Evidence map›Paper›PMID 21775436›Full record

ArticleThe Journal of biological chemistry2011

Atomic force microscopy reveals the architecture of the epithelial sodium channel (ENaC).

Andrew P Stewart, Silke Haerteis, Alexei Diakov, Christoph Korbmacher, J Michael Edwardson

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
–field-weighted citation impact
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

38 citing papers in PubMed.

  1. Epithelial NaComprehensive Physiology · 2024
    Review
  2. Bile acids regulate the epithelial NaThe Journal of physiology · 2022
    Article
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  6. Article
  7. Review
  8. N-linked glycans are required on epithelial NaAmerican journal of physiology. Renal physiology · 2018
    Article
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  13. Review
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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

5 authors.

Andrew P StewartDepartment of Pharmacology, University of Cambridge, Tennis Court Road, Cambridge CB2 1PD, United Kingdom.
Silke Haerteis
Alexei Diakov
Christoph Korbmacher
J Michael Edwardson

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The epithelial sodium channel (ENaC) is a member of the ENaC/degenerin superfamily. ENaC is a heteromultimer containing three homologous subunits (α, β, and γ); however, the subunit stoichiometry is still controversial. Here, we addressed this issue using atomic force microscopy imaging of complexes between isolated ENaC and antibodies/Fab fragments directed against specific epitope tags on the α-, β- and γ-subunits. We show that for α-, β- and γ-ENaC alone, pairs of antibodies decorate the channel at an angle of 120°, indicating that the individual subunits assemble as homotrimers. A similar approach demonstrates that αβγ-ENaC assembles as a heterotrimer containing one copy of each subunit. Intriguingly, all four subunit combinations also produce higher-order structures containing two or three individual trimers. The trimer-of-trimers organization would account for earlier reports that ENaC contains eight to nine subunits.

Indexed as

Microscopy, Atomic ForceAnimalsCell MembraneEpithelial Sodium ChannelsHEK293 CellsHumansImmunoglobulin Fab FragmentsProtein Structure, QuaternaryProtein SubunitsXenopus laevisEpithelial Sodium ChannelsImmunoglobulin Fab FragmentsProtein Subunits

Identifiers

PMID21775436
PMCPMC3173231

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

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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.