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Alzheimer amyloid-beta peptide aggre...

Gorman, Paul Martin.

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Alzheimer amyloid-beta peptide aggregation: A potential in vivo model of early aggregate formation.

Record Type:	Electronic resources : Monograph/item
Title/Author:	Alzheimer amyloid-beta peptide aggregation: A potential in vivo model of early aggregate formation./
Author:	Gorman, Paul Martin.
Description:	90 p.
Notes:	Source: Masters Abstracts International, Volume: 41-03, page: 0743.
Contained By:	Masters Abstracts International41-03.
Subject:	Biophysics, Medical. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=MQ74053
ISBN:	0612740536

Alzheimer amyloid-beta peptide aggregation: A potential in vivo model of early aggregate formation.
Gorman, Paul Martin.

Alzheimer amyloid-beta peptide aggregation: A potential in vivo model of early aggregate formation. - 90 p.

Source: Masters Abstracts International, Volume: 41-03, page: 0743.

Thesis (M.Sc.)--University of Toronto (Canada), 2002.

Alzheimer's Disease (AD) is neuropathologically characterized by the presence of senile plaques, neurofibrillary tangles and selective neuronal loss. The polymerization of the amyloid-beta peptide (Abeta) to form the fibrillar core of senile plaques is associated with neurodegeneration. Researchers have thus investigated this fibrillogenic process as well as the toxicity of the Abeta fibrils. Recent discoveries, however, suggest that early intermediate structures possess potent neurotoxic potential. Therefore, we sought to examine the early events of Abeta oligomerization. It is known that one of the major routes of Abeta production is via the endocytic-recycling pathway, hence we investigated aggregation at the endosomal pH of 6. At endosomal pH, Abeta40 associates via a branched pathway to form a variety of Abeta aggregates. We investigated the kinetics and equilibrium between them. The following thesis provides an introduction to Alzheimer's disease and an in-depth assessment into the new insights provided by this research.

ISBN: 0612740536Subjects--Topical Terms:

1017681
Biophysics, Medical.

Alzheimer amyloid-beta peptide aggregation: A potential in vivo model of early aggregate formation.
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520 $a Alzheimer's Disease (AD) is neuropathologically characterized by the presence of senile plaques, neurofibrillary tangles and selective neuronal loss. The polymerization of the amyloid-beta peptide (Abeta) to form the fibrillar core of senile plaques is associated with neurodegeneration. Researchers have thus investigated this fibrillogenic process as well as the toxicity of the Abeta fibrils. Recent discoveries, however, suggest that early intermediate structures possess potent neurotoxic potential. Therefore, we sought to examine the early events of Abeta oligomerization. It is known that one of the major routes of Abeta production is via the endocytic-recycling pathway, hence we investigated aggregation at the endosomal pH of 6. At endosomal pH, Abeta40 associates via a branched pathway to form a variety of Abeta aggregates. We investigated the kinetics and equilibrium between them. The following thesis provides an introduction to Alzheimer's disease and an in-depth assessment into the new insights provided by this research.
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