Evidence map›Paper›PMID 32029478›Full record

ArticleThe Journal of biological chemistry2020

TNF receptor-associated factor 6 interacts with ALS-linked misfolded superoxide dismutase 1 and promotes aggregation.

Sabrina Semmler, Myriam Gagné, Pranav Garg, Sarah R Pickles, Charlotte Baudouin, Emeline Hamon-Keromen, Laurie Destroismaisons, Yousra Khalfallah, Mathilde Chaineau, Elise Caron and 12 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.6field-weighted citation impact, top 13% 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

13 citing papers in PubMed, 23 citations in OpenAlex.

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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

22 authors at 9 institutions in 3 countries.

Sabrina SemmlerDepartment of Neurology and Neurosurgery, McGill University, Montréal, Quebec H3A 2B4, Canada.
Myriam GagnéCentre de Recherche du Centre Hospitalier de Université de Montréal, Montréal, Quebec H2X 0A9, Canada.
Pranav GargDepartment of Physics and Astronomy, University of British Columbia, Vancouver, British Columbia V6T 1Z1, Canada.ORCID 0000-0002-8591-7664
Sarah R PicklesCentre de Recherche du Centre Hospitalier de Université de Montréal, Montréal, Quebec H2X 0A9, Canada.
Charlotte BaudouinCentre de Recherche du Centre Hospitalier de Université de Montréal, Montréal, Quebec H2X 0A9, Canada.
Emeline Hamon-KeromenCentre de Recherche du Centre Hospitalier de Université de Montréal, Montréal, Quebec H2X 0A9, Canada.
Laurie DestroismaisonsCentre de Recherche du Centre Hospitalier de Université de Montréal, Montréal, Quebec H2X 0A9, Canada.
Yousra KhalfallahCentre de Recherche du Centre Hospitalier de Université de Montréal, Montréal, Quebec H2X 0A9, Canada.
Mathilde ChaineauDepartment of Neurology and Neurosurgery, McGill University, Montréal, Quebec H3A 2B4, Canada.
Elise CaronCentre de Recherche du Centre Hospitalier de Université de Montréal, Montréal, Quebec H2X 0A9, Canada.
Andrew N BayneDepartment of Pharmacology and Therapeutics, McGill University, Montréal, Quebec H3A 2B4, Canada.
Jean-François TrempeDepartment of Pharmacology and Therapeutics, McGill University, Montréal, Quebec H3A 2B4, Canada.
Neil R CashmanDepartment of Medicine (Neurology), University of British Columbia and Vancouver Coastal Health Research Institute, Brain Research Centre, Vancouver, British Columbia V6T 2B5, Canada.ORCID 0000-0002-0080-1006
Alexandra T StarHuman Health Therapeutics Portfolio, National Research Council of Canada, Ottawa, Ontario, K1A 0R6, Canada.
Arsalan S HaqqaniHuman Health Therapeutics Portfolio, National Research Council of Canada, Ottawa, Ontario, K1A 0R6, Canada.
Thomas M DurcanDepartment of Neurology and Neurosurgery, McGill University, Montréal, Quebec H3A 2B4, Canada.
Elizabeth M MeieringDepartment of Chemistry, Guelph-Waterloo Centre for Graduate Work in Chemistry and Biochemistry, University of Waterloo, Waterloo, Ontario N2L 3G1, Canada.
Janice RobertsonTanz Centre for Research in Neurodegenerative Diseases, University of Toronto, Toronto, Ontario M5T 0S8, Canada.
Nathalie GrandvauxCentre de Recherche du Centre Hospitalier de Université de Montréal, Montréal, Quebec H2X 0A9, Canada.
Steven S PlotkinDepartment of Physics and Astronomy, University of British Columbia, Vancouver, British Columbia V6T 1Z1, Canada.
Heidi M McBrideDepartment of Neurology and Neurosurgery, McGill University, Montréal, Quebec H3A 2B4, Canada.
Christine Vande VeldeCentre de Recherche du Centre Hospitalier de Université de Montréal, Montréal, Quebec H2X 0A9, Canada c.vande.velde@umontreal.ca.ORCID 0000-0001-5926-1529
Centre Hospitalier de l’Université de Montréal · CAMontreal Neurological Institute and Hospital · CAMcGill University · CANational Research Council Canada · CAUniversity of British Columbia · CASorbonne Université · FRUniversity of Toronto · CAUniversity of Waterloo · CAVancouver Coastal Health · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Amyotrophic lateral sclerosis (ALS) is a fatal disease, characterized by the selective loss of motor neurons leading to paralysis. Mutations in the gene encoding superoxide dismutase 1 (SOD1) are the second most common cause of familial ALS, and considerable evidence suggests that these mutations result in an increase in toxicity due to protein misfolding. We previously demonstrated in the SOD1

Indexed as

Amyotrophic Lateral SclerosisAnimalsAntibodiesCell LineDisease Models, AnimalMitochondriaMutagenesis, Site-DirectedNF-kappa BProtein AggregatesProtein FoldingRatsRats, TransgenicRNA InterferenceRNA, Small InterferingSuperoxide Dismutase-1TNF Receptor-Associated Factor 6AntibodiesNF-kappa BProtein AggregatesRNA, Small InterferingSuperoxide Dismutase-1TNF Receptor-Associated Factor 6amyotrophic lateral sclerosis (ALS) (Lou Gehrig disease)mitochondriaprotein aggregationprotein misfoldingsuperoxide dismutase (SOD)TNF receptor–associated factor (TRAF)ubiquitin

Identifiers

PMID32029478
PMCPMC7086032
OpenAlexW3005330843

What OpenQuestion holds

Textmetadata
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.