Jennifer L. Mayes

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According to the "amyloid cascade" hypothesis of Alzheimer disease, the formation of Aβ fibrils and senile plaques in the brain initiates a cascade of events leading to the formation of neurofibrillary tangles, neurodegeneration, and the symptom of dementia. Recently, however, emphasis has shifted away from amyloid fibrils as the predominant toxic form of(More)
Using a method based on ESR spectroscopy and spin-trapping, we have shown that Abeta (amyloid beta-peptide) (implicated in Alzheimer's disease), alpha-synuclein (implicated in Parkinson's disease), ABri (British dementia peptide) (responsible for familial British dementia), certain toxic fragments of the prion protein (implicated in the transmissible(More)
Session RPE (SRPE) permits subjective ratings of global effort following exercise. SRPE is useful for evaluating training load; however, mediating factors are not well understood. This study compared SRPE among treadmill trials at a clamped workload with a varied duration. Ten subjects (VO2max: 48.9 ± 10.5 ml kg−1 min−1) completed a maximal-exertion(More)
The formation of beta-amyloid (Abeta) deposits in the brain is likely to be a seminal step in the development of Alzheimer's disease. Recent studies support the hypothesis that Abeta soluble oligomers are toxic to cells and have potent effects on memory and learning. Inhibiting the early stages of Abeta aggregation could, therefore, provide a novel approach(More)
Considerable evidence points to oxidative stress in the brain as an important event in the early stages of Alzheimer's disease (AD). The transition metal ions of Cu, Fe, and Zn are all enriched in the amyloid cores of senile plaques in AD. Those of Cu and Fe are redox active and bind to Aβ in vitro. When bound, they can facilitate the reduction of oxygen to(More)
The aggregation of amyloid-β peptides into protein fibres is one of the main neuropathological features of Alzheimer's disease (AD). While imaging of amyloid-β aggregate morphology in vitro is extremely important for understanding AD pathology and in the development of aggregation inhibitors, unfortunately, potentially highly toxic, early aggregates are(More)
The aggregation of amyloid-b peptides into protein fibres is one of the main neuropathological features of Alzheimer’s disease (AD). While imaging of amyloid-b aggregate morphology in vitro is extremely important for understanding AD pathology and in the development of aggregation inhibitors, unfortunately, potentially highly toxic, early aggregates are(More)
One of the hallmarks of AD (Alzheimer's disease) is the formation of senile plaques in the brain, which contain fibrils composed of Aβ (amyloid β-peptide). According to the 'amyloid cascade' hypothesis, the aggregation of Aβ initiates a sequence of events leading to the formation of neurofibrillary tangles, neurodegeneration, and on to the main symptom of(More)
Human amylin (hA), which is toxic to islet β-cells, can self-generate H(2)O(2), and this process is greatly enhanced in the presence of Cu(II) ions. Here we show that carbonyl groups, a marker of oxidative modification, were formed in hA incubated in the presence of Cu(II) ions or Cu(II) ions plus H(2)O(2), but not in the presence of H(2)O(2) alone.(More)
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