Evidence map›Paper›PMID 37238710›Full record

ReviewBiomolecules2023

The Effect of Calorie Restriction on Protein Quality Control in Yeast.

Petter Uvdal, Sviatlana Shashkova

Open access · goldAbstract readReview
In one paragraph

Review in Biomolecules, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
1.0field-weighted citation impact, top 25% 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

4 citing papers in PubMed, 5 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. 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

2 authors at 1 institution in 1 country.

Petter UvdalDepartment of Physics, University of Gothenburg, 405 30 Göteborg, Sweden.
Sviatlana ShashkovaDepartment of Physics, University of Gothenburg, 405 30 Göteborg, Sweden.ORCID 0000-0002-4641-3295
University of Gothenburg · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Initially, protein aggregates were regarded as a sign of a pathological state of the cell. Later, it was found that these assemblies are formed in response to stress, and that some of them serve as signalling mechanisms. This review has a particular focus on how intracellular protein aggregates are related to altered metabolism caused by different glucose concentrations in the extracellular environment. We summarise the current knowledge of the role of energy homeostasis signalling pathways in the consequent effect on intracellular protein aggregate accumulation and removal. This covers regulation at different levels, including elevated protein degradation and proteasome activity mediated by the Hxk2 protein, the enhanced ubiquitination of aberrant proteins through Torc1/Sch9 and Msn2/Whi2, and the activation of autophagy mediated through

Indexed as

Saccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsCaloric RestrictionDNA-Binding ProteinsGlucoseProtein AggregatesTranscription FactorsDNA-Binding ProteinsGlucoseMSN2 protein, S cerevisiaeProtein AggregatesSaccharomyces cerevisiae ProteinsTranscription FactorsWhi2 protein, S cerevisiaeage-related diseasesautophagycalorie restrictioncarbon metabolismdegradationHsp104misfolded proteinsneurodegenerative diseasesprotein aggregationprotein quality controlSaccharomyces cerevisiaestress responseyeast

Identifiers

PMID37238710
PMCPMC10216387
OpenAlexW4376644230

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.