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/ In cerebrospinal fluid ER chaperones ERp57 and calreticulin bind beta-amyloid. In cerebrospinal fluid ER chaperones ERp57 and calreticulin bind beta-amyloid. Biochem. Biophys. Res. Commun. (0006-291X) 2005 imex curation Erickson RR., Dunning LM., Olson DA., Cohen SJ., Davis AT., Wood WG., Kratzke RA., Holtzman JL. Neurodegeneration - Publications depicting interactions involved in neurodegenerative diseases. Synapse - Interactions of proteins with an established role in the presynapse. Apoptosis - Interactions involving proteins with a function related to apoptosis Alzheimers - Interactions investigated in the context of Alzheimers disease abeta-ERp57(PDIA3) complex was isolated by immunochromatography with antibodies to to ERp57 and abeta bound to CNBr-activated Sepharose. The ERp57 and abeta in the eluates were identified by immunoblotting. holtz003@umn.edu 27-Oct-2007: Contacted by JYOTI. Only protein-protein interactions in vitro In vitro pull down pull down western blot western blot Immuno blot Immuno blot Erickson RR., Dunning LM., Olson DA., Cohen SJ., Davis AT., Wood WG., Kratzke RA., Holtzman JL. Synapse - Interactions of proteins with an established role in the presynapse. abeta-ERp57(PDIA3) complex was isolated by immunochromatography with antibodies to to ERp57 and abeta bound to CNBr-activated Sepharose. The ERp57 and abeta in the eluates were identified by immunoblotting. holtz003@umn.edu Accepted 2007-FEB-26 by ORCHARD. 27-Oct-2007: Contacted by JYOTI. Biochem. Biophys. Res. Commun. (0006-291X) 2005 Only protein-protein interactions imex curation In cerebrospinal fluid ER chaperones ERp57 and calreticulin bind beta-amyloid. In cerebrospinal fluid ER chaperones ERp57 and calreticulin bind beta-amyloid. Biochem. Biophys. Res. Commun. (0006-291X) 2005 imex curation Erickson RR., Dunning LM., Olson DA., Cohen SJ., Davis AT., Wood WG., Kratzke RA., Holtzman JL. Neurodegeneration - Publications depicting interactions involved in neurodegenerative diseases. Synapse - Interactions of proteins with an established role in the presynapse. Apoptosis - Interactions involving proteins with a function related to apoptosis Alzheimers - Interactions investigated in the context of Alzheimers disease abeta-ERp57(PDIA3) complex was isolated by immunochromatography with antibodies to to ERp57 and abeta bound to CNBr-activated Sepharose. The ERp57 and abeta in the eluates were identified by immunoblotting. holtz003@umn.edu 27-Oct-2007: Contacted by JYOTI. Only protein-protein interactions human Homo sapiens Human comig non denat gel comigration in non denaturing gel electrophoresis comig non denat gel western blot western blot Immuno blot Immuno blot Erickson RR., Dunning LM., Olson DA., Cohen SJ., Davis AT., Wood WG., Kratzke RA., Holtzman JL. Synapse - Interactions of proteins with an established role in the presynapse. A number of antibodies for each target are used in the publication, the specific antibodies used for figure 2 are not specified. abeta-ERp57(PDIA3) complex was isolated by immunochromatography with antibodies to to ERp57 and abeta bound to CNBr-activated Sepharose. The ERp57 and abeta in the eluates were identified by immunoblotting. holtz003@umn.edu Accepted 2007-FEB-26 by ORCHARD. chicken polyclonal to ERp57 (previously described in Chen, Biochemistry 25 (1996) 5892-5986, rabbit polyclonal to Abeta (R1282, gift from D. Selkow, harvard medical School), anti calreticulin. Biochem. Biophys. Res. Commun. (0006-291X) 2005 Only protein-protein interactions imex curation pdia3_human Protein disulfide-isomerase A3 Disulfide isomerase ER-60 Endoplasmic reticulum resident protein 60 58 kDa microsomal protein Endoplasmic reticulum resident protein 57 58 kDa glucose-regulated protein PDIA3 ERP60 GRP58 ERP57 protein protein human Homo sapiens Human MRLRRLALFPGVALLLAAARLAAASDVLELTDDNFESRISDTGSAGLMLVEFFAPWCGHCKRLAPEYEAAATRLKGIVPLAKVDCTANTNTCNKYGVSGYPTLKIFRDGEEAGAYDGPRTADGIVSHLKKQAGPASVPLRTEEEFKKFISDKDASIVGFFDDSFSEAHSEFLKAASNLRDNYRFAHTNVESLVNEYDDNGEGIILFRPSHLTNKFEDKTVAYTEQKMTSGKIKKFIQENIFGICPHMTEDNKDLIQGKDLLIAYYDVDYEKNAKGSNYWRNRVMMVAKKFLDAGHKLNFAVASRKTFSHELSDFGLESTAGEIPVVAIRTAKGEKFVMQEEFSRDGKALERFLQDYFDGNLKRYLKSEPIPESNDGPVKVVVAENFDEIVNNENKDVLIEFYAPWCGHCKNLEPKYKELGEKLSKDPNIVIAKMDATANDVPSPYEVRGFPTIYFSPANKKLNPKKYEGGRELSDFISYLQREATNPPVIQEEKPKKKKKAQEDL DIP protein P30101 original sequence version: 82 529E5B6692D0D7E9 calr_human Calreticulin CRP55 Calregulin HACBP Endoplasmic reticulum resident protein 60 grp60 CALR CRTC protein protein human Homo sapiens Human MLLSVPLLLGLLGLAVAEPAVYFKEQFLDGDGWTSRWIESKHKSDFGKFVLSSGKFYGDEEKDKGLQTSQDARFYALSASFEPFSNKGQTLVVQFTVKHEQNIDCGGGYVKLFPNSLDQTDMHGDSEYNIMFGPDICGPGTKKVHVIFNYKGKNVLINKDIRCKDDEFTHLYTLIVRPDNTYEVKIDNSQVESGSLEDDWDFLPPKKIKDPDASKPEDWDERAKIDDPTDSKPEDWDKPEHIPDPDAKKPEDWDEEMDGEWEPPVIQNPEYKGEWKPRQIDNPDYKGTWIHPEIDNPEYSPDPSIYAYDNFGVLGLDLWQVKSGTIFDNFLITNDEAYAEEFGNETWGVTKAAEKQMKDKQDEEQRLKEEEEDKKRKEEEEAEDKEDDEDKDEDEEDEEDKEEDEEEDVPGQAKDEL BC37C3C0F1054FB2 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 app-pdia3 1 3 unspecified role unspecified role prey prey 5 unspecified role unspecified role bait bait physical association physical association Figure 3, channel 3. pdia3-app 1 5 unspecified role unspecified role prey prey 3 unspecified role unspecified role bait bait physical association physical association Figure 3, channel 4. app-2 2 5 unspecified role unspecified role neutral component neutral component 3 unspecified role unspecified role neutral component neutral component 4 unspecified role unspecified role neutral component neutral component association association The authors comment that their findings suggest that the ERp57 (PDIA3) is bound to abeta and that calreticulin is bound to the PDIA3. Figure 1 and 2.