Evidence map›Paper›PMID 30203378›Full record

ArticleMetabolic brain disease2018

Changes in biophysical characteristics of PFN1 due to mutation causing amyotrophic lateral sclerosis.

Mina Nekouei, Parviz Ghezellou, Atousa Aliahmadi, Sareh Arjmand, Mahmoud Kiaei, Alireza Ghassempour

Abstract read
In one paragraph

Article in Metabolic brain disease, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

10 citing papers in PubMed, 14 citations in OpenAlex.

  1. Article
  2. Article
  3. Modelling amyotrophic lateral sclerosis in rodents.Nature reviews. Neuroscience · 2022
    Review
  4. Article
  5. ALS-linked PFN1 variants exhibit loss and gain of functions in the context of formin-induced actin polymerization.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. 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

6 authors at 2 institutions in 2 countries.

Mina NekoueiDepartment of Phytochemistry, Medicinal Plants and Drugs Research Institute, Shahid Beheshti University, G.C., Evin, Tehran, Iran.
Parviz GhezellouDepartment of Phytochemistry, Medicinal Plants and Drugs Research Institute, Shahid Beheshti University, G.C., Evin, Tehran, Iran.
Atousa AliahmadiDepartment of Biology, Medicinal Plants and Drugs Research Institute, Shahid Beheshti University, G.C., Evin, Tehran, Iran.
Sareh ArjmandProtein Research Center, Shahid Beheshti University, G.C., Evin, Tehran, Iran.
Mahmoud KiaeiDepartment of Pharmacology and Toxicology, Department of Neurology, Department of Geriatrics, University of Arkansas for Medical Sciences, Little Rock, AR, 72205, USA. mkiaei@uams.edu.ORCID http://orcid.org/0000-0002-0802-1426
Alireza GhassempourDepartment of Phytochemistry, Medicinal Plants and Drugs Research Institute, Shahid Beheshti University, G.C., Evin, Tehran, Iran. a-ghassempour@sbu.ac.ir.
Shahid Beheshti University · IRUniversity of Arkansas Medical Center · US

Funding

The Role o f Tetrahydrobiopterin (BH4) Bioavailability in Radiation-induced Skin InjuryP20GM109005 · NIGMS · UNIV OF ARKANSAS FOR MED SCIS · PI WOLFE, TATIANA · 2015 to 2024
$21.1M
Telemedicine CoreP30GM110702 · NIGMS · UNIV OF ARKANSAS FOR MED SCIS · PI GARCIA-RILL, EDGAR E. · 2014 to 2018
$6.1M
Development of a New ALS Mouse Model that Targets Profilin1 and Actin FilamentsR21NS088653 · NINDS · UNIV OF ARKANSAS FOR MED SCIS · PI KIAEI, MAHMOUD · 2015 to 2016
$410k
Alpha-Tubulin Mutation and Motor Neuron DiseaseR03NS101334 · NINDS · UNIV OF ARKANSAS FOR MED SCIS · PI KIAEI, MAHMOUD · 2017 to 2018
$149k
NIGMS NIH HHS P20 GM109005NIGMS NIH HHS P30 GM110702NINDS NIH HHS R03 NS101334NINDS NIH HHS R21 NS088653
6 · The paper itself

Abstract

Single amino acid mutations in profilin 1 (PFN1) have been found to cause amyotrophic lateral sclerosis (ALS). Recently, we developed a mouse model for ALS using a PFN1 mutation (glycine 118 to valine, G118V), and we are now interested in understanding how PFN1 becomes toxically lethal with only one amino acid substitution. Therefore, we studied mutation-related changes in the PFN1 protein and hypothesized that such changes significantly disturb its structure. Initially, we expressed and studied the purified PFN1

Indexed as

Amyotrophic Lateral SclerosisHumansMutationProfilinsProtein AggregatesProtein Structure, SecondaryRecombinant ProteinsPFN1 protein, humanProfilinsProtein AggregatesRecombinant ProteinsActin binding domainAggregationALSPFN1G118VPFN1WT

Identifiers

PMID30203378
PMCPMC6230493
OpenAlexW2891644066

What OpenQuestion holds

Textmetadata
LicenceTDM
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.