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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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Genetic correlation between amyotrophic lateral sclerosis and schizophrenia

Russell L. McLaughlin, +488 more
TL;DR: It is likely that shared neurobiological mechanisms between these two disorders will engender novel hypotheses in future preclinical and clinical studies, and five potential novel ALS-associated loci are identified using conditional false discovery rate analysis.
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Lewy Bodies in the Amygdala: Increase of α-Synuclein Aggregates in Neurodegenerative Diseases With Tau-Based Inclusions

TL;DR: Abnormal alpha-synuclein aggregation in the amygdala is disease selective, but not restricted to disorders of alpha- synuclein and beta-amyloid, and compatible with the notion that tau aggregates predispose neurons to develop secondary LBs.
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Degradative organelles containing mislocalized α- and β-synuclein proliferate in presenilin-1 null neurons

TL;DR: It is demonstrated that PS1 deficiency also leads to the formation of degradative vacuoles and to the aberrant translocation of presynaptic α- and β-synuclein proteins to these organelles in the perikarya of primary neurons, concomitant with significant increases in the levels of both synucleins.
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Age-dependent synuclein pathology following traumatic brain injury in mice.

TL;DR: This model of age-dependent TBI-induced transient alterations in alpha-Syn provides an opportunity to examine possible links between TBI and mechanisms of disease in synucleinopathies.
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Intraneuronal APP, Not Free Aβ Peptides in 3xTg-AD Mice: Implications for Tau versus Aβ-Mediated Alzheimer Neurodegeneration

TL;DR: It is demonstrated that tau pathology forms independently from Aβ peptide generation in this mouse model, and the findings warrant further study as to the role of aberrant APP accumulation in this unique model of AD.