Evidence map›Paper›PMID 26517910›Full record

ReviewBiochemical Society transactions2015

Peroxisomal ABC transporters: functions and mechanism.

Alison Baker, David J Carrier, Theresia Schaedler, Hans R Waterham, Carlo W van Roermund, Frederica L Theodoulou

Open access · hybridAbstract readReview
In one paragraph

Review in Biochemical Society transactions, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
4.1field-weighted citation impact, top 5% 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

44 citing papers in PubMed, 88 citations in OpenAlex.

  1. Article
  2. Article
  3. Molecular mechanism of substrate transport by human peroxisomal ABCD3.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Peroxisomal ABC Transporters: An Update.International journal of molecular sciences · 2021
    Review
  19. Review
  20. The Pathophysiological Role of CoA.International journal of molecular sciences · 2020
    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

6 authors at 3 institutions in 2 countries.

Alison BakerCentre for Plant Sciences, School of Molecular and Cellular Biology, University of Leeds, Leeds LS2 9JT, U.K. A.baker@leeds.ac.uk.
David J CarrierCentre for Plant Sciences, School of Molecular and Cellular Biology, University of Leeds, Leeds LS2 9JT, U.K.
Theresia SchaedlerBiological Chemistry and Crop Protection Department, Rothamsted Research, Harpenden, AL5 2JQ, U.K.
Hans R WaterhamLaboratory of Genetic Metabolic Diseases, Departments of Pediatrics and Clinical Chemistry, Academic Medical Center, University of Amsterdam, 1105 AZ Amsterdam, The Netherlands.
Carlo W van RoermundLaboratory of Genetic Metabolic Diseases, Departments of Pediatrics and Clinical Chemistry, Academic Medical Center, University of Amsterdam, 1105 AZ Amsterdam, The Netherlands.
Frederica L Theodoulou
Amsterdam UMC Location University of Amsterdam · NLUniversity of Leeds · GBRothamsted Research · GB

Funding

Biotechnology and Biological Sciences Research Council BB/L001012/1Biotechnology and Biological Sciences Research Council BB/L001691/1
6 · The paper itself

Abstract

Peroxisomes are arguably the most biochemically versatile of all eukaryotic organelles. Their metabolic functions vary between different organisms, between different tissue types of the same organism and even between different developmental stages or in response to changed environmental conditions. New functions for peroxisomes are still being discovered and their importance is underscored by the severe phenotypes that can arise as a result of peroxisome dysfunction. The β-oxidation pathway is central to peroxisomal metabolism, but the substrates processed are very diverse, reflecting the diversity of peroxisomes across species. Substrates for β-oxidation enter peroxisomes via ATP-binding cassette (ABC) transporters of subfamily D; (ABCD) and are activated by specific acyl CoA synthetases for further metabolism. Humans have three peroxisomal ABCD family members, which are half transporters that homodimerize and have distinct but partially overlapping substrate specificity; Saccharomyces cerevisiae has two half transporters that heterodimerize and plants have a single peroxisomal ABC transporter that is a fused heterodimer and which appears to be the single entry point into peroxisomes for a very wide variety of β-oxidation substrates. Our studies suggest that the Arabidopsis peroxisomal ABC transporter AtABCD1 accepts acyl CoA substrates, cleaves them before or during transport followed by reactivation by peroxisomal synthetases. We propose that this is a general mechanism to provide specificity to this class of transporters and by which amphipathic compounds are moved across peroxisome membranes.

Indexed as

Arabidopsis ProteinsATP-Binding Cassette TransportersCoenzyme A LigasesFatty AcidsHumansModels, MolecularOxidation-ReductionPeroxisomesProtein ConformationSaccharomyces cerevisiae ProteinsArabidopsis ProteinsATP-Binding Cassette TransportersCoenzyme A LigasesFatty AcidsSaccharomyces cerevisiae Proteinsacyl-CoAasymmetryATP-binding cassette (ABC) transporterperoxisomethioesteraseβ-oxidation

Identifiers

PMID26517910
PMCPMC4652930
OpenAlexW2263338593

What OpenQuestion holds

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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.