Dimebon reduces the levels of aggregated amyloidogenic protein forms in detergent-insoluble fractions in vivo

Ustyugov, A. A., Shelkovnikova, Tatyana ORCID: https://orcid.org/0000-0003-1367-5309, Kokhan, V. S., Khritankova, I. V., Peters, Owen Morgan ORCID: https://orcid.org/0000-0002-6824-0663, Buchman, Vladimir L. ORCID: https://orcid.org/0000-0002-7631-8352, Bachurin, S. O. and Ninkina, Natalia ORCID: https://orcid.org/0000-0001-8570-5648 2012. Dimebon reduces the levels of aggregated amyloidogenic protein forms in detergent-insoluble fractions in vivo. Bulletin of Experimental Biology and Medicine 152 (6) , pp. 731-733. 10.1007/s10517-012-1618-7

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Abstract

Aggregation of proteins liable to assembling into fi brils with subsequent formation of amyloid incorporations is an important component in the pathogenesis of many neurodegenerative diseases. Dimebon, a Russian drug, reduces the content of detergent-insoluble fi brillar forms of synuclein, the main protein component of pathological incorporations in neurons of transgenic mouse strain used in the study.

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Schools > Biosciences
Subjects:	R Medicine > RC Internal medicine > RC0321 Neuroscience. Biological psychiatry. Neuropsychiatry R Medicine > RM Therapeutics. Pharmacology
Uncontrolled Keywords:	dimebon; neurodegeneration; synucleins; transgenic animals
Additional Information:	Translated from Byulleten” Eksperimental’noi Biologii i Meditsiny, Vol. 152, No. 12, pp. 674-677, December, 2011
Publisher:	Springer
ISSN:	0007-4888
Last Modified:	07 Aug 2024 22:28
URI:	https://orca.cardiff.ac.uk/id/eprint/32556

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