ArticleMolecular cell2004
Expansion and compression of a protein folding intermediate by GroEL.
Article in Molecular cell, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 44 papers, 1 of them a synthesis that pooled it.
What it found
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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.
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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.
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Who cites it
44 citing papers in PubMed, 1 synthesis or guideline pooled it, 93 citations in OpenAlex.
- How soluble misfolded proteins bypass chaperones at the molecular level.Nature communications · 2023Pooled it
- High-Throughput Detection of Cyanobacterial Form I Rubisco Assembly.ACS synthetic biology · 2026Article
- GroEL/ES chaperonin unfolds then encapsulates a nascent protein on the ribosome.Nature communications · 2025Article
- Single Particle Dynamics of Protein Aggregation and Disaggregation in the Presence of the sHsp Proteins IbpAB.Biochemistry · 2025Article
- Trigger factor accelerates nascent chain compaction and folding.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Protein chain collapse modulation and folding stimulation by GroEL-ES.Science advances · 2022Article
- Cryo-EM structures of GroEL:ESiScience · 2022Article
- The Impact of Hidden Structure on Aggregate Disassembly by Molecular Chaperones.Frontiers in molecular biosciences · 2022Article
- Development and application of multicolor burst analysis spectroscopy.Biophysical journal · 2021Article
- Redefining Molecular Chaperones as Chaotropes.Frontiers in molecular biosciences · 2021Review
- Chaperonin facilitates protein folding by avoiding initial polypeptide collapse.Journal of biochemistry · 2018Article
- A two-domain folding intermediate of RuBisCO in complex with the GroEL chaperonin.International journal of biological macromolecules · 2018Article
- GroEL actively stimulates folding of the endogenous substrate protein PepQ.Nature communications · 2017Article
- Differential conformational modulations of MreB folding upon interactions with GroEL/ES and TRiC chaperonin components.Scientific reports · 2016Article
- Multiple chaperonins in bacteria--novel functions and non-canonical behaviors.Cell stress & chaperones · 2015Review
- How do chaperonins fold protein?Biophysics (Nagoya-shi, Japan) · 2015Review
- Molecular chaperones are nanomachines that catalytically unfold misfolded and alternatively folded proteins.Cellular and molecular life sciences : CMLS · 2014Review
- The C-terminal tails of the bacterial chaperonin GroEL stimulate protein folding by directly altering the conformation of a substrate protein.The Journal of biological chemistry · 2014Article
- ATP-driven molecular chaperone machines.Biopolymers · 2013Review
- Repetitive protein unfolding by the trans ring of the GroEL-GroES chaperonin complex stimulates folding.The Journal of biological chemistry · 2013Article
Corrections and comments
- Erratum issued
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The GroEL-GroES chaperonin system is required for the assisted folding of many essential proteins. The precise nature of this assistance remains unclear, however. Here we show that denatured RuBisCO from Rhodospirillum rubrum populates a stable, nonaggregating, and kinetically trapped monomeric state at low temperature. Productive folding of this nonnative intermediate is fully dependent on GroEL, GroES, and ATP. Reactivation of the trapped RuBisCO monomer proceeds through a series of GroEL-induced structural rearrangements, as judged by resonance energy transfer measurements between the amino- and carboxy-terminal domains of RuBisCO. A general mechanism used by GroEL to push large, recalcitrant proteins like RuBisCO toward their native states thus appears to involve two steps: partial unfolding or rearrangement of a nonnative protein upon capture by a GroEL ring, followed by spatial constriction within the GroEL-GroES cavity that favors or enforces compact, folding-competent intermediate states.
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Registered trials
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.