Loading...
Please wait, while we are loading the content...
Similar Documents
Presenilin, Notch, and the genesis and treatment of Alzheimer's disease.
| Content Provider | Semantic Scholar |
|---|---|
| Author | Selkoe, Dennis J. |
| Copyright Year | 2001 |
| Abstract | Elucidation of the proteolytic processing of the amyloid beta-protein precursor (APP) has revealed that one of the two proteases (gamma-secretase) that cleave APP to release amyloid beta-protein (Abeta) is likely to be presenilin. Presenilin also mediates the gamma-secretase-like cleavage of Notch receptors to enable signaling by their cytoplasmic domains. Therefore, APP and Notch may be the first identified substrates of a unique intramembranous aspartyl protease that has presenilin as its active-site component. In view of the evidence for a central role of cerebral build-up of Abeta in the pathogenesis of Alzheimer's disease, this disorder appears to have arisen in the human population as a late-life consequence of the conservation of a critical developmental pathway. |
| Starting Page | 84 |
| Ending Page | 91 |
| Page Count | 8 |
| File Format | PDF HTM / HTML |
| Alternate Webpage(s) | http://www.pnas.org/content/98/20/11039.full.pdf |
| PubMed reference number | 11572965v1 |
| Volume Number | 98 |
| Issue Number | 20 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Language | English |
| Access Restriction | Open |
| Subject Keyword | Alzheimer's Disease Amyloid beta-Peptides Amyloid beta-Protein Precursor Aspartic Acid Proteases Auditory Perceptual Disorders Endopeptidases Gonadotropin-Releasing Hormone Receptor Presenilins Receptors, Notch gamma-Secretase secretase |
| Content Type | Text |
| Resource Type | Article |
