Published in
Springer Verlag, Bulletin of Experimental Biology and Medicine, 6(152), p. 731-733
DOI: 10.1007/s10517-012-1618-7
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Dimebon Reduces the Levels of Aggregated Amyloidogenic Protein Forms in Detergent-Insoluble Fractions In Vivo
Journal article published in 2012 by
Ustyugov Aa,
A. A. Ustyugov 
,
Kokhan Vs,
Buchman Vl,
T. A. Shelkovnikova,
Shelkovnikova Ta,
V. S. Kokhan,
Khritankova Iv,
I. V. Khritankova,
O. Peters,
V. L. Buchman,
S. O. Bachurin,
Bachurin So,
N. N. Ninkina,
Ninkina Nn
,
Kokhan Vs,
Buchman Vl,
T. A. Shelkovnikova,
Shelkovnikova Ta,
V. S. Kokhan,
Khritankova Iv,
I. V. Khritankova,
O. Peters,
V. L. Buchman,
S. O. Bachurin,
Bachurin So,
N. N. Ninkina,
Ninkina Nn
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Abstract
Aggregation of proteins liable to assembling into fibrils 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 fibrillar forms of synuclein, the main protein component of pathological incorporations in neurons of transgenic mouse strain used in the study.