Evidence map›Paper›PMID 24306783›Full record

ArticleJournal of chemical ecology1986

Binding and hydrolysis of radiolabeled pheromone and several analogs by male-specific antennal proteins of the mothAntheraea polyphemus.

G D Prestwich, R G Vogt, L M Riddiford

Abstract read
PubMed Publisher
In one paragraph

Article in Journal of chemical ecology, 1986. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
9.2field-weighted citation impact, top 2% 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

9 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. 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

3 authors at 2 institutions in 1 country.

G D PrestwichDepartment of Chemistry, State University of New York, 11794-3400, Stony Brook, New York.
R G Vogt
L M Riddiford
University of Washington · USStony Brook University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Sensory hair proteins from antennae of males of the wild silk moth,Antheraea polyphemus (Lepidoptera, Saturniidae) were incubated with radiolabeled 6E,11Z-hexadecadienyl acetate in the presence of unlabeled pheromone analogs as competitive inhibitors. The two extracellular proteins of importance, a highly active sensillar esterase and an abundant 15,000 mol wt binding protein, interact to degrade labeled pheromone less efficiently in the presence of certain unsaturated acetate analogs of the natural pheromone.Enzymatic hydrolysis of the acetate (or diazoacetate) was also examined for three pheromone analogs: [11,12-(3)H2]-6E,11Z-hexadecadienyl diazoacetate, [11,12-(3)H2]-hexadecyl acetate, and [9,10-(3)H2]-9Z-tetradecenyl acetate. The former two are poor substrates at concentrations over four orders of magnitude. The 9Z-14:Ac, however, is the best alternative substrate for this in vitro pheromone metabolism system. Unlabeled 9Z-14: Ac is also the best competitive inhibitor of the hydrolysis of labeled 6E, 11Z-16: Ac. Whereas the tritiated natural pheromone shows a flat response (ca. 40% conversion) to increasing concentrations from 3 × 10(-9) to 3 × 10(-6) M, tritiated 9Z-14: Ac is degraded more rapidly at higher concentrations.

Identifiers

PMID24306783
OpenAlexW1981265274

What OpenQuestion holds

Textmetadata
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.