Evidence map›Paper›PMID 30222709›Full record

ReviewPharmacogenetics and genomics2018

Functional expression of human arylamine N-acetyltransferase NAT1*10 and NAT1*11 alleles: a mini review.

David W Hein, Giannoulis Fakis, Sotiria Boukouvala

Open access · greenAbstract readReview
In one paragraph

Review in Pharmacogenetics and genomics, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.4field-weighted citation impact, top 22% 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

9 citing papers in PubMed, 21 citations in OpenAlex.

  1. Article
  2. Article
  3. Acetyl coenzyme A kinetic studies onFrontiers in pharmacology · 2022
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Hypermethylation ofFrontiers in genetics · 2019
    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

3 authors at 2 institutions in 2 countries.

David W HeinDepartment of Pharmacology and Toxicology, University of Louisville Health Sciences Center, Louisville, Kentucky, USA.
Giannoulis FakisDepartment of Molecular Biology and Genetics, Democritus University of Thrace, Alexandroupolis, Greece.
Sotiria BoukouvalaDepartment of Molecular Biology and Genetics, Democritus University of Thrace, Alexandroupolis, Greece.
Democritus University of Thrace · GRKosair Charities · US

Funding

Role of oxidized linoleic acid metabolites in the pathogenesis of alcoholic liver diseaseP20GM113226 · NIGMS · UNIVERSITY OF LOUISVILLE · PI MCCLAIN, CRAIG J. · 2016 to 2025
$24.1M
Superfund Training CoreP42ES023716 · NIEHS · UNIVERSITY OF LOUISVILLE · PI SRIVASTAVA, SANJAY · 2017 to 2025
$18.1M
The Role of Nutrition in the Development/Progression of Alcohol-Induced Organ InjuryP50AA024337 · NIAAA · UNIVERSITY OF LOUISVILLE · PI CRAIG J. MCCLAIN · 2016 to 2026
$17.9M
University of Louisville Cancer Education ProgramR25CA134283 · NCI · UNIVERSITY OF LOUISVILLE · PI HEIN, DAVID W, KIDD, LA CREIS RENEE · 2011 to 2022
$3.1M
NCI NIH HHS R25 CA134283NIAAA NIH HHS P50 AA024337NIEHS NIH HHS P42 ES023716NIGMS NIH HHS P20 GM113226
6 · The paper itself

Abstract

The arylamine N-acetyltransferase (NAT) nomenclature committee assigns functional phenotypes for human arylamine N-acetyltransferase 1 (NAT1) alleles in those instances in which the committee determined a consensus has been achieved in the scientific literature. In the most recent nomenclature update, the committee announced that functional phenotypes for NAT1*10 and NAT1*11 alleles were not provided owing to a lack of consensus. Phenotypic inconsistencies observed among various studies for NAT1*10 and NAT1*11 may be owing to variable allelic expression among different tissues, the limitations of the genotyping assays (which mostly relied on techniques not involving direct DNA sequencing), the differences in recombinant protein expression systems used (bacteria, yeast, and mammalian cell lines) and/or the known inherent instability of human NAT1 protein, which requires very careful handling of native and recombinant cell lysates. Three recent studies provide consistent evidence of the mechanistic basis underlying the functional phenotype of NAT1*10 and NAT1*11 as 'increased-activity' alleles. Some NAT1 variants (e.g. NAT1*14, NAT1*17, and NAT1*22) may be designated as 'decreased-activity' alleles and other NAT1 variants (e.g. NAT1*15 and NAT1*19) may be designated as 'no-activity' alleles compared with the NAT1*4 reference allele. We propose that phenotypic designations as 'rapid' and 'slow' acetylator should be discontinued for NAT1 alleles, although these designations remain very appropriate for NAT2 alleles.

Indexed as

AcetylationAllelesArylamine N-AcetyltransferaseGene Expression RegulationHumansIsoenzymesKineticsArylamine N-AcetyltransferaseIsoenzymesN-acetyltransferase 1NAT2 protein, human

Identifiers

PMID30222709
PMCPMC6208141
OpenAlexW2895469189

What OpenQuestion 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 OpenQuestion graph.