ArticleeLife2020
Measuring protein stability in the GroEL chaperonin cage reveals massive destabilization.
Article in eLife, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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.
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.
Who cites it
10 citing papers in PubMed.
- Cis-Acting Chaperoning by Macromolecular Tethering: A Built-In Layer of Cellular Chaperoning.International journal of molecular sciences · 2026Review
- Crowding-induced stabilization and destabilization in a single protein.Protein science : a publication of the Protein Society · 2025Article
- Exploring Novel Antibiotics by Targeting the GroEL/GroES Chaperonin System.ACS pharmacology & translational science · 2025Review
- Beyond Misfolding: A New Paradigm for the Relationship Between Protein Folding and Aggregation.International journal of molecular sciences · 2024Review
- An outmoded in vitro-inferred mechanism for chaperonin-accelerated protein refolding is confirmed in cells by cryo-electron tomography.Cell stress & chaperones · 2024Article
- Synonymous and non-synonymous codon substitutions can alleviate dependence on GroEL for folding.Protein science : a publication of the Protein Society · 2024Article
- From Microstates to Macrostates in the Conformational Dynamics of GroEL: A Single-Molecule Förster Resonance Energy Transfer Study.The journal of physical chemistry letters · 2023Article
- A diminished hydrophobic effect inside the GroEL/ES cavity contributes to protein substrate destabilization.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- A Conceptual Framework for Integrating Cellular Protein Folding, Misfolding and Aggregation.Life (Basel, Switzerland) · 2021Review
- Retardation of Folding Rates of Substrate Proteins in the Nanocage of GroEL.Biochemistry · 2021Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
The thermodynamics of protein folding in bulk solution have been thoroughly investigated for decades. By contrast, measurements of protein substrate stability inside the GroEL/ES chaperonin cage have not been reported. Such measurements require stable encapsulation, that is no escape of the substrate into bulk solution during experiments, and a way to perturb protein stability without affecting the chaperonin system itself. Here, by establishing such conditions, we show that protein stability in the chaperonin cage is reduced dramatically by more than 5 kcal mol
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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.