ArticleProceedings of the National Academy of Sciences of the United States of America2010
Single-molecule spectroscopy of protein folding in a chaperonin cage.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 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
57 citing papers in PubMed.
- Static and dynamic rough energy landscapes can lead to identical diffusivity.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- The dimerization domain of SARS-CoV-2 nucleocapsid protein is partially disordered and forms a dynamic high-affinity dimer.Cell reports. Physical science · 2025Article
- An outmoded in vitro-inferred mechanism for chaperonin-accelerated protein refolding is confirmed in cells by cryo-electron tomography.Cell stress & chaperones · 2024Article
- Stabilization of interdomain closure by a G protein inhibitor.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Synonymous and non-synonymous codon substitutions can alleviate dependence on GroEL for folding.Protein science : a publication of the Protein Society · 2024Article
- A billion years of evolution manifest in nanosecond protein dynamics.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Rapid droplet-based mixing for single-molecule spectroscopy.Nature methods · 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
- Thiosulfate-Cyanide Sulfurtransferase a Mitochondrial Essential Enzyme: From Cell Metabolism to the Biotechnological Applications.International journal of molecular sciences · 2022Review
- Non-Equilibrium Protein Folding and Activation by ATP-Driven Chaperones.Biomolecules · 2022Article
- Fast slow folding of an outer membrane porin.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Chaperones Skp and SurA dynamically expand unfolded OmpX and synergistically disassemble oligomeric aggregates.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Article
- Stochastic Modelling ofMolecules (Basel, Switzerland) · 2021Article
- Retardation of Folding Rates of Substrate Proteins in the Nanocage of GroEL.Biochemistry · 2021Article
- Measuring protein stability in the GroEL chaperonin cage reveals massive destabilization.eLife · 2020Article
- Mapping Multiple Distances in a Multidomain Protein for the Identification of Folding Intermediates.Biophysical journal · 2020Article
- Iterative annealing mechanism explains the functions of the GroEL and RNA chaperones.Protein science : a publication of the Protein Society · 2020Review
- Biosensors for Detection of Human Placental Pathologies: A Review of Emerging Technologies and Current Trends.Translational research : the journal of laboratory and clinical medicine · 2019Review
- Chaperonin facilitates protein folding by avoiding initial polypeptide collapse.Journal of biochemistry · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Molecular chaperones are known to be essential for avoiding protein aggregation in vivo, but it is still unclear how they affect protein folding mechanisms. We use single-molecule Förster resonance energy transfer to follow the folding of a protein inside the GroEL/GroES chaperonin cavity over a time range from milliseconds to hours. Our results show that confinement in the chaperonin decelerates the folding of the C-terminal domain in the substrate protein rhodanese, but leaves the folding rate of the N-terminal domain unaffected. Microfluidic mixing experiments indicate that strong interactions of the substrate with the cavity walls impede the folding process, but the folding hierarchy is preserved. Our results imply that no universal chaperonin mechanism exists. Rather, a competition between intra- and intermolecular interactions determines the folding rates and mechanisms of a substrate inside the GroEL/GroES cage.
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.