ArticleCell2011
ClpX(P) generates mechanical force to unfold and translocate its protein substrates.
Article in Cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 156 papers, 1 of them a synthesis that pooled it.
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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
156 citing papers in PubMed, 1 synthesis or guideline pooled it, 301 citations in OpenAlex.
- The proteasome as a druggable target with multiple therapeutic potentialities: Cutting and non-cutting edges.Pharmacology & therapeutics · 2020Pooled it
- Structural modeling reveals the mechanism of motor ATPase coordination during type IV pilus retraction.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Influence of SmpB and ClpX interactions and interactomes on the transcription profile of Mycobacterium tuberculosis.The Biochemical journal · 2026Article
- Substrate-interacting pore loops of two ATPase subunits determine the degradation efficiency of the 26S proteasome.Nature communications · 2026Article
- DNA translocation by the CMG helicase: the helical inchworm model.Biochemical Society transactions · 2026Review
- Linked dimers of the AAA+ ATPase Msp1 reveal energetic demands and mechanistic plasticity for substrate extraction from lipid bilayers.FEBS letters · 2026Article
- The local mechanostructural properties of protein cargoes regulate nucleocytoplasmic transport.Nature physics · 2026Article
- Planar lightsheet optical tweezer pLOT for 2D trapping and imaging of freely-moving live cells.Communications biology · 2025Article
- Structural landscape of the degrading 26S proteasome reveals conformation-specific binding of TXNL1.Nature structural & molecular biology · 2025Article
- Structure of the central Staphylococcus aureus AAA+ protease MecA/ClpC/ClpP.Communications biology · 2025Article
- SNARE disassembly requires Sec18/NSF side loading.Nature structural & molecular biology · 2025Article
- The Potential of Nanopore Technologies in Peptide and Protein Sensing for Biomarker Detection.Biosensors · 2025Review
- Recent Advances in the Structural Studies of the Proteolytic ClpP/ClpX Molecular Machine.Biomolecules · 2025Review
- SNARE disassembly requires Sec18/NSF side-loading.bioRxiv : the preprint server for biology · 2025Article
- Structural landscape of AAA+ ATPase motor states in the substrate-degrading human 26S proteasome reveals conformation-specific binding of TXNL1.bioRxiv : the preprint server for biology · 2024Article
- A proteolytic AAA+ machine poised to unfold protein substrates.Nature communications · 2024Article
- Article
- Structural and mechanistic studies on human LONP1 redefine the hand-over-hand translocation mechanism.bioRxiv : the preprint server for biology · 2024Article
- Structural anisotropy results in mechano-directional transport of proteins across nuclear pores.Nature physics · 2024Article
- Degron-controlled protein degradation inbioRxiv : the preprint server for biology · 2023Article
96 more citing papers are in PubMed but not listed here.
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
Abstract
AAA(+) unfoldases denature and translocate polypeptides into associated peptidases. We report direct observations of mechanical, force-induced protein unfolding by the ClpX unfoldase from E. coli, alone, and in complex with the ClpP peptidase. ClpX hydrolyzes ATP to generate mechanical force and translocate polypeptides through its central pore. Threading is interrupted by pauses that are found to be off the main translocation pathway. ClpX's translocation velocity is force dependent, reaching a maximum of 80 aa/s near-zero force and vanishing at around 20 pN. ClpX takes 1, 2, or 3 nm steps, suggesting a fundamental step-size of 1 nm and a certain degree of intersubunit coordination. When ClpX encounters a folded protein, it either overcomes this mechanical barrier or slips on the polypeptide before making another unfolding attempt. Binding of ClpP decreases the slip probability and enhances the unfolding efficiency of ClpX. Under the action of ClpXP, GFP unravels cooperatively via a transient intermediate.
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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.