{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Cupp-Sutton KA"],"funding":["NIH NIAID","NIAID NIH HHS","Oklahoma Center for the Advancement of Science and Technology","NCI NIH HHS"],"pagination":["e5187"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12649780"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["60(11)"],"pubmed_abstract":["Protein function can vary due to changes in primary structure, such as post-translational modification (PTM), truncation, or amino acid replacement, and functional proteomics methods focus on elucidating changes in the function of proteins in biological pathways. Thermal proteome profiling (TPP) is a powerful functional proteomics approach that analyzes the thermal stability of proteins by exposing them to a temperature gradient to facilitate thermal denaturation, followed by analysis of the remaining folded proteins. Current TPP methods, however, utilize bottom-up methods that require protein digestion and can obscure relevant information regarding the structure of the intact proteoform. In this study, we have developed a top-down (TD) TPP approach to study intact proteoform stability as "],"journal":["Journal of mass spectrometry : JMS"],"pubmed_title":["Top-Down Thermal Proteome Profiling (TD-TPP) for Functional Characterization of the Intact Proteoforms in Complex Samples."],"pmcid":["PMC12649780"],"funding_grant_id":["R01AI141625","R01 AI141625","U19 AI062629","HR23-169","R61 CA297964","2U19AI062629"],"pubmed_authors":["Cupp-Sutton KA","Guo Y","Wu S","Welborn T"],"additional_accession":[]},"is_claimable":false,"name":"Top-Down Thermal Proteome Profiling (TD-TPP) for Functional Characterization of the Intact Proteoforms in Complex Samples.","description":"Protein function can vary due to changes in primary structure, such as post-translational modification (PTM), truncation, or amino acid replacement, and functional proteomics methods focus on elucidating changes in the function of proteins in biological pathways. Thermal proteome profiling (TPP) is a powerful functional proteomics approach that analyzes the thermal stability of proteins by exposing them to a temperature gradient to facilitate thermal denaturation, followed by analysis of the remaining folded proteins. Current TPP methods, however, utilize bottom-up methods that require protein digestion and can obscure relevant information regarding the structure of the intact proteoform. In this study, we have developed a top-down (TD) TPP approach to study intact proteoform stability as ","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Nov","modification":"2026-06-05T18:46:46.813Z","creation":"2026-05-20T03:13:33.195Z"},"accession":"S-EPMC12649780","cross_references":{"pubmed":["41069150"],"doi":["10.1002/jms.5187"]}}