Evidence map›Paper›PMID 28655765›Full record

ArticleThe Journal of biological chemistry2017

Parallel homodimer structures of the extracellular domains of the voltage-gated sodium channel β4 subunit explain its role in cell-cell adhesion.

Hideaki Shimizu, Asako Tosaki, Noboru Ohsawa, Yoshiko Ishizuka-Katsura, Shisako Shoji, Haruko Miyazaki, Fumitaka Oyama, Takaho Terada, Mikako Shirouzu, Shun-Ichi Sekine and 2 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.8field-weighted citation impact, top 29% 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

11 citing papers in PubMed, 15 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Review
  7. Supramolecular clustering of the cardiac sodium channel Nav1.5 in HEK293F cells, with and without the auxiliary β3-subunit.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2020
    Article
  8. mFrontiers in genetics · 2020
    Article
  9. Article
  10. Review
  11. 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

12 authors at 5 institutions in 1 country.

Hideaki ShimizuFrom the RIKEN Systems and Structural Biology Center, Tsurumi, Yokohama 230-0045, Japan.
Asako Tosakithe Laboratory for Structural Neuropathology, RIKEN Brain Science Institute, Wako, Saitama 351-0198, Japan.
Noboru OhsawaFrom the RIKEN Systems and Structural Biology Center, Tsurumi, Yokohama 230-0045, Japan.
Yoshiko Ishizuka-KatsuraFrom the RIKEN Systems and Structural Biology Center, Tsurumi, Yokohama 230-0045, Japan.
Shisako ShojiFrom the RIKEN Systems and Structural Biology Center, Tsurumi, Yokohama 230-0045, Japan.
Haruko Miyazakithe Laboratory for Structural Neuropathology, RIKEN Brain Science Institute, Wako, Saitama 351-0198, Japan.
Fumitaka Oyamathe Laboratory for Structural Neuropathology, RIKEN Brain Science Institute, Wako, Saitama 351-0198, Japan.
Takaho TeradaFrom the RIKEN Systems and Structural Biology Center, Tsurumi, Yokohama 230-0045, Japan.
Mikako ShirouzuFrom the RIKEN Systems and Structural Biology Center, Tsurumi, Yokohama 230-0045, Japan.
Shun-Ichi SekineFrom the RIKEN Systems and Structural Biology Center, Tsurumi, Yokohama 230-0045, Japan.
Nobuyuki Nukinathe Laboratory for Structural Neuropathology, RIKEN Brain Science Institute, Wako, Saitama 351-0198, Japan.
Shigeyuki YokoyamaFrom the RIKEN Systems and Structural Biology Center, Tsurumi, Yokohama 230-0045, Japan, yokoyama@riken.jp.
Systems Biology Institute · JPRIKEN · JPRIKEN Center for Brain Science · JPDoshisha University · JPJuntendo University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Voltage-gated sodium channels (VGSCs) are transmembrane proteins required for the generation of action potentials in excitable cells and essential for propagating electrical impulses along nerve cells. VGSCs are complexes of a pore-forming α subunit and auxiliary β subunits, designated as β1/β1B-β4 (encoded by

Indexed as

Models, MolecularAnimalsCell AdhesionCHO CellsCricetulusCrystallography, X-RayCysteineCystineDimerizationHumansHydrogen BondingHydrophobic and Hydrophilic InteractionsMicePeptide FragmentsProtein ConformationProtein Conformation, beta-StrandCysteineCystinePeptide FragmentsRecombinant Fusion ProteinsRecombinant ProteinsSCN4B protein, humanScn4b protein, mouseVoltage-Gated Sodium Channel beta-4 Subunitcell adhesiondimerimmunoglobulin-like domainmembrane proteinNavβ4SCN4Bsodium channelX-ray crystallography

Identifiers

PMID28655765
PMCPMC5555201
OpenAlexW2724820194

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.