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Barry D. Greenberg

Researcher at Pfizer

Publications -  37
Citations -  2156

Barry D. Greenberg is an academic researcher from Pfizer. The author has contributed to research in topics: Amyloid precursor protein & Senile plaques. The author has an hindex of 21, co-authored 29 publications receiving 2065 citations. Previous affiliations of Barry D. Greenberg include Case Western Reserve University & University of Pennsylvania.

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Potentially amyloidogenic, carboxyl-terminal derivatives of the amyloid protein precursor.

TL;DR: This analysis showed that the beta APP is normally processed into a complex set of 8- to 12-kilodalton carboxyl-terminal derivatives, and the two largest derivatives in human brain have the entire beta AP at or near their amino terminus and are likely to be intermediates in the pathway leading to amyloid deposition.
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Senile plaque neurites in Alzheimer disease accumulate amyloid precursor protein.

TL;DR: The findings suggest that APP accumulation in senile plaque neurites occurs prior to tau accumulation and is therefore more closely related to appearance of neuritic dystrophy.
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Neuronal and microglial involvement in β-amyloid protein deposition in Alzheimer's disease

TL;DR: The findings suggest that neuronally derived APP is the source for senile plaque beta-amyloid protein, while microglia may act as processing cells in Alzheimer's disease patients.
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Defined neurofilament, tau, and beta-amyloid precursor protein epitopes distinguish Alzheimer from non-Alzheimer senile plaques

TL;DR: Differences between the complement of beta-APP, tau, and NF protein epitopes in AD versus non-AD brains implicate a defect involving one or more steps in the posttranslational modification, degradation, or elimination of these proteins in AD brains, and this may account for the massive numbers of SPs that characterize AD.
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Expression patterns of β‐amyloid precursor protein (β‐APP) in neural and nonneural human tissues from alzheimer's disease and control subjects

TL;DR: β‐APPs produced in the brain are sources of β‐APP peptides that accumulate as senile plaques in AD, and are detectable only in a limited number of nonneural tissues.