ArticleInsect biochemistry and molecular biology2011
Identification and characterization of two arylalkylamine N-acetyltransferases in the yellow fever mosquito, Aedes aegypti.
Article in Insect biochemistry and molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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.
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.
Who cites it
18 citing papers in PubMed, 44 citations in OpenAlex.
- A Testis-Specific Aralkylamine N-Acetyltransferase Regulates Dimorphic Sperm Function and Male Fertility in Moths.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Decoding color variation: genome-wide characterization and expression analysis of pigment pathways in Neocaridina denticulata.BMC genomics · 2026Article
- Backbone resonance assignments of dopamine N-acetyltransferase in free and cofactor-bound states.Biomolecular NMR assignments · 2025Article
- AANAT1 regulates insect midgut detoxification through the ROS/CncC pathway.Communications biology · 2024Article
- Functional Characterization of ArylalkylamineAntioxidants (Basel, Switzerland) · 2022Article
- Melatonin biosynthesis pathways in nature and its production in engineered microorganisms.Synthetic and systems biotechnology · 2022Review
- Identification of catalytically distinct arylalkylamine N-acetyltransferase splicoforms from Tribolium castaneum.Protein expression and purification · 2020Article
- An essential role of acetyl coenzyme A in the catalytic cycle of insect arylalkylamine N-acetyltransferase.Communications biology · 2020Article
- Three Melanin Pathway Genes,International journal of molecular sciences · 2019Article
- Identification of aaNAT5b as a spermine N-acetyltransferase in the mosquito, Aedes aegypti.PloS one · 2018Article
- Insect ArylalkylamineFrontiers in molecular biosciences · 2018Review
- Critical Analysis of the Melanogenic Pathway in Insects and Higher Animals.International journal of molecular sciences · 2016Review
- Article
- Probing the chemical mechanism and critical regulatory amino acid residues of Drosophila melanogaster arylalkylamine N-acyltransferase like 2.Insect biochemistry and molecular biology · 2015Article
- Aspartate Decarboxylase is Required for a Normal Pupa Pigmentation Pattern in the Silkworm, Bombyx mori.Scientific reports · 2015Article
- Structures and functions of insect arylalkylamine N-acetyltransferase (iaaNAT); a key enzyme for physiological and behavioral switch in arthropods.Frontiers in physiology · 2015Article
- Evolution of insect arylalkylamine N-acetyltransferases: structural evidence from the yellow fever mosquito, Aedes aegypti.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- A visible dominant marker for insect transgenesis.Nature communications · 2012Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
In this study we provide a molecular and biochemical identification of two arylalkylamine N-acetyltransferases (aaNAT) from Aedes aegypti mosquitoes. N-acetyldopamine, the enzyme product of aaNAT, was detected in Ae. aegypti, indicating the presence of an aaNAT in this mosquito. A BLAST search of the Ae. aegypti genome, using sequence information from an activity-verified Drosophila aaNAT, identified thirteen putative aaNAT sequences sharing 13-48% sequence identity with the Drosophila enzyme. Eight of the thirteen putative aaNAT proteins were expressed using a bacterial expression system. Screening of purified recombinant proteins against 5-hydroxytryptamine, dopamine, methoxytryptamine, norepinephrine, octopamine, tryptamine, and tyramine substrates, established that two of the putative aaNATs are active to the tested arylalkylamines. We therefore named them aaNAT1 and 2, respectively. Analysis of the transcriptional profiles of the two aaNAT genes from Ae. aegypti revealed that aaNAT1 is more abundant in the whole body of larvae and pupae, and aaNAT2 is more abundant in the head of adult mosquitoes. Based on their substrate and transcriptional profiles, together with previous reports from other insects, we suggest that the two aaNATs play diverse roles in Ae. aegypti, with aaNAT1 primarily involved in sclerotization and aaNAT2 mainly in neurotransmitter inactivation. Our data provide a beginning to a more comprehensive understanding of the biochemistry and physiology of aaNATs from the Ae. aegypti and serve as a reference for studying the aaNAT family of proteins from other insect species.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.