Evidence map›Paper›PMID 24386013›Full record

ArticleJournal of chemical biology2013

Transient conformational remodeling of folding proteins by GroES-individually and in concert with GroEL.

Satish Babu Moparthi, Daniel Sjölander, Laila Villebeck, Bengt-Harald Jonsson, Per Hammarström, Uno Carlsson

Abstract read
In one paragraph

Article in Journal of chemical biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing 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

5 citing papers in PubMed.

  1. Heat shock protein 10 as a chaperone modulating α-synuclein amyloid fibril formation.Protein science : a publication of the Protein Society · 2026
    Article
  2. Article
  3. Frontiers in microbiology · 2017
    Article
  4. Article
  5. 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

6 authors.

Satish Babu MoparthiIFM-Department of Chemistry, Linköping University, 581 83 Linköping, Sweden ; Institut Fresnel, CNRS UMR 7249, Aix-Marseille Université, Ecole Centrale Marseille, Marseille, France.
Daniel SjölanderIFM-Department of Chemistry, Linköping University, 581 83 Linköping, Sweden.
Laila VillebeckIFM-Department of Chemistry, Linköping University, 581 83 Linköping, Sweden.
Bengt-Harald JonssonIFM-Department of Chemistry, Linköping University, 581 83 Linköping, Sweden.
Per HammarströmIFM-Department of Chemistry, Linköping University, 581 83 Linköping, Sweden.
Uno CarlssonIFM-Department of Chemistry, Linköping University, 581 83 Linköping, Sweden.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The commonly accepted dogma of the bacterial GroE chaperonin system entails protein folding mediated by cycles of several ATP-dependent sequential steps where GroEL interacts with the folding client protein. In contrast, we herein report GroES-mediated dynamic remodeling (expansion and compression) of two different protein substrates during folding: the endogenous substrate MreB and carbonic anhydrase (HCAII), a well-characterized protein folding model. GroES was also found to influence GroEL binding induced unfolding and compression of the client protein underlining the synergistic activity of both chaperonins, even in the absence of ATP. This previously unidentified activity by GroES should have important implications for understanding the chaperonin mechanism and cellular stress response. Our findings necessitate a revision of the GroEL/ES mechanism.

Indexed as

Carbonic anhydraseChaperoneFRETMolten globuleMreBProtein folding

Identifiers

PMID24386013
PMCPMC3877409

What OpenQuestion holds

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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.