Thermal profiling reveals phenylalanine hydroxylase as an off-target of panobinostat

Monitoring Drug Target Engagement in Cells and Tissues Using the Cellular Thermal Shift Assay

Molina, D. M., Jafari, R., Ignatushchenko, M., Seki, T., Larsson, E. A., Dan, C., Sreekumar, L., Cao, Y., & Nordlund, P. (2013) · Science · doi:10.1126/science.1233606 · Cited by 2,261

A Human Protein Atlas for Normal and Cancer Tissues Based on Antibody Proteomics

Uhlén, M., Björling, E., Agaton, C., Szigyarto, C. A., Amini, B., Andersen, E., Andersson, A., Angelidou, P., Asplund, A., Asplund, C., et al. (2005) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m500279-mcp200 · Cited by 1,560

Tracking cancer drugs in living cells by thermal profiling of the proteome

Savitski, M. M., Reinhard, F. B. M., Franken, H., Werner, T., Savitski, M. F., Eberhard, D., Molina, D. M., Jafari, R., Dovega, R. B., Klaeger, S., et al. (2014) · Science · doi:10.1126/science.1255784 · Cited by 1,187

Target identification and mechanism of action in chemical biology and drug discovery

Schenone, M., Dančík, V., Wagner, B. K., & Clemons, P. A. (2013) · Nature Chemical Biology · doi:10.1038/nchembio.1199 · Cited by 1,147

Chemoproteomics profiling of HDAC inhibitors reveals selective targeting of HDAC complexes

Bantscheff, M., Hopf, C., Savitski, M. M., Dittmann, A., Grandi, P., Michon, A.-M., Schlegl, J., Abraham, Y., Becher, I., Bergamini, G., et al. (2011) · Nature Biotechnology · doi:10.1038/nbt.1759 · Cited by 659

Thermal proteome profiling for unbiased identification of direct and indirect drug targets using multiplexed quantitative mass spectrometry

Franken, H., Mathieson, T., Childs, D., Sweetman, G. M. A., Werner, T., Tögel, I., Doce, C., Gade, S., Bantscheff, M., Drewes, G., et al. (2015) · Nature Protocols · doi:10.1038/nprot.2015.101 · Cited by 651

Target Identification for Small Bioactive Molecules: Finding the Needle in the Haystack

Ziegler, S., Pries, V., Hedberg, C., & Waldmann, H. (2013) · Angewandte Chemie International Edition · doi:10.1002/anie.201208749 · Cited by 473

Development of the pan-DAC inhibitor panobinostat (LBH589): Successes and challenges

Atadja, P. W. (2009) · Cancer Letters · doi:10.1016/j.canlet.2009.02.019 · Cited by 427

Thermal proteome profiling monitors ligand interactions with cellular membrane proteins

Reinhard, F. B. M., Eberhard, D., Werner, T., Franken, H., Childs, D., Doce, C., Savitski, M. F., Huber, W. K., Bantscheff, M., Savitski, M. M., et al. (2015) · Nature Methods · doi:10.1038/nmeth.3652 · Cited by 310

The Cellular Thermal Shift Assay: A Novel Biophysical Assay for In Situ Drug Target Engagement and Mechanistic Biomarker Studies

Molina, D. M., & Nordlund, P. (2015) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010715-103715 · Cited by 301

Improved in situ characterization of protein complex dynamics at scale with thermal proximity co-aggregation

Sun, S., Zheng, Z., Wang, J., Li, F., He, A., Lai, K., Zhang, S., Lu, J., Tian, R., & Tan, C. S. H. (2023) · Nature Communications · doi:10.1038/s41467-023-43526-2 · Cited by 21

A Simplified Thermal Proteome Profiling Approach to Screen Protein Targets of a Ligand

Zhang, X., Ruan, C., Zhu, H., Li, K., Zhang, W., Wang, K., Hu, L., & Ye, M. (2020) · PROTEOMICS · doi:10.1002/pmic.201900372 · Cited by 21

From Phenotypic Hit to Chemical Probe: Chemical Biology Approaches to Elucidate Small Molecule Action in Complex Biological Systems

Pasquer, Q. T. L., Tsakoumagkos, I. A., & Hoogendoorn, S. (2020) · Molecules · doi:10.3390/molecules25235702 · Cited by 21

Target deconvolution with matrix-augmented pooling strategy reveals cell-specific drug-protein interactions

Ji, H., Lu, X. M., Zhao, S., Wang, Q., Liao, B. Y., Bauer, L. G., Huber, K., Luo, R., Tian, R., & Tan, C. S. H. (2023) · Cell chemical biology · doi:10.1016/j.chembiol.2023.08.002 · Cited by 21

Impact of Mass Spectrometry-Based Technologies and Strategies on Chemoproteomics as a Tool for Drug Discovery

McClure, R. A., & Williams, J. D. (2018) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.8b00181 · Cited by 21

Large-scale characterization of drug mechanism of action using proteome-wide thermal shift assaysPreprint

Vranken, J. G. V., Li, J., Mintseris, J., Wei, T.-Y., Sniezek, C. M., Gadzuk-Shea, M. M., Gygi, S. P., & Schweppe, D. K. (2024) · eLife · doi:10.7554/elife.95595 · Cited by 22

Highly potent quinoxalinediones inhibit α-hemolysin and ameliorate Staphylococcus aureus lung infections

Shekhar, A., Lucrezia, R. D., Jerye, K., Korotkov, V. S., Harmrolfs, K., Rox, K., Weich, H. A., Ghai, I., Delhommel, F., Becher, I., et al. (2025) · Cell Host & Microbe · doi:10.1016/j.chom.2025.03.006 · Cited by 20

Microparticle-Assisted Precipitation Screening Method for Robust Drug Target Identification

Lyu, J., Ruan, C., Zhang, X., Wang, Y., Li, K., & Ye, M. (2020) · Analytical Chemistry · doi:10.1021/acs.analchem.0c02756 · Cited by 20

Chemoproteomics for Plasmodium Parasite Drug Target Discovery

Lu, K., Mansfield, C. R., Fitzgerald, M. C., & Derbyshire, E. R. (2021) · ChemBioChem · doi:10.1002/cbic.202100155 · Cited by 20

Application of Bioactive Thermal Proteome Profiling to Decipher the Mechanism of Action of the Lipid Lowering 132-Hydroxy-pheophytin Isolated from a Marine Cyanobacteria

del Amor, A. C., Freitas, S., Urbatzka, R., Fresnedo, O., & Cristóbal, S. (2019) · Marine Drugs · doi:10.3390/md17060371 · Cited by 20

Über bisherige Denkweisen hinaus – neue Wirkstoffe zur Überwindung der Antibiotika‐Krise

Lakemeyer, M., Zhao, W., Mandl, F. A. M., Hammann, P., & Sieber, S. A. (2018) · Angewandte Chemie · doi:10.1002/ange.201804971 · Cited by 18

Characterizing physical protein targets of chemical contaminants with chemical proteomics: Is it time to fill a crucial environmental toxicology knowledge gap?

Hall, D. R., & Peng, H. (2020) · Comparative Biochemistry and Physiology Part D Genomics and Proteomics · doi:10.1016/j.cbd.2020.100655 · Cited by 18

Thermal Proteome Profiling in Zebrafish Reveals Effects of Napabucasin on Retinoic Acid Metabolism

Leijten, N. M., Bakker, P. A., Spaink, H. P., den Hertog, J., & Lemeer, S. (2020) · Molecular & Cellular Proteomics · doi:10.1074/mcp.ra120.002273 · Cited by 18

ProSAP: a GUI software tool for statistical analysis and assessment of thermal stability data

Ji, H., Lu, X. M., Zheng, Z., Sun, S., & Tan, C. S. H. (2022) · Briefings in Bioinformatics · doi:10.1093/bib/bbac057 · Cited by 16

A Bayesian semi-parametric model for thermal proteome profiling

Fang, S., Kirk, P., Bantscheff, M., Lilley, K. S., & Crook, O. M. (2021) · Communications Biology · doi:10.1038/s42003-021-02306-8 · Cited by 18

Thermal unfolding methods in drug discovery

Llowarch, P., Usselmann, L. E. J., Ivanov, D. P., & Holdgate, G. A. (2023) · Biophysics Reviews · doi:10.1063/5.0144141 · Cited by 17

Identification of Celecoxib-Targeted Proteins Using Label-Free Thermal Proteome Profiling on Rat Hippocampus

Gholizadeh, E., Karbalaei, R., Khaleghian, A., Salimi, M., Gilany, K., Soliymani, R., Tanoli, Z., Rezadoost, H., Baumann, M., Jafari, M., et al. (2021) · Molecular Pharmacology · doi:10.1124/molpharm.120.000210 · Cited by 18

New applications of advanced instrumental techniques for the characterization of food allergenic proteins

Benedé, S., Lozano‐Ojalvo, D., Cristóbal, S., Costa, J. S., D'Auria, E., Veličković, T. Ć., Garrido‐Arandia, M., Karakaya, S., Mafra, I., Mazzucchelli, G., et al. (2021) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2021.1931806 · Cited by 17

Dextromethorphan inhibits collagen and collagen-like cargo secretion to ameliorate lung fibrosis

Khan, M. M., Galea, G., Jung, J. E., Zukowska, J., Lauer, D., Tuechler, N., Halavatyi, A. A., Tischer, C., Haberkant, P., Stein, F., et al. (2024) · Science Translational Medicine · doi:10.1126/scitranslmed.adj3087 · Cited by 16

Hidden information on protein function in censuses of proteome foldedness

Cox, D., Ang, C.-S., Nillegoda, N. B., Reid, G. E., & Hatters, D. M. (2022) · Nature Communications · doi:10.1038/s41467-022-29661-2 · Cited by 16

A phenotypic screen of the Global Health Priority Box identifies an insecticide with anthelmintic activity

Shanley, H. T., Taki, A. C., Byrne, J. J., Nguyen, N., Wells, T. N. C., Jabbar, A., Sleebs, B. E., & Gasser, R. B. (2024) · Parasites & Vectors · doi:10.1186/s13071-024-06183-y · Cited by 15

Toward the analysis of functional proteoforms using mass spectrometry-based stability proteomics

Kang, J., Seshadri, M., Cupp‐Sutton, K. A., & Wu, S. (2023) · Frontiers in Analytical Science · doi:10.3389/frans.2023.1186623 · Cited by 14

The potential of cross-linking mass spectrometry in the development of protein–protein interaction modulators

Ruwolt, M., Piazza, I., & Liu, F. (2023) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2023.102648 · Cited by 14

Mechanistic Insights into a CDK9 Inhibitor Via Orthogonal Proteomics Methods

Hendricks, J. A., Beaton, N., Chernobrovkin, A. L., Miele, E., Hamza, G. M., Ricchiuto, P., Tomlinson, R., Friman, T., Borenstain, C., Barlaam, B. C., et al. (2021) · ACS Chemical Biology · doi:10.1021/acschembio.1c00488 · Cited by 14

A Comparative Study of Target Engagement Assays for HDAC1 Inhibitor Profiling

Asawa, R. R., Zakharov, A. V., Niehoff, T., Ata, C., Jadhav, A., Henderson, M. J., Simeonov, A. M., & Martinez, N. J. (2019) · SLAS DISCOVERY · doi:10.1177/2472555219883625 · Cited by 14

The right tools for the job: the central role for next generation chemical probes and chemistry-based target deconvolution methods in phenotypic drug discovery

Jörg, M., & Madden, K. S. (2021) · RSC Medicinal Chemistry · doi:10.1039/d1md00022e · Cited by 14

Structure-activity relationship and target investigation of 2-aryl quinolines with nematocidal activity

Shanley, H. T., Taki, A. C., Nguyen, N. H., Wang, T., Byrne, J. J., Ang, C., Leeming, M. G., Nie, S., Williamson, N. A., Zheng, Y., et al. (2024) · International Journal for Parasitology Drugs and Drug Resistance · doi:10.1016/j.ijpddr.2024.100522 · Cited by 13

Experimental and data analysis advances in thermal proteome profiling

Figueroa‐Navedo, A. M., & Ivanov, A. R. (2024) · Cell Reports Methods · doi:10.1016/j.crmeth.2024.100717 · Cited by 14

Thermal Proteome Profiling for Drug Target Identification and Probing of Protein States

Sauer, P., & Bantscheff, M. (2023) · Methods in molecular biology · doi:10.1007/978-1-0716-3457-8_5 · Cited by 12

Global Mapping of Metalloproteomes

Zeng, X., Cheng, Y., & Wang, C. (2021) · Biochemistry · doi:10.1021/acs.biochem.1c00404 · Cited by 14

Target Discovery Using Thermal Proteome Profiling

Sridharan, S., Günthner, I., Becher, I., Savitski, M. M., & Bantscheff, M. (2019) · Wiley eBooks · doi:10.1002/9781118970195.ch11 · Cited by 13

Integrated Protein Solubility Shift Assays for Comprehensive Drug Target Identification on a Proteome-Wide Scale

Zhang, X., Ruan, C., Wang, Y., Wang, K., Liu, X., Lyu, J., & Ye, M. (2023) · Analytical Chemistry · doi:10.1021/acs.analchem.3c00072 · Cited by 11

Large-scale characterization of drug mechanism of action using proteome-wide thermal shift assays

Vranken, J. G. V., Li, J., Mintseris, J., Wei, T.-Y., Sniezek, C. M., Gadzuk-Shea, M. M., Gygi, S. P., & Schweppe, D. K. (2024) · eLife · doi:10.7554/elife.95595.3 · Cited by 11

Poly-pharmacology of existing drugs: How to crack the code?

Mouysset, B., Grand, M. L., Camoin, L., & Pasquier, E. (2024) · Cancer Letters · doi:10.1016/j.canlet.2024.216800 · Cited by 11

Interaction profiling methods to map protein and pathway targets of bioactive ligands

Huang, J., Coukos, J. S., & Moellering, R. E. (2020) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2020.02.001 · Cited by 10

PACTS-Assisted Thermal Proteome Profiling for Use in Identifying Peptide-Interacting Proteins

Zhao, T., Tian, J., Wang, X., Hao, Y., Xu, M., Zhao, Y., Liu, X., Chen, Y., & Jia, C. (2022) · Analytical Chemistry · doi:10.1021/acs.analchem.2c00581 · Cited by 10

A Matrix-Assisted Laser Desorption/Ionization Time-of-Flight Assay Identifies Nilotinib as an Inhibitor of Inflammation in Acute Myeloid Leukemia

Marín‐Rubio, J. L., Heap, R. E., Dueñas, M. E., Heunis, T. D. J., Dannoura, A., Inns, J., Scott, J., Simpson, A. J., Blair, H. J., Heidenreich, O. T., et al. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.2c00671 · Cited by 10

Deoxycytidine kinase (dCK) inhibition is synthetic lethal with BRCA2 deficiency

Guantay, L., Garro, C., Siri, S. O., Pansa, M. F., Ghidelli, S., Paviolo, N. S., Racca, A. C., Nicotra, V. E., Radu, C. G., Bocco, J. L., et al. (2023) · Drug Resistance Updates · doi:10.1016/j.drup.2023.100932 · Cited by 10

Progress in mass spectrometry approaches to profiling protein–protein interactions in the studies of the innate immune system

Kim, D., & Nita‐Lazar, A. (2024) · Journal of Proteins and Proteomics · doi:10.1007/s42485-024-00156-6 · Cited by 9

Affinity Enrichment Chemoproteomics for Target Deconvolution and Selectivity Profiling

Werner, T., Steidel, M., Eberl, H. C., & Bantscheff, M. (2021) · Methods in molecular biology · doi:10.1007/978-1-0716-1024-4_17 · Cited by 9

Identifying Protein–Drug Interactions in Cell Lysates Using Histidine Hydrogen Deuterium Exchange

Miyagi, M., Tanaka, K., Watanabe, S., Kondo, J., & Kishimoto, T. (2021) · Analytical Chemistry · doi:10.1021/acs.analchem.1c02283 · Cited by 9

Small Molecule Arranged Thermal Proximity Coaggregation (smarTPCA)—A Novel Approach to Characterize Protein–Protein Interactions in Living Cells by Similar Isothermal Dose–Responses

Lenz, T., & Stühler, K. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23105605 · Cited by 9

Towards a systematic map of the functional role of protein phosphorylationPreprint

Viéitez, C., Busby, B. P., Ochoa, D., Mateus, A., Galardini, M., Jawed, A., Memon, D., Potel, C. M., Vonesch, S. C., Szu‐Tu, C., et al. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/872770 · Cited by 9

Emerging trends in chemoproteomics: Mapping the landscape of protein–metabolite interactions

Wan, N., Liu, C., Hao, H., & Ye, H. (2025) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2025.102631 · Cited by 8

Studying Target–Engagement of Anti-Infectives by Solvent-Induced Protein Precipitation and Quantitative Mass Spectrometry

Bizzarri, L., Steinbrunn, D., Quennesson, T., Lacour, A., Bianchino, G. I., Bravo, P., Chaignon, P., Lohse, J., Mäser, P., Seemann, M., et al. (2024) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.4c00417 · Cited by 8

A Chemoproteomic Approach for System-Wide and Site-Specific Uncovering of Functional Protein N-Glycosylation

Wang, G., Ma, S., Song, H., Liang, Y., Li, X., Zhang, L., Lu, H., & Zhang, Y. (2025) · Journal of the American Chemical Society · doi:10.1021/jacs.5c08065 · Cited by 8

Lysosomal protein thermal stability does not correlate with cellular half-life: global observations and a case study of tripeptidyl-peptidase 1

Collier, A. M., Nemtsova, Y., Kuber, N., Banach-Petrosky, W. A., Modak, A., Sleat, D. E., Nanda, V., & Lobel, P. (2020) · Biochemical Journal · doi:10.1042/bcj20190874 · Cited by 8

Label-Free Quantitative Thermal Proteome Profiling Reveals Target Transcription Factors with Activities Modulated by MC3R Signaling

Sandbaumhüter, F. A., Nezhyva, M., Andrén, P. E., & Jansson, E. T. (2023) · Analytical Chemistry · doi:10.1021/acs.analchem.3c03643 · Cited by 8

Proteomic tools to study drug function

Mulder, C., Leijten, N. M., & Lemeer, S. (2018) · Current Opinion in Systems Biology · doi:10.1016/j.coisb.2018.05.002 · Cited by 8

MS methods to study macromolecule-ligand interaction: Applications in drug discovery

Sirtori, F. R., Altomare, A., Carini, M., Aldini, G., & Regazzoni, L. (2018) · Methods · doi:10.1016/j.ymeth.2018.06.005 · Cited by 8

Direct label-free methods for identification of target proteins in agrochemicals

Zhao, B., Liu, N., Chen, L., Geng, S., Fan, Z., & Xing, J. (2020) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2020.07.237 · Cited by 8

Thermal proteome profiling and machine learning modeling for dissecting chemical-protein interactions in environmental toxicology: A mini-review and perspectives

Wu, Z., Fu, Z., Yu, X., & Chen, J. (2024) · Critical Reviews in Environmental Science and Technology · doi:10.1080/10643389.2024.2320753 · Cited by 7

Improved drug target deconvolution with PISA‐DIA using an extended, overlapping temperature gradient

Emery‐Corbin, S. J., Yousef, J. M., Adhikari, S., Sumardy, F., Nhu, D., van Delft, M. F., Lessène, G., Dziekan, J. M., Webb, A. I., & Dagley, L. F. (2024) · PROTEOMICS · doi:10.1002/pmic.202300644 · Cited by 7

Investigation of Cellular Response to the HSP90 Inhibition in Human Cells Through Thermal Proteome Profiling

Yin, K., & Wu, R. (2023) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2023.100560 · Cited by 7

A novel antifolate suppresses growth of FPGS-deficient cells and overcomes methotrexate resistance

van der Krift, F., Zijlmans, D. W., Shukla, R., Javed, A., Koukos, P. I., Schwarz, L. L. E., Timmermans‐Sprang, E. P. M., Maas, P. E. M., Gahtory, D., van den Nieuwboer, M., et al. (2023) · Life Science Alliance · doi:10.26508/lsa.202302058 · Cited by 7

Structure activity relationship and target prediction for ABX464 analogues in Caenorhabditis elegans

Shanley, H. T., Taki, A. C., Nguyen, N. H., Wang, T., Byrne, J. J., Ang, C., Leeming, M. G., Nie, S., Williamson, N. A., Zheng, Y., et al. (2023) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2023.117540 · Cited by 7

In-depth characterization of Staurosporine induced proteome thermal stability changesPreprint

Chernobrovkin, A. L., Lengqvist, J., Körner, C. C., Amadio, D., Friman, T., & Molina, D. M. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.03.13.990606 · Cited by 7

Integrated thermal proteome and thermal proximity co-aggregation profiling identifies ATP6V1C1 as a novel anti-cancer drug target

Zhang, S., Li, F., Wang, J., Dong, Y. J., Luo, J.-F., Huang, X., Li, Y., Zhu, G., Qi, S. N., Shen, H., et al. (2025) · International Journal of Biological Sciences · doi:10.7150/ijbs.106843 · Cited by 6

Thermal proteome profiling of itaconate interactome in macrophages

Meng, Y., Wei, T., Zhang, C., Yu, A., Liu, Y., Xiao, J., & Wang, C. (2025) · Chemical Science · doi:10.1039/d5sc02378e · Cited by 6

Expanding the Reach of Membrane Protein–Ligand Interaction Studies Through the Integration of Mass Spectrometry and Membrane Mimetics

Lambos, J. C., Bhattacharya, A., Al‐Seragi, M., & Duong, F. (2025) · PROTEOMICS · doi:10.1002/pmic.70057 · Cited by 9

Hepatocyte proteome destabilization and novel targets for PFASs unveiled through combined thermal proteome profiling and deep transfer learning

Wu, Z., Zou, Y., Yang, K., Yu, X., Fu, Z., Le, X. C., & Chen, J. (2025) · Journal of Hazardous Materials · doi:10.1016/j.jhazmat.2025.140458 · Cited by 6

Spike-In Proteome Enhances Data-Independent Acquisition for Thermal Proteome Profiling

Wang, Q., Chen, Q., Lin, Y., He, D., Ji, H., & Tan, C. S. H. (2024) · Analytical Chemistry · doi:10.1021/acs.analchem.4c04837 · Cited by 6

Natural product drupacine acting on a novel herbicidal target shikimate dehydrogenase

Ma, S., Yu, H., Wang, M., Cui, T., Zhao, Y., Zhang, X., Wang, C., Li, M., Zhang, L., & Dong, J. (2023) · Pesticide Biochemistry and Physiology · doi:10.1016/j.pestbp.2023.105480 · Cited by 6

Orthogonal Strategies for Profiling Potential Cellular Targets of Anandamide and Cannabidiol

Tang, G., Lim, Y., Wang, W., Ye, Z., Zhang, C., & Yao, S. Q. (2023) · Chemistry - A European Journal · doi:10.1002/chem.202300682 · Cited by 6

Design and synthesis of bioreductive prodrugs of class I histone deacetylase inhibitors and their biological evaluation in virally transfected acute myeloid leukemia cells

Abdelsalam, M. A. M., Zmyslia, M., Schmidtkunz, K., Vecchio, A., Hilscher, S., Ibrahim, H. S., Schutkowski, M., Jung, M., Jessen‐Trefzer, C., & Sippl, W. (2023) · Archiv der Pharmazie · doi:10.1002/ardp.202300536 · Cited by 5

A novel L-shaped ortho-quinone analog suppresses glioblastoma progression by targeting acceleration of AR degradation and regulating PI3K/AKT pathway

Zhang, T., Pan, W., Tan, X., Yu, J., Cheng, S., Wei, S., Fan, K., Wang, L., Luo, H., & Hu, X. (2024) · Biochemical Pharmacology · doi:10.1016/j.bcp.2024.116398 · Cited by 5

Epigenetic drug target deconvolution by mass spectrometry–based technologies

Noberini, R., & Bonaldi, T. (2019) · Nature Structural & Molecular Biology · doi:10.1038/s41594-019-0279-x · Cited by 6

Synergistic Effects of PARP Inhibition and Cholesterol Biosynthesis Pathway Modulation

Rutkowska, A., Eberl, H. C., Werner, T., Hennrich, M. L., Sévin, D. C., Petretich, M., Reddington, J. P., Pocha, S. M., Gade, S., Martinez-Segura, A., et al. (2024) · Cancer Research Communications · doi:10.1158/2767-9764.crc-23-0549 · Cited by 5

Selective chemical probes can untangle the complexity of the plant cell endomembrane system

Ma, Q., Chang, M., Drakakaki, G., & Russinova, E. (2022) · Current Opinion in Plant Biology · doi:10.1016/j.pbi.2022.102223 · Cited by 5

Proteomics contributions to epigenetic drug discovery

Noberini, R., & Bonaldi, T. (2023) · PROTEOMICS · doi:10.1002/pmic.202200435 · Cited by 5

GPMelt: A hierarchical Gaussian process framework to explore the dark meltome of thermal proteome profiling experiments

Sueur, C. L., Rattray, M., & Savitski, M. M. (2024) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1011632 · Cited by 9

Proteome thermal stability reflects organ physiology and identifies drug-target engagement in vivoPreprint

Perrin, J., Werner, T., Kurzawa, N., Childs, D., Kalxdorf, M., Rutkowska, A., Poeckel, D., Sévin, D. C., Stonehouse, E., Strohmer, K., et al. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/500306 · Cited by 5

LiP-Quant, an automated chemoproteomic approach to identify drug targets in complex proteomesPreprint

Piazza, I., Beaton, N., Bruderer, R., Knobloch, T., Barbisan, C., Siepe, I., Rinner, O., de Souza, N., Picotti, P., & Reiter, L. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/860072 · Cited by 5

Off-target identification by chemical proteomics for the understanding of drug side effects

Song, Y., Luo, L., & Wang, K. (2020) · Expert Review of Proteomics · doi:10.1080/14789450.2020.1873134 · Cited by 5

TP-MAP - an Integrated Software Package for the Analysis of 1D and 2D Thermal Profiling DataPreprint

Feyertag, F., & Huber, K. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.02.22.432361 · Cited by 4

Large-scale characterization of drug mechanism of action using proteome-wide thermal shift assaysPreprint

Vranken, J. G. V., Li, J., Mintseris, J., Wei, T.-Y., Sniezek, C. M., Gadzuk-Shea, M. M., Gygi, S. P., & Schweppe, D. K. (2024) · eLife · doi:10.7554/elife.95595.2 · Cited by 6

Top‐Down Thermal Proteome Profiling (TD‐TPP) for Functional Characterization of the Intact Proteoforms in Complex Samples

Cupp‐Sutton, K. A., Guo, Y., Welborn, T., & Wu, S. (2025) · Journal of Mass Spectrometry · doi:10.1002/jms.5187 · Cited by 4

A BRET biosensor for measuring uncompetitive engagement of PRMT5 complexes in cells

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