ArticleNature communications2016
Crystal structures of APOBEC3G N-domain alone and its complex with DNA.
Article in Nature communications, 2016. 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.
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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.
- Structure of full-length APOBEC3B bound to EBV BORF2 reveals coordinated neutralization of a cancer-associated mutator.Research square · 2026Article
- Review
- Guardian ubiquitin E3 ligases target cancer-associated APOBEC3 deaminases for degradation to promote human genome integrity.Nature communications · 2026Article
- Article
- Affinity Tag-Free Purification of SARS-CoV-2 N Protein and Its Crystal Structure in Complex with ssDNA.Biomolecules · 2024Article
- Molecular mechanism for regulating APOBEC3G DNA editing function by the non-catalytic domain.Nature communications · 2024Article
- Structural insights into PPP2R5A degradation by HIV-1 Vif.Nature structural & molecular biology · 2024Article
- Structure-based prediction of protein-nucleic acid binding using graph neural networks.Biophysical reviews · 2024Review
- The RNA tether model for human chromosomal translocation fragile zones.Trends in biochemical sciences · 2024Review
- Molecular mechanism for regulating APOBEC3G DNA editing function by the non-catalytic domain.bioRxiv : the preprint server for biology · 2024Article
- Synthesis of 1,4-azaphosphinine nucleosides and evaluation as inhibitors of human cytidine deaminase and APOBEC3A.Beilstein journal of organic chemistry · 2024Article
- Structure-guided inhibition of the cancer DNA-mutating enzyme APOBEC3A.Nature communications · 2023Article
- Structural insights into RNA bridging between HIV-1 Vif and antiviral factor APOBEC3G.Nature communications · 2023Article
- Structure-guided inhibition of the cancer DNA-mutating enzyme APOBEC3A.bioRxiv : the preprint server for biology · 2023Article
- Structural basis for HIV-1 antagonism of host APOBEC3G via Cullin E3 ligase.Science advances · 2023Article
- Two different kinds of interaction modes of deaminase APOBEC3A with single-stranded DNA in solution detected by nuclear magnetic resonance.Protein science : a publication of the Protein Society · 2022Article
- New Insights Into the Lineage-Specific Expansion and Functional Diversification of Lamprey AID/APOBEC Family.Frontiers in immunology · 2022Article
- Article
- Multifaceted HIV-1 Vif interactions with human E3 ubiquitin ligase and APOBEC3s.The FEBS journal · 2021Article
- Interactions of APOBEC3s with DNA and RNA.Current opinion in structural biology · 2021Review
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
4 authors.
Funding
Abstract
APOBEC3G (A3G) is a potent restriction factor of HIV-1. The N-terminal domain of A3G (A3G-CD1) is responsible for oligomerization and nucleic acid binding, both of which are essential for anti-HIV activity. As a countermeasure, HIV-1 viral infectivity factor (Vif) binds A3G-CD1 to mediate A3G degradation. The structural basis for the functions of A3G-CD1 remains elusive. Here, we report the crystal structures of a primate A3G-CD1 (rA3G-CD1) alone and in complex with single-stranded DNA (ssDNA). rA3G-CD1 shares a conserved core structure with the previously determined catalytic APOBECs, but displays unique features for surface charge, dimerization and nucleic acid binding. Its co-crystal structure with ssDNA reveals how the conformations of loops and residues surrounding the Zn-coordinated centre (Zn-centre) change upon DNA binding. The dimerization interface of rA3G-CD1 is important for oligomerization, nucleic acid binding and Vif-mediated degradation. These findings elucidate the molecular basis of antiviral mechanism and HIV-Vif targeting of A3G.
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