Evidence map›Paper›PMID 32044385›Full record

ReviewBiochimica et biophysica acta. Molecular cell research2020

The diversity of ACBD proteins - From lipid binding to protein modulators and organelle tethers.

Markus Islinger, Joseph L Costello, Suzan Kors, Eric Soupene, Timothy P Levine, Frans A Kuypers, Michael Schrader

Open access · hybridAbstract readReview
In one paragraph

Review in Biochimica et biophysica acta. Molecular cell research, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

26 citing papers in PubMed, 53 citations in OpenAlex.

  1. Article
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  3. Article
  4. Review
  5. Article
  6. Review
  7. A Novel HomozygousMolecular syndromology · 2024
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
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  19. TSPO protein binding partners in bacteria, animals, and plants.Journal of bioenergetics and biomembranes · 2021
    Review
  20. Article
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

7 authors at 3 institutions in 2 countries.

Markus IslingerInstitute of Neuroanatomy, Medical Faculty Manheim, University of Heidelberg, 68167 Mannheim, Germany.
Joseph L CostelloCollege of Life and Environmental Sciences, Biosciences, University of Exeter, Exeter EX4 4QD, Devon, UK.
Suzan KorsCollege of Life and Environmental Sciences, Biosciences, University of Exeter, Exeter EX4 4QD, Devon, UK.
Eric SoupeneChildren's Hospital Oakland Research Institute, Oakland, CA 94609, USA.
Timothy P LevineUCL Institute of Ophthalmology, London EC1V 9EL, UK.
Frans A KuypersChildren's Hospital Oakland Research Institute, Oakland, CA 94609, USA.
Michael SchraderCollege of Life and Environmental Sciences, Biosciences, University of Exeter, Exeter EX4 4QD, Devon, UK. Electronic address: m.schrader@exeter.ac.uk.
University of Exeter · GBUniversity College London · GBUniversity Hospital Heidelberg · DE

Funding

Biotechnology and Biological Sciences Research Council BB/M011801/1Biotechnology and Biological Sciences Research Council BB/N01541X/1Biotechnology and Biological Sciences Research Council BB/P003818/1Biotechnology and Biological Sciences Research Council BB/T002255/1Medical Research Council CIC 08135Medical Research Council MR/N0137941/1Medical Research Council MR/T019409/1
6 · The paper itself

Abstract

Members of the large multigene family of acyl-CoA binding domain containing proteins (ACBDs) share a conserved motif required for binding of Coenzyme A esterified fatty acids of various chain length. These proteins are present in the three kingdoms of life, and despite their predicted roles in cellular lipid metabolism, knowledge about the precise functions of many ACBD proteins remains scarce. Interestingly, several ACBD proteins are now suggested to function at organelle contact sites, and are recognized as host interaction proteins for different pathogens including viruses and bacteria. Here, we present a thorough phylogenetic analysis of the ACBD family and discuss their structure and evolution. We summarize recent findings on the various functions of animal and fungal ACBDs with particular focus on peroxisomes, the role of ACBD proteins at organelle membranes, and their increasing recognition as targets for pathogens.

Indexed as

AnimalsCarrier ProteinsEvolution, MolecularFungal ProteinsFungiLipid MetabolismModels, MolecularNeoplasmsPhylogenyProtein ConformationProtein DomainsCarrier ProteinsFungal ProteinsAcyl-CoA binding domain containing proteinFFAT motifLipid metabolismMembrane contact sitesPathogen host interactionPeroxisomes

Identifiers

PMID32044385
PMCPMC7057175
OpenAlexW3005154756

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.