Evidence map›Paper›PMID 28243699›Full record

ReviewCellular and molecular life sciences : CMLS2017

Deciphering the BAR code of membrane modulators.

Ulrich Salzer, Julius Kostan, Kristina Djinović-Carugo

Abstract readReview
In one paragraph

Review in Cellular and molecular life sciences : CMLS, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
–field-weighted citation impact
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

36 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. MTSS1: beyond the integration of actin and membrane dynamics.Cellular and molecular life sciences : CMLS · 2024
    Review
  5. Article
  6. Article
  7. PACSIN2 regulates platelet integrin β1 hemostatic function.Journal of thrombosis and haemostasis : JTH · 2023
    Article
  8. Article
  9. Article
  10. Review
  11. A mechanical-thermodynamic model for understanding endocytosis of COVID-19 virus SARS-CoV-2.Proceedings of the Institution of Mechanical Engineers. Part C. Journal of mechanical engineering science · 2022
    Article
  12. Review
  13. Article
  14. CaFrontiers in molecular neuroscience · 2022
    Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  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

3 authors.

Ulrich SalzerMax F. Perutz Laboratories, Department of Medical Biochemistry, Medical University of Vienna, Dr. Bohr-Gasse 9, 1030, Vienna, Austria.
Julius KostanMax F. Perutz Laboratories, Department of Structural and Computational Biology, University of Vienna, Campus Vienna Biocenter 5, 1030, Vienna, Austria.
Kristina Djinović-CarugoMax F. Perutz Laboratories, Department of Structural and Computational Biology, University of Vienna, Campus Vienna Biocenter 5, 1030, Vienna, Austria. kristina.djinovic@univie.ac.at.ORCID 0000-0003-0252-2972

Funding

Austrian Science Fund FWF I 1593Austrian Science Fund FWF I 525
6 · The paper itself

Abstract

The BAR domain is the eponymous domain of the "BAR-domain protein superfamily", a large and diverse set of mostly multi-domain proteins that play eminent roles at the membrane cytoskeleton interface. BAR domain homodimers are the functional units that peripherally associate with lipid membranes and are involved in membrane sculpting activities. Differences in their intrinsic curvatures and lipid-binding properties account for a large variety in membrane modulating properties. Membrane activities of BAR domains are further modified and regulated by intramolecular or inter-subunit domains, by intermolecular protein interactions, and by posttranslational modifications. Rather than providing detailed cell biological information on single members of this superfamily, this review focuses on biochemical, biophysical, and structural aspects and on recent findings that paradigmatically promote our understanding of processes driven and modulated by BAR domains.

Indexed as

AnimalsCell MembraneHumansMembrane ProteinsPhosphorylationProtein BindingProtein DomainsProtein Interaction MappingMembrane ProteinsF-BAR domainI-BAR domainlipid bindingMembrane curvatureMembrane remodellingN-BAR domain

Identifiers

PMID28243699
PMCPMC5487894

What Socratic 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 Socratic graph.