ReviewNature reviews. Chemistry2021
Exploring new targets and chemical space with affinity selection-mass spectrometry.
Review in Nature reviews. Chemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
45 citing papers in PubMed.
- Review
- Scaling covalent ligand discovery through dynamic combinatorial library-versus-proteome screening.Nature communications · 2026Article
- Biophysical Sensing Tools in Drug Discovery: Integrating Kinetics, Thermodynamics, Cellular Target Engagement and Structure.Sensors (Basel, Switzerland) · 2026Review
- Integration of palladium-catalyzed C-N coupling into self-encoded libraries for accelerated hit discovery.RSC chemical biology · 2026Article
- Quantifying Protein Homodimer Affinities and the Effect of Molecular Glues and Interface Residues Using Native Mass Spectrometry.Journal of the American Chemical Society · 2026Article
- Target-Centric Multiplexed Screening of an Herbal Extract Identifies a Novel Dual AACS central science · 2026Article
- Breaking the boundaries of affinity selection-mass spectrometry: From ligand screening to target-ligand interaction insights.Journal of pharmaceutical analysis · 2026Review
- Direct-to-Biology Enabled Molecular Glue Discovery.Journal of the American Chemical Society · 2026Article
- Mass Spectrometry Proteomics: A Key to Faster Drug Discovery.Journal of medicinal chemistry · 2026Review
- Integrating high-resolution bioassay profiling with affinity-based ligand fishing for unveiling galloylated derivatives as novel catechol-Journal of pharmaceutical analysis · 2026Article
- Enantioselective protein affinity selection mass spectrometry (E-ASMS).Nature communications · 2025Article
- High-Frequency Microfluidic Fractionation for Compound-Resolved Bioactivity-Based Metabolomics.Analytical chemistry · 2025Article
- Affinity Selection-Mass Spectrometry for the Identification of Ligands of Acetylcholinesterase fromACS omega · 2025Article
- Barcode-free hit discovery from massive libraries enabled by automated small molecule structure annotation.Nature communications · 2025Article
- Tryptoline Stereoprobe Elaboration Identifies Inhibitors of the GRPEL1-HSPA9 Chaperone Complex.bioRxiv : the preprint server for biology · 2025Article
- DNA-encoded library screening uncovers potent DNMT2 inhibitors targeting a cryptic allosteric binding site.iScience · 2025Article
- The Discovery of a Novel Anticoagulant Mechanism: Factor XI Activation Inhibitors.ACS pharmacology & translational science · 2025Article
- Protein-ligand data at scale to support machine learning.Nature reviews. Chemistry · 2025Review
- Neural Spectral Prediction for Structure Elucidation with Tandem Mass Spectrometry.bioRxiv : the preprint server for biology · 2025Article
- Differential scanning fluorimetry followed by microscale thermophoresis and/or isothermal titration calorimetry as an efficient tool for ligand screening.Biophysical reviews · 2025Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Affinity selection-mass spectrometry (AS-MS) is a high-throughput screening (HTS) technique for drug discovery that enables rapid screening of large collections of compounds to identify ligands for a specific biomolecular target. AS-MS is a binding assay that is insensitive to the functional effects a ligand might have, which is important because it lets us identify novel ligands irrespective of their binding site. This approach is gaining popularity, notably due to its role in the emergence of useful agents for targeted protein degradation. This Perspective highlights the use of AS-MS techniques to explore broad chemical space and identify small-molecule ligands for biological targets that have proven challenging to address with other screening paradigms. We present chemical structures of reported AS-MS hits to illustrate the potential of this screening approach to deliver high-quality hits for further optimization. AS-MS has, thus, evolved from being an infrequent alternative to traditional HTS or DNA-encoded library strategies to now firmly establishing itself as a HTS approach for drug discovery.
Identifiers
37118102What OpenQuestion holds
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.