Globular and pre-fibrillar prion aggregates are toxic to neuronal cells and perturb their electrophysiology.
Prion diseases are characterised at autopsy by neuronal loss and accumulation of amorphous protein aggregates and/or amyloid fibrils in the brains of humans and animals. These protein deposits result from the conversion of the cellular, mainly alpha-helical prion protein (PrP(C)) to the beta-sheet-r...
Main Authors: | Sanghera, N, Wall, M, Vénien-Bryan, C, Pinheiro, T |
---|---|
Format: | Journal article |
Language: | English |
Published: |
2008
|
Similar Items
-
Structural changes of the prion protein in lipid membranes leading to aggregation and fibrillization.
by: Kazlauskaite, J, et al.
Published: (2003) -
An unusual soluble beta-turn-rich conformation of prion is involved in fibril formation and toxic to neuronal cells.
by: Kazlauskaite, J, et al.
Published: (2005) -
Twisting transition between crystalline and fibrillar phases of aggregated peptides.
by: Knowles, T, et al.
Published: (2012) -
Structural features distinguishing infectious ex vivo mammalian prions from non-infectious fibrillar assemblies generated in vitro
by: Terry, Cassandra, et al.
Published: (2019) -
Copper refolding of prion protein.
by: Wong, B, et al.
Published: (2000)