Evidence map›Paper›PMID 27806264›Full record

ArticleBiophysical journal2016

Membrane Shape Instability Induced by Protein Crowding.

Zhiming Chen, Ehsan Atefi, Tobias Baumgart

Abstract read
In one paragraph

Article in Biophysical journal, 2016. 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
–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

26 citing papers in PubMed.

  1. VAMP8 function reveals tight linkage between endocytic recycling and endocytosis.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Macromolecular Crowding in Mitochondria.Sub-cellular biochemistry · 2025
    Review
  3. Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Cellular Membranes, a Versatile Adaptive Composite Material.Frontiers in cell and developmental biology · 2020
    Review
  11. Clustering and dynamics of crowded proteins near membranes and their influence on membrane bending.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  12. Article
  13. Kinetics of Histidine-Tagged Protein Association to Nickel-Decorated Liposome Surfaces.Langmuir : the ACS journal of surfaces and colloids · 2019
    Article
  14. Article
  15. Review
  16. Review
  17. Review
  18. Simulations of N-BAR Protein Interactions with Membranes.Journal of physics D: Applied physics · 2018
    Article
  19. Review
  20. The 2018 biomembrane curvature and remodeling roadmap.Journal of physics D: Applied physics · 2018
    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.

Zhiming ChenDepartment of Chemistry, University of Pennsylvania, Philadelphia, Pennsylvania.
Ehsan AtefiDepartment of Chemistry, University of Pennsylvania, Philadelphia, Pennsylvania; Department of Chemical Engineering, University of Pennsylvania, Philadelphia, Pennsylvania.
Tobias BaumgartDepartment of Chemistry, University of Pennsylvania, Philadelphia, Pennsylvania. Electronic address: baumgart@sas.upenn.edu.

Funding

PSOC@Penn Education and OutreachU54CA193417 · NCI · UNIVERSITY OF PENNSYLVANIA · PI DISCHER, DENNIS E. · 2015 to 2020
$10.5M
Membrane shape transition control in cellular membrane trafficking phenomenaR01GM097552 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI BAUMGART, TOBIAS · 2011 to 2023
$4.5M
NCI NIH HHS U54 CA193417NIGMS NIH HHS R01 GM097552
6 · The paper itself

Abstract

Peripheral proteins can bend membranes through several different mechanisms, including scaffolding, wedging, oligomerization, and crowding. The crowding effect in particular has received considerable attention recently, in part because it is a colligative mechanism-implying that it could, in principle, be explored by any peripheral protein. Here we sought to clarify to what extent this mechanism is exploited by endocytic accessory proteins. We quantitatively investigate membrane curvature generation by means of a GUV shape stability assay. We found that the amount of crowding required to induce membrane curvature is correlated with membrane tension. Importantly, we also revealed that at the same membrane tension, the crowding mechanism requires far higher protein coverage to induce curvature changes compared to those observed for the endophilin BAR domain, serving here as an example of an endocytic accessory protein. Our results are important for the design of membrane-targeted biosensors as well as the understanding of mechanisms of biological membrane shaping.

Indexed as

Cell MembraneEndocytosisMembrane ProteinsProtein DomainsStress, MechanicalUnilamellar LiposomesMembrane ProteinsUnilamellar Liposomes

Identifiers

PMID27806264
PMCPMC5103033

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.