scholarly journals β-Amyloid 42; prion protein (PRNP; PrP; CD230)

2012 ◽  
Vol 5 (36) ◽  
pp. 953-953
Keyword(s):  
Prion Protein ◽  
Β Amyloid

scholarly journals Erratum: Characterizing affinity epitopes between prion protein and β-amyloid using an epitope mapping immunoassay

2014 ◽  
Vol 46 (5) ◽  
pp. e96-e96
Author(s):  
Mino Kang ◽  
Su Yeon Kim ◽  
Seong Soo A An ◽  
Young Ran Ju
Keyword(s):  
Prion Protein ◽  
Epitope Mapping ◽  
Β Amyloid

Caspase-3 activation by β-amyloid and prion protein peptides is independent from their neurotoxic effect

2000 ◽  
Vol 293 (3) ◽  
pp. 207-210 ◽  
Author(s):  
Javier Sáez-Valero ◽  
Nadia Angeretti ◽  
Gianluigi Forloni
Keyword(s):  
Prion Protein ◽  
Caspase 3 ◽  
Neurotoxic Effect ◽  
Β Amyloid

scholarly journals β-amyloid oligomers and prion protein

Prion ◽  
2011 ◽  
Vol 5 (1) ◽  
pp. 10-15 ◽  
Author(s):  
Gianluigi Forloni ◽  
Claudia Balducci
Keyword(s):  
Prion Protein ◽  
Amyloid Oligomers ◽  
Β Amyloid

Amyloidogenic metal-binding proteins: new investigative pathways

2008 ◽  
Vol 36 (6) ◽  
pp. 1299-1303 ◽  
Author(s):  
Paul Davies ◽  
Sarah N. Fontaine ◽  
Dima Moualla ◽  
Xiaoyan Wang ◽  
Josephine A. Wright ◽  
...  
Keyword(s):  
Amyloid Precursor Protein ◽  
Neurodegenerative Diseases ◽  
Prion Protein ◽  
Metal Binding ◽  
Binding Proteins ◽  
Normal Function ◽  
Amyloidogenic Proteins ◽  
Logical Reason ◽  
Associated Proteins ◽  
Β Amyloid

Neurodegenerative diseases remain perplexing and problematic for modern research. Those associated with amyloidogenic proteins have often been lumped together simply because those proteins aggregate. However, research has identified a more logical reason to group some of these diseases together. The associated proteins not only aggregate, but also bind copper. The APP (amyloid precursor protein) binds copper in an N-terminal region. Binding of copper has been suggested to influence generation of β-amyloid from the protein. PrP (prion protein) binds copper, and this appears to be necessary for its normal function and might also reduce its probability of conversion into an infectious prion. α-Synuclein, a protein associated with Parkinson's disease, also binds copper, but, in this case, it potentially increases the rate at which the protein aggregates. The similarities between these proteins, in terms of metal binding, has allowed us to investigate them using similar approaches. In the present review, we discuss some of these approaches.

scholarly journals Extending the functional characteristics of naturally occurring autoantibodies against β-Amyloid, Prion Protein and α-Synuclein

PLoS ONE ◽  
2018 ◽  
Vol 13 (8) ◽  
pp. e0202954 ◽  
Author(s):  
Alexandra Albus ◽  
Maike Gold ◽  
Jan-Philipp Bach ◽  
Monika Burg-Roderfeld ◽  
Marit Jördens ◽  
...  
Keyword(s):  
Prion Protein ◽  
Functional Characteristics ◽  
Naturally Occurring ◽  
Β Amyloid

Cellular prion protein modulates β-amyloid deposition in aged APP/PS1 transgenic mice

2013 ◽  
Vol 34 (12) ◽  
pp. 2793-2804 ◽  
Author(s):  
Lara Ordóñez-Gutiérrez ◽  
Juan María Torres ◽  
Rosalina Gavín ◽  
Marta Antón ◽  
Ana Isabel Arroba-Espinosa ◽  
...  
Keyword(s):  
Transgenic Mice ◽  
Prion Protein ◽  
Amyloid Deposition ◽  
Cellular Prion Protein ◽  
Β Amyloid
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