Large-scale analysis of redox-sensitive conditionally disordered protein regions reveal their widespread nature and key roles in high-level eukaryotic processes

Gábor Erdos; Bálint Mészáros; Dana Reichmann; Zsuzsanna Dosztányi

The detailed examples are all modulated through either of the two main redox-sensitive structural elements: disulfide bridges or metal ion clusters. However, the biological functions of these proteins vary, and as a consequence, their mutations lead to very heterogeneous phenotypic alterations. These alterations are enabled by the distinct biological processes and pathways in which these proteins are embedded. Table 2 also shows the relevant molecular, pathway/network, and cellular level processes of the mutated proteins. In some cases the biological processes are not entirely clear, but the majority of the proteins do reflect the general trends of processes utilizing redox-sensitive structural switches (Figure 4) . The copyright holder for this preprint (which was not peer-reviewed) is the author/funder.