Evidence map›Paper›PMID 36499097›Full record

ArticleInternational journal of molecular sciences2022

Understanding In Vitro Pathways to Drug Discovery for TDP-43 Proteinopathies.

Hei W A Cheng, Timothy B Callis, Andrew P Montgomery, Jonathan J Danon, William T Jorgensen, Yazi D Ke, Lars M Ittner, Eryn L Werry, Michael Kassiou

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2022. 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
0.2field-weighted citation impact, top 42% 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, 2 citations in OpenAlex.

  1. Molecular Mechanisms of Dementia.International journal of molecular sciences · 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

9 authors at 2 institutions in 1 country.

Hei W A ChengSchool of Medical Sciences, Faculty of Medicine and Health, The University of Sydney, Sydney, NSW 2006, Australia.
Timothy B CallisSchool of Chemistry, Faculty of Science, The University of Sydney, Sydney, NSW 2006, Australia.
Andrew P MontgomerySchool of Chemistry, Faculty of Science, The University of Sydney, Sydney, NSW 2006, Australia.ORCID 0000-0002-1819-3619
Jonathan J DanonSchool of Chemistry, Faculty of Science, The University of Sydney, Sydney, NSW 2006, Australia.ORCID 0000-0001-6242-1941
William T JorgensenSchool of Chemistry, Faculty of Science, The University of Sydney, Sydney, NSW 2006, Australia.
Yazi D KeDepartment of Biomedical Sciences, Faculty of Medicine and Health Sciences, 2 Technology Place, Macquarie University, Sydney, NSW 2109, Australia.ORCID 0000-0002-1423-0451
Lars M IttnerDepartment of Biomedical Sciences, Faculty of Medicine and Health Sciences, 2 Technology Place, Macquarie University, Sydney, NSW 2109, Australia.
Eryn L WerrySchool of Chemistry, Faculty of Science, The University of Sydney, Sydney, NSW 2006, Australia.
Michael KassiouSchool of Chemistry, Faculty of Science, The University of Sydney, Sydney, NSW 2006, Australia.
The University of Sydney · AUMacquarie University · AU

Funding

National Health and Medical Research Council APP1132524, APP1154692, GNT2008066
6 · The paper itself

Abstract

The use of cellular models is a common means to investigate the potency of therapeutics in pre-clinical drug discovery. However, there is currently no consensus on which model most accurately replicates key aspects of amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD) pathology, such as accumulation of insoluble, cytoplasmic transactive response DNA-binding protein (TDP-43) and the formation of insoluble stress granules. Given this, we characterised two TDP-43 proteinopathy cellular models that were based on different aetiologies of disease. The first was a sodium arsenite-induced chronic oxidative stress model and the second expressed a disease-relevant TDP-43 mutation (TDP-43 M337V). The sodium arsenite model displayed most aspects of TDP-43, stress granule and ubiquitin pathology seen in human ALS/FTD donor tissue, whereas the mutant cell line only modelled some aspects. When these two cellular models were exposed to small molecule chemical probes, different effects were observed across the two models. For example, a previously disclosed sulfonamide compound decreased cytoplasmic TDP-43 and increased soluble levels of stress granule marker TIA-1 in the cellular stress model without impacting these levels in the mutant cell line. This study highlights the challenges of using cellular models in lead development during drug discovery for ALS and FTD and reinforces the need to perform assessments of novel therapeutics across a variety of cell lines and aetiological models.

Indexed as

Amyotrophic Lateral SclerosisFrontotemporal DementiaTDP-43 ProteinopathiesArsenitesDrug DiscoveryHumansSodium CompoundsArsenitessodium arseniteSodium Compoundsamyotrophic lateral sclerosisfrontotemporal dementiaproteinopathystress granulesTDP-43

Identifiers

PMID36499097
PMCPMC9738080
OpenAlexW4310030152

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.