "2011" @default.
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