ArticleNature chemical biology2017
Ligand-promoted protein folding by biased kinetic partitioning.
Article in Nature chemical biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 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.
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
10 citing papers in PubMed.
- Marginal Stability of the YB1 Cold-Shock Domain in Cells Enables Binding of Multiple Nucleic Acids.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Unraveling the role of MAG, PTEN, and NOTCH1 in axonal regeneration: a network analysis and molecular dynamics study of siRNA/drugs/nanocarriers interactions.Journal of translational medicine · 2025Article
- Rational correction of pathogenic conformational defects in HTRA1.Nature communications · 2024Article
- The Proteome Folding Problem and Cellular Proteostasis.Journal of molecular biology · 2021Review
- Article
- Kinetic versus thermodynamic control of mutational effects on protein homeostasis: A perspective from computational modeling and experiment.Protein science : a publication of the Protein Society · 2019Article
- Melting Down Protein Stability: PAPS Synthase 2 in Patients and in a Cellular Environment.Frontiers in molecular biosciences · 2019Review
- Stilbene Boronic Acids Form a Covalent Bond with Human Transthyretin and Inhibit Its Aggregation.Journal of medicinal chemistry · 2017Article
- Protein folding: Illuminating chaperone activity.Nature chemical biology · 2017Article
- Cognate Ligand Chaperoning: a Novel Mechanism for the Post-translational Regulation of Neurotransmitter Receptor Biogenesis.Frontiers in cellular neuroscience · 2017Article
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6 authors.
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Abstract
Protein folding in cells occurs in the presence of high concentrations of endogenous binding partners, and exogenous binding partners have been exploited as pharmacological chaperones. A combined mathematical modeling and experimental approach shows that a ligand improves the folding of a destabilized protein by biasing the kinetic partitioning between folding and alternative fates (aggregation or degradation). Computationally predicted inhibition of test protein aggregation and degradation as a function of ligand concentration are validated by experiments in two disparate cellular systems.
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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.