Evidence map›Paper›PMID 24563850›Full record

ReviewRedox biology2014

Molecular chaperones and proteostasis regulation during redox imbalance.

Katerina Niforou, Christina Cheimonidou, Ioannis P Trougakos

Open access · goldAbstract readReview
In one paragraph

Review in Redox biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 111 papers.

0numbers the graph read from it
0cells of the map it votes in
111citing papers in PubMed
11.7field-weighted citation impact, top 1% 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

111 citing papers in PubMed, 241 citations in OpenAlex.

  1. Article
  2. Review
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  17. Biomedicines · 2024
    Article
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    Article
  19. Article
  20. Article

51 more citing papers are in PubMed but not listed here.

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

3 authors at 1 institution in 1 country.

Katerina NiforouDepartment of Cell Biology and Biophysics, Faculty of Biology, University of Athens, Panepistimiopolis, Athens 15784, Greece.
Christina CheimonidouDepartment of Cell Biology and Biophysics, Faculty of Biology, University of Athens, Panepistimiopolis, Athens 15784, Greece.
Ioannis P TrougakosDepartment of Cell Biology and Biophysics, Faculty of Biology, University of Athens, Panepistimiopolis, Athens 15784, Greece.
National and Kapodistrian University of Athens · GR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Free radicals originate from both exogenous environmental sources and as by-products of the respiratory chain and cellular oxygen metabolism. Sustained accumulation of free radicals, beyond a physiological level, induces oxidative stress that is harmful for the cellular homeodynamics as it promotes the oxidative damage and stochastic modification of all cellular biomolecules including proteins. In relation to proteome stability and maintenance, the increased concentration of oxidants disrupts the functionality of cellular protein machines resulting eventually in proteotoxic stress and the deregulation of the proteostasis (homeostasis of the proteome) network (PN). PN curates the proteome in the various cellular compartments and the extracellular milieu by modulating protein synthesis and protein machines assembly, protein recycling and stress responses, as well as refolding or degradation of damaged proteins. Molecular chaperones are key players of the PN since they facilitate folding of nascent polypeptides, as well as holding, folding, and/or degradation of unfolded, misfolded, or non-native proteins. Therefore, the expression and the activity of the molecular chaperones are tightly regulated at both the transcriptional and post-translational level at organismal states of increased oxidative and, consequently, proteotoxic stress, including ageing and various age-related diseases (e.g. degenerative diseases and cancer). In the current review we present a synopsis of the various classes of intra- and extracellular chaperones, the effects of oxidants on cellular homeodynamics and diseases and the redox regulation of chaperones.

Indexed as

AnimalsElectron TransportEndoplasmic ReticulumEndoplasmic Reticulum Chaperone BiPFree RadicalsHeat-Shock ProteinsHomeostasisHumansModels, BiologicalMolecular ChaperonesOxidantsOxidation-ReductionOxidative StressProteasome Endopeptidase ComplexProtein FoldingProtein Processing, Post-TranslationalEndoplasmic Reticulum Chaperone BiPFree RadicalsHeat-Shock ProteinsHSPA5 protein, humanMolecular ChaperonesOxidantsProteasome Endopeptidase ComplexProteinsProteomeReactive Nitrogen SpeciesReactive Oxygen SpeciesAGEs, Advanced Glycation End ProductsALS, Autophagy Lysosome SystemAP-1, Activator Protein-1ChaperonesCLU, apolipoprotein J/ClusterinDiseasesEPMs, Enzymatic Protein ModificationsERAD, ER-Associated protein DegradationER, Endoplasmic ReticulumFree radicalsGPx7, Glutathione Peroxidase 7GRP78, Glucose Regulated Protein of 78 kDaHb, HaemoglobinHSF1, Heat Shock transcription Factor-1HSP, Heat Shock ProteinKeap1, Kelch-like ECH-associated protein 1NADH, Nicotinamide Adenine DinucleotideNEPMs, Non-Enzymatic Protein ModificationsNOS, Nitric Oxide SynthaseNOx, NAD(P)H OxidaseNrf2, NF-E2-related factor 2Oxidative stressPDI, Protein Disulfide IsomerasePDR, Proteome Damage ResponsesPN, Proteostasis NetworkProteomeRedox signallingRNS, Reactive Nitrogen SpeciesROS, Reactive Oxygen SpeciesUPR, Unfolded Protein ResponseUPS, Ubiquitin Proteasome Systemα(2)M, α(2)-Macroglobulin

Identifiers

PMID24563850
PMCPMC3926111
OpenAlexW2071645144

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.