ArticleJournal of the American Chemical Society2025
In-Cell Residue-Resolved NMR of Micromolar α-Synuclein and Tau at 310 K.
Article in Journal of the American Chemical Society, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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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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Who cites it
1 citing paper in PubMed.
- Metal Binding to Tau Protein: Physiological and Pathological Relevance.Biochemistry · 2026Review
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Authors and funding
6 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Aggregates of nonglobular proteins are associated with several degenerative disorders, e.g., α-synuclein and tau involved in Parkinson's and Alzheimer's diseases. Do these proteins undergo progressive changes in their conformations and interactions in pathologic situations? In-cell NMR provides atomic-scale information in live cells but, until now, only at ∼283 K in the case of unfolded proteins. Here, we report new labeling and acquisition methods enabling in-cell NMR at 310 K to study these proteins at micromolar concentrations, i.e., native cellular abundances. We used stable human cell lines expressing α-synuclein or tau upon induction in a culture medium supplemented with
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