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Dimerization inhibitors of HIV-1 reverse transcriptase, protease and integrase: A single mode of inhibition for the three HIV enzymes?

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Authors
Camarasa Rius, María José; Velázquez Díaz, Sonsoles; San Félix García, Ana; Pérez Pérez, María Jesús; Gago Badenas, FedericoUniversity of Alcalá Author
Identifiers
Permanent link (URI): http://hdl.handle.net/10017/5071
DOI: 10.1016/j.antiviral.2006.05.021
Publisher
Elsevier
Date
2006
Affiliation
Universidad de Alcalá. Departamento de Farmacología
Bibliographic citation
Antiviral Research 71 (2006) 260 267
Keywords
HIV-1
Reverse transcriptase
Integrase
Protease
Document type
info:eu-repo/semantics/article
Version
info:eu-repo/semantics/publishedVersion
Publisher's version
http://dx.doi.org/10.1016/j.antiviral.2006.05.021
Access rights
info:eu-repo/semantics/openAccess
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Abstract
The genome of human immunodeficiency virus type 1 (HIV-1) encodes 15 distinct proteins, three of which provide essential enzymatic functions: a reverse transcriptase (RT), an integrase (IN), and a protease (PR). Since these enzymes are all homodimers, pseudohomodimers or multimers, disruption of protein-protein interactions in these retroviral enzymes may constitute an alternative way to achieve HIV-1 inhibition. A growing number. of dimerization inhibitors for these enzymes is being reported. This mini review summarizes some approaches that have been followed for the development of compounds that inhibit those three enzymes by interfering with the dimerization interfaces between the enzyme subunits. (c) 2006 Elsevier B.V. All rights reserved.
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