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This study found that enzymatic conversion of Arg-51 in S100A3 protein to citrulline promotes homotetramer assembly, potentially increasing Ca²⁺ binding required for hair cuticular barrier formation.

This review focuses on S100A6, a Ca²⁺-binding protein, detailing its role in cell functions, the regulation of its expression, and its potential as a biomarker and therapeutic target in various diseases.

This study reported significant upregulation and release of S100A4 in psoriatic skin, which may actively contribute to psoriasis pathogenesis.

In this study, the researchers identified the specific subcellular localization of the protein S100A3 in the endocuticle and cortex of human hair shafts.

This review discusses the role and interactions of the calcium-binding protein S100A6 in cellular processes and its association with various diseases, highlighting the need for further research to fully understand its biological impact.