Diversity in the CDR3 region of V(H) is sufficient for most antibody specificities.
By John Xu, M. Davis. Immunity, 2000
787 citations recorded by the source corpus.
Subfields: Hematology, Immunology, Radiology, Nuclear Medicine and Imaging
View Paper: https://www.semanticscholar.org/paper/b23c06a12c89956209f3c58ccfb06f8aed672579
How researchers see this paper
The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.
In Hematology
In Immunology
In Radiology, Nuclear Medicine and Imaging
Citations in the corpus
- Immunoglobulin Analysis Tool: A Novel Tool for the Analysis of Human and Mouse Heavy and Light Chain Transcripts (2012, background): “The DH gene segments frequently encode for the core of the CDR-H3, which prototypically lies at the center of the classical antigen-binding site and which therefore can make direct contact with antigen and principally determines Ig specificity (Kabat and Wu, 1991; Padlan, 1994; Xu and Davis, 2000; C”
- Selecting and screening recombinant antibody libraries (2005, background): “Medium-affinity antibodies are readily isolated from relatively small nonimmune libraries or from synthetic antibody libraries diversified in just one or two CDRs or in just one of the two chains, which reflects the situation in transgenic mice with restricted antibody repertoire”
- Antigen recognition by γδ T cells (2007, background): “The only antigens that seemed to be unrecognizable by Igs generated from the arbitrarily chosen VH in that system were bacterial polysaccharides (13).”