{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Lomize AL"],"funding":["Division of Biological Infrastructure","National Science Foundation of Sri Lanka"],"pagination":["e4318"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9047035"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["31(5)"],"pubmed_abstract":["The Membranome database provides comprehensive structural information on single-pass (i.e., bitopic) membrane proteins from six evolutionarily distant organisms, including protein-protein interactions, complexes, mutations, experimental structures, and models of transmembrane α-helical dimers. We present a new version of this database, Membranome 3.0, which was significantly updated by revising the set of 5,758 bitopic proteins and incorporating models generated by AlphaFold 2 in the database. The AlphaFold models were parsed into structural domains located at the different membrane sides, modified to exclude low-confidence unstructured terminal regions and signal sequences, validated through comparison with available experimental structures, and positioned with respect to membrane boundar"],"journal":["Protein science : a publication of the Protein Society"],"pubmed_title":["Membranome 3.0: Database of single-pass membrane proteins with AlphaFold models."],"pmcid":["PMC9047035"],"funding_grant_id":["1855425"],"pubmed_authors":["Todd SC","Outeiral C","Pogozheva ID","Deane CM","Cherepanov S","Schnitzer KA","Lomize AL"],"additional_accession":[]},"is_claimable":false,"name":"Membranome 3.0: Database of single-pass membrane proteins with AlphaFold models.","description":"The Membranome database provides comprehensive structural information on single-pass (i.e., bitopic) membrane proteins from six evolutionarily distant organisms, including protein-protein interactions, complexes, mutations, experimental structures, and models of transmembrane α-helical dimers. We present a new version of this database, Membranome 3.0, which was significantly updated by revising the set of 5,758 bitopic proteins and incorporating models generated by AlphaFold 2 in the database. The AlphaFold models were parsed into structural domains located at the different membrane sides, modified to exclude low-confidence unstructured terminal regions and signal sequences, validated through comparison with available experimental structures, and positioned with respect to membrane boundar","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 May","modification":"2025-04-04T21:33:15.698Z","creation":"2025-04-04T21:33:15.698Z"},"accession":"S-EPMC9047035","cross_references":{"pubmed":["35481632"],"doi":["10.1002/pro.4318"]}}