Abstract

Protein misfolding and amyloid aggregation underlie various aging-related neurodegenerative diseases, such as Alzheimer's disease and Parkinson's disease. Although amyloid aggregates share a common cross-β sheet structural motif formed by similar amino acid sequences, aggregation intermediates are highly dynamic, transitory, and heterogeneous in terms of their structures and sizes. Transient amyloid binding (TAB) superresolution (SR) microscopy is a versatile method for studying a variety of amyloid structures without the need for covalent labeling or immunostaining.

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