Evidence map›Paper›PMID 35620056›Full record

ArticleFrontiers in cell and developmental biology2022

The Lipid-Binding Defective Dynamin 2 Mutant in Charcot-Marie-Tooth Disease Impairs Proper Actin Bundling and Actin Organization in Glomerular Podocytes.

Eriko Hamasaki, Natsuki Wakita, Hiroki Yasuoka, Hikaru Nagaoka, Masayuki Morita, Eizo Takashima, Takayuki Uchihashi, Tetsuya Takeda, Tadashi Abe, Ji-Won Lee and 7 more

Open access · goldAbstract read
In one paragraph

Article in Frontiers in cell and developmental biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed, 9 citations in OpenAlex.

  1. Article
  2. Article
  3. Dynamin-dependent entry ofResearch square · 2023
    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

17 authors at 6 institutions in 2 countries.

Eriko HamasakiDepartment of Neuroscience, Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama University, Okayama, Japan.
Natsuki WakitaDepartment of Neuroscience, Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama University, Okayama, Japan.
Hiroki YasuokaDepartment of Neuroscience, Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama University, Okayama, Japan.
Hikaru NagaokaDivision of Malaria Research, Proteo-Science Center, Ehime University, Matsuyama, Japan.
Masayuki MoritaDivision of Malaria Research, Proteo-Science Center, Ehime University, Matsuyama, Japan.
Eizo TakashimaDivision of Malaria Research, Proteo-Science Center, Ehime University, Matsuyama, Japan.
Takayuki UchihashiDepartment of Physics, Nagoya University, Nagoya, Japan.
Tetsuya TakedaDepartment of Neuroscience, Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama University, Okayama, Japan.
Tadashi AbeDepartment of Neuroscience, Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama University, Okayama, Japan.
Ji-Won LeeDepartment of Pharmacology, Faculty and Graduate School of Dental Medicine, Hokkaido University, Sapporo, Japan.
Tadahiro IimuraDepartment of Pharmacology, Faculty and Graduate School of Dental Medicine, Hokkaido University, Sapporo, Japan.
Moin A SaleemBristol Renal, Translational Health Sciences, Bristol Medical School, University of Bristol, Bristol, United Kingdom.
Naohisa OgoCenter for Drug Discovery, Graduate School of Pharmaceutical Sciences, University of Shizuoka, Shizuoka, Japan.
Akira AsaiCenter for Drug Discovery, Graduate School of Pharmaceutical Sciences, University of Shizuoka, Shizuoka, Japan.
Akihiro NaritaGraduate School of Science, Nagoya University, Nagoya, Japan.
Kohji TakeiDepartment of Neuroscience, Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama University, Okayama, Japan.
Hiroshi YamadaDepartment of Neuroscience, Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama University, Okayama, Japan.
Okayama University · JPEhime University · JPHokkaido University · JPNagoya University · JPUniversity of Shizuoka · JPUniversity of Bristol · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Dynamin is an endocytic protein that functions in vesicle formation by scission of invaginated membranes. Dynamin maintains the structure of foot processes in glomerular podocytes by directly and indirectly interacting with actin filaments. However, molecular mechanisms underlying dynamin-mediated actin regulation are largely unknown. Here, biochemical and cell biological experiments were conducted to uncover how dynamin modulates interactions between membranes and actin in human podocytes. Actin-bundling, membrane tubulating, and GTPase activities of dynamin were examined

Indexed as

actinbundleCMTdynaminGTPasepodocyte

Identifiers

PMID35620056
PMCPMC9127447
OpenAlexW4280518866

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.