ArticleCell reports2019
Cryo-EM Structures of the Hsp104 Protein Disaggregase Captured in the ATP Conformation.
Article in Cell reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 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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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
22 citing papers in PubMed.
- Heat Shock Protein and Disaggregase Influencing the Casein Structuralisation.International journal of molecular sciences · 2025Article
- Mapping Hsp104 interactions using cross-linking mass spectrometry.FEBS open bio · 2025Article
- Structure of the M. tuberculosis DnaK-GrpE complex reveals how key DnaK roles are controlled.Nature communications · 2024Article
- A concerted ATPase cycle of the protein transporter AAA-ATPase Bcs1.Nature communications · 2023Article
- Structural basis of impaired disaggregase function in the oxidation-sensitive SKD3 mutant causing 3-methylglutaconic aciduria.Nature communications · 2023Article
- Bioinformatics Analysis, Expression Profiling, and Functional Characterization of Heat Shock Proteins inBioengineering (Basel, Switzerland) · 2023Article
- Article
- Deciphering the mechanism and function of Hsp100 unfoldases from protein structure.Biochemical Society transactions · 2022Article
- Hsp104 N-terminal domain interaction with substrates plays a regulatory role in protein disaggregation.The FEBS journal · 2022Article
- Recent structural insights into the mechanism of ClpP protease regulation by AAA+ chaperones and small molecules.The Journal of biological chemistry · 2022Review
- Molecular mechanisms of amyloid disaggregation.Journal of advanced research · 2022Review
- Factors underlying asymmetric pore dynamics of disaggregase and microtubule-severing AAA+ machines.Biophysical journal · 2021Article
- Structural basis for aggregate dissolution and refolding by the Mycobacterium tuberculosis ClpB-DnaK bi-chaperone system.Cell reports · 2021Article
- Hsp100 Molecular Chaperone ClpB and Its Role in Virulence of Bacterial Pathogens.International journal of molecular sciences · 2021Review
- Resisting the Heat: Bacterial Disaggregases Rescue Cells From Devastating Protein Aggregation.Frontiers in molecular biosciences · 2021Review
- Structural and kinetic basis for the regulation and potentiation of Hsp104 function.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Structure of the Bcs1 AAA-ATPase suggests an airlock-like translocation mechanism for folded proteins.Nature structural & molecular biology · 2020Article
- Resolving the TorsinA Oligomerization Conundrum: The Glycan Hypothesis.Frontiers in molecular biosciences · 2020Article
- The molecular principles governing the activity and functional diversity of AAA+ proteins.Nature reviews. Molecular cell biology · 2020Review
- Cryo-EM structure of substrate-freeCurrent research in structural biology · 2019Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Hsp104 is a ring-forming, ATP-driven molecular machine that recovers functional protein from both stress-denatured and amyloid-forming aggregates. Although Hsp104 shares a common architecture with Clp/Hsp100 protein unfoldases, different and seemingly conflicting 3D structures have been reported. Examining the structure of Hsp104 poses considerable challenges because Hsp104 readily hydrolyzes ATP, whereas ATP analogs can be slowly turned over and are often contaminated with other nucleotide species. Here, we present the single-particle electron cryo-microscopy (cryo-EM) structures of a catalytically inactive Hsp104 variant (Hsp104
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