ArticleCell reports2015
Identification of the HIV-1 Vif and Human APOBEC3G Protein Interface.
Article in Cell reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
What it found
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Who cites it
47 citing papers in PubMed, 59 citations in OpenAlex.
- Aminopeptidase N is a receptor for hedgehog merbecoviruses.Nature microbiology · 2026Article
- Strain-specific epistasis shapes fitness landscapes of APOBEC3G antagonism by HIV-1 Vif proteins.Science advances · 2026Article
- Review
- Exploring coronavirus cell entry with functional viromics.Journal of virology · 2026Review
- Fitness Landscapes of APOBEC3G Antagonism by HIV-1 Vif proteins.bioRxiv : the preprint server for biology · 2025Article
- APOBEC3G Antagonism by Vif, or When Structure Meets Biological and Evolutionary Studies.Annual review of virology · 2025Review
- ACE2 from Pipistrellus abramus bats is a receptor for HKU5 coronaviruses.Nature communications · 2025Article
- Deciphering lentiviral Vpr/Vpx determinants required for HUSH and SAMHD1 antagonism highlights the molecular plasticity of these evolutionary conflicts.Journal of virology · 2025Article
- Article
- Article
- Structural insights into PPP2R5A degradation by HIV-1 Vif.Nature structural & molecular biology · 2024Article
- Structural insights into RNA bridging between HIV-1 Vif and antiviral factor APOBEC3G.Nature communications · 2023Article
- Article
- Structural basis for HIV-1 antagonism of host APOBEC3G via Cullin E3 ligase.Science advances · 2023Article
- HIV-1 Vif Gained Breadth in APOBEC3G Specificity after Cross-Species Transmission of Its Precursors.Journal of virology · 2022Article
- The interplay between pathogens and Atg8 family proteins: thousand-faced interactions.FEBS open bio · 2021Review
- Examination of the APOBEC3 Barrier to Cross Species Transmission of Primate Lentiviruses.Viruses · 2021Review
- Characterization of an A3G-VifMolecular & cellular proteomics : MCP · 2021Article
- A role for gorilla APOBEC3G in shaping lentivirus evolution including transmission to humans.PLoS pathogens · 2020Article
- Review
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
Human cells express natural antiviral proteins, such as APOBEC3G (A3G), that potently restrict HIV replication. As a counter-defense, HIV encodes the accessory protein Vif, which binds A3G and mediates its proteasomal degradation. Our structural knowledge on how Vif and A3G interact is limited, because a co-structure is not available. We identified specific points of contact between Vif and A3G by using functional assays with full-length A3G, patient-derived Vif variants, and HIV forced evolution. These anchor points were used to model and validate the Vif-A3G interface. The resultant co-structure model shows that the negatively charged β4-α4 A3G loop, which contains primate-specific variation, is the core Vif binding site and forms extensive interactions with a positively charged pocket in HIV Vif. Our data present a functional map of this viral-host interface and open avenues for targeted approaches to block HIV replication by obstructing the Vif-A3G interaction.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.