ReviewPLoS pathogens2010
Inositol hexakisphosphate-induced autoprocessing of large bacterial protein toxins.
Review in PLoS pathogens, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 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
45 citing papers in PubMed, 71 citations in OpenAlex.
- Cysteine proteases and how YabG fits into clan CD of the MEROPS database.Journal of bacteriology · 2025Review
- Article
- Allosterically switchable network orientsProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Biantennary N-glycans As Receptors for MARTX Toxins inbioRxiv : the preprint server for biology · 2024Article
- Molecular basis of TMPRSS2 recognition by Paeniclostridium sordellii hemorrhagic toxin.Nature communications · 2024Article
- Structural basis of the activation of MARTX cysteine protease domain from Vibrio vulnificus.PloS one · 2024Article
- Structural dynamics of the CROPs domain control stability and toxicity of Paeniclostridium sordellii lethal toxin.Nature communications · 2023Article
- ThemBio · 2022Article
- Structural dynamics of receptor recognition and pH-induced dissociation of full-length Clostridioides difficile Toxin B.PLoS biology · 2022Article
- Host manipulation by bacterial type III and type IV secretion system effector proteases.Cellular microbiology · 2021Review
- A MARTX ToxinmBio · 2020Article
- An engineered chimeric toxin that cleaves activated mutant and wild-type RAS inhibits tumor growth.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- TheScience signaling · 2020Article
- TheFrontiers in microbiology · 2020Article
- Makes caterpillars floppy-like effector-containing MARTX toxins require host ADP-ribosylation factor (ARF) proteins for systemic pathogenicity.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Structure of the full-length Clostridium difficile toxin B.Nature structural & molecular biology · 2019Article
- The Modes of Action of MARTX Toxin Effector Domains.Toxins · 2018Review
- The bacterial Ras/Rap1 site-specific endopeptidase RRSP cleaves Ras through an atypical mechanism to disrupt Ras-ERK signaling.Science signaling · 2018Article
- Coordinated delivery and function of bacterial MARTX toxin effectors.Molecular microbiology · 2018Review
- The role of toxins in Clostridium difficile infection.FEMS microbiology reviews · 2017Review
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
Large bacterial protein toxins autotranslocate functional effector domains to the eukaryotic cell cytosol, resulting in alterations to cellular functions that ultimately benefit the infecting pathogen. Among these toxins, the clostridial glucosylating toxins (CGTs) produced by Gram-positive bacteria and the multifunctional-autoprocessing RTX (MARTX) toxins of Gram-negative bacteria have distinct mechanisms for effector translocation, but a shared mechanism of post-translocation autoprocessing that releases these functional domains from the large holotoxins. These toxins carry an embedded cysteine protease domain (CPD) that is activated for autoprocessing by binding inositol hexakisphosphate (InsP(6)), a molecule found exclusively in eukaryotic cells. Thus, InsP(6)-induced autoprocessing represents a unique mechanism for toxin effector delivery specifically within the target cell. This review summarizes recent studies of the structural and molecular events for activation of autoprocessing for both CGT and MARTX toxins, demonstrating both similar and potentially distinct aspects of autoprocessing among the toxins that utilize this method of activation and effector delivery.
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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.