Abstract |
Viral proteins have enabled the design of selective and efficacious treatments for viral diseases. While focus in this area has been on viral enzymes, it appears that multifunctional viral proteins may be even more susceptible to small molecule interference. As exemplified by HIV capsid, small molecule inhibitors can bind to multiple binding sites on the capsid protein and induce or prevent protein interactions and conformational changes. Resistance selection is complicated by the fact that the capsid proteins have to engage in different protein interactions at different times of the life cycle. Viral capsid assembly and disassembly have therefore emerged as highly sensitive processes that could deliver a new generation of antiviral agents across viral diseases.
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Authors | Klaus Klumpp, Thibaut Crépin |
Journal | Current opinion in virology
(Curr Opin Virol)
Vol. 5
Pg. 63-71
(Apr 2014)
ISSN: 1879-6265 [Electronic] Netherlands |
PMID | 24607800
(Publication Type: Journal Article, Review)
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Copyright | Copyright © 2014 Elsevier B.V. All rights reserved. |
Chemical References |
- Anti-HIV Agents
- Capsid Proteins
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Topics |
- Animals
- Anti-HIV Agents
(pharmacology)
- Capsid Proteins
(antagonists & inhibitors, genetics, metabolism)
- HIV Infections
(drug therapy, virology)
- HIV-1
(drug effects, genetics, metabolism)
- Humans
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