ArticleJournal of molecular evolution1996
Antibody-antigen recognition: a canonical structure paradigm.
Article in Journal of molecular evolution, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
11 citing papers in PubMed.
- Structural and immunological basis of cross-reactivity between dengue and Zika infections: Implications in serosurveillance in endemic regions.Frontiers in microbiology · 2023Review
- Phage Display Libraries for Antibody Therapeutic Discovery and Development.Antibodies (Basel, Switzerland) · 2019Review
- Deciphering evolution of immune recognition in antibodies.BMC structural biology · 2018Article
- Structurally Mapping Antibody Repertoires.Frontiers in immunology · 2018Article
- Defining the complementarities between antibodies and haptens to refine our understanding and aid the prediction of a successful binding interaction.BMC biotechnology · 2015Article
- SAbDab: the structural antibody database.Nucleic acids research · 2014Article
- Exploring peptide mimics for the production of antibodies against discontinuous protein epitopes.Molecular immunology · 2010Article
- Use of molecular modeling and site-directed mutagenesis to define the structural basis for the immune response to carbohydrate xenoantigens.BMC immunology · 2007Article
- Protective and nonprotective human immunoglobulin M monoclonal antibodies to Cryptococcus neoformans glucuronoxylomannan manifest different specificities and gene use profiles.Infection and immunity · 2004Article
- Structure-function relationships for human antibodies to pneumococcal capsular polysaccharide from transgenic mice with human immunoglobulin Loci.Infection and immunity · 2002Article
- Random-peptide libraries and antigen-fragment libraries for epitope mapping and the development of vaccines and diagnostics.Current opinion in chemical biology · 2001Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The antibodies of known three-dimensional structure exhibit a definite number of conformations (canonical structures) for five of six hypervariable loops. In the present study it was found that approximately 85% of the immunoglobulin sequences analyzed fall into a small number of canonical structure combinations, representing only 3% of the total possible. These structures were classified into six distinct groups, depending on the type of antigen with which they interact. Within each loop, the positions responsible for maintaining these canonical structures show a use frequency of amino acids that fits an inverse power law, whereas the use frequency of the amino acids responsible for the detailed antigenic specificity follows an exponential distribution. We propose an evolutionary interpretation that connects these data, using the fact that the inverse power law is generated by statistical processes of the type that yield a wealth curve and the fact that exponential distribution is generated by processes that are not biased by past history.
Indexed as
Identifiers
8995065What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.