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

Evaluation of loss and change of specificity resulting from random mutagenesis of an antibody VH region.

Journal of immunology (Baltimore, Md. : 1950) - 15 Dec 1995

Casson L P, Manser T

Abstract excerpt

Most data available from in vivo sources regarding the impact of somatic hypermutation on Ab V region structure and function are heavily biased due to the influence of clonal selection. In an effort to address this issue directly, we "randomly" introduced point mutations throughout the length of the VH region of an anti-p-azophenylarsonate (Ars) Ab expressed as an Fab in the phage display format. This was...

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 Cloning, Molecular
Share to Mice

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

Share to Molecular Sequence Data

Share to Mutagenesis

Share to Mutation

Share to Polymerase Chain Reaction

Share to Recombinant Fusion Proteins

Source

Identifiers

PMID: 7499849

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

Evaluation of loss and change of specificity resulting from random mutagenesis of an antibody VH region.PMID 7499849Read ↗

Clustered H chain somatic mutations shared by anti-p-azophenylarsonate antibodies confer enhanced affinity and ablate the cross-reactive idiotype.Semantic proximity Read ↗

Structural correlates of high antibody affinity: three engineered amino acid substitutions can increase the affinity of an anti-p-azophenylarsonate antibody 200-fold.Semantic proximity Read ↗

Conservation of binding site geometry among p-azophenylarsonate-specific antibodies.Semantic proximity Read ↗

Altering the antibody repertoire via transgene homologous recombination: evidence for global and clone-autonomous regulation of antigen-driven B cell differentiation.Semantic proximity Read ↗

Generation and analysis of random point mutations in an antibody CDR2 sequence: many mutated antibodies lose their ability to bind antigen.Semantic proximity Read ↗

Mutational analysis of arsonate binding by a CRIA+ antibody. VH and VL junctional diversity are essential for binding activity.Semantic proximity Read ↗

The molecular and biochemical characterization of mutant monoclonal antibodies with increased antigen binding.Semantic proximity Read ↗

Somatic origin of T-cell epitopes within antibody variable regions: significance to monoclonal therapy and genesis of systemic autoimmune disease.Semantic proximity Read ↗

Verification of a model of a F(ab) complex with phenylarsonate by oligonucleotide-directed mutagenesis.Semantic proximity Read ↗

Problems in using statistical analysis of replacement and silent mutations in antibody genes for determining antigen-driven affinity selection.Semantic proximity Read ↗

Directed molecular evolution by somatic hypermutation.Semantic proximity Read ↗

In vitro evolution of single-chain antibodies using mRNA displaySemantic proximity Read ↗

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