Evidence map›Paper›PMID 37895291›Full record

ReviewGenes2023

Recent Progress on Genetically Modified Animal Models for Membrane Skeletal Proteins: The 4.1 and MPP Families.

Nobuo Terada, Yurika Saitoh, Masaki Saito, Tomoki Yamada, Akio Kamijo, Takahiro Yoshizawa, Takeharu Sakamoto

Open access · goldAbstract readReview
In one paragraph

Review in Genes, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.7field-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

1 citing paper in PubMed, 4 citations in OpenAlex.

  1. 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

7 authors at 3 institutions in 1 country.

Nobuo TeradaHealth Science Division, Department of Medical Sciences, Shinshu University Graduate School of Medicine, Science and Technology, Matsumoto City, Nagano 390-8621, Japan.
Yurika SaitohHealth Science Division, Department of Medical Sciences, Shinshu University Graduate School of Medicine, Science and Technology, Matsumoto City, Nagano 390-8621, Japan.
Masaki SaitoSchool of Pharma-Science, Teikyo University, Itabashi-ku, Tokyo 173-8605, Japan.ORCID 0000-0001-7259-4248
Tomoki YamadaHealth Science Division, Department of Medical Sciences, Shinshu University Graduate School of Medicine, Science and Technology, Matsumoto City, Nagano 390-8621, Japan.
Akio KamijoHealth Science Division, Department of Medical Sciences, Shinshu University Graduate School of Medicine, Science and Technology, Matsumoto City, Nagano 390-8621, Japan.
Takahiro YoshizawaDivision of Animal Research, Research Center for Advanced Science and Technology, Shinshu University, Matsumoto City, Nagano 390-8621, Japan.ORCID 0000-0002-9938-6569
Takeharu SakamotoDepartment of Cancer Biology, Institute of Biomedical Science, Kansai Medical University, Hirakata City, Osaka 573-1010, Japan.ORCID 0000-0002-1225-1902
Shinshu University · JPKansai Medical University · JPTeikyo University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The protein 4.1 and membrane palmitoylated protein (MPP) families were originally found as components in the erythrocyte membrane skeletal protein complex, which helps maintain the stability of erythrocyte membranes by linking intramembranous proteins and meshwork structures composed of actin and spectrin under the membranes. Recently, it has been recognized that cells and tissues ubiquitously use this membrane skeletal system. Various intramembranous proteins, including adhesion molecules, ion channels, and receptors, have been shown to interact with the 4.1 and MPP families, regulating cellular and tissue dynamics by binding to intracellular signal transduction proteins. In this review, we focus on our previous studies regarding genetically modified animal models, especially on 4.1G, MPP6, and MPP2, to describe their functional roles in the peripheral nervous system, the central nervous system, the testis, and bone formation. As the membrane skeletal proteins are located at sites that receive signals from outside the cell and transduce signals inside the cell, it is necessary to elucidate their molecular interrelationships, which may broaden the understanding of cell and tissue functions.

Indexed as

Cytoskeletal ProteinsMembrane ProteinsAnimalsAnimals, Genetically ModifiedHumansIon ChannelsMalePeripheral Nervous SystemCytoskeletal ProteinsIon ChannelsMembrane Proteinsbone formationmembrane palmitoylated proteinmembrane skeletonnervous systemprotein 4.1Gtestis

Identifiers

PMID37895291
PMCPMC10606877
OpenAlexW4387653585

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.