ArticleBiophysical journal2019
Hsp104 and Potentiated Variants Can Operate as Distinct Nonprocessive Translocases.
Article in Biophysical journal, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 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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Who cites it
16 citing papers in PubMed, 30 citations in OpenAlex.
- Stress granules and protein aggregates reveal intracellular resource competition.bioRxiv : the preprint server for biology · 2025Article
- Quantitative insights into processivity of an Hsp100 protein disaggregase on folded proteins.Biophysical journal · 2025Article
- Enabling simultaneous photoluminescence spectroscopy and X-ray footprinting mass spectrometry to study protein conformation and interactions.Analytical methods : advancing methods and applications · 2025Article
- Single turnover transient state kinetics reveals processive protein unfolding catalyzed byeLife · 2024Article
- The middle domain of Hsp104 can ensure substrates are functional after processing.PLoS genetics · 2024Article
- Tuning Hsp104 specificity to selectively detoxify α-synuclein.Molecular cell · 2023Article
- Insights and Perspectives on the Role of Proteostasis and Heat Shock Proteins in Fungal Infections.Microorganisms · 2023Review
- Unique structural features govern the activity of a human mitochondrial AAA+ disaggregase, Skd3.Cell reports · 2022Article
- AAA+ proteins: one motor, multiple ways to work.Biochemical Society transactions · 2022Review
- The yeast molecular chaperone, Hsp104, influences transthyretin aggregate formation.Frontiers in molecular neuroscience · 2022Article
- Drivers of Hsp104 potentiation revealed by scanning mutagenesis of the middle domain.Protein science : a publication of the Protein Society · 2021Article
- Kinetic Analysis of AAA+ Translocases by Combined Fluorescence and Anisotropy Methods.Biophysical journal · 2020Article
- AAA+ proteins: converging mechanisms, diverging functions.Nature structural & molecular biology · 2020Article
- 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
- Structural and mechanistic insights into Hsp104 function revealed by synchrotron X-ray footprinting.The Journal of biological chemistry · 2020Article
- Article
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
Abstract
Heat shock protein (Hsp) 104 is a hexameric ATPases associated with diverse cellular activities motor protein that enables cells to survive extreme stress. Hsp104 couples the energy of ATP binding and hydrolysis to solubilize proteins trapped in aggregated structures. The mechanism by which Hsp104 disaggregates proteins is not completely understood but may require Hsp104 to partially or completely translocate polypeptides across its central channel. Here, we apply transient state, single turnover kinetics to investigate the ATP-dependent translocation of soluble polypeptides by Hsp104 and Hsp104
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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.