In the present study we have used a transgenic mouse line overexpressing an amyloidogenic protein, gamma-synuclein, in the nervous system to address the effect of dimebon on proteinopathy progression. Chronic dimebon administration increased lifespan in these transgenic mice, furthermore, using histological and biochemical approaches we have demonstrated that dimebon reduced the number of amyloid inclusions in the spinal cord of transgenic animals and decreased the content of ubiquitinated proteins in the detergent-insoluble fraction of the spinal cord. These effects are likely to occur at the level of aggregated protein species, since transgene expression remained unaltered during dimebon administration. Thus, pathological protein aggregation serves as one of dimebon targets in neurodegeneration.