ArticleBioconjugate chemistry2026
A Cysteine-Specific Cationization Strategy for Versatile Antibody Production against Intrinsically Disordered Proteins.
Article in Bioconjugate chemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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Who cites it
1 citing paper in PubMed.
- Conformational stability and domain-specific structural features of tumor autoantigens regulate autoantibody epitope propensity.Protein science : a publication of the Protein Society · 2026Article
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11 authors.
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Abstract
Several autoantigens relevant to the immune system, especially those targeted by autoantibodies induced by antitumor responses, tend to be rich in disordered regions and are prone to aggregation. This inherent instability presents significant challenges for the production, purification, and analysis of autoantigens in laboratory settings. Cysteine-specific cationization can effectively solubilize and purify these challenging proteins, allowing the isolation of full-length water-soluble antigens in their denatured state. The purified antigens enable accurate multiplex autoantibody assays using a suspension Luminex bead array platform. However, well-validated positive control antibodies are essential to ensuring precise clinical diagnosis. In this study, we prepared and characterized a panel of control antibodies by immunizing rabbits with cysteine-specific
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