Evidence map›Paper›PMID 22927409›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2012

An insect-specific P450 oxidative decarbonylase for cuticular hydrocarbon biosynthesis.

Yue Qiu, Claus Tittiger, Claude Wicker-Thomas, Gaëlle Le Goff, Sharon Young, Eric Wajnberg, Thierry Fricaux, Nathalie Taquet, Gary J Blomquist, René Feyereisen

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 163 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
163citing papers in PubMed, 1 pooled it
–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

163 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Article
  3. Article
  4. Article
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  7. Article
  8. Article
  9. Complex Roles of Insect Cytochrome P450s in Chemical Adaptation.International journal of biological sciences · 2026
    Review
  10. Article
  11. Article
  12. Article
  13. Directed evolution of hydrocarbon-producing enzymes.Biotechnology for biofuels and bioproducts · 2025
    Review
  14. Article
  15. Article
  16. Article
  17. Via Air or Rhizosphere: The Phytotoxicity ofPlants (Basel, Switzerland) · 2025
    Review
  18. Article
  19. Review
  20. Article

103 more citing papers are in PubMed but not listed here.

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.

Yue QiuDepartment of Biochemistry and Molecular Biology, University of Nevada, Reno, NV 89557, USA.
Claus Tittiger
Claude Wicker-Thomas
Gaëlle Le Goff
Sharon Young
Eric Wajnberg
Thierry Fricaux
Nathalie Taquet
Gary J Blomquist
René Feyereisen

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Insects use hydrocarbons as cuticular waterproofing agents and as contact pheromones. Although their biosynthesis from fatty acyl precursors is well established, the last step of hydrocarbon biosynthesis from long-chain fatty aldehydes has remained mysterious. We show here that insects use a P450 enzyme of the CYP4G family to oxidatively produce hydrocarbons from aldehydes. Oenocyte-directed RNAi knock-down of Drosophila CYP4G1 or NADPH-cytochrome P450 reductase results in flies deficient in cuticular hydrocarbons, highly susceptible to desiccation, and with reduced viability upon adult emergence. The heterologously expressed enzyme converts C(18)-trideuterated octadecanal to C(17)-trideuterated heptadecane, showing that the insect enzyme is an oxidative decarbonylase that catalyzes the cleavage of long-chain aldehydes to hydrocarbons with the release of carbon dioxide. This process is unlike cyanobacteria that use a nonheme diiron decarbonylase to make alkanes from aldehydes with the release of formate. The unique and highly conserved insect CYP4G enzymes are a key evolutionary innovation that allowed their colonization of land.

Indexed as

AldehydesAnimalsAnimal ShellsBiosynthetic PathwaysCytochrome P-450 Enzyme SystemDrosophilaHydrocarbonsImmunohistochemistryMicroscopy, ConfocalMicrosomesMolecular StructureNADPH-Ferrihemoprotein ReductaseRNA InterferenceAldehydesCytochrome P-450 Enzyme SystemHydrocarbonsNADPH-Ferrihemoprotein Reductase

Identifiers

PMID22927409
PMCPMC3443174

What OpenQuestion holds

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Read underepoch 390

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.