ArticleProceedings of the National Academy of Sciences of the United States of America2015
Assaying the kinetics of protein denaturation catalyzed by AAA+ unfolding machines and proteases.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
19 citing papers in PubMed, 35 citations in OpenAlex.
- ClpA- and ClpAP-catalyzed unfolding and translocation are differentially coupled to ATP binding.Biophysical journal · 2026Article
- Structure of the central Staphylococcus aureus AAA+ protease MecA/ClpC/ClpP.Communications biology · 2025Article
- Bioinformatic identification of ClpI, a distinct class of Clp unfoldases in Actinomycetota.Frontiers in microbiology · 2023Article
- The activated ClpP peptidase forcefully grips a protein substrate.Biophysical journal · 2022Article
- Hinokiflavone Attenuates the Virulence of Methicillin-Resistant Staphylococcus aureus by Targeting Caseinolytic Protease P.Antimicrobial agents and chemotherapy · 2022Article
- Modular and coordinated activity of AAA+ active sites in the double-ring ClpA unfoldase of the ClpAP protease.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Kinetic Analysis of AAA+ Translocases by Combined Fluorescence and Anisotropy Methods.Biophysical journal · 2020Article
- The Non-dominant AAA+ Ring in the ClpAP Protease Functions as an Anti-stalling Motor to Accelerate Protein Unfolding and Translocation.Cell reports · 2020Article
- Examination of the nucleotide-linked assembly mechanism of E. coli ClpA.Protein science : a publication of the Protein Society · 2019Article
- Roles of the ClpX IGF loops in ClpP association, dissociation, and protein degradation.Protein science : a publication of the Protein Society · 2019Article
- Hinge-Linker Elements in the AAA+ Protein Unfoldase ClpX Mediate Intersubunit Communication, Assembly, and Mechanical Activity.Biochemistry · 2018Article
- Reversible inhibition of the ClpP protease via an N-terminal conformational switch.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Time-resolved neutron scattering provides new insight into protein substrate processing by a AAA+ unfoldase.Scientific reports · 2017Article
- Comparative Analysis of the Structure and Function of AAA+ Motors ClpA, ClpB, and Hsp104: Common Threads and Disparate Functions.Frontiers in molecular biosciences · 2017Review
- AAA-ATPases in Protein Degradation.Frontiers in molecular biosciences · 2017Review
- The Proteasomal ATPases Use a Slow but Highly Processive Strategy to Unfold Proteins.Frontiers in molecular biosciences · 2017Article
- A Structurally Dynamic Region of the HslU Intermediate Domain Controls Protein Degradation and ATP Hydrolysis.Structure (London, England : 1993) · 2016Article
- Mechanistic insights into bacterial AAA+ proteases and protein-remodelling machines.Nature reviews. Microbiology · 2016Review
- Dissection of Axial-Pore Loop Function during Unfolding and Translocation by a AAA+ Proteolytic Machine.Cell reports · 2015Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
ATP-dependent molecular machines of the AAA+ superfamily unfold or remodel proteins in all cells. For example, AAA+ ClpX and ClpA hexamers collaborate with the self-compartmentalized ClpP peptidase to unfold and degrade specific proteins in bacteria and some eukaryotic organelles. Although degradation assays are straightforward, robust methods to assay the kinetics of enzyme-catalyzed protein unfolding in the absence of proteolysis have been lacking. Here, we describe a FRET-based assay in which enzymatic unfolding converts a mixture of donor-labeled and acceptor-labeled homodimers into heterodimers. In this assay, ClpX is a more efficient protein-unfolding machine than ClpA both kinetically and in terms of ATP consumed. However, ClpP enhances the mechanical activities of ClpA substantially, and ClpAP degrades the dimeric substrate faster than ClpXP. When ClpXP or ClpAP engage the dimeric subunit, one subunit is actively unfolded and degraded, whereas the other subunit is passively unfolded by loss of its partner and released. This assay should be broadly applicable for studying the mechanisms of AAA+ proteases and remodeling chaperones.
Indexed as
Identifiers
What OpenQuestion holds
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.