D
Dmitry I. Cherny
Researcher at University of Leicester
Publications - 41
Citations - 2974
Dmitry I. Cherny is an academic researcher from University of Leicester. The author has contributed to research in topics: DNA & Recognition sequence. The author has an hindex of 26, co-authored 41 publications receiving 2745 citations. Previous affiliations of Dmitry I. Cherny include Max Planck Society & Pierre-and-Marie-Curie University.
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Dependence of α-synuclein aggregate morphology on solution conditions
TL;DR: It is demonstrated that the morphology of a-synuclein aggregates is highly sensitive to solution conditions, implying that the fibrillar state does not necessarily represent the predominant or most functionally significant aggregated state under physiological conditions.
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Structural characterization of copper(II) binding to α-synuclein: Insights into the bioinorganic chemistry of Parkinson's disease
Rodolfo M. Rasia,Carlos W. Bertoncini,Derek Marsh,Wolfgang Hoyer,Dmitry I. Cherny,Markus Zweckstetter,Christian Griesinger,Thomas M. Jovin,Claudio O. Fernández +8 more
TL;DR: It is demonstrated here that Cu(II) ions are effective in accelerating AS aggregation at physiologically relevant concentrations without altering the resultant fibrillar structures.
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LPS receptor (CD14): a receptor for phagocytosis of Alzheimer’s amyloid peptide
Yang Liu,Silke Walter,Massimiliano Stagi,Dmitry I. Cherny,Maryse Letiembre,Walter J. Schulz-Schaeffer,Holger Heine,Botond Penke,Harald Neumann,Klaus Fassbender +9 more
TL;DR: A direct role of CD14 in Abeta(42) phagocytosis is demonstrated, and a pronounced CD14 immunoreactivity on parenchymal microglia spatially correlated to characteristic Alzheimer's disease lesion sites in brain sections of Alzheimer’s disease patients but not inbrain sections of control subjects are detected.
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Impact of the Acidic C-Terminal Region Comprising Amino Acids 109−140 on α-Synuclein Aggregation in Vitro†
TL;DR: The effects of the C-terminus on aggregation cannot be rationalized merely by a contribution to the protein net charge, but rather suggest a specific role of aa109-140 in the regulation of aggregation, presumably involving formation of intramolecular contacts.
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Cellular Polyamines Promote the Aggregation of α-Synuclein
TL;DR: It is concluded that the polyamines at physiological concentrations can modulate the propensity of α-synuclein to form fibrils and may hence play a role in the formation of cytosolic α- synuclein aggregates.