Olga A Morozova

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Fibrils composed of tau protein are a pathological hallmark of several neurodegenerative disorders including Alzheimer's disease (AD). Here we show that when recombinant tau protein is seeded with paired helical filaments (PHFs) isolated from AD brain, the amyloid formed shares many of the structural features of AD PHFs. In contrast, tau amyloids formed(More)
The bacteriolytic activity of interleukin-2 and hen egg white lysozyme against 34 different species of microorganisms has been studied. It was found that 6 species of microorganisms are lysed in the presence of interleukin-2. All interleukin-2-sensitive microorganisms belong either to the Enterobacteriaceae, Bacillaceae, or the Lactobacillaceae family. It(More)
Tauopathies encompass a broad family of neurodegenerative diseases, including Alzheimer's disease, which are characterized by the fibrillization of the microtubule-associated tau protein. The normal function of tau is to stabilize and promote the assembly of microtubules in neuronal axons. Sequestration of tau into amyloid fibrils results in destabilization(More)
Many neurodegenerative diseases are associated with deposits of aggregated protein in the brain. The molecular pathways through which soluble proteins misfold to form amyloids and large protein aggregates often include diverse oligomeric species, only some of which progress to the amyloid state. Here we show that prefibrillar huntingtin (HTT) oligomers,(More)
Stress may contribute to the development of gastric ulcer disease. The results of our previous investigations suggest that glucocorticoids released during acute stress act as gastroprotective hormones, and not as ulcerogenic agents as has been generally accepted for a long time. In this study, we investigated whether corticotropin-releasing factor (CRF) may(More)
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