ReviewMolecular microbiology2011
The unfolding story of anthrax toxin translocation.
Review in Molecular microbiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 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
43 citing papers in PubMed, 72 citations in OpenAlex.
- Beyond the Static Caliper: Dynamical Translocases and the Mathematical Imperative for Single-Molecule Proteomics.bioRxiv : the preprint server for biology · 2026Article
- Structural basis for the assembly and translocation of the Vip1-Vip2 insecticidal toxin from Bacillus thuringiensis.Nature communications · 2026Article
- Solution Structures ofToxins · 2021Article
- Article
- Anthrax toxin translocation complex reveals insight into the lethal factor unfolding and refolding mechanism.Scientific reports · 2021Article
- Atomic Structures of Anthrax Prechannel Bound with Full-Length Lethal and Edema Factors.Structure (London, England : 1993) · 2020Article
- Tetanus ToxinmSphere · 2020Article
- Atomic structures of anthrax toxin protective antigen channels bound to partially unfolded lethal and edema factors.Nature communications · 2020Article
- Effect of late endosomal DOBMP lipid and traditional model lipids of electrophysiology on the anthrax toxin channel activity.Biochimica et biophysica acta. Biomembranes · 2018Article
- A Dual Role for theFrontiers in microbiology · 2018Article
- Targeting and inactivation of bacterial toxins by human defensins.Biological chemistry · 2017Review
- Laboratory evolution of artificially expanded DNA gives redesignable aptamers that target the toxic form of anthrax protective antigen.Nucleic acids research · 2016Article
- Cross-inhibition of pathogenic agents and the host proteins they exploit.Scientific reports · 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
- Inhibiting bacterial toxins by channel blockage.Pathogens and disease · 2016Review
- Molecular assembly of lethal factor enzyme and pre-pore heptameric protective antigen in early stage of translocation.Journal of molecular modeling · 2016Article
- Peptide Probes Reveal a Hydrophobic Steric Ratchet in the Anthrax Toxin Protective Antigen Translocase.Journal of molecular biology · 2015Article
- Role of the α Clamp in the Protein Translocation Mechanism of Anthrax Toxin.Journal of molecular biology · 2015Article
- Identification of agents effective against multiple toxins and viruses by host-oriented cell targeting.Scientific reports · 2015Article
- Influence of chemical denaturants on the activity, fold and zinc status of anthrax lethal factor.Biochemistry and biophysics 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
2 authors at 1 institution in 1 country.
Funding
Abstract
The essential cellular functions of secretion and protein degradation require a molecular machine to unfold and translocate proteins either across a membrane or into a proteolytic complex. Protein translocation is also critical for microbial pathogenesis, namely bacteria can use translocase channels to deliver toxic proteins into a target cell. Anthrax toxin (Atx), a key virulence factor secreted by Bacillus anthracis, provides a robust biophysical model to characterize transmembrane protein translocation. Atx is comprised of three proteins: the translocase component, protective antigen (PA) and two enzyme components, lethal factor (LF) and oedema factor (OF). Atx forms an active holotoxin complex containing a ring-shaped PA oligomer bound to multiple copies of LF and OF. These complexes are endocytosed into mammalian host cells, where PA forms a protein-conducting translocase channel. The proton motive force unfolds and translocates LF and OF through the channel. Recent structure and function studies have shown that LF unfolds during translocation in a force-dependent manner via a series of metastable intermediates. Polypeptide-binding clamps located throughout the PA channel catalyse substrate unfolding and translocation by stabilizing unfolding intermediates through the formation of a series of interactions with various chemical groups and α-helical structure presented by the unfolding polypeptide during 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.