Evidence map›Paper›PMID 18280460›Full record

ArticleBiochemical pharmacology2008

Mouse N-acetyltransferase type 2, the homologue of human N-acetyltransferase type 1.

Akane Kawamura, Isaac Westwood, Larissa Wakefield, Hilary Long, Naixia Zhang, Kylie Walters, Christina Redfield, Edith Sim

Open access · hybridAbstract readComparative Study
In one paragraph

Article in Biochemical pharmacology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

16 citing papers in PubMed, 45 citations in OpenAlex.

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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

8 authors at 2 institutions in 2 countries.

Akane KawamuraDepartment of Pharmacology, University of Oxford, Mansfield Road, Oxford OX1 3QT, United Kingdom.
Isaac Westwood
Larissa Wakefield
Hilary Long
Naixia Zhang
Kylie Walters
Christina Redfield
Edith Sim
University of Oxford · GBUniversity of Minnesota · US

Funding

Wellcome Trust 079440
6 · The paper itself

Abstract

There is increasing evidence that human arylamine N-acetyltransferase type 1 (NAT1, EC 2.3.1.5), although first identified as a homologue of a drug-metabolising enzyme, appears to be a marker in human oestrogen receptor positive breast cancer. Mouse Nat2 is the mouse equivalent of human NAT1. The development of mouse models of breast cancer is important, and it is essential to explore the biological role of mouse Nat2. We have therefore produced mouse Nat2 as a recombinant protein and have investigated its substrate specificity profile in comparison with human NAT1. In addition, we have tested the effects of inhibitors on mouse Nat2, including compounds which are endogenous and exogenous steroids. We show that tamoxifen, genistein and diethylstilbestrol inhibit mouse Nat2. The steroid analogue, bisphenol A, also inhibits mouse Nat2 enzymic activity and is shown by NMR spectroscopy, through shifts in proton peaks, to bind close to the active site. A three-dimensional structure for human NAT1 has recently been released, and we have used this crystal structure to generate a model of the mouse Nat2 structure. We propose that a conformational change in the structure is required in order for ligands to bind to the active site of the protein.

Indexed as

Sequence Homology, Amino AcidAnimalsArylamine N-AcetyltransferaseCells, CulturedCricetinaeHumansIsoenzymesMiceProtein Structure, TertiarySubstrate SpecificityArylamine N-AcetyltransferaseIsoenzymesN-acetyltransferase 1Nat2 enzyme, mouse

Identifiers

PMID18280460
PMCPMC2279149
OpenAlexW2069455052

What OpenQuestion holds

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LicenceCC BY
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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.