ReviewCellular and molecular life sciences : CMLS2010
Reconciling theories of chaperonin accelerated folding with experimental evidence.
Review in Cellular and molecular life sciences : CMLS, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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.
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
23 citing papers in PubMed.
- Context Dependency of Hydrophobicity in Intrinsically Disordered Proteins: Insights from a New Dewetting Free Energy-Based Hydrophobicity Scale.The journal of physical chemistry. B · 2025Article
- Energy landscape remodeling mechanism of Hsp70-chaperone-accelerated protein folding.Biophysical journal · 2021Article
- Retardation of Folding Rates of Substrate Proteins in the Nanocage of GroEL.Biochemistry · 2021Article
- Redefining Molecular Chaperones as Chaotropes.Frontiers in molecular biosciences · 2021Review
- Chloroplast Chaperonin-Mediated Targeting of a Thylakoid Membrane Protein.The Plant cell · 2020Article
- Substrate protein dependence of GroEL-GroES interaction cycle revealed by high-speed atomic force microscopy imaging.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018Article
- The exclusive effects of chaperonin on the behavior of proteins with 52 knot.PLoS computational biology · 2018Article
- GroEL actively stimulates folding of the endogenous substrate protein PepQ.Nature communications · 2017Article
- Visualizing chaperone-assisted protein folding.Nature structural & molecular biology · 2016Article
- Dynamic Complexes in the Chaperonin-Mediated Protein Folding Cycle.Frontiers in molecular biosciences · 2016Review
- Engineering and Evolution of Molecular Chaperones and Protein Disaggregases with Enhanced Activity.Frontiers in molecular biosciences · 2016Review
- Asp-52 in combination with Asp-398 plays a critical role in ATP hydrolysis of chaperonin GroEL.The Journal of biological chemistry · 2014Article
- 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
- GroEL/ES chaperonin modulates the mechanism and accelerates the rate of TIM-barrel domain folding.Cell · 2014Article
- Repetitive protein unfolding by the trans ring of the GroEL-GroES chaperonin complex stimulates folding.The Journal of biological chemistry · 2013Article
- Where soft matter meets living matter--protein structure, stability, and folding in the cell.Current opinion in structural biology · 2013Review
- A sticky cage can slow down folding.Biophysical journal · 2013Article
- Extended surfaces modulate hydrophobic interactions of neighboring solutes.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Simulation of chaperonin effect on protein folding: a shift from nucleation-condensation to framework mechanism.Journal of the American Chemical Society · 2011Article
- Archaeal-like chaperonins in bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
For the last 20 years, a large volume of experimental and theoretical work has been undertaken to understand how chaperones like GroEL can assist protein folding in the cell. The most accepted explanation appears to be the simplest: GroEL, like most other chaperones, helps proteins fold by preventing aggregation. However, evidence suggests that, under some conditions, GroEL can play a more active role by accelerating protein folding. A large number of models have been proposed to explain how this could occur. Focused experiments have been designed and carried out using different protein substrates with conclusions that support many different mechanisms. In the current article, we attempt to see the forest through the trees. We review all suggested mechanisms for chaperonin-mediated folding and weigh the plausibility of each in light of what we now know about the most stringent, essential, GroEL-dependent protein substrates.
Indexed as
Identifiers
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.