ArticleNature communications2024
Streamlined analysis of drug targets by proteome integral solubility alteration indicates organ-specific engagement.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 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
18 citing papers in PubMed.
- ThermoTargetMiner as a proteome integral solubility alteration target database for prospective drugs against lung cancer.Communications chemistry · 2026Article
- Global protein-ligand binding affinity profiling via photocatalytic labeling.Nature communications · 2026Article
- Robotic perturbation proteomics and AI agents enable scalable drug mechanism discovery.bioRxiv : the preprint server for biology · 2026Article
- Peptide-centric local stability assay (PELSA) for sensitive identification of ligand-targeting proteins and binding sites at proteome scale.Nature protocols · 2026Review
- Regulation of RNA-binding proteins by small biomolecules.Nature reviews. Molecular cell biology · 2026Review
- Advancing DIA-Based Limited Proteolysis Workflows: Introducing DIA-LiPA.Analytical chemistry · 2026Article
- Real-time visualization of drug-target interactions in native subcellular microenvironments for lysosome-targeted drug discovery.Journal of pharmaceutical analysis · 2026Article
- High-throughput peptide-centric local stability assay extends protein-ligand identification to membrane proteins, tissues and bacteria.Nature structural & molecular biology · 2026Article
- Chemical perturbation reveals a cytoskeletal-trafficking vulnerability inFrontiers in pharmacology · 2026Article
- Proteome-Wide Monitoring of Drug Action in Living Cells Using a Novel Label-Free Solvent-Based Shift Assay.Molecular & cellular proteomics : MCP · 2025Article
- Proteolytic profiling of human plasma reveals an immunoactive complement C3 fragment.The EMBO journal · 2025Article
- Solvent-induced partial cellular fixation decodes proteome-wide drug targets and downstream pathways in living cells.Nature communications · 2025Article
- High-throughput proteome integral solubility alteration assay for low cell input using One-Tip.Communications chemistry · 2025Article
- Evaluating Biocompatibility: From Classical Techniques to State-of-the-Art Functional Proteomics.Nanomaterials (Basel, Switzerland) · 2025Review
- Characterization of dsRNA binding proteins through solubility analysis identifies ZNF385A as a dsRNA homeostasis regulator.Nature communications · 2025Article
- Recent Advances in Mass Spectrometry-Based Bottom-Up Proteomics.Analytical chemistry · 2025Review
- Biocontrol potential of newly isolatedFrontiers in microbiology · 2025Article
- One-Pot Time-Induced Proteome Integral Solubility Alteration Assay for Automated and Sensitive Drug-Target Identification.Analytical chemistry · 2024Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors.
Funding
Abstract
Proteins are the primary targets of almost all small molecule drugs. However, even the most selectively designed drugs can potentially target several unknown proteins. Identification of potential drug targets can facilitate design of new drugs and repurposing of existing ones. Current state-of-the-art proteomics methodologies enable screening of thousands of proteins against a limited number of drug molecules. Here we report the development of a label-free quantitative proteomics approach that enables proteome-wide screening of small organic molecules in a scalable, reproducible, and rapid manner by streamlining the proteome integral solubility alteration (PISA) assay. We used rat organs ex-vivo to determine organ specific targets of medical drugs and enzyme inhibitors to identify drug targets for common drugs such as Ibuprofen. Finally, global drug profiling revealed overarching trends of how small molecules affect the proteome through either direct or indirect protein interactions.
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What Socratic 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 Socratic graph.