Evidence map›Paper›PMID 26489798›Full record

ReviewThe Journal of general virology2016

Role of the single deaminase domain APOBEC3A in virus restriction, retrotransposition, DNA damage and cancer.

Yaqiong Wang, Kimberly Schmitt, Kejun Guo, Mario L Santiago, Edward B Stephens

Open access · greenAbstract readReview
In one paragraph

Review in The Journal of general virology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

10 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
  2. Article
  3. Early reduction of SARS-CoV-2-replication in bronchial epithelium by kinin BJournal of molecular medicine (Berlin, Germany) · 2022
    Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
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

5 authors at 2 institutions in 1 country.

Yaqiong WangDepartment of Microbiology, Molecular Genetics and Immunology, University of Kansas Medical Center, 3901 Rainbow Blvd, Kansas City, KS 66160, USA.
Kimberly SchmittDepartment of Microbiology, Molecular Genetics and Immunology, University of Kansas Medical Center, 3901 Rainbow Blvd, Kansas City, KS 66160, USA.
Kejun GuoDepartments of Medicine, Microbiology and Immunology, University of Colorado Denver Medical School, Aurora, CO 80045, USA.
Mario L SantiagoDepartments of Medicine, Microbiology and Immunology, University of Colorado Denver Medical School, Aurora, CO 80045, USA.
Edward B StephensDepartment of Microbiology, Molecular Genetics and Immunology, University of Kansas Medical Center, 3901 Rainbow Blvd, Kansas City, KS 66160, USA.
University of Kansas Medical Center · USUniversity of Colorado Denver · US

Funding

Innate Restriction Factor Modulation of Retrovirus-specific Humoral ImmunityR01AI090795 · NIAID · UNIVERSITY OF COLORADO DENVER · PI SANTIAGO, MARIO LUIS · 2010 to 2013
$2.8M
A Novel Mechanism of Restriction by an APOBEC3 ProteinR21AI108391 · NIAID · UNIVERSITY OF KANSAS MEDICAL CENTER · PI STEPHENS, EDWARD BRICE · 2014 to 2015
$415k
NIAID NIH HHS R01 AI090795NIAID NIH HHS R21 AI108391
6 · The paper itself

Abstract

The apolipoprotein mRNA editing enzyme catalytic polypeptide-like 3 (APOBEC3; A3) proteins are a family of seven cytidine deaminases (A3A, A3B, A3C, A3D, A3F, A3G and A3H) that restrict certain viral infections. These innate defence factors are best known for their ability to restrict the replication of human immunodeficiency virus type 1 (HIV-1) lacking a functional Vif protein (HIV-1Δvif) through the deamination of cytidine residues to uridines during reverse transcription, ultimately leading to lethal G → A changes in the viral genome. The best studied of the A3 proteins has been APOBEC3G because of its potent activity against HIV-1Δvif. However, one member of this family, A3A, has biological properties that make it unique among the A3 proteins. In this review, we will focus on the structural and phylogenetic features of the human and non-human primate A3A proteins, their role in the restriction of retroviruses and other viruses, and current findings on other biological properties affected by this protein.

Indexed as

DNA DamageRecombination, GeneticAnimalsCytidine DeaminaseHumansNeoplasmsPrimatesRetroviridaeRetroviridae InfectionsCytidine Deaminase

Identifiers

PMID26489798
PMCPMC5972328
OpenAlexW2111479429

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.