ArticleProceedings of the National Academy of Sciences of the United States of America2018
A folding nucleus and minimal ATP binding domain of Hsp70 identified by single-molecule force spectroscopy.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed.
- Visualizing dynamic tubulin folding in chaperonin TRiC from nonnative nucleus to final native state.Nature communications · 2025Article
- Single-molecule study of the dynamics of the molecular chaperone Hsp70 during the functional cycle.Biochemical Society transactions · 2025Review
- Prediction of the Stability of Protein Substructures Using AI/ML Techniques.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Visualizing nucleation, condensation and propagation of β-tubulin folding in chaperonin TRiC.bioRxiv : the preprint server for biology · 2024Article
- Human Small Heat Shock Protein B8 Inhibits Protein Aggregation without Affecting the Native Folding Process.Journal of the American Chemical Society · 2023Article
- The cofactor-dependent folding mechanism of Drosophila cryptochrome revealed by single-molecule pulling experiments.Nature communications · 2023Article
- Direct observation of chemo-mechanical coupling in DnaK by single-molecule force experiments.Biophysical journal · 2022Article
- Single-molecule experiments reveal the elbow as an essential folding guide in SMC coiled-coil arms.Biophysical journal · 2022Article
- Single-molecule mechanical studies of chaperones and their clients.Biophysics reviews · 2022Review
- Direct observation of chaperone-modulated talin mechanics with single-molecule resolution.Communications biology · 2022Article
- Allosteric Inter-Domain Contacts in Bacterial Hsp70 Are Located in Regions That Avoid Insertion and Deletion Events.International journal of molecular sciences · 2022Article
- Co-Translational Folding of Multi-Domain Proteins.Frontiers in molecular biosciences · 2022Review
- Interpretation of Single-Molecule Force Experiments on Proteins Using Normal Mode Analysis.Nanomaterials (Basel, Switzerland) · 2021Article
- Classifying Residues in Mechanically Stable and Unstable Substructures Based on a Protein Sequence: The Case Study of the DnaK Hsp70 Chaperone.Nanomaterials (Basel, Switzerland) · 2021Article
- Facile tethering of stable and unstable proteins for optical tweezers experiments.Biophysical journal · 2021Article
- Studying protein folding in health and disease using biophysical approaches.Emerging topics in life sciences · 2021Article
- Energy-dependent protein folding: modeling how a protein folding machine may work.F1000Research · 2021Article
- Studying heat shock proteins through single-molecule mechanical manipulation.Cell stress & chaperones · 2020Review
- Entropy-Based Strategies for Rapid Pre-Processing and Classification of Time Series Data from Single-Molecule Force Experiments.Entropy (Basel, Switzerland) · 2020Article
- Single-Molecule Studies of Protein Folding with Optical Tweezers.Annual review of biochemistry · 2020Review
Corrections and comments
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The folding pathways of large proteins are complex, with many of them requiring the aid of chaperones and others folding spontaneously. Along the folding pathways, partially folded intermediates are frequently populated; their role in the driving of the folding process is unclear. The structures of these intermediates are generally not amenable to high-resolution structural techniques because of their transient nature. Here we employed single-molecule force measurements to scrutinize the hierarchy of intermediate structures along the folding pathway of the nucleotide binding domain (NBD) of
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