Evidence map›Paper›PMID 32054832›Full record

ArticleNature communications2020

FMN reduces Amyloid-β toxicity in yeast by regulating redox status and cellular metabolism.

Xin Chen, Boyang Ji, Xinxin Hao, Xiaowei Li, Frederik Eisele, Thomas Nyström, Dina Petranovic

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
7.0field-weighted citation impact, top 2% 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

39 citing papers in PubMed, 67 citations in OpenAlex.

  1. Article
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  5. Review
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  8. Article
  9. RewiringMetabolic engineering communications · 2024
    Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Alzheimer's Disease: Significant Benefit from the Yeast-Based Models.International journal of molecular sciences · 2023
    Review
  17. Article
  18. Article
  19. Article
  20. Vitamin B3 Biotech · 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

7 authors at 3 institutions in 2 countries.

Xin ChenDivision of Systems and Synthetic Biology, Department of Biology and Biological Engineering, Chalmers University of Technology, SE41296, Gothenburg, Sweden.ORCID http://orcid.org/0000-0003-2788-1314
Boyang JiDivision of Systems and Synthetic Biology, Department of Biology and Biological Engineering, Chalmers University of Technology, SE41296, Gothenburg, Sweden.
Xinxin HaoInstitute for Biomedicine, Sahlgrenska Academy, Centre for Ageing and Health-AgeCap, University of Gothenburg, SE40530, Gothenburg, Sweden.ORCID http://orcid.org/0000-0001-5758-6290
Xiaowei LiDivision of Systems and Synthetic Biology, Department of Biology and Biological Engineering, Chalmers University of Technology, SE41296, Gothenburg, Sweden.
Frederik EiseleInstitute for Biomedicine, Sahlgrenska Academy, Centre for Ageing and Health-AgeCap, University of Gothenburg, SE40530, Gothenburg, Sweden.ORCID http://orcid.org/0000-0001-9995-5816
Thomas NyströmInstitute for Biomedicine, Sahlgrenska Academy, Centre for Ageing and Health-AgeCap, University of Gothenburg, SE40530, Gothenburg, Sweden.ORCID http://orcid.org/0000-0001-5489-2903
Dina PetranovicDivision of Systems and Synthetic Biology, Department of Biology and Biological Engineering, Chalmers University of Technology, SE41296, Gothenburg, Sweden. dina.petranovic@chalmers.se.
Chalmers University of Technology · SEUniversity of Gothenburg · SENovo Nordisk Foundation · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Alzheimer's disease (AD) is defined by progressive neurodegeneration, with oligomerization and aggregation of amyloid-β peptides (Aβ) playing a pivotal role in its pathogenesis. In recent years, the yeast Saccharomyces cerevisiae has been successfully used to clarify the roles of different human proteins involved in neurodegeneration. Here, we report a genome-wide synthetic genetic interaction array to identify toxicity modifiers of Aβ42, using yeast as the model organism. We find that FMN1, the gene encoding riboflavin kinase, and its metabolic product flavin mononucleotide (FMN) reduce Aβ42 toxicity. Classic experimental analyses combined with RNAseq show the effects of FMN supplementation to include reducing misfolded protein load, altering cellular metabolism, increasing NADH/(NADH + NAD

Indexed as

alpha-SynucleinAlzheimer DiseaseAmyloid beta-PeptidesFlavin MononucleotideGenes, SyntheticGenome, FungalHumansHuntingtin ProteinModels, GeneticMutationOxidation-ReductionOxidoreductasesPeptide FragmentsPhosphotransferases (Alcohol Group Acceptor)Protein FoldingProteolysisalpha-SynucleinAmyloid beta-Peptidesamyloid beta-protein (1-42)Flavin MononucleotideHTT protein, humanHuntingtin ProteinOxidoreductasesPeptide FragmentsPhosphotransferases (Alcohol Group Acceptor)Riboflavinriboflavin kinaseSaccharomyces cerevisiae ProteinsSMM1 protein, S cerevisiae

Identifiers

PMID32054832
PMCPMC7018843
OpenAlexW3006584233

What Socratic 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 Socratic graph.