Evidence map›Paper›PMID 22045812›Full record

ArticleThe Journal of biological chemistry2012

Identification of a new fatty acid synthesis-transport machinery at the peroxisomal membrane.

Merle Hillebrand, Søren W Gersting, Amelie S Lotz-Havla, Annika Schäfer, Hendrik Rosewich, Oliver Valerius, Ania C Muntau, Jutta Gärtner

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
0.7field-weighted citation impact, top 31% 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

21 citing papers in PubMed, 38 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Peroxisomal ABC Transporters: An Update.International journal of molecular sciences · 2021
    Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Fatty Acid Synthase: An Emerging Target in Cancer.Molecules (Basel, Switzerland) · 2020
    Review
  11. Article
  12. Article
  13. Review
  14. Review
  15. Article
  16. Article
  17. Review
  18. Article
  19. Review
  20. 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

8 authors at 2 institutions in 1 country.

Merle HillebrandDepartment of Pediatrics and Pediatric Neurology, Faculty of Medicine, Georg August University, 37075 Göttingen, Germany.
Søren W GerstingDepartment of Molecular Pediatrics, Dr. von Hauner Children's Hospital, Ludwig Maximilians University, 80337 Munich, Germany.
Amelie S Lotz-HavlaDepartment of Molecular Pediatrics, Dr. von Hauner Children's Hospital, Ludwig Maximilians University, 80337 Munich, Germany.
Annika SchäferDepartment of Dermatology, Venereology, and Allergology, Faculty of Medicine Georg August University, 37075 Göttingen, Germany.
Hendrik RosewichDepartment of Pediatrics and Pediatric Neurology, Faculty of Medicine, Georg August University, 37075 Göttingen, Germany.
Oliver ValeriusInstitute of Microbiology and Genetics, Department of Molecular Microbiology and Genetics, Georg August University, 37077 Göttingen, Germany.
Ania C MuntauDepartment of Molecular Pediatrics, Dr. von Hauner Children's Hospital, Ludwig Maximilians University, 80337 Munich, Germany.
Jutta GärtnerDepartment of Pediatrics and Pediatric Neurology, Faculty of Medicine, Georg August University, 37075 Göttingen, Germany. Electronic address: gaertnj@med.uni-goettingen.de.
University of Göttingen · DELudwig-Maximilians-Universität München · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The neurodegenerative disease X-linked adrenoleukodystrophy (X-ALD) is characterized by the abnormal accumulation of very long chain fatty acids. Mutations in the gene encoding the peroxisomal ATP-binding cassette half-transporter, adrenoleukodystrophy protein (ALDP), are the primary cause of X-ALD. To gain a better understanding of ALDP dysfunction, we searched for interaction partners of ALDP and identified binary interactions to proteins with functions in fatty acid synthesis (ACLY, FASN, and ACC) and activation (FATP4), constituting a thus far unknown fatty acid synthesis-transport machinery at the cytoplasmic side of the peroxisomal membrane. This machinery adds to the knowledge of the complex mechanisms of peroxisomal fatty acid metabolism at a molecular level and elucidates potential epigenetic mechanisms as regulatory processes in the pathogenesis and thus the clinical course of X-ALD.

Indexed as

Acetyl-CoA CarboxylaseAdrenoleukodystrophyATP-Binding Cassette TransportersATP Binding Cassette Transporter, Subfamily D, Member 1Biological TransportFatty AcidsFatty Acid SynthasesFatty Acid Transport ProteinsFluorescence Resonance Energy TransferHeLa CellsHumansImmunoprecipitationIntracellular MembranesPeroxisomesSpectrum AnalysisABCD1 protein, humanABCD3 protein, humanAcetyl-CoA CarboxylaseATP-Binding Cassette TransportersATP Binding Cassette Transporter, Subfamily D, Member 1Fatty AcidsFatty Acid SynthasesFatty Acid Transport Proteins

Identifiers

PMID22045812
PMCPMC3249072
OpenAlexW2049230832

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.