Evidence map›Paper›PMID 25567098›Full record

ReviewOpen biology2015

A new look at sodium channel β subunits.

Sivakumar Namadurai, Nikitha R Yereddi, Fiona S Cusdin, Christopher L H Huang, Dimitri Y Chirgadze, Antony P Jackson

Open access · goldAbstract readReview
In one paragraph

Review in Open biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed
5.9field-weighted citation impact, top 3% 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

63 citing papers in PubMed, 102 citations in OpenAlex.

  1. Review
  2. Review
  3. Critical role of extracellular loops in differential modulations of TTX-sensitive and TTX-resistant NaProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  4. A Novel Function of NaFASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025
    Article
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3 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.

Sivakumar NamaduraiDepartment of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge CB2 1QW, UK.
Nikitha R YereddiDepartment of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge CB2 1QW, UK.
Fiona S CusdinDepartment of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge CB2 1QW, UK.
Christopher L H HuangPhysiological Laboratory, University of Cambridge, Cambridge CB2 3EG, UK.
Dimitri Y ChirgadzeDepartment of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge CB2 1QW, UK.
Antony P JacksonDepartment of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge CB2 1QW, UK apj10@cam.ac.uk.ORCID http://orcid.org/0000-0002-2895-7387
University of Cambridge · GB

Funding

British Heart Foundation PG/14/79/31102Medical Research Council M001288/1Medical Research Council MR/M001288/1
6 · The paper itself

Abstract

Voltage-gated sodium (Nav) channels are intrinsic plasma membrane proteins that initiate the action potential in electrically excitable cells. They are a major focus of research in neurobiology, structural biology, membrane biology and pharmacology. Mutations in Nav channels are implicated in a wide variety of inherited pathologies, including cardiac conduction diseases, myotonic conditions, epilepsy and chronic pain syndromes. Drugs active against Nav channels are used as local anaesthetics, anti-arrhythmics, analgesics and anti-convulsants. The Nav channels are composed of a pore-forming α subunit and associated β subunits. The β subunits are members of the immunoglobulin (Ig) domain family of cell-adhesion molecules. They modulate multiple aspects of Nav channel behaviour and play critical roles in controlling neuronal excitability. The recently published atomic resolution structures of the human β3 and β4 subunit Ig domains open a new chapter in the study of these molecules. In particular, the discovery that β3 subunits form trimers suggests that Nav channel oligomerization may contribute to the functional properties of some β subunits.

Indexed as

Action PotentialsAmino Acid SequenceAnimalsEvolution, MolecularHumansIon Channel GatingMolecular Sequence DataVoltage-Gated Sodium Channel beta SubunitsVoltage-Gated Sodium Channel beta Subunitsion channelopathiessodium channel β subunitsX-ray crystallography

Identifiers

PMID25567098
PMCPMC4313373
OpenAlexW2118753760

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.