Statements in which the resource exists.
SubjectPredicateObjectContext
pubmed-article:11432849rdf:typepubmed:Citationlld:pubmed
pubmed-article:11432849lifeskim:mentionsumls-concept:C0033382lld:lifeskim
pubmed-article:11432849lifeskim:mentionsumls-concept:C0872078lld:lifeskim
pubmed-article:11432849lifeskim:mentionsumls-concept:C0441655lld:lifeskim
pubmed-article:11432849lifeskim:mentionsumls-concept:C1412365lld:lifeskim
pubmed-article:11432849lifeskim:mentionsumls-concept:C1514562lld:lifeskim
pubmed-article:11432849lifeskim:mentionsumls-concept:C0439855lld:lifeskim
pubmed-article:11432849lifeskim:mentionsumls-concept:C1522492lld:lifeskim
pubmed-article:11432849lifeskim:mentionsumls-concept:C0379528lld:lifeskim
pubmed-article:11432849pubmed:issue35lld:pubmed
pubmed-article:11432849pubmed:dateCreated2001-8-27lld:pubmed
pubmed-article:11432849pubmed:abstractTextMutations in presenilin (PS) genes cause early-onset familial Alzheimer's disease by increasing production of the amyloidogenic form of amyloid beta peptides ending at residue 42 (Abeta42). PS is an evolutionarily conserved multipass transmembrane protein, and all known PS proteins contain a proline-alanine-leucine-proline (PALP) motif starting at proline (P) 414 (amino acid numbering based on human PS2) at the C terminus. Furthermore, missense mutations that replace the first proline of PALP with leucine (P414L) lead to a loss-of-function of PS in Drosophila melanogaster and Caenorhabditis elegans. To elucidate the roles of the PALP motif in PS structure and function, we analyzed neuro2a as well as PS1/2 null fibroblast cell lines transfected with human PS harboring mutations at the PALP motif. P414L mutation in PS2 (and its equivalent in PS1) abrogated stabilization, high molecular weight complex formation, and entry to Golgi/trans-Golgi network of PS proteins, resulting in failure of Abeta42 overproduction on familial Alzheimer's disease mutant basis as well as of site-3 cleavage of Notch. These data suggest that the first proline of the PALP motif plays a crucial role in the stabilization and formation of the high molecular weight complex of PS, the latter being the active form with intramembrane proteolytic activities.lld:pubmed
pubmed-article:11432849pubmed:languageenglld:pubmed
pubmed-article:11432849pubmed:journalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:11432849pubmed:citationSubsetIMlld:pubmed
pubmed-article:11432849pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:11432849pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:11432849pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:11432849pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:11432849pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:11432849pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:11432849pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:11432849pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:11432849pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:11432849pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:11432849pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:11432849pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:11432849pubmed:statusMEDLINElld:pubmed
pubmed-article:11432849pubmed:monthAuglld:pubmed
pubmed-article:11432849pubmed:issn0021-9258lld:pubmed
pubmed-article:11432849pubmed:authorpubmed-author:TomitaTTlld:pubmed
pubmed-article:11432849pubmed:authorpubmed-author:TakasugiNNlld:pubmed
pubmed-article:11432849pubmed:authorpubmed-author:IwatsuboTTlld:pubmed
pubmed-article:11432849pubmed:authorpubmed-author:TakikawaRRlld:pubmed
pubmed-article:11432849pubmed:authorpubmed-author:MorohashiYYlld:pubmed
pubmed-article:11432849pubmed:authorpubmed-author:De StrooperBBlld:pubmed
pubmed-article:11432849pubmed:authorpubmed-author:WatabikiTTlld:pubmed
pubmed-article:11432849pubmed:authorpubmed-author:KopanRRlld:pubmed
pubmed-article:11432849pubmed:issnTypePrintlld:pubmed
pubmed-article:11432849pubmed:day31lld:pubmed
pubmed-article:11432849pubmed:volume276lld:pubmed
pubmed-article:11432849pubmed:ownerNLMlld:pubmed
pubmed-article:11432849pubmed:authorsCompleteYlld:pubmed
pubmed-article:11432849pubmed:pagination33273-81lld:pubmed
pubmed-article:11432849pubmed:dateRevised2009-11-19lld:pubmed
pubmed-article:11432849pubmed:meshHeadingpubmed-meshheading:11432849...lld:pubmed
pubmed-article:11432849pubmed:meshHeadingpubmed-meshheading:11432849...lld:pubmed
pubmed-article:11432849pubmed:meshHeadingpubmed-meshheading:11432849...lld:pubmed
pubmed-article:11432849pubmed:meshHeadingpubmed-meshheading:11432849...lld:pubmed
pubmed-article:11432849pubmed:meshHeadingpubmed-meshheading:11432849...lld:pubmed
pubmed-article:11432849pubmed:meshHeadingpubmed-meshheading:11432849...lld:pubmed
pubmed-article:11432849pubmed:meshHeadingpubmed-meshheading:11432849...lld:pubmed
pubmed-article:11432849pubmed:meshHeadingpubmed-meshheading:11432849...lld:pubmed
pubmed-article:11432849pubmed:meshHeadingpubmed-meshheading:11432849...lld:pubmed
pubmed-article:11432849pubmed:meshHeadingpubmed-meshheading:11432849...lld:pubmed
pubmed-article:11432849pubmed:meshHeadingpubmed-meshheading:11432849...lld:pubmed
pubmed-article:11432849pubmed:meshHeadingpubmed-meshheading:11432849...lld:pubmed
pubmed-article:11432849pubmed:meshHeadingpubmed-meshheading:11432849...lld:pubmed
pubmed-article:11432849pubmed:meshHeadingpubmed-meshheading:11432849...lld:pubmed
pubmed-article:11432849pubmed:meshHeadingpubmed-meshheading:11432849...lld:pubmed
pubmed-article:11432849pubmed:meshHeadingpubmed-meshheading:11432849...lld:pubmed
pubmed-article:11432849pubmed:meshHeadingpubmed-meshheading:11432849...lld:pubmed
pubmed-article:11432849pubmed:meshHeadingpubmed-meshheading:11432849...lld:pubmed
pubmed-article:11432849pubmed:meshHeadingpubmed-meshheading:11432849...lld:pubmed
pubmed-article:11432849pubmed:meshHeadingpubmed-meshheading:11432849...lld:pubmed
pubmed-article:11432849pubmed:meshHeadingpubmed-meshheading:11432849...lld:pubmed
pubmed-article:11432849pubmed:meshHeadingpubmed-meshheading:11432849...lld:pubmed
pubmed-article:11432849pubmed:meshHeadingpubmed-meshheading:11432849...lld:pubmed
pubmed-article:11432849pubmed:meshHeadingpubmed-meshheading:11432849...lld:pubmed
pubmed-article:11432849pubmed:meshHeadingpubmed-meshheading:11432849...lld:pubmed
pubmed-article:11432849pubmed:year2001lld:pubmed
pubmed-article:11432849pubmed:articleTitleThe first proline of PALP motif at the C terminus of presenilins is obligatory for stabilization, complex formation, and gamma-secretase activities of presenilins.lld:pubmed
pubmed-article:11432849pubmed:affiliationDepartment of Neuropathology and Neuroscience, Graduate School of Pharmaceutical Sciences, University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan.lld:pubmed
pubmed-article:11432849pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:11432849pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:11432849lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:11432849lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:11432849lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:11432849lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:11432849lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:11432849lld:pubmed