scholarly journals Differences in the Cellular Uptake and Intracellular Itineraries of Amyloid Beta Proteins 40 and 42: Ramifications for the Alzheimer’s Drug Discovery

2012 ◽  
Vol 9 (7) ◽  
pp. 1887-1897 ◽  
Author(s):  
Rajesh S. Omtri ◽  
Michael W. Davidson ◽  
Balasubramaniam Arumugam ◽  
Joseph F. Poduslo ◽  
Karunya K. Kandimalla
Keyword(s):  
Drug Discovery ◽  
Cellular Uptake ◽  
Amyloid Beta ◽  
Beta Proteins ◽  
Amyloid Beta Proteins

Detection of Amyloid-Beta Proteins during Fibrillization Process by Liposome-Immobilized Microcantilevers in Microfluidic Channel

2015 ◽  
Author(s):  
M. Sohgawa ◽  
Z. Zhang ◽  
Y. Abe ◽  
T. Abe ◽  
K. Yamashita ◽  
...  
Keyword(s):  
Amyloid Beta ◽  
Microfluidic Channel ◽  
Beta Proteins ◽  
Amyloid Beta Proteins

scholarly journals Cross-seeding of wild-type and hereditary variant-type amyloid beta-proteins in the presence of gangliosides

2005 ◽  
Vol 95 (4) ◽  
pp. 1167-1176 ◽  
Author(s):  
Naoki Yamamoto ◽  
Katsumi Matsuzaki ◽  
Katsuhiko Yanagisawa
Keyword(s):  
Amyloid Beta ◽  
Wild Type ◽  
Variant Type ◽  
Beta Proteins ◽  
Amyloid Beta Proteins

Dendron-Modified Polystyrene Microtiter Plate: Surface Characterization with Picoforce AFM and Influence of Spacing between Immobilized Amyloid Beta Proteins

Langmuir ◽  
2008 ◽  
Vol 24 (24) ◽  
pp. 14296-14305 ◽  
Author(s):  
Dhruvajyoti Roy ◽  
Ju-Won Kwak ◽  
Wan Joo Maeng ◽  
Hyungjun Kim ◽  
Joon Won Park
Keyword(s):  
Amyloid Beta ◽  
Surface Characterization ◽  
Microtiter Plate ◽  
Plate Surface ◽  
Polystyrene Microtiter Plate ◽  
Beta Proteins ◽  
Amyloid Beta Proteins ◽  
Modified Polystyrene

P3-091: Specific conformational detection of beta-sheet rich amyloid beta proteins using conformationally dynamic Pronucleon™ peptides

2008 ◽  
Vol 4 ◽  
pp. T544-T545
Author(s):  
Gretchen L. Schieber ◽  
Roxanne Duan ◽  
Jonathan Moll ◽  
Craig Nelsen ◽  
Andrew Nyborg ◽  
...  
Keyword(s):  
Amyloid Beta ◽  
Beta Sheet ◽  
Beta Proteins ◽  
Amyloid Beta Proteins

Effects of a behaviorally active antibody on the brain uptake and clearance of amyloid beta proteins

Peptides ◽  
2005 ◽  
Vol 26 (2) ◽  
pp. 287-294 ◽  
Author(s):  
William A. Banks ◽  
Patrizia Pagliari ◽  
Ryota Nakaoke ◽  
John E. Morley
Keyword(s):  
Amyloid Beta ◽  
Brain Uptake ◽  
Beta Proteins ◽  
Amyloid Beta Proteins ◽  
The Brain

scholarly journals Amyloid Beta Proteins Modified by PUFA Oxidation Products in Alzheimer's Disease Brain

2018 ◽  
Vol 114 (3) ◽  
pp. 229a-230a
Author(s):  
Haralambos A. Mourelatos ◽  
Hiroaki Komatsu ◽  
Ran Furman ◽  
Giuseppe Grasso ◽  
Paul H. Axelsen
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Amyloid Beta ◽  
Oxidation Products ◽  
Beta Proteins ◽  
Amyloid Beta Proteins

500 Aggregations of amyloid beta-proteins in the presence of metal ions

2003 ◽  
Vol 144 ◽  
pp. s134 ◽  
Author(s):  
K. Yano ◽  
N. Hirosawa ◽  
Y. Sakamoto ◽  
H. Katayama ◽  
T. Moriguchi
Keyword(s):  
Metal Ions ◽  
Amyloid Beta ◽  
Beta Proteins ◽  
Amyloid Beta Proteins

scholarly journals Dielectrophoresis of Amyloid-Beta Proteins as a Microfluidic Template for Alzheimer’s Research

2019 ◽  
Vol 20 (14) ◽  
pp. 3595 ◽  
Author(s):  
Salman Ali Al-Ahdal ◽  
Aminuddin Bin Ahmad Kayani ◽  
Mohd Anuar Md Ali ◽  
Jun Yuan Chan ◽  
Talal Ali ◽  
...  
Keyword(s):  
Amyloid Beta ◽  
High Frequency ◽  
Low Temperatures ◽  
Electrode Array ◽  
Transformation Process ◽  
Yeast Cells ◽  
Negative Change ◽  
Beta Proteins ◽  
Higher Temperature ◽  
Amyloid Beta Proteins

We employed dielectrophoresis to a yeast cell suspension containing amyloid-beta proteins (Aβ) in a microfluidic environment. The Aβ was separated from the cells and characterized using the gradual dissolution of Aβ as a function of the applied dielectrophoretic parameters. We established the gradual dissolution of Aβ under specific dielectrophoretic parameters. Further, Aβ in the fibril form at the tip of the electrode dissolved at high frequency. This was perhaps due to the conductivity of the suspending medium changing according to the frequency, which resulted in a higher temperature at the tips of the electrodes, and consequently in the breakdown of the hydrogen bonds. However, those shaped as spheroidal monomers experienced a delay in the Aβ fibril transformation process. Yeast cells exposed to relatively low temperatures at the base of the electrode did not experience a positive or negative change in viability. The DEP microfluidic platform incorporating the integrated microtip electrode array was able to selectively manipulate the yeast cells and dissolve the Aβ to a controlled extent. We demonstrate suitable dielectrophoretic parameters to induce such manipulation, which is highly relevant for Aβ-related colloidal microfluidic research and could be applied to Alzheimer’s research in the future.

Is Olfactory Epithelium Biopsy Useful for Confirming Alzheimer’s Disease?

2018 ◽  
Vol 128 (3) ◽  
pp. 184-192 ◽  
Author(s):  
Maria Dantas Costa Lima Godoy ◽  
Marco Aurélio Fornazieri ◽  
Richard L. Doty ◽  
Fábio de Rezende Pinna ◽  
José Marcelo Farfel ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Amyloid Beta ◽  
Olfactory Epithelium ◽  
Clinical Symptoms ◽  
Middle Turbinate ◽  
Superior Turbinate ◽  
Significant Difference ◽  
Amyloid Beta Proteins

Objectives: The clinical symptoms of Alzheimer’s disease (AD) are preceded by a long asymptomatic period associated with “silent” deposition of aberrant paired helical filament (PHF)-tau and amyloid-beta proteins in brain tissue. Similar depositions have been reported within the olfactory epithelium (OE), a tissue that can be biopsied in vivo. The degree to which such biopsies are useful in identifying AD is controversial. This postmortem study had 3 main goals: first, to quantify the relative densities of AD-related proteins in 3 regions of the olfactory neuroepithelium, namely, the nasal septum, middle turbinate, and superior turbinate; second, to establish whether such densities are correlated among these epithelial regions as well as with semi-quantitative ratings of general brain cortex pathology; and third, to evaluate correlations between the protein densities and measures of antemortem cognitive function. Methods: Postmortem blocks of olfactory mucosa were obtained from 12 AD cadavers and 24 controls and subjected to amyloid-beta and PHF-tau immunohistochemistry. Results: We observed marked heterogeneity in the presence of the biomarkers of tau and amyloid-beta among the targeted olfactory epithelial regions. No significant difference was observed between the cadavers with AD and the controls regarding the concentration of these proteins in any of these epithelial regions. Only one correlation significant was evident, namely, that between the tau protein densities of the middle and the upper turbinate ( r = .58, P = .002). Conclusion: AD-related biomarker heterogeneity, which has not been previously demonstrated, makes comparisons across studies difficult and throws into question the usefulness of OE amyloid-beta and PHF-tau biopsies in detecting AD.

scholarly journals Amyloid seeds formed by cellular uptake, concentration, and aggregation of the amyloid-beta peptide

2009 ◽  
Vol 106 (48) ◽  
pp. 20324-20329 ◽  
Author(s):  
X. Hu ◽  
S. L. Crick ◽  
G. Bu ◽  
C. Frieden ◽  
R. V. Pappu ◽  
...  
Keyword(s):  
Cellular Uptake ◽  
Amyloid Beta ◽  
Amyloid Beta Peptide ◽  
Beta Peptide
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