Publications by authors named "A I Sulatskaya"
The transition of β-barrel proteins from a soluble to an amyloid form is biologically significant in some cases but may lead to functional activity loss. In particular, odorant-binding proteins' (OBPs) fibrils are unable to bind odorant molecules potentially contributing to olfactory dysfunction. As shown previously, OBPs' fibrillogenesis is initiated by uncoupling of protein C-terminal fragment from the β-barrel and exposing amyloidogenic sites.
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- Over the past decade, research has focused on developing treatments for severe systemic and neurodegenerative diseases by targeting and degrading harmful amyloid deposits without significant side effects.
- This study investigates the impact of the immune enzyme MMP9 on various amyloids linked to Alzheimer's, Parkinson's, and other diseases, revealing that its effectiveness is influenced by the size of amyloid clusters.
- MMP9 degrades amyloids by disrupting their internal structures rather than just breaking hydrogen bonds, which helps avoid potential side effects from other anti-amyloid therapies while promoting the breakdown and safe handling of amyloid aggregates.
In the original publication [...
View Article and Find Full Text PDFBackground: The accumulation of ordered protein aggregates, amyloid fibrils, accompanies various neurodegenerative diseases (such as Parkinson's, Huntington's, Alzheimer's, etc.) and causes a wide range of systemic and local amyloidoses (such as insulin, hemodialysis amyloidosis, etc.).
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