@article{savitski_tracking_2014,
	title = {Tracking cancer drugs in living cells by thermal profiling of the proteome},
	volume = {346},
	url = {https://www-science-org.ezp-prod1.hul.harvard.edu/doi/full/10.1126/science.1255784},
	doi = {10.1126/science.1255784},
	abstract = {The thermal stability of proteins can be used to assess ligand binding in living cells. We have generalized this concept by determining the thermal profiles of more than 7000 proteins in human cells by means of mass spectrometry. Monitoring the effects of small-molecule ligands on the profiles delineated more than 50 targets for the kinase inhibitor staurosporine. We identified the heme biosynthesis enzyme ferrochelatase as a target of kinase inhibitors and suggest that its inhibition causes the phototoxicity observed with vemurafenib and alectinib. Thermal shifts were also observed for downstream effectors of drug treatment. In live cells, dasatinib induced shifts in BCR-ABL pathway proteins, including CRK/CRKL. Thermal proteome profiling provides an unbiased measure of drug-target engagement and facilitates identification of markers for drug efficacy and toxicity.},
	number = {6205},
	urldate = {2023-11-29},
	journal = {Science},
	author = {Savitski, Mikhail M. and Reinhard, Friedrich B. M. and Franken, Holger and Werner, Thilo and Savitski, Maria Fälth and Eberhard, Dirk and Molina, Daniel Martinez and Jafari, Rozbeh and Dovega, Rebecca Bakszt and Klaeger, Susan and Kuster, Bernhard and Nordlund, Pär and Bantscheff, Marcus and Drewes, Gerard},
	month = oct,
	year = {2014},
	note = {Publisher: American Association for the Advancement of Science},
	pages = {1255784},
}

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Monitoring the effects of small-molecule ligands on the profiles delineated more than 50 targets for the kinase inhibitor staurosporine. We identified the heme biosynthesis enzyme ferrochelatase as a target of kinase inhibitors and suggest that its inhibition causes the phototoxicity observed with vemurafenib and alectinib. Thermal shifts were also observed for downstream effectors of drug treatment. In live cells, dasatinib induced shifts in BCR-ABL pathway proteins, including CRK/CRKL. Thermal proteome profiling provides an unbiased measure of drug-target engagement and facilitates identification of markers for drug efficacy and toxicity.","number":"6205","urldate":"2023-11-29","journal":"Science","author":[{"propositions":[],"lastnames":["Savitski"],"firstnames":["Mikhail","M."],"suffixes":[]},{"propositions":[],"lastnames":["Reinhard"],"firstnames":["Friedrich","B.","M."],"suffixes":[]},{"propositions":[],"lastnames":["Franken"],"firstnames":["Holger"],"suffixes":[]},{"propositions":[],"lastnames":["Werner"],"firstnames":["Thilo"],"suffixes":[]},{"propositions":[],"lastnames":["Savitski"],"firstnames":["Maria","Fälth"],"suffixes":[]},{"propositions":[],"lastnames":["Eberhard"],"firstnames":["Dirk"],"suffixes":[]},{"propositions":[],"lastnames":["Molina"],"firstnames":["Daniel","Martinez"],"suffixes":[]},{"propositions":[],"lastnames":["Jafari"],"firstnames":["Rozbeh"],"suffixes":[]},{"propositions":[],"lastnames":["Dovega"],"firstnames":["Rebecca","Bakszt"],"suffixes":[]},{"propositions":[],"lastnames":["Klaeger"],"firstnames":["Susan"],"suffixes":[]},{"propositions":[],"lastnames":["Kuster"],"firstnames":["Bernhard"],"suffixes":[]},{"propositions":[],"lastnames":["Nordlund"],"firstnames":["Pär"],"suffixes":[]},{"propositions":[],"lastnames":["Bantscheff"],"firstnames":["Marcus"],"suffixes":[]},{"propositions":[],"lastnames":["Drewes"],"firstnames":["Gerard"],"suffixes":[]}],"month":"October","year":"2014","note":"Publisher: American Association for the Advancement of Science","pages":"1255784","bibtex":"@article{savitski_tracking_2014,\n\ttitle = {Tracking cancer drugs in living cells by thermal profiling of the proteome},\n\tvolume = {346},\n\turl = {https://www-science-org.ezp-prod1.hul.harvard.edu/doi/full/10.1126/science.1255784},\n\tdoi = {10.1126/science.1255784},\n\tabstract = {The thermal stability of proteins can be used to assess ligand binding in living cells. We have generalized this concept by determining the thermal profiles of more than 7000 proteins in human cells by means of mass spectrometry. Monitoring the effects of small-molecule ligands on the profiles delineated more than 50 targets for the kinase inhibitor staurosporine. We identified the heme biosynthesis enzyme ferrochelatase as a target of kinase inhibitors and suggest that its inhibition causes the phototoxicity observed with vemurafenib and alectinib. Thermal shifts were also observed for downstream effectors of drug treatment. In live cells, dasatinib induced shifts in BCR-ABL pathway proteins, including CRK/CRKL. Thermal proteome profiling provides an unbiased measure of drug-target engagement and facilitates identification of markers for drug efficacy and toxicity.},\n\tnumber = {6205},\n\turldate = {2023-11-29},\n\tjournal = {Science},\n\tauthor = {Savitski, Mikhail M. and Reinhard, Friedrich B. 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