ArticleNature chemical biology2009
Mechanistic and structural insights into the proteolytic activation of Vibrio cholerae MARTX toxin.
Article in Nature chemical biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.
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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.
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Who cites it
52 citing papers in PubMed, 78 citations in OpenAlex.
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- Elongation Factor Tu Acts as a Chaperone to Activate an Antibacterial RNase Toxin.Molecular microbiology · 2026Article
- Cysteine proteases and how YabG fits into clan CD of the MEROPS database.Journal of bacteriology · 2025Review
- Facile expression of proteins with desired N-terminal amino acid via an engineered cysteine protease domain.Communications biology · 2025Article
- Reactions of SleC, Its Structure and Inhibition in Mitigation of Spore Germination inJournal of the American Chemical Society · 2025Article
- Dissemination of pathogenic bacteria is reinforced by a MARTX toxin effector duet.Nature communications · 2024Article
- Structural basis of the activation of MARTX cysteine protease domain from Vibrio vulnificus.PloS one · 2024Article
- C-terminal modification and functionalization of proteins via a self-cleavage tag triggered by a small molecule.Nature communications · 2023Article
- ThemBio · 2022Article
- Exotoxin-Targeted Drug Modalities as Antibiotic Alternatives.ACS infectious diseases · 2022Review
- Article
- Differential effects of 'resurrecting' Csp pseudoproteases during Clostridioides difficile spore germination.The Biochemical journal · 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
- CavityPlus: a web server for protein cavity detection with pharmacophore modelling, allosteric site identification and covalent ligand binding ability prediction.Nucleic acids research · 2018Article
- Targeting and inactivation of bacterial toxins by human defensins.Biological chemistry · 2017Review
- Architecture of the type IV coupling protein complex of Legionella pneumophila.Nature microbiology · 2017Article
- New ligation independent cloning vectors for expression of recombinant proteins with a self-cleaving CPD/6xHis-tag.BMC biotechnology · 2017Article
- Actin activates Pseudomonas aeruginosa ExoY nucleotidyl cyclase toxin and ExoY-like effector domains from MARTX toxins.Nature communications · 2016Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
MARTX toxins modulate the virulence of a number of Gram-negative Vibrio species. This family of toxins is defined by the presence of a cysteine protease domain (CPD), which proteolytically activates the Vibrio cholerae MARTX toxin. Although recent structural studies of the CPD have uncovered a new allosteric activation mechanism, the mechanism of CPD substrate recognition or toxin processing is unknown. Here we show that interdomain cleavage of MARTXVc enhances effector domain function. We also identify the first small-molecule inhibitors of this protease domain and present the 2.35-A structure of the CPD bound to one of these inhibitors. This structure, coupled with biochemical and mutational studies of the toxin, reveals the molecular basis of CPD substrate specificity and underscores the evolutionary relationship between the CPD and the clan CD caspase proteases. These studies are likely to prove valuable for devising new antitoxin strategies for a number of bacterial pathogens.
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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.