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

Structural determinants of the human idiotype HibId-1.

Journal of molecular recognition : JMR - 1 Jan 2000

Reason D C, O'Connor A P, Lucas A H

Abstract excerpt

The human antibody response to the capsular polysaccharide of Haemophilus influenzae type b is predominated by antibodies expressing a light-chain-associated idiotype designated HibId-1. HibId-1 is expressed by kappa light chains encoded by either the A2 or A18 variable region genes. In this report we use site-directed mutagenesis and molecular modeling to show that HibId-1 expression is determined by residues in...

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 Bacterial Capsules
Share to Immunoglobulin Fab Fragments

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

Share to Immunoglobulin Idiotypes

Share to Mice, Inbred BALB C

Share to Models, Molecular

Share to Polysaccharides, Bacterial

Share to Protein Conformation

Source

Identifiers

PMID: 11757072
DOI: 10.1002/jmr.548

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

Structural determinants of the human idiotype HibId-1.PMID 11757072Read ↗

Structural definition by antibody engineering of an idiotypic determinant.Semantic proximity Read ↗

Allelic polymorphism controls autoreactivity and vaccine elicitation of human broadly neutralizing antibodies against influenza virus.Semantic proximity Read ↗

Structures of Preferred Human IgV Genes-Based Protective Antibodies Identify How Conserved Residues Contact Diverse Antigens and Assign Source of Specificity to CDR3 Loop Variation.Semantic proximity Read ↗

Molecular characteristics of antibodies bearing an anti-DNA-associated idiotype.Semantic proximity Read ↗

Idiotope structure and genetic diversity in anti-streptococcal group A carbohydrate antibodies.Semantic proximity Read ↗

Defining the recognition elements of Lewis Y-reactive antibodies.Semantic proximity Read ↗

Humanization of the anti-CD18 antibody 6.7: an unexpected effect of a framework residue in binding to antigen.Semantic proximity Read ↗

Immunoglobulin light chain variable region gene sequences for human antibodies to Haemophilus influenzae type b capsular polysaccharide are dominated by a limited number of V kappa and V lambda segments and VJ combinations.Semantic proximity Read ↗

Replacement of TCR Dβ With Immunoglobulin DH DSP2.3 Imposes a Tyrosine-Enriched TCR Repertoire and Adversely Affects T Cell Development.Semantic proximity Read ↗

The sequences encoded by immunoglobulin diversity (DH) gene segments play key roles in controlling B‐cell development, antigen‐binding site diversity, and antibody productionSemantic proximity Read ↗

Identification and Characterization of a Peptide That Specifically Binds the Human, Broadly Neutralizing Anti-Human Immunodeficiency Virus Type 1 Antibody b12Semantic proximity Read ↗

Epitope-specific antibody response is controlled by immunoglobulin VH polymorphismsSemantic proximity Read ↗

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