DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Mechanism of amyloid plaque formation suggests an intracellular basis of Abeta pathogenicity. Mechanism of amyloid plaque formation suggests an intracellular basis of Abeta pathogenicity. Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Friedrich RP., Tepper K., Rönicke R., Soom M., Westermann M., Reymann K., Kaether C., Fändrich M., Friedrich RP., Tepper K., Rönicke R., Soom M., Westermann M., Reymann K., Kaether C., Fändrich M. Alzheimers - Interactions investigated in the context of Alzheimers disease Only protein-protein interactions in vitro In vitro tem transmission electron microscopy tem predetermined predetermined participant predetermined Friedrich RP., Tepper K., Rönicke R., Soom M., Westermann M., Reymann K., Kaether C., Fändrich M. Alzheimers - Interactions investigated in the context of Alzheimers disease DIP original experiment: DIP-219205X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx Mechanism of amyloid plaque formation suggests an intracellular basis of Abeta pathogenicity. Mechanism of amyloid plaque formation suggests an intracellular basis of Abeta pathogenicity. Mechanism of amyloid plaque formation suggests an intracellular basis of Abeta pathogenicity. Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Friedrich RP., Tepper K., Rönicke R., Soom M., Westermann M., Reymann K., Kaether C., Fändrich M., Friedrich RP., Tepper K., Rönicke R., Soom M., Westermann M., Reymann K., Kaether C., Fändrich M. Alzheimers - Interactions investigated in the context of Alzheimers disease Only protein-protein interactions in vitro In vitro fluorescence spectr classical fluorescence spectroscopy fluorescence spectr predetermined predetermined participant predetermined Friedrich RP., Tepper K., Rönicke R., Soom M., Westermann M., Reymann K., Kaether C., Fändrich M. Alzheimers - Interactions investigated in the context of Alzheimers disease DIP original experiment: DIP-219204X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx Mechanism of amyloid plaque formation suggests an intracellular basis of Abeta pathogenicity. p05067-pro_0000000093 Amyloid-beta protein 40 APP A4 AD1 ABPP Alzheimer disease amyloid protein Cerebral vascular amyloid peptide PreA4 Protease nexin-II APPI Amyloid precursor protein Amyloid-beta A4 protein Alzheimer disease amyloid A4 protein homolog Amyloid-beta (A4) precursor protein protein protein human Homo sapiens Human DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV 672 711 D563D7858C3768F1 app-app-93 2 3 unspecified role unspecified role unspecified role unspecified role in vitro In vitro 3 unspecified role unspecified role unspecified role unspecified role in vitro In vitro direct interaction direct interaction app-app-94 1 3 unspecified role unspecified role unspecified role unspecified role in vitro In vitro 3 unspecified role unspecified role unspecified role unspecified role in vitro In vitro direct interaction direct interaction