25 results on '"Iashchishyn, Igor"'
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2. Spiders Use Structural Conversion of Globular Amyloidogenic Domains to Make Strong Silk Fibers
3. Spider Silk Protein Forms Amyloid‐Like Nanofibrils through a Non‐Nucleation‐Dependent Polymerization Mechanism (Small 46/2023)
4. ApoE Isoforms Inhibit Amyloid Aggregation of Proinflammatory Protein S100A9.
5. S100A9-Driven Amyloid-Neuroinflammatory Cascade in Traumatic Brain Injury as a Precursor State for Alzheimer’s Disease
6. Co-aggregation of pro-inflammatory S100A9 with α-synuclein in Parkinson’s disease: ex vivo and in vitro studies
7. Co-Aggregation of S100A9 with DOPA and Cyclen-Based Compounds Manifested in Amyloid Fibril Thickening without Altering Rates of Self-Assembly
8. Elongation of wood fibers combines features of diffuse and tip growth
9. Polyoxometalates as Effective Nano-inhibitors of Amyloid Aggregation of Pro-inflammatory S100A9 Protein Involved in Neurodegenerative Diseases
10. Natural Compound from Olive Oil Inhibits S100A9 Amyloid Formation and Cytotoxicity: Implications for Preventing Alzheimer’s Disease
11. Cholesterol‐containing lipid nanodiscs promote an α‐synuclein binding mode that accelerates oligomerization
12. Templating S100A9 amyloids on Aβ fibrillar surfaces revealed by charge detection mass spectrometry, microscopy, kinetic and microfluidic analyses
13. Additional file 1: of Co-aggregation of pro-inflammatory S100A9 with α-synuclein in Parkinson’s disease: ex vivo and in vitro studies
14. Cholesterol is a strong promotor of an α-Synuclein membrane binding mode that accelerates oligomerization
15. Pro-Inflammatory S100A9 Protein Aggregation Promoted by NCAM1 Peptide Constructs
16. Cholesterol‐containing lipid nanodiscs promote an α‐synuclein binding mode that accelerates oligomerization.
17. Templating S100A9 amyloids on Aβ fibrillar surfaces revealed by charge detection mass spectrometry, microscopy, kinetic and microfluidic analyses.
18. Intranasally Administered S100A9 Amyloids Induced Cellular Stress, Amyloid Seeding, and Behavioral Impairment in Aged Mice
19. Finke–Watzky Two-Step Nucleation–Autocatalysis Model of S100A9 Amyloid Formation: Protein Misfolding as “Nucleation” Event
20. Proinflammatory and amyloidogenic S100A9 induced by traumatic brain injury in mouse model.
21. Additional file 2: of Co-aggregation of pro-inflammatory S100A9 with α-synuclein in Parkinson’s disease: ex vivo and in vitro studies
22. Additional file 2: of Co-aggregation of pro-inflammatory S100A9 with α-synuclein in Parkinson’s disease: ex vivo and in vitro studies
23. Co-aggregation of S100A9 with DOPA and cyclen-based compounds manifested in amyloid fibril thickening without altering rates of self-assembly
24. Templating S100A9 amyloids on Aβ fibrillar surfaces revealed by charge detection mass spectrometry, microscopy, kinetic and microfluidic analyses
25. Immunochemical Detection of α-Synuclein Autoantibodies in Parkinson's Disease: Correlation between Plasma and Cerebrospinal Fluid Levels.
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