Abstract
The T-20 peptide targets the HIV envelope glycoprotein, inducing dose-dependent reductions in plasma HIV RNA that are equivalent to those induced by existing drugs ( pages 1302–1307 ).
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References
Kilby, J.M. et al. Potent suppression of HIV-1 replication in humans by T-20, a peptide inhibitor of gp41-mediated virus entry. Nature Med. 4, 1302–1307 (1998).
Wild, C., Oas, T., McDanal, C., Bolognesi, D. & Matthews, T. A synthetic peptide inhibitor of HIV replication: Correlation between solution structure and viral inhibition. Proc. Natl. Acad. Sci. USA 89, 10537–10541 (1992).
Chan, D.C., Fass, D., Berger, J.M. & Kim. P.S. Core structure of gp41 from the HIV envelope glycoprotein. Cell 89, 263–273 (1997).
Wei, X. et al. Viral dynamics in human immunodeficiency virus type 1 infection. Nature 37, 117–122 (1995).
Ho, D.D. et al. Rapid turnover of plasma virions and CD4 lymphocytes in HIV-1 infection. Nature 373, 123–126 (1995).
Rimsky, L.T., Shugars, D.C. & Matthews, T. Determinants of HIV-1 resistance to gp41-derived inhibitory peptides. J. Virol. 72, 986– 992 (1998).
Rice, W.G. et al. Inhibitors of HIV nucleocapsid protein zinc fingers as candidates for the treatment of AIDS. Science 270, 1194–1197 (1995).
Mei, H.-Y. et al. Inhibitors of protein-RNA complexation that target the RNA: Specific recognition of human immunodeficiency virus type 1 TAR RNA by small organic molecules. Biochemistry (in the press).
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Richman, D. Nailing down another HIV target . Nat Med 4, 1232–1233 (1998). https://doi.org/10.1038/3209
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DOI: https://doi.org/10.1038/3209
