Evidence map›Paper›PMID 25834780›Full record

ArticleFEBS open bio2015

Oligomer-dependent and -independent chaperone activity of sHsps in different stressed conditions.

Liang Liu, Jiyun Chen, Bo Yang, Yonghua Wang

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in FEBS open bio, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Review
  2. Domain interactions determine the conformational ensemble of the periplasmic chaperone SurA.Protein science : a publication of the Protein Society · 2020
    Article
  3. Article
  4. 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

4 authors.

Liang LiuSchool of Bioscience and Bioengineering, South China University of Technology, Guangzhou 510006, China.
Jiyun ChenInstitute of Systems Biomedicine and Department of Biophysics, School of Basic Medical Sciences, Peking University Health Science Center, Beijing 100191, China.
Bo YangSchool of Bioscience and Bioengineering, South China University of Technology, Guangzhou 510006, China.
Yonghua WangCollege of Light Industry and Food Sciences, South China University of Technology, Guangzhou 510641, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A great number of studies have proven that sHsps protect cells by inhibiting protein aggregation under heat stress, while little is known about their function to protect cells under acid stress. In this work, we show that Hsp20.1 and Hsp14.1 oligomers dissociated to smaller oligomeric species or even dimer/monomer at low pH (pH 4.0 and pH 2.0), whereas no prominent quaternary structural changes were seen at 50 °C. Both oligomers and smaller oligomeric species exhibited abilities to suppress client aggregation at low pH and at 50 °C. These results suggest that sHsps may function in different modes in different stressed conditions.

Indexed as

Acid stressCTE, C-terminal extensionEM, electron microscopyHsp14.0, Sulfolobus tokodaii heat shock protein 14.0Hsp14.1, Sulfolobus solfataricus heat shock 14.1Hsp20.1, Sulfolobus solfataricus heat shock 20.1MDH, malate dehydrogenaseMolecular chaperoneSEC, size exclusion chromatographysHsps, small heat shock proteinsSmall heat shock protein (sHsp)Temperature stress

Identifiers

PMID25834780
PMCPMC4359974

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Registered trials

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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.