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

Full text not available from this repository.

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:	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

Citation Data

Cited 9 times in Scopus. View in Scopus. Powered By Scopus® Data

Actions (repository staff only)

Edit Item