ArticleInfection and immunity2002
In vivo modifications of small GTPase Rac and Cdc42 by Bordetella dermonecrotic toxin.
Article in Infection and immunity, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 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.
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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
11 citing papers in PubMed, 28 citations in OpenAlex.
- Mechanisms of Pertussis Toxin Action: ADP-Ribosylation and Its Role in Pertussis Pathogenesis.Toxins · 2026Review
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- Histaminylation of glutamine residues is a novel posttranslational modification implicated in G-protein signaling.FEBS letters · 2012Article
- Cellular and molecular action of the mitogenic protein-deamidating toxin from Pasteurella multocida.The FEBS journal · 2011Review
- Association of Bordetella dermonecrotic toxin with the extracellular matrix.BMC microbiology · 2010Article
- Recent insights into Pasteurella multocida toxin and other G-protein-modulating bacterial toxins.Future microbiology · 2010Review
- Transglutaminase activation in neurodegenerative diseases.Future neurology · 2009Article
- Mycobacterium avium genes MAV_5138 and MAV_3679 are transcriptional regulators that play a role in invasion of epithelial cells, in part by their regulation of CipA, a putative surface protein interacting with host cell signaling pathways.Journal of bacteriology · 2009Article
- Identification of a receptor-binding domain of Bordetella dermonecrotic toxin.Infection and immunity · 2002Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bordetella dermonecrotic toxin (DNT) is known to activate the small GTPase Rho through deamidation or polyamination. In this study, we examined whether Rac and Cdc42, the two other members of the Rho family, serve as intracellular targets for the toxin. Immunoprecipitation and immunoblot assays revealed that DNT deamidated or polyaminated intracellular Rac and Cdc42. After the modifications, both Rac and Cdc42 lost their GTP-hydrolyzing, but not GTP-binding, activities. The interactions of the modified Rac and Cdc42 with their respective effectors were strictly dependent on GTP. MC3T3-E1 cells treated with DNT at high concentrations demonstrated extensive formations of lamellipodia and filopodia, which indicate the intracellular activation of Rac and Cdc42, respectively.
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Registered trials
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