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Supersaturation-Dependent Formation of Amyloid Fibrils †.
- Published in:
- Molecules, 2022, v. 27, n. 14, p. N.PAG, doi. 10.3390/molecules27144588
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- Article
Phosphatidylinositol-3,4,5-trisphosphate interacts with alpha-synuclein and initiates its aggregation and formation of Parkinson's disease-related fibril polymorphism.
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- Acta Neuropathologica, 2023, v. 145, n. 5, p. 573, doi. 10.1007/s00401-023-02555-3
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- Article
Nucleus factory on cavitation bubble for amyloid β fibril.
- Published in:
- Scientific Reports, 2016, p. 22015, doi. 10.1038/srep22015
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- Article
Macromolecular crowding and supersaturation protect hemodialysis patients from the onset of dialysis-related amyloidosis.
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- Nature Communications, 2022, v. 13, n. 1, p. 1, doi. 10.1038/s41467-022-33247-3
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- Article
Synchronized resistive-pulse analysis with flow visualization for single micro- and nanoscale objects driven by optical vortex in double orifice.
- Published in:
- Scientific Reports, 2021, v. 11, n. 1, p. 1, doi. 10.1038/s41598-021-87822-7
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- Article
Mechanisms of polyphosphate-induced amyloid fibril formation triggered by breakdown of supersaturation.
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- Biophysics & Physicobiology, 2023, v. 20, n. 1, p. 1, doi. 10.2142/biophysico.bppb-v20.0013
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- Article
Two-step screening method to identify α-synuclein aggregation inhibitors for Parkinson's disease.
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- Scientific Reports, 2022, v. 12, n. 1, p. 1, doi. 10.1038/s41598-021-04131-9
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- Article