{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Hawley SA"],"funding":["Wellcome Trust"],"pagination":["453"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10778976"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["25(1)"],"pubmed_abstract":["AMP-activated protein kinase (AMPK) is the central component of a signalling pathway that senses energy stress and triggers a metabolic switch away from anabolic processes and towards catabolic processes. There has been a prolonged focus in the pharmaceutical industry on the development of AMPK-activating drugs for the treatment of metabolic disorders such as Type 2 diabetes and non-alcoholic fatty liver disease. However, recent findings suggest that AMPK inhibitors might be efficacious for treating certain cancers, especially lung adenocarcinomas, in which the <i>PRKAA1</i> gene (encoding the α1 catalytic subunit isoform of AMPK) is often amplified. Here, we study two potent AMPK inhibitors, BAY-3827 and SBI-0206965. Despite not being closely related structurally, the treatment of cells w"],"journal":["International journal of molecular sciences"],"pubmed_title":["BAY-3827 and SBI-0206965: Potent AMPK Inhibitors That Paradoxically Increase Thr172 Phosphorylation."],"pmcid":["PMC10778976"],"funding_grant_id":["204766"],"pubmed_authors":["Hawley SA","Russell FM","Ross FA","Hardie DG"],"additional_accession":[]},"is_claimable":false,"name":"BAY-3827 and SBI-0206965: Potent AMPK Inhibitors That Paradoxically Increase Thr172 Phosphorylation.","description":"AMP-activated protein kinase (AMPK) is the central component of a signalling pathway that senses energy stress and triggers a metabolic switch away from anabolic processes and towards catabolic processes. There has been a prolonged focus in the pharmaceutical industry on the development of AMPK-activating drugs for the treatment of metabolic disorders such as Type 2 diabetes and non-alcoholic fatty liver disease. However, recent findings suggest that AMPK inhibitors might be efficacious for treating certain cancers, especially lung adenocarcinomas, in which the <i>PRKAA1</i> gene (encoding the α1 catalytic subunit isoform of AMPK) is often amplified. Here, we study two potent AMPK inhibitors, BAY-3827 and SBI-0206965. Despite not being closely related structurally, the treatment of cells w","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Dec","modification":"2025-04-03T22:51:36.608Z","creation":"2024-12-04T08:31:47.548Z"},"accession":"S-EPMC10778976","cross_references":{"pubmed":["38203624"],"doi":["10.3390/ijms25010453"]}}