ArticleCell chemical biology2024
Identification of clickable HIV-1 capsid-targeting probes for viral replication inhibition.
Article in Cell chemical biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Capsid-Targeting Biologic Achieves Broad HIV-1 Neutralization with a High Barrier to Resistance.International journal of molecular sciences · 2026Article
- Damaging the conical morphology of HIV-1 capsid by targeting the FG-binding pocket and disfavoring pentameric subunits needed for core closure.bioRxiv : the preprint server for biology · 2026Article
- Antiviral drug discovery and development: challenges and future directions.Signal transduction and targeted therapy · 2026Review
- Structure-Aided Design of a LuxR-Type Quorum Sensing SuFEx-Based Potential Inhibitor: Covalent or Competitive Inhibition?Biomolecules · 2026Article
- Research progress on HIV-1 structural proteins and antiviral therapies.Frontiers in immunology · 2026Review
- Design, synthesis and profiling of highly potent antivirals targeting emerging drug-resistant HIV-1 variants.bioRxiv : the preprint server for biology · 2025Article
- Clicking viruses-with chemistry toward mechanisms in infection.Journal of virology · 2025Review
- Advances in sulfonyl exchange chemical biology: expanding druggable target space.Chemical science · 2025Review
Corrections and comments
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Authors and funding
18 authors.
Funding
Abstract
Of the targets for HIV-1 therapeutics, the capsid core is a relatively unexploited but alluring drug target due to its indispensable roles throughout virus replication. Because of this, we aimed to identify "clickable" covalent modifiers of the HIV-1 capsid protein (CA) for future functionalization. We screened a library of fluorosulfate compounds that can undergo sulfur(VI) fluoride exchange (SuFEx) reactions, and five compounds were identified as hits. These molecules were further characterized for antiviral effects. Several compounds impacted in vitro capsid assembly. One compound, BBS-103, covalently bound CA via a SuFEx reaction to Tyr145 and had antiviral activity in cell-based assays by perturbing virus production, but not uncoating. The covalent binding of compounds that target the HIV-1 capsid could aid in the future design of antiretroviral drugs or chemical probes that will help study aspects of HIV-1 replication.
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Registered trials
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