ReviewMethods in enzymology2026
Time-resolved solid-state nuclear magnetic resonance studies of amyloid-β oligomer formation.
Review in Methods in enzymology, 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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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Abstract
Although much is known about the molecular structures of mature amyloid fibrils, based primarily on extensive studies by solid-state nuclear magnetic resonance (ssNMR) and cryogenic electron microscopy (cryo-EM), relatively little is known about the structures of oligomers that form in the initial stages of self-assembly by amyloid-forming peptides and proteins. Time-resolved ssNMR methods with millisecond time resolution have been developed recently to address problems of this type, based on a combination of technologies for rapid mixing, rapid freezing, and low-temperature ssNMR with signal enhancements from dynamic nuclear polarization (DNP). This chapter reviews current time-resolved ssNMR methods, discusses aspects of these methods that have not been emphasized in previous publications, and summarizes information about the molecular mechanism of amyloid-β oligomer formation obtained from time-resolved ssNMR.
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