Evidence map›Paper›PMID 33228720›Full record

ArticleMolecular brain2020

Focal loss of the paranodal domain protein Neurofascin155 in the internal capsule impairs cortically induced muscle activity in vivo.

Kazuo Kunisawa, Nobuhiko Hatanaka, Takeshi Shimizu, Kenta Kobayashi, Yasuyuki Osanai, Akihiro Mouri, Qian Shi, Manzoor A Bhat, Atsushi Nambu, Kazuhiro Ikenaka

Open access · goldAbstract read
In one paragraph

Article in Molecular brain, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.1field-weighted citation impact, top 58% 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

2 citing papers in PubMed, 6 citations in OpenAlex.

  1. Article
  2. 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

10 authors at 3 institutions in 2 countries.

Kazuo KunisawaDivision of Neurobiology and Bioinformatics, National Institute for Physiological Sciences, Okazaki, 444-8787, Japan.
Nobuhiko HatanakaDepartment of Physiological Sciences, SOKENDAI (The Graduate University for Advanced Studies), Okazaki, 444-8787, Japan. hatanaka@nips.ac.jp.ORCID 0000-0001-8793-1438
Takeshi ShimizuDivision of Neurobiology and Bioinformatics, National Institute for Physiological Sciences, Okazaki, 444-8787, Japan.
Kenta KobayashiDepartment of Physiological Sciences, SOKENDAI (The Graduate University for Advanced Studies), Okazaki, 444-8787, Japan.
Yasuyuki OsanaiDivision of Neurobiology and Bioinformatics, National Institute for Physiological Sciences, Okazaki, 444-8787, Japan.
Akihiro MouriDepartment of Regulatory Science for Evaluation and Development of Pharmaceuticals and Devices, Fujita Health University Graduate School of Health Sciences, Toyoake, 470-1192, Japan.
Qian ShiDepartment of Cellular and Integrative Physiology, School of Medicine, University of Texas Health Science Center, San Antonio, 78229-3900, USA.
Manzoor A BhatDepartment of Cellular and Integrative Physiology, School of Medicine, University of Texas Health Science Center, San Antonio, 78229-3900, USA.
Atsushi NambuDepartment of Physiological Sciences, SOKENDAI (The Graduate University for Advanced Studies), Okazaki, 444-8787, Japan.
Kazuhiro IkenakaDivision of Neurobiology and Bioinformatics, National Institute for Physiological Sciences, Okazaki, 444-8787, Japan.
The Graduate University for Advanced Studies, SOKENDAI · JPFujita Health University · JPThe University of Texas Health Science Center at San Antonio · US

Funding

Molecular Organization &Function of Paranodal JunctionsR01GM063074 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI BHAT, MANZOOR A. · 2001 to 2023
$5.8M
NIGMS NIH HHS R01 GM063074
6 · The paper itself

Abstract

Paranodal axoglial junctions are essential for rapid nerve conduction and the organization of axonal domains in myelinated axons. Neurofascin155 (Nfasc155) is a glial cell adhesion molecule that is also required for the assembly of these domains. Previous studies have demonstrated that general ablation of Nfasc155 disorganizes these domains, reduces conduction velocity, and disrupts motor behaviors. Multiple sclerosis (MS), a typical disorder of demyelination in the central nervous system, is reported to have autoantibody to Nfasc. However, the impact of focal loss of Nfasc155, which may occur in MS patients, remains unclear. Here, we examined whether restricted focal loss of Nfasc155 affects the electrophysiological properties of the motor system in vivo. Adeno-associated virus type5 (AAV5) harboring EGFP-2A-Cre was injected into the glial-enriched internal capsule of floxed-Neurofascin (Nfasc

Indexed as

AnimalsCell Adhesion MoleculesCerebral CortexDependovirusElectromyographyIntegrasesInternal CapsuleMiceMusclesNerve Growth FactorsCell Adhesion MoleculesCre recombinaseIntegrasesNerve Growth FactorsNfasc protein, mouseElectromyogramMotor systemMultiple sclerosisNeurofascin155Paranodal junction

Identifiers

PMID33228720
PMCPMC7685608
OpenAlexW3110099305

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.