Evidence map›Paper›PMID 39934620›Full record

ArticleBiomolecular NMR assignments2025

Backbone resonance assignments of dopamine N-acetyltransferase in free and cofactor-bound states.

Chu-Ya Wu, Yi-Zong Lee, I-Chen Hu, Liang-Yuan Chiu, Wei-Cheng Ding, Jing Wang, Shih-Che Sue, Shin-Ichi Tate, Ping-Chiang Lyu

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Biomolecular NMR assignments, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
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

1 citing paper in PubMed.

  1. 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

9 authors.

Chu-Ya WuInstitute of Bioinformatics and Structural Biology, National Tsing Hua University, No. 101, Section 2, Kuang-Fu Road, Hsinchu, 300044, Taiwan.
Yi-Zong LeeInstitute of Bioinformatics and Structural Biology, National Tsing Hua University, No. 101, Section 2, Kuang-Fu Road, Hsinchu, 300044, Taiwan.
I-Chen HuInstitute of Bioinformatics and Structural Biology, National Tsing Hua University, No. 101, Section 2, Kuang-Fu Road, Hsinchu, 300044, Taiwan.
Liang-Yuan ChiuInstitute of Bioinformatics and Structural Biology, National Tsing Hua University, No. 101, Section 2, Kuang-Fu Road, Hsinchu, 300044, Taiwan.
Wei-Cheng DingInstitute of Bioinformatics and Structural Biology, National Tsing Hua University, No. 101, Section 2, Kuang-Fu Road, Hsinchu, 300044, Taiwan.
Jing WangDepartment of Mathematical and Life Sciences, Graduate School of Integrated Sciences for Life, Hiroshima University, 1-3-1 Kagamiyama, Higashi-Hiroshima, Hiroshima, 739-8526, Japan.
Shih-Che SueInstitute of Bioinformatics and Structural Biology, National Tsing Hua University, No. 101, Section 2, Kuang-Fu Road, Hsinchu, 300044, Taiwan.
Shin-Ichi TateDepartment of Mathematical and Life Sciences, Graduate School of Integrated Sciences for Life, Hiroshima University, 1-3-1 Kagamiyama, Higashi-Hiroshima, Hiroshima, 739-8526, Japan.
Ping-Chiang LyuInstitute of Bioinformatics and Structural Biology, National Tsing Hua University, No. 101, Section 2, Kuang-Fu Road, Hsinchu, 300044, Taiwan. pclyu@mx.nthu.edu.tw.

Funding

National Science and Technology Council 106-2311-B-007-004-MY3
6 · The paper itself

Abstract

Dopamine N-acetyltransferase (Dat), belonging to the GCN5-related N-acetyltransferase (GNAT) superfamily, is an arylalkylamine N-acetyltransferase (AANAT) that is involved in insects neurotransmitter inactivation and the development of insect cuticle sclerotization. By using the cofactor acetyl coenzyme A (Ac-CoA) as an acetyl group donor, Dat produces acetyl-dopamine through the reaction with dopamine. Although AANATs share similar structural features with the GNAT family, they have low sequence identities among insect AANATs (~ 40%) and between insect AANATs and vertebrate AANATs (~ 12%). A common noticed feature in GNATs is the Ac-CoA-binding induced conformational change, and this is important for further selection and catalysis of its substrate. In AANATs, the conformational changes help the sequential binding mechanism. Here, we report the

Indexed as

Acetyl Coenzyme AArylalkylamine N-AcetyltransferaseDrosophila melanogasterNuclear Magnetic Resonance, BiomolecularAnimalsProtein BindingAcetyl Coenzyme AArylalkylamine N-AcetyltransferaseAANATArylalkylamineDopamine N-acetyltransferase (Dat)GNATN-acetyltransferaseNMR

Identifiers

PMID39934620
PMCPMC12116598

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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.