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

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

Bioconjugate chemistry - 1 Jan 2000

Debinski W, Pastan I

Abstract excerpt

Pseudomonas exotoxin A (PE) is a protein composed of 613 amino acids arranged into three major, and one minor, domains. Immunotoxins (ITs) containing PE38, a mutant form of PE which lacks the cell binding domain (Ia, amino acids 1-252) and 16 amino acids from domain Ib (amino acids 365-380), are extremely potent cytotoxic agents which can cause a complete regression of various human carcinomas grown in nude mice....

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 Antineoplastic Agents
Share to Bacterial Toxins

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

Share to Carcinoma, Squamous Cell

Share to Escherichia coli

Share to Lysine

Share to Mice, Nude

Source

Identifiers

PMID: 8199233
DOI: 10.1021/bc00025a006

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

An immunotoxin with increased activity and homogeneity produced by reducing the number of lysine residues in recombinant Pseudomonas exotoxin.PMID 8199233Read ↗

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

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

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

Recombinant immunotoxin for cancer treatment with low immunogenicity by identification and silencing of human T-cell epitopesSemantic proximity Read ↗

Removal of B-cell epitopes for decreasing immunogenicity in recombinant immunotoxin against B-cell malignancies.Semantic proximity Read ↗

Characterization of the B Cell Epitopes Associated with a Truncated Form of Pseudomonas Exotoxin (PE38) Used to Make Immunotoxins for the Treatment of Cancer PatientsSemantic proximity Read ↗

A protease-resistant immunotoxin against CD22 with greatly increased activity against CLL and diminished animal toxicity.Semantic proximity Read ↗

Mutations of two lysine residues in the CDR loops of a recombinant immunotoxin that reduce its sensitivity to chemical derivatization.Semantic proximity Read ↗

A variant of exotoxin A that forms potent and specific chemically conjugated immunotoxins.Semantic proximity Read ↗

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

Transforming growth factor alpha-Pseudomonas exotoxin fusion protein prolongs survival of nude mice bearing tumor xenografts.Semantic proximity Read ↗

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