ArticleCell2013
Nucleotide binding and conformational switching in the hexameric ring of a AAA+ machine.
Article in Cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 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.
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
65 citing papers in PubMed.
- Identification of intracellular target of antimicrobial peptide EWAMP-R in bacteria.Communications biology · 2026Article
- Recent Advances in the Structural Studies of the Proteolytic ClpP/ClpX Molecular Machine.Biomolecules · 2025Review
- Conformations of Bcs1L undergoing ATP hydrolysis suggest a concerted translocation mechanism for folded iron-sulfur protein substrate.Nature communications · 2024Article
- Autoinhibition of a clamp-loader ATPase revealed by deep mutagenesis and cryo-EM.Nature structural & molecular biology · 2024Article
- Structure and function of ClpXP, a AAA+ proteolytic machine powered by probabilistic ATP hydrolysis.Critical reviews in biochemistry and molecular biology · 2022Review
- An empirical energy landscape reveals mechanism of proteasome in polypeptide translocation.eLife · 2022Article
- A DNA packaging motor inchworms along one strand allowing it to adapt to alternative double-helical structures.Nature communications · 2021Article
- Extreme parsimony in ATP consumption by 20S complexes in the global disassembly of single SNARE complexes.Nature communications · 2021Article
- Gain of SpontaneousFrontiers in bioengineering and biotechnology · 2021Article
- Article
- Multistep substrate binding and engagement by the AAA+ ClpXP protease.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Article
- The Intrinsically Disordered N-terminal Extension of the ClpS Adaptor Reprograms Its Partner AAA+ ClpAP Protease.Journal of molecular biology · 2020Article
- Article
- Stairway to translocation: AAA+ motor structures reveal the mechanisms of ATP-dependent substrate translocation.Protein science : a publication of the Protein Society · 2020Review
- Structural insights into ATP hydrolysis by the MoxR ATPase RavA and the LdcI-RavA cage-like complex.Communications biology · 2020Article
- Cryo-EM structure of the ClpXP protein degradation machinery.Nature structural & molecular biology · 2019Article
- Roles of the ClpX IGF loops in ClpP association, dissociation, and protein degradation.Protein science : a publication of the Protein Society · 2019Article
- Initial Characterization of the Two ClpP Paralogs ofJournal of bacteriology · 2019Article
- An Allosteric Interaction Network Promotes Conformation State-Dependent Eviction of the Nas6 Assembly Chaperone from Nascent 26S Proteasomes.Cell reports · 2019Article
5 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
6 authors.
Funding
Abstract
ClpX, a AAA+ ring homohexamer, uses the energy of ATP binding and hydrolysis to power conformational changes that unfold and translocate target proteins into the ClpP peptidase for degradation. In multiple crystal structures, some ClpX subunits adopt nucleotide-loadable conformations, others adopt unloadable conformations, and each conformational class exhibits substantial variability. Using mutagenesis of individual subunits in covalently tethered hexamers together with fluorescence methods to assay the conformations and nucleotide-binding properties of these subunits, we demonstrate that dynamic interconversion between loadable and unloadable conformations is required to couple ATP hydrolysis by ClpX to mechanical work. ATP binding to different classes of subunits initially drives staged allosteric changes, which set the conformation of the ring to allow hydrolysis and linked mechanical steps. Subunit switching between loadable and unloadable conformations subsequently isomerizes or resets the configuration of the nucleotide-loaded ring and is required for mechanical function.
Indexed as
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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.