ArticleProceedings of the National Academy of Sciences of the United States of America2012
Global analysis of chaperone effects using a reconstituted cell-free translation system.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 92 papers, 2 of them syntheses that pooled it.
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Who cites it
92 citing papers in PubMed, 2 syntheses or guidelines pooled it, 182 citations in OpenAlex.
- Cell-Free Approach for Non-canonical Amino Acids Incorporation Into Polypeptides.Frontiers in bioengineering and biotechnology · 2020Pooled it
- Differential proteostatic regulation of insoluble and abundant proteins.Bioinformatics (Oxford, England) · 2019Pooled it
- Role of Hsp70 chaperone in client-protein folding elucidated by Markov state modeling and NMR restraint-assisted molecular dynamics simulations.Biophysical journal · 2026Article
- High-throughput mutational analysis of FProtein science : a publication of the Protein Society · 2026Article
- Integrating multimodal features with deep learning for protein solubility prediction.Journal of cheminformatics · 2026Article
- Approaches to Study Proteins Encoded by Essential Genes.Proteins · 2026Review
- Chaperone dependency during biogenesis does not correlate with chaperone dependency during refolding.Molecular systems biology · 2026Article
- Autonomous biogenesis of all thirty proteins of the Escherichia coli translation machinery.Nature communications · 2025Article
- Effect of the Bacterial Chaperones SecB and Trigger Factor (TF) on the Folding Dynamics and In Vitro Translocation of Cytoplasmic and Secretory Model Proteins.International journal of molecular sciences · 2025Article
- Online monitoring of the mitochondrial respiration activity and protein formation in the Almost Living Cell-free Expression (ALiCE) system.BMC biotechnology · 2025Article
- Lipid Modification and Membrane Localization of Proteins in Cell-Free System.ACS synthetic biology · 2025Article
- Chaperone Dependency during Primary Protein Biogenesis Does Not Correlate with Chaperone Dependency duringbioRxiv : the preprint server for biology · 2025Article
- Long-Term Protein Synthesis with PURE in a Mesoscale Dialysis System.ACS synthetic biology · 2025Article
- ATP Regeneration from Pyruvate in the PURE System.ACS synthetic biology · 2025Article
- Cell-Free Gene Expression: Methods and Applications.Chemical reviews · 2025Review
- A review on computational models for predicting protein solubility.Journal of microbiology (Seoul, Korea) · 2025Review
- HSP47 at the Crossroads of Thrombosis and Collagen Dynamics: Unlocking Therapeutic Horizons and Debates.TH open : companion journal to thrombosis and haemostasis · 2025Review
- Promoting the production of challenging proteins via induced expression in CHO cells and modified cell-free lysates harboring T7 RNA polymerase and mutant eIF2α.Synthetic and systems biotechnology · 2024Article
- N-Terminal Amino Acid Affects the Translation Efficiency at Lower Temperatures in a Reconstituted Protein Synthesis System.International journal of molecular sciences · 2024Article
- Mapping Protein-Protein Interactions at Birth: Single-Particle Cryo-EM Analysis of a Ribosome-Nascent Globin Complex.ACS central science · 2024Article
32 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein folding is often hampered by protein aggregation, which can be prevented by a variety of chaperones in the cell. A dataset that evaluates which chaperones are effective for aggregation-prone proteins would provide an invaluable resource not only for understanding the roles of chaperones, but also for broader applications in protein science and engineering. Therefore, we comprehensively evaluated the effects of the major Escherichia coli chaperones, trigger factor, DnaK/DnaJ/GrpE, and GroEL/GroES, on ∼800 aggregation-prone cytosolic E. coli proteins, using a reconstituted chaperone-free translation system. Statistical analyses revealed the robustness and the intriguing properties of chaperones. The DnaK and GroEL systems drastically increased the solubilities of hundreds of proteins with weak biases, whereas trigger factor had only a marginal effect on solubility. The combined addition of the chaperones was effective for a subset of proteins that were not rescued by any single chaperone system, supporting the synergistic effect of these chaperones. The resource, which is accessible via a public database, can be used to investigate the properties of proteins of interest in terms of their solubilities and chaperone effects.
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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.