pubmed-article:10801872 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:10801872 | lifeskim:mentions | umls-concept:C1330957 | lld:lifeskim |
pubmed-article:10801872 | lifeskim:mentions | umls-concept:C1454853 | lld:lifeskim |
pubmed-article:10801872 | lifeskim:mentions | umls-concept:C1254042 | lld:lifeskim |
pubmed-article:10801872 | lifeskim:mentions | umls-concept:C0596311 | lld:lifeskim |
pubmed-article:10801872 | lifeskim:mentions | umls-concept:C1875696 | lld:lifeskim |
pubmed-article:10801872 | pubmed:issue | 40 | lld:pubmed |
pubmed-article:10801872 | pubmed:dateCreated | 2000-10-23 | lld:pubmed |
pubmed-article:10801872 | pubmed:abstractText | Amyloid beta-peptide is generated by two sequential proteolytic cleavages mediated by beta-secretase (BACE) and gamma-secretase. BACE was recently identified as a membrane-associated aspartyl protease. We have now analyzed the maturation and pro-peptide cleavage of BACE. Pulse-chase experiments revealed that BACE is post-translationally modified during transport to the cell surface, which can be monitored by a significant increase in the molecular mass. The increase in molecular mass is caused by complex N-glycosylation. Treatment with tunicamycin and N-glycosidase F led to a BACE derivative with a molecular weight corresponding to an unmodified version. In contrast, the mature form of BACE was resistant to endoglycosidase H treatment. The cytoplasmic tail of BACE was required for efficient maturation and trafficking through the Golgi; a BACE variant lacking the cytoplasmic tail undergoes inefficient maturation. In contrast a soluble BACE variant that does not contain a membrane anchor matured more rapidly than full-length BACE. Pro-BACE was predominantly located within the endoplasmic reticulum. Pro-peptide cleavage occurred immediately before full maturation and trafficking through the Golgi. | lld:pubmed |
pubmed-article:10801872 | pubmed:language | eng | lld:pubmed |
pubmed-article:10801872 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10801872 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:10801872 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10801872 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:10801872 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10801872 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10801872 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10801872 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10801872 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10801872 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10801872 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10801872 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:10801872 | pubmed:month | Oct | lld:pubmed |
pubmed-article:10801872 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:10801872 | pubmed:author | pubmed-author:SteinerHH | lld:pubmed |
pubmed-article:10801872 | pubmed:author | pubmed-author:MeyerCC | lld:pubmed |
pubmed-article:10801872 | pubmed:author | pubmed-author:KaiserHH | lld:pubmed |
pubmed-article:10801872 | pubmed:author | pubmed-author:WalterJJ | lld:pubmed |
pubmed-article:10801872 | pubmed:author | pubmed-author:WillerHH | lld:pubmed |
pubmed-article:10801872 | pubmed:author | pubmed-author:MulthaupGG | lld:pubmed |
pubmed-article:10801872 | pubmed:author | pubmed-author:HaassCC | lld:pubmed |
pubmed-article:10801872 | pubmed:author | pubmed-author:CapellAA | lld:pubmed |
pubmed-article:10801872 | pubmed:author | pubmed-author:LammichSS | lld:pubmed |
pubmed-article:10801872 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:10801872 | pubmed:day | 6 | lld:pubmed |
pubmed-article:10801872 | pubmed:volume | 275 | lld:pubmed |
pubmed-article:10801872 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:10801872 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:10801872 | pubmed:pagination | 30849-54 | lld:pubmed |
pubmed-article:10801872 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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pubmed-article:10801872 | pubmed:year | 2000 | lld:pubmed |
pubmed-article:10801872 | pubmed:articleTitle | Maturation and pro-peptide cleavage of beta-secretase. | lld:pubmed |
pubmed-article:10801872 | pubmed:affiliation | Adolf Butenandt-Institute, Department of Biochemistry, Laboratory for Alzheimer's Disease Research, Ludwig-Maximilians-University, 80336 Munich, Germany. | lld:pubmed |
pubmed-article:10801872 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:10801872 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
entrez-gene:23621 | entrezgene:pubmed | pubmed-article:10801872 | lld:entrezgene |
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