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- W4228996812 abstract "Proteins that normally function in amyloid form are found in bacteria, yeast, plants and vertebrates, including humans. In particular, amyloid fibrils and amyloid-like structures are described in the germ cells of various organisms. Recently we showed that in chicken oocytes there are some nuclear structures that are stained by the amyloid-specific dye thioflavin S. Here we demonstrate that thioflavin S binds giant terminal RNP aggregates in chicken lampbrush chromosomes. However, these structures are not stained with Congo red and conformation-dependent anti-amyloid antibodies. Thus, thioflavin S stains chromosome-associated proteins that do not have amyloid properties. These data indicate that thioflavin S must be used with caution when identifying new functional and pathological amyloids." @default.
- W4228996812 created "2022-05-08" @default.
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- W4228996812 date "2022-05-04" @default.
- W4228996812 modified "2023-10-14" @default.
- W4228996812 title "Thioflavin S binds non-amyloid protein structures in lampbrush chromosomes of <em>Gallus gallus domesticus</em>" @default.
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- W4228996812 doi "https://doi.org/10.21638/spbu03.2022.106" @default.
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