ReviewJournal of pharmaceutical sciences2008
High-field solution NMR spectroscopy as a tool for assessing protein interactions with small molecule ligands.
Review in Journal of pharmaceutical sciences, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
25 citing papers in PubMed.
- NMR Studies on Protein-Ligand Interactions.International journal of molecular sciences · 2026Review
- Conjugation of Microalgal Phenolics and Protein for Bioactivity and Bioaccessibility Enhancement.Foods (Basel, Switzerland) · 2026Article
- Large-Scale Production of Secretome From Human Dental Pulp Stem Cells for Articular Cartilage Regeneration.Stem cells international · 2026Article
- A method for estimation of plasma protein binding using diffusion ordered NMR spectroscopy (DOSY).RSC medicinal chemistry · 2024Article
- Hierarchical Composite Self-Sorted Supramolecular Gel Noodles.Advanced materials (Deerfield Beach, Fla.) · 2023Article
- A simple and sensitive detection of the binding ligands by using the receptor aggregation and NMR spectroscopy: a test case of the maltose binding protein.Journal of biomolecular NMR · 2021Article
- An amphipathic Bax core dimer forms part of the apoptotic pore wall in the mitochondrial␣membrane.The EMBO journal · 2021Article
- Small molecule inhibitors against PD-1/PD-L1 immune checkpoints and current methodologies for their development: a review.Cancer cell international · 2021Review
- Using NMR spectroscopy to investigate the role played by copper in prion diseases.Neurological sciences : official journal of the Italian Neurological Society and of the Italian Society of Clinical Neurophysiology · 2020Review
- Rational drug-design approach supported with thermodynamic studies - a peptide leader for the efficient bi-substrate inhibitor of protein kinase CK2.Scientific reports · 2019Article
- NMR of Macromolecular Assemblies and Machines at 1 GHz and Beyond: New Transformative Opportunities for Molecular Structural Biology.Methods in molecular biology (Clifton, N.J.) · 2018Review
- Iterative Molecular Dynamics-Rosetta Membrane Protein Structure Refinement Guided by Cryo-EM Densities.Journal of chemical theory and computation · 2017Article
- Intracellular Concentration Gradients That Mirror External Gradients in Microfluidic Flows: A Computational Analysis.Cellular and molecular bioengineering · 2017Article
- Modern Technologies of Solution Nuclear Magnetic Resonance Spectroscopy for Three-dimensional Structure Determination of Proteins Open Avenues for Life Scientists.Computational and structural biotechnology journal · 2017Review
- Data quality in drug discovery: the role of analytical performance in ligand binding assays.Journal of computer-aided molecular design · 2015Article
- Stability analysis of an inline peptide-based conjugate for metal delivery: nickel(II)-claMP Tag epidermal growth factor as a model system.Journal of pharmaceutical sciences · 2015Article
- Drug screening strategy for human membrane proteins: from NMR protein backbone structure to in silica- and NMR-screened hits.Biochemical and biophysical research communications · 2014Article
- GpIbα interacts exclusively with exosite II of thrombin.Journal of molecular biology · 2014Article
- Correlating structure and function of drug-metabolizing enzymes: progress and ongoing challenges.Drug metabolism and disposition: the biological fate of chemicals · 2014Review
- The quiet renaissance of protein nuclear magnetic resonance.Biochemistry · 2013Review
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
The ability of a small molecule to bind and modify the activity of a protein target at a specific site greatly impacts the success of drugs in the pharmaceutical industry. One of the most important tools for evaluating these interactions has been high-field solution nuclear magnetic resonance (NMR) because of its unique ability to examine even weak protein-drug interactions at high resolution. NMR can be used to evaluate the structural, thermodynamic and kinetic aspects of a binding reaction. The basis of NMR screening experiments is that binding causes a perturbation in the physical properties of both molecules. Unique properties of small and macromolecules allow selective detection of either the protein target or ligand, even in a mixture of compounds. This review outlines current methodologies for assessing protein-ligand interactions from the perspectives of the protein target and ligand and delineates the fundamental principles for understanding NMR approaches in drug research. Advances in instrumentation, pulse sequences, isotopic labeling strategies, and the development of competition experiments support the study of higher molecular weight protein targets, facilitate higher-throughput and expand the range of binding affinities that can be evaluated, enhancing the utility of NMR for identifying and characterizing potential therapeutics to druggable protein targets.
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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.