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Sevigny, Jeff; Chiao, Ping; Bussière, Thierry; Weinreb, Paul H; Williams, Leslie; Maier, Marcel; Dunstan, Robert; Salloway, Stephen; Chen, Tianle; Ling, Yan; O'Gorman, John; Qian, Fang; Arastu, Mahin; Li, Mingwei; Chollate, Sowmya; Brennan, Melanie S; Quintero-Monzon, Omar; Scannevin, Robert H; Arnold, H Moore; Engber, Thomas; Rhodes, Kenneth; Ferrero, James; Hang, Yaming; Mikulskis, Alvydas; Grimm, Jan; Hock, Christoph; Nitsch, Roger M; Sandrock, Alfred
Nature (London), 09/2016, Letnik: 537, Številka: 7618Journal Article
Alzheimer's disease (AD) is characterized by deposition of amyloid-β (Aβ) plaques and neurofibrillary tangles in the brain, accompanied by synaptic dysfunction and neurodegeneration. Antibody-based immunotherapy against Aβ to trigger its clearance or mitigate its neurotoxicity has so far been unsuccessful. Here we report the generation of aducanumab, a human monoclonal antibody that selectively targets aggregated Aβ. In a transgenic mouse model of AD, aducanumab is shown to enter the brain, bind parenchymal Aβ, and reduce soluble and insoluble Aβ in a dose-dependent manner. In patients with prodromal or mild AD, one year of monthly intravenous infusions of aducanumab reduces brain Aβ in a dose- and time-dependent manner. This is accompanied by a slowing of clinical decline measured by Clinical Dementia Rating-Sum of Boxes and Mini Mental State Examination scores. The main safety and tolerability findings are amyloid-related imaging abnormalities. These results justify further development of aducanumab for the treatment of AD. Should the slowing of clinical decline be confirmed in ongoing phase 3 clinical trials, it would provide compelling support for the amyloid hypothesis.
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JCR | SNIP | JCR | SNIP | JCR | SNIP | JCR | SNIP |
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Vir: Osebne bibliografije
in: SICRIS
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