Evidence map›Paper›PMID 24084862›Full record

ArticleNature cell biology2013

Q-bodies monitor the quinary state of the protein fold.

Daniela Martino Roth, William E Balch

Abstract readNews
PubMed Publisher
In one paragraph

Article in Nature cell biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing 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

6 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. 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

2 authors.

Daniela Martino RothThe Scripps Research Institute, Department of Cell and Molecular Biology, 10555 North Torrey Pines Road, La Jolla, California 92037, USA.
William E Balch

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cytoplasmic compartments containing misfolded proteins targeted for degradation, named Q-bodies, have been identified. Q-body formation is a dynamic process that actively manages the metastable state of the protein fold through small heat shock proteins and the Hsp70-Hsp90-Hsp110 proteostasis system to promote cellular fitness under both physiological and stress conditions.

Indexed as

Protein FoldingAnimalsHeat-Shock ProteinsHumansProteinsProtein StabilityProteolysisSignal TransductionHeat-Shock ProteinsProteins

Identifiers

PMID24084862

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.