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Wherein CP interacts with the accessible Met-rich motifs to form the [Pt(Met)Cl(NH 3 ) 2 ] intermediate, which induces a conformational change in Ctr1 and allows CP to pass laterally through the axis of the trimeric Ctr1 channel and move inward via the intermolecular sulfursulfur process exchange (Liang et al., 2009

Matrix metalloproteinases (MMPs) are the enzymes that degrade matrix proteins, and their activity is held in check by tissue inhibitors of metalloproteinases (TIMPs)

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When the amino group of one molecule joins with the acid group of another, a new molecule that now is made up of two amino acids forms