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The unique Alzheimer's β-amyloid triangular fibril has a cavity along the fibril axis under physiological conditions

Elucidating the structure of Aβ(1–40) fibrils is of interest in Alzheimer's disease research because it is required for designing therapeutics that target Aβ(1–40) fibril formation at an early stage of the disease. M35 is a crucial residue because of its potential oxidation and its strong inter...

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Main Authors: Miller, Yifat, Ma, Buyong, Nussinov, Ruth
Formato: Artigo
Idioma:Inglês
Publicado: 2011
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Acceso en liña:https://ncbi.nlm.nih.gov/pmc/articles/PMC3045480/
https://ncbi.nlm.nih.gov/pubmed/21299220
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/ja1100273
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