Evidence map›Paper›PMID 27216889›Full record

ArticleScientific reports2016

Structure-based site-directed photo-crosslinking analyses of multimeric cell-adhesive interactions of voltage-gated sodium channel β subunits.

Hideaki Shimizu, Haruko Miyazaki, Noboru Ohsawa, Shisako Shoji, Yoshiko Ishizuka-Katsura, Asako Tosaki, Fumitaka Oyama, Takaho Terada, Kensaku Sakamoto, Mikako Shirouzu and 3 more

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. 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
1.3field-weighted citation impact, top 22% 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, 13 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. 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
  5. Article
  6. Crystal structures of CaProceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  7. Review
  8. Review
  9. Article
  10. Article
  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

13 authors at 2 institutions in 1 country.

Hideaki ShimizuRIKEN Systems and Structural Biology Center, Tsurumi, Yokohama 230-0045, Japan.
Haruko MiyazakiLaboratory for Structural Neuropathology, RIKEN Brain Science Institute, Wako, Saitama 351-0198, Japan.
Noboru OhsawaRIKEN Systems and Structural Biology Center, Tsurumi, Yokohama 230-0045, Japan.
Shisako ShojiRIKEN Systems and Structural Biology Center, Tsurumi, Yokohama 230-0045, Japan.
Yoshiko Ishizuka-KatsuraRIKEN Systems and Structural Biology Center, Tsurumi, Yokohama 230-0045, Japan.
Asako TosakiLaboratory for Structural Neuropathology, RIKEN Brain Science Institute, Wako, Saitama 351-0198, Japan.
Fumitaka OyamaLaboratory for Structural Neuropathology, RIKEN Brain Science Institute, Wako, Saitama 351-0198, Japan.
Takaho TeradaRIKEN Systems and Structural Biology Center, Tsurumi, Yokohama 230-0045, Japan.
Kensaku SakamotoRIKEN Systems and Structural Biology Center, Tsurumi, Yokohama 230-0045, Japan.
Mikako ShirouzuRIKEN Systems and Structural Biology Center, Tsurumi, Yokohama 230-0045, Japan.
Shun-Ichi SekineRIKEN Systems and Structural Biology Center, Tsurumi, Yokohama 230-0045, Japan.
Nobuyuki NukinaLaboratory for Structural Neuropathology, RIKEN Brain Science Institute, Wako, Saitama 351-0198, Japan.
Shigeyuki YokoyamaRIKEN Systems and Structural Biology Center, Tsurumi, Yokohama 230-0045, Japan.
Systems Biology Institute · JPRIKEN Center for Brain Science · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The β1, β2, and β4 subunits of voltage-gated sodium channels reportedly function as cell adhesion molecules. The present crystallographic analysis of the β4 extracellular domain revealed an antiparallel arrangement of the β4 molecules in the crystal lattice. The interface between the two antiparallel β4 molecules is asymmetric, and results in a multimeric assembly. Structure-based mutagenesis and site-directed photo-crosslinking analyses of the β4-mediated cell-cell adhesion revealed that the interface between the antiparallel β4 molecules corresponds to that in the trans homophilic interaction for the multimeric assembly of β4 in cell-cell adhesion. This trans interaction mode is also employed in the β1-mediated cell-cell adhesion. Moreover, the β1 gene mutations associated with generalized epilepsy with febrile seizures plus (GEFS+) impaired the β1-mediated cell-cell adhesion, which should underlie the GEFS+ pathogenesis. Thus, the structural basis for the β-subunit-mediated cell-cell adhesion has been established.

Indexed as

Amino Acid SubstitutionAnimalsCell AdhesionMiceMutagenesis, Site-DirectedMutation, MissenseProtein DomainsVoltage-Gated Sodium Channel beta-1 SubunitVoltage-Gated Sodium Channel beta-4 SubunitVoltage-Gated Sodium Channel beta-1 SubunitVoltage-Gated Sodium Channel beta-4 Subunit

Identifiers

PMID27216889
PMCPMC4877568
OpenAlexW2394671791

What OpenQuestion holds

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LicenceCC BY
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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.