ThermoTargetMiner as a proteome integral solubility alteration target database for prospective drugs against lung cancer
Lyu, H.; Gharibi, H.; Sokolova, B.; Voiland, A.; Nilsson, B.; Meng, Z.; Gaetani, M.; Saei, A. A.; Zubarev, R.
Show abstract
Knowledge of the targets of therapeutic compounds is vital for understanding their action mechanisms and side effects, but such valuable data is seldom available. The multiple complementary techniques needed for comprehensive target characterization must combine data reliability with sufficient analysis throughput. Here, we leveraged the Proteome Integral Solubility Alteration (PISA) assay to comprehensively characterize the targets of 67 approved drugs and candidate compounds against lung cancer. The analysis was performed on two cell lines representing different lung cancer phenotypes and novel targets for 77% of the tested molecules were found. Comparison of the protein solubility shifts in lysate vs. living cells highlighted the targets directly interacting with the compounds. As PISA analysis is now joining the arsenal of fast and reliable target characterization techniques, the presented database, ThermoTargetMiner, will become a useful resource in lung cancer research.
Matching journals
The top 7 journals account for 50% of the predicted probability mass.
Similar papers in this journal
- Above-Filter Digestion Proteomics reveals drug targets and localizes ligand binding site 97%
- A Comparison of Quantitative Mass Spectrometric Methods for Drug Target Identification by Thermal Proteome Profiling 94%
- Structural Dynamics of the Ubiquitin Specific Protease USP30 in Complex with a Cyanopyrrolidine-Containing Covalent Inhibitor 94%
Similar papers in this journal
- CETSA MS profiling for a comparative assessment of FDA approved antivirals repurposed for COVID-19 therapy identifies Trip13 as a Remdesivir off-target 96%
- A tale of two tails - efficient profiling of protein degraders by specific functional and target engagement readouts 96%
- MICRO-TAG enzyme complementation enables quantification of cellular drug-target engagement in temperature series 93%
Similar papers in this journal
- A Proteomic Platform to Identify Off-Target Proteins Associated with Therapeutic Modalities that Induce Protein Degradation or Gene Silencing 95%
- Rapid Resistance To Bet Inhibitors Is Mediated By Fgfr1 In Glioblastoma 94%
- Selective Impact of ALK and MELK Inhibition on ERα Stability and Cell Proliferation in Cell Lines Representing Distinct Molecular Phenotypes of Breast Cancer 93%
Similar papers in this journal
- Temporal and Spatial Characterization of CUL3KLHL20-driven Targeted Degradation of BET family, BRD Proteins by the Macrocycle-based Degrader BTR2004 94%
- Confounding factors in targeted degradation of short-lived proteins 94%
- A New Platform for Label-Free, Proximal Cellular Pharmacodynamic Assays: Identification of Glutaminase Inhibitors Using Infrared Matrix-Assisted Laser Desorption Electrospray Ionization Mass Spectrometry 93%
Similar papers in this journal
- System-wide profiling by proteome integral solubility alteration assay of drug residence times for target characterization 97%
- Single Cell Chemical Proteomics (SCCP) Interrogates the Timing and Heterogeneity of Cancer Cell Commitment to Death 95%
- A Hit Prioritization Strategy for Compound Library Screening Using LiP-MS and Molecular Dynamics Simulations Applied to KRas G12D Inhibitors 93%
"Similar papers" are the closest papers from that journal in the model's embedding space. They show what the match is built on, but the ranking comes mostly from a classifier over the whole training set, not from these examples alone.