Evidence map›Paper›PMID 36764293›Full record

ArticleCell2023

A molecular device for the redox quality control of GroEL/ES substrates.

Emile Dupuy, Sander Egbert Van der Verren, Jiusheng Lin, Mark Alan Wilson, Alix Vincent Dachsbeck, Felipe Viela, Emmanuelle Latour, Alexandra Gennaris, Didier Vertommen, Yves Frédéric Dufrêne and 4 more

Open access · greenAbstract read
In one paragraph

Article in Cell, 2023. 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
2.9field-weighted citation impact, top 9% 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

4 citing papers in PubMed, 19 citations in OpenAlex.

  1. Article
  2. Heterologous production of epothilones inSynthetic and systems biotechnology · 2026
    Article
  3. Review
  4. Review
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

14 authors at 5 institutions in 4 countries.

Emile DupuyWELBIO, Avenue Hippocrate 75, 1200 Brussels, Belgium; de Duve Institute, Université catholique de Louvain, Avenue Hippocrate 75, 1200 Brussels, Belgium.
Sander Egbert Van der VerrenStructural Biology Brussels, Vrije Universiteit Brussel, 1050 Brussels, Belgium; Structural and Molecular Microbiology, Structural Biology Research Center, VIB, 1050 Brussels, Belgium.
Jiusheng LinDepartment of Biochemistry and the Redox Biology Center, University of Nebraska, Lincoln, NE 68588, USA.
Mark Alan WilsonDepartment of Biochemistry and the Redox Biology Center, University of Nebraska, Lincoln, NE 68588, USA.
Alix Vincent DachsbeckWELBIO, Avenue Hippocrate 75, 1200 Brussels, Belgium; de Duve Institute, Université catholique de Louvain, Avenue Hippocrate 75, 1200 Brussels, Belgium.
Felipe VielaLouvain Institute of Biomolecular Science and Technology, Université Catholique de Louvain, Croix du Sud 4-5, 1348 Louvain-la-neuve, Belgium.
Emmanuelle LatourWELBIO, Avenue Hippocrate 75, 1200 Brussels, Belgium; de Duve Institute, Université catholique de Louvain, Avenue Hippocrate 75, 1200 Brussels, Belgium.
Alexandra GennarisWELBIO, Avenue Hippocrate 75, 1200 Brussels, Belgium; de Duve Institute, Université catholique de Louvain, Avenue Hippocrate 75, 1200 Brussels, Belgium.
Didier Vertommende Duve Institute, Université catholique de Louvain, Avenue Hippocrate 75, 1200 Brussels, Belgium.
Yves Frédéric DufrêneLouvain Institute of Biomolecular Science and Technology, Université Catholique de Louvain, Croix du Sud 4-5, 1348 Louvain-la-neuve, Belgium.
Bogdan Iuliu IorgaWELBIO, Avenue Hippocrate 75, 1200 Brussels, Belgium; de Duve Institute, Université catholique de Louvain, Avenue Hippocrate 75, 1200 Brussels, Belgium; Université Paris-Saclay, CNRS UPR 2301, Institut de Chimie des Substances Naturelles, 91198 Gif-sur-Yvette, France.
Camille Véronique GoemansWELBIO, Avenue Hippocrate 75, 1200 Brussels, Belgium; de Duve Institute, Université catholique de Louvain, Avenue Hippocrate 75, 1200 Brussels, Belgium; European Molecular Biology Laboratory, Meyerhofstrasse 1, 69117 Heidelberg, Germany. Electronic address: camille.goemans@embl.de.
Han RemautStructural Biology Brussels, Vrije Universiteit Brussel, 1050 Brussels, Belgium; Structural and Molecular Microbiology, Structural Biology Research Center, VIB, 1050 Brussels, Belgium. Electronic address: han.remaut@vub.be.
Jean-François ColletWELBIO, Avenue Hippocrate 75, 1200 Brussels, Belgium; de Duve Institute, Université catholique de Louvain, Avenue Hippocrate 75, 1200 Brussels, Belgium. Electronic address: jfcollet@uclouvain.be.
de Duve Institute · BEUCLouvain · BEUniversity of Nebraska–Lincoln · USVrije Universiteit Brussel · BECentre National de la Recherche Scientifique · FR

Funding

Time-Resolved X-ray Crystallography of Dynamics in Cysteine-Dependent EnzymesR01GM139978 · NIGMS · UNIVERSITY OF NEBRASKA LINCOLN · PI WILSON, MARK A. · 2020 to 2023
$1.2M
NIGMS NIH HHS R01 GM139978
6 · The paper itself

Abstract

Hsp60 chaperonins and their Hsp10 cofactors assist protein folding in all living cells, constituting the paradigmatic example of molecular chaperones. Despite extensive investigations of their structure and mechanism, crucial questions regarding how these chaperonins promote folding remain unsolved. Here, we report that the bacterial Hsp60 chaperonin GroEL forms a stable, functionally relevant complex with the chaperedoxin CnoX, a protein combining a chaperone and a redox function. Binding of GroES (Hsp10 cofactor) to GroEL induces CnoX release. Cryoelectron microscopy provided crucial structural information on the GroEL-CnoX complex, showing that CnoX binds GroEL outside the substrate-binding site via a highly conserved C-terminal α-helix. Furthermore, we identified complexes in which CnoX, bound to GroEL, forms mixed disulfides with GroEL substrates, indicating that CnoX likely functions as a redox quality-control plugin for GroEL. Proteins sharing structural features with CnoX exist in eukaryotes, suggesting that Hsp60 molecular plugins have been conserved through evolution.

Indexed as

Molecular ChaperonesProtein FoldingChaperonin 10Chaperonin 60ChaperoninsCryoelectron MicroscopyOxidation-ReductionChaperonin 10Chaperonin 60ChaperoninsMolecular Chaperoneschaperoneschaperoninprotein foldingproteostasisredoxthioredoxinTPR

Identifiers

PMID36764293
PMCPMC10044410
OpenAlexW4319728571

What OpenQuestion holds

Textmetadata
LicenceTDM
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.