DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu The extracellular chaperone clusterin sequesters oligomeric forms of the amyloid-β(1-40) peptide. The extracellular chaperone clusterin sequesters oligomeric forms of the amyloid-β(1-40) peptide. Nature structural & molecular biology 2011 imex curation Narayan P., Orte A., Clarke RW., Bolognesi B., Hook S., Ganzinger KA., Meehan S., Wilson MR., Dobson CM., Klenerman D., Narayan P., Orte A., Clarke RW., Bolognesi B., Hook S., Ganzinger KA., Meehan S., Wilson MR., Dobson CM., Klenerman D. Alzheimers - Interactions investigated in the context of Alzheimers disease Only protein-protein interactions in vitro In vitro confocal microscopy confocal microscopy predetermined predetermined participant predetermined Narayan P., Orte A., Clarke RW., Bolognesi B., Hook S., Ganzinger KA., Meehan S., Wilson MR., Dobson CM., Klenerman D. Alzheimers - Interactions investigated in the context of Alzheimers disease DIP original experiment: DIP-255382X Nature structural & molecular biology 2011 IMEx The extracellular chaperone clusterin sequesters oligomeric forms of the amyloid-β(1-40) peptide. The extracellular chaperone clusterin sequesters oligomeric forms of the amyloid-β(1-40) peptide. The extracellular chaperone clusterin sequesters oligomeric forms of the amyloid-β(1-40) peptide. Nature structural & molecular biology 2011 imex curation Narayan P., Orte A., Clarke RW., Bolognesi B., Hook S., Ganzinger KA., Meehan S., Wilson MR., Dobson CM., Klenerman D., Narayan P., Orte A., Clarke RW., Bolognesi B., Hook S., Ganzinger KA., Meehan S., Wilson MR., Dobson CM., Klenerman D. Alzheimers - Interactions investigated in the context of Alzheimers disease Only protein-protein interactions in vitro In vitro confocal microscopy confocal microscopy predetermined predetermined participant predetermined Narayan P., Orte A., Clarke RW., Bolognesi B., Hook S., Ganzinger KA., Meehan S., Wilson MR., Dobson CM., Klenerman D. Alzheimers - Interactions investigated in the context of Alzheimers disease DIP original experiment: DIP-255386X Nature structural & molecular biology 2011 IMEx The extracellular chaperone clusterin sequesters oligomeric forms of the amyloid-β(1-40) peptide. The extracellular chaperone clusterin sequesters oligomeric forms of the amyloid-β(1-40) peptide. The extracellular chaperone clusterin sequesters oligomeric forms of the amyloid-β(1-40) peptide. Nature structural & molecular biology 2011 imex curation Narayan P., Orte A., Clarke RW., Bolognesi B., Hook S., Ganzinger KA., Meehan S., Wilson MR., Dobson CM., Klenerman D., Narayan P., Orte A., Clarke RW., Bolognesi B., Hook S., Ganzinger KA., Meehan S., Wilson MR., Dobson CM., Klenerman D. 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 Narayan P., Orte A., Clarke RW., Bolognesi B., Hook S., Ganzinger KA., Meehan S., Wilson MR., Dobson CM., Klenerman D. Alzheimers - Interactions investigated in the context of Alzheimers disease DIP original experiment: DIP-255378X Nature structural & molecular biology 2011 IMEx The extracellular chaperone clusterin sequesters oligomeric forms of the amyloid-β(1-40) peptide. The extracellular chaperone clusterin sequesters oligomeric forms of the amyloid-β(1-40) peptide. The extracellular chaperone clusterin sequesters oligomeric forms of the amyloid-β(1-40) peptide. Nature structural & molecular biology 2011 imex curation Narayan P., Orte A., Clarke RW., Bolognesi B., Hook S., Ganzinger KA., Meehan S., Wilson MR., Dobson CM., Klenerman D., Narayan P., Orte A., Clarke RW., Bolognesi B., Hook S., Ganzinger KA., Meehan S., Wilson MR., Dobson CM., Klenerman D. Alzheimers - Interactions investigated in the context of Alzheimers disease Only protein-protein interactions in vitro In vitro aggregation aggregation assay aggregation predetermined predetermined participant predetermined Narayan P., Orte A., Clarke RW., Bolognesi B., Hook S., Ganzinger KA., Meehan S., Wilson MR., Dobson CM., Klenerman D. Alzheimers - Interactions investigated in the context of Alzheimers disease DIP original experiment: DIP-255380X Nature structural & molecular biology 2011 IMEx The extracellular chaperone clusterin sequesters oligomeric forms of the amyloid-β(1-40) peptide. The extracellular chaperone clusterin sequesters oligomeric forms of the amyloid-β(1-40) peptide. The extracellular chaperone clusterin sequesters oligomeric forms of the amyloid-β(1-40) peptide. Nature structural & molecular biology 2011 imex curation Narayan P., Orte A., Clarke RW., Bolognesi B., Hook S., Ganzinger KA., Meehan S., Wilson MR., Dobson CM., Klenerman D., Narayan P., Orte A., Clarke RW., Bolognesi B., Hook S., Ganzinger KA., Meehan S., Wilson MR., Dobson CM., Klenerman D. Alzheimers - Interactions investigated in the context of Alzheimers disease Only protein-protein interactions in vitro In vitro fluorescence imaging fluorescence microscopy fluorescence imaging predetermined predetermined participant predetermined Narayan P., Orte A., Clarke RW., Bolognesi B., Hook S., Ganzinger KA., Meehan S., Wilson MR., Dobson CM., Klenerman D. Alzheimers - Interactions investigated in the context of Alzheimers disease DIP original experiment: DIP-255384X Nature structural & molecular biology 2011 IMEx The extracellular chaperone clusterin sequesters oligomeric forms of the amyloid-β(1-40) peptide. The extracellular chaperone clusterin sequesters oligomeric forms of the amyloid-β(1-40) peptide. The extracellular chaperone clusterin sequesters oligomeric forms of the amyloid-β(1-40) peptide. Nature structural & molecular biology 2011 imex curation Narayan P., Orte A., Clarke RW., Bolognesi B., Hook S., Ganzinger KA., Meehan S., Wilson MR., Dobson CM., Klenerman D., Narayan P., Orte A., Clarke RW., Bolognesi B., Hook S., Ganzinger KA., Meehan S., Wilson MR., Dobson CM., Klenerman D. Alzheimers - Interactions investigated in the context of Alzheimers disease Only protein-protein interactions in vitro In vitro fluorescence imaging fluorescence microscopy fluorescence imaging predetermined predetermined participant predetermined Narayan P., Orte A., Clarke RW., Bolognesi B., Hook S., Ganzinger KA., Meehan S., Wilson MR., Dobson CM., Klenerman D. Alzheimers - Interactions investigated in the context of Alzheimers disease DIP original experiment: DIP-255385X Nature structural & molecular biology 2011 IMEx The extracellular chaperone clusterin sequesters oligomeric forms of the amyloid-β(1-40) peptide. The extracellular chaperone clusterin sequesters oligomeric forms of the amyloid-β(1-40) peptide. The extracellular chaperone clusterin sequesters oligomeric forms of the amyloid-β(1-40) peptide. Nature structural & molecular biology 2011 imex curation Narayan P., Orte A., Clarke RW., Bolognesi B., Hook S., Ganzinger KA., Meehan S., Wilson MR., Dobson CM., Klenerman D., Narayan P., Orte A., Clarke RW., Bolognesi B., Hook S., Ganzinger KA., Meehan S., Wilson MR., Dobson CM., Klenerman D. Alzheimers - Interactions investigated in the context of Alzheimers disease Only protein-protein interactions in vitro In vitro confocal microscopy confocal microscopy predetermined predetermined participant predetermined Narayan P., Orte A., Clarke RW., Bolognesi B., Hook S., Ganzinger KA., Meehan S., Wilson MR., Dobson CM., Klenerman D. Alzheimers - Interactions investigated in the context of Alzheimers disease DIP original experiment: DIP-255381X Nature structural & molecular biology 2011 IMEx The extracellular chaperone clusterin sequesters oligomeric forms of the amyloid-β(1-40) peptide. The extracellular chaperone clusterin sequesters oligomeric forms of the amyloid-β(1-40) peptide. The extracellular chaperone clusterin sequesters oligomeric forms of the amyloid-β(1-40) peptide. Nature structural & molecular biology 2011 imex curation Narayan P., Orte A., Clarke RW., Bolognesi B., Hook S., Ganzinger KA., Meehan S., Wilson MR., Dobson CM., Klenerman D., Narayan P., Orte A., Clarke RW., Bolognesi B., Hook S., Ganzinger KA., Meehan S., Wilson MR., Dobson CM., Klenerman D. 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 Narayan P., Orte A., Clarke RW., Bolognesi B., Hook S., Ganzinger KA., Meehan S., Wilson MR., Dobson CM., Klenerman D. Alzheimers - Interactions investigated in the context of Alzheimers disease DIP original experiment: DIP-255379X Nature structural & molecular biology 2011 IMEx The extracellular chaperone clusterin sequesters oligomeric forms of the amyloid-β(1-40) peptide. The extracellular chaperone clusterin sequesters oligomeric forms of the amyloid-β(1-40) peptide. The extracellular chaperone clusterin sequesters oligomeric forms of the amyloid-β(1-40) peptide. Nature structural & molecular biology 2011 imex curation Narayan P., Orte A., Clarke RW., Bolognesi B., Hook S., Ganzinger KA., Meehan S., Wilson MR., Dobson CM., Klenerman D., Narayan P., Orte A., Clarke RW., Bolognesi B., Hook S., Ganzinger KA., Meehan S., Wilson MR., Dobson CM., Klenerman D. Alzheimers - Interactions investigated in the context of Alzheimers disease Only protein-protein interactions in vitro In vitro fluorescence imaging fluorescence microscopy fluorescence imaging predetermined predetermined participant predetermined Narayan P., Orte A., Clarke RW., Bolognesi B., Hook S., Ganzinger KA., Meehan S., Wilson MR., Dobson CM., Klenerman D. Alzheimers - Interactions investigated in the context of Alzheimers disease DIP original experiment: DIP-255383X Nature structural & molecular biology 2011 IMEx The extracellular chaperone clusterin sequesters oligomeric forms of the amyloid-β(1-40) peptide. 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 clus_human Clusterin CLU APOJ CLI KUB1 Complement-associated protein SP-40,40 Complement cytolysis inhibitor NA1/NA2 Apolipoprotein J Testosterone-repressed prostate message 2 Ku70-binding protein 1 Aging-associated gene 4 protein AAG4 Sulfated glycoprotein 2 protein protein human Homo sapiens Human MMKTLLLFVGLLLTWESGQVLGDQTVSDNELQEMSNQGSKYVNKEIQNAVNGVKQIKTLIEKTNEERKTLLSNLEEAKKKKEDALNETRESETKLKELPGVCNETMMALWEECKPCLKQTCMKFYARVCRSGSGLVGRQLEEFLNQSSPFYFWMNGDRIDSLLENDRQQTHMLDVMQDHFSRASSIIDELFQDRFFTREPQDTYHYLPFSLPHRRPHFFFPKSRIVRSLMPFSPYEPLNFHAMFQPFLEMIHEAQQAMDIHFHSPAFQHPPTEFIREGDDDRTVCREIRHNSTGCLRMKDQCDKCREILSVDCSTNNPSQAKLRRELDESLQVAERLTRKYNELLKSYQWKMLNTSSLLEQLNEQFNWVSRLANLTQGEDQYYLRVTTVASHTSDSDVPSGVTEVVVKLFDSDPITVTVPVEVSRKNPKFMETVAEKALQEYRKKHREE DIP protein P10909 original sequence version: 151 9583DE4CCECC169F app-app-76 3 10 unspecified role unspecified role unspecified role unspecified role chemical synthesis Chemical synthesis (Chemical synthesis) 10 unspecified role unspecified role unspecified role unspecified role chemical synthesis Chemical synthesis (Chemical synthesis) direct interaction direct interaction app-clu-1 6 11 unspecified role unspecified role unspecified role unspecified role Alexa647-label Alexa647-label alexa label alexa label undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined human Homo sapiens Human 10 unspecified role unspecified role unspecified role unspecified role HiLyteFluor488-label HiLyteFluor488-label hilyte 488 hilyte fluor 488 hilyte 488 undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined [EBI-15960339]N-terminal positions must always be 1. Actual positions : 0-0 [EBI-15960339]0-0 in vitro In vitro direct interaction direct interaction app-app-77 8 10 unspecified role unspecified role unspecified role unspecified role in vitro In vitro 10 unspecified role unspecified role unspecified role unspecified role in vitro In vitro direct interaction direct interaction app-app-78 1 10 unspecified role unspecified role unspecified role unspecified role HiLyteFluor647-label HiLyteFluor647-label fluorescent dye fluorescent dye label fluorescent dye undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined [EBI-20763966]N-terminal positions must always be 1. Actual positions : 0-0 [EBI-20763966]0-0 chemical synthesis Chemical synthesis (Chemical synthesis) 10 unspecified role unspecified role unspecified role unspecified role HiLyteFluor647-label HiLyteFluor647-label fluorescent dye fluorescent dye label fluorescent dye undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined [EBI-15960376]N-terminal positions must always be 1. Actual positions : 0-0 [EBI-15960376]0-0 chemical synthesis Chemical synthesis (Chemical synthesis) direct interaction direct interaction app-app-79 9 10 unspecified role unspecified role unspecified role unspecified role HiLyteFluor488-label HiLyteFluor488-label hilyte 488 hilyte fluor 488 hilyte 488 undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined [EBI-20763979]N-terminal positions must always be 1. Actual positions : 0-0 [EBI-20763979]0-0 chemical synthesis Chemical synthesis (Chemical synthesis) 10 unspecified role unspecified role unspecified role unspecified role HiLyteFluor488-label HiLyteFluor488-label hilyte 488 hilyte fluor 488 hilyte 488 undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined [EBI-15960394]N-terminal positions must always be 1. Actual positions : 0-0 [EBI-15960394]0-0 chemical synthesis Chemical synthesis (Chemical synthesis) direct interaction direct interaction app-clu-2 4 11 unspecified role unspecified role unspecified role unspecified role human Homo sapiens Human 10 unspecified role unspecified role unspecified role unspecified role chemical synthesis Chemical synthesis (Chemical synthesis) direct interaction direct interaction app-clu-3 2 11 unspecified role unspecified role unspecified role unspecified role Alexa647-label Alexa647-label alexa label alexa label undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined human Homo sapiens Human 10 unspecified role unspecified role unspecified role unspecified role HiLyteFluor488-label HiLyteFluor488-label hilyte 488 hilyte fluor 488 hilyte 488 undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined [EBI-15960429]N-terminal positions must always be 1. Actual positions : 0-0 [EBI-15960429]0-0 chemical synthesis Chemical synthesis (Chemical synthesis) direct interaction direct interaction app-app-80 7 10 unspecified role unspecified role unspecified role unspecified role HiLyteFluor488-label HiLyteFluor488-label hilyte 488 hilyte fluor 488 hilyte 488 undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined [EBI-20763982]N-terminal positions must always be 1. Actual positions : 0-0 [EBI-20763982]0-0 chemical synthesis Chemical synthesis (Chemical synthesis) 10 unspecified role unspecified role unspecified role unspecified role HiLyteFluor488-label HiLyteFluor488-label hilyte 488 hilyte fluor 488 hilyte 488 undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined [EBI-15960450]N-terminal positions must always be 1. Actual positions : 0-0 [EBI-15960450]0-0 chemical synthesis Chemical synthesis (Chemical synthesis) direct interaction direct interaction app-app-81 5 10 unspecified role unspecified role unspecified role unspecified role HiLyteFluor647-label HiLyteFluor647-label fluorescent dye fluorescent dye label fluorescent dye undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined [EBI-20763985]N-terminal positions must always be 1. Actual positions : 0-0 [EBI-20763985]0-0 chemical synthesis Chemical synthesis (Chemical synthesis) 10 unspecified role unspecified role unspecified role unspecified role HiLyteFluor647-label HiLyteFluor647-label fluorescent dye fluorescent dye label fluorescent dye undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined [EBI-15960468]N-terminal positions must always be 1. Actual positions : 0-0 [EBI-15960468]0-0 chemical synthesis Chemical synthesis (Chemical synthesis) direct interaction direct interaction