ArticleAccounts of chemical research2026
Structures and Dynamics of Tau Assemblies from Solid-State NMR.
Article in Accounts of chemical research, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
ConspectusAggregation of the microtubule-associated protein tau into β-sheet fibrils is a hallmark of many neurodegenerative diseases. Understanding the molecular mechanism of tau aggregation requires elucidating the structure and dynamics of fibrillar tau as the end product of aggregation, membrane-bound tau involved in nucleation and intercellular transmission of the aggregates, and microtubule-bound tau as the physiological state of the protein. Using solid-state NMR spectroscopy, we have obtained detailed information about these tau assemblies. Full-length tau fibrils formed in the presence of heparin adopt homogeneous structures that depend on the number of microtubule-binding repeats and that differ from
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