Publications by authors named "C J Glynn"

Pathological tau fibrils in progressive supranuclear palsy, frontotemporal dementia, chronic traumatic encephalopathy, and Alzheimer's disease each have unique conformations, and post-translational modifications that correlate with unique disease characteristics. However, within Alzheimer's disease (AD), both fibrillar (sarkosyl insoluble (AD SARK tau)), and nonfibrillar (aqueous extractable high molecular weight (AD HMW tau)) preparations have been suggested to be seed-competent. We now explore if these preparations are similar or distinct in their in vivo seeding characteristics.

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Proteins exhibiting prion-like properties are implicated in tauopathies. The prion-like traits of tau influence disease progression and correlate with severity. Techniques to measure tau bioactivity such as RT-QuIC and biosensor cells lack spatial specificity.

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Tree diversity can promote both predator abundance and diversity. However, whether this translates into increased predation and top-down control of herbivores across predator taxonomic groups and contrasting environmental conditions remains unresolved. We used a global network of tree diversity experiments (TreeDivNet) spread across three continents and three biomes to test the effects of tree species richness on predation across varying climatic conditions of temperature and precipitation.

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Soft bioelectronic devices exhibit motion-adaptive properties for neural interfaces to investigate complex neural circuits. Here, we develop a fabrication approach through the control of metamorphic polymers' amorphous-crystalline transition to miniaturize and integrate multiple components into hydrogel bioelectronics. We attain an about 80% diameter reduction in chemically cross-linked polyvinyl alcohol hydrogel fibers in a fully hydrated state.

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Article Synopsis
  • Scientists are studying 'prion-like' behavior in diseases where proteins fold incorrectly, forming structures called amyloids that can spread like prions.
  • These prion-like proteins can move through cells and change other proteins, making them misfold too.
  • Recent imaging techniques have helped researchers discover similarities between different forms of these amyloids and prions, leading to new ideas about how they cause diseases.
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