Author: Gábor Erdos; Bálint Mészáros; Dana Reichmann; Zsuzsanna Dosztányi
Title: Large-scale analysis of redox-sensitive conditionally disordered protein regions reveal their widespread nature and key roles in high-level eukaryotic processes Document date: 2018_9_10
ID: 99m0gt06_45
Snippet: In conclusion, the results presented in this study show that many protein regions rely on metal binding disulfide bonds for stability, which are potentially redox-regulated, and involve structural transitions from an ordered state to a disordered state, or vice versa. The abundance of these types of regions dramatically increases from yeast to human, and involves a wide range of processes related to multicellularity, signaling and regulation of t.....
Document: In conclusion, the results presented in this study show that many protein regions rely on metal binding disulfide bonds for stability, which are potentially redox-regulated, and involve structural transitions from an ordered state to a disordered state, or vice versa. The abundance of these types of regions dramatically increases from yeast to human, and involves a wide range of processes related to multicellularity, signaling and regulation of transcription and translation.
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