ArticleeLife2018
Conserved conformational selection mechanism of Hsp70 chaperone-substrate interactions.
Article in eLife, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
47 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
- Enhanced Sensitivity and Resolution in Biomolecular CEST NMR Experiments Using the Extended Hadamard Encoding Scheme.Analytical chemistry · 2025Article
- Mechanisms of assembly and function of the Hsp70-Hsp40 chaperone machinery.Molecular cell · 2025Article
- Kinetic Dissection of Proton-Coupled Conformational Transitions in Nucleic Acids by Integrating pH-Dependent NMR and Chemical Modifications.Journal of the American Chemical Society · 2025Article
- Advances in the structures, mechanisms and targeting of molecular chaperones.Signal transduction and targeted therapy · 2025Review
- Native Fold Delay and its implications for co-translational chaperone binding and protein aggregation.Nature communications · 2025Article
- Ligand-induced protein transition state stabilization switches the binding pathway from conformational selection to induced fit.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Folding correctors can restore CFTR posttranslational folding landscape by allosteric domain-domain coupling.Nature communications · 2023Article
- Probing excited stateMethods (San Diego, Calif.) · 2023Article
- Studying micro to millisecond protein dynamics using simple amideJournal of biomolecular NMR · 2023Article
- The roles of molecular chaperones in regulating cell metabolism.FEBS letters · 2023Review
- Distribution and solvent exposure of Hsp70 chaperone binding sites across the Escherichia coli proteome.Proteins · 2023Article
- ThePlants (Basel, Switzerland) · 2022Article
- Real-time single-molecule observation of chaperone-assisted protein folding.Science advances · 2022Article
- Conformational dynamics of the Hsp70 chaperone throughout key steps of its ATPase cycle.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Computationally-Aided Modeling of Hsp70-Client Interactions: Past, Present, and Future.The journal of physical chemistry. B · 2022Article
- Non-Equilibrium Protein Folding and Activation by ATP-Driven Chaperones.Biomolecules · 2022Article
- Elucidating the mechanisms underlying protein conformational switching using NMR spectroscopy.Journal of magnetic resonance open · 2022Article
- Structural basis of protein substrate processing by human mitochondrial high-temperature requirement A2 protease.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Assembly mechanism of early Hsp90-Cdc37-kinase complexes.Science advances · 2022Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Molecular recognition is integral to biological function and frequently involves preferred binding of a molecule to one of several exchanging ligand conformations in solution. In such a process the bound structure can be selected from the ensemble of interconverting ligands
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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.