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In contrast, another study showed that the mutant enzymes A4V, G85R, and G93A had a higher affinity for copper than the wild type protein, and that this aberrant copper binding was mediated by cysteine 111 (Watanabe et al., 2007), implying that the enzyme binds copper in an alternate site (Figure 1A)

Phytochemical, ethanomedicinal and pharmacological applications of escin from Aesculus hippocastanum L

These mediators activate signaling pathways that lead to the differentiation and proliferation of goblet cells, resulting in increased mucin production, the gel-forming component of mucus [70]

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