Evidence map›Paper›PMID 28393888›Full record

ArticleScientific reports2017

Molecular basis for the behavioral effects of the odorant degrading enzyme Esterase 6 in Drosophila.

Faisal Younus, Nicholas J Fraser, Chris W Coppin, Jian-Wei Liu, Galen J Correy, Thomas Chertemps, Gunjan Pandey, Martine Maïbèche, Colin J Jackson, John G Oakeshott

Abstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing 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

21 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Olfactory coding in honeybees.Cell and tissue research · 2021
    Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Genomics Analysis of L-DOPA Exposure inG3 (Bethesda, Md.) · 2019
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

10 authors.

Faisal YounusCSIRO Land and Water, Black Mountain, Canberra, ACT, 2601, Australia.
Nicholas J FraserResearch School of Chemistry, Australian National University, Canberra, ACT, 2601, Australia.
Chris W CoppinCSIRO Land and Water, Black Mountain, Canberra, ACT, 2601, Australia.
Jian-Wei LiuCSIRO Land and Water, Black Mountain, Canberra, ACT, 2601, Australia.
Galen J CorreyResearch School of Chemistry, Australian National University, Canberra, ACT, 2601, Australia.
Thomas ChertempsUniversité Pierre et Marie Curie, Institut d'Ecologie et des Sciences de l'Environnement de Paris, 75252, Paris, France.
Gunjan PandeyCSIRO Land and Water, Black Mountain, Canberra, ACT, 2601, Australia.
Martine MaïbècheUniversité Pierre et Marie Curie, Institut d'Ecologie et des Sciences de l'Environnement de Paris, 75252, Paris, France.
Colin J JacksonResearch School of Chemistry, Australian National University, Canberra, ACT, 2601, Australia.
John G OakeshottCSIRO Land and Water, Black Mountain, Canberra, ACT, 2601, Australia.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Previous electrophysiological and behavioural studies implicate esterase 6 in the processing of the pheromone cis-vaccenyl acetate and various food odorants that affect aggregation and reproductive behaviours. Here we show esterase 6 has relatively high activity against many of the short-mid chain food esters, but negligible activity against cis-vaccenyl acetate. The crystal structure of esterase 6 confirms its substrate-binding site can accommodate many short-mid chain food esters but not cis-vaccenyl acetate. Immunohistochemical assays show esterase 6 is expressed in non-neuronal cells in the third antennal segment that could be accessory or epidermal cells surrounding numerous olfactory sensilla, including basiconics involved in food odorant detection. Esterase 6 is also produced in trichoid sensilla, but not in the same cell types as the cis-vaccenyl acetate binding protein LUSH. Our data support a model in which esterase 6 acts as a direct odorant degrading enzyme for many bioactive food esters, but not cis-vaccenyl acetate.

Indexed as

OdorantsAnimalsArthropod AntennaeBehavior, AnimalCarboxylesteraseCatalytic DomainDrosophila melanogasterDrosophila ProteinsKineticsModels, MolecularReceptors, OdorantStructural Homology, ProteinSubstrate SpecificityCarboxylesteraseDrosophila ProteinsEst-6 protein, DrosophilaOrco protein, DrosophilaReceptors, Odorant

Identifiers

PMID28393888
PMCPMC5385555

What OpenQuestion holds

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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.