scholarly journals A Key Role for Lysine Residues in Amyloid β-Protein Folding, Assembly, and Toxicity

2012 ◽  
Vol 3 (6) ◽  
pp. 473-481 ◽  
Author(s):  
Sharmistha Sinha ◽  
Dahabada H. J. Lopes ◽  
Gal Bitan
Keyword(s):  
Protein Folding ◽  
Amyloid Β ◽  
Amyloid Β Protein ◽  
Β Protein ◽  
Lysine Residues

Elucidating Amyloid β-Protein Folding and Assembly:  A Multidisciplinary Approach

2006 ◽  
Vol 39 (9) ◽  
pp. 635-645 ◽  
Author(s):  
David B. Teplow ◽  
Noel D. Lazo ◽  
Gal Bitan ◽  
Summer Bernstein ◽  
Thomas Wyttenbach ◽  
...  
Keyword(s):  
Protein Folding ◽  
Multidisciplinary Approach ◽  
Amyloid Β ◽  
Amyloid Β Protein ◽  
Β Protein ◽  
Protein Folding And Assembly

scholarly journals Extracellular Protein Aggregates Colocalization and Neuronal Dystrophy in Comorbid Alzheimer’s and Creutzfeldt–Jakob Disease: A Micromorphological Pilot Study on 20 Brains

2021 ◽  
Vol 22 (4) ◽  
pp. 2099
Author(s):  
Nikol Jankovska ◽  
Tomas Olejar ◽  
Radoslav Matej
Keyword(s):  
Prion Protein ◽  
Fluorescent Microscopy ◽  
Amyloid Β ◽  
Amyloid Β Protein ◽  
Β Protein ◽  
Key Characteristics ◽  
Jakob Disease ◽  
Immunohistochemical Methods ◽  
Confocal Fluorescent Microscopy ◽  
Codon 129

Alzheimer’s disease (AD) and sporadic Creutzfeldt–Jakob disease (sCJD) are both characterized by extracellular pathologically conformed aggregates of amyloid proteins—amyloid β-protein (Aβ) and prion protein (PrPSc), respectively. To investigate the potential morphological colocalization of Aβ and PrPSc aggregates, we examined the hippocampal regions (archicortex and neocortex) of 20 subjects with confirmed comorbid AD and sCJD using neurohistopathological analyses, immunohistochemical methods, and confocal fluorescent microscopy. Our data showed that extracellular Aβ and PrPSc aggregates tended to be, in most cases, located separately, and “compound” plaques were relatively rare. We observed PrPSc plaque-like structures in the periphery of the non-compact parts of Aβ plaques, as well as in tau protein-positive dystrophic structures. The AD ABC score according to the NIA-Alzheimer’s association guidelines, and prion protein subtype with codon 129 methionine–valine (M/V) polymorphisms in sCJD, while representing key characteristics of these diseases, did not correlate with the morphology of the Aβ/PrPSc co-aggregates. However, our data showed that PrPSc aggregation could dominate during co-aggregation with non-compact Aβ in the periphery of Aβ plaques.

scholarly journals Correction to: Amyloid β-protein oligomers promote the uptake of tau fibril seeds potentiating intracellular tau aggregation

2021 ◽  
Vol 13 (1) ◽  
Author(s):  
Woo Shik Shin ◽  
Jing Di ◽  
Qin Cao ◽  
Binsen Li ◽  
Paul M. Seidler ◽  
...  
Keyword(s):  
Amyloid Β ◽  
Amyloid Β Protein ◽  
Β Protein ◽  
Tau Aggregation

An amendment to this paper has been published and can be accessed via the original article.

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