DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Methionine oxidation induces amyloid fibril formation by full-length apolipoprotein A-I. Methionine oxidation induces amyloid fibril formation by full-length apolipoprotein A-I. Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Wong YQ., Binger KJ., Howlett GJ., Griffin MD. Only protein-protein interactions in vitro In vitro light microscopy light microscopy predetermined predetermined participant predetermined Wong YQ., Binger KJ., Howlett GJ., Griffin MD. DIP original experiment: DIP-215951X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx Methionine oxidation induces amyloid fibril formation by full-length apolipoprotein A-I. Methionine oxidation induces amyloid fibril formation by full-length apolipoprotein A-I. Methionine oxidation induces amyloid fibril formation by full-length apolipoprotein A-I. Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Wong YQ., Binger KJ., Howlett GJ., Griffin MD. Only protein-protein interactions in vitro In vitro x-ray fiber diffrac x-ray fiber diffraction X-ray X-ray x-ray fiber diffrac predetermined predetermined participant predetermined Wong YQ., Binger KJ., Howlett GJ., Griffin MD. DIP original experiment: DIP-215949X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx Methionine oxidation induces amyloid fibril formation by full-length apolipoprotein A-I. Methionine oxidation induces amyloid fibril formation by full-length apolipoprotein A-I. Methionine oxidation induces amyloid fibril formation by full-length apolipoprotein A-I. Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Wong YQ., Binger KJ., Howlett GJ., Griffin MD. Only protein-protein interactions in vitro In vitro solution sedimentati cosedimentation in solution solution sedimentati predetermined predetermined participant predetermined Wong YQ., Binger KJ., Howlett GJ., Griffin MD. DIP original experiment: DIP-215948X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx Methionine oxidation induces amyloid fibril formation by full-length apolipoprotein A-I. Methionine oxidation induces amyloid fibril formation by full-length apolipoprotein A-I. Methionine oxidation induces amyloid fibril formation by full-length apolipoprotein A-I. Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Wong YQ., Binger KJ., Howlett GJ., Griffin MD. Only protein-protein interactions in vitro In vitro fluorescence spectr classical fluorescence spectroscopy fluorescence spectr predetermined predetermined participant predetermined Wong YQ., Binger KJ., Howlett GJ., Griffin MD. DIP original experiment: DIP-215947X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx Methionine oxidation induces amyloid fibril formation by full-length apolipoprotein A-I. Methionine oxidation induces amyloid fibril formation by full-length apolipoprotein A-I. Methionine oxidation induces amyloid fibril formation by full-length apolipoprotein A-I. Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Wong YQ., Binger KJ., Howlett GJ., Griffin MD. Only protein-protein interactions in vitro In vitro tem transmission electron microscopy tem predetermined predetermined participant predetermined Wong YQ., Binger KJ., Howlett GJ., Griffin MD. DIP original experiment: DIP-215950X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx Methionine oxidation induces amyloid fibril formation by full-length apolipoprotein A-I. apoa1_human Apolipoprotein A-I APOA1 Apolipoprotein A1 protein protein human Homo sapiens Human MKAAVLTLAVLFLTGSQARHFWQQDEPPQSPWDRVKDLATVYVDVLKDSGRDYVSQFEGSALGKQLNLKLLDNWDSVTSTFSKLREQLGPVTQEFWDNLEKETEGLRQEMSKDLEEVKAKVQPYLDDFQKKWQEEMELYRQKVEPLRAELQEGARQKLHELQEKLSPLGEEMRDRARAHVDALRTHLAPYSDELRQRLAARLEALKENGGARLAEYHAKATEHLSTLSEKAKPALEDLRQGLLPVLESFKVSFLSALEEYTKKLNTQ DIP protein P02647 original sequence version: 116 DIP protein P02647 original sequence version: 125 DIP protein P02647 original sequence version: 147 DIP protein P02647 original sequence version: 162 1A28B8366E620310 apoa1-3 1 6 unspecified role unspecified role unspecified role unspecified role human Homo sapiens Human direct interaction direct interaction apoa1-4 4 6 unspecified role unspecified role unspecified role unspecified role human Homo sapiens Human direct interaction direct interaction apoa1-5 3 6 unspecified role unspecified role unspecified role unspecified role human Homo sapiens Human direct interaction direct interaction apoa1-6 2 6 unspecified role unspecified role unspecified role unspecified role human Homo sapiens Human direct interaction direct interaction apoa1-7 5 6 unspecified role unspecified role unspecified role unspecified role human Homo sapiens Human direct interaction direct interaction