{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Hakhverdyan Z"],"funding":["Novo Nordisk Fonden","NIGMS NIH HHS"],"pagination":["553-60"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4449307"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["12(6)"],"pubmed_abstract":["We must reliably map the interactomes of cellular macromolecular complexes in order to fully explore and understand biological systems. However, there are no methods to accurately predict how to capture a given macromolecular complex with its physiological binding partners. Here, we present a screening method that comprehensively explores the parameters affecting the stability of interactions in affinity-captured complexes, enabling the discovery of physiological binding partners in unparalleled detail. We have implemented this screen on several macromolecular complexes from a variety of organisms, revealing novel profiles for even well-studied proteins. Our approach is robust, economical and automatable, providing inroads to the rigorous, systematic dissection of cellular interactomes."],"journal":["Nature methods"],"pubmed_title":["Rapid, optimized interactomic screening."],"pmcid":["PMC4449307"],"funding_grant_id":["P50 GM076547","U54 GM103511","P41 GM103314","NNF12OC0001211","P41 GM109824"],"pubmed_authors":["Hough LE","Jensen TH","Dilworth DJ","Oroskar AR","Domanski M","Rout MP","Molloy KR","Hakhverdyan Z","LaCava J","Chait BT","Sherman V","Aitchison JD","Keegan S","Fenyo D","Oroskar AA"],"additional_accession":[]},"is_claimable":false,"name":"Rapid, optimized interactomic screening.","description":"We must reliably map the interactomes of cellular macromolecular complexes in order to fully explore and understand biological systems. However, there are no methods to accurately predict how to capture a given macromolecular complex with its physiological binding partners. Here, we present a screening method that comprehensively explores the parameters affecting the stability of interactions in affinity-captured complexes, enabling the discovery of physiological binding partners in unparalleled detail. We have implemented this screen on several macromolecular complexes from a variety of organisms, revealing novel profiles for even well-studied proteins. Our approach is robust, economical and automatable, providing inroads to the rigorous, systematic dissection of cellular interactomes.","dates":{"release":"2015-01-01T00:00:00Z","publication":"2015 Jun","modification":"2025-04-18T16:38:44.617Z","creation":"2019-03-27T01:52:26Z"},"accession":"S-EPMC4449307","cross_references":{"pubmed":["25938370"],"doi":["10.1038/nmeth.3395"]}}