Affiliation: Uniformed Services University of the Health Sciences
Monahan Z, Ryan V, Janke A, Burke K, Rhoads S, Zerze G, et al. Phosphorylation of the FUS low-complexity domain disrupts phase separation, aggregation, and toxicity. EMBO J. 2017;36:2951-2967 pubmed publisher
..Hence, post-translational modification may be a mechanism by which cells control physiological assembly and prevent pathological protein aggregation, suggesting a potential treatment pathway amenable to pharmacologic modulation. ..
Rhoads S, Monahan Z, Yee D, Shewmaker F. The Role of Post-Translational Modifications on Prion-Like Aggregation and Liquid-Phase Separation of FUS. Int J Mol Sci. 2018;19: pubmed publisher
..FUS is post-translationally modified at numerous positions, which affect both its localization and aggregation propensity. These modifications may influence FUS-linked pathology and serve as therapeutic targets. ..