ReviewArchives of biochemistry and biophysics2012
Aggregate reactivation mediated by the Hsp100 chaperones.
Review in Archives of biochemistry and biophysics, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 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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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.
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Who cites it
43 citing papers in PubMed.
- Comparative genomics and tadpole intestinal metabarcoding suggest a potential cyanobacteria-amphibian trophic link in hot-spring ecosystems.Frontiers in microbiology · 2026Article
- Article
- Tandem repeats of highly bioluminescent NanoLuc are refolded noncanonically by the Hsp70 machinery.Protein science : a publication of the Protein Society · 2024Article
- Sequence elements within the PEXEL motif and its downstream region modulate PTEX-dependent protein export in Plasmodium falciparum.Traffic (Copenhagen, Denmark) · 2024Article
- Ancestors in the Extreme: A Genomics View of Microbial Diversity in Hypersaline Aquatic Environments.Results and problems in cell differentiation · 2024Article
- Simple model systems reveal conserved mechanisms of Alzheimer's disease and related tauopathies.Molecular neurodegeneration · 2023Review
- The Functionality of IbpA fromInternational journal of molecular sciences · 2023Article
- Review
- Proteostasis in aging-associated ocular disease.Molecular aspects of medicine · 2022Review
- Evaluating EcxR for Its Possible Role inInternational journal of molecular sciences · 2022Article
- ESKAPE Pathogens: Looking at Clp ATPases as Potential Drug Targets.Antibiotics (Basel, Switzerland) · 2022Review
- Article
- A revised mechanism for how Plasmodium falciparum recruits and exports proteins into its erythrocytic host cell.PLoS pathogens · 2022Article
- Host cell stress response as a predictor of COVID-19 infectivity and disease progression.Frontiers in molecular biosciences · 2022Review
- Caseinolytic Proteins (Clp) in the GenusMolecules (Basel, Switzerland) · 2021Article
- Hsp100 Molecular Chaperone ClpB and Its Role in Virulence of Bacterial Pathogens.International journal of molecular sciences · 2021Review
- Short-chain reactive probes as tools to unravel theChemical science · 2021Article
- Does Inter-Organellar Proteostasis Impact Yeast Quality and Performance During Beer Fermentation?Frontiers in genetics · 2020Article
- The huntingtin inclusion is a dynamic phase-separated compartment.Life science alliance · 2019Article
- Hsp104 facilitates the endoplasmic-reticulum-associated degradation of disease-associated and aggregation-prone substrates.Protein science : a publication of the Protein Society · 2019Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Hsp100 family of molecular chaperones shows a unique capability to resolubilize and reactivate aggregated proteins. The Hsp100-mediated protein disaggregation is linked to the activity of other chaperones from the Hsp70 and Hsp40 families. The best-studied members of the Hsp100 family are the bacterial ClpB and Hsp104 from yeast. Hsp100 chaperones are members of a large super-family of energy-driven conformational "machines" known as AAA+ ATPases. This review describes the current mechanistic model of the chaperone-induced protein disaggregation and explains how the structural architecture of Hsp100 supports disaggregation and how the co-chaperones may participate in the Hsp100-mediated reactions.
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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.