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

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

PloS one - 8 Nov 2010

Kintzer Alexander F, Sterling Harry J, Tang Iok I, Williams Evan R, Krantz Bryan A

Abstract excerpt

BACKGROUND: Anthrax toxin is comprised of protective antigen (PA), lethal factor (LF), and edema factor (EF). These proteins are individually nontoxic; however, when PA assembles with LF and EF, it produces lethal toxin and edema toxin, respectively. Assembly occurs either on cell surfaces or in plasma. In each milieu, PA assembles into a mixture of heptameric and octameric complexes that bind LF and EF. While...

Read the complete abstract on PubMed

Topics

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

Share to Antigens, Bacterial
Share to Bacterial Toxins

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Circular Dichroism

Share to Macromolecular Substances

Share to Mass Spectrometry

Share to Microfilament Proteins

Share to Protein Multimerization

Share to Receptors, Peptide

Source

Open in PubMed Open full text

Identifiers

PMID: 21079738
DOI: 10.1371/journal.pone.0013888
PMCID: PMC2975657

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Anthrax toxin receptor drives protective antigen oligomerization and stabilizes the heptameric and octameric oligomer by a similar mechanism.PMID 21079738Read ↗

Self-association of the transmembrane domain of an anthrax toxin receptor.Semantic proximity Read ↗

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

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

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

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

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

Membrane translocation by anthrax toxin.Semantic proximity Read ↗

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

Direct imaging of anthrax intoxication in animals reveals shared and individual functions of CMG-2 and TEM-8 in cellular toxin entrySemantic proximity Read ↗

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

Dominant-negative mutants of a toxin subunit: an approach to therapy of anthrax.Semantic proximity Read ↗

Selection and evaluation of the immunogenicity of protective antigen mutants as anthrax vaccine candidates.Semantic proximity Read ↗

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