Cellular prion protein acquires resistance to proteolytic degradation following copper ion binding

2004 ◽  
Vol 385 (8) ◽  
Author(s):  
Thorsten Kuczius ◽  
Anne Buschmann ◽  
Wenlan Zhang ◽  
Helge Karch ◽  
Karsten Becker ◽  
...  
Keyword(s):  
Prion Protein ◽  
Copper Ion ◽  
Cellular Prion Protein ◽  
Proteolytic Degradation ◽  
Ion Binding

Copper(II) Ion Binding to Cellular Prion Protein

2008 ◽  
Vol 48 (2) ◽  
pp. 283-287 ◽  
Author(s):  
Jernej Zidar ◽  
Elizabeta T. Pirc ◽  
Milan Hodošček ◽  
Peter Bukovec
Keyword(s):  
Prion Protein ◽  
Cellular Prion Protein ◽  
Ion Binding

ChemInform Abstract: Copper(II) Ion Binding to Cellular Prion Protein.

ChemInform ◽  
2008 ◽  
Vol 39 (21) ◽  
Author(s):  
Jernej Zidar ◽  
Elizabeta T. Pirc ◽  
Milan Hodoscek ◽  
Peter Bukovec
Keyword(s):  
Prion Protein ◽  
Cellular Prion Protein ◽  
Ion Binding

scholarly journals Pharmacological inactivation of the prion protein by targeting a folding intermediate

2021 ◽  
Vol 4 (1) ◽  
Author(s):  
Giovanni Spagnolli ◽  
Tania Massignan ◽  
Andrea Astolfi ◽  
Silvia Biggi ◽  
Marta Rigoli ◽  
...  
Keyword(s):  
Prion Protein ◽  
Prion Diseases ◽  
Cellular Prion Protein ◽  
Surface Glycoprotein ◽  
Folding Intermediate ◽  
Biological Regulation ◽  
Cell Surface Glycoprotein ◽  
Folding Intermediates ◽  
Protein Levels ◽  
Small Molecule Ligands

AbstractRecent computational advancements in the simulation of biochemical processes allow investigating the mechanisms involved in protein regulation with realistic physics-based models, at an atomistic level of resolution. These techniques allowed us to design a drug discovery approach, named Pharmacological Protein Inactivation by Folding Intermediate Targeting (PPI-FIT), based on the rationale of negatively regulating protein levels by targeting folding intermediates. Here, PPI-FIT was tested for the first time on the cellular prion protein (PrP), a cell surface glycoprotein playing a key role in fatal and transmissible neurodegenerative pathologies known as prion diseases. We predicted the all-atom structure of an intermediate appearing along the folding pathway of PrP and identified four different small molecule ligands for this conformer, all capable of selectively lowering the load of the protein by promoting its degradation. Our data support the notion that the level of target proteins could be modulated by acting on their folding pathways, implying a previously unappreciated role for folding intermediates in the biological regulation of protein expression.

Peptide NMHRYPNQ of the Cellular Prion Protein (PrPC) Inhibits Aggregation and Is a Potential Key for Understanding Prion–Prion Interactions

2009 ◽  
Vol 392 (1) ◽  
pp. 198-207 ◽  
Author(s):  
Dirk Rehders ◽  
Birgit Claasen ◽  
Lars Redecke ◽  
Alexander Buschke ◽  
Caroline Reibe ◽  
...  
Keyword(s):  
Prion Protein ◽  
Cellular Prion Protein
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