Evidence map›Paper›PMID 30712872›Full record

ArticleCell2019

Molecular Discrimination between Two Conformations of Sphingomyelin in Plasma Membranes.

Shreya Endapally, Donna Frias, Magdalena Grzemska, Austin Gay, Diana R Tomchick, Arun Radhakrishnan

Open access · bronzeAbstract read
In one paragraph

Article in Cell, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 96 papers.

0numbers the graph read from it
0cells of the map it votes in
96citing papers in PubMed
7.3field-weighted citation impact, top 2% 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

96 citing papers in PubMed, 157 citations in OpenAlex.

  1. Lipidome of Endemic FishMembranes · 2026
    Article
  2. Visualization of the interaction between sphingomyelin and cholesterol in lipid bilayer membranes.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
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  8. Observational
  9. Construction of a linezolid-resistant strain of methicillin-susceptibleFrontiers in cellular and infection microbiology · 2026
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  18. Review
  19. Review
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36 more citing papers are in PubMed but not listed here.

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

6 authors at 1 institution in 1 country.

Shreya EndapallyDepartment of Molecular Genetics, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA.
Donna FriasDepartment of Molecular Genetics, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA.
Magdalena GrzemskaDepartment of Biophysics, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA.
Austin GayDepartment of Molecular Genetics, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA.
Diana R TomchickDepartment of Biophysics, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA.
Arun RadhakrishnanDepartment of Molecular Genetics, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA. Electronic address: arun.radhakrishnan@utsouthwestern.edu.
The University of Texas Southwestern Medical Center · US

Funding

TRANSCRIPTIONAL REGULATION OF LDL RECEPTOR PROMOTERP01HL020948 · NHLBI · UT SOUTHWESTERN MEDICAL CENTER · PI GOLDSTEIN, JOSEPH L · 1985 to 2021
$103.1M
American Heart Association-American Stroke Association 12SDG12040267NHLBI NIH HHS P01 HL020948
6 · The paper itself

Abstract

Sphingomyelin and cholesterol are essential lipids that are enriched in plasma membranes of animal cells, where they interact to regulate membrane properties and many intracellular signaling processes. Despite intense study, the interaction between these lipids in membranes is not well understood. Here, structural and biochemical analyses of ostreolysin A (OlyA), a protein that binds to membranes only when they contain both sphingomyelin and cholesterol, reveal that sphingomyelin adopts two distinct conformations in membranes when cholesterol is present. One conformation, bound by OlyA, is induced by stoichiometric, exothermic interactions with cholesterol, properties that are consistent with sphingomyelin/cholesterol complexes. In its second conformation, sphingomyelin is free from cholesterol and does not bind OlyA. A point mutation abolishes OlyA's ability to discriminate between these two conformations. In cells, levels of sphingomyelin/cholesterol complexes are held constant over a wide range of plasma membrane cholesterol concentrations, enabling precise regulation of the chemical activity of cholesterol.

Indexed as

AnimalsCell LineCell MembraneCholesterolFungal ProteinsHemolysin ProteinsHumansMembrane MicrodomainsMolecular ConformationSphingomyelinsCholesterolFungal ProteinsHemolysin ProteinsostreolysinSphingomyelinsALOD4cholesterolcholesterol homeostasislipid sensorsostreolysin Aplasma membrane structuresphingomyelinsphingomyelin/cholesterol complexes

Identifiers

PMID30712872
PMCPMC6428426
OpenAlexW2914180594

What OpenQuestion holds

Textmetadata
LicenceTDM
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.