ArticleeLife2014
Head-to-tail interactions of the coiled-coil domains regulate ClpB activity and cooperation with Hsp70 in protein disaggregation.
Article in eLife, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 81 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.
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Who cites it
81 citing papers in PubMed, 146 citations in OpenAlex.
- How does protein aggregate structure affect mechanisms of disaggregation?Biochemical Society transactions · 2025Review
- Uvr motifs regulate the chloroplast Clp chaperone-protease system.Trends in plant science · 2025Review
- Design principles to tailor Hsp104 therapeutics.Cell reports · 2024Article
- Genome-Wide Identification of theInternational journal of molecular sciences · 2024Article
- Unmasking AlphaFold to integrate experiments and predictions in multimeric complexes.Nature communications · 2024Article
- Identification of ClpB, a molecular chaperone involved in the stress tolerance and virulence of Streptococcus agalactiae.Veterinary research · 2024Article
- Design principles to tailor Hsp104 therapeutics.bioRxiv : the preprint server for biology · 2024Article
- Chaperone regulation of biomolecular condensates.Frontiers in biophysics · 2024Article
- Bioinformatics analysis and alternative polyadenylation in Heat Shock Proteins 70 (HSP70) family members.International journal of physiology, pathophysiology and pharmacology · 2024Article
- Development of heat-shock resistance inApplied and environmental microbiology · 2023Article
- Responses of the tree peony (Paeonia suffruticosa, Paeoniaceae) cultivar 'Yu Hong' to heat stress revealed by iTRAQ-based quantitative proteomics.Proteome science · 2022Article
- Chaperones directly and efficiently disperse stress-triggered biomolecular condensates.Molecular cell · 2022Article
- The Impact of Hidden Structure on Aggregate Disassembly by Molecular Chaperones.Frontiers in molecular biosciences · 2022Article
- A Review: Molecular Chaperone-mediated Folding, Unfolding and Disaggregation of Expressed Recombinant Proteins.Cell biochemistry and biophysics · 2021Review
- Structural basis for aggregate dissolution and refolding by the Mycobacterium tuberculosis ClpB-DnaK bi-chaperone system.Cell reports · 2021Article
- Entropic Inhibition: How the Activity of a AAA+ Machine Is Modulated by Its Substrate-Binding Domain.ACS chemical biology · 2021Article
- VESPER: global and local cryo-EM map alignment using local density vectors.Nature communications · 2021Article
- Reconstruction of Three-Dimensional Conformations of Bacterial ClpB from High-Speed Atomic-Force-Microscopy Images.Frontiers in molecular biosciences · 2021Article
- Resisting the Heat: Bacterial Disaggregases Rescue Cells From Devastating Protein Aggregation.Frontiers in molecular biosciences · 2021Review
- Genome-wide analysis of the HSP101/CLPB gene family for heat tolerance in hexaploid wheat.Scientific reports · 2020Article
21 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
10 authors at 3 institutions in 2 countries.
Funding
Abstract
The hexameric AAA+ chaperone ClpB reactivates aggregated proteins in cooperation with the Hsp70 system. Essential for disaggregation, the ClpB middle domain (MD) is a coiled-coil propeller that binds Hsp70. Although the ClpB subunit structure is known, positioning of the MD in the hexamer and its mechanism of action are unclear. We obtained electron microscopy (EM) structures of the BAP variant of ClpB that binds the protease ClpP, clearly revealing MD density on the surface of the ClpB ring. Mutant analysis and asymmetric reconstructions show that MDs adopt diverse positions in a single ClpB hexamer. Adjacent, horizontally oriented MDs form head-to-tail contacts and repress ClpB activity by preventing Hsp70 interaction. Tilting of the MD breaks this contact, allowing Hsp70 binding, and releasing the contact in adjacent subunits. Our data suggest a wavelike activation of ClpB subunits around the ring.DOI: http://dx.doi.org/10.7554/eLife.02481.001.
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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.