ReviewJournal of biomolecular NMR2018
Late metabolic precursors for selective aromatic residue labeling.
Review in Journal of biomolecular NMR, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- Leveraging relaxation-optimizedNature chemistry · 2025Article
- NMR-driven structure-based drug discovery by unveiling molecular interactions.Communications chemistry · 2025Review
- Expanding the Toolset of Biomolecular NMR with Efficient and Cost-EffectiveChemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- Synthesis of aChembiochem : a European journal of chemical biology · 2025Article
- Towards cost-effective side-chain isotope labelling of proteins expressed in human cells.Journal of biomolecular NMR · 2024Article
- Disentangling the Complexity in Protein Complexes Using Complementary Isotope-Labeling and Multiple-Receiver NMR Spectroscopy.Journal of the American Chemical Society · 2024Article
- Improved spectral resolution of [Journal of biomolecular NMR · 2023Article
- Cell-free synthesis of proteins with selectivelyMagnetic resonance (Gottingen, Germany) · 2023Article
- Specific isotopic labelling and reverse labelling for protein NMR spectroscopy: using metabolic precursors in sample preparation.Biochemical Society transactions · 2022Review
- Long-range structural preformation in yes-associated protein precedes encounter complex formation with TEAD.iScience · 2022Article
- Article
- Synthesis of Isotopically Labeled, Spin-Isolated Tyrosine and Phenylalanine for Protein NMR Applications.Organic letters · 2021Article
- PI by NMR: Probing CH-π Interactions in Protein-Ligand Complexes by NMR Spectroscopy.Angewandte Chemie (International ed. in English) · 2020Article
- Site-selectiveJournal of biomolecular NMR · 2019Article
- Aromatic Ring Dynamics, Thermal Activation, and Transient Conformations of a 468 kDa Enzyme by SpecificJournal of the American Chemical Society · 2019Article
- Advanced isotopic labeling for the NMR investigation of challenging proteins and nucleic acids.Journal of biomolecular NMR · 2018Article
Corrections and comments
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Authors and funding
9 authors.
Funding
Abstract
In recent years, we developed a toolbox of heavy isotope containing compounds, which serve as metabolic amino acid precursors in the E. coli-based overexpression of aromatic residue labeled proteins. Our labeling techniques show excellent results both in terms of selectivity and isotope incorporation levels. They are additionally distinguished by low sample production costs and meet the economic demands to further implement protein NMR spectroscopy as a routinely used method in drug development processes. Different isotopologues allow for the assembly of optimized protein samples, which fulfill the requirements of various NMR experiments to elucidate protein structures, analyze conformational dynamics, or probe interaction surfaces. In the present article, we want to summarize the precursors we developed so far and give examples of their special value in the probing of protein-ligand interaction.
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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.