Evidence map›Paper›PMID 27585283›Full record

ReviewChemical reviews2016

Functions and Malfunctions of Mammalian DNA-Cytosine Deaminases.

Sachini U Siriwardena, Kang Chen, Ashok S Bhagwat

Open access · greenAbstract readReview
In one paragraph

Review in Chemical reviews, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 87 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
87citing papers in PubMed, 1 pooled it
12.2field-weighted citation impact, top 1% 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

87 citing papers in PubMed, 1 synthesis or guideline pooled it, 145 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Article
  4. HAMMER: Hairpin-based APOBEC3A-mediated mRNA editing reporter.bioRxiv : the preprint server for biology · 2026
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
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  11. Review
  12. B-Cell Epigenetic Modulation of IgA Response by 5-Azacytidine and IgA Nephropathy.Journal of the American Society of Nephrology : JASN · 2024
    Article
  13. Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

27 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

3 authors at 2 institutions in 1 country.

Sachini U SiriwardenaDepartment of Chemistry, Wayne State University , Detroit, Michigan 48202, United States.
Kang ChenDepartment of Obstetrics and Gynecology, Wayne State University , Detroit, Michigan 48201, United States.
Ashok S BhagwatDepartment of Chemistry, Wayne State University , Detroit, Michigan 48202, United States.
Wayne State University · USNational Institutes of Health · US

Funding

Tumor Biology and Microenvironment (Program 1)P30CA022453 · NCI · WAYNE STATE UNIVERSITY · PI PAUL M STEMMER · 1985 to 2026
$68.4M
Human MAIT celis in airway mucosal immune responses to intracellular infectionsU01AI095776 · NIAID · OREGON HEALTH & SCIENCE UNIVERSITY · PI LEWINSOHN, DAVID M. · 2011 to 2015
$8.9M
TRANSCRIPTION--INDUCED MUTATIONSR01GM057200 · NIGMS · WAYNE STATE UNIVERSITY · PI BHAGWAT, ASHOK S · 1998 to 2014
$2.6M
Mechanism of Humoral Immune Defects in Autoimmune Polyglandular Syndrome Type 1R21AI122256 · NIAID · WAYNE STATE UNIVERSITY · PI CHEN, KANG · 2016 to 2017
$419k
NCI NIH HHS P30 CA022453NIAID NIH HHS R21 AI122256NIAID NIH HHS U01 AI095776NIGMS NIH HHS R01 GM057200
6 · The paper itself

Abstract

The AID/APOBEC family enzymes convert cytosines in single-stranded DNA to uracils, causing base substitutions and strand breaks. They are induced by cytokines produced during the body's inflammatory response to infections, and they help combat infections through diverse mechanisms. AID is essential for the maturation of antibodies and causes mutations and deletions in antibody genes through somatic hypermutation (SHM) and class-switch recombination (CSR) processes. One member of the APOBEC family, APOBEC1, edits mRNA for a protein involved in lipid transport. Members of the APOBEC3 subfamily in humans (APOBEC3A, APOBEC3B, APOBEC3C, APOBEC3D, APOBEC3F, APOBEC3G, and APOBEC3H) inhibit infections of viruses such as HIV-1, HBV, and HCV, and retrotransposition of endogenous retroelements through mutagenic and nonmutagenic mechanisms. There is emerging consensus that these enzymes can cause mutations in the cellular genome at replication forks or within transcription bubbles depending on the physiological state of the cell and the phase of the cell cycle during which they are expressed. We describe here the state of knowledge about the structures of these enzymes, regulation of their expression, and both the advantageous and deleterious consequences of their expression, including carcinogenesis. We highlight similarities among them and present a holistic view of their regulation and function.

Indexed as

AICDA (Activation-Induced Cytidine Deaminase)AnimalsAPOBEC DeaminasesCytidine DeaminaseDNAMammalsAICDA (Activation-Induced Cytidine Deaminase)APOBEC DeaminasesCytidine DeaminaseDNA

Identifiers

PMID27585283
PMCPMC5528147
OpenAlexW2513500966

What Socratic holds

Textmetadata
LicenceTDM
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 Socratic graph.