pubmed-article:14576165 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:14576165 | lifeskim:mentions | umls-concept:C0162638 | lld:lifeskim |
pubmed-article:14576165 | lifeskim:mentions | umls-concept:C0205145 | lld:lifeskim |
pubmed-article:14576165 | lifeskim:mentions | umls-concept:C0524637 | lld:lifeskim |
pubmed-article:14576165 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
pubmed-article:14576165 | lifeskim:mentions | umls-concept:C0010656 | lld:lifeskim |
pubmed-article:14576165 | lifeskim:mentions | umls-concept:C0299212 | lld:lifeskim |
pubmed-article:14576165 | lifeskim:mentions | umls-concept:C1418985 | lld:lifeskim |
pubmed-article:14576165 | lifeskim:mentions | umls-concept:C0449258 | lld:lifeskim |
pubmed-article:14576165 | lifeskim:mentions | umls-concept:C1514570 | lld:lifeskim |
pubmed-article:14576165 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
pubmed-article:14576165 | pubmed:issue | 3 | lld:pubmed |
pubmed-article:14576165 | pubmed:dateCreated | 2004-1-12 | lld:pubmed |
pubmed-article:14576165 | pubmed:abstractText | The Alzheimer's disease-associated presenilin (PS) 1 is intimately involved in gamma-secretase cleavage of beta-amyloid precursor protein and other proteins. In addition, PS1 plays a role in beta-catenin signaling and in the regulation of apoptosis. Here we demonstrate that phosphorylation of PS1 is regulated by two independent signaling pathways involving protein kinase (PK) A and PKC and that both kinases can directly phosphorylate the large hydrophilic domain of PS1 in vitro and in cultured cells. A phosphorylation site at serine residue 346 was identified that is selectively phosphorylated by PKC but not by PKA. This site is localized within a recognition motif for caspases, and phosphorylation strongly inhibits proteolytic processing of PS1 by caspase activity during apoptosis. Moreover, PS1 phosphorylation reduces the progression of apoptosis. Our data indicate that phosphorylation/dephosphorylation at the caspase recognition site provides a mechanism to reversibly regulate properties of PS1 in apoptosis. | lld:pubmed |
pubmed-article:14576165 | pubmed:language | eng | lld:pubmed |
pubmed-article:14576165 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14576165 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:14576165 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14576165 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14576165 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14576165 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14576165 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14576165 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14576165 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14576165 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14576165 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14576165 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:14576165 | pubmed:month | Jan | lld:pubmed |
pubmed-article:14576165 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:14576165 | pubmed:author | pubmed-author:FluhrerRegina... | lld:pubmed |
pubmed-article:14576165 | pubmed:author | pubmed-author:WalterJochenJ | lld:pubmed |
pubmed-article:14576165 | pubmed:author | pubmed-author:HaassChristia... | lld:pubmed |
pubmed-article:14576165 | pubmed:author | pubmed-author:FriedleinArno... | lld:pubmed |
pubmed-article:14576165 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:14576165 | pubmed:day | 16 | lld:pubmed |
pubmed-article:14576165 | pubmed:volume | 279 | lld:pubmed |
pubmed-article:14576165 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:14576165 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:14576165 | pubmed:pagination | 1585-93 | lld:pubmed |
pubmed-article:14576165 | pubmed:dateRevised | 2011-11-2 | lld:pubmed |
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pubmed-article:14576165 | pubmed:meshHeading | pubmed-meshheading:14576165... | lld:pubmed |
pubmed-article:14576165 | pubmed:year | 2004 | lld:pubmed |
pubmed-article:14576165 | pubmed:articleTitle | Phosphorylation of presenilin 1 at the caspase recognition site regulates its proteolytic processing and the progression of apoptosis. | lld:pubmed |
pubmed-article:14576165 | pubmed:affiliation | Department of Neurology, University of Bonn, Sigmund-Freud-Strasse 25, 53127 Bonn, Germany. | lld:pubmed |
pubmed-article:14576165 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:14576165 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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