Evidence map›Paper›PMID 26541343›Full record

ReviewMedical molecular morphology2016

Involvement of membrane skeletal molecules in the Schmidt-Lanterman incisure in Schwann cells.

Nobuo Terada, Yurika Saitoh, Akio Kamijo, Shinichi Ohno, Nobuhiko Ohno

Abstract readReview
PubMed Publisher
In one paragraph

Review in Medical molecular morphology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.8field-weighted citation impact, top 27% 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

8 citing papers in PubMed, 12 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. In focus in HCB.Histochemistry and cell biology · 2019
    Article
  7. Article
  8. 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

5 authors at 2 institutions in 1 country.

Nobuo TeradaDivision of Health Sciences, Shinshu University Graduate School of Medicine, 3-1-1 Asahi, Matsumoto City, Nagano, 390-8621, Japan. nobuot@shinshu-u.ac.jp.
Yurika SaitohDepartment of Anatomy and Molecular Histology, Interdisciplinary Graduate School of Medicine and Engineering, University of Yamanashi, 1110 Shimokato, Chuo City, Yamanashi, Japan.
Akio KamijoDivision of Health Sciences, Shinshu University Graduate School of Medicine, 3-1-1 Asahi, Matsumoto City, Nagano, 390-8621, Japan.
Shinichi OhnoDepartment of Anatomy and Molecular Histology, Interdisciplinary Graduate School of Medicine and Engineering, University of Yamanashi, 1110 Shimokato, Chuo City, Yamanashi, Japan.
Nobuhiko OhnoDepartment of Anatomy and Molecular Histology, Interdisciplinary Graduate School of Medicine and Engineering, University of Yamanashi, 1110 Shimokato, Chuo City, Yamanashi, Japan.
University of Yamanashi · JPShinshu University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Membrane skeletal networks form a two-dimensional lattice structure beneath erythrocyte membranes. 4.1R-MPP (membrane palmitoylated protein) 1-glycophorin C is one of the basic molecular complexes of the membrane skeleton. An analogous molecular complex, 4.1G-MPP6-cell adhesion molecule 4 (CADM4), is incorporated into the Schmidt-Lanterman incisure (SLI), a truncated cone shape in the myelin internode that is a specific feature of myelinated nerve fibers formed in Schwann cells in the peripheral nervous system. In this review, the dynamic structure of peripheral nerve fibers under stretching conditions is demonstrated using in vivo cryotechnique. The structures of nerve fibers had a beaded appearance, and the heights of SLI circular-truncated cones increased at the narrow sites of nerve fibers under the stretched condition. The height of SLI-truncated cones was lower in 4.1G-deficient nerve fibers than in wild-type nerve fibers. 4.1G was essential for the molecular targeting of MPP6 and CADM4 in SLI. The signal transduction protein, Src, was also involved in the 4.1G-MPP6-CADM4 molecular complex. The phosphorylation of Src was altered by the deletion of 4.1G. Thus, we herein demonstrate a membrane skeletal molecular complex in SLI that has potential roles in the regulation of adhesion and signal transduction as well as in structural stability in Schwann cells.

Indexed as

AnimalsCell Adhesion MoleculesCell Membrane StructuresCytoskeletal ProteinsGuanylate KinasesHumansImmunoglobulinsMembrane ProteinsMultiprotein ComplexesNerve FibersPhosphorylationSchwann CellsCADM4 protein, humanCell Adhesion MoleculesCytoskeletal Proteinserythrocyte membrane band 4.1 proteinGuanylate KinasesImmunoglobulinsMembrane ProteinsMultiprotein ComplexesMembrane palmitoylated protein familyMembrane skeletonProtein 4.1 familySchmidt–Lanterman incisureSchwann cell

Identifiers

PMID26541343
OpenAlexW2169399810

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.