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/ Agrin binds to beta-amyloid (Abeta), accelerates abeta fibril formation, and is localized to Abeta deposits in Alzheimer's disease brain. Agrin binds to beta-amyloid (Abeta), accelerates abeta fibril formation, and is localized to Abeta deposits in Alzheimer's disease brain. Mol. Cell. Neurosci. (1044-7431) 2000 imex curation Cotman SL., Halfter W., Cole GJ. Neurodegeneration - Publications depicting interactions involved in neurodegenerative diseases. Apoptosis - Interactions involving proteins with a function related to apoptosis Alzheimers - Interactions investigated in the context of Alzheimers disease Paraffin or frozen sections of Alzheimer's disease brains pretreated with formic acid and stained woth polyclonal antisera recognising Abeta (1-40) or human Agrin. Abeta (1-40) peptide sequence confirmed to correspond to human sequence following correspondence with author (GC). gcole@nccu.edu 27-Oct-2007: Contacted by JYOTI. Only protein-protein interactions human Homo sapiens Human light microscopy light microscopy immunostaining immunostaining Cotman SL., Halfter W., Cole GJ. Apoptosis - Interactions involving proteins with a function related to apoptosis Paraffin or frozen sections of Alzheimer's disease brains pretreated with formic acid and stained woth polyclonal antisera recognising Abeta (1-40) or human Agrin. Abeta (1-40) peptide sequence confirmed to correspond to human sequence following correspondence with author (GC). gcole@nccu.edu Accepted 2007-JUN-22 by ORCHARD. 27-Oct-2007: Contacted by JYOTI. Mol. Cell. Neurosci. (1044-7431) 2000 Only protein-protein interactions imex curation Agrin binds to beta-amyloid (Abeta), accelerates abeta fibril formation, and is localized to Abeta deposits in Alzheimer's disease brain. Agrin binds to beta-amyloid (Abeta), accelerates abeta fibril formation, and is localized to Abeta deposits in Alzheimer's disease brain. Mol. Cell. Neurosci. (1044-7431) 2000 imex curation Cotman SL., Halfter W., Cole GJ. Neurodegeneration - Publications depicting interactions involved in neurodegenerative diseases. Apoptosis - Interactions involving proteins with a function related to apoptosis Alzheimers - Interactions investigated in the context of Alzheimers disease Paraffin or frozen sections of Alzheimer's disease brains pretreated with formic acid and stained woth polyclonal antisera recognising Abeta (1-40) or human Agrin. Abeta (1-40) peptide sequence confirmed to correspond to human sequence following correspondence with author (GC). gcole@nccu.edu 27-Oct-2007: Contacted by JYOTI. Only protein-protein interactions in vitro In vitro footprinting footprinting predetermined predetermined participant predetermined Cotman SL., Halfter W., Cole GJ. Apoptosis - Interactions involving proteins with a function related to apoptosis Paraffin or frozen sections of Alzheimer's disease brains pretreated with formic acid and stained woth polyclonal antisera recognising Abeta (1-40) or human Agrin. Abeta (1-40) peptide sequence confirmed to correspond to human sequence following correspondence with author (GC). gcole@nccu.edu Accepted 2007-JUN-22 by ORCHARD. 27-Oct-2007: Contacted by JYOTI. Mol. Cell. Neurosci. (1044-7431) 2000 Only protein-protein interactions imex curation Agrin binds to beta-amyloid (Abeta), accelerates abeta fibril formation, and is localized to Abeta deposits in Alzheimer's disease brain. Agrin binds to beta-amyloid (Abeta), accelerates abeta fibril formation, and is localized to Abeta deposits in Alzheimer's disease brain. Mol. Cell. Neurosci. (1044-7431) 2000 imex curation Cotman SL., Halfter W., Cole GJ. Neurodegeneration - Publications depicting interactions involved in neurodegenerative diseases. Apoptosis - Interactions involving proteins with a function related to apoptosis Alzheimers - Interactions investigated in the context of Alzheimers disease Paraffin or frozen sections of Alzheimer's disease brains pretreated with formic acid and stained woth polyclonal antisera recognising Abeta (1-40) or human Agrin. Abeta (1-40) peptide sequence confirmed to correspond to human sequence following correspondence with author (GC). gcole@nccu.edu 27-Oct-2007: Contacted by JYOTI. Only protein-protein interactions in vitro In vitro elisa enzyme linked immunosorbent assay ELISA ELISA elisa antibody detection identification by antibody antibody detection Cotman SL., Halfter W., Cole GJ. Apoptosis - Interactions involving proteins with a function related to apoptosis Paraffin or frozen sections of Alzheimer's disease brains pretreated with formic acid and stained woth polyclonal antisera recognising Abeta (1-40) or human Agrin. Abeta (1-40) peptide sequence confirmed to correspond to human sequence following correspondence with author (GC). gcole@nccu.edu Accepted 2007-JUN-22 by ORCHARD. Mol. Cell. Neurosci. (1044-7431) 2000 Only protein-protein interactions imex curation Agrin binds to beta-amyloid (Abeta), accelerates abeta fibril formation, and is localized to Abeta deposits in Alzheimer's disease brain. Agrin binds to beta-amyloid (Abeta), accelerates abeta fibril formation, and is localized to Abeta deposits in Alzheimer's disease brain. Mol. Cell. Neurosci. (1044-7431) 2000 imex curation Cotman SL., Halfter W., Cole GJ. Neurodegeneration - Publications depicting interactions involved in neurodegenerative diseases. Apoptosis - Interactions involving proteins with a function related to apoptosis Alzheimers - Interactions investigated in the context of Alzheimers disease Paraffin or frozen sections of Alzheimer's disease brains pretreated with formic acid and stained woth polyclonal antisera recognising Abeta (1-40) or human Agrin. Abeta (1-40) peptide sequence confirmed to correspond to human sequence following correspondence with author (GC). gcole@nccu.edu 27-Oct-2007: Contacted by JYOTI. Only protein-protein interactions in vitro In vitro cosedimentation cosedimentation western blot western blot Immuno blot Immuno blot Cotman SL., Halfter W., Cole GJ. Apoptosis - Interactions involving proteins with a function related to apoptosis Paraffin or frozen sections of Alzheimer's disease brains pretreated with formic acid and stained woth polyclonal antisera recognising Abeta (1-40) or human Agrin. Abeta (1-40) peptide sequence confirmed to correspond to human sequence following correspondence with author (GC). gcole@nccu.edu Accepted 2007-JUN-22 by ORCHARD. 27-Oct-2007: Contacted by JYOTI. Mol. Cell. Neurosci. (1044-7431) 2000 Only protein-protein interactions imex curation Agrin binds to beta-amyloid (Abeta), accelerates abeta fibril formation, and is localized to Abeta deposits in Alzheimer's disease brain. Agrin binds to beta-amyloid (Abeta), accelerates abeta fibril formation, and is localized to Abeta deposits in Alzheimer's disease brain. Mol. Cell. Neurosci. (1044-7431) 2000 imex curation Cotman SL., Halfter W., Cole GJ. Neurodegeneration - Publications depicting interactions involved in neurodegenerative diseases. Apoptosis - Interactions involving proteins with a function related to apoptosis Alzheimers - Interactions investigated in the context of Alzheimers disease Paraffin or frozen sections of Alzheimer's disease brains pretreated with formic acid and stained woth polyclonal antisera recognising Abeta (1-40) or human Agrin. Abeta (1-40) peptide sequence confirmed to correspond to human sequence following correspondence with author (GC). gcole@nccu.edu 27-Oct-2007: Contacted by JYOTI. Only protein-protein interactions human Homo sapiens Human light microscopy light microscopy immunostaining immunostaining Cotman SL., Halfter W., Cole GJ. Apoptosis - Interactions involving proteins with a function related to apoptosis Paraffin or frozen sections of Alzheimer's disease brains pretreated with formic acid and stained woth polyclonal antisera recognising Abeta (1-40) or human Agrin. Abeta (1-40) peptide sequence confirmed to correspond to human sequence following correspondence with author (GC). gcole@nccu.edu Accepted 2007-JUN-22 by ORCHARD. 27-Oct-2007: Contacted by JYOTI. Mol. Cell. Neurosci. (1044-7431) 2000 Only protein-protein interactions imex curation agrin_chick Agrin AGRN AGRIN protein protein chick Gallus gallus (Chicken) Chicken MGGSGAAATLALGLALGLALGGWANCPERELQRREEEANVVLTGTVEEIMNVDPVHHTYSCKVRVWRYLKGKDIVTHEILLDGGNKVVIGGFGDPLICDNQVSTGDTRIFFVNPAPQYMWPAHRNELMLNSSLMRITLRNLEEVEHCVEEHRKLLADKPNSYFTQTPPTPRDACRGMLCGFGAVCERSPTDPSQASCVCKKTACPVVVAPVCGSDYSTYSNECELEKAQCNQQRRIKVISKGPCGSKDPCAEVTCSFGSTCVRSADGQTAGCVCPASCSGVAESIVCGSDGKDYRSECDLNKHACDKQENVFKKFDGACDPCKGILNDMNRVCRVNPRTRRVELLSRPENCPSKREPVCGDDGVTYASECVMGRTGAIRGLEIQKVRSGQCQHQDKCKDECKFNAVCLKRWHARCSCDRITCDGTYRPVCARDSRTYSNDCERQKAECHQKAAIPVKHSGPCDLGTPSPCLSVECTFGATCVVKNREPVCECQQVCQGRYDPVCGSDNRTYGNPCELNAMACVLKREIRVKHKGPCDRCGKCQFGAICEAETGRCVCPTECVPSSQPVCGTDGNTYGSECELHVRACTQQKNILVAAQGDCKSCGTTVCSFGSTCVGGQCVCPRCEQQPLAQVCGTDGLTYDNRCELRAASCQQQKSIEVAKMGPCEDECGSGGSGSGDGSECEQDRCRHYGGWWDEDAEDDRCVCDFTCLAVPRSPVCGSDDVTYANECELKKTRCEKRQNLYVTSQGACRALTTTPPPLPVVHCSQTIYGCCPDNMTLALGVGAAGCPSTCQCNPYGSYGGTCDPATGQCSCKPGVGGLKCDRCEPGFWNFRGIVTDSKSGCTPCNCDPVGSVRDDCEQMTGLCSCKTGITGMKCNQCPNGSKMGMAGCEKDPSAPKSCEEMSCEFGATCVEVNGFAHCECPSPLCSEANMTKVCGSDGVTYGDQCQLKTIACRQGQLITVKHVGQCHESITHTSHTMPPTPLPTLPLDKLIVPPPLQLTTQAPEPTELATTSLLMEASPTTRSHPTTRRVTTTRPVTTPWMTHGVLKTTVRPLSTSPVVLATTQPPYAESGSAEGSGDQEMSISGDQESSGAGSAGEEEVEESQVTPTPAIERATCYNTPLGCCSDGKTAAADAEGSNCPATKVFQGVLILEEVEGQELFYTPEMADPKSELFGETARSIESALDELFRNSDVKNDFKSIRVRDLGQSSAVRVIVESHFDPATSYTAADVQAASLKQIRASKKRTILVKKPQQEHVKFMDFDWIPRIFTTTITTTTATTMAPATTRRHTTASAATTAHILRQDTVGHPSAKLAAPASTRRPTSTLPTTARRKPTRQPPSTTKKPSRPCDSHPCLHGGTCEDDGREFTCRCPAGKGGAVCEKPIRYFIPSFGGKSYLAFKMMKAYHTVRIAMEFRATELSGLLLYNGQNRGKDFISLALVGGFVELRFNTGSGTGVITSKVRVEPGKWHQLVVNRNRRSGMLAVDGEHVSGESPTGTDGLNLDTDLFVGGAPEDQMAVVAERTAATVGLKGSIRLLDVNNQMYDLREKGSDVLYGSGVGECGNDPCHPNPCHHGASCHVKEAEMFHCECLHSYTGPTCADERNPCDPTPCHISATCLVLPEGGAMCACPMGREGEFCERVTEQDHTMPFLPEFNGFSYLELNGLQTLFLTCRQMSMEVVFLAKSPSGMIFYNGQKTDGKGDFVSLALHDGYLEYRYDLGKGAAVLRSKEPVPLNTWISVLLERSGRKGVMRINNGERVMGESPKSRKVPHAFLNLKEPFYVGGAPDFSKLARAAAISTSFYGAVQRISIKGVPLLKEQHIRSAVEISTFRAHPCTQKPNPCQNGGTCSPRLESYECACQRGFSGAHCEKVIIEKAAGDAEAIAFDGRTYMEYHNAVTKSHLSNEIPAPDALDYPAEPSEKALQSNHFELSIKTEATQGLILWSGKGLERSDYIALAIVDGFVQMMYDLGSKPVVLRSTVPINTNHWTHIKAYRVQREGSLQVGNEAPITGSSPLGATQLDTDGALWLGGMERLSVAHKLPKAYSTGFIGCIRDVIVDRQELHLVEDALNNPTILHCSAK 87FEFE1A11664F0E agrin_human Agrin AGRN AGRIN protein protein human Homo sapiens Human MAGRSHPGPLRPLLPLLVVAACVLPGAGGTCPERALERREEEANVVLTGTVEEILNVDPVQHTYSCKVRVWRYLKGKDLVARESLLDGGNKVVISGFGDPLICDNQVSTGDTRIFFVNPAPPYLWPAHKNELMLNSSLMRITLRNLEEVEFCVEDKPGTHFTPVPPTPPDACRGMLCGFGAVCEPNAEGPGRASCVCKKSPCPSVVAPVCGSDASTYSNECELQRAQCSQQRRIRLLSRGPCGSRDPCSNVTCSFGSTCARSADGLTASCLCPATCRGAPEGTVCGSDGADYPGECQLLRRACARQENVFKKFDGPCDPCQGALPDPSRSCRVNPRTRRPEMLLRPESCPARQAPVCGDDGVTYENDCVMGRSGAARGLLLQKVRSGQCQGRDQCPEPCRFNAVCLSRRGRPRCSCDRVTCDGAYRPVCAQDGRTYDSDCWRQQAECRQQRAIPSKHQGPCDQAPSPCLGVQCAFGATCAVKNGQAACECLQACSSLYDPVCGSDGVTYGSACELEATACTLGREIQVARKGPCDRCGQCRFGALCEAETGRCVCPSECVALAQPVCGSDGHTYPSECMLHVHACTHQISLHVASAGPCETCGDAVCAFGAVCSAGQCVCPRCEHPPPGPVCGSDGVTYGSACELREAACLQQTQIEEARAGPCEQAECGSGGSGSGEDGDCEQELCRQRGGIWDEDSEDGPCVCDFSCQSVPGSPVCGSDGVTYSTECELKKARCESQRGLYVAAQGACRGPTFAPLPPVAPLHCAQTPYGCCQDNITAARGVGLAGCPSACQCNPHGSYGGTCDPATGQCSCRPGVGGLRCDRCEPGFWNFRGIVTDGRSGCTPCSCDPQGAVRDDCEQMTGLCSCKPGVAGPKCGQCPDGRALGPAGCEADASAPATCAEMRCEFGARCVEESGSAHCVCPMLTCPEANATKVCGSDGVTYGNECQLKTIACRQGLQISIQSLGPCQEAVAPSTHPTSASVTVTTPGLLLSQALPAPPGALPLAPSSTAHSQTTPPPSSRPRTTASVPRTTVWPVLTVPPTAPSPAPSLVASAFGESGSTDGSSDEELSGDQEASGGGSGGLEPLEGSSVATPGPPVERASCYNSALGCCSDGKTPSLDAEGSNCPATKVFQGVLELEGVEGQELFYTPEMADPKSELFGETARSIESTLDDLFRNSDVKKDFRSVRLRDLGPGKSVRAIVDVHFDPTTAFRAPDVARALLRQIQVSRRRSLGVRRPLQEHVRFMDFDWFPAFITGATSGAIAAGATARATTASRLPSSAVTPRAPHPSHTSQPVAKTTAAPTTRRPPTTAPSRVPGRRPPAPQQPPKPCDSQPCFHGGTCQDWALGGGFTCSCPAGRGGAVCEKVLGAPVPAFEGRSFLAFPTLRAYHTLRLALEFRALEPQGLLLYNGNARGKDFLALALLDGRVQLRFDTGSGPAVLTSAVPVEPGQWHRLELSRHWRRGTLSVDGETPVLGESPSGTDGLNLDTDLFVGGVPEDQAAVALERTFVGAGLRGCIRLLDVNNQRLELGIGPGAATRGSGVGECGDHPCLPNPCHGGAPCQNLEAGRFHCQCPPGRVGPTCADEKSPCQPNPCHGAAPCRVLPEGGAQCECPLGREGTFCQTASGQDGSGPFLADFNGFSHLELRGLHTFARDLGEKMALEVVFLARGPSGLLLYNGQKTDGKGDFVSLALRDRRLEFRYDLGKGAAVIRSREPVTLGAWTRVSLERNGRKGALRVGDGPRVLGESPKSRKVPHTVLNLKEPLYVGGAPDFSKLARAAAVSSGFDGAIQLVSLGGRQLLTPEHVLRQVDVTSFAGHPCTRASGHPCLNGASCVPREAAYVCLCPGGFSGPHCEKGLVEKSAGDVDTLAFDGRTFVEYLNAVTESELANEIPVPETLDSGALHSEKALQSNHFELSLRTEATQGLVLWSGKATERADYVALAIVDGHLQLSYNLGSQPVVLRSTVPVNTNRWLRVVAHREQREGSLQVGNEAPVTGSSPLGATQLDTDGALWLGGLPELPVGPALPKAYGTGFVGCLRDVVVGRHPLHLLEDAVTKPELRPCPTP 8B3E3D0FF65517F0 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 agrn-p05067pro 4 8 unspecified role unspecified role prey prey 6 unspecified role unspecified role bait bait chick Gallus gallus (Chicken) Chicken physical association physical association An immunopositive smear from 400 to 600 kDa (representative of agrin?s appearance when separated by SDS?PAGE) was seen in the pellet fraction when agrin was coincubated with Ab (1?40). No agrin was observed in the pellet fraction when Ab (1?40) was omitted from the incubation (B). Fig. 4 agrn-p05067pro 5 8 unspecified role unspecified role neutral component neutral component 7 unspecified role unspecified role neutral component neutral component colocalization colocalization Immunostaing of Agrin and Abeta (1-40) observed in neuritic plaques in the hippocampus of a 62 year old AD patient. Human Agrin antibody generated by rabbit immunization with a human agrin fusion protein (amino acids 780-1210) representing the N terminal half of the protein. anti Abeta (1-40) was purchased from Sigma. Fig 6C and D agrn-p05067pro-2 1 8 unspecified role unspecified role neutral component neutral component 7 unspecified role unspecified role neutral component neutral component colocalization colocalization Immunostaing of Agrin and Abeta (1-40) observed in senile plaques in the frontal cortex of a 92 year old AD patient. Human Agrin antibody generated by rabbit immunization with a human agrin fusion protein (amino acids 780-1210) representing the N terminal half of the protein. anti Abeta (1-40) was purchased from Sigma. Fig 6A and B agrn-p05067pro-3 1 8 unspecified role unspecified role neutral component neutral component 7 unspecified role unspecified role neutral component neutral component colocalization colocalization Immunostaing of Agrin and Abeta (1-40) observed in the microvasculature in the frontal cortex of a 92 year old patient. Human Agrin antibody generated by rabbit immunization with a human agrin fusion protein (amino acids 780-1210) representing the N terminal half of the protein. anti Abeta (1-40) was purchased from Sigma. Fig 6E and F agrn-p05067pro-1 2 6 unspecified role unspecified role neutral component neutral component chick Gallus gallus (Chicken) Chicken 8 unspecified role unspecified role neutral component neutral component direct interaction direct interaction Fig. 2 agrn-p05067pro 3 8 unspecified role unspecified role prey prey 6 unspecified role unspecified role bait bait chick Gallus gallus (Chicken) Chicken direct interaction direct interaction Nitrous acid treatment (removal of heparan sulphate GAG side chains)of Agrin almost completly abolished binding to fibrilla Abeta. Non fibrilla Abeta did not bind to Agrin. Fig. 1