Evidence map›Paper›PMID 11154338›Full record

ArticlePlant physiology2001

Tomato allene oxide synthase and fatty acid hydroperoxide lyase, two cytochrome P450s involved in oxylipin metabolism, are targeted to different membranes of chloroplast envelope.

J E Froehlich, A Itoh, G A Howe

Open access · bronzeAbstract read
In one paragraph

Article in Plant physiology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.

0numbers the graph read from it
0cells of the map it votes in
66citing papers in PubMed
5.9field-weighted citation impact, top 3% 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

66 citing papers in PubMed, 234 citations in OpenAlex.

  1. Article
  2. The GhWRKY70-International journal of molecular sciences · 2026
    Article
  3. Understanding the role of oxylipins inFrontiers in plant science · 2025
    Review
  4. Cytochromes P450 evolution in the plant terrestrialization context.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2024
    Review
  5. Article
  6. Review
  7. Epoxyalcohol Synthase Branch of Lipoxygenase Cascade.Current issues in molecular biology · 2024
    Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Review
  13. Head-Group Acylation of Chloroplast Membrane Lipids.Molecules (Basel, Switzerland) · 2021
    Review
  14. Article
  15. Expression ofFrontiers in plant science · 2021
    Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article

6 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

3 authors at 1 institution in 1 country.

J E FroehlichDepartment of Energy-Plant Research Laboratory, Michigan State University, East Lansing, Michigan 48824, USA.
A Itoh
G A Howe
Michigan State University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Allene oxide synthase (AOS) and hydroperoxide lyase (HPL) are related cytochrome P450s that metabolize a common fatty acid hydroperoxide substrate to different classes of bioactive oxylipins within chloroplasts. Here, we report the use of in vitro import assays to investigate the targeting of tomato (Lycopersicon esculentum) AOS (LeAOS) and HPL (LeHPL) to isolated chloroplasts. LeAOS, which contains a typical N-terminal transit peptide, was targeted to the inner envelope membrane by a route that requires both ATP and proteinase-sensitive components on the surface of chloroplasts. Imported LeAOS was peripherally associated with the inner envelope; the bulk of the protein facing the stroma. LeHPL, which lacks a typical chloroplast-targeting sequence, was targeted to the outer envelope by an ATP-independent and protease-insensitive pathway. Imported LeHPL was integrated into the outer envelope with most of the protein exposed to the inter-membrane space. We conclude that LeAOS and LeHPL are routed to different envelope membranes by distinct targeting pathways. Partitioning of AOS and HPL to different envelope membranes suggests differences in the spatial organization of these two branches of oxylipin metabolism.

Indexed as

Aldehyde-LyasesAmino Acid SequenceBase SequenceChloroplastsCytochrome P-450 Enzyme SystemDNA PrimersIntracellular MembranesIntramolecular OxidoreductasesMolecular Sequence DataMutagenesis, Site-DirectedPisum sativumRecombinant ProteinsSequence AlignmentSequence Homology, Amino AcidSolanum lycopersicumAldehyde-LyasesCytochrome P-450 Enzyme SystemDNA Primershydroperoxide isomerasehydroperoxide lyaseIntramolecular OxidoreductasesRecombinant Proteins

Identifiers

PMID11154338
PMCPMC61011
OpenAlexW2100037274

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.