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- W1994753280 abstract "N-Myristoyltransferase (NMT) isozymes, i.e., NMT1 and NMT2, are essential host factors for the AIDS-causing human immunodeficiency virus type-1 (HIV-1), by which the viral proteins Pr55(gag) and Nef are N-myristoylated. N-Myristoylation is important for the membrane targeting of modified proteins. Since it is predicted that approximately 0.5% of all proteins in the human genome are N-myristoylated, selective inhibition of closely HIV-1-associated NMT isozymes is thought to be important for the improvement of specificity in the anti-HIV-1 strategy with the inhibition of NMT function. NMT isozymes contain two characteristic structures, the N-terminal region and the catalytic region. Here, it was shown that the N-terminal region of each NMT isozyme is required for isozyme-specific binding to the ribosome. The specific binding of each isozyme to the ribosome was associated with HIV-1 production, in which NMT1 and NMT2 in the ribosome were suggested to be mainly related to Pr55(gag) and Nef, respectively. These results indicate that the N-terminal region that mediates binding to the ribosome can become a target for NMT-isozyme-specific inhibition, which could block HIV-1 production." @default.
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- W1994753280 date "2010-01-01" @default.
- W1994753280 modified "2023-10-16" @default.
- W1994753280 title "Suppression of Human Immunodeficiency Virus Type-1 Production by Coexpression of Catalytic-Region-Deleted N-Myristoyltransferase Mutants" @default.
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- W1994753280 doi "https://doi.org/10.1248/bpb.33.2018" @default.
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