scholarly journals Early and Selective Impairments in Axonal Transport Kinetics of Synaptic Cargoes Induced by Soluble Amyloid β-Protein Oligomers

Traffic ◽  
2012 ◽  
Vol 13 (5) ◽  
pp. 681-693 ◽  
Author(s):  
Yong Tang ◽  
David A. Scott ◽  
Utpal Das ◽  
Steven D. Edland ◽  
Kryslaine Radomski ◽  
...  
Keyword(s):  
Axonal Transport ◽  
Amyloid Β ◽  
Transport Kinetics ◽  
Amyloid Β Protein ◽  
Β Protein ◽  
Kinetics Of

Kinetics of secretion of amyloid β-protein and secreted APP

1994 ◽  
Vol 19 ◽  
pp. S169
Author(s):  
Wataru Araki ◽  
Kunishita Tatsuhide ◽  
Tabira Takeshi
Keyword(s):  
Amyloid Β ◽  
Amyloid Β Protein ◽  
Β Protein ◽  
Kinetics Of

Kinetics of peptide secondary structure conversion during amyloid β-protein fibrillogenesis

2012 ◽  
Vol 301 ◽  
pp. 95-102 ◽  
Author(s):  
Timothy Steckmann ◽  
Zubair Awan ◽  
Bernard S. Gerstman ◽  
Prem P. Chapagain
Keyword(s):  
Secondary Structure ◽  
Amyloid Β ◽  
Amyloid Β Protein ◽  
Β Protein ◽  
Peptide Secondary Structure ◽  
Kinetics Of

scholarly journals Kinetics of Amyloid β-Protein Degradation Determined by Novel Fluorescence- and Fluorescence Polarization-based Assays

2003 ◽  
Vol 278 (39) ◽  
pp. 37314-37320 ◽  
Author(s):  
Malcolm A. Leissring ◽  
Alice Lu ◽  
Margaret M. Condron ◽  
David B. Teplow ◽  
Ross L. Stein ◽  
...  
Keyword(s):  
Protein Degradation ◽  
Fluorescence Polarization ◽  
Amyloid Β ◽  
Amyloid Β Protein ◽  
Β Protein ◽  
Kinetics Of

scholarly journals Glutamate and Amyloid β-Protein Rapidly Inhibit Fast Axonal Transport in Cultured Rat Hippocampal Neurons by Different Mechanisms

2003 ◽  
Vol 23 (26) ◽  
pp. 8967-8977 ◽  
Author(s):  
Hiromi Hiruma ◽  
Takashi Katakura ◽  
Sanae Takahashi ◽  
Takafumi Ichikawa ◽  
Tadashi Kawakami
Keyword(s):  
Axonal Transport ◽  
Hippocampal Neurons ◽  
Amyloid Β ◽  
Amyloid Β Protein ◽  
Fast Axonal Transport ◽  
Β Protein

scholarly journals Dual Effect of Thioflavin T on the Nucleation Kinetics of Amyloid β-Protein 40

2016 ◽  
Vol 32 (6) ◽  
pp. 1391-1396 ◽  
Author(s):  
Song LI ◽  
◽  
Fu-Feng LIU ◽  
Lin-Ling YU ◽  
Yan-Jiao ZHAO ◽  
...  
Keyword(s):  
Amyloid Β ◽  
Thioflavin T ◽  
Amyloid Β Protein ◽  
Nucleation Kinetics ◽  
Dual Effect ◽  
Β Protein ◽  
Kinetics Of

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.

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