ArticleProtein science : a publication of the Protein Society2017
A multispecific monoclonal antibody G2 recognizes at least three completely different epitope sequences with high affinity.
Article in Protein science : a publication of the Protein Society, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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2 citing papers in PubMed, 11 citations in OpenAlex.
- Mechanistic Insight into Poly-Reactivity of Immune Antibodies upon Acid Denaturation or Arginine Mutation in Antigen-Binding Regions.Antibodies (Basel, Switzerland) · 2023Review
- A spatial similarity of stereochemical environments formed by amino acid residues defines a common epitope of two non-homologous proteins.Scientific reports · 2019Article
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6 authors at 2 institutions in 1 country.
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Abstract
A monoclonal antibody (mAb) G2 possesses an unusual characteristic of reacting with at least three proteins (ATP6V1C1, SEPT3, and C6H10orf76) other than its original antigen, chicken prion protein (ChPrP). The epitopes on ChPrP and ATP6V1C1 have been identified previously. In this study, we identified the epitope in the third protein, SEPT3. Interestingly, there was no amino acid sequence similarity among the epitopes on the three proteins. These epitopes had high binding affinities to G2 (K
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