Evidence map›Paper›PMID 17909564›Full record

ArticleThe pharmacogenomics journal2008

Functional effects of single nucleotide polymorphisms in the coding region of human N-acetyltransferase 1.

Y Zhu, D W Hein

Open access · greenAbstract read
In one paragraph

Article in The pharmacogenomics journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.3field-weighted citation impact, top 21% 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

20 citing papers in PubMed, 46 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Acetyl coenzyme A kinetic studies onFrontiers in pharmacology · 2022
    Article
  6. HumanFrontiers in pharmacology · 2022
    Article
  7. Article
  8. Case Study 10: A Case to Investigate Acetyl Transferase Kinetics.Methods in molecular biology (Clifton, N.J.) · 2021
    Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. 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
  18. Review
  19. Meat intake, heterocyclic amine exposure, and metabolizing enzyme polymorphisms in relation to colorectal polyp risk.Cancer epidemiology, biomarkers & prevention : a publication of the American Association for Cancer Research, cosponsored by the American Society of Preventive Oncology · 2008
    Article
  20. 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

2 authors at 1 institution in 1 country.

Y ZhuDepartment of Pharmacology and Toxicology and James Graham Brown Cancer Center, University of Louisville School of Medicine, Louisville, KY 40292, USA.
D W Hein
University of Louisville · US

Funding

PHARMACOGENETICS OF DRUG &CARCINOGEN METABOLISMR01CA034627 · NCI · UNIVERSITY OF NORTH DAKOTA · PI HEIN, DAVID W · 1985 to 2009
$3.1M
NCI NIH HHS CA-34627NCI NIH HHS R01 CA034627
6 · The paper itself

Abstract

Genetic variants of human N-acetyltransferase 1 (NAT1) are associated with cancer and birth defects. N- and O-acetyltransferase catalytic activities, Michaelis-Menten kinetic constants (K(m) and V(max)) and steady-state expression levels of NAT1-specific mRNA and protein were determined for the reference NAT1*4 and variant human NAT1 haplotypes possessing single nucleotide polymorphisms (SNPs) in the open reading frame. Although none of the SNPs caused a significant effect on steady-state levels of NAT1-specific mRNA, C97T(R33stop), C190T(R64W), C559T (R187stop) and A752T(D251V) each reduced NAT1 protein level and/or N- and O-acetyltransferase catalytic activities to levels below detection. G560A(R187Q) substantially reduced NAT1 protein level and catalytic activities and increased substrate K(m). The G445A(V149I), G459A(synonymous) and T640G(S214A) haplotype present in NAT1*11 significantly (P<0.05) increased NAT1 protein level and catalytic activity. Neither T21G(synonymous), T402C(synonymous), A613G(M205V), T777C(synonymous), G781A(E261K) nor A787G(I263V) significantly affected K(m), catalytic activity, mRNA or protein level. These results suggest heterogeneity among slow NAT1 acetylator phenotypes.

Indexed as

Polymorphism, Single NucleotideAcetylationAmino Acid SubstitutionArylamine N-AcetyltransferaseBiocatalysisHaplotypesHumansIsoenzymesKineticsRNA, MessengerArylamine N-AcetyltransferaseIsoenzymesN-acetyltransferase 1RNA, Messenger

Identifiers

PMID17909564
PMCPMC2575040
OpenAlexW2058372101

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.