Up-and-down topological mode of amyloid β-peptide lying on hydrophilic/hydrophobic interface of ganglioside clusters

Protein backbone angle restraints from searching a database for chemical shift and sequence homology

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Attenuated <i>T</i> ₂ relaxation by mutual cancellation of dipole–dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution

Konstantin Pervushin, Roland Riek, Gerhard Wider et al. · Proceedings of the National Academy of Sciences · 1997 · 2.5K citations · Full text

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Experimental Constraints on Quaternary Structure in Alzheimer's β-Amyloid Fibrils

Aneta T. Petkova, Wai‐Ming Yau, Robert Tycko · Biochemistry · 2005 · 1.1K citations · Full text

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Mechanism of coupled folding and binding of an intrinsically disordered protein

Kenji Sugase, H. Jane Dyson, Peter E. Wright · Nature · 2007 · 1K citations

Life Sciences, Biochemistry, Biophysics +12

GM1 ganglioside–bound amyloid β–protein (Aβ): A possible form of preamyloid in Alzheimer's disease

Katsuhiko Yanagisawa, Asano Odaka, Nobuhiro Suzuki et al. · Nature Medicine · 1995 · 549 citations

Life Sciences, Biochemistry, Neuroscience +12