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Basic Characteristics of Mutations
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Mutation Site
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K103N |
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Mutation Site Sentence
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Moreover, WT62 decreased the DNA polymerase function of K103 N/Y181 C double mutant (KY) HIV-1 RT by around 80 %. |
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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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-
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Functional Impact and Mechanisms
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Disease
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Acquired Immunodeficiency Syndrome
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Immune
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- |
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Target Gene
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-
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Clinical and Epidemiological Correlations
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Clinical Information
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- |
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Treatment
|
RT |
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Location
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- |
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Literature Information
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PMID
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33095511
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Title
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Characterization of New DNA Aptamers for Anti-HIV-1 Reverse Transcriptase
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Author
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Ratanabunyong S,Aeksiri N,Yanaka S,Yagi-Utsumi M,Kato K,Choowongkomon K,Hannongbua S
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Journal
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Chembiochem : a European journal of chemical biology
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Journal Info
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2021 Mar 2;22(5):915-923
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Abstract
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HIV-1 RT is a necessary enzyme for retroviral replication, which is the main target for antiviral therapy against AIDS. Effective anti-HIV-1 RT drugs are divided into two groups; nucleoside inhibitors (NRTI) and non-nucleoside inhibitors (NNRTI), which inhibit DNA polymerase. In this study, new DNA aptamers were isolated as anti-HIV-1 RT inhibitors. The selected DNA aptamer (WT62) presented with high affinity and inhibition against wild-type (WT) HIV-1 RT and gave a KD value of 75.10+/-0.29 nM and an IC(50) value of 84.81+/-8.54 nM. Moreover, WT62 decreased the DNA polymerase function of K103 N/Y181 C double mutant (KY) HIV-1 RT by around 80 %. Furthermore, the ITC results showed that this aptamer has small binding enthalpies with both WT and KY HIV-1 RTs through which the complex might form a hydrophobic interaction or noncovalent bonding. The NMR result also suggested that the WT62 aptamer could bind with both WT and KY mutant HIV-1 RTs at the connection domain.
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Sequence Data
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-
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