{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["23(10)"],"submitter":["Lenz T"],"pubmed_abstract":["Chemical biology and the application of small molecules has proven to be a potent perturbation strategy, especially for the functional elucidation of proteins, their networks, and regulators. In recent years, the cellular thermal shift assay (CETSA) and its proteome-wide extension, thermal proteome profiling (TPP), have proven to be effective tools for identifying interactions of small molecules with their target proteins, as well as off-targets in living cells. Here, we asked the question whether isothermal dose-response (ITDR) CETSA can be exploited to characterize secondary effects downstream of the primary binding event, such as changes in post-translational modifications or protein-protein interactions (PPI). By applying ITDR-CETSA to MAPK14 kinase inhibitor treatment of living HL-60 "],"journal":["International journal of molecular sciences"],"pagination":["5605"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9147192"],"repository":["biostudies-literature"],"pubmed_title":["<u>S</u>mall <u>M</u>olecule <u>Ar</u>ranged <u>T</u>hermal <u>P</u>roximity <u>C</u>o<u>a</u>ggregation (smarTPCA)-A Novel Approach to Characterize Protein-Protein Interactions in Living Cells by Similar Isothermal Dose-Responses."],"pmcid":["PMC9147192"],"pubmed_authors":["Lenz T","Stuhler K"],"additional_accession":[]},"is_claimable":false,"name":"<u>S</u>mall <u>M</u>olecule <u>Ar</u>ranged <u>T</u>hermal <u>P</u>roximity <u>C</u>o<u>a</u>ggregation (smarTPCA)-A Novel Approach to Characterize Protein-Protein Interactions in Living Cells by Similar Isothermal Dose-Responses.","description":"Chemical biology and the application of small molecules has proven to be a potent perturbation strategy, especially for the functional elucidation of proteins, their networks, and regulators. In recent years, the cellular thermal shift assay (CETSA) and its proteome-wide extension, thermal proteome profiling (TPP), have proven to be effective tools for identifying interactions of small molecules with their target proteins, as well as off-targets in living cells. Here, we asked the question whether isothermal dose-response (ITDR) CETSA can be exploited to characterize secondary effects downstream of the primary binding event, such as changes in post-translational modifications or protein-protein interactions (PPI). By applying ITDR-CETSA to MAPK14 kinase inhibitor treatment of living HL-60 ","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 May","modification":"2026-04-08T09:42:05.026Z","creation":"2024-11-06T15:41:56.301Z"},"accession":"S-EPMC9147192","cross_references":{"pubmed":["35628420"],"doi":["10.3390/ijms23105605"]}}