ArticleProceedings of the National Academy of Sciences of the United States of America1996
Engineering human immunodeficiency virus 1 protease heterodimers as macromolecular inhibitors of viral maturation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
10 citing papers in PubMed.
- Applications of Click Chemistry in the Development of HIV Protease Inhibitors.International journal of medicinal chemistry · 2018Review
- Function-based mutation-resistant synthetic signaling device activated by HIV-1 proteolysis.ACS synthetic biology · 2015Article
- Antiviral activity of α-helical stapled peptides designed from the HIV-1 capsid dimerization domain.Retrovirology · 2011Article
- Novel macromolecular inhibitors of human immunodeficiency virus-1 protease.Protein engineering, design & selection : PEDS · 2008Article
- Article
- Host ABCE1 is at plasma membrane HIV assembly sites and its dissociation from Gag is linked to subsequent events of virus production.Traffic (Copenhagen, Denmark) · 2007Article
- Targeting human immunodeficiency virus type 1 assembly, maturation and budding.Drug target insights · 2007Article
- Herpesvirus protease inhibition by dimer disruption.Journal of virology · 2004Article
- Computational study of protein specificity: the molecular basis of HIV-1 protease drug resistance.Proceedings of the National Academy of Sciences of the United States of America · 2001Article
- The protease and the assembly protein of Kaposi's sarcoma-associated herpesvirus (human herpesvirus 8).Journal of virology · 1997Article
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Authors and funding
4 authors.
Funding
Abstract
Dimerization of human immunodeficiency virus type 1 protease (HIV-1 PR) monomers is an essential prerequisite for viral proteolytic activity and the subsequent generation of infectious virus particles. Disruption of the dimer interface inhibits this activity as does formation of heterodimers between wild-type and defective monomers. A structure-based approach was used to identify amino acid substitutions at the dimer interface of HIV-1 PR that facilitate preferential association of heterodimers and inhibit self-association of the defective monomers. Expression of the designed PR monomers inhibits activity of wild-type HIV-1 PR and viral infectivity when assayed in an ex vivo model system. These results show that it is possible to design PR monomers as macromolecular inhibitors that may provide an alternative to small molecule inhibitors for the treatment of HIV infection.
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