Disubstituted Bis-THF Moieties as New P2 Ligands in Nonpeptidal HIV-1 Protease Inhibitors (II)
Author:
Affiliation:
1. University of Southampton, School of Chemistry, Highfield, Southampton SO17 1BJ, United Kingdom
2. Janssen Pharmaceutica NV, Turnhoutseweg 30, 2340 Beerse, Belgium
3. Lund University, MAX-lab, Ole Römers väg 1, SE-223 63 Lund, Sweden
Funder
Tibotec
Publisher
American Chemical Society (ACS)
Subject
Drug Discovery,Molecular Medicine
Link
https://pubs.acs.org/doi/pdf/10.1021/acs.jmedchem.5b00358
Reference50 articles.
1. Cleavage of HIV-1gagPolyprotein Synthesized In Vitro: Sequential Cleavage by the Viral Protease
2. How does a symmetric dimer recognize an asymmetric substrate? a substrate complex of HIV-1 protease
3. Substrate Shape Determines Specificity of Recognition for HIV-1 Protease
4. The p2 domain of human immunodeficiency virus type 1 Gag regulates sequential proteolytic processing and is required to produce fully infectious virions
5. Sequential Steps in Human Immunodeficiency Virus Particle Maturation Revealed by Alterations of Individual Gag Polyprotein Cleavage Sites
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