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

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

2013 ◽  
Vol 45 (8) ◽  
pp. e34-e34 ◽  
Author(s):  
Mino Kang ◽  
Su Yeon Kim ◽  
Seong Soo A An ◽  
Young Ran Ju
Keyword(s):  
Prion Protein ◽  
Epitope Mapping ◽  
Β Amyloid

Epitope mapping on bovine prion protein using chemical cross-linking and mass spectrometry

2008 ◽  
Vol 43 (2) ◽  
pp. 185-195 ◽  
Author(s):  
Tatiana Pimenova ◽  
Alexis Nazabal ◽  
Bernd Roschitzki ◽  
Jan Seebacher ◽  
Oliver Rinner ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Prion Protein ◽  
Epitope Mapping ◽  
Cross Linking ◽  
Chemical Cross Linking

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 Epitope Mapping Immunoassay Analysis of the Interaction between β-Amyloid and Fibrinogen

2019 ◽  
Vol 20 (3) ◽  
pp. 496 ◽  
Author(s):  
Vo Van Giau ◽  
Seong An
Keyword(s):  
Mouse Models ◽  
Central Region ◽  
Epitope Mapping ◽  
Polyclonal Antibodies ◽  
Fibrin Clot ◽  
Fibrin Deposition ◽  
Therapeutic Approaches ◽  
Substantial Evidence ◽  
Blood Clots ◽  
Β Amyloid

The vast majority of patients with Alzheimer’s disease (AD) suffer from impaired cerebral circulation. Substantial evidence indicates that fibrinogen (Fbg) and fibrin clot formation play an important role in this circulatory dysfunction in AD. Fbg interacts with β-amyloid (1-42) (Aβ), forming plasmin-resistant abnormal blood clots, and increased fibrin deposition has been discovered in the brains of AD patients and mouse models. In this study, biochemical approaches and the epitope mapping immunoassay were employed to characterize binding epitopes within the Fbg and complementary epitopes in Aβ. We discovered the Aβ5–25 peptide as the most critical region for the interaction, which can be inhibited by specific monoclonal and polyclonal antibodies against the central region of Aβ. Aβ binding to Fbg may block plasmin-mediated fibrin cleavage at this site, resulting in the generation of increased levels of plasmin-resistant fibrin degradation fragments. Our study elucidates the Aβ–Fbg interaction that may involve the mechanism by which Aβ–Fbg binding delays fibrinolysis by plasmin, providing valuable information in the development of therapeutic approaches for AD.

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