Evidence map›Paper›PMID 24367644›Full record

ArticlePloS one2013

APOBEC3G oligomerization is associated with the inhibition of both Alu and LINE-1 retrotransposition.

Takayoshi Koyama, Juan Fernando Arias, Yukie Iwabu, Masaru Yokoyama, Hideaki Fujita, Hironori Sato, Kenzo Tokunaga

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
3.2field-weighted citation impact, top 9% 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

12 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Post-transcriptional regulation of LINE-1 retrotransposition by AID/APOBEC and ADAR deaminases.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2018
    Review
  10. Review
  11. Article
  12. Review
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

7 authors at 2 institutions in 1 country.

Takayoshi KoyamaDepartment of Pathology, National Institute of Infectious Diseases, Tokyo, Japan.
Juan Fernando AriasDepartment of Pathology, National Institute of Infectious Diseases, Tokyo, Japan.
Yukie IwabuDepartment of Pathology, National Institute of Infectious Diseases, Tokyo, Japan.
Masaru YokoyamaPathogen Genomics Center, National Institute of Infectious Diseases, Tokyo, Japan.
Hideaki FujitaFaculty of Pharmaceutical Sciences, Nagasaki International University, Nagasaki, Japan.
Hironori SatoPathogen Genomics Center, National Institute of Infectious Diseases, Tokyo, Japan.
Kenzo TokunagaDepartment of Pathology, National Institute of Infectious Diseases, Tokyo, Japan.
National Institute of Infectious Diseases · JPNagasaki International University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Alu and LINE-1 (L1), which constitute ~11% and ~17% of the human genome, respectively, are transposable non-LTR retroelements. They transpose not only in germ cells but also in somatic cells, occasionally causing cancer. We have previously demonstrated that antiretroviral restriction factors, human APOBEC3 (hA3) proteins (A-H), differentially inhibit L1 retrotransposition. In this present study, we found that hA3 members also restrict Alu retrotransposition at differential levels that correlate with those observed previously for L1 inhibition. Through deletion analyses based on the best-characterized hA3 member human APOBEC3G (hA3G), its N-terminal 30 amino acids were required for its inhibitory activity against Alu retrotransposition. The inhibitory effect of hA3G on Alu retrotransposition was associated with its oligomerization that was affected by the deletion of its N-terminal 30 amino acids. Through structural modeling, the amino acids 24 to 28 of hA3G were predicted to be located at the interface of the dimer. The mutation of these residues resulted in abrogated hA3G oligomerization, and consistently abolished the inhibitory activity of hA3G against Alu retrotransposition. Importantly, the anti-L1 activity of hA3G was also associated with hA3G oligomerization. These results suggest that the inhibitory activities of hA3G against Alu and L1 retrotransposition might involve a common mechanism.

Indexed as

Protein MultimerizationAlu ElementsAPOBEC-3G DeaminaseCytidine DeaminaseHEK293 CellsHeLa CellsHumansLong Interspersed Nucleotide ElementsModels, MolecularProtein Structure, QuaternaryAPOBEC-3G DeaminaseAPOBEC3G protein, humanCytidine Deaminase

Identifiers

PMID24367644
PMCPMC3868573
OpenAlexW2008372222

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

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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.