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Lansbury, P.T. (1999) Evolution of amyloid: What normal protein folding may tell us about fibrillogenesis and disease. Proceedings of National Academy Sciences of the USA, 96, 3342-3344. doi: 10.1073/pnas.96.7.3342

has been cited by the following article:

• TITLE: Spatial structure of beta-amyloid Aβ1-40 in complex with a biological membrane model

  AUTHORS: Konstantin S. Usachev, Andrey V. Filippov, Oleg N. Antzutkin, Vladimir V. Klochkov

  KEYWORDS: 1H NMR; Two-Dimensional NMR (TOCSY, NOESY) Spectroscopy; Alzheimer’s Disease; Beta-Amyloid; Oligopeptides; Micelle

  JOURNAL NAME: Advances in Alzheimer's Disease, Vol.1 No.3, December 21, 2012

  ABSTRACT: The spatial structure of beta-amyloid Aβ1-40 in complex with sodium dodecyl sulfate micelles as a model membrane system was investigated by 1H-1H two-dimensional NMR (TOCSY, NOESY) spectroscopy and molecular dynamic method calculations. On the basis of NOE and chemical shifts changes data, spatial structure of the complex beta-amyloid-model of the cell surface membrane was obtained.