IntAct European Bioinformatics Institute IntAct intact http://www.ebi.ac.uk/ http://www.ebi.ac.uk/intact/query/${ac} EBI-[0-9]+|IA:[0-9]+ INTerAction database (IntAct) provides an open source database and toolkit for the storage, presentation and analysis of molecular interactions. http://www.ebi.ac.uk/intact European Bioinformatics Institute; Wellcome Trust Genome Campus; Hinxton, Cambridge; CB10 1SD; United Kingdom http://www.ebi.ac.uk/intact/ Apolipoprotein A-I directly interacts with amyloid precursor protein and inhibits A beta aggregation and toxicity. Apolipoprotein A-I directly interacts with amyloid precursor protein and inhibits A beta aggregation and toxicity. Biochemistry (0006-2960) 2001 Koldamova RP., Lefterov IM., Lefterova MI., Lazo JS. Neurodegeneration - Publications depicting interactions involved in neurodegenerative diseases. Synapse - Interactions of proteins with an established role in the presynapse. Alzheimers - Interactions investigated in the context of Alzheimers disease Apoptosis - Interactions involving proteins with a function related to apoptosis Fig. 1B. lazo@pitt.edu A human liver library was screened. yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast 2 hybrid two hybrid 2H 2h Gal4 transcription regeneration two-hybrid yeast two hybrid 2-hybrid classical two hybrid classical two hybrid 2H two-hybrid 2-hybrid Gal4 transcription regeneration 2h yeast two hybrid Y2H Y-2H 2 hybrid predetermined predetermined participant predetermined Koldamova RP., Lefterov IM., Lefterova MI., Lazo JS. Synapse - Interactions of proteins with an established role in the presynapse. Fig. 1B. lazo@pitt.edu Annotation to indicate that this entry has been checked and accepted by a senior curator. A human liver library was screened. Biochemistry (0006-2960) 2001 Apolipoprotein A-I directly interacts with amyloid precursor protein and inhibits A beta aggregation and toxicity. Apolipoprotein A-I directly interacts with amyloid precursor protein and inhibits A beta aggregation and toxicity. Biochemistry (0006-2960) 2001 Koldamova RP., Lefterov IM., Lefterova MI., Lazo JS. Neurodegeneration - Publications depicting interactions involved in neurodegenerative diseases. Synapse - Interactions of proteins with an established role in the presynapse. Alzheimers - Interactions investigated in the context of Alzheimers disease Apoptosis - Interactions involving proteins with a function related to apoptosis Fig. 1B. lazo@pitt.edu A human liver library was screened. in vitro In vitro elisa enzyme linked immunosorbent assay ELISA ELISA elisa antibody detection identification by antibody antibody detection Koldamova RP., Lefterov IM., Lefterova MI., Lazo JS. Synapse - Interactions of proteins with an established role in the presynapse. Fig. 1B. lazo@pitt.edu Annotation to indicate that this entry has been checked and accepted by a senior curator. A human liver library was screened. Biochemistry (0006-2960) 2001 Apolipoprotein A-I directly interacts with amyloid precursor protein and inhibits A beta aggregation and toxicity. Apolipoprotein A-I directly interacts with amyloid precursor protein and inhibits A beta aggregation and toxicity. Biochemistry (0006-2960) 2001 Koldamova RP., Lefterov IM., Lefterova MI., Lazo JS. Neurodegeneration - Publications depicting interactions involved in neurodegenerative diseases. Synapse - Interactions of proteins with an established role in the presynapse. Alzheimers - Interactions investigated in the context of Alzheimers disease Apoptosis - Interactions involving proteins with a function related to apoptosis Fig. 1B. lazo@pitt.edu A human liver library was screened. yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast 2 hybrid two hybrid 2H 2h Gal4 transcription regeneration two-hybrid yeast two hybrid 2-hybrid classical two hybrid classical two hybrid 2H two-hybrid 2-hybrid Gal4 transcription regeneration 2h yeast two hybrid Y2H Y-2H 2 hybrid full dna sequence full identification by DNA sequencing full dna sequence Koldamova RP., Lefterov IM., Lefterova MI., Lazo JS. Synapse - Interactions of proteins with an established role in the presynapse. Fig. 1B. lazo@pitt.edu Annotation to indicate that this entry has been checked and accepted by a senior curator. A human liver library was screened. Biochemistry (0006-2960) 2001 Apolipoprotein A-I directly interacts with amyloid precursor protein and inhibits A beta aggregation and toxicity. Apolipoprotein A-I directly interacts with amyloid precursor protein and inhibits A beta aggregation and toxicity. Biochemistry (0006-2960) 2001 Koldamova RP., Lefterov IM., Lefterova MI., Lazo JS. Neurodegeneration - Publications depicting interactions involved in neurodegenerative diseases. Synapse - Interactions of proteins with an established role in the presynapse. Alzheimers - Interactions investigated in the context of Alzheimers disease Apoptosis - Interactions involving proteins with a function related to apoptosis Fig. 1B. lazo@pitt.edu A human liver library was screened. in vitro In vitro far western blotting far western blotting Affinity blotting Affinity blotting polyclonal western polyclonal antibody western blot polyclonal western Koldamova RP., Lefterov IM., Lefterova MI., Lazo JS. Synapse - Interactions of proteins with an established role in the presynapse. Fig. 1B. lazo@pitt.edu Annotation to indicate that this entry has been checked and accepted by a senior curator. A human liver library was screened. Biochemistry (0006-2960) 2001 Apolipoprotein A-I directly interacts with amyloid precursor protein and inhibits A beta aggregation and toxicity. Apolipoprotein A-I directly interacts with amyloid precursor protein and inhibits A beta aggregation and toxicity. Biochemistry (0006-2960) 2001 Koldamova RP., Lefterov IM., Lefterova MI., Lazo JS. Neurodegeneration - Publications depicting interactions involved in neurodegenerative diseases. Synapse - Interactions of proteins with an established role in the presynapse. Alzheimers - Interactions investigated in the context of Alzheimers disease Apoptosis - Interactions involving proteins with a function related to apoptosis Fig. 1B. lazo@pitt.edu A human liver library was screened. in vitro In vitro anti tag coip anti tag coimmunoprecipitation anti tag coip monoclonal western monoclonal antibody western blot monoclonal western Koldamova RP., Lefterov IM., Lefterova MI., Lazo JS. Synapse - Interactions of proteins with an established role in the presynapse. N-terminal anti-APP and anti-apoA-1 monoclonal antibodies were used. Fig. 1B. lazo@pitt.edu Annotation to indicate that this entry has been checked and accepted by a senior curator. A human liver library was screened. Biochemistry (0006-2960) 2001 a4_human Amyloid-beta precursor protein APP A4 AD1 Alzheimer disease amyloid protein ABPP PreA4 Cerebral vascular amyloid peptide 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 MLPGLALLLLAAWTARALEVPTDGNAGLLAEPQIAMFCGRLNMHMNVQNGKWDSDPSGTKTCIDTKEGILQYCQEVYPELQITNVVEANQPVTIQNWCKRGRKQCKTHPHFVIPYRCLVGEFVSDALLVPDKCKFLHQERMDVCETHLHWHTVAKETCSEKSTNLHDYGMLLPCGIDKFRGVEFVCCPLAEESDNVDSADAEEDDSDVWWGGADTDYADGSEDKVVEVAEEEEVAEVEEEEADDDEDDEDGDEVEEEAEEPYEEATERTTSIATTTTTTTESVEEVVREVCSEQAETGPCRAMISRWYFDVTEGKCAPFFYGGCGGNRNNFDTEEYCMAVCGSAMSQSLLKTTQEPLARDPVKLPTTAASTPDAVDKYLETPGDENEHAHFQKAKERLEAKHRERMSQVMREWEEAERQAKNLPKADKKAVIQHFQEKVESLEQEAANERQQLVETHMARVEAMLNDRRRLALENYITALQAVPPRPRHVFNMLKKYVRAEQKDRQHTLKHFEHVRMVDPKKAAQIRSQVMTHLRVIYERMNQSLSLLYNVPAVAEEIQDEVDELLQKEQNYSDDVLANMISEPRISYGNDALMPSLTETKTTVELLPVNGEFSLDDLQPWHSFGADSVPANTENEVEPVDARPAADRGLTTRPGSGLTNIKTEEISEVKMDAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIATVIVITLVMLKKKQYTSIHHGVVEVDAAVTPEERHLSKMQQNGYENPTYKFFEQMQN DIP protein P05067 original sequence version: 160 DIP protein P05067 original sequence version: 207 DIP protein P05067 original sequence version: 185 DIP protein P05067 original sequence version: 188 A12EE761403740F5 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 app-apoa1-1 3 6 unspecified role unspecified role bait bait yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast 7 unspecified role unspecified role prey prey yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast physical association physical association app-apoa1-2 1 6 unspecified role unspecified role prey prey ectodomain binding region binding-associated region binding region undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast 7 unspecified role unspecified role bait bait yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast physical association physical association The cytoplasmic tail of APP was not found to interact with apoA-1. Additionally the beta-gal activity was significantly higher for the APP ectodomain fragment interaction than for the full length APP interaction with apoA-1. Postulated that the transmembrane region and cytoplasmic tail of the full-length APP may impose some conformational hindrance for interaction with apoA-1. app-apoa1-3 5 6 unspecified role unspecified role bait bait in vitro In vitro 7 unspecified role unspecified role prey prey in vitro In vitro physical association physical association app-apoa-6 4 7 unspecified role unspecified role bait bait 6 unspecified role unspecified role prey prey amyloid beta binding region binding-associated region binding region undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined in vitro In vitro physical association physical association The APP protein was in the cleaved form of Amyolid beta peptide (1-40). A 1:17 molar ratio of apoA-1 to Amyloid beta was used in the interaction. app-apoa-5 2 7 unspecified role unspecified role prey prey 6 unspecified role unspecified role bait bait amyloid beta binding region binding-associated region binding region undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined physical association physical association