ArticleNucleic acids research2017
Cytidine deaminase efficiency of the lentiviral viral restriction factor APOBEC3C correlates with dimerization.
Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 49 citations in OpenAlex.
- A viral APOBEC3 antagonist distinguishes HHV-6A from HHV-6B.Nature communications · 2026Article
- Mechanisms of APOBEC3 Packaging into HIV-1.Viruses · 2026Review
- DNA secondary structures in BCL2 and MYC elicit activation-induced cytidine deaminase binding and activity.Nucleic acids research · 2026Article
- Review
- Article
- Article
- Evolvability of cancer-associated genes under APOBEC3A/B selection.bioRxiv : the preprint server for biology · 2023Article
- Article
- Similar deamination activities but different phenotypic outcomes induced by APOBEC3 enzymes in breast epithelial cells.Frontiers in genome editing · 2023Article
- The current toolbox for APOBEC drug discovery.Trends in pharmacological sciences · 2022Review
- Divergence in Dimerization and Activity of Primate APOBEC3C.Journal of molecular biology · 2021Article
- Examination of the APOBEC3 Barrier to Cross Species Transmission of Primate Lentiviruses.Viruses · 2021Review
- Review
- Review
- APOBEC1 cytosine deaminase activity on single-stranded DNA is suppressed by replication protein A.Nucleic acids research · 2021Article
- Retroviral Restriction Factors and Their Viral Targets: Restriction Strategies and Evolutionary Adaptations.Microorganisms · 2020Review
- Single-nucleotide polymorphism of the DNA cytosine deaminase APOBEC3H haplotype I leads to enzyme destabilization and correlates with lung cancer.NAR cancer · 2020Article
- Review
- Article
- Deamination hotspots among APOBEC3 family members are defined by both target site sequence context and ssDNA secondary structure.Nucleic acids research · 2020Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
The seven APOBEC3 (A3) enzymes in primates restrict HIV/SIV replication to differing degrees by deaminating cytosine in viral (-)DNA, which forms promutagenic uracils that inactivate the virus. A polymorphism in human APOBEC3C (A3C) that encodes an S188I mutation increases the enzymatic activity of the protein and its ability to restrict HIV-1, and correlates with increased propensity to form dimers. However, other hominid A3C proteins only have an S188, suggesting they should be less active like the common form of human A3C. Nonetheless, here we demonstrate that chimpanzee and gorilla A3C have approximately equivalent activity to human A3C I188 and that chimpanzee and gorilla A3C form dimers at the same interface as human A3C S188I, but through different amino acids. For each of these hominid A3C enzymes, dimerization enables processivity on single-stranded DNA and results in higher levels of mutagenesis during reverse transcription in vitro and in cells. For increased mutagenic activity, formation of a dimer was more important than specific amino acids and the dimer interface is unique from other A3 enzymes. We propose that dimerization is a predictor of A3C enzyme activity.
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Registered trials
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