Evidence map›Paper›PMID 38861223›Full record

ArticleNeuromolecular medicine2024

Protein Disulfide Isomerase Endoplasmic Reticulum Protein 57 (ERp57) is Protective Against ALS-Associated Mutant TDP-43 in Neuronal Cells.

Sonam Parakh, Emma R Perri, Marta Vidal, Zeinab Takalloo, Cyril J Jagaraj, Prachi Mehta, Shu Yang, Colleen J Thomas, Ian P Blair, Yuning Hong and 1 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Neuromolecular medicine, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
–field-weighted citation impact
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

4 citing papers in PubMed.

  1. Article
  2. Article
  3. Spatial protein redistribution: wandering but not lost.Cellular and molecular life sciences : CMLS · 2025
    Review
  4. Review
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

11 authors.

Sonam ParakhMotor Neuron Disease Research Centre, Macquarie Medical School, Faculty of Medicine, Health and Human Sciences, Macquarie University, Sydney, 2109, Australia.
Emma R PerriMotor Neuron Disease Research Centre, Macquarie Medical School, Faculty of Medicine, Health and Human Sciences, Macquarie University, Sydney, 2109, Australia.
Marta VidalMotor Neuron Disease Research Centre, Macquarie Medical School, Faculty of Medicine, Health and Human Sciences, Macquarie University, Sydney, 2109, Australia.
Zeinab TakallooMotor Neuron Disease Research Centre, Macquarie Medical School, Faculty of Medicine, Health and Human Sciences, Macquarie University, Sydney, 2109, Australia.
Cyril J JagarajMotor Neuron Disease Research Centre, Macquarie Medical School, Faculty of Medicine, Health and Human Sciences, Macquarie University, Sydney, 2109, Australia.
Prachi MehtaMotor Neuron Disease Research Centre, Macquarie Medical School, Faculty of Medicine, Health and Human Sciences, Macquarie University, Sydney, 2109, Australia.
Shu YangMotor Neuron Disease Research Centre, Macquarie Medical School, Faculty of Medicine, Health and Human Sciences, Macquarie University, Sydney, 2109, Australia.
Colleen J ThomasDepartment of Microbiology, Anatomy, Physiology and Pharmacology, School of Agriculture, Biomedicine and Environment, La Trobe University, Melbourne, VIC, 3086, Australia.
Ian P BlairMotor Neuron Disease Research Centre, Macquarie Medical School, Faculty of Medicine, Health and Human Sciences, Macquarie University, Sydney, 2109, Australia.
Yuning HongLa Trobe Institute for Molecular Science, La Trobe University, Melbourne, VIC, 3086, Australia.
Julie D AtkinMotor Neuron Disease Research Centre, Macquarie Medical School, Faculty of Medicine, Health and Human Sciences, Macquarie University, Sydney, 2109, Australia. julie.atkin@mq.edu.au.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Amyotrophic Lateral Sclerosis (ALS) is a severe neurodegenerative disease affecting motor neurons. Pathological forms of Tar-DNA binding protein-43 (TDP-43), involving its mislocalisation to the cytoplasm and the formation of misfolded inclusions, are present in almost all ALS cases (97%), and ~ 50% cases of the related condition, frontotemporal dementia (FTD), highlighting its importance in neurodegeneration. Previous studies have shown that endoplasmic reticulum protein 57 (ERp57), a member of the protein disulphide isomerase (PDI) family of redox chaperones, is protective against ALS-linked mutant superoxide dismutase (SOD1) in neuronal cells and transgenic SOD1

Indexed as

Amyotrophic Lateral SclerosisDNA-Binding ProteinsInclusion BodiesProtein Disulfide-IsomerasesAnimalsCell NucleusCytoplasmHumansMiceMutationNeuronsSuperoxide Dismutase-1DNA-Binding ProteinsPDIA3 protein, humanProtein Disulfide-IsomerasesSuperoxide Dismutase-1TARDBP protein, humanALS—Amyotrophic lateral sclerosisERp57—Endoplasmic reticulum protein 57ER stressPDI—Protein disulphide isomeraseTDP-43 pathology

Identifiers

PMID38861223
PMCPMC11166824

What OpenQuestion holds

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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.