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

Structure and interaction with model membranes of a CNBR peptide of diphtheria toxin B fragment.

Journal de physiologie - 1 Jan 1990

Cabiaux V, Phalipon A, Kaczorek M, Collier R J, Ruysschaert J M

Abstract excerpt

The mechanism by which diphtheria toxin (DT) crosses the endosomal membrane to exert its biological activity in the cell cytoplasm is still poorly understood. By measuring the change in conductance of planar lipid bilayers induced by cyanogen bromide peptides of fragment B of DT, we have identified a domain that could be involved in the pH-dependent membrane interaction of DT. Moreover, infrared spectroscopy has...

Topics

Diphtheria Toxin
Lipid Bilayers
Membranes
Mutation
Peptide Fragments
Spectrophotometry, Infrared

Source

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Identifiers

PMID: 2079663

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-2079663-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

0

discussions

0

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structure and interaction with model membranes of a CNBR peptide of diphtheria toxin B fragment.PMID 2079663Read ↗

pH-dependent insertion of proteins into membranes: B-chain mutation of diphtheria toxin that inhibits membrane translocation, Glu-349----Lys.Semantic proximity Read ↗

Role of acidic residues in helices TH8-TH9 in membrane interactions of the diphtheria toxin T domain.Semantic proximity Read ↗

Behavior of the N-terminal helices of the diphtheria toxin T domain during the successive steps of membrane interaction.Semantic proximity Read ↗

Membrane translocation assay based on proteolytic cleavage: application to diphtheria toxin T domain.Semantic proximity Read ↗

Replacement of C-terminal histidines uncouples membrane insertion and translocation in diphtheria toxin T-domain.Semantic proximity Read ↗

Effects of mutations in proline 345 on insertion of diphtheria toxin into model membranes.Semantic proximity Read ↗

Structure of the Diphtheria Toxin at Acidic pH: Implications for the Conformational Switching of the Translocation Domain.Semantic proximity Read ↗

Lipid interaction of diphtheria toxin and mutants. A study with phospholipid and protein monolayers.Semantic proximity Read ↗

Elimination of the disulphide bridge in fragment B of diphtheria toxin: effect on membrane insertion, channel formation, and ATP binding.Semantic proximity Read ↗

Translocation domain mutations affecting cellular toxicity identify the Clostridium difficile toxin B pore.Semantic proximity Read ↗

Structure function relationships in diphtheria toxin channels: II. A residue responsible for the channel's dependence on trans pH.Semantic proximity Read ↗

The pH-Dependent Trigger in Diphtheria Toxin T Domain Comes with a Safety Latch.Semantic proximity Read ↗

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