pubmed-article:14970212 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:14970212 | lifeskim:mentions | umls-concept:C0086282 | lld:lifeskim |
pubmed-article:14970212 | lifeskim:mentions | umls-concept:C1330957 | lld:lifeskim |
pubmed-article:14970212 | lifeskim:mentions | umls-concept:C0085151 | lld:lifeskim |
pubmed-article:14970212 | lifeskim:mentions | umls-concept:C1514570 | lld:lifeskim |
pubmed-article:14970212 | lifeskim:mentions | umls-concept:C0596311 | lld:lifeskim |
pubmed-article:14970212 | lifeskim:mentions | umls-concept:C1709694 | lld:lifeskim |
pubmed-article:14970212 | lifeskim:mentions | umls-concept:C1709059 | lld:lifeskim |
pubmed-article:14970212 | lifeskim:mentions | umls-concept:C1314939 | lld:lifeskim |
pubmed-article:14970212 | lifeskim:mentions | umls-concept:C1517488 | lld:lifeskim |
pubmed-article:14970212 | pubmed:issue | 18 | lld:pubmed |
pubmed-article:14970212 | pubmed:dateCreated | 2004-4-26 | lld:pubmed |
pubmed-article:14970212 | pubmed:abstractText | 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. | lld:pubmed |
pubmed-article:14970212 | pubmed:language | eng | lld:pubmed |
pubmed-article:14970212 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14970212 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:14970212 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14970212 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14970212 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14970212 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14970212 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14970212 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14970212 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14970212 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14970212 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14970212 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14970212 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:14970212 | pubmed:month | Apr | lld:pubmed |
pubmed-article:14970212 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:14970212 | pubmed:author | pubmed-author:BeyreutherKon... | lld:pubmed |
pubmed-article:14970212 | pubmed:author | pubmed-author:MastersColin... | lld:pubmed |
pubmed-article:14970212 | pubmed:author | pubmed-author:WeidemannAndr... | lld:pubmed |
pubmed-article:14970212 | pubmed:author | pubmed-author:EggertSimoneS | lld:pubmed |
pubmed-article:14970212 | pubmed:author | pubmed-author:PaligaKrzyszt... | lld:pubmed |
pubmed-article:14970212 | pubmed:author | pubmed-author:SobaPeterP | lld:pubmed |
pubmed-article:14970212 | pubmed:author | pubmed-author:EvinGenevieve... | lld:pubmed |
pubmed-article:14970212 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:14970212 | pubmed:day | 30 | lld:pubmed |
pubmed-article:14970212 | pubmed:volume | 279 | lld:pubmed |
pubmed-article:14970212 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:14970212 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:14970212 | pubmed:pagination | 18146-56 | lld:pubmed |
pubmed-article:14970212 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
pubmed-article:14970212 | pubmed:meshHeading | pubmed-meshheading:14970212... | lld:pubmed |
pubmed-article:14970212 | pubmed:meshHeading | pubmed-meshheading:14970212... | lld:pubmed |
pubmed-article:14970212 | pubmed:meshHeading | pubmed-meshheading:14970212... | lld:pubmed |
pubmed-article:14970212 | pubmed:meshHeading | pubmed-meshheading:14970212... | lld:pubmed |
pubmed-article:14970212 | pubmed:meshHeading | pubmed-meshheading:14970212... | lld:pubmed |
pubmed-article:14970212 | pubmed:meshHeading | pubmed-meshheading:14970212... | lld:pubmed |
pubmed-article:14970212 | pubmed:meshHeading | pubmed-meshheading:14970212... | lld:pubmed |
pubmed-article:14970212 | pubmed:meshHeading | pubmed-meshheading:14970212... | lld:pubmed |
pubmed-article:14970212 | pubmed:meshHeading | pubmed-meshheading:14970212... | lld:pubmed |
pubmed-article:14970212 | pubmed:meshHeading | pubmed-meshheading:14970212... | lld:pubmed |
pubmed-article:14970212 | pubmed:meshHeading | pubmed-meshheading:14970212... | lld:pubmed |
pubmed-article:14970212 | pubmed:meshHeading | pubmed-meshheading:14970212... | lld:pubmed |
pubmed-article:14970212 | pubmed:meshHeading | pubmed-meshheading:14970212... | lld:pubmed |
pubmed-article:14970212 | pubmed:meshHeading | pubmed-meshheading:14970212... | lld:pubmed |
pubmed-article:14970212 | pubmed:year | 2004 | lld:pubmed |
pubmed-article:14970212 | pubmed:articleTitle | 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. | lld:pubmed |
pubmed-article:14970212 | pubmed:affiliation | Zentrum für Molekulare Biologie Heidelberg, ZMBH, INF 282, 69120 Heidelberg, Germany. s.eggert@zmbh.uni-heidelberg.de | lld:pubmed |
pubmed-article:14970212 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:14970212 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
entrez-gene:333 | entrezgene:pubmed | pubmed-article:14970212 | lld:entrezgene |
entrez-gene:334 | entrezgene:pubmed | pubmed-article:14970212 | lld:entrezgene |
http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:14970212 | lld:entrezgene |
http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:14970212 | lld:entrezgene |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:14970212 | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:14970212 | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:14970212 | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:14970212 | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:14970212 | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:14970212 | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:14970212 | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:14970212 | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:14970212 | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:14970212 | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:14970212 | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:14970212 | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:14970212 | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:14970212 | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:14970212 | lld:pubmed |