Publications by authors named "Jennifer Y O'Shea"
The fibrillary aggregation of α-synuclein is a hallmark of Parkinson's disease (PD) and a potential target for diagnostics and therapeutics. Although substantial effort has been devoted to the development of positron emission tomography (PET) probes for detecting α-synuclein aggregates, no clinically suitable tracer has been reported. The design and synthesis of 43 new -(6-methoxypyridin-3-yl)quinolin-2-amine derivatives and an evaluation of their α-synuclein binding affinity is reported here.
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- * The researchers developed a new method to enhance the extraction of these alpha-synuclein fibrils from postmortem tissue, using solid state nuclear magnetic resonance (SSNMR) to analyze their atomic structure.
- * Their findings reveal that the fibrils from Lewy body dementia consist of both single and double protofilaments, and display structural similarities to previously studied twisted fibrils; this could aid in understanding disease mechanisms and developing new treatments.
Quantifying regional α -synuclein, amyloid β, and tau accumulation in lewy body dementia.
Ann Clin Transl Neurol
February 2022
Objective: Parkinson disease (PD) is defined by the accumulation of misfolded α-synuclein (α-syn) in Lewy bodies and Lewy neurites. It affects multiple cortical and subcortical neuronal populations. The majority of people with PD develop dementia, which is associated with Lewy bodies in neocortex and referred to as Lewy body dementia (LBD).
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