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- aggregation1
- cellular prion protein1
- DLS1
- dynamic light scattering1
- fluorescence recovery after photobleaching1
- FRAP1
- intrinsically disordered protein1
- liquid-liquid phase separation1
- maltose-binding protein1
- neurodegenerative disease1
- prion disease1
- prion protein1
- protein self-assembly1
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JBC Communications
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- Accelerated CommunicationOpen Access
The N-terminal domain of the prion protein is required and sufficient for liquid–liquid phase separation: A crucial role of the Aβ-binding domain
Journal of Biological ChemistryVol. 297Issue 1100860Published online: June 5, 2021- Janine Kamps
- Yu-Hsuan Lin
- Rosario Oliva
- Verian Bader
- Roland Winter
- Konstanze F. Winklhofer
- and others
Cited in Scopus: 8Formation of biomolecular condensates through liquid–liquid phase separation (LLPS) has been described for several pathogenic proteins linked to neurodegenerative diseases and is discussed as an early step in the formation of protein aggregates with neurotoxic properties. In prion diseases, neurodegeneration and formation of infectious prions is caused by aberrant folding of the cellular prion protein (PrPC). PrPC is characterized by a large intrinsically disordered N-terminal domain and a structured C-terminal globular domain.