ArticleNature structural & molecular biology2008
GroEL stimulates protein folding through forced unfolding.
Article in Nature structural & molecular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 78 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.
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Who cites it
78 citing papers in PubMed, 156 citations in OpenAlex.
- GroEL/ES chaperonin unfolds then encapsulates a nascent protein on the ribosome.Nature communications · 2025Article
- Catalyzing Protein Folding by Chaperones.Biology · 2025Review
- Single Particle Dynamics of Protein Aggregation and Disaggregation in the Presence of the sHsp Proteins IbpAB.Biochemistry · 2025Article
- Structural basis of substrate progression through the bacterial chaperonin cycle.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- 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 proteome-wide map of chaperone-assisted protein refolding in a cytosol-like milieu.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- 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
- Bordetella pertussis whole cell immunization protects against Pseudomonas aeruginosa infections.NPJ vaccines · 2022Article
- Article
- Heterologous expression of naturally evolved putative de novo proteins with chaperones.Protein science : a publication of the Protein Society · 2022Article
- Large Chaperone Complexes Through the Lens of Nuclear Magnetic Resonance Spectroscopy.Annual review of biophysics · 2022Review
- Protein chain collapse modulation and folding stimulation by GroEL-ES.Science advances · 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
- Function and Fiber-Type Specific Distribution of Hsp60 and αB-Crystallin in Skeletal Muscles: Role of Physical Exercise.Biology · 2021Review
- Redefining Molecular Chaperones as Chaotropes.Frontiers in molecular biosciences · 2021Review
- Circuit Topology Analysis of Polymer Folding Reactions.ACS central science · 2020Review
- Single-Molecule Studies of Protein Folding with Optical Tweezers.Annual review of biochemistry · 2020Review
- Back to GroEL-Assisted Protein Folding: GroES Binding-Induced Displacement of Denatured Proteins from GroEL to Bulk Solution.Biomolecules · 2020Article
- Contact Order Is a Determinant for the Dependence of GFP Folding on the Chaperonin GroEL.Biophysical journal · 2019Article
18 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Many proteins cannot fold without the assistance of chaperonin machines like GroEL and GroES. The nature of this assistance, however, remains poorly understood. Here we demonstrate that unfolding of a substrate protein by GroEL enhances protein folding. We first show that capture of a protein on the open ring of a GroEL-ADP-GroES complex, GroEL's physiological acceptor state for non-native proteins in vivo, leaves the substrate protein in an unexpectedly compact state. Subsequent binding of ATP to the same GroEL ring causes rapid, forced unfolding of the substrate protein. Notably, the fraction of the substrate protein that commits to the native state following GroES binding and protein release into the GroEL-GroES cavity is proportional to the extent of substrate-protein unfolding. Forced protein unfolding is thus a central component of the multilayered stimulatory mechanism used by GroEL to drive protein folding.
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What OpenQuestion holds
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.