ArticleJournal of virology2008
Two regions within the amino-terminal half of APOBEC3G cooperate to determine cytoplasmic localization.
Article in Journal of virology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
62 citing papers in PubMed, 74 citations in OpenAlex.
- Full-length structure of the anti-viral and pro-tumor DNA deaminase APOBEC3B.bioRxiv : the preprint server for biology · 2026Article
- Mechanisms of APOBEC3 Packaging into HIV-1.Viruses · 2026Review
- APOBEC3-Related Editing and Non-Editing Determinants of HIV-1 and HTLV-1 Restriction.International journal of molecular sciences · 2025Review
- Engineered deaminases as a key component of DNA and RNA editing tools.Molecular therapy. Nucleic acids · 2023Review
- Evolutionary potential of the monkeypox genome arising from interactions with human APOBEC3 enzymes.bioRxiv : the preprint server for biology · 2023Article
- Article
- Evolutionary potential of the monkeypox genome arising from interactions with human APOBEC3 enzymes.Virus evolution · 2023Article
- Ancestral APOBEC3B Nuclear Localization Is Maintained in Humans and Apes and Altered in Most Other Old World Primate Species.mSphere · 2022Article
- Exploring ABOBEC3A and APOBEC3B substrate specificity and their role in HPV positive head and neck cancer.iScience · 2022Article
- APOBEC3: Friend or Foe in Human Papillomavirus Infection and Oncogenesis?Annual review of virology · 2022Review
- The current toolbox for APOBEC drug discovery.Trends in pharmacological sciences · 2022Review
- Highly-potent, synthetic APOBEC3s restrict HIV-1 through deamination-independent mechanisms.PLoS pathogens · 2021Article
- Targeting natural splicing plasticity of APOBEC3B restricts its expression and mutagenic activity.Communications biology · 2021Article
- Review
- Characterization of an A3G-VifMolecular & cellular proteomics : MCP · 2021Article
- Article
- The DNA Cytosine Deaminase APOBEC3B is a Molecular Determinant of Platinum Responsiveness in Clear Cell Ovarian Cancer.Clinical cancer research : an official journal of the American Association for Cancer Research · 2020Article
- The Role of RNA in HIV-1 Vif-Mediated Degradation of APOBEC3H.Journal of molecular biology · 2019Article
- The spectrum of APOBEC3 activity: From anti-viral agents to anti-cancer opportunities.DNA repair · 2019Review
- A Rabbit Monoclonal Antibody against the Antiviral and Cancer Genomic DNA Mutating Enzyme APOBEC3B.Antibodies (Basel, Switzerland) · 2019Article
2 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 2 institutions in 3 countries.
Funding
Abstract
APOBEC3G limits the replication of human immunodeficiency virus type 1, other retroviruses, and retrotransposons. It localizes predominantly to the cytoplasm of cells, which is consistent with a model wherein cytosolic APOBEC3G packages into assembling virions, where it exerts its antiviral effect by deaminating viral cDNA cytosines during reverse transcription. To define the domains of APOBEC3G that determine cytoplasmic localization, comparisons were made with APOBEC3B, which is predominantly nuclear. APOBEC3G/APOBEC3B chimeric proteins mapped a primary subcellular localization determinant to a region within the first 60 residues of each protein. A panel of 25 APOBEC3G mutants, each with a residue replaced by the corresponding amino acid of APOBEC3B, revealed that several positions within this region were particularly important, with Y19D showing the largest effect. The mislocalization phenotype of these mutants was only apparent in the context of the amino-terminal half of APOBEC3G and not the full-length protein, suggesting the existence of an additional localization determinant. Indeed, a panel of five single amino acid substitutions within the region from amino acids 113 to 128 had little effect by themselves but, in combination with Y19D, two substitutions-F126S and W127A-caused full-length APOBEC3G to redistribute throughout the cell. The critical localization-determining residues were predicted to cluster on a common solvent-exposed surface, suggesting a model in which these two regions of APOBEC3G combine to mediate an intermolecular interaction that controls subcellular localization.
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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.