ArticleAntimicrobial agents and chemotherapy2001
Role of human immunodeficiency virus (HIV) type 1 envelope in the anti-HIV activity of the betulinic acid derivative IC9564.
Article in Antimicrobial agents and chemotherapy, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 85 citations in OpenAlex.
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- Enhancing Betulinic Acid Dissolution Rate and Improving Antitumor Activity via Nanosuspension Constructed by Anti-Solvent Technique.Drug design, development and therapy · 2020Article
- Promiscuous, Multi-Target Lupane-Type Triterpenoids Inhibits Wild Type and Drug Resistant HIV-1 Replication Through the Interference With Several Targets.Frontiers in pharmacology · 2018Article
- Structure Optimization of Aloperine Derivatives as HIV-1 Entry Inhibitors.ACS medicinal chemistry letters · 2017Article
- Identification of potent maturation inhibitors against HIV-1 clade C.Scientific reports · 2016Article
- Ionic derivatives of betulinic acid exhibit antiviral activity against herpes simplex virus type-2 (HSV-2), but not HIV-1 reverse transcriptase.Bioorganic & medicinal chemistry letters · 2015Article
- Glycol chitosan incorporated retinoic acid chlorochalcone (RACC) nanoparticles in the treatment of Osteosarcoma.Lipids in health and disease · 2015Article
- New betulinic acid derivatives for bevirimat-resistant human immunodeficiency virus type-1.Journal of medicinal chemistry · 2013Article
- Review
- Ionic derivatives of betulinic acid as novel HIV-1 protease inhibitors.Journal of enzyme inhibition and medicinal chemistry · 2012Article
- Synthesis of betulinic acid derivatives as entry inhibitors against HIV-1 and bevirimat-resistant HIV-1 variants.Bioorganic & medicinal chemistry letters · 2012Article
- Docking study of HIV-1 reverse transcriptase with phytochemicals.Bioinformation · 2011Article
- A low-molecular-weight entry inhibitor of both CCR5- and CXCR4-tropic strains of human immunodeficiency virus type 1 targets a novel site on gp41.Journal of virology · 2010Article
- Phenotypic susceptibility to bevirimat in isolates from HIV-1-infected patients without prior exposure to bevirimat.Antimicrobial agents and chemotherapy · 2010Article
- HIV entry inhibitors and their potential in HIV therapy.Medicinal research reviews · 2009Review
- Proteasome regulators: activators and inhibitors.Current medicinal chemistry · 2009Review
- Betulinic acid derivatives that target gp120 and inhibit multiple genetic subtypes of human immunodeficiency virus type 1.Antimicrobial agents and chemotherapy · 2008Article
- Activation and inhibition of the proteasome by betulinic acid and its derivatives.FEBS letters · 2007Article
- Anti-AIDS agents 69. Moronic acid and other triterpene derivatives as novel potent anti-HIV agents.Journal of medicinal chemistry · 2006Article
- Inhibition of human immunodeficiency virus type 1 entry by a binding domain of Porphyromonas gingivalis gingipain.Antimicrobial agents and chemotherapy · 2006Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
The betulinic acid derivative IC9564 is a potent anti-human immunodeficiency virus (anti-HIV) compound that can inhibit both HIV primary isolates and laboratory-adapted strains. However, this compound did not affect the replication of simian immunodeficiency virus and respiratory syncytial virus. Results from a syncytium formation assay indicated that IC9564 blocked HIV type 1 (HIV-1) envelope-mediated membrane fusion. Analysis of a chimeric virus derived from exchanging envelope regions between IC9564-sensitive and IC9564-resistant viruses indicated that regions within gp120 and the N-terminal 25 amino acids (fusion domain) of gp41 are key determinants for the drug sensitivity. By developing a drug-resistant mutant from the NL4-3 virus, two mutations were found within the gp120 region and one was found within the gp41 region. The mutations are G237R and R252K in gp120 and R533A in the fusion domain of gp41. The mutations were reintroduced into the NL4-3 envelope and analyzed for their role in IC9564 resistance. Both of the gp120 mutations contributed to the drug sensitivity. On the contrary, the gp41 mutation (R533A) did not appear to affect the IC9564 sensitivity. These results suggest that HIV-1 gp120 plays a key role in the anti-HIV-1 activity of IC9564.
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