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Mykhailo Girych

Researcher at University of Helsinki

Publications -  23
Citations -  455

Mykhailo Girych is an academic researcher from University of Helsinki. The author has contributed to research in topics: Tropomyosin receptor kinase B & Lipid bilayer. The author has an hindex of 6, co-authored 19 publications receiving 222 citations. Previous affiliations of Mykhailo Girych include Aalto University & University of Kharkiv.

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Molecular electrometer and binding of cations to phospholipid bilayers

TL;DR: It is shown that by interpreting changes in the choline headgroup order parameters according to the 'molecular electrometer' concept, one can directly compare the ion binding affinities between simulations and experiments, and strongly support the view that in contrast to Ca2+ and other multivalent ions, Na- and other monovalent ions do not specifically bind to phosphatidylcholine lipid bilayers at sub-molar concentrations.
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Combined thioflavin T-Congo red fluorescence assay for amyloid fibril detection

TL;DR: A novel combined ThT-CR fluorescence assay for amyloid identification is designed, which not only strengthens the reliability of the ThT assay, but also provides new opportunities for structural characterization of amyloids fibrils.
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Cyanine dyes derived inhibition of insulin fibrillization

TL;DR: Two possible mechanisms by which cyanines can inhibit the insulin fibrillization are highlighted: i) stabilization of the native protein structure followed by the retardation of the protein nucleation (all dyes); and ii) blocking the lateral extension of β-sheets via the dye-protein stacking interactions (3-3, 3-5, 5-3 and 5-9).
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Interaction of thioflavin T with amyloid fibrils of apolipoprotein A-I N-terminal fragment: resonance energy transfer study.

TL;DR: Förster resonance energy transfer between tryptophan as a donor and Thioflavin T as an acceptor was employed to obtain structural information on the amyloid fibrils formed by apoA-I variant 1-83/G26R/W@8 to provide evidence for the presence of two types of ThT binding sites with similar stoichiometries.