Evidence map›Paper›PMID 34830074›Full record

ReviewInternational journal of molecular sciences2021

Metals in ALS TDP-43 Pathology.

Lassi Koski, Cecilia Ronnevi, Elina Berntsson, Sebastian K T S Wärmländer, Per M Roos

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed, 1 pooled it
2.0field-weighted citation impact, top 11% 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

18 citing papers in PubMed, 1 synthesis or guideline pooled it, 28 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Review
  5. Review
  6. Review
  7. Article
  8. Review
  9. Review
  10. Article
  11. Review
  12. Consequences of Disturbing Manganese Homeostasis.International journal of molecular sciences · 2023
    Review
  13. Review
  14. Article
  15. Article
  16. Studying Peptide-Metal Ion Complex Structures by Solution-State NMR.International journal of molecular sciences · 2022
    Review
  17. Review
  18. 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

5 authors at 4 institutions in 2 countries.

Lassi KoskiInstitute of Environmental Medicine, Karolinska Institutet, 171 77 Stockholm, Sweden.
Cecilia RonneviCapio St. Göran Hospital, 112 19 Stockholm, Sweden.
Elina BerntssonDepartment of Biochemistry and Biophysics, Stockholm University, 106 91 Stockholm, Sweden.
Sebastian K T S WärmländerDepartment of Biochemistry and Biophysics, Stockholm University, 106 91 Stockholm, Sweden.
Per M RoosInstitute of Environmental Medicine, Karolinska Institutet, 171 77 Stockholm, Sweden.ORCID 0000-0003-3202-9687
Karolinska Institutet · SESaint Göran Hospital · SEStockholm University · SETallinn University of Technology · EE

Funding

Kamprad Research Foundation 001Karolinska Institutet IMM strategic grants 001Magnus Bergvall foundation 001Ulla-Carin Lindquist Foundation for ALS Research 001
6 · The paper itself

Abstract

Amyotrophic lateral sclerosis (ALS), Alzheimer's disease, Parkinson's disease and similar neurodegenerative disorders take their toll on patients, caregivers and society. A common denominator for these disorders is the accumulation of aggregated proteins in nerve cells, yet the triggers for these aggregation processes are currently unknown. In ALS, protein aggregation has been described for the SOD1, C9orf72, FUS and TDP-43 proteins. The latter is a nuclear protein normally binding to both DNA and RNA, contributing to gene expression and mRNA life cycle regulation. TDP-43 seems to have a specific role in ALS pathogenesis, and ubiquitinated and hyperphosphorylated cytoplasmic inclusions of aggregated TDP-43 are present in nerve cells in almost all sporadic ALS cases. ALS pathology appears to include metal imbalances, and environmental metal exposure is a known risk factor in ALS. However, studies on metal-to-TDP-43 interactions are scarce, even though this protein seems to have the capacity to bind to metals. This review discusses the possible role of metals in TDP-43 aggregation, with respect to ALS pathology.

Indexed as

Amyotrophic Lateral SclerosisMetalsMutationC9orf72 ProteinDNA-Binding ProteinsEnvironmental ExposureHumansProtein Aggregation, PathologicalRNA-Binding Protein FUSSuperoxide Dismutase-1C9orf72 ProteinC9orf72 protein, humanDNA-Binding ProteinsFUS protein, humanMetalsRNA-Binding Protein FUSSOD1 protein, humanSuperoxide Dismutase-1TARDBP protein, humanamyloidmetal exposuremetallopathymetal–protein bindingneurodegenerationprotein aggregationproteinopathy

Identifiers

PMID34830074
PMCPMC8622279
OpenAlexW3213606763

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.