Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Structural basis of actin recognition and arginine ADP-ribosylation by <i>Clostridium perfringens</i> ι-toxin

19 May 2008

Abstract excerpt

The ADP-ribosylating toxins (ADPRTs) produced by pathogenic bacteria modify intracellular protein and affect eukaryotic cell function. Actin-specific ADPRTs (including Clostridium perfringens iota-toxin and Clostridium botulinum C2 toxin) ADP-ribosylate G-actin at Arg-177, leading to disorganization of the cytoskeleton and cell death. Although the structures of many actin-specific ADPRTs are available, the...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Antimicrobial Resistance in Staphylococcus
Share to Clostridium difficile and Clostridium perfringens research
Share to Toxin Mechanisms and Immunotoxins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 18490658
DOI: 10.1073/pnas.0801215105

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural basis of actin recognition and arginine ADP-ribosylation by <i>Clostridium perfringens</i> ι-toxinPMID 18490658Read ↗

Characterization of the enzymatic component of Clostridium perfringens iota-toxin.Semantic proximity Read ↗

Molecular Mechanisms of the Cytotoxicity of ADP-Ribosylating ToxinsSemantic proximity Read ↗

Structural basis for the NAD-hydrolysis mechanism and the ARTT-loop plasticity of C3 exoenzymes.Semantic proximity Read ↗

Photox, a Novel Actin-targeting Mono-ADP-ribosyltransferase from Photorhabdus luminescensSemantic proximity Read ↗

Novel bacterial ADP-ribosylating toxins: structure and functionSemantic proximity Read ↗

Clostridial Binary Toxins: Iota and C2 Family PortraitsSemantic proximity Read ↗

Crystal structure of the C3bot-RalA complex reveals a novel type of action of a bacterial exoenzyme.Semantic proximity Read ↗

Widespread repurposing of the human CD38 ADP-ribosyl cyclase fold for toxicity in antibacterial and anti-eukaryotic bacterial polymorphic toxinsSemantic proximity Read ↗

Structural dynamics of AAA+ ATPase Drg1 and mechanism of benzo-diazaborine inhibitionSemantic proximity Read ↗

Characterization of C3larvinA, a novel RhoA-targeting ADP-ribosyltransferase toxin produced by the honey bee pathogen, Paenibacillus larvae.Semantic proximity Read ↗

ADP-ribosylation from molecular mechanisms to therapeutic implicationsSemantic proximity Read ↗

Structural basis for inhibition of the AAA-ATPase Drg1 by diazaborine.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.