Evidence map›Paper›PMID 30863976›Full record

ArticleActa neuropathologica2019

The molecular pathogenesis of superoxide dismutase 1-linked ALS is promoted by low oxygen tension.

Isil Keskin, Elin Forsgren, Manuela Lehmann, Peter M Andersen, Thomas Brännström, Dale J Lange, Matthis Synofzik, Ulrika Nordström, Per Zetterström, Stefan L Marklund and 1 more

Open access · hybridAbstract read
In one paragraph

Article in Acta neuropathologica, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
2.5field-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

11 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
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  11. Risk Factors and Emerging Therapies in Amyotrophic Lateral Sclerosis.International journal of molecular sciences · 2019
    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 at 3 institutions in 3 countries.

Isil KeskinDepartment of Medical Biosciences, Pathology, Umeå University, 90185, Umeå, Sweden.
Elin ForsgrenDepartment of Pharmacology and Clinical Neuroscience, Umeå University, 90187, Umeå, Sweden.
Manuela LehmannDepartment of Pharmacology and Clinical Neuroscience, Umeå University, 90187, Umeå, Sweden.
Peter M AndersenDepartment of Pharmacology and Clinical Neuroscience, Umeå University, 90187, Umeå, Sweden.
Thomas BrännströmDepartment of Medical Biosciences, Pathology, Umeå University, 90185, Umeå, Sweden.
Dale J LangeDepartment of Neurology, Hospital for Special Surgery and Weill Cornell Medical Center, New York, NY, 10021, USA.
Matthis SynofzikDepartment of Neurodegenerative Diseases, Hertie Institute for Clinical Brain Research, University of Tübingen, Tübingen, Germany.
Ulrika NordströmDepartment of Pharmacology and Clinical Neuroscience, Umeå University, 90187, Umeå, Sweden.
Per ZetterströmDepartment of Medical Biosciences, Clinical Chemistry, Umeå University, 90185, Umeå, Sweden.
Stefan L MarklundDepartment of Medical Biosciences, Clinical Chemistry, Umeå University, 90185, Umeå, Sweden. stefan.marklund@umu.se.
Jonathan D GilthorpeDepartment of Pharmacology and Clinical Neuroscience, Umeå University, 90187, Umeå, Sweden. jonathan.gilthorpe@umu.se.ORCID 0000-0002-6884-4774
Umeå University · SEGerman Center for Neurodegenerative Diseases · DEHospital for Special Surgery · US

Funding

Bertil Hållstens Forskningsstiftelse NAElse Kröner-Fresenius-Stiftung NAHjärnfonden FO2015-0234Kempestiftelserna NAKnut och Alice Wallenbergs Stiftelse 2012.0091Neuroförbundet NAStratneuro (SE) NATorsten Söderbergs Stiftelse NAUlla-Carin Lindquist Stiftelse (SE) NAVästerbotten Läns Landsting NAVetenskapsrådet 2015-02804
6 · The paper itself

Abstract

Mutations in superoxide dismutase 1 (SOD1) cause amyotrophic lateral sclerosis (ALS). Disease pathogenesis is linked to destabilization, disorder and aggregation of the SOD1 protein. However, the non-genetic factors that promote disorder and the subsequent aggregation of SOD1 have not been studied. Mainly located to the reducing cytosol, mature SOD1 contains an oxidized disulfide bond that is important for its stability. Since O

Indexed as

Amyotrophic Lateral SclerosisFibroblastsHumansMotor NeuronsMutationOxygenSuperoxide Dismutase-1OxygenSuperoxide Dismutase-1Amyotrophic lateral sclerosis (ALS)Disulfide bondOxygen tensionPatient-derived cellsProtein aggregationProtein disorderSuperoxide dismutase 1 (SOD1)

Identifiers

PMID30863976
PMCPMC6570705
OpenAlexW2951838907

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.