Robert Tycko

TL;DR: A structural model for amyloid fibrils formed by the 40-residue β-amyloid peptide associated with Alzheimer's disease (Aβ1–40) is presented, based on a set of experimental constraints from solid state NMR spectroscopy and incorporates the cross-β structural motif established by x-ray fiber diffraction.

TL;DR: It is discovered that exposure of cell or tissue lysates to a biotinylated isoxazole (b-isox) chemical precipitated hundreds of RNA-binding proteins with significant overlap to the constituents of RNA granules, offering a framework for understanding the function of LC sequences as well as an organizing principle for cellular structures that are not membrane bound.

TL;DR: Using electron microscopy and solid-state nuclear magnetic resonance measurements on fibrils formed by the 40-residue β-amyloid peptide of Alzheimer's disease (Aβ1–40), it is shown that different fibril morphologies have different underlying molecular structures, that the predominant structure can be controlled by subtle variations infibril growth conditions, and that both morphology and molecular structure are self-propagating when fibrs grow from preformed seeds.

TL;DR: A full structural model for amyloid fibrils formed by the 40-residue β-amyloid peptide associated with Alzheimer's disease (Aβ1–40), based on numerous constraints from solid state NMR and electron microscopy is described.

TL;DR: Solid-state nuclear magnetic resonance measurements on fibrils formed by the 40-residue beta-amyloid peptide associated with Alzheimer's disease are described and full molecular models using restrained molecular dynamics simulations and restrained energy minimization are constructed.