ReviewProtein science : a publication of the Protein Society1997
GroEL-mediated protein folding.
Review in Protein science : a publication of the Protein Society, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 86 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
86 citing papers in PubMed, 339 citations in OpenAlex.
- Seryl phosphorylation modulates chaperonin function of Mycobacterial chaperonin, Cpn60.1.Cell stress & chaperones · 2026Article
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- Photoacoustic Flow Cytometry Using Functionalized Microspheres for Selective Detection of Bacteria.Micromachines · 2023Article
- Structural visualization of the tubulin folding pathway directed by human chaperonin TRiC/CCT.Cell · 2022Article
- Large Chaperone Complexes Through the Lens of Nuclear Magnetic Resonance Spectroscopy.Annual review of biophysics · 2022Review
- Integrating single-molecule FRET and biomolecular simulations to study diverse interactions between nucleic acids and proteins.Essays in biochemistry · 2021Review
- Ligand Binding Introduces Significant Allosteric Shifts in the Locations of Protein Fluctuations.Frontiers in molecular biosciences · 2021Article
- Article
- Analogs of nitrofuran antibiotics are potent GroEL/ES inhibitor pro-drugs.Bioorganic & medicinal chemistry · 2020Article
- Complex Destabilization in the Mitochondrial Chaperonin Hsp60 Leads to Disease.Frontiers in molecular biosciences · 2020Review
- HSP60/10 chaperonin systems are inhibited by a variety of approved drugs, natural products, and known bioactive molecules.Bioorganic & medicinal chemistry letters · 2019Article
- Essential Oils as an Intervention Strategy to ReduceFrontiers in microbiology · 2019Review
- Hydroxybiphenylamide GroEL/ES Inhibitors Are Potent Antibacterials against Planktonic and Biofilm Forms of Staphylococcus aureus.Journal of medicinal chemistry · 2018Article
- Sulfonamido-2-arylbenzoxazole GroEL/ES Inhibitors as Potent Antibacterials against Methicillin-Resistant Staphylococcus aureus (MRSA).Journal of medicinal chemistry · 2018Article
- Modeling protein folding in vivo.Biology direct · 2018Article
- Single-Ring Intermediates Are Essential for Some Chaperonins.Frontiers in molecular biosciences · 2018Article
- Molecular chaperones maximize the native state yield on biological times by driving substrates out of equilibrium.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- The human mitochondrial Hsp60 in the APO conformation forms a stable tetradecameric complex.Cell cycle (Georgetown, Tex.) · 2017Article
- Chaperonin-Based Biolayer Interferometry To Assess the Kinetic Stability of Metastable, Aggregation-Prone Proteins.Biochemistry · 2016Article
26 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
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
I. Architecture of GroEL and GroES and the reaction pathway A. Architecture of the chaperonins B. Reaction pathway of GroEL-GroES-mediated folding II. Polypeptide binding A. A parallel network of chaperones binding polypeptides in vivo B. Polypeptide binding in vitro 1. Role of hydrophobicity in recognition 2. Homologous proteins with differing recognition-differences in primary structure versus effects on folding pathway 3. Conformations recognized by GroEL a. Refolding studies b. Binding of metastable intermediates c. Conformations while stably bound at GroEL 4. Binding constants and rates of association 5. Conformational changes in the substrate protein associated with binding by GroEL a. Observations b. Kinetic versus thermodynamic action of GroEL in mediating unfolding c. Crossing the energy landscape in the presence of GroEL III. ATP binding and hydrolysis-driving the reaction cycle IV. GroEL-GroES-polypeptide ternary complexes-the folding-active cis complex A. Cis and trans ternary complexes B. Symmetric complexes C. The folding-active intermediate of a chaperonin reaction-cis ternary complex D. The role of the cis space in the folding reaction E. Folding governed by a "timer" mechanism F. Release of nonnative polypeptides during the GroEL-GroES reaction G. Release of both native and nonnative forms under physiologic conditions H. A role for ATP binding, as well as hydrolysis, in the folding cycle V. Concluding remarks.
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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.