| pubmed-article:10509383 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10509383 | lifeskim:mentions | umls-concept:C0299212 | lld:lifeskim |
| pubmed-article:10509383 | lifeskim:mentions | umls-concept:C0276496 | lld:lifeskim |
| pubmed-article:10509383 | lifeskim:mentions | umls-concept:C1418985 | lld:lifeskim |
| pubmed-article:10509383 | lifeskim:mentions | umls-concept:C0599155 | lld:lifeskim |
| pubmed-article:10509383 | lifeskim:mentions | umls-concept:C1709694 | lld:lifeskim |
| pubmed-article:10509383 | lifeskim:mentions | umls-concept:C1704666 | lld:lifeskim |
| pubmed-article:10509383 | lifeskim:mentions | umls-concept:C1517892 | lld:lifeskim |
| pubmed-article:10509383 | lifeskim:mentions | umls-concept:C0208973 | lld:lifeskim |
| pubmed-article:10509383 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:10509383 | pubmed:dateCreated | 1999-12-2 | lld:pubmed |
| pubmed-article:10509383 | pubmed:abstractText | 1. Full-length form of human presenilin 1 (PS1) is processed and an N-terminal fragment (28 KD) and C-terminal fragment (19 KD) are generated. To elucidate the possible role of presenilin mutations in Alzheimer's disease (AD), the authors analyze the effects of AD-linked mutations on PS1 processing in cultured cells. 2. Complementary DNAs encoding genes for human PS1 harboring twenty-nine missense mutations linked with familial Alzheimer's disease (FAD) were introduced into PC12 cells. Human PS1 exogenously expressed in the cells was detected by immunoblotting using a monoclonal antibody that recognized the N-terminal region of human PS1. The amounts of full-length form (48 KD) and N-terminal fragment (28 KD) of PS1 was quantified by densitometrical analysis. 3. The ratio of the N-terminal fragment to total PS1 was reduced by twenty-nine mutations. The specific effects on PS1 processing varied according to mutation. 4. These results suggest that AD-linked missense mutations of PS1 are involved in neurodegeneration via inhibition of PS1 processing. | lld:pubmed |
| pubmed-article:10509383 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10509383 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10509383 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10509383 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10509383 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10509383 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10509383 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10509383 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10509383 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:10509383 | pubmed:issn | 0278-5846 | lld:pubmed |
| pubmed-article:10509383 | pubmed:author | pubmed-author:HondaTT | lld:pubmed |
| pubmed-article:10509383 | pubmed:author | pubmed-author:MurayamaMM | lld:pubmed |
| pubmed-article:10509383 | pubmed:author | pubmed-author:TakashimaAA | lld:pubmed |
| pubmed-article:10509383 | pubmed:author | pubmed-author:SudVV | lld:pubmed |
| pubmed-article:10509383 | pubmed:author | pubmed-author:MurayamaOO | lld:pubmed |
| pubmed-article:10509383 | pubmed:author | pubmed-author:NihonmatsuNN | lld:pubmed |
| pubmed-article:10509383 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10509383 | pubmed:volume | 23 | lld:pubmed |
| pubmed-article:10509383 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10509383 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10509383 | pubmed:pagination | 905-13 | lld:pubmed |
| pubmed-article:10509383 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:10509383 | pubmed:meshHeading | pubmed-meshheading:10509383... | lld:pubmed |
| pubmed-article:10509383 | pubmed:meshHeading | pubmed-meshheading:10509383... | lld:pubmed |
| pubmed-article:10509383 | pubmed:meshHeading | pubmed-meshheading:10509383... | lld:pubmed |
| pubmed-article:10509383 | pubmed:meshHeading | pubmed-meshheading:10509383... | lld:pubmed |
| pubmed-article:10509383 | pubmed:meshHeading | pubmed-meshheading:10509383... | lld:pubmed |
| pubmed-article:10509383 | pubmed:meshHeading | pubmed-meshheading:10509383... | lld:pubmed |
| pubmed-article:10509383 | pubmed:meshHeading | pubmed-meshheading:10509383... | lld:pubmed |
| pubmed-article:10509383 | pubmed:meshHeading | pubmed-meshheading:10509383... | lld:pubmed |
| pubmed-article:10509383 | pubmed:meshHeading | pubmed-meshheading:10509383... | lld:pubmed |
| pubmed-article:10509383 | pubmed:meshHeading | pubmed-meshheading:10509383... | lld:pubmed |
| pubmed-article:10509383 | pubmed:meshHeading | pubmed-meshheading:10509383... | lld:pubmed |
| pubmed-article:10509383 | pubmed:meshHeading | pubmed-meshheading:10509383... | lld:pubmed |
| pubmed-article:10509383 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:10509383 | pubmed:articleTitle | Twenty-nine missense mutations linked with familial Alzheimer's disease alter the processing of presenilin 1. | lld:pubmed |
| pubmed-article:10509383 | pubmed:affiliation | Laboratory for Alzheimer's Disease, Brain Science Institute, RIKEN, Saitama, Japan. | lld:pubmed |
| pubmed-article:10509383 | pubmed:publicationType | Journal Article | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10509383 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10509383 | lld:pubmed |
