Evidence map›Paper›PMID 20965419›Full record

ReviewMolecular cell2010

Protein quality control in the cytosol and the endoplasmic reticulum: brothers in arms.

Alexander Buchberger, Bernd Bukau, Thomas Sommer

Abstract readReview
PubMed Publisher
In one paragraph

Review in Molecular cell, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 266 papers.

0numbers the graph read from it
0cells of the map it votes in
266citing papers in PubMed
–field-weighted citation impact
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

266 citing papers in PubMed.

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  4. Mechanisms suppressing noncoding translation.Trends in cell biology · 2025
    Review
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206 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors.

Alexander BuchbergerDepartment of Biochemistry, Biocenter, University of Würzburg, Am Hubland, 97074 Würzburg, Germany. alexander.buchberger@biozentrum.uni-wuerzburg.de
Bernd Bukau
Thomas Sommer

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In cells, both newly synthesized and pre-existing proteins are constantly endangered by misfolding and aggregation. The accumulation of damaged proteins can perturb cellular homeostasis and provoke aging, pathological states, and even cell death. To avert these dangers, cells have developed powerful quality control strategies that counteract protein damage in a compartment-specific way. Here, we compare the protein quality control systems of the eukaryotic cytosol and the endoplasmic reticulum, focusing on the principles of damage recognition, the triage decisions between chaperone-mediated refolding and proteolytic elimination of damaged proteins, the repair of misfolded and aggregated protein species, and the mechanisms by which perturbations of protein homeostasis are sensed to induce compartment-specific stress responses.

Indexed as

AnimalsCytosolEndoplasmic ReticulumEukaryotic CellsHomeostasisHumansModels, BiologicalMolecular ChaperonesProtein FoldingProteinsMolecular ChaperonesProteins

Identifiers

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.