Evidence map›Paper›PMID 25658350›Full record

ArticleEssays in biochemistry2015

Functions of cholera toxin B-subunit as a raft cross-linker.

Charles A Day, Anne K Kenworthy

Abstract read
In one paragraph

Article in Essays in biochemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

47 citing papers in PubMed, 89 citations in OpenAlex.

  1. Protein-enhanced small molecule disruptors of ordered membrane domains.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  9. Sorting of complex sphingolipids within the cellular endomembrane systems.Frontiers in cell and developmental biology · 2024
    Review
  10. Article
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  14. Ganglioside GM1 and the Central Nervous System.International journal of molecular sciences · 2023
    Review
  15. Article
  16. Article
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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.

Charles A Day*Department of Molecular Physiology and Biophysics, Vanderbilt University School of Medicine, Nashville, TN 37232, U.S.A.
Anne K Kenworthy*Department of Molecular Physiology and Biophysics, Vanderbilt University School of Medicine, Nashville, TN 37232, U.S.A.
Vanderbilt University · US

Funding

MOLECULAR BIOPHYSICS TRAINING PROGRAM AT VANDERBILTT32GM008320 · NIGMS · VANDERBILT UNIVERSITY · PI CHAZIN, WALTER J. · 1989 to 2023
$7.9M
KIDNEY DISEASES RESEARCH TRAINING PROGRAMT32DK007013 · NIDDK · MAYO CLINIC ROCHESTER · PI LIESKE, JOHN C · 1986 to 2023
$3.7M
Function and assembly of toxin-stabilized domainsR01GM106720 · NIGMS · VANDERBILT UNIVERSITY · PI KENWORTHY, ANNE K · 2013 to 2020
$2.7M
Regulation of Microdomain Structure in Living CellsR01GM073846 · NIGMS · VANDERBILT UNIVERSITY · PI KENWORTHY, ANNE K · 2006 to 2010
$1.3M
NIDDK NIH HHS 5 T32 DK007013-35NIDDK NIH HHS T32 DK007013NIGMS NIH HHS R01 GM073846NIGMS NIH HHS R01 GM106720NIGMS NIH HHS T32 GM008320
6 · The paper itself

Abstract

Lipid rafts are putative complexes of lipids and proteins in cellular membranes that are proposed to function in trafficking and signalling events. CTxB (cholera toxin B-subunit) has emerged as one of the most studied examples of a raft-associated protein. Consisting of the membrane-binding domain of cholera toxin, CTxB binds up to five copies of its lipid receptor on the plasma membrane of the host cell. This multivalency of binding gives the toxin the ability to reorganize underlying membrane structure by cross-linking otherwise small and transient lipid rafts. CTxB thus serves as a useful model for understanding the properties and functions of protein-stabilized domains. In the present chapter, we summarize current evidence that CTxB associates with and cross-links lipid rafts, discuss how CTxB binding modulates the architecture and dynamics of membrane domains, and describe the functional consequences of this cross-linking behaviour on toxin uptake into cells via endocytosis.

Indexed as

AnimalsBinding SitesCell MembraneChlorocebus aethiopsCholera ToxinCOS CellsCross-Linking ReagentsEndocytosisHumansMembrane MicrodomainsModels, MolecularProtein BindingSignal TransductionUnilamellar LiposomesCholera ToxinCross-Linking ReagentsUnilamellar Liposomes

Identifiers

PMID25658350
PMCPMC4346142
OpenAlexW2124947642

What OpenQuestion holds

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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.