| http://purl.uniprot.org/citations/1512244 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/1512244 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/1512244 | http://www.w3.org/2000/01/rdf-schema#comment | "Tau with unusually slow mobilities in sodium dodecyl sulfate-polyacrylamide gel electrophoresis was purified from the Sarkosyl-insoluble pellet of Alzheimer's disease brain homogenates. Such species of tau (PHF-tau) are considered to construct the framework of the sodium dodecyl sulfate-soluble form of paired helical filaments (PHF). Detailed comparison of peptide maps of PHF-tau and normal tau before and after dephosphorylation pointed to three anomalously eluted peaks which contained abnormally phosphorylated peptides, residues 191-225, 226-240, 260-267, and 386-438, according to the numbering of the longest tau isoform (Goedert, M., Spillantini, M. G., Jakes, R., Rutherford, D., and Crowther, R. A. (1989) Neuron 3, 519-526). Protein sequence and mass spectrometric analyses localized Thr-231 and Ser-235 as the abnormal phosphorylation sites and further indicated that each tau 1 site (residues 191-225) and the most carboxyl-terminal portion of the protein (residues 386-438) carries more than two abnormal phosphates. Ser-262 was also phosphorylated in a fraction of PHF-tau. Modifications other than phosphorylation, removal of the initiator methionine, and N alpha-acetylation at the amino terminus and deamidation at 2 asparaginyl residues were found in PHF-tau, but these modifications were also present in normal tau."xsd:string |
| http://purl.uniprot.org/citations/1512244 | http://purl.org/dc/terms/identifier | "doi:10.1016/s0021-9258(18)41890-x"xsd:string |
| http://purl.uniprot.org/citations/1512244 | http://purl.org/dc/terms/identifier | "doi:10.1016/s0021-9258(18)41890-x"xsd:string |
| http://purl.uniprot.org/citations/1512244 | http://purl.uniprot.org/core/author | "Hasegawa M."xsd:string |
| http://purl.uniprot.org/citations/1512244 | http://purl.uniprot.org/core/author | "Hasegawa M."xsd:string |
| http://purl.uniprot.org/citations/1512244 | http://purl.uniprot.org/core/author | "Suzuki M."xsd:string |
| http://purl.uniprot.org/citations/1512244 | http://purl.uniprot.org/core/author | "Suzuki M."xsd:string |
| http://purl.uniprot.org/citations/1512244 | http://purl.uniprot.org/core/author | "Titani K."xsd:string |
| http://purl.uniprot.org/citations/1512244 | http://purl.uniprot.org/core/author | "Titani K."xsd:string |
| http://purl.uniprot.org/citations/1512244 | http://purl.uniprot.org/core/author | "Ihara Y."xsd:string |
| http://purl.uniprot.org/citations/1512244 | http://purl.uniprot.org/core/author | "Ihara Y."xsd:string |
| http://purl.uniprot.org/citations/1512244 | http://purl.uniprot.org/core/author | "Takio K."xsd:string |
| http://purl.uniprot.org/citations/1512244 | http://purl.uniprot.org/core/author | "Takio K."xsd:string |
| http://purl.uniprot.org/citations/1512244 | http://purl.uniprot.org/core/author | "Morishima-Kawashima M."xsd:string |
| http://purl.uniprot.org/citations/1512244 | http://purl.uniprot.org/core/author | "Morishima-Kawashima M."xsd:string |
| http://purl.uniprot.org/citations/1512244 | http://purl.uniprot.org/core/date | "1992"xsd:gYear |
| http://purl.uniprot.org/citations/1512244 | http://purl.uniprot.org/core/date | "1992"xsd:gYear |
| http://purl.uniprot.org/citations/1512244 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/1512244 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/1512244 | http://purl.uniprot.org/core/pages | "17047-17054"xsd:string |
| http://purl.uniprot.org/citations/1512244 | http://purl.uniprot.org/core/pages | "17047-17054"xsd:string |
| http://purl.uniprot.org/citations/1512244 | http://purl.uniprot.org/core/title | "Protein sequence and mass spectrometric analyses of tau in the Alzheimer's disease brain."xsd:string |
| http://purl.uniprot.org/citations/1512244 | http://purl.uniprot.org/core/title | "Protein sequence and mass spectrometric analyses of tau in the Alzheimer's disease brain."xsd:string |