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- W1996653300 abstract "Targeted molecular dynamics (TMD) simulations allowed for identifying the chemical/structural features of the nucleotide-competitive HIV-1 inhibitor DAVP-1, which is responsible for the disruption of the T-shape motif between Try183 and Trp229 of the reverse transcriptase (RT). DAVP-1 promoted the opening of a connection “gate” between allosteric and catalytic sites of HIV-1 RT, thus explaining its peculiar mechanism of action and providing useful insights to develop novel nucleotide-competitive RT inhibitors." @default.
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- W1996653300 date "2013-11-25" @default.
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- W1996653300 title "Unconventional Plasticity of HIV-1 Reverse Transcriptase: How Inhibitors Could Open a Connection “Gate” between Allosteric and Catalytic Sites" @default.
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- W1996653300 doi "https://doi.org/10.1021/ci400414s" @default.
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