Oligomerization of the human prion protein proceeds via a molten globule intermediate.
The conformational transition of the human prion protein from an alpha-helical to a beta-sheet-rich structure is believed to be the critical event in prion pathogenesis. The molecular mechanism of misfolding and the role of intermediate states during this transition remain poorly understood. To over...
Главные авторы: | Gerber, R, Tahiri-Alaoui, A, Hore, P, James, W |
---|---|
Формат: | Journal article |
Язык: | English |
Опубликовано: |
2007
|
Схожие документы
-
Conformational pH dependence of intermediate states during oligomerization of the human prion protein.
по: Gerber, R, и др.
Опубликовано: (2008) -
Inter-oligomer interactions of the human prion protein are modulated by the polymorphism at codon 129.
по: Gerber, R, и др.
Опубликовано: (2008) -
Methionine 129 variant of human prion protein oligomerizes more rapidly than the valine 129 variant: implications for disease susceptibility to Creutzfeldt-Jakob disease.
по: Tahiri-Alaoui, A, и др.
Опубликовано: (2004) -
Molecular heterosis of prion protein beta-oligomers. A potential mechanism of human resistance to disease.
по: Tahiri-Alaoui, A, и др.
Опубликовано: (2006) -
The presence of valine at residue 129 in human prion protein accelerates amyloid formation.
по: Baskakov, I, и др.
Опубликовано: (2005)