scholarly journals Differential effects of divalent cations on elk prion protein fibril formation and stability

Prion ◽  
2018 ◽  
Vol 12 (1) ◽  
pp. 63-71 ◽  
Author(s):  
Daniel Samorodnitsky ◽  
Eric M. Nicholson
Keyword(s):  
Prion Protein ◽  
Divalent Cations ◽  
Fibril Formation ◽  
Differential Effects ◽  
Protein Fibril

Structural mechanisms of oligomer and amyloid fibril formation by the prion protein

2018 ◽  
Vol 54 (49) ◽  
pp. 6230-6242 ◽  
Author(s):  
Ishita Sengupta ◽  
Jayant B. Udgaonkar
Keyword(s):  
Prion Protein ◽  
Amyloid Fibril ◽  
Fibril Formation ◽  
Aggregation Mechanism ◽  
Amyloid Fibril Formation ◽  
Structural Mechanisms

The aggregation mechanism of the prion protein is highly heterogeneous.

scholarly journals Pressure Reveals Unique Conformational Features in Prion Protein Fibril Diversity

2019 ◽  
Vol 9 (1) ◽  
Author(s):  
Joan Torrent ◽  
Davy Martin ◽  
Sylvie Noinville ◽  
Yi Yin ◽  
Marie Doumic ◽  
...  
Keyword(s):  
Prion Protein ◽  
Protein Fibril

Prion Protein Aggregation Induced by Copper(II) and Heparan Sulfate. Pressure-dependent Switch of Reaction Pathways

2008 ◽  
Vol 63 (6) ◽  
pp. 747-755 ◽  
Author(s):  
Driss El Moustaine ◽  
Joan Torrent ◽  
Reinhard Lange
Keyword(s):  
Heparan Sulfate ◽  
Prion Protein ◽  
Conformational Changes ◽  
Atmospheric Pressure ◽  
Amyloid Fibrils ◽  
Copper Ions ◽  
Fibril Formation ◽  
Cellular Prion Protein ◽  
Reaction Pathways ◽  
Structural Alterations

Copper ions (Cu2+) and heparan sulfate (HS) are suspected to act as regulatory agents in the conversion of cellular prion protein (PrPC) to its infectious isoform. However, the mechanism of this reaction is still largely unknown. Our previous report suggested multidimensional pathways for structural alterations of PrP, which may be modulated by high pressure (HP). Here we use HP to investigate the effects of Cu2+ and HS binding on PrP conformational changes and assembly. In the presence of Cu2+, amyloid fibrils are formed only under HP. In contrast, in the presence of HS, fibrils are formed at atmospheric pressure, but not under HP. Both compounds appear to compete for the same binding site, since HS-supported fibril formation is quenched by Cu2+. Inversely, Cu2+- mediated fibril formation under HP is inhibited by HS.

Aggregation and Amyloid Fibril Formation of the Prion Protein Is Accelerated in the Presence of Glycogen

2008 ◽  
Vol 11 (2) ◽  
pp. 365-369 ◽  
Author(s):  
Giannantonio Panza ◽  
Jan Stöhr ◽  
Eva Birkmann ◽  
Detlev Riesner ◽  
Dieter Willbold ◽  
...  
Keyword(s):  
Prion Protein ◽  
Amyloid Fibril ◽  
Fibril Formation ◽  
Amyloid Fibril Formation

The Sulfate Moieties of Glycosaminoglycans Are Critical for the Enhancement of β-Amyloid Protein Fibril Formation

2001 ◽  
Vol 72 (4) ◽  
pp. 1681-1687 ◽  
Author(s):  
Gerardo M. Castillo ◽  
Widia Lukito ◽  
Thomas N. Wight ◽  
Alan D. Snow
Keyword(s):  
Fibril Formation ◽  
Amyloid Protein ◽  
Β Amyloid ◽  
Protein Fibril

Type IV collagen prevents amyloid β-protein fibril formation

Life Sciences ◽  
2002 ◽  
Vol 70 (13) ◽  
pp. 1555-1564 ◽  
Author(s):  
Yoichi Kiuchi ◽  
Yoshihiko Isobe ◽  
Kiyomi Fukushima
Keyword(s):  
Type Iv Collagen ◽  
Amyloid Β ◽  
Fibril Formation ◽  
Amyloid Β Protein ◽  
Type Iv ◽  
Β Protein ◽  
Protein Fibril

scholarly journals Conformational change, aggregation and fibril formation induced by detergent treatments of cellular prion protein

2008 ◽  
Vol 79 (3) ◽  
pp. 669-678 ◽  
Author(s):  
Liang-Wen Xiong ◽  
Lynne D. Raymond ◽  
Stanley F. Hayes ◽  
Gregory J. Raymond ◽  
Byron Caughey
Keyword(s):  
Conformational Change ◽  
Prion Protein ◽  
Fibril Formation ◽  
Cellular Prion Protein
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