Evidence map›Paper›PMID 21474780›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2011

Membrane texture induced by specific protein binding and receptor clustering: active roles for lipids in cellular function.

E B Watkins, C E Miller, J Majewski, T L Kuhl

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
3.9field-weighted citation impact, top 6% 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

33 citing papers in PubMed, 78 citations in OpenAlex.

  1. Review
  2. Article
  3. Significance of Receptor Mobility in Multivalent Binding on Lipid Membranes.Angewandte Chemie (International ed. in English) · 2022
    Review
  4. Review
  5. Article
  6. Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Review
  17. The plasma membrane as a capacitor for energy and metabolism.American journal of physiology. Cell physiology · 2016
    Review
  18. Budding Yeast: An Ideal Backdrop forFrontiers in cell and developmental biology · 2016
    Review
  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

4 authors at 3 institutions in 1 country.

E B WatkinsBiophysics Graduate Group, University of California, Davis, CA 95616, USA.
C E Miller
J Majewski
T L Kuhl
University of California, Davis · USLos Alamos National Laboratory · USStanford Synchrotron Radiation Lightsource · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Biological membranes are complex, self-organized structures that define boundaries and compartmentalize space in living matter. Composed of a wide variety of lipid and protein molecules, these responsive surfaces mediate transmembrane signaling and material transport within the cell and with its environment. It is well known that lipid membrane properties change as a function of composition and phase state, and that protein-lipid interactions can induce changes in the membrane's properties and biochemical response. Here, molecular level changes in lipid organization induced by multivalent toxin binding were investigated using grazing incidence X-ray diffraction. Structural changes to lipid monolayers at the air-water interface and bilayers at the solid-water interface were studied before and after specific binding of cholera toxin to membrane embedded receptors. At biologically relevant surface pressures, protein binding perturbed lipid packing within monolayers and bilayers resulting in topological defects and the emergence of a new orientationally textured lipid phase. In bilayers this altered lipid order was transmitted from the receptor laden exterior membrane leaflet to the inner leaflet, representing a potential mechanism for lipid mediated outside-in signaling by multivalent protein binding. It is further hypothesized that cell-surface micro-domains exhibiting this type of lipid order may serve as nucleation sites for vesicle formation in clathrin independent endocytosis of cholera toxin.

Indexed as

Membranes, ArtificialModels, BiologicalCell MembraneCholera ToxinEndocytosisMembrane LipidsMembrane ProteinsSignal TransductionCholera ToxinMembrane LipidsMembrane ProteinsMembranes, Artificial

Identifiers

PMID21474780
PMCPMC3084047
OpenAlexW2170393159

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.