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/ http://www.ebi.ac.uk/ lee-2006b-1 Dequalinium-induced protofibril formation of alpha-synuclein. in vitro In vitro comig non denat gel comigration in non denaturing gel electrophoresis comig non denat gel predetermined predetermined participant predetermined Lee CH., Kim HJ., Lee JH., Cho HJ., Kim J., Chung KC., Jung S., Paik SR. BioCreative - Critical Assessment of Information Extraction systems in Biology Alpha-synuclein was incubated with for 30 minutes at 37C with various concetrations of Dequalinium (C10-DQ) or dequalinium analogue with C14-linker (C14-DQ) prior to cross-linking. srpaik@snu.ac.kr J. Biol. Chem. (0021-9258) 2006 Only protein-protein interactions imex curation lee-2006b-2 Dequalinium-induced protofibril formation of alpha-synuclein. in vitro In vitro biophysical biophysical predetermined predetermined participant predetermined Lee CH., Kim HJ., Lee JH., Cho HJ., Kim J., Chung KC., Jung S., Paik SR. BioCreative - Critical Assessment of Information Extraction systems in Biology Alpha-synuclein was incubated with for 30 minutes at 37C with various concetrations of Dequalinium (C10-DQ) or dequalinium analogue with C14-linker (C14-DQ) prior to cross-linking. srpaik@snu.ac.kr J. Biol. Chem. (0021-9258) 2006 Only protein-protein interactions imex curation lee-2006b-3 Dequalinium-induced protofibril formation of alpha-synuclein. in vitro In vitro fluorescence spectr classical fluorescence spectroscopy fluorescence spectr predetermined predetermined participant predetermined Lee CH., Kim HJ., Lee JH., Cho HJ., Kim J., Chung KC., Jung S., Paik SR. BioCreative - Critical Assessment of Information Extraction systems in Biology Alpha-synuclein was incubated with for 30 minutes at 37C with various concetrations of Dequalinium (C10-DQ) or dequalinium analogue with C14-linker (C14-DQ) prior to cross-linking. srpaik@snu.ac.kr J. Biol. Chem. (0021-9258) 2006 Only protein-protein interactions imex curation lee-2006b-4 Dequalinium-induced protofibril formation of alpha-synuclein. in vitro In vitro tem transmission electron microscopy tem predetermined predetermined participant predetermined Lee CH., Kim HJ., Lee JH., Cho HJ., Kim J., Chung KC., Jung S., Paik SR. BioCreative - Critical Assessment of Information Extraction systems in Biology Alpha-synuclein was incubated with for 30 minutes at 37C with various concetrations of Dequalinium (C10-DQ) or dequalinium analogue with C14-linker (C14-DQ) prior to cross-linking. srpaik@snu.ac.kr J. Biol. Chem. (0021-9258) 2006 Only protein-protein interactions imex curation lee-2006b-5 Dequalinium-induced protofibril formation of alpha-synuclein. in vitro In vitro 3d-em 3D electron microscopy 3D-EM electron tomog predetermined predetermined participant predetermined Lee CH., Kim HJ., Lee JH., Cho HJ., Kim J., Chung KC., Jung S., Paik SR. BioCreative - Critical Assessment of Information Extraction systems in Biology Alpha-synuclein was incubated with for 30 minutes at 37C with various concetrations of Dequalinium (C10-DQ) or dequalinium analogue with C14-linker (C14-DQ) prior to cross-linking. srpaik@snu.ac.kr J. Biol. Chem. (0021-9258) 2006 Only protein-protein interactions imex curation lee-2006b-6 Dequalinium-induced protofibril formation of alpha-synuclein. in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Lee CH., Kim HJ., Lee JH., Cho HJ., Kim J., Chung KC., Jung S., Paik SR. BioCreative - Critical Assessment of Information Extraction systems in Biology Alpha-synuclein was incubated with for 30 minutes at 37C with various concetrations of Dequalinium (C10-DQ) or dequalinium analogue with C14-linker (C14-DQ) prior to cross-linking. srpaik@snu.ac.kr J. Biol. Chem. (0021-9258) 2006 Only protein-protein interactions imex curation syua_human Alpha-synuclein Non-A beta component of AD amyloid Non-A4 component of amyloid precursor SNCA NACP PARK1 protein protein human Homo sapiens Human MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA scna-3 Oligomerisation of alpha-synuclein 504433 N/A 504439 unspecified role unspecified role neutral component neutral component c terminal sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false Stoichiometry: 2.0 direct interaction direct interaction false false false dequalinium The protein was self-oligomerized by dequalinium, which gave rise to the ladder formation on N-[2-hydroxy-1,1- bis(hydroxymethyl)ethyl]glycine/SDS-PAGE in the presence of a coupling reagent of N-(ethoxycarbonyl)-2-ethoxy-1,2-dihydroquinoline. Figure 2, 3 and 4 scna-1 Oligomerisation of alpha-synuclein 504434 N/A 504439 unspecified role unspecified role neutral component neutral component direct interaction direct interaction false false false Figure 7A and 7C As dequalinium concentrations increased (1.4, 14, and 140micro molar) the final turbidities were also increased. As the length of hydrocarbon chain was varied among C4, C6, and C10 at a fixed concentration of 50 micro molar, the final turbidity was increased with apparent reduction in the lag period. scna-2 Oligomerisation of alpha-synuclein 504435 N/A 504439 unspecified role unspecified role neutral component neutral component c terminal sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false direct interaction direct interaction false false false Figure 7B and 7D The final thioflavin-T binding fluorescence obtained in the presence of the analogues of alpha-synclein was lower than that of the aggregates prepared with alpha-synuclein alone scna Oligomerisation of alpha-synuclein 504436 N/A 504439 unspecified role unspecified role neutral component neutral component direct interaction direct interaction false false false Figure 9 In the presence of 50micro molar dequalinium, the highest peak due to the oligomeric protein aggregates was obtained at the void volume, although the condition caused most rapid protein aggregation with the highest final turbidity scna-4 Oligomerisation of alpha-synuclein 504437 N/A 504439 unspecified role unspecified role neutral component neutral component direct interaction direct interaction false false false Figure 8 and 10 By measuring various granular structures revealed under AFM, their average diameters were estimated as 39 nm (SE = 9), scna-5 Oligomerisation of alpha-synuclein 504438 N/A 504439 unspecified role unspecified role neutral component neutral component direct interaction direct interaction false false false Figure 9 The authors state that "Intriguingly, the oligomer- containing peak was increased as dequalinium level was raised. In the presence of 50 micro molar dequalinium, the highest peak due to the oligomeric protein aggregates was obtained at the void volume, although the condition caused most rapid protein aggregation with the highest final turbidity (Fig. 9). This finding data clearly indicated that dequalinium favored the oligomer formation and also prevented further development into the amyloids."