ArticleCommunications biology2025
Protein structure and interactions elucidated with in-cell NMR for different cell cycle phases and in 3D human tissue models.
Article in Communications biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Real-time NMR analysis of glutamine metabolism for screening anti-cancer agents in living cells.Magnetic resonance letters · 2027Article
- RNA circularization preserves dynamics and enables in-cell relaxation NMR.Nucleic acids research · 2026Article
- Endogenous Site-Specific Encoding of Trifluoromethyl-Bearing Phenylalanine and Tryptophan for in-CellJournal of the American Chemical Society · 2026Article
- How does NMR support SARS-CoV-2 protein-ligand interaction studies?Analytical and bioanalytical chemistry · 2026Review
- In-Cell Residue-Resolved NMR of Micromolar α-Synuclein and Tau at 310 K.Journal of the American Chemical Society · 2025Article
- Protein structure and interactions elucidated with in-cell NMR for different cell cycle phases and in 3D human tissue models.Communications biology · 2025Article
Corrections and comments
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Authors and funding
14 authors.
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Abstract
Most of our knowledge of protein structure and function originates from experiments performed with purified proteins resuspended in dilute, buffered solutions. However, most proteins function in crowded intracellular environments with complex compositions. Significant efforts have been made to develop tools to study proteins in their native cellular settings. Among these tools, in-cell NMR spectroscopy has been the sole technique for characterizing proteins in the intracellular space of living cells at atomic resolution and physiological temperature. Nevertheless, due to technological constraints, in-cell NMR studies have been limited to asynchronous single-cell suspensions, precluding obtaining information on protein behavior in different cellular states. In this study, we present a methodology that allows for obtaining an atomically resolved NMR readout of protein structure and interactions in living human cells synchronized in specific cell cycle phases and within 3D models of human tissue. The described approach opens avenues for investigating how protein structure or drug recognition responds to cell-cell communication or changes in intracellular space composition during transitions among cell cycle phases.
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Registered trials
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