ArticleThe Journal of biological chemistry2008
APOBEC3G subunits self-associate via the C-terminal deaminase domain.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 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.
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Who cites it
36 citing papers in PubMed, 48 citations in OpenAlex.
- Small-Angle X-ray Scattering Models of APOBEC3B Catalytic Domain in a Complex with a Single-Stranded DNA Inhibitor.Viruses · 2021Article
- The Role of APOBECs in Viral Replication.Microorganisms · 2020Review
- Understanding the structural basis of HIV-1 restriction by the full length double-domain APOBEC3G.Nature communications · 2020Article
- Modeling the Embrace of a Mutator: APOBEC Selection of Nucleic Acid Ligands.Trends in biochemical sciences · 2018Review
- Solution structure of extracellular loop of human β4 subunit of BK channel and its biological implication on ChTX sensitivity.Scientific reports · 2018Article
- Dimerization regulates both deaminase-dependent and deaminase-independent HIV-1 restriction by APOBEC3G.Nature communications · 2017Article
- Review
- Structural determinants of APOBEC3B non-catalytic domain for molecular assembly and catalytic regulation.Nucleic acids research · 2017Article
- Mechanism of Enhanced HIV Restriction by Virion Coencapsidated Cytidine Deaminases APOBEC3F and APOBEC3G.Journal of virology · 2017Article
- The double-domain cytidine deaminase APOBEC3G is a cellular site-specific RNA editing enzyme.Scientific reports · 2016Article
- Structural and functional assessment of APOBEC3G macromolecular complexes.Methods (San Diego, Calif.) · 2016Article
- APOBEC3G-Mediated G-to-A Hypermutation of the HIV-1 Genome: The Missing Link in Antiviral Molecular Mechanisms.Frontiers in microbiology · 2016Review
- RNA binding to APOBEC3G induces the disassembly of functional deaminase complexes by displacing single-stranded DNA substrates.Nucleic acids research · 2015Article
- Characterization of the Catalytic Domain of Human APOBEC3B and the Critical Structural Role for a Conserved Methionine.Journal of molecular biology · 2015Article
- Crystal structure of DNA cytidine deaminase ABOBEC3G catalytic deamination domain suggests a binding mode of full-length enzyme to single-stranded DNA.The Journal of biological chemistry · 2015Article
- Atomic force microscopy studies of APOBEC3G oligomerization and dynamics.Journal of structural biology · 2013Article
- Binding of RNA by APOBEC3G controls deamination-independent restriction of retroviruses.Nucleic acids research · 2013Article
- HIV-1 viral infectivity factor (Vif) alters processive single-stranded DNA scanning of the retroviral restriction factor APOBEC3G.The Journal of biological chemistry · 2013Article
- Retroviral restriction factor APOBEC3G delays the initiation of DNA synthesis by HIV-1 reverse transcriptase.PloS one · 2013Article
- Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Human APOBEC3G (hA3G) is a cytidine deaminase active on HIV single-stranded DNA. Small angle x-ray scattering and molecular envelope restorations predicted a C-terminal dimeric model for RNA-depleted hA3G in solution. Each subunit was elongated, suggesting that individual domains of hA3G are solvent-exposed and therefore may interact with other macromolecules even as isolated substructures. In this study, co-immunoprecipitation and in-cell quenched fluorescence resonance energy transfer assays reveal that hA3G forms RNA-independent oligomers through interactions within its C terminus. Residues 209-336 were necessary and sufficient for homoligomerization. N-terminal domains of hA3G were unable to multimerize but remained functional for Gag and viral infectivity factor (Vif) interactions when expressed apart from the C terminus. These findings corroborate the small angle x-ray scattering structural model and are instructive for development of high throughput screens that target specific domains and their functions to identify HIV/AIDS therapeutics.
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What OpenQuestion holds
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.