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A Critical Role of Ser26 Hydrogen Bonding in A beta 42 Assembly and Toxicity

Autor: Roychaudhuri, R, Huynh, T-PV, Whitaker, TR, Hodara, E, Condron, MM, Teplow, DB

Publikováno v: Roychaudhuri, R; Huynh, T-PV; Whitaker, TR; Hodara, E; Condron, MM; & Teplow, DB. (2017). A Critical Role of Ser26 Hydrogen Bonding in A beta 42 Assembly and Toxicity. BIOCHEMISTRY, 56(48), 6321-6324. doi: 10.1021/acs.biochem.7b00772. UCLA: Retrieved from: http://www.escholarship.org/uc/item/4rk8407b

Amyloid β-protein (Aβ) assembly is a seminal process in Alzheimer's disease. Elucidating the mechanistic features of this process is thought to be vital for the design and targeting of therapeutic agents. Computational studies of the most pathologi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od_______325::990c1299091c6f49a380e0acfbaece71
http://www.escholarship.org/uc/item/4rk8407b

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C-terminal turn stability determines assembly differences between Aβ40 and Aβ42

Autor: Roychaudhuri, R, Yang, M, Deshpande, A, Cole, GM, Frautschy, S, Lomakin, A, Benedek, GB, Teplow, DB

Publikováno v: Journal of molecular biology, vol 425, iss 2
Roychaudhuri, R; Yang, M; Deshpande, A; Cole, GM; Frautschy, S; Lomakin, A; et al.(2013). C-terminal turn stability determines assembly differences between Aβ40 and Aβ42. Journal of Molecular Biology, 425(2), 292-308. doi: 10.1016/j.jmb.2012.11.006. UCLA: Retrieved from: http://www.escholarship.org/uc/item/3d00182s

Oligomerization of the amyloid β-protein (Aβ) is a seminal event in Alzheimer's disease. Aβ42, which is only two amino acids longer than Aβ40, is particularly pathogenic. Why this is so has not been elucidated fully. We report here results of com

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::647eb37b3c87a5fc8ff068ae8f4476fe
https://escholarship.org/uc/item/3d00182s

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