Evidence map›Paper›PMID 25811483›Full record

ArticlePloS one2015

Effect of receptor dimerization on membrane lipid raft structure continuously quantified on single cells by camera based fluorescence correlation spectroscopy.

Heng Huang, M Fethullah Simsek, Weixiang Jin, Arnd Pralle

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.9field-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

18 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Spot size variation FCS in simulations of the 2D Ising model.Journal of physics D: Applied physics · 2016
    Article
  15. Article
  16. Article
  17. Review
  18. 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 1 institution in 1 country.

Heng HuangDepartment of Physics, University at Buffalo the State University of New York, Buffalo, New York, United States of America.
M Fethullah SimsekDepartment of Physics, University at Buffalo the State University of New York, Buffalo, New York, United States of America.
Weixiang JinDepartment of Physics, University at Buffalo the State University of New York, Buffalo, New York, United States of America.
Arnd PralleDepartment of Physics, University at Buffalo the State University of New York, Buffalo, New York, United States of America; Department of Biophysics and Physiology, University at Buffalo the State University of New York, Buffalo, New York, United States of America.
University at Buffalo, State University of New York · US

Funding

Membrane biophysics of enterotoxin mediated immunomodulationR21AI097879 · NIAID · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI PRALLE, ARND · 2012 to 2013
$415k
NIAID NIH HHS R21 AI097879
6 · The paper itself

Abstract

Membrane bound cell signaling is modulated by the membrane ultra-structure, which itself may be affected by signaling. However, measuring the interaction of membrane proteins with membrane structures in intact cells in real-time poses considerable challenges. In this paper we present a non-destructive fluorescence method that quantifies these interactions in single cells, and is able to monitor the same cell continuously to observe small changes. This approach combines total internal fluorescence microscopy with fluorescence correlation spectroscopy to measure the protein's diffusion and molecular concentration in different sized areas simultaneously. It correctly differentiates proteins interacting with membrane fences from proteins interacting with cholesterol-stabilized domains, or lipid rafts. This method detects small perturbations of the membrane ultra-structure or of a protein's tendency to dimerize. Through continuous monitoring of single cells, we demonstrate how dimerization of GPI-anchored proteins increases their association with the structural domains. Using a dual-color approach we study the effect of dimerization of one GPI-anchored protein on another type of GPI-anchored protein expressed in the same cell. Scans over the cell surface reveal a correlation between cholesterol stabilized domains and membrane cytoskeleton.

Indexed as

Protein MultimerizationActininCholesterolDiffusionFolate Receptors, GPI-AnchoredGreen Fluorescent ProteinsMembrane MicrodomainsMembrane ProteinsPhotographyProtein Structure, TertiarySingle-Cell AnalysisSpectrometry, FluorescenceActininCholesterolFolate Receptors, GPI-AnchoredGreen Fluorescent ProteinsMembrane Proteins

Identifiers

PMID25811483
PMCPMC4374828
OpenAlexW1976045660

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.