Evidence map›Paper›PMID 27386166›Full record

ReviewWorm

Interplay between redox and protein homeostasis.

Diogo R Feleciano, Kristin Arnsburg, Janine Kirstein

Open access · bronzeAbstract readReview
In one paragraph

Review in Worm. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
0.9field-weighted citation impact, top 26% 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

10 citing papers in PubMed, 14 citations in OpenAlex.

  1. Targeting proteostasis pathways for cancer therapy.Journal of pharmaceutical analysis · 2025
    Review
  2. Article
  3. Review
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  5. Review
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  10. Long-Term Exercise Protects against Cellular Stresses in Aged Mice.Oxidative medicine and cellular longevity · 2018
    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

3 authors at 1 institution in 1 country.

Diogo R FelecianoLeibniz-Institut für Molekulare Pharmakologie im Forschungsverbund Berlin e.V. , Berlin, Germany.
Kristin ArnsburgLeibniz-Institut für Molekulare Pharmakologie im Forschungsverbund Berlin e.V. , Berlin, Germany.
Janine KirsteinLeibniz-Institut für Molekulare Pharmakologie im Forschungsverbund Berlin e.V. , Berlin, Germany.
Forschungsverbund Berlin · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The subcellular compartments of eukaryotic cells are characterized by different redox environments. Whereas the cytosol, nucleus and mitochondria are more reducing, the endoplasmic reticulum represents a more oxidizing environment. As the redox level controls the formation of intra- and inter-molecular disulfide bonds, the folding of proteins is tightly linked to its environment. The proteostasis network of each compartment needs to be adapted to the compartmental redox properties. In addition to chaperones, also members of the thioredoxin superfamily can influence the folding of proteins by regulation of cysteine reduction/oxidation. This review will focus on thioredoxin superfamily members and chaperones of C. elegans, which play an important role at the interface between redox and protein homeostasis. Additionally, this review will highlight recent methodological developments on in vivo and in vitro assessment of the redox state and their application to provide insights into the high complexity of redox and proteostasis networks of C. elegans.

Indexed as

agingchaperonesendoplasmic reticulumERO-1PDIproteostasisredox homeostasisthioredoxintrx-domainunfolded protein response

Identifiers

PMID27386166
PMCPMC4911977
OpenAlexW2324341023

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.