ArticleNature chemical biology2012
Chemical chaperones assist intracellular folding to buffer mutational variations.
Article in Nature chemical biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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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.
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Who cites it
44 citing papers in PubMed, 106 citations in OpenAlex.
- Direct observation and quantification of single nanocondensates of the low complexity domain of TDP-43.Nature communications · 2026Article
- The Regulation of TDP-43 Structure and Phase Transitions: A Review.The protein journal · 2025Review
- Folding pathway of a discontinuous two-domain protein.Nature communications · 2024Article
- When Phased without Water: Biophysics of Cellular Desiccation, from Biomolecules to Condensates.Chemical reviews · 2023Review
- 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
- Host-Guest Complexation by β-Cyclodextrin Enhances the Solubility of an Esterified Protein.Molecular pharmaceutics · 2022Article
- Conserved and divergent chaperoning effects of Hsp60/10 chaperonins on protein folding landscapes.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Pharmacological targeting of endoplasmic reticulum stress in disease.Nature reviews. Drug discovery · 2022Review
- Chemical rescue of mutant proteins in living Saccharomyces cerevisiae cells by naturally occurring small molecules.G3 (Bethesda, Md.) · 2021Article
- Clinically Relevant Mutations of Mycobacterial GatCAB Inform Regulation of Translational Fidelity.mBio · 2021Article
- Chemical Chaperones Modulate the Formation of Metabolite Assemblies.International journal of molecular sciences · 2021Article
- Recent advances in understanding the role of proteostasis.Faculty reviews · 2021Review
- Osmolytes dynamically regulate mutant Huntingtin aggregation and CREB function in Huntington's disease cell models.Scientific reports · 2020Article
- Distinct metabolic states of a cell guide alternate fates of mutational buffering through altered proteostasis.Nature communications · 2020Article
- Taurine Induces an Ordered but Functionally Inactive Conformation in Intrinsically Disordered Casein Proteins.Scientific reports · 2020Article
- Single-residue physicochemical characteristics kinetically partition membrane protein self-assembly and aggregation.The Journal of biological chemistry · 2020Article
- Guanidine hydrochloride reactivates an ancient septin hetero-oligomer assembly pathway in budding yeast.eLife · 2020Article
- Getting CD19 Into Shape: Expression of Natively Folded "Difficult-to- Express" CD19 for Staining and Stimulation of CAR-T Cells.Frontiers in bioengineering and biotechnology · 2020Article
- Improvement of Soluble Production of Reteplase inAdvanced biomedical research · 2019Article
- A Chemical Chaperone Decouples TDP-43 Disordered Domain Phase Separation from Fibrillation.Biochemistry · 2018Article
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9 authors at 2 institutions in 1 country.
Funding
Abstract
Hidden genetic variations have the potential to lead to the evolution of new traits. Molecular chaperones, which assist protein folding, may conceal genetic variations in protein-coding regions. Here we investigate whether the chemical milieu of cells has the potential to alleviate intracellular protein folding, a possibility that could implicate osmolytes in concealing genetic variations. We found that the model osmolyte trimethylamine N-oxide (TMAO) can buffer mutations that impose kinetic traps in the folding pathways of two model proteins. Using this information, we rationally designed TMAO-dependent mutants in vivo, starting from a TMAO-independent protein. We show that different osmolytes buffer a unique spectrum of mutations. Consequently, the chemical milieu of cells may alter the folding pathways of unique mutant variants in polymorphic populations and lead to unanticipated spectra of genetic buffering.
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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.