{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Hoogerbrugge G"],"funding":["US Army Research Office","Welch Foundation","National Institutes of Health","National Institute of General Medical Sciences"],"pagination":["101484"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12828403"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["25(1)"],"pubmed_abstract":["Large macromolecular assemblies are integral to most cellular processes, making their identification and structural characterization an important strategy for advancing our understanding of protein functions. In this pilot study, we investigated large multiprotein assemblies from the cytoplasm of the slime mold Dictyostelium discoideum using shotgun electron microscopy, the combined application of mass spectrometry-based proteomics and cryo-EM to heterogenous mixtures of proteins. With its similarities in cell structure and behavior to mammalian cells, D. discoideum has long served as an invaluable model organism, particularly in the study of immune cell chemotaxis, phagocytosis, bacterial infection, and other processes. We subjected D. discoideum soluble protein complexes to two-step frac"],"journal":["Molecular & cellular proteomics : MCP"],"pubmed_title":["Serendipity and the Slime Mold: A Visual Survey of High-Molecular-Weight Protein Assemblies Reveals the Structure of the Polyketide Synthase Pks16."],"pmcid":["PMC12828403"],"funding_grant_id":["F-1515","R35 GM122480","F-2245","R01 GM106112","W911NF-12-1-0390"],"pubmed_authors":["Keatinge-Clay AT","Hoogerbrugge G","Marcotte EM"],"additional_accession":[]},"is_claimable":false,"name":"Serendipity and the Slime Mold: A Visual Survey of High-Molecular-Weight Protein Assemblies Reveals the Structure of the Polyketide Synthase Pks16.","description":"Large macromolecular assemblies are integral to most cellular processes, making their identification and structural characterization an important strategy for advancing our understanding of protein functions. In this pilot study, we investigated large multiprotein assemblies from the cytoplasm of the slime mold Dictyostelium discoideum using shotgun electron microscopy, the combined application of mass spectrometry-based proteomics and cryo-EM to heterogenous mixtures of proteins. With its similarities in cell structure and behavior to mammalian cells, D. discoideum has long served as an invaluable model organism, particularly in the study of immune cell chemotaxis, phagocytosis, bacterial infection, and other processes. We subjected D. discoideum soluble protein complexes to two-step frac","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Dec","modification":"2026-06-13T05:05:47.149Z","creation":"2026-06-13T03:09:15.884Z"},"accession":"S-EPMC12828403","cross_references":{"pubmed":["41380999"],"doi":["10.1016/j.mcpro.2025.101484"]}}