ArticleJournal of proteome research2023
Comparison of Quantitative Mass Spectrometric Methods for Drug Target Identification by Thermal Proteome Profiling.
Article in Journal of proteome research, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 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
20 citing papers in PubMed, 36 citations in OpenAlex.
- Cell-type-specific proximity labeling of organ secretomes reveals energy balance-dependent proteomic remodeling.Cell reports · 2026Article
- Data-Independent Acquisition (DIA) Strategy for Measuring Protein Stability Using Stability of Proteins from Rates of Oxidation (SPROX).Journal of the American Society for Mass Spectrometry · 2026Article
- Analysis of tumor stem cell recruitment and integration in microvascular architectural heterogeneity during oral mucosal carcinogenesis: an in vivo experimental study.Journal of translational medicine · 2026Article
- Cell type-specific proximity labeling of organ secretomes reveals energy balance-dependent proteomic remodeling.bioRxiv : the preprint server for biology · 2026Article
- Mass Spectrometry Proteomics: A Key to Faster Drug Discovery.Journal of medicinal chemistry · 2026Review
- Pathway coessentiality mapping reveals complex II is required for de novo purine biosynthesis in acute myeloid leukaemia.Nature metabolism · 2025Article
- Expanding the Reach of Membrane Protein-Ligand Interaction Studies Through the Integration of Mass Spectrometry and Membrane Mimetics.Proteomics · 2025Review
- Studying Target-Engagement of Anti-Infectives by Solvent-Induced Protein Precipitation and Quantitative Mass Spectrometry.ACS infectious diseases · 2024Article
- One-Pot Time-Induced Proteome Integral Solubility Alteration Assay for Automated and Sensitive Drug-Target Identification.Analytical chemistry · 2024Article
- Characterizing protein-protein interactions with thermal proteome profiling.Current opinion in structural biology · 2024Review
- Streamlined analysis of drug targets by proteome integral solubility alteration indicates organ-specific engagement.Nature communications · 2024Article
- Exploring the anticancer mechanism of cardiac glycosides using proteome integral solubility alteration approach.Cancer medicine · 2024Article
- I'm Walking into Spiderwebs: Making Sense of Protein-Protein Interaction Data.Journal of proteome research · 2024Review
- Chemoproteomics validates selective targeting ofeLife · 2024Article
- Investigating Antiprotozoal Chemotherapies with Novel Proteomic Tools-Chances and Limitations: A Critical Review.International journal of molecular sciences · 2024Review
- Stability-based approaches in chemoproteomics.Expert reviews in molecular medicine · 2024Review
- Tapioca: a platform for predicting de novo protein-protein interactions in dynamic contexts.Nature methods · 2024Article
- Experimental and data analysis advances in thermal proteome profiling.Cell reports methods · 2024Review
- High-throughput drug target discovery using a fully automated proteomics sample preparation platform.Chemical science · 2024Article
- Toward the analysis of functional proteoforms using mass spectrometry-based stability proteomics.Frontiers in analytical science · 2023Article
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 at 1 institution in 1 country.
Funding
Abstract
Thermal proteome profiling (TPP) provides a powerful approach to studying proteome-wide interactions of small therapeutic molecules and their target and off-target proteins, complementing phenotypic-based drug screens. Detecting differences in thermal stability due to target engagement requires high quantitative accuracy and consistent detection. Isobaric tandem mass tags (TMTs) are used to multiplex samples and increase quantification precision in TPP analysis by data-dependent acquisition (DDA). However, advances in data-independent acquisition (DIA) can provide higher sensitivity and protein coverage with reduced costs and sample preparation steps. Herein, we explored the performance of different DIA-based label-free quantification approaches compared to TMT-DDA for thermal shift quantitation. Acute myeloid leukemia cells were treated with losmapimod, a known inhibitor of MAPK14 (p38α). Label-free DIA approaches, and particularly the library-free mode in DIA-NN, were comparable of TMT-DDA in their ability to detect target engagement of losmapimod with MAPK14 and one of its downstream targets, MAPKAPK3. Using DIA for thermal shift quantitation is a cost-effective alternative to labeled quantitation in the TPP pipeline.
Indexed as
Identifiers
What 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.