DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Experimental characterization of disordered and ordered aggregates populated during the process of amyloid fibril formation. Experimental characterization of disordered and ordered aggregates populated during the process of amyloid fibril formation. Proceedings of the National Academy of Sciences of the United States of America 2009 imex curation Carulla N., Zhou M., Arimon M., Gairí M., Giralt E., Robinson CV., Dobson CM. Only protein-protein interactions in vitro In vitro tem transmission electron microscopy tem predetermined predetermined participant predetermined Carulla N., Zhou M., Arimon M., Gairí M., Giralt E., Robinson CV., Dobson CM. DIP original experiment: DIP-134188X Proceedings of the National Academy of Sciences of the United States of America 2009 IMEx Experimental characterization of disordered and ordered aggregates populated during the process of amyloid fibril formation. Experimental characterization of disordered and ordered aggregates populated during the process of amyloid fibril formation. Experimental characterization of disordered and ordered aggregates populated during the process of amyloid fibril formation. Proceedings of the National Academy of Sciences of the United States of America 2009 imex curation Carulla N., Zhou M., Arimon M., Gairí M., Giralt E., Robinson CV., Dobson CM. Only protein-protein interactions in vitro In vitro h1-h2 ms mass spectrometry study of hydrogen/deuterium exchange h1-h2 ms predetermined predetermined participant predetermined Carulla N., Zhou M., Arimon M., Gairí M., Giralt E., Robinson CV., Dobson CM. DIP original experiment: DIP-134185X Proceedings of the National Academy of Sciences of the United States of America 2009 IMEx Experimental characterization of disordered and ordered aggregates populated during the process of amyloid fibril formation. Experimental characterization of disordered and ordered aggregates populated during the process of amyloid fibril formation. Experimental characterization of disordered and ordered aggregates populated during the process of amyloid fibril formation. Proceedings of the National Academy of Sciences of the United States of America 2009 imex curation Carulla N., Zhou M., Arimon M., Gairí M., Giralt E., Robinson CV., Dobson CM. Only protein-protein interactions in vitro In vitro atomic force microsc atomic force microscopy AFM AFM atomic force microsc predetermined predetermined participant predetermined Carulla N., Zhou M., Arimon M., Gairí M., Giralt E., Robinson CV., Dobson CM. DIP original experiment: DIP-134187X Proceedings of the National Academy of Sciences of the United States of America 2009 IMEx Experimental characterization of disordered and ordered aggregates populated during the process of amyloid fibril formation. Experimental characterization of disordered and ordered aggregates populated during the process of amyloid fibril formation. Experimental characterization of disordered and ordered aggregates populated during the process of amyloid fibril formation. Proceedings of the National Academy of Sciences of the United States of America 2009 imex curation Carulla N., Zhou M., Arimon M., Gairí M., Giralt E., Robinson CV., Dobson CM. Only protein-protein interactions in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Carulla N., Zhou M., Arimon M., Gairí M., Giralt E., Robinson CV., Dobson CM. DIP original experiment: DIP-134186X Proceedings of the National Academy of Sciences of the United States of America 2009 IMEx Experimental characterization of disordered and ordered aggregates populated during the process of amyloid fibril formation. p85a_bovin Phosphatidylinositol 3-kinase regulatory subunit alpha Phosphatidylinositol 3-kinase 85 kDa regulatory subunit alpha PIK3R1 protein protein bovin Bos taurus (Bovine) Bovine MSAEGYQYRALYDYKKEREEDIDLHLGDILTVNKGSLVALGFSDGQEAKPEEIGWLNGYNETTGERGDFPGTYVEYIGRKKISPPTPKPRPPRPLPVAPGPSKTEADSEQQASTLPDLAEQFAPPDVAPPLLIKLVEAIEKKGLECSTLYRTQSSSNPAELRQLLDCDTASLDLEMFDVHVLADAFKRYLLDLPNPVIPVAVSSELISLAPEVQSSEEYIQLLKKLIRSPSIPHQYWLTLQYLLKHFFKLSQTSSKNLLNARVLSELFSPLLFRFPAASSENTEHLIKIIEILISTEWNERQPAPALPPKPPKPTTVANNGMNNNMSLQDAEWYWGDISREEVNEKLRDTADGTFLVRDASTKMHGDYTLTLRKGGNNKLIKIFHRDGKYGFSDPLTFNSVVELINHYRNESLAQYNPKLDVKLLYPVSKYQQDQVVKEDNIEAVGKKLHEYNTQFQEKSREYDRLYEDYTRTSQEIQMKRTAIEAFNETIKIFEEQCQTQERYSKEYIEKFKREGNETEIQRIMHNYEKLKSRISEIVDSRRRLEEDLKKQAAEYREIDKRMNSIKPDLIQLRKTRDQYLMWLTQKGVRQKKLNEWLGNENTEDQYSLVEDDEDLPHHDEKTWNVGSSNRNKAENLLRGKRDGTFLVRESSKQGCYACSVVVDGEVKHCVINKTATGYGFAEPYNLYSSLKELVLHYQHTSLVQHNDSLNVTLAYPVYAQQRR DIP protein P23727 original sequence version: 108 EBDF6E754BBF7321 pik3r1-1 1 5 unspecified role unspecified role unspecified role unspecified role Region 1-84 Region 1-84 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction pik3r1-3 2 5 unspecified role unspecified role unspecified role unspecified role Region 1-84 Region 1-84 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction pik3r1-4 4 5 unspecified role unspecified role unspecified role unspecified role Region 1-84 Region 1-84 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction pik3r1-5 3 5 unspecified role unspecified role unspecified role unspecified role Region 1-84 Region 1-84 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction