{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Ivanisenko NV"],"funding":["Deutsche Forschungsgemeinschaft (DFG)","EC | European Regional Development Fund (ERDF)","Wilhelm Sander-Stiftung (Wilhelm Sander Foundation)","RWTH Aachen | Medizinische Fakultät, RWTH Aachen University (Faculty of Medicine, RWTH Aachen University)"],"pagination":["3231-3265"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12130296"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["44(11)"],"pubmed_abstract":["The necrosome is the key macromolecular signaling platform initiating necroptosis, i.e., a RIPK1/RIPK3-dependent program of cell death with an important role in the control of inflammation in multicellular organisms. However, the composition and structure of the necrosome remain incompletely understood. Here we use biochemical assays, quantitative mass spectrometry, and AlphaFold modeling to decipher the composition and derive a structural model of the CD95L/BV6-induced necrosome. We identify RIPK1 as the central component of the necrosome, forming the core of this complex. In addition, AlphaFold modeling provides insights into the structural mechanisms underlying RIPK1 oligomerization, highlighting the critical role of type-II interactions between the Death Domains (DDs) of FADD and RIPK1"],"journal":["The EMBO journal"],"pubmed_title":["Oligomerised RIPK1 is the main core component of the CD95 necrosome."],"pmcid":["PMC12130296"],"funding_grant_id":["START-Program,Az. 57/22","LA 2386","ALBB","2017.008.02"],"pubmed_authors":["Lavrik IN","Hillert-Richter LK","Konig C","Feoktistova MA","Panayotova-Dimitrova D","Ivanisenko NV","Richter M","Pietkiewicz S","Kaehne T"],"additional_accession":[]},"is_claimable":false,"name":"Oligomerised RIPK1 is the main core component of the CD95 necrosome.","description":"The necrosome is the key macromolecular signaling platform initiating necroptosis, i.e., a RIPK1/RIPK3-dependent program of cell death with an important role in the control of inflammation in multicellular organisms. However, the composition and structure of the necrosome remain incompletely understood. Here we use biochemical assays, quantitative mass spectrometry, and AlphaFold modeling to decipher the composition and derive a structural model of the CD95L/BV6-induced necrosome. We identify RIPK1 as the central component of the necrosome, forming the core of this complex. In addition, AlphaFold modeling provides insights into the structural mechanisms underlying RIPK1 oligomerization, highlighting the critical role of type-II interactions between the Death Domains (DDs) of FADD and RIPK1","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Jun","modification":"2026-06-01T11:32:05.921Z","creation":"2026-04-08T11:55:02.253Z"},"accession":"S-EPMC12130296","cross_references":{"pubmed":["40240880"],"doi":["10.1038/s44318-025-00433-0"]}}