Simulations of biomolecules: characterization of the early steps in the pH-induced conformational conversion of the hamster, bovine and human forms of the prion protein

2002 ◽  
Vol 360 (1795) ◽  
pp. 1165-1178 ◽  
Author(s):  
Darwin O. V. Alonso ◽  
Chahm An ◽  
Valerie Daggett
Keyword(s):  
Prion Protein ◽  
Conformational Conversion

scholarly journals Structural characterization of POM 6 Fab and mouse prion protein complex identifies key regions for prions conformational conversion

FEBS Journal ◽  
2018 ◽  
Vol 285 (9) ◽  
pp. 1701-1714 ◽  
Author(s):  
Pravas Kumar Baral ◽  
Mridula Swayampakula ◽  
Adriano Aguzzi ◽  
Michael N. G. James
Keyword(s):  
Prion Protein ◽  
Structural Characterization ◽  
Protein Complex ◽  
Conformational Conversion

scholarly journals Characterization of four new monoclonal antibodies against the distal N-terminal region of PrPc

2014 ◽  
Author(s):  
Alessandro Didonna ◽  
Anja Colja Venturini ◽  
Katrina Hartman ◽  
Tanja Vranac ◽  
Vladka Curin Serbec ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Prion Protein ◽  
Biochemical Characterization ◽  
Prion Diseases ◽  
Physiological Role ◽  
Prion Infection ◽  
Promising Tool ◽  
C Terminus ◽  
N Terminus

Prion diseases are a group of fatal neurodegenerative disorders that affect humans and animals. They are characterized by the accumulation in the central nervous system of a pathological form of the host-encoded prion protein (PrPC). The prion protein is a membrane glycoprotein that consists of two domains: a globular, structured C-terminus and an unstructured N-terminus. The N-terminal part of the protein is involved in different functions in both health and disease. In the present work we discuss the production and biochemical characterization of a panel of four monoclonal antibodies (mAbs) against the distal N-terminus of PrPC using a well-established methodology based on the immunization of Prnp0/0 mice. Additionally, we show their ability to block prion (PrPSc) replication at nanomolar concentrations in a cell culture model of prion infection. These mAbs represent a promising tool for prion diagnostics and for studying the physiological role of the N-terminal domain of PrPC.

scholarly journals Prion protein and prion disease at a glance

2021 ◽  
Vol 134 (17) ◽  
Author(s):  
Caihong Zhu ◽  
Adriano Aguzzi
Keyword(s):  
Prion Protein ◽  
Prion Disease ◽  
Neurodegenerative Disorders ◽  
Prion Diseases ◽  
Amyloid Β ◽  
Cellular Prion Protein ◽  
Future Studies ◽  
Associated Proteins ◽  
Main Component ◽  
Conformational Conversion

ABSTRACT Prion diseases are neurodegenerative disorders caused by conformational conversion of the cellular prion protein (PrPC) into scrapie prion protein (PrPSc). As the main component of prion, PrPSc acts as an infectious template that recruits and converts normal cellular PrPC into its pathogenic, misfolded isoform. Intriguingly, the phenomenon of prionoid, or prion-like, spread has also been observed in many other disease-associated proteins, such as amyloid β (Aβ), tau and α-synuclein. This Cell Science at a Glance and the accompanying poster highlight recently described physiological roles of prion protein and the advanced understanding of pathogenesis of prion disease they have afforded. Importantly, prion protein may also be involved in the pathogenesis of other neurodegenerative disorders such as Alzheimer's and Parkinson's disease. Therapeutic studies of prion disease have also exploited novel strategies to combat these devastating diseases. Future studies on prion protein and prion disease will deepen our understanding of the pathogenesis of a broad spectrum of neurodegenerative conditions.

scholarly journals Characterization of Recombinant, Membrane-attached Full-length Prion Protein

2004 ◽  
Vol 279 (24) ◽  
pp. 25058-25065 ◽  
Author(s):  
Heike Eberl ◽  
Peter Tittmann ◽  
Rudi Glockshuber
Keyword(s):  
Prion Protein ◽  
Full Length

Characterization of the F198S prion protein mutation: Enhanced glycosylation and defective refolding

2005 ◽  
Vol 7 (2) ◽  
pp. 159-171 ◽  
Author(s):  
Syed I.A. Zaidi ◽  
Sandra L. Richardson ◽  
Sabina Capellari ◽  
Li Song ◽  
Mark A. Smith ◽  
...  
Keyword(s):  
Prion Protein ◽  
Protein Mutation

scholarly journals Characterization of Detergent-insoluble Complexes Containing the Cellular Prion Protein and Its Scrapie Isoform

1997 ◽  
Vol 272 (10) ◽  
pp. 6324-6331 ◽  
Author(s):  
Naava Naslavsky ◽  
Ronit Stein ◽  
Anat Yanai ◽  
Gilgi Friedlander ◽  
Albert Taraboulos
Keyword(s):  
Prion Protein ◽  
Cellular Prion Protein

Proteomics Approach to Identify the Interacting Partners of Cellular Prion Protein and Characterization of Rab7a Interaction in Neuronal Cells

2011 ◽  
Vol 10 (7) ◽  
pp. 3123-3135 ◽  
Author(s):  
Saima Zafar ◽  
Nicolas von Ahsen ◽  
Michael Oellerich ◽  
Inga Zerr ◽  
Walter J. Schulz-Schaeffer ◽  
...  
Keyword(s):  
Prion Protein ◽  
Neuronal Cells ◽  
Cellular Prion Protein ◽  
Proteomics Approach
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