Evidence map›Paper›PMID 17591675›Full record

ArticleDrug metabolism and disposition: the biological fate of chemicals2007

Functional analysis of the human N-acetyltransferase 1 major promoter: quantitation of tissue expression and identification of critical sequence elements.

Anwar Husain, Xiaoyan Zhang, Mark A Doll, J Christopher States, David F Barker, David W Hein

Open access · greenAbstract read
In one paragraph

Article in Drug metabolism and disposition: the biological fate of chemicals, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

22 citing papers in PubMed, 51 citations in OpenAlex.

  1. Article
  2. Human ArylamineFrontiers in pharmacology · 2021
    Article
  3. Case Study 10: A Case to Investigate Acetyl Transferase Kinetics.Methods in molecular biology (Clifton, N.J.) · 2021
    Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Functional effects of genetic polymorphisms in the N-acetyltransferase 1 coding and 3' untranslated regions.Birth defects research. Part A, Clinical and molecular teratology · 2011
    Article
  17. Review
  18. Article
  19. Article
  20. Systemic functional expression of N-acetyltransferase polymorphism in the F344 Nat2 congenic rat.Drug metabolism and disposition: the biological fate of chemicals · 2008
    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

6 authors at 1 institution in 1 country.

Anwar HusainDepartment of Pharmacology and Toxicology, James Graham Brown Cancer Center, University of Louisville School of Medicine, Louisville, KY 40292, USA.
Xiaoyan Zhang
Mark A Doll
J Christopher States
David F Barker
David W Hein
University of Louisville Hospital · US

Funding

PHARMACOGENETICS OF DRUG &CARCINOGEN METABOLISMR01CA034627 · NCI · UNIVERSITY OF NORTH DAKOTA · PI HEIN, DAVID W · 1985 to 2009
$3.1M
Genetic polymorphisms in 5'-UTR of human NAT1 and NAT2F30ES012557 · NIEHS · UNIVERSITY OF LOUISVILLE · PI HUSAIN, ANWAR · 2003 to 2006
$143k
NCI NIH HHS CA34627NCI NIH HHS R01 CA034627NIEHS NIH HHS ES12557NIEHS NIH HHS F30 ES012557
6 · The paper itself

Abstract

Arylamine N-acetyltransferase 1 (NAT1) plays an important role in the biotransformation of xenobiotics, and genetic variants have been implicated in susceptibility to cancer and birth defects. A specific and quantitative reverse transcription-polymerase chain reaction assay for transcription from the major NAT1 promoter detected high expression with limited variability in human tissues. A 213-base pair (bp) minimal promoter was identified by transfection of luciferase reporter constructs into MCF-7 and HepG2 cell lines. Alignment of the 213-bp region with paralogous and orthologous promoters revealed two conserved region segments, one of which overlaps a 16-bp perfect palindrome. Transfection of luciferase constructs with artificial mutations in the minimal promoter defined two sites important for promoter function. One of these sites included a close match to the Sp1 transcription factor binding consensus sequence. Electrophoretic mobility shift assays (EMSAs), followed by competitive and supershift analyses, confirmed the Sp1 binding. Mutation of the highly conserved portion of the 16-bp palindrome reduced promoter activity more than 3-fold, and an EMSA shift was detected with an oligonucleotide, 200L29, which spans this segment. The 200L29 EMSA shift could not be competed by consensus Sp1 or AP-2 oligonucleotides, and may represent binding of a transcription factor that is common to N-acetyltransferase genes in humans and other species.

Indexed as

AnimalsArylamine N-AcetyltransferaseBase SequenceCattleCloning, MolecularDatabases, GeneticElectrophoretic Mobility Shift AssayExonsGene Expression Regulation, EnzymologicHumansIsoenzymesMiceMolecular Sequence DataMutationPromoter Regions, GeneticRatsArylamine N-AcetyltransferaseIsoenzymesN-acetyltransferase 1RNATranscription Factors

Identifiers

PMID17591675
PMCPMC2085369
OpenAlexW2096358451

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.