ArticleInternational journal of molecular sciences2019
Fine Mapping of Glutamate Decarboxylase 65 Epitopes Reveals Dependency on Hydrophobic Amino Acids for Specific Interactions.
Article in International journal of molecular sciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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Who cites it
7 citing papers in PubMed, 9 citations in OpenAlex.
- Peptide Antibodies: Current Status.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Antibody Cross-Reactivity in Auto-Immune Diseases.International journal of molecular sciences · 2023Review
- Determination of crucial epitopes in the sperm protein calsperin employing synthetic peptides and monoclonal antibodies.Journal of peptide science : an official publication of the European Peptide Society · 2023Article
- Production and Characterization of Peptide Antibodies to the C-Terminal of Frameshifted Calreticulin Associated with Myeloproliferative Diseases.International journal of molecular sciences · 2022Article
- Epitope Mapping of Monoclonal Antibodies to Calreticulin Reveals That Charged Amino Acids Are Essential for Antibody Binding.Antibodies (Basel, Switzerland) · 2021Article
- Molecular Recognition and Advances in Antibody Design and Antigenic Peptide Targeting.International journal of molecular sciences · 2020Article
- Peptides, Antibodies, Peptide Antibodies and More.International journal of molecular sciences · 2019Review
Corrections and comments
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Authors and funding
6 authors at 4 institutions in 2 countries.
Funding
Abstract
Characterization of multiple antibody epitopes has revealed the necessity of specific groups of amino acid residues for reactivity. This applies to the majority of antibody-antigen interactions, where especially charged and hydrophilic amino acids have been reported to be essential for antibody reactivity. This study describes thorough characterization of glutamic acid decarboxylase (GAD) 65 antigenic epitopes, an immunodominant autoantigen in type 1 diabetes (T1D). As linear epitopes are sparsely described for GAD65 in T1D, we aimed to identify and thoroughly characterize two GAD65 antibodies using immunoassays. A monoclonal antibody recognized an epitope in the N-terminal domain of GAD65,
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Registered trials
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