Evidence map›Paper›PMID 15809227›Full record

ArticleNucleic acids research2005

Mutational comparison of the single-domained APOBEC3C and double-domained APOBEC3F/G anti-retroviral cytidine deaminases provides insight into their DNA target site specificities.

Marc-André Langlois, Rupert C L Beale, Silvestro G Conticello, Michael S Neuberger

Open access · goldAbstract readComparative Study
In one paragraph

Article in Nucleic acids research, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 131 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
131citing papers in PubMed, 1 pooled it
4.8field-weighted citation impact, top 4% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

131 citing papers in PubMed, 1 synthesis or guideline pooled it, 181 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. Journal of virology · 2025
    Article
  6. Article
  7. Review
  8. Article
  9. Myelodysplasia and transgene inactivation in X-CGD-γ retroviral gene therapy: The usual suspects and new players.Molecular therapy : the journal of the American Society of Gene Therapy · 2023
    Article
  10. Article
  11. The current toolbox for APOBEC drug discovery.Trends in pharmacological sciences · 2022
    Review
  12. Review
  13. Interactions of APOBEC3s with DNA and RNA.Current opinion in structural biology · 2021
    Review
  14. Review
  15. Review
  16. Article
  17. Review
  18. Article
  19. Article
  20. Article

71 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Marc-André LangloisMedical Research Council Laboratory of Molecular Biology, Division of Protein and Nucleic Acid Chemistry Hills Road, Cambridge CB2 2QH, UK.
Rupert C L Beale
Silvestro G Conticello
Michael S Neuberger
MRC Laboratory of Molecular Biology · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Human APOBEC3F and APOBEC3G are double-domained deaminases that can catalyze dC-->dU deamination in HIV-1 and MLV retroviral DNA replication intermediates, targeting T-C or C-C dinucleotides, respectively. HIV-1 antagonizes their action through its vif gene product, which has been shown (at least in the case of APOBEC3G) to interact with the N-terminal domain of the deaminase, triggering its degradation. Here, we compare APOBEC3F and APOBEC3G to APOBEC3C, a single-domained deaminase that can also act on both HIV-1 and MLV. We find that whereas APOBEC3C contains all the information necessary for both Vif-binding and cytidine deaminase activity in a single domain, it is the C-terminal domain of APOBEC3F and APOBEC3G that confer their target site specificity for cytidine deamination. We have exploited the fact that APOBEC3C, whilst highly homologous to the C-terminal domain of APOBEC3F, exhibits a distinct target site specificity (preferring Y-C dinucleotides) in order to identify residues in APOBEC3F that might affect its target site specificity. We find that this specificity can be altered by single amino acid substitutions at several distinct positions, suggesting that the strong dependence of APOBEC3-mediated deoxycytidine deamination on the 5'-flanking nucleotide is sensitive to relatively subtle changes in the APOBEC3 structure. The approach has allowed the isolation of APOBEC3 DNA mutators that exhibit novel target site preferences.

Indexed as

Amino Acid SubstitutionAnti-Retroviral AgentsAPOBEC-3G DeaminaseCytidine DeaminaseCytosine DeaminaseDNA Mutational AnalysisDNA, ViralHumansLeukemia Virus, MurineNucleoside DeaminasesProteinsRecombinant Fusion ProteinsRepressor ProteinsSubstrate SpecificityAnti-Retroviral AgentsAPOBEC3C protein, humanAPOBEC3F protein, humanAPOBEC-3G DeaminaseAPOBEC3G protein, humanCytidine DeaminaseCytosine DeaminaseDNA, ViralNucleoside DeaminasesProteinsRecombinant Fusion ProteinsRepressor Proteins

Identifiers

PMID15809227
PMCPMC1074398
OpenAlexW1995691974

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.