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 recombinant immunotoxin containing a disulfide-stabilized Fv fragment.

15 Aug 1993

Abstract excerpt

B3(dsFv)-PE38KDEL is a recombinant immunotoxin composed of the Fv region of monoclonal antibody B3 connected to a truncated form of Pseudomonas exotoxin (PE38KDEL), in which the unstable Fv heterodimer (composed of heavy- and light-chain variable regions) is held together and stabilized by a disulfide bond [termed disulfide-stabilized Fv (dsFV)]. A computer modeled structure of the B3(Fv), made by mutating and...

Read the complete abstract on PubMed

Topics

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

Share to Bacteriophages and microbial interactions
Share to Monoclonal and Polyclonal Antibodies Research
Share to Toxin Mechanisms and Immunotoxins

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

Source

Identifiers

PMID: 8356052
DOI: 10.1073/pnas.90.16.7538

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 recombinant immunotoxin containing a disulfide-stabilized Fv fragment.PMID 8356052Read ↗

Design of interchain disulfide bonds in the framework region of the Fv fragment of the monoclonal antibody B3Semantic proximity Read ↗

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

The disulfide bonds in antibody variable domains: effects on stability, folding in vitro, and functional expression in Escherichia coli.Semantic proximity Read ↗

Improved stability and yield of Fv targeted superantigen by introducing both linker and disulfide bond into the targeting moiety.Semantic proximity Read ↗

Immunotoxins with decreased immunogenicity and improved activity.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 ↗

Disulfide bond introduction for general stabilization of immunoglobulin heavy-chain variable domains.Semantic proximity Read ↗

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

Evaluation of disulfide bond position to enhance the thermal stability of a highly stable single domain antibody.Semantic proximity Read ↗

Genetic construction and characterization of an anti-monkey CD3 single-chain immunotoxin with a truncated diphtheria toxin.Semantic proximity Read ↗

Improved cytotoxic activity toward cell lines and fresh leukemia cells of a mutant anti-CD22 immunotoxin obtained by antibody phage display.Semantic proximity Read ↗

Functional Divergence in the Affinity and Stability of Non-Canonical Cysteines and Non-Canonical Disulfide Bonds: Insights from a VHH and VNAR Study.Semantic proximity Read ↗

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