Sarah H. Shahmoradian

The paper identifies sequence changes that bias tau aggregation toward CTE-like structures using mutagenesis and structural analysis.

This study identifies DUF4062 as TIR-like NADases involved in bacterial antiphage defense and eukaryotic RNA vault function through structural and biochemical analyses.

This study identifies cysteine residues as critical for tau aggregation and propagation in cells, both spontaneously and when seeded.

The paper introduces miOPM, a reconfigurable LSFM platform that enables high-resolution imaging across multiple spatial scales and refractive indices.

This paper provides a protocol for correlative light and electron microscopy (CLEM) optimized for analyzing human brain tissue, enabling detailed ultrastructural analysis and characterization of subcellular features.

The paper identifies amino acids critical for tau strain propagation by analyzing their role in amyloid templating across different tauopathies.

The paper determines the cryo-EM structure of Alzheimer's disease tau filaments bound by the PET ligand MK-6240, revealing key binding interactions that inform ligand design.

SymDOCK is a docking method that exploits symmetry in amyloid fibrils to predict ligand stacking, successfully reproducing known structures and predicting a new one before its determination.

This study uses cryo-electron tomography to analyze the structure of mutant huntingtin exon 1 and polyQ aggregates, revealing structural heterogeneity and a 'polyQ core' model.

The paper presents a method for high-resolution reconstruction of whole mouse brain vasculature using synchrotron-based tomography and analyzes its structural properties.

The paper uses high-resolution imaging and biophysical methods to show that Lewy pathology in Parkinson's disease consists mainly of a crowded membranous medley of vesicles and dysmorphic organelles, with only a small fraction containing proteinaceous filaments.