Destabilization of polar interactions in the prion protein triggers misfolding and oligomerization

2021 ◽  
Author(s):  
Suhas H Bhate ◽  
Jayant B Udgaonkar ◽  
Ranabir Das
Keyword(s):  
Prion Protein ◽  
Polar Interactions

Metallic prions

2004 ◽  
Vol 71 ◽  
pp. 193-202 ◽  
Author(s):  
David R Brown
Keyword(s):  
Prion Protein ◽  
Binding Capacity ◽  
Normal Function ◽  
Transmissible Spongiform Encephalopathies ◽  
Published Data ◽  
Normal Brain ◽  
Copper Binding ◽  
Loss Of Function ◽  
Spongiform Encephalopathies ◽  
The Brain

Prion diseases, also referred to as transmissible spongiform encephalopathies, are characterized by the deposition of an abnormal isoform of the prion protein in the brain. However, this aggregated, fibrillar, amyloid protein, termed PrPSc, is an altered conformer of a normal brain glycoprotein, PrPc. Understanding the nature of the normal cellular isoform of the prion protein is considered essential to understanding the conversion process that generates PrPSc. To this end much work has focused on elucidation of the normal function and activity of PrPc. Substantial evidence supports the notion that PrPc is a copper-binding protein. In conversion to the abnormal isoform, this Cu-binding activity is lost. Instead, there are some suggestions that the protein might bind other metals such as Mn or Zn. PrPc functions currently under investigation include the possibility that the protein is involved in signal transduction, cell adhesion, Cu transport and resistance to oxidative stress. Of these possibilities, only a role in Cu transport and its action as an antioxidant take into consideration PrPc's Cu-binding capacity. There are also more published data supporting these two functions. There is strong evidence that during the course of prion disease, there is a loss of function of the prion protein. This manifests as a change in metal balance in the brain and other organs and substantial oxidative damage throughout the brain. Thus prions and metals have become tightly linked in the quest to understand the nature of transmissible spongiform encephalopathies.

CHARACTERISTICS OF ALLELE POOL OF THE ROMANOV SHEEP BREED FOR THE PRION PROTEIN GENE ASSOCIATED WITH GENETIC SUSTAINABILITY TO SCRAPIE

2017 ◽  
Vol 52 (6) ◽  
pp. 1157-1165
Author(s):  
E.A. Gladyr ◽  
◽  
T.E. Deniskova ◽  
V.A. Bagirov ◽  
O.V. Kostyunina ◽  
...  
Keyword(s):  
Prion Protein ◽  
Protein Gene ◽  
Sheep Breed ◽  
Prion Protein Gene ◽  
Allele Pool

A Unique Functional Feature of the Recombinant Bovine Prion Protein Fragment

2014 ◽  
Author(s):  
Ying Zhai ◽  
Na Li ◽  
Dachuan Zhang ◽  
Qi Li ◽  
Guoping Zhou ◽  
...  
Keyword(s):  
Prion Protein ◽  
Protein Fragment ◽  
Functional Feature
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