Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10537114 | Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics | 2013 | 14 Pages |
Abstract
⺠Many prion-like sequences are intrinsically disordered protein interaction domains. ⺠They promote phase transitions and the formation of large macromolecular assemblies. ⺠Prion-like domains may be essential for the spatiotemporal organization of the cell. ⺠The structural flexibility also makes them prone to misfold and aggregate. ⺠As a consequence, they are emerging as causes of protein misfolding diseases.
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Related Topics
Physical Sciences and Engineering
Chemistry
Analytical Chemistry
Authors
Liliana Malinovska, Sonja Kroschwald, Simon Alberti,