Molecular structure of β-amyloid fibrils in Alzheimer's disease brain tissue.

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Published in Cell on September 12, 2013

Authors

Jun-Xia Lu1, Wei Qiang, Wai-Ming Yau, Charles D Schwieters, Stephen C Meredith, Robert Tycko

Author Affiliations

1: Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0520, USA.

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Combined use of residual dipolar couplings and solution X-ray scattering to rapidly probe rigid-body conformational transitions in a non-phosphorylatable active-site mutant of the 128 kDa enzyme I dimer. J Am Chem Soc (2010) 1.03

Evidence from solid-state NMR for nonhelical conformations in the transmembrane domain of the amyloid precursor protein. Biophys J (2011) 1.02

HIV fusion peptide penetrates, disorders, and softens T-cell membrane mimics. J Mol Biol (2010) 1.02

Segmental polymorphism in a functional amyloid. Biophys J (2011) 1.01

Protein structure refinement using 13C alpha chemical shift tensors. J Am Chem Soc (2009) 1.01

Structural and dynamical characterization of tubular HIV-1 capsid protein assemblies by solid state nuclear magnetic resonance and electron microscopy. Protein Sci (2010) 1.01

Sedimentation studies on human amylin fail to detect low-molecular-weight oligomers. Biophys J (2008) 1.00

Probing the role of backbone hydrogen bonding in beta-amyloid fibrils with inhibitor peptides containing ester bonds at alternate positions. Biochemistry (2003) 1.00

Using the experimentally determined components of the overall rotational diffusion tensor to restrain molecular shape and size in NMR structure determination of globular proteins and protein-protein complexes. J Am Chem Soc (2009) 0.99