Evidence map›Paper›PMID 33712199›Full record

ArticleMethods in enzymology2021

The use of anthrolysin O and ostreolysin A to study cholesterol in cell membranes.

Kristen A Johnson, Arun Radhakrishnan

Open access · greenAbstract read
In one paragraph

Article in Methods in enzymology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
9.4field-weighted citation impact, top 1% 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

15 citing papers in PubMed, 25 citations in OpenAlex.

  1. Design and structural basis of selective nonsteroidal inhibitors of aster cholesterol trafficking.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
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  5. Lysosomal glucocerebrosidase is needed for ciliary Hedgehog signaling: A convergent pathway contributing to Parkinson's disease.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  6. Article
  7. Monitoring Accessible Cholesterol Levels in Immune Cells.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  8. Article
  9. Lipid regulation of the glucagon receptor family.The Journal of endocrinology · 2024
    Review
  10. Article
  11. Article
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  15. 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

2 authors at 1 institution in 1 country.

Kristen A JohnsonDepartment of Molecular Genetics, University of Texas Southwestern Medical Center, Dallas, TX, United States.
Arun RadhakrishnanDepartment of Molecular Genetics, University of Texas Southwestern Medical Center, Dallas, TX, United States. 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
NHLBI NIH HHS P01 HL020948
6 · The paper itself

Abstract

Cholesterol is a major component of the plasma membranes (PMs) of animal cells, comprising 35-40mol% of total PM lipids. Recent studies using cholesterol-binding bacterial toxins such as domain 4 of Anthrolysin O (ALOD4) and fungal toxins such as Ostreolysin A (OlyA) have revealed new insights into the organization of PM cholesterol. These studies have defined three distinct pools of PM cholesterol-a fixed pool that is essential for membrane integrity, a sphingomyelin (SM)-sequestered pool that can be detected by OlyA, and a third pool that is accessible and can be detected by ALOD4. Accessible cholesterol is available to interact with proteins and transport to the endoplasmic reticulum (ER), and controls many cellular signaling processes including cholesterol homeostasis, Hedgehog signaling, and bacterial and viral infection. Here, we provide detailed descriptions for the use of ALOD4 and OlyA, both of which are soluble and non-lytic proteins, to study cholesterol organization in the PMs of animal cells. Furthermore, we describe two new versions of ALOD4 that we have developed to increase the versatility of this probe in cellular studies. One is a dual His

Indexed as

Hedgehog ProteinsHemolysin ProteinsAnimalsCell MembraneCholesterolFungal ProteinsCholesterolFungal ProteinsHedgehog ProteinsHemolysin ProteinsostreolysinCholesterol-binding toxinsCholesterol sensorsCholesterol traffickingEndoplasmic reticulumFluorescence imaging of cholesterol poolsPlasma membrane cholesterol pools

Identifiers

PMID33712199
PMCPMC8034815
OpenAlexW3130024773

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.