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regulated
3 studies tagged regulated, dated 2003-04-18 to 2011-01-13. Bibliography: BibTeX (.bib) · RIS (.ris)
Newest in this topic
- Effect of glycogen synthase kinase 3 β-mediated presenilin 1 phosphorylation on amyloid β production is negatively regulated by insulin receptor cleavage 2011-01-13
- APP processing is regulated by cytoplasmic phosphorylation 2003-10-01
- Notch and Presenilin: regulated intramembrane proteolysis links development and degeneration 2003-04-18
Studies
3 studies carry this tag.
Date range
2003 to 2011
Top journals
- Annual review of neuroscience 1
- Neuroscience 1
- The Journal of cell biology 1
Newest first, then by address. Each study has a usefulness score out of 100 (rubric version 4.0); tap a score to see what makes it up. Tags were assigned automatically from each study's title and summary. The same studies as a filter in the library.
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Presenilin 1 (PS1), a causative molecule of familial Alzheimer's disease (AD), is known to be an unprimed substrate of glycogen synthase kinase 3 β (GSK3β) [Twomey and McCarthy (2006) FEBS Lett 580:4015-4020] and is phosphorylated at serine 353, 357 residues in its cytoplasmic loop region [Kirschenbaum et al. (2001) J Biol Chem 276:7366-7375].
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Amyloid-beta peptide (Abeta) aggregate in senile plaque is a key characteristic of Alzheimer's disease (AD).
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Intensive studies of three proteins--Presenilin, Notch, and the amyloid precursor protein (APP)--have led to the recognition of a direct intersection between early development and late-life neurodegeneration.