Discover Community Create You

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

Self-association of the transmembrane domain of an anthrax toxin receptor.

Journal of molecular biology - 30 Jun 2006

Go Mandy Y, Kim Sanguk, Partridge Anthony W, Melnyk Roman A, Rath Arianna, Deber Charles M, Mogridge Jeremy

Abstract excerpt

Protective antigen (PA), lethal factor (LF) and edema factor (EF) are secreted individually by Bacillus anthracis. These components of anthrax toxin must then assemble into complexes to intoxicate mammalian cells. Toxin assembly initiates when molecules of PA bind mammalian receptors ANTXR1/2 and are cleaved by surface proteases into 20 kDa and 63 kDa fragments. After PA20 dissociates, receptor-bound PA63...

Read the complete abstract on PubMed

Topics

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

Share to Anthrax
Share to Antigens, Bacterial
Share to Bacillus anthracis

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Bacterial Toxins

Share to Computational Biology

Share to Computer Simulation

Share to Fluorescence Resonance Energy Transfer

Share to Protein Structure, Secondary

Source

Identifiers

PMID: 16756998
DOI: 10.1016/j.jmb.2006.04.072

Genes

ANTXR1
SDS

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Self-association of the transmembrane domain of an anthrax toxin receptor.PMID 16756998Read ↗

Anthrax toxin receptor drives protective antigen oligomerization and stabilizes the heptameric and octameric oligomer by a similar mechanism.Semantic proximity Read ↗

Cytotoxic activity of Bacillus anthracis protective antigen observed in a macrophage cell line overexpressing ANTXR1.Semantic proximity Read ↗

Anthrax toxin: receptor binding, internalization, pore formation, and translocation.Semantic proximity Read ↗

Binding of filamentous actin to anthrax toxin receptor 1 decreases its association with protective antigen.Semantic proximity Read ↗

A dominant negative mutant of Bacillus anthracis protective antigen inhibits anthrax toxin action in vivo.Semantic proximity Read ↗

Engineering anthrax toxin variants that exclusively form octamers and their application to targeting tumors.Semantic proximity Read ↗

Membrane translocation by anthrax toxin.Semantic proximity Read ↗

Involvement of domain 3 in oligomerization by the protective antigen moiety of anthrax toxin.Semantic proximity Read ↗

An approach to characterizing single-subunit mutations in multimeric prepores and pores of anthrax protective antigen.Semantic proximity Read ↗

Anthrax toxin receptor 1/tumor endothelial marker 8: mutation of conserved inserted domain residues overrides cytosolic control of protective antigen binding.Semantic proximity Read ↗

Characterization of dominant-negative forms of anthrax protective antigen.Semantic proximity Read ↗

Self-association of TPR domains: Lessons learned from a designed, consensus-based TPR oligomer.Semantic proximity Read ↗

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