Evidence map›Paper›PMID 20944667›Full record

ReviewNature reviews. Molecular cell biology2010

Cellular strategies for controlling protein aggregation.

Jens Tyedmers, Axel Mogk, Bernd Bukau

Abstract readReview
PubMed Publisher
In one paragraph

Review in Nature reviews. Molecular cell biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 434 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
434citing papers in PubMed, 1 pooled it
–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

434 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Review
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  9. Hsp70s regulate circadian rhythm by interacting with PERIOD.Cell communication and signaling : CCS · 2026
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374 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.

Jens TyedmersZentrum für Molekulare Biologie der Universität Heidelberg (ZMBH), DKFZ-ZMBH Alliance, Im Neuenheimer Feld 282, D-69,120 Heidelberg, Germany. j.tyedmers@zmbh.uni-heidelberg.de
Axel Mogk
Bernd Bukau

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The aggregation of misfolded proteins is associated with the perturbation of cellular function, ageing and various human disorders. Mounting evidence suggests that protein aggregation is often part of the cellular response to an imbalanced protein homeostasis rather than an unspecific and uncontrolled dead-end pathway. It is a regulated process in cells from bacteria to humans, leading to the deposition of aggregates at specific sites. The sequestration of misfolded proteins in such a way is protective for cell function as it allows for their efficient solubilization and refolding or degradation by components of the protein quality-control network. The organized aggregation of misfolded proteins might also allow their asymmetric distribution to daughter cells during cell division.

Indexed as

Protein FoldingAnimalsAutophagyCell Physiological PhenomenaHeat-Shock ProteinsHumansModels, BiologicalModels, MolecularProteasome Endopeptidase ComplexProteinsHeat-Shock ProteinsProteasome Endopeptidase ComplexProteins

Identifiers

PMID20944667

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.