| http://purl.uniprot.org/citations/14970212 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/14970212 | http://www.w3.org/2000/01/rdf-schema#comment | "Amyloid precursor protein (APP) processing is of major interest in Alzheimer's disease research, since sequential cleavages by beta- and gamma-secretase lead to the formation of the 4-kDa amyloid Abeta protein peptide that accumulates in Alzheimer's disease brain. The processing of APP involves proteolytic conversion by different secretases leading to alpha-, beta-, gamma-, delta-, and epsilon-cleavages. Since modulation of these cleavages represents a rational therapeutic approach to control amyloid formation, its interference with the processing of the members of the APP gene family is of considerable importance. By using C-terminally tagged constructs of APLP-1 and APLP-2 and the untagged proteins, we have characterized their proteolytic C-terminal fragments produced in stably transfected SH-SY5Y cells. Pharmacological manipulation with specific protease inhibitors revealed that both homologues are processed by alpha- and gamma-secretase-like cleavages, and that their intracellular domains can be released by cleavage at epsilon-sites. APLP-2 processing appears to be the most elaborate and to involve alternative cleavage sites. We show that APLP-1 is the only member of the APP gene family for which processing can be influenced by N-glycosylation. Additionally, we were able to detect p3-like fragments of APLP-1 and p3-like and Abeta-like fragments of APLP-2 in the media of stably transfected SH-SY5Y cells."xsd:string |
| http://purl.uniprot.org/citations/14970212 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m311601200"xsd:string |
| http://purl.uniprot.org/citations/14970212 | http://purl.uniprot.org/core/author | "Beyreuther K."xsd:string |
| http://purl.uniprot.org/citations/14970212 | http://purl.uniprot.org/core/author | "Eggert S."xsd:string |
| http://purl.uniprot.org/citations/14970212 | http://purl.uniprot.org/core/author | "Evin G."xsd:string |
| http://purl.uniprot.org/citations/14970212 | http://purl.uniprot.org/core/author | "Masters C.L."xsd:string |
| http://purl.uniprot.org/citations/14970212 | http://purl.uniprot.org/core/author | "Paliga K."xsd:string |
| http://purl.uniprot.org/citations/14970212 | http://purl.uniprot.org/core/author | "Weidemann A."xsd:string |
| http://purl.uniprot.org/citations/14970212 | http://purl.uniprot.org/core/author | "Soba P."xsd:string |
| http://purl.uniprot.org/citations/14970212 | http://purl.uniprot.org/core/date | "2004"xsd:gYear |
| http://purl.uniprot.org/citations/14970212 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/14970212 | http://purl.uniprot.org/core/pages | "18146-18156"xsd:string |
| http://purl.uniprot.org/citations/14970212 | http://purl.uniprot.org/core/title | "The proteolytic processing of the amyloid precursor protein gene family members APLP-1 and APLP-2 involves alpha-, beta-, gamma-, and epsilon-like cleavages: modulation of APLP-1 processing by n-glycosylation."xsd:string |
| http://purl.uniprot.org/citations/14970212 | http://purl.uniprot.org/core/volume | "279"xsd:string |
| http://purl.uniprot.org/citations/14970212 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/14970212 |
| http://purl.uniprot.org/citations/14970212 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/14970212 |
| http://purl.uniprot.org/uniprot/#_A0A140VJE9-mappedCitation-14970212 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/14970212 |
| http://purl.uniprot.org/uniprot/#_A4UCT6-mappedCitation-14970212 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/14970212 |
| http://purl.uniprot.org/uniprot/#_B2R5S2-mappedCitation-14970212 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/14970212 |
| http://purl.uniprot.org/uniprot/#_B4DTV1-mappedCitation-14970212 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/14970212 |
| http://purl.uniprot.org/uniprot/#_B7Z4G8-mappedCitation-14970212 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/14970212 |
| http://purl.uniprot.org/uniprot/#_B7Z4Q2-mappedCitation-14970212 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/14970212 |
| http://purl.uniprot.org/uniprot/#_B4DKY3-mappedCitation-14970212 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/14970212 |
| http://purl.uniprot.org/uniprot/#_B4E3I5-mappedCitation-14970212 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/14970212 |