{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Nakamura T"],"funding":["Bundesministerium für Bildung und Forschung","Courant Forschungszentrum Geobiologie, Georg-August-Universität Göttingen","Deutsche Forschungsgemeinschaft","European Research Council","Horizon 2020 Framework Programme","Horizon 2020","BMBF Berlin","JSPS","Japan Society for the Promotion of Science"],"pagination":["100710"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10985226"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["4(3)"],"pubmed_abstract":["Ferroptosis, a regulated cell death hallmarked by unrestrained lipid peroxidation, plays a pivotal role in the pathophysiology of various diseases, making it a promising therapeutic target. Glutathione peroxidase 4 (GPX4) prevents ferroptosis by reducing (phospho)lipid hydroperoxides, yet evaluation of its actual activity has remained arduous. Here, we present a tangible method using affinity-purified GPX4 to capture a snapshot of its native activity. Next to measuring GPX4 activity, this improved method allows for the investigation of mutational GPX4 activity, exemplified by the GPX4<sup>U46C</sup> mutant lacking selenocysteine at its active site, as well as the evaluation of GPX4 inhibitors, such as RSL3, as a showcase. Furthermore, we apply this method to the second ferroptosis guardian"],"journal":["Cell reports methods"],"pubmed_title":["A tangible method to assess native ferroptosis suppressor activity."],"pmcid":["PMC10985226"],"funding_grant_id":["461507177","22H02278","471011418","GA 884754","18K08198","22KK0253","20KK0363","CO 291/10-1","461385412","01EJ2205B","TRR 353"],"pubmed_authors":["Mishima E","Nakagawa K","Ito J","Wahida A","Nakamura T","Mourao ASD","Conrad M"],"additional_accession":[]},"is_claimable":false,"name":"A tangible method to assess native ferroptosis suppressor activity.","description":"Ferroptosis, a regulated cell death hallmarked by unrestrained lipid peroxidation, plays a pivotal role in the pathophysiology of various diseases, making it a promising therapeutic target. Glutathione peroxidase 4 (GPX4) prevents ferroptosis by reducing (phospho)lipid hydroperoxides, yet evaluation of its actual activity has remained arduous. Here, we present a tangible method using affinity-purified GPX4 to capture a snapshot of its native activity. Next to measuring GPX4 activity, this improved method allows for the investigation of mutational GPX4 activity, exemplified by the GPX4<sup>U46C</sup> mutant lacking selenocysteine at its active site, as well as the evaluation of GPX4 inhibitors, such as RSL3, as a showcase. Furthermore, we apply this method to the second ferroptosis guardian","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Mar","modification":"2026-06-03T04:40:20.004Z","creation":"2024-12-04T06:18:56.762Z"},"accession":"S-EPMC10985226","cross_references":{"pubmed":["38401540"],"doi":["10.1016/j.crmeth.2024.100710"]}}