ArticleNature protocols2016
Protein-observed (19)F-NMR for fragment screening, affinity quantification and druggability assessment.
Article in Nature protocols, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
What it found
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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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
53 citing papers in PubMed.
- NMR Studies on Protein-Ligand Interactions.International journal of molecular sciences · 2026Review
- Enhancing NMR Signals in Liquids by Fluorine-19 Overhauser Dynamic Nuclear Polarization (DNP) and Hyperpolarization Transfer to Carbon-13.Angewandte Chemie (International ed. in English) · 2025Article
- Direct detection of an NH-π hydrogen bond in an intrinsically disordered peptide.Nature communications · 2025Article
- BPTF Target Engagement by Acetylated H2A.Z Photoaffinity Probes.Biochemistry · 2025Article
- Residue-Specific Incorporation of Noncanonical Amino Acids in Auxotrophic Hosts:Chemical reviews · 2025Review
- High-Efficiency Trifluoromethyl-Methionine Incorporation into Cyclophilin A by Cell-Free Synthesis forAngewandte Chemie (International ed. in English) · 2025Article
- Site-Specific Incorporation of Fluorinated Prolines into Proteins and Their Impact on Neighbouring Residues.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- Perspectives on Applications ofMolecules (Basel, Switzerland) · 2024Review
- Multiplexed Native Mass Spectrometry Determination of Ligand Selectivity for Fatty Acid-Binding Proteins.ACS medicinal chemistry letters · 2024Article
- Controlling the incorporation of fluorinated amino acids in human cells and its structural impact.Protein science : a publication of the Protein Society · 2024Article
- Protein-Engineered Fibers For Drug Encapsulation Traceable viaACS applied nano materials · 2023Article
- UsingACS nanoscience Au · 2023Article
- Carbon-Centered Radicals in Protein Manipulation.ACS central science · 2023Review
- Synthesis of Trifluoromethylated Monoterpene Amino Alcohols.Molecules (Basel, Switzerland) · 2022Article
- Development of a single cultureJournal of fluorine chemistry · 2022Article
- Alternative Mechanisms for DNA Engagement by BET Bromodomain-Containing Proteins.Biochemistry · 2022Article
- Interactions between S100A9 and Alpha-Synuclein: Insight from NMR Spectroscopy.International journal of molecular sciences · 2022Article
- Druggable Allosteric Sites in β-Propeller Lectins.Angewandte Chemie (International ed. in English) · 2022Article
- Review
- FastAnalytical chemistry · 2021Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors.
Funding
Abstract
NMR spectroscopy can be used to quantify the binding affinity between proteins and low-complexity molecules, termed 'fragments'; this versatile screening approach allows researchers to assess the druggability of new protein targets. Protein-observed (19)F-NMR (PrOF NMR) using (19)F-labeled amino acids generates relatively simple spectra that are able to provide dynamic structural information toward understanding protein folding and function. Changes in these spectra upon the addition of fragment molecules can be observed and quantified. This protocol describes the sequence-selective labeling of three proteins (the first bromodomains of Brd4 and BrdT, and the KIX domain of the CREB-binding protein) using commercially available fluorinated aromatic amino acids and fluorinated precursors as example applications of the method developed by our research group. Fragment-screening approaches are discussed, as well as Kd determination, ligand-efficiency calculations and druggability assessment, i.e., the ability to target these proteins using small-molecule ligands. Experiment times on the order of a few minutes and the simplicity of the NMR spectra obtained make this approach well-suited to the investigation of small- to medium-sized proteins, as well as the screening of multiple proteins in the same experiment.
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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.