Evidence map›Paper›PMID 36656070›Full record

ReviewAnnals of botany2023

Caleosin/peroxygenases: multifunctional proteins in plants.

Abdulsamie Hanano, Elizabeth Blée, Denis J Murphy

Open access · bronzeAbstract readReview
In one paragraph

Review in Annals of botany, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
6.4field-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

16 citing papers in PubMed, 35 citations in OpenAlex.

  1. Review
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  4. Review
  5. Article
  6. Article
  7. Characterization ofPlants (Basel, Switzerland) · 2025
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Molecular Machinery of Lipid Droplet Degradation and Turnover in Plants.International journal of molecular sciences · 2023
    Review
  16. Review
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 3 institutions in 3 countries.

Abdulsamie HananoDepartment of Molecular Biology and Biotechnology, Atomic Energy Commission of Syria (AECS), Damascus, Syria.ORCID 0000-0002-1699-106X
Elizabeth BléeFormer Head of Phyto-oxylipins laboratory, Institute of Plant Molecular Biology, University of Strasbourg, France.
Denis J MurphySchool of Applied Sciences, University of South Wales, Treforest, UK.ORCID 0000-0002-5291-2445
Atomic Energy Commission of Syria · SYUniversité de Strasbourg · FRUniversity of South Wales · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundCaleosin/peroxygenases (CLO/PXGs) are a family of multifunctional proteins that are ubiquitous in land plants and are also found in some fungi and green algae. CLO/PXGs were initially described as a class of plant lipid-associated proteins with some similarities to the oleosins that stabilize lipid droplets (LDs) in storage tissues, such as seeds. However, we now know that CLO/PXGs have more complex structures, distributions and functions than oleosins. Structurally, CLO/PXGs share conserved domains that confer specific biochemical features, and they have diverse localizations and functions. SCOPE: This review surveys the structural properties of CLO/PXGs and their biochemical roles. In addition to their highly conserved structures, CLO/PXGs have peroxygenase activities and are involved in several aspects of oxylipin metabolism in plants. The enzymatic activities and the spatiotemporal expression of CLO/PXGs are described and linked with their wider involvement in plant physiology. Plant CLO/PXGs have many roles in both biotic and abiotic stress responses in plants and in their responses to environmental toxins. Finally, some intriguing developments in the biotechnological uses of CLO/PXGs are addressed.

conclusionsIt is now two decades since CLO/PXGs were first recognized as a new class of lipid-associated proteins and only 15 years since their additional enzymatic functions as a new class of peroxygenases were discovered. There are many interesting research questions that remain to be addressed in future physiological studies of plant CLO/PXGs and in their recently discovered roles in the sequestration and, possibly, detoxification of a wide variety of lipidic xenobiotics that can challenge plant welfare.

Indexed as

Plant ProteinsPlantsCalcium-Binding ProteinsLipidsMixed Function OxygenasesCalcium-Binding Proteinscaleosin protein, Sesamum indicumLipidsMixed Function OxygenasesperoxygenasePlant ProteinsCaleosinlipid dropletsoxylipinsperoxygenaseplant lipidsstress responses

Identifiers

PMID36656070
PMCPMC10072107
OpenAlexW4317481251

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.