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

A variant of exotoxin A that forms potent and specific chemically conjugated immunotoxins.

The Journal of biological chemistry - 5 May 1993

Chaudry G J, Fulton R J, Draper R K

Abstract excerpt

To introduce a free sulfhydryl into Pseudomonas aeruginosa exotoxin A (ETA), methionine 161 in domain I of the toxin was changed to cysteine by site-directed mutagenesis. The free sulfhydryl provides a convenient site for covalent attachment of ETA to other proteins in the production of chimeric toxins. The mutation was then introduced into a variant of ETA that is impaired in receptor binding, termed ETA-60EF61,...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Antibodies, Monoclonal
Share to Base Sequence

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

Share to Carrier Proteins

Share to Cloning, Molecular

Share to Escherichia coli

Share to Genetic Variation

Source

Identifiers

PMID: 8486636

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

A variant of exotoxin A that forms potent and specific chemically conjugated immunotoxins.PMID 8486636Read ↗

An immunotoxin with increased activity and homogeneity produced by reducing the number of lysine residues in recombinant Pseudomonas exotoxin.Semantic proximity Read ↗

Immunotoxins with decreased immunogenicity and improved activity.Semantic proximity Read ↗

Identification and elimination of an immunodominant T-cell epitope in recombinant immunotoxins based on Pseudomonas exotoxin A.Semantic proximity Read ↗

Engineering immunotoxin-equipped effector cells and evaluation in primary human immune cellsSemantic proximity Read ↗

Recombinant immunotoxins containing the VH or VL domain of monoclonal antibody B3 fused to Pseudomonas exotoxin.Semantic proximity Read ↗

Pseudomonas exotoxin A mutants. Replacement of surface-exposed residues in domain III with cysteine residues that can be modified with polyethylene glycol in a site-specific manner.Semantic proximity Read ↗

Rationally designed chemokine-based toxin targeting the viral G protein-coupled receptor US28 potently inhibits cytomegalovirus infection in vivoSemantic proximity Read ↗

A recombinant immunotoxin engineered for increased stability by adding a disulfide bond has decreased immunogenicity.Semantic proximity Read ↗

Mutations in diphtheria toxin to improve immunotoxin selectivity and understand toxin entry into cells.Semantic proximity Read ↗

Genetically manipulated bacterial toxin as a new generation mucosal adjuvant.Semantic proximity Read ↗

Efficient neutralization of antibody-resistant forms of anthrax toxin by a soluble receptor decoy inhibitor.Semantic proximity Read ↗

Pseudomonas exotoxin A mutants. Replacement of surface exposed residues in domain II with cysteine residues that can be modified with polyethylene glycol in a site-specific manner.Semantic proximity Read ↗

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