Evidence map›Paper›PMID 29853641›Full record

ArticleThe Journal of biological chemistry2018

A hydrophobic low-complexity region regulates aggregation of the yeast pyruvate kinase Cdc19 into amyloid-like aggregates

Erica Grignaschi, Gea Cereghetti, Fulvio Grigolato, Marie R G Kopp, Stefano Caimi, Lenka Faltova, Shady Saad, Matthias Peter, Paolo Arosio

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

14 citing papers in PubMed, 34 citations in OpenAlex.

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  8. Protein aggregation and the evolution of stress resistance in clinical yeast.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2021
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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

9 authors at 1 institution in 1 country.

Erica GrignaschiDepartment of Chemistry and Applied Biosciences, Institute for Chemical and Bioengineering, ETH Zurich, 8093 Zurich, Switzerland.
Gea CereghettiDepartment of Biology, Institute for Biochemistry, ETH Zurich, 8093 Zurich, Switzerland.
Fulvio GrigolatoDepartment of Chemistry and Applied Biosciences, Institute for Chemical and Bioengineering, ETH Zurich, 8093 Zurich, Switzerland.
Marie R G KoppDepartment of Chemistry and Applied Biosciences, Institute for Chemical and Bioengineering, ETH Zurich, 8093 Zurich, Switzerland.
Stefano CaimiDepartment of Chemistry and Applied Biosciences, Institute for Chemical and Bioengineering, ETH Zurich, 8093 Zurich, Switzerland.
Lenka FaltovaDepartment of Chemistry and Applied Biosciences, Institute for Chemical and Bioengineering, ETH Zurich, 8093 Zurich, Switzerland.
Shady SaadDepartment of Biology, Institute for Biochemistry, ETH Zurich, 8093 Zurich, Switzerland.
Matthias PeterDepartment of Biology, Institute for Biochemistry, ETH Zurich, 8093 Zurich, Switzerland.
Paolo ArosioDepartment of Chemistry and Applied Biosciences, Institute for Chemical and Bioengineering, ETH Zurich, 8093 Zurich, Switzerland. Electronic address: paolo.arosio@chem.ethz.ch.
ETH Zurich · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cells form stress granules (SGs) upon stress stimuli to protect sensitive proteins and RNA from degradation. In the yeast

Indexed as

Alzheimer DiseaseAmyloidAmyloid beta-PeptidesCell Cycle ProteinsHumansHydrophobic and Hydrophilic InteractionsInsulinPeptide FragmentsProtein AggregatesProtein Structure, QuaternaryPyruvate KinaseSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAmyloidAmyloid beta-Peptidesamyloid beta-protein (1-42)Cdc19 protein, S cerevisiaeCell Cycle ProteinsInsulinPeptide FragmentsProtein AggregatesPyruvate KinaseSaccharomyces cerevisiae Proteinsamyloidogenic proteinAβ42cell compartmentalizationfunctional amyloidshydrophobic-hydrophilic interfaceprotein aggregationprotein-nucleic acid interactionprotein-protein interactionprotein self-assemblystress granule

Identifiers

PMID29853641
PMCPMC6065187
OpenAlexW2805813833

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.