ArticlePloS one2014
Interaction of APOBEC3A with DNA assessed by atomic force microscopy.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
19 citing papers in PubMed, 24 citations in OpenAlex.
- Guardian ubiquitin E3 ligases target cancer-associated APOBEC3 deaminases for degradation to promote human genome integrity.Nature communications · 2026Article
- Three-Way DNA Junction as an End Label for DNA in Atomic Force Microscopy Studies.International journal of molecular sciences · 2022Article
- Atomic force microscopy-A tool for structural and translational DNA research.APL bioengineering · 2021Review
- Detection of Hepatitis C Virus Core Protein in Serum Using Aptamer-Functionalized AFM Chips.Micromachines · 2019Article
- Probing The Structure And Dynamics Of Nucleosomes Using Atomic Force Microscopy Imaging.Journal of visualized experiments : JoVE · 2019Article
- Modeling the Embrace of a Mutator: APOBEC Selection of Nucleic Acid Ligands.Trends in biochemical sciences · 2018Review
- The Antiviral and Cancer Genomic DNA Deaminase APOBEC3H Is Regulated by an RNA-Mediated Dimerization Mechanism.Molecular cell · 2018Article
- Enzyme cycling contributes to efficient induction of genome mutagenesis by the cytidine deaminase APOBEC3B.Nucleic acids research · 2017Article
- Review
- Roles of APOBEC3A and APOBEC3B in Human Papillomavirus Infection and Disease Progression.Viruses · 2017Review
- Nanoscale Characterization of Interaction of APOBEC3G with RNA.Biochemistry · 2017Article
- Functions and Malfunctions of Mammalian DNA-Cytosine Deaminases.Chemical reviews · 2016Review
- Structural and functional assessment of APOBEC3G macromolecular complexes.Methods (San Diego, Calif.) · 2016Article
- Single-Molecule Force Spectroscopy Studies of APOBEC3A-Single-Stranded DNA Complexes.Biochemistry · 2016Article
- Functional requirements of AID's higher order structures and their interaction with RNA-binding proteins.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- APOBEC3G Interacts with ssDNA by Two Modes: AFM Studies.Scientific reports · 2015Article
- The ssDNA Mutator APOBEC3A Is Regulated by Cooperative Dimerization.Structure (London, England : 1993) · 2015Article
- A computational analysis of the structural determinants of APOBEC3's catalytic activity and vulnerability to HIV-1 Vif.Virology · 2014Article
- Suppression of APOBEC3-mediated restriction of HIV-1 by Vif.Frontiers in microbiology · 2014Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
The APOBEC3 family of DNA cytosine deaminases functions to block the spread of endogenous retroelements and retroviruses including HIV-1. Potency varies among family members depending on the type of parasitic substrate. APOBEC3A (A3A) is unique among the human enzymes in that it is expressed predominantly in myeloid lineage cell types, it is strongly induced by innate immune agonists such as type 1 interferon, and it has the capacity to accommodate both normal and 5-methyl cytosine nucleobases. Here we apply atomic force microscopy (AFM) to characterize the interaction between A3A and single- and double-stranded DNA using a hybrid DNA approach in which a single-stranded region is flanked by defined length duplexes. AFM image analyses reveal A3A binding to single-stranded DNA, and that this interaction becomes most evident (∼80% complex yield) at high protein-to-DNA ratios (at least 100∶1). A3A is predominantly monomeric when bound to single-stranded DNA, and it is also monomeric in solution at concentrations as high as 50 nM. These properties agree well with recent, biochemical, biophysical, and structural studies. However, these characteristics contrast with those of the related enzyme APOBEC3G, which in similar assays can exist as a monomer but tends to form oligomers in a concentration-dependent manner. These AFM data indicate that A3A has intrinsic biophysical differences that distinguish it from APOBEC3G. The potential relationships between these properties and biological functions in innate immunity are discussed.
Indexed as
Identifiers
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.