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John Q. Trojanowski

Researcher at University of Pennsylvania

Publications -  1538
Citations -  245534

John Q. Trojanowski is an academic researcher from University of Pennsylvania. The author has contributed to research in topics: Dementia & Alzheimer's disease. The author has an hindex of 226, co-authored 1467 publications receiving 213948 citations. Previous affiliations of John Q. Trojanowski include Vanderbilt University & University of California, San Francisco.

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The Levels of Soluble versus Insoluble Brain Aβ Distinguish Alzheimer's Disease from Normal and Pathologic Aging

TL;DR: The data suggest that pathologic aging is a transition state between normal aging and AD, and imply that a progressive shift of brain Abeta1-40 and AbETA1-42 from soluble to insoluble pools and a profound increase in the levels of insoluble Abeta 1-40 plays mechanistic roles in the onset and/or progression of AD.
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Age-Dependent Emergence and Progression of a Tauopathy in Transgenic Mice Overexpressing the Shortest Human Tau Isoform

TL;DR: Inclusions in tau-immunoreactive filaments were present in cortical and brainstem neurons but were most abundant in spinal cord neurons, where they were associated with axon degeneration, diminished microtubules (MTs), and reduced axonal transport in ventral roots, as well as spinal cord gliosis and motor weakness.
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MRI of hippocampal volume loss in early Alzheimer's disease in relation to ApoE genotype and biomarkers.

TL;DR: The demonstration of considerable hippocampal loss in mild cognitive impairment and Alzheimer's disease patients over only 6 months and accelerated loss over 12 months illustrates the power of MRI to track morphological brain changes over time in a large multisite setting.
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Alpha-synuclein cortical Lewy bodies correlate with dementia in Parkinson’s disease

TL;DR: CLBs detected by α-synuclein antibodies in patients with PD are a more sensitive and specific correlate of dementia than the presence of Alzheimer’s pathology, which was present in a minority of the cases in this series.
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The acetylation of tau inhibits its function and promotes pathological tau aggregation

TL;DR: It is demonstrated that tau acetylation inhibits tau function via impaired tau-microtubule interactions and promotes pathological tau aggregation, and suggests tau K280 acetylations is a potential target for drug discovery and biomarker development for AD and related tauopathies.