ReviewBiochemical Society transactions2025
Single-molecule study of the dynamics of the molecular chaperone Hsp70 during the functional cycle.
Review in Biochemical Society transactions, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
2 citing papers in PubMed.
- In silico identification of selective cyclodecapeptide inhibitors targeting Plasmodium falciparum Grp78 chaperone.Journal of computer-aided molecular design · 2026Article
- Genomic and Transcriptomic Profiling of a Highly VirulentMicroorganisms · 2025Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The 70-kDa heat shock protein, Hsp70, is a key chaperone involved in cellular protein homeostasis. The structure of the Hsp70 protein family is highly conserved, including a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). ATP binding and hydrolysis in the NBD of Hsp70 regulates the binding and release of substrates in the SBD via interdomain allosteric communication. Growing evidence shows that the conformational dynamics of Hsp70 are crucial for its function, which are difficult to probe by traditional bulk-based methods. Single-molecule techniques are emerging as powerful tools to explore the dynamics of proteins that are obscured in bulk measurements. In this review, we summarize recent progress in the study of the molecular dynamics of Hsp70 and its interactions with cochaperones and substrates using single-molecule fluorescence spectroscopy and single-molecule force spectroscopy. We discuss how the application of single-molecule techniques facilitates a deeper understanding of the mechanistic details of the chaperone functions of Hsp70.
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Registered trials
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