Article
Identifying amyloid-related diseases by mapping mutations in low-complexity protein domains to pathologies.
Nature structural & molecular biology - 1 Jun 2022
Murray Kevin A, Hughes Michael P, Hu Carolyn J, Sawaya Michael R, Salwinski Lukasz, Pan Hope, French Samuel W, Seidler Paul M, Eisenberg David S
Abstract excerpt
Proteins including FUS, hnRNPA2, and TDP-43 reversibly aggregate into amyloid-like fibrils through interactions of their low-complexity domains (LCDs). Mutations in LCDs can promote irreversible amyloid aggregation and disease. We introduce a computational approach to identify mutations in LCDs of disease-associated proteins predicted to increase propensity for amyloid aggregation. We identify several...
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