ArticleNature2009
High-resolution multi-dimensional NMR spectroscopy of proteins in human cells.
Article in Nature, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 174 papers.
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Who cites it
174 citing papers in PubMed, 464 citations in OpenAlex.
- High-resolution NMR spectroscopy of proteins in intact mitochondria.Nature chemical biology · 2026Article
- Review
- In-cell NMR spectroscopy: advancements, applications, challenges, and future directions in structural biology.Magma (New York, N.Y.) · 2026Review
- Fast three-dimensional NMR spectroscopy reconstruction based on Hankel matrix with two-directional sliding windows.Magnetic resonance letters · 2026Article
- Real Time Pulse Chase (RTPC) In-Cell NMR Spectroscopy Reveals Critical Metabolites in Subminute Metabolism of Undifferentiated and Differentiated Human Neuronal Cells.Analytical chemistry · 2026Article
- Too close for comfort: Self-crowding transforms protein structure and stability beyond volume exclusion.Protein science : a publication of the Protein Society · 2026Article
- Special Issue "Application of NMR Spectroscopy in Biomolecules".International journal of molecular sciences · 2026Article
- Live Metabolomics with NMR.Analytical chemistry · 2026Review
- Pathogenic Proteins Through the Lens of NMR Spectroscopy: Structural and Functional Insights into Disease.Cell biochemistry and biophysics · 2025Review
- NMR in the Age of Modern Biomedical Research and Drug Discovery.Journal of molecular biology · 2025Review
- Intracellular Binding of Novel Fluorinated Compounds to Carbonic Anhydrase Isoforms Explored by In-CellJournal of medicinal chemistry · 2025Article
- Single-molecule methods for characterizing receptor dimers reveal metastable opioid receptor homodimers that induce functional modulation.Nature communications · 2025Article
- Dynamical interactions among protocell populations: Implications for membrane-mediated chemical evolution.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025Article
- Pushing Sensitivity and Specificity Limits in Native Structural Biology:Journal of the American Chemical Society · 2025Article
- Spatially resolved DNP-assisted NMR illuminates the conformational ensemble of α-synuclein in intact viable cells.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Deep learning network for NMR spectra reconstruction in time-frequency domain and quality assessment.Nature communications · 2025Article
- Exploring Glycan-Lectin Interactions in Natural-Like Environments: A View Using NMR Experiments Inside Cell and on Cell Surface.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- Protein structure and interactions elucidated with in-cell NMR for different cell cycle phases and in 3D human tissue models.Communications biology · 2025Article
- Ubiquitin's Conformational Heterogeneity as Discerned by Nuclear Magnetic Resonance Spectroscopy.Chembiochem : a European journal of chemical biology · 2024Review
- In the Beginning: Let Hydration Be Coded in Proteins for Manifestation and Modulation by Salts and Adenosine Triphosphate.International journal of molecular sciences · 2024Review
114 more citing papers are in PubMed but not listed here.
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Authors and funding
11 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In-cell NMR is an isotope-aided multi-dimensional NMR technique that enables observations of conformations and functions of proteins in living cells at the atomic level. This method has been successfully applied to proteins overexpressed in bacteria, providing information on protein-ligand interactions and conformations. However, the application of in-cell NMR to eukaryotic cells has been limited to Xenopus laevis oocytes. Wider application of the technique is hampered by inefficient delivery of isotope-labelled proteins into eukaryote somatic cells. Here we describe a method to obtain high-resolution two-dimensional (2D) heteronuclear NMR spectra of proteins inside living human cells. Proteins were delivered to the cytosol by the pyrenebutyrate-mediated action of cell-penetrating peptides linked covalently to the proteins. The proteins were subsequently released from cell-penetrating peptides by endogenous enzymatic activity or by autonomous reductive cleavage. The heteronuclear 2D spectra of three different proteins inside human cells demonstrate the broad application of this technique to studying interactions and protein processing. The in-cell NMR spectra of FKBP12 (also known as FKBP1A) show the formation of specific complexes between the protein and extracellularly administered immunosuppressants, demonstrating the utility of this technique in drug screening programs. Moreover, in-cell NMR spectroscopy demonstrates that ubiquitin has much higher hydrogen exchange rates in the intracellular environment, possibly due to multiple interactions with endogenous proteins.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.