Evidence map›Paper›PMID 27427355›Full record

ArticleScientific reports2016

Two fatty acyl reductases involved in moth pheromone biosynthesis.

Binu Antony, Bao-Jian Ding, Ken'Ichi Moto, Saleh A Aldosari, Abdulrahman S Aldawood

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
3.6field-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

13 citing papers in PubMed, 50 citations in OpenAlex.

  1. Fatty Acid Origin of Insect Pheromones.Advances in experimental medicine and biology · 2026
    Review
  2. Article
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  11. Transcriptome Analysis ofFrontiers in endocrinology · 2021
    Article
  12. Production of Long Chain Fatty Alcohols Found in Bumblebee Pheromones byFrontiers in bioengineering and biotechnology · 2020
    Article
  13. 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

5 authors at 3 institutions in 3 countries.

Binu AntonyKing Saud University, Department of Plant Protection, Chair of Date Palm Research, College of Food and Agricultural Sciences, Riyadh 11451, Saudi Arabia.
Bao-Jian DingLund University, Department of Biology, Lund 22362, Sweden.
Ken'Ichi MotoRIKEN, Lipid Biology Laboratory, Wako, Saitama 351-0198, Japan.
Saleh A AldosariKing Saud University, Department of Plant Protection, Chair of Date Palm Research, College of Food and Agricultural Sciences, Riyadh 11451, Saudi Arabia.
Abdulrahman S AldawoodKing Saud University, Department of Plant Protection, Chair of Date Palm Research, College of Food and Agricultural Sciences, Riyadh 11451, Saudi Arabia.
King Saud University · SALund University · SERIKEN · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Fatty acyl reductases (FARs) constitute an evolutionarily conserved gene family found in all kingdoms of life. Members of the FAR gene family play diverse roles, including seed oil synthesis, insect pheromone biosynthesis, and mammalian wax biosynthesis. In insects, FAR genes dedicated to sex pheromone biosynthesis (pheromone-gland-specific fatty acyl reductase, pgFAR) form a unique clade that exhibits substantial modifications in gene structure and possesses unique specificity and selectivity for fatty acyl substrates. Highly selective and semi-selective 'single pgFARs' produce single and multicomponent pheromone signals in bombycid, pyralid, yponomeutid and noctuid moths. An intriguing question is how a 'single reductase' can direct the synthesis of several fatty alcohols of various chain lengths and isomeric forms. Here, we report two active pgFARs in the pheromone gland of Spodoptera, namely a semi-selective, C14:acyl-specific pgFAR and a highly selective, C16:acyl-specific pgFAR, and demonstrate that these pgFARs play a pivotal role in the formation of species-specific signals, a finding that is strongly supported by functional gene expression data. The study envisages a new area of research for disclosing evolutionary changes associated with C14- and C16-specific FARs in moth pheromone biosynthesis.

Indexed as

Aldehyde OxidoreductasesAmino Acid SequenceAnimalsAnimal StructuresBiological AssayBiosynthetic PathwaysCloning, MolecularFatty AcidsFatty AlcoholsGas Chromatography-Mass SpectrometryInsect ProteinsLikelihood FunctionsMothsOrgan SpecificityPhylogenyReal-Time Polymerase Chain ReactionAldehyde OxidoreductasesFatty AcidsFatty AlcoholsInsect ProteinsSex Attractants

Identifiers

PMID27427355
PMCPMC4947906
OpenAlexW2490769227

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.