Molecular polymorphism of Aβ in Alzheimer's disease

Harry LeVine; Lary C. Walker

doi:10.1016/j.neurobiolaging.2008.05.026

Molecular polymorphism of Aβ in Alzheimer's disease

Harry LeVine, Lary C. Walker

Molecular and Cellular Biochemistry

Research output: Contribution to journal › Comment/debate

49 Scopus citations

Abstract

Alzheimer's disease is defined pathologically by the presence of senile plaques, which consist primarily of extracellular aggregates of fibrillar Aβ peptide, and neurofibrillary tangles, which are abnormal, intracellular bundles of fibrillar tau protein. The advent of amyloid binding agents as diagnostic imaging probes for Alzheimer's disease (AD) has made it imperative to understand at a molecular and disease level what these ligands are reporting. In addition to improving the accuracy of diagnosis, we argue that these selective ligands can serve as probes for molecular polymorphisms that may govern the pathogenicity of abnormal protein aggregates.

Original language	English
Pages (from-to)	542-548
Number of pages	7
Journal	Neurobiology of Aging
Volume	31
Issue number	4
DOIs	https://doi.org/10.1016/j.neurobiolaging.2008.05.026
State	Published - Apr 2010

Bibliographical note

Funding Information:
Support is acknowledged from the Woodruff Foundation, NIH RR-00165, P01 AG026423-01A2, and from the Sanders-Brown Center on Aging and Chandler Medical Center of the University of Kentucky.

Funding

Support is acknowledged from the Woodruff Foundation, NIH RR-00165, P01 AG026423-01A2, and from the Sanders-Brown Center on Aging and Chandler Medical Center of the University of Kentucky.

Funders	Funder number
Chandler Medical Center of the University of Kentucky
Sanders-Brown Center on Aging
National Institutes of Health (NIH)	RR-00165, P01 AG026423-01A2
National Institute on Aging	P01AG005119
Woodruff Foundation

Keywords

Congo Red
High affinity binding
PIB
Polythiophene
Stoichiometry
Thioflavine T
Transgenic mice

ASJC Scopus subject areas

General Neuroscience
Aging
Developmental Biology
Clinical Neurology
Geriatrics and Gerontology

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10.1016/j.neurobiolaging.2008.05.026

Cite this

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title = "Molecular polymorphism of Aβ in Alzheimer's disease",

abstract = "Alzheimer's disease is defined pathologically by the presence of senile plaques, which consist primarily of extracellular aggregates of fibrillar Aβ peptide, and neurofibrillary tangles, which are abnormal, intracellular bundles of fibrillar tau protein. The advent of amyloid binding agents as diagnostic imaging probes for Alzheimer's disease (AD) has made it imperative to understand at a molecular and disease level what these ligands are reporting. In addition to improving the accuracy of diagnosis, we argue that these selective ligands can serve as probes for molecular polymorphisms that may govern the pathogenicity of abnormal protein aggregates.",

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author = "Harry LeVine and Walker, \{Lary C.\}",

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AU - Walker, Lary C.

N1 - Funding Information: Support is acknowledged from the Woodruff Foundation, NIH RR-00165, P01 AG026423-01A2, and from the Sanders-Brown Center on Aging and Chandler Medical Center of the University of Kentucky.

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N2 - Alzheimer's disease is defined pathologically by the presence of senile plaques, which consist primarily of extracellular aggregates of fibrillar Aβ peptide, and neurofibrillary tangles, which are abnormal, intracellular bundles of fibrillar tau protein. The advent of amyloid binding agents as diagnostic imaging probes for Alzheimer's disease (AD) has made it imperative to understand at a molecular and disease level what these ligands are reporting. In addition to improving the accuracy of diagnosis, we argue that these selective ligands can serve as probes for molecular polymorphisms that may govern the pathogenicity of abnormal protein aggregates.

AB - Alzheimer's disease is defined pathologically by the presence of senile plaques, which consist primarily of extracellular aggregates of fibrillar Aβ peptide, and neurofibrillary tangles, which are abnormal, intracellular bundles of fibrillar tau protein. The advent of amyloid binding agents as diagnostic imaging probes for Alzheimer's disease (AD) has made it imperative to understand at a molecular and disease level what these ligands are reporting. In addition to improving the accuracy of diagnosis, we argue that these selective ligands can serve as probes for molecular polymorphisms that may govern the pathogenicity of abnormal protein aggregates.

KW - Congo Red

KW - High affinity binding

KW - PIB

KW - Polythiophene

KW - Stoichiometry

KW - Thioflavine T

KW - Transgenic mice

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Molecular polymorphism of Aβ in Alzheimer's disease

Abstract

Bibliographical note

Funding

Keywords

ASJC Scopus subject areas

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