Evidence map›Paper›PMID 35245117›Full record

ArticleScience advances2022

Protein chain collapse modulation and folding stimulation by GroEL-ES.

Mohsin M Naqvi, Mario J Avellaneda, Andrew Roth, Eline J Koers, Antoine Roland, Vanda Sunderlikova, Günter Kramer, Hays S Rye, Sander J Tans

Open access · goldAbstract read
In one paragraph

Article in Science advances, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.3field-weighted citation impact, top 11% of its field
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

17 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
  2. Calmodulin assists during co-translational folding of the KProtein science : a publication of the Protein Society · 2026
    Article
  3. Article
  4. Article
  5. Review
  6. Trigger factor accelerates nascent chain compaction and folding.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. Article
  8. G-quadruplexes catalyze protein folding by reshaping the energetic landscape.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  9. Article
  10. Article
  11. Article
  12. Review
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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

9 authors at 3 institutions in 3 countries.

Mohsin M NaqviAMOLF, Science Park 104, 1098 XG Amsterdam, Netherlands.ORCID 0000-0002-4358-4195
Mario J AvellanedaAMOLF, Science Park 104, 1098 XG Amsterdam, Netherlands.ORCID 0000-0001-6406-524X
Andrew RothDepartment of Biochemistry and Biophysics, Texas A&M University, College Station, TX 77845, USA.ORCID 0000-0002-5490-8634
Eline J KoersAMOLF, Science Park 104, 1098 XG Amsterdam, Netherlands.ORCID 0000-0002-5352-9069
Antoine RolandAMOLF, Science Park 104, 1098 XG Amsterdam, Netherlands.
Vanda SunderlikovaAMOLF, Science Park 104, 1098 XG Amsterdam, Netherlands.
Günter KramerCenter for Molecular Biology of Heidelberg University (ZMBH), DKFZ-ZMBH Alliance, Im Neuenheimer Feld 282, Heidelberg D-69120, Germany.ORCID 0000-0001-7552-8393
Hays S RyeDepartment of Biochemistry and Biophysics, Texas A&M University, College Station, TX 77845, USA.ORCID 0000-0002-9420-3137
Sander J TansAMOLF, Science Park 104, 1098 XG Amsterdam, Netherlands.ORCID 0000-0002-7131-2568
Institute for Atomic and Molecular Physics · NLTexas A&M University · USGerman Cancer Research Center · DE

Funding

Mechanisms of Chaperonin-Mediated Protein FoldingR01GM065421 · NIGMS · TEXAS A&M UNIVERSITY · PI RYE, HAYS S · 2003 to 2013
$2.5M
Mechanism of protein aggregate recognition and disassembly by molecular chaperonesR01GM134063 · NIGMS · TEXAS A&M AGRILIFE RESEARCH · PI RYE, HAYS S · 2019 to 2022
$1.4M
Mechanism of membrane fission at the recycling endosomeR01GM114405 · NIGMS · TEXAS A&M AGRILIFE RESEARCH · PI RYE, HAYS S · 2015 to 2018
$1.2M
NIGMS NIH HHS R01 GM065421NIGMS NIH HHS R01 GM114405NIGMS NIH HHS R01 GM134063
6 · The paper itself

Abstract

The collapse of polypeptides is thought important to protein folding, aggregation, intrinsic disorder, and phase separation. However, whether polypeptide collapse is modulated in cells to control protein states is unclear. Here, using integrated protein manipulation and imaging, we show that the chaperonin GroEL-ES can accelerate the folding of proteins by strengthening their collapse. GroEL induces contractile forces in substrate chains, which draws them into the cavity and triggers a general compaction and discrete folding transitions, even for slow-folding proteins. This collapse enhancement is strongest in the nucleotide-bound states of GroEL and is aided by GroES binding to the cavity rim and by the amphiphilic C-terminal tails at the cavity bottom. Collapse modulation is distinct from other proposed GroEL-ES folding acceleration mechanisms, including steric confinement and misfold unfolding. Given the prevalence of collapse throughout the proteome, we conjecture that collapse modulation is more generally relevant within the protein quality control machinery.

Identifiers

PMID35245117
PMCPMC8896798
OpenAlexW4220891546

What OpenQuestion holds

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LicenceCC BY-NC
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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.