Evidence map›Paper›PMID 10545131›Full record

ReviewThe Journal of physiology1999

Functional domains within the degenerin/epithelial sodium channel (Deg/ENaC) superfamily of ion channels.

D J Benos, B A Stanton

Open access · bronzeAbstract readReview
In one paragraph

Review in The Journal of physiology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
61citing papers in PubMed, 1 pooled it
2.6field-weighted citation impact, top 10% 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

61 citing papers in PubMed, 1 synthesis or guideline pooled it, 168 citations in OpenAlex.

  1. Pooled it
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  5. Review
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  7. Review
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  9. Article
  10. Tumor necrosis factor-α impairs cerebral blood flow in pregnant rats: role of vascular β-epithelial NaAmerican journal of physiology. Heart and circulatory physiology · 2020
    Article
  11. Article
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  15. Article
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  18. Regulation of epithelial sodium channels in urokinase plasminogen activator deficiency.American journal of physiology. Lung cellular and molecular physiology · 2014
    Article
  19. Article
  20. δ ENaC: a novel divergent amiloride-inhibitable sodium channel.American journal of physiology. Lung cellular and molecular physiology · 2012
    Review

1 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

2 authors at 2 institutions in 1 country.

D J BenosDepartment of Physiology and Biophysics, University of Alabama at Birmingham, 1918 University Boulevard, Birmingham, AL 35294-0005, USA. benos@physiology.uab.edu
B A Stanton
Dartmouth College · USUniversity of Alabama at Birmingham · US

Funding

SODIUM ENTRY INTO AMILORIDE-SENSITIVE EPITHELIAR01DK037206 · NIDDK · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI FULLER, CATHERINE M · 1986 to 2014
$3.9M
ELECTRONEUTRAL H SECRETION IN DISTAL NEPHRONR01DK034533 · NIDDK · DARTMOUTH COLLEGE · PI STANTON, BRUCE A. · 1986 to 2006
$2.1M
CATION SELECTIVITY, CONDUCTION, AND CA++ BLOCK OF ENACR01DK056095 · NIDDK · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI BENOS, DALE J · 1999 to 2002
$593k
Sodium Entry into Amiloride-Sensitive EpitheliaR56DK037206 · NIDDK · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI BENOS, DALE J · 2009 to 2009
$363k
NIDDK NIH HHS DK34533NIDDK NIH HHS DK37206NIDDK NIH HHS DK56095NIDDK NIH HHS R01 DK034533NIDDK NIH HHS R01 DK037206NIDDK NIH HHS R56 DK037206
6 · The paper itself

Abstract

Application of recombinant DNA technology and electrophysiology to the study of amiloride-sensitive Na+ channels has resulted in an enormous increase in the understanding of the structure-function relationships of these channels. Moreover, this knowledge has permitted the elucidation of the physiological roles of these ion channels in cellular processes as diverse as transepithelial salt and water movement, taste perception, volume regulation, nociception, neuronal function, mechanosensation, and even defaecation. Although members of this ever-growing superfamily of ion channels (the Deg/ENaC superfamily) share little amino acid identity, they are all organized similarly, namely, two short N- and C-termini, two short membrane-spanning segments, and a very large extracellular loop domain. In this brief Topical Review, we discuss the structural features of each domain of this Deg/ENaC superfamily and, using ENaC as a model, show how each domain relates to overall channel function.

Indexed as

Amino Acid SequenceAnimalsCytoplasmDegenerin Sodium ChannelsEpithelial Sodium ChannelsIon ChannelsMolecular Sequence DataNerve Tissue ProteinsSodium ChannelsDegenerin Sodium ChannelsEpithelial Sodium ChannelsIon ChannelsNerve Tissue ProteinsSodium Channels

Identifiers

PMID10545131
PMCPMC2269617
OpenAlexW2065864299

What OpenQuestion holds

Textmetadata
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.