matrixdb Institut de Biologie et de Chimie des Prot\u00c3\u00a9ines, 7, passage du Vercors 69 367 Lyon cedex 07 FRANCE matrixdb@ibcp.fr http://matrixdb.ibcp.fr Collagenous Alzheimer amyloid plaque component assembles amyloid fibrils into protease resistant aggregates. Collagenous Alzheimer amyloid plaque component assembles amyloid fibrils into protease resistant aggregates. The FEBS journal 2005 imex curation Söderberg L., Dahlqvist C., Kakuyama H., Thyberg J., Ito A., Winblad B., Näslund J., Tjernberg LO. camilla.dahlqvist@neurotec.ki.se 22-Jun-2016: Contacted by IntAct-Help. Only protein-protein interactions imex curation in vitro In vitro fluorescence fluorescence technology fluorescence predetermined predetermined participant predetermined Söderberg L., Dahlqvist C., Kakuyama H., Thyberg J., Ito A., Winblad B., Näslund J., Tjernberg LO. camilla.dahlqvist@neurotec.ki.se Accepted 2016-APR-27 AT 14:16 BST AT 14:16 BST by ORCHARD The FEBS journal 2005 Only protein-protein interactions imex curation imex curation Collagenous Alzheimer amyloid plaque component assembles amyloid fibrils into protease resistant aggregates. Collagenous Alzheimer amyloid plaque component assembles amyloid fibrils into protease resistant aggregates. The FEBS journal 2005 imex curation Söderberg L., Dahlqvist C., Kakuyama H., Thyberg J., Ito A., Winblad B., Näslund J., Tjernberg LO. camilla.dahlqvist@neurotec.ki.se 22-Jun-2016: Contacted by IntAct-Help. Only protein-protein interactions imex curation in vitro In vitro electron microscopy electron microscopy Electron crystallography Electron cryomicroscopy Electron crystallography Electron cryomicroscopy predetermined predetermined participant predetermined Söderberg L., Dahlqvist C., Kakuyama H., Thyberg J., Ito A., Winblad B., Näslund J., Tjernberg LO. camilla.dahlqvist@neurotec.ki.se Accepted 2016-APR-27 AT 14:16 BST AT 14:16 BST by ORCHARD The FEBS journal 2005 Only protein-protein interactions imex curation imex curation Collagenous Alzheimer amyloid plaque component assembles amyloid fibrils into protease resistant aggregates. Collagenous Alzheimer amyloid plaque component assembles amyloid fibrils into protease resistant aggregates. The FEBS journal 2005 imex curation Söderberg L., Dahlqvist C., Kakuyama H., Thyberg J., Ito A., Winblad B., Näslund J., Tjernberg LO. camilla.dahlqvist@neurotec.ki.se 22-Jun-2016: Contacted by IntAct-Help. Only protein-protein interactions imex curation in vitro In vitro aggregation aggregation assay aggregation predetermined predetermined participant predetermined Söderberg L., Dahlqvist C., Kakuyama H., Thyberg J., Ito A., Winblad B., Näslund J., Tjernberg LO. camilla.dahlqvist@neurotec.ki.se Accepted 2016-APR-27 AT 14:16 BST AT 14:16 BST by ORCHARD The FEBS journal 2005 Only protein-protein interactions imex curation imex curation Mock publication and experiment for abstract interactions that are not interaction evidences. Mock publication and experiment for abstract interactions that are not interaction evidences. unspecified method Collagenous Alzheimer amyloid plaque component assembles amyloid fibrils into protease resistant aggregates. Collagenous Alzheimer amyloid plaque component assembles amyloid fibrils into protease resistant aggregates. The FEBS journal 2005 imex curation Söderberg L., Dahlqvist C., Kakuyama H., Thyberg J., Ito A., Winblad B., Näslund J., Tjernberg LO. camilla.dahlqvist@neurotec.ki.se 22-Jun-2016: Contacted by IntAct-Help. Only protein-protein interactions imex curation in vitro In vitro solid phase assay solid phase assay predetermined predetermined participant predetermined Söderberg L., Dahlqvist C., Kakuyama H., Thyberg J., Ito A., Winblad B., Näslund J., Tjernberg LO. camilla.dahlqvist@neurotec.ki.se Accepted 2016-APR-27 AT 14:16 BST AT 14:16 BST by ORCHARD The FEBS journal 2005 Only protein-protein interactions imex curation imex curation tht Thioflavin T small molecule small molecule chemical synthesis Chemical synthesis (Chemical synthesis) p05067-pro_0000000092 Amyloid-beta protein 42 Alzheimer disease amyloid protein Cerebral vascular amyloid peptide APP A4 AD1 ABPP 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 DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA 672 713 3AC85563D7858C37 q9bxs0-3 Collagen alpha-1(XXV) chain COL25A1 Alzheimer disease amyloid-associated protein CLAC-P protein protein human Homo sapiens Human MLLKKHAGKGGGREPRSEDPTPAEQHCARTMPPCAVLAALLSVVAVVSCLYLGVKTNDLQARIAALESAKGAPSIHLLPDTLDHLKTMVQEKVERLLAQKSYEHMAKIRIAREAPSECNCPAGPPGKRGKRGRRGESGPPGPPGPKGDKGEQGDQGPRMVFPKINHGFLSADQQLIKRRLIKGDQGQAGPPGPPGPPGPRGPPGDTGKDGPRGMPGVPGEPGKPGEQGLMGPLGPPGQKGSIGAPGIPGMNGQKGEPGLPGAVGQNGIPGPKGEPGEQGEKGDAGENGPKGDTGEKGDPGSSAAGIKGEPGESGRPGQKGEPGFIGPQGEPGLPGLPGTKGERGEAGPPGRGERGEPGAPGPKGKQGESGTRGPKGSKGDRGEKGDSGAQGPRGPPGQKGDQGATEIIDYNGNLHEALQRITTLTVTGPPGPPGPQGLQGPKGEQGSPGIPGMDGEQGLKGSKGDMGDPGMTGEKGGIGLPGLPGANGMKGEKGDSGMPGPQGPSIIGPPGPPGPHGPPGPMGPHGLPGPKGTDGPMGPHGPAGPKGERGEKGAMGEPGPRGPYGLPLGPDGLPMPGCWQK D4F26C1293B70F3B 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-collagen_xxv_3_human-1 3 12 unspecified role unspecified role neutral component neutral component tag His tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range Binding site Binding site sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain tag myc tag myc tag myc tag EUKLISEED epitope tag EUKLISEED epitope tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range human-293 Homo sapiens transformed primary embryonal kidney cells Human 293 Transformed human primary embryonal kidney cells. The Cell type named 293 is synonymous with HEK-293. 9 unspecified role unspecified role neutral component neutral component chemical synthesis Chemical synthesis (Chemical synthesis) direct interaction direct interaction Figure 1A The experiment was performed with (Abeta1–40) fibrils app-collagen_xxv_3_human-2 2 12 unspecified role unspecified role neutral component neutral component tag His tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range Binding site Binding site sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain tag myc tag myc tag myc tag EUKLISEED epitope tag EUKLISEED epitope tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range human-293 Homo sapiens transformed primary embryonal kidney cells Human 293 Transformed human primary embryonal kidney cells. The Cell type named 293 is synonymous with HEK-293. 9 unspecified role unspecified role neutral component neutral component chemical synthesis Chemical synthesis (Chemical synthesis) direct interaction direct interaction Figure 1C and 4B The experiment was performed with (Abeta1–40) fibrils app-collagen_xxv_3_human-3 5 12 unspecified role unspecified role neutral component neutral component tag His tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range Binding site Binding site sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain tag myc tag myc tag myc tag EUKLISEED epitope tag EUKLISEED epitope tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range human-293 Homo sapiens transformed primary embryonal kidney cells Human 293 Transformed human primary embryonal kidney cells. The Cell type named 293 is synonymous with HEK-293. 7 unspecified role unspecified role neutral component neutral component chemical synthesis Chemical synthesis (Chemical synthesis) 6 unspecified role unspecified role neutral component neutral component chemical synthesis Chemical synthesis (Chemical synthesis) physical association physical association Figure 4C The experiment was performed with (Abeta1–42) fibrils app-collagen_xxv_3_human-4 1 9 unspecified role unspecified role neutral component neutral component chemical synthesis Chemical synthesis (Chemical synthesis) 6 unspecified role unspecified role neutral component neutral component chemical synthesis Chemical synthesis (Chemical synthesis) 12 unspecified role unspecified role neutral component neutral component tag myc tag myc tag myc tag EUKLISEED epitope tag EUKLISEED epitope tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range tag His tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range Binding site Binding site sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain human-293 Homo sapiens transformed primary embryonal kidney cells Human 293 Transformed human primary embryonal kidney cells. The Cell type named 293 is synonymous with HEK-293. physical association physical association Figures 3A and 4A collagen-xxv-3_human Type XXV collagen Collagen type XXV trimer, variant 3 Type XXV collagen COL25A1 trimer 8 unspecified role unspecified role direct interaction direct interaction human Homo sapiens Human stable complex stable complex biological system reconstruction evidence based on inference from background scientific knowledge used in manual assertion biological system reconstruction evidence based on inference from background scientific knowledge used in manual assertion Type II orientated transmembrane collagen. Inhibits fibrillization of beta amyloid peptide during the elongation phase. Has also been shown to assemble amyloid fibrils into protease-resistant aggregates. Binds heparin. Homotrimer Triple-helices consisting of about 1000 amino acids per chain forming a coiled coil structure. Each polypeptide forms a left-handed helix in which every third residue, glycine, comes into the centre of the superhelix. Sylvie Ricard-Blum, MatrixDB Accepted 2016-MAR-31 by ORCHARD