Evidence map›Paper›PMID 23894621›Full record

ArticlePloS one2013

A conserved aspartic acid is important for agonist (VUAA1) and odorant/tuning receptor-dependent activation of the insect odorant co-receptor (Orco).

Brijesh N Kumar, Robert W Taylor, Gregory M Pask, Laurence J Zwiebel, Richard D Newcomb, David L Christie

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.1field-weighted citation impact, top 14% 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

20 citing papers in PubMed, 42 citations in OpenAlex.

  1. Article
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  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. The Two Main Olfactory Receptor Families inFrontiers in cellular neuroscience · 2018
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Peripheral olfactory signaling in insects.Current opinion in insect science · 2014
    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

6 authors at 3 institutions in 2 countries.

Brijesh N KumarSchool of Biological Sciences, University of Auckland, Auckland, New Zealand.
Robert W Taylor
Gregory M Pask
Laurence J Zwiebel
Richard D Newcomb
David L Christie
Vanderbilt University · USUniversity of Auckland · NZPlant & Food Research · NZ

Funding

Examination of Odorant Receptors in Vector MosquitoesR01AI056402 · NIAID · VANDERBILT UNIVERSITY · PI ZWIEBEL, LAURENCE J · 2003 to 2013
$4.0M
Examination of the Molecular Mechanisms of Mosquito Odorant ReceptorsF31DC011989 · NIDCD · VANDERBILT UNIVERSITY · PI PASK, GREGORY M · 2011 to 2012
$44k
NIAID NIH HHS AI056402NIAID NIH HHS R01 AI056402NIDCD NIH HHS DC011989NIDCD NIH HHS F31 DC011989Wellcome Trust 096919
6 · The paper itself

Abstract

Insect odorant receptors function as heteromeric odorant-gated cation channels comprising a conventional odorant-sensitive tuning receptor, and a conserved co-receptor (Orco). An Orco agonist, VUAA1, is able to activate both heteromeric and homomeric Orco-containing channels. Very little is known about specific residues in Orco that contribute to cation permeability and gating. We investigated the importance of two conserved Asp residues, one in each of transmembrane domains 5 and 7, for channel function by mutagenesis. Drosophila melanogaster Orco and its substitution mutants were expressed in HEK cells and VUAA1-stimulated channel activity was determined by Ca(2+) influx and whole-cell patch clamp electrophysiology. Substitution of D466 in transmembrane 7 with amino acids other than glutamic acid resulted in a substantial reduction in channel activity. The D466E Orco substitution mutant was ~2 times more sensitive to VUAA1. The permeability of the D466E Orco mutant to cations was unchanged relative to wild-type Orco. When D466E Orco is co-expressed with a conventional tuning odorant receptor, the heteromeric complex also shows increased sensitivity to an odorant. Thus, the effect of the D466E mutation is not specific to VUAA1 agonism or dependent on homomeric Orco assembly. We suggest the gain-of-activation characteristic of the D466E mutant identifies an amino acid that is likely to be important for activation of both heteromeric and homomeric insect odorant receptor channels.

Indexed as

Amino Acid SubstitutionAnimalsAnophelesDrosophila melanogasterDrosophila ProteinsInsect ProteinsMutagenesisProtein Structure, TertiaryReceptors, OdorantThioglycolatesTriazolesDrosophila ProteinsInsect ProteinsN-(4-ethylphenyl)-2-((4-ethyl-5-(3-pyridinyl)-4H-1,2,4-triazol-3-yl)thio)acetamideOR22a protein, DrosophilaReceptors, OdorantThioglycolatesTriazoles

Identifiers

PMID23894621
PMCPMC3720905
OpenAlexW2041082630

What OpenQuestion holds

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Registered trials

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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.