DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Structure and biochemical analysis of the heparin-induced E1 dimer of the amyloid precursor protein. Structure and biochemical analysis of the heparin-induced E1 dimer of the amyloid precursor protein. Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Dahms SO., Hoefgen S., Roeser D., Schlott B., Gührs KH., Than ME. Only protein-protein interactions ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Dahms SO., Hoefgen S., Roeser D., Schlott B., Gührs KH., Than ME. DIP original experiment: DIP-216350X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx Structure and biochemical analysis of the heparin-induced E1 dimer of the amyloid precursor protein. Structure and biochemical analysis of the heparin-induced E1 dimer of the amyloid precursor protein. Structure and biochemical analysis of the heparin-induced E1 dimer of the amyloid precursor protein. Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Dahms SO., Hoefgen S., Roeser D., Schlott B., Gührs KH., Than ME. Only protein-protein interactions ecolx Escherichia coli sls static light scattering sls predetermined predetermined participant predetermined Dahms SO., Hoefgen S., Roeser D., Schlott B., Gührs KH., Than ME. DIP original experiment: DIP-216352X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx Structure and biochemical analysis of the heparin-induced E1 dimer of the amyloid precursor protein. Structure and biochemical analysis of the heparin-induced E1 dimer of the amyloid precursor protein. Structure and biochemical analysis of the heparin-induced E1 dimer of the amyloid precursor protein. Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Dahms SO., Hoefgen S., Roeser D., Schlott B., Gührs KH., Than ME. Only protein-protein interactions ecolx Escherichia coli molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Dahms SO., Hoefgen S., Roeser D., Schlott B., Gührs KH., Than ME. DIP original experiment: DIP-216351X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx Structure and biochemical analysis of the heparin-induced E1 dimer of the amyloid precursor protein. Structure and biochemical analysis of the heparin-induced E1 dimer of the amyloid precursor protein. Structure and biochemical analysis of the heparin-induced E1 dimer of the amyloid precursor protein. Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Dahms SO., Hoefgen S., Roeser D., Schlott B., Gührs KH., Than ME. Only protein-protein interactions ecolx Escherichia coli dls dynamic light scattering dls predetermined predetermined participant predetermined Dahms SO., Hoefgen S., Roeser D., Schlott B., Gührs KH., Than ME. DIP original experiment: DIP-216353X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx Structure and biochemical analysis of the heparin-induced E1 dimer of the amyloid precursor protein. p05067-4 Amyloid-beta precursor protein APP A4 AD1 ABPP Alzheimer disease amyloid protein Cerebral vascular amyloid peptide PreA4 Protease nexin-II APPI PreA4 695 Amyloid precursor protein Amyloid-beta A4 protein Alzheimer disease amyloid A4 protein homolog Amyloid-beta (A4) precursor protein protein protein human Homo sapiens Human MLPGLALLLLAAWTARALEVPTDGNAGLLAEPQIAMFCGRLNMHMNVQNGKWDSDPSGTKTCIDTKEGILQYCQEVYPELQITNVVEANQPVTIQNWCKRGRKQCKTHPHFVIPYRCLVGEFVSDALLVPDKCKFLHQERMDVCETHLHWHTVAKETCSEKSTNLHDYGMLLPCGIDKFRGVEFVCCPLAEESDNVDSADAEEDDSDVWWGGADTDYADGSEDKVVEVAEEEEVAEVEEEEADDDEDDEDGDEVEEEAEEPYEEATERTTSIATTTTTTTESVEEVVRVPTTAASTPDAVDKYLETPGDENEHAHFQKAKERLEAKHRERMSQVMREWEEAERQAKNLPKADKKAVIQHFQEKVESLEQEAANERQQLVETHMARVEAMLNDRRRLALENYITALQAVPPRPRHVFNMLKKYVRAEQKDRQHTLKHFEHVRMVDPKKAAQIRSQVMTHLRVIYERMNQSLSLLYNVPAVAEEIQDEVDELLQKEQNYSDDVLANMISEPRISYGNDALMPSLTETKTTVELLPVNGEFSLDDLQPWHSFGADSVPANTENEVEPVDARPAADRGLTTRPGSGLTNIKTEEISEVKMDAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIATVIVITLVMLKKKQYTSIHHGVVEVDAAVTPEERHLSKMQQNGYENPTYKFFEQMQN DIP protein P05067-4 original sequence version: 183 DIP protein P05067-4 original sequence version: 198 DIP protein P05067-4 original sequence version: 224 A major isoform. 4F6EA0139F969D56 app-113 4 5 unspecified role unspecified role unspecified role unspecified role Region 18-190 Region 18-190 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction app-3 1 5 unspecified role unspecified role unspecified role unspecified role Region 18-190 Region 18-190 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction app-4 3 5 unspecified role unspecified role unspecified role unspecified role Region 18-190 Region 18-190 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction app-5 2 5 unspecified role unspecified role unspecified role unspecified role Region 18-190 Region 18-190 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction