ReviewProtein science : a publication of the Protein Society2012
Ratcheting up protein translocation with anthrax toxin.
Review in Protein science : a publication of the Protein Society, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 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
39 citing papers in PubMed, 67 citations in OpenAlex.
- Beyond the Static Caliper: Dynamical Translocases and the Mathematical Imperative for Single-Molecule Proteomics.bioRxiv : the preprint server for biology · 2026Article
- Thermodynamic Stability Is a Strong Predictor for the Delivery of DARPins to the Cytosol via Anthrax Toxin.Pharmaceutics · 2021Article
- Anthrax toxin translocation complex reveals insight into the lethal factor unfolding and refolding mechanism.Scientific reports · 2021Article
- Natural and Designed Toxins for Precise Therapy: Modern Approaches in Experimental Oncology.International journal of molecular sciences · 2021Review
- TheMicrobiology spectrum · 2019Review
- Probing Translocation in Mutants of the Anthrax Channel: Atomically Detailed Simulations with Milestoning.The journal of physical chemistry. B · 2018Article
- Effect of endosomal acidification on small ion transport through the anthrax toxin PAFEBS letters · 2017Article
- The Impact of Protonation on Early Translocation of Anthrax Lethal Factor: Kinetics from Molecular Dynamics Simulations and Milestoning Theory.Journal of the American Chemical Society · 2017Article
- Targeting and inactivation of bacterial toxins by human defensins.Biological chemistry · 2017Review
- Relevance of the alternate conductance states of anthrax toxin channel.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Dynamic Phenylalanine Clamp Interactions Define Single-Channel Polypeptide Translocation through the Anthrax Toxin Protective Antigen Channel.Journal of molecular biology · 2017Article
- Laboratory evolution of artificially expanded DNA gives redesignable aptamers that target the toxic form of anthrax protective antigen.Nucleic acids research · 2016Article
- Membrane insertion of a Tc toxin in near-atomic detail.Nature structural & molecular biology · 2016Article
- Peptide- and proton-driven allosteric clamps catalyze anthrax toxin translocation across membranes.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Forces from the Portal Govern the Late-Stage DNA Transport in a Viral DNA Packaging Nanomotor.Biophysical journal · 2016Article
- Tumor Targeting and Drug Delivery by Anthrax Toxin.Toxins · 2016Review
- The Physics and Physical Chemistry of Molecular Machines.Chemphyschem : a European journal of chemical physics and physical chemistry · 2016Review
- Inhibiting bacterial toxins by channel blockage.Pathogens and disease · 2016Review
- Article
- Bacterial amyloid formation: structural insights into curli biogensis.Trends in microbiology · 2015Review
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 2 institutions in 1 country.
Funding
Abstract
Energy-consuming nanomachines catalyze the directed movement of biopolymers in the cell. They are found both dissolved in the aqueous cytosol as well as embedded in lipid bilayers. Inquiries into the molecular mechanism of nanomachine-catalyzed biopolymer transport have revealed that these machines are equipped with molecular parts, including adjustable clamps, levers, and adaptors, which interact favorably with substrate polypeptides. Biological nanomachines that catalyze protein transport, known as translocases, often require that their substrate proteins unfold before translocation. An unstructured protein chain is likely entropically challenging to bind, push, or pull in a directional manner, especially in a way that produces an unfolding force. A number of ingenious solutions to this problem are now evident in the anthrax toxin system, a model used to study protein translocation. Here we highlight molecular ratchets and current research on anthrax toxin translocation. A picture is emerging of proton-gradient-driven anthrax toxin translocation, and its associated ratchet mechanism likely applies broadly to other systems. We suggest a cyclical thermodynamic order-to-disorder mechanism (akin to a heat-engine cycle) is central to underlying protein translocation: peptide substrates nonspecifically bind to molecular clamps, which possess adjustable affinities; polypeptide substrates compress into helical structures; these clamps undergo proton-gated switching; and the substrate subsequently expands regaining its unfolded state conformational entropy upon translocation.
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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.