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Basic Characteristics of Mutations
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Mutation Site
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Q475A |
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Mutation Site Sentence
|
Besides, both compounds were tested also on RTs mutated in two amino acid residues within the RNase H domain, Q475A and A502F, part of conserved regions of RNase H domain, that have been shown to be involved in the binding of RNase H inhibitors into a pocket close to the RNase H catalytic site but acting as allosteric RNase H inhibitors. |
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Mutation Level
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Amino acid level |
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Mutation Type
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Nonsynonymous substitution |
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Gene/Protein/Region
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RT |
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Standardized Encoding Gene
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gag-pol:155348
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Genotype/Subtype
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HIV-1 |
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Viral Reference
|
-
|
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Functional Impact and Mechanisms
|
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Disease
|
HIV Infections
|
|
Immune
|
- |
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Target Gene
|
-
|
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Clinical and Epidemiological Correlations
|
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Clinical Information
|
- |
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Treatment
|
NNRTIs;efavirenz (EFV) |
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Location
|
- |
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Literature Information
|
|
PMID
|
32183488
|
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Title
|
2-(Arylamino)-6-(trifluoromethyl)nicotinic Acid Derivatives: New HIV-1 RT Dual Inhibitors Active on Viral Replication
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Author
|
Corona A,Onnis V,Del Vecchio C,Esposito F,Cheng YC,Tramontano E
|
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Journal
|
Molecules (Basel, Switzerland)
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Journal Info
|
2020 Mar 15;25(6):1338
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Abstract
|
The persistence of the AIDS epidemic, and the life-long treatment required, indicate the constant need of novel HIV-1 inhibitors. In this scenario the HIV-1 Reverse Transcriptase (RT)-associated ribonuclease H (RNase H) function is a promising drug target. Here we report a series of compounds, developed on the 2-amino-6-(trifluoromethyl)nicotinic acid scaffold, studied as promising RNase H dual inhibitors. Among the 44 tested compounds, 34 inhibited HIV-1 RT-associated RNase H function in the low micromolar range, and seven of them showed also to inhibit viral replication in cell-based assays with a selectivity index up to 10. The most promising compound, 21, inhibited RNase H function with an IC(50) of 14 microM and HIV-1 replication in cell-based assays with a selectivity index greater than 10. Mode of action studies revealed that compound 21 is an allosteric dual-site compound inhibiting both HIV-1 RT functions, blocking the polymerase function also in presence of mutations carried by circulating variants resistant to non-nucleoside inhibitors, and the RNase H function interacting with conserved regions within the RNase H domain. Proving compound 21 as a promising lead for the design of new allosteric RNase H inhibitors active against viral replication with not significant cytotoxic effects.
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Sequence Data
|
-
|
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