ArticleBiophysical journal2017
Thermodynamic Bounds on the Ultra- and Infra-affinity of Hsp70 for Its Substrates.
Article in Biophysical journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 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
7 citing papers in PubMed, 16 citations in OpenAlex.
- Stochastic thermodynamics for biological functions.Quantitative biology (Beijing, China) · 2025Review
- Active unfolding of the glucocorticoid receptor by the Hsp70/Hsp40 chaperone system in single-molecule mechanical experiments.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Allosteric Inter-Domain Contacts in Bacterial Hsp70 Are Located in Regions That Avoid Insertion and Deletion Events.International journal of molecular sciences · 2022Article
- 3-Hydroxykynurenine as a Potential Ligand for Hsp70 Proteins and Its Effects on Drosophila Memory After Heat Shock.Molecular neurobiology · 2022Article
- Chaperones directly and efficiently disperse stress-triggered biomolecular condensates.Molecular cell · 2022Article
- Biochemical Convergence of Mitochondrial Hsp70 System Specialized in Iron-Sulfur Cluster Biogenesis.International journal of molecular sciences · 2020Article
- Interlinked GTPase cascades provide a motif for both robust switches and oscillators.Journal of the Royal Society, Interface · 2019Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The 70 kDa heat shock protein Hsp70 has several essential functions in living systems, such as protecting cells against protein aggregation, assisting protein folding, remodeling protein complexes, and driving translocation into organelles. These functions require high affinity for nonspecific amino acid sequences that are ubiquitous in proteins. It has been recently shown that this high affinity, called ultra-affinity, depends on a process driven out of equilibrium by ATP hydrolysis. Here, we establish the thermodynamic bounds for ultra-affinity, and further show that the same reaction scheme can in principle be used both to strengthen and to weaken affinities (leading in this case to infra-affinity). We show that cofactors are essential to achieve affinity beyond the equilibrium range. Finally, biological implications are discussed.
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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.