{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Borchers J"],"funding":["Studienstiftung des Deutschen Volkes","Deutsche Forschungsgemeinschaft","Universitätsklinikum Würzburg"],"pagination":["367-386"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12858599"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["100(1)"],"pubmed_abstract":["Ochratoxin A (OTA), a mycotoxin commonly found as a contaminant in a variety of foods, is known for its ability to cause kidney damage and tumors in rodents. Recent research indicates that replicative stress leading to aberrant mitoses and subsequent genetic instability may play a key role in OTA carcinogenicity. However, the specific molecular targets of OTA and early key events leading to replicative stress and mitotic disruption remain to be determined. In this study, a chemoproteomic workflow was employed to identify proteins that directly interact with OTA and its non-chlorinated analog ochratoxin B (OTB). To this end, OTA and OTB were immobilized on a stationary phase through covalent coupling to amine-functionalized agarose beads via their carboxy group. OTA-and OTB-functionalized b"],"journal":["Archives of toxicology"],"pubmed_title":["Identification of small GTPases as potential target proteins of the mycotoxin and renal carcinogen ochratoxin A."],"pmcid":["PMC12858599"],"funding_grant_id":["462675411"],"pubmed_authors":["Borchers J","Perugino F","Pedroni L","Schlosser A","Lamer S","Dellafiora L","Lutz L","Mally A"],"additional_accession":[]},"is_claimable":false,"name":"Identification of small GTPases as potential target proteins of the mycotoxin and renal carcinogen ochratoxin A.","description":"Ochratoxin A (OTA), a mycotoxin commonly found as a contaminant in a variety of foods, is known for its ability to cause kidney damage and tumors in rodents. Recent research indicates that replicative stress leading to aberrant mitoses and subsequent genetic instability may play a key role in OTA carcinogenicity. However, the specific molecular targets of OTA and early key events leading to replicative stress and mitotic disruption remain to be determined. In this study, a chemoproteomic workflow was employed to identify proteins that directly interact with OTA and its non-chlorinated analog ochratoxin B (OTB). To this end, OTA and OTB were immobilized on a stationary phase through covalent coupling to amine-functionalized agarose beads via their carboxy group. OTA-and OTB-functionalized b","dates":{"release":"2026-01-01T00:00:00Z","publication":"2026 Jan","modification":"2026-06-14T06:09:29.447Z","creation":"2026-06-14T03:15:21.139Z"},"accession":"S-EPMC12858599","cross_references":{"pubmed":["40952447"],"doi":["10.1007/s00204-025-04189-8"]}}