scholarly journals Impact of Electronic Polarization on Preformed, β-Strand Rich Homogenous and Heterogenous Amyloid Oligomers

2021 ◽  
Author(s):  
Kelsie M. King ◽  
Amanda K. Sharp ◽  
Darcy S. Davidson ◽  
Anne M. Brown ◽  
Justin A. Lemkul
Keyword(s):  
Electronic Polarization ◽  
Amyloid Oligomers

scholarly journals Amyloid Oligomers Exacerbate Tau Pathology in a Mouse Model of Tauopathy

2012 ◽  
Vol 11 (4) ◽  
pp. 165-181 ◽  
Author(s):  
Maj-Linda B. Selenica ◽  
Milene Brownlow ◽  
Jeffy P. Jimenez ◽  
Daniel C. Lee ◽  
Gabriela Pena ◽  
...  
Keyword(s):  
Mouse Model ◽  
Tau Pathology ◽  
Amyloid Oligomers

scholarly journals Exploring amyloid oligomers with peptide model systems

2021 ◽  
Vol 64 ◽  
pp. 106-115
Author(s):  
Tuan D. Samdin ◽  
Adam G. Kreutzer ◽  
James S. Nowick
Keyword(s):  
Model Systems ◽  
Amyloid Oligomers

scholarly journals Cell stiffness and ROS level alterations in living neurons mediated by β-amyloid oligomers measured by scanning ion-conductance microscopy.

2021 ◽  
Vol 27 (S1) ◽  
pp. 500-502
Author(s):  
Oleg Suchalko ◽  
Roman Timoshenko ◽  
Alexander Vaneev ◽  
Vasilii Kolmogorov ◽  
Nikita Savin ◽  
...  
Keyword(s):  
Cell Stiffness ◽  
Ion Conductance ◽  
Scanning Ion Conductance Microscopy ◽  
Amyloid Oligomers ◽  
Β Amyloid ◽  
Living Neurons

scholarly journals The role of amyloid oligomers in neurodegenerative pathologies

2021 ◽  
Author(s):  
Cameron Wells ◽  
Samuel Brennan ◽  
Matt Keon ◽  
Lezanne Ooi
Keyword(s):  
Amyloid Oligomers

Visualization of spontaneous electronic polarization in Pb ion of ferroelectric PbTiO3 by synchrotron-radiation x-ray diffraction

2020 ◽  
Vol 117 (25) ◽  
pp. 252905
Author(s):  
Tomohiro Abe ◽  
Sangwook Kim ◽  
Chikako Moriyoshi ◽  
Yuuki Kitanaka ◽  
Yuji Noguchi ◽  
...  
Keyword(s):  
Synchrotron Radiation ◽  
X Ray Diffraction ◽  
Electronic Polarization ◽  
X Ray

scholarly journals Stabilization of neurotoxic Alzheimer amyloid-  oligomers by protein engineering

2010 ◽  
Vol 107 (35) ◽  
pp. 15595-15600 ◽  
Author(s):  
A. Sandberg ◽  
L. M. Luheshi ◽  
S. Sollvander ◽  
T. Pereira de Barros ◽  
B. Macao ◽  
...  
Keyword(s):  
Protein Engineering ◽  
Amyloid Oligomers

Diffusible amyloid oligomers trigger systemic amyloidosis in mice

2008 ◽  
Vol 415 (2) ◽  
pp. 207-215 ◽  
Author(s):  
Sivanesan Senthilkumar ◽  
Edwin Chang ◽  
Rajadas Jayakumar
Keyword(s):  
Protein A ◽  
Mouse Tissue ◽  
Cytokine Induction ◽  
Amyloidogenic Proteins ◽  
Enhancing Factor ◽  
Amyloid Oligomers ◽  
Apparent Relationship ◽  
Amyloid Enhancing Factor ◽  
Local Accumulation

AA (amyloid protein A) amyloidosis in mice is markedly accelerated when the animals are given, in addition to an inflammatory stimulus, an intravenous injection of protein extracted from AA-laden mouse tissue. Previous findings affirm that AA fibrils can enhance the in vivo amyloidogenic process by a nucleation seeding mechanism. Accumulating evidence suggests that globular aggregates rather than fibrils are the toxic entities responsible for cell death. In the present study we report on structural and morphological features of AEF (amyloid-enhancing factor), a compound extracted and partially purified from amyloid-laden spleen. Surprisingly, the chief amyloidogenic material identified in the active AEF was diffusible globular oligomers. This partially purified active extract triggered amyloid deposition in vital organs when injected intravenously into mice. This implies that such a phenomenon could have been inflicted through the nucleation seeding potential of toxic oligomers in association with altered cytokine induction. In the present study we report an apparent relationship between altered cytokine expression and AA accumulation in systemically inflamed tissues. The prevalence of serum AA monomers and proteolytic oligomers in spleen AEF is consistent to suggest that extrahepatic serum AA processing might lead to local accumulation of amyloidogenic proteins at the serum AA production site.

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