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Newest in this topic

  1. 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
  2. APP processing is regulated by cytoplasmic phosphorylation 2003-10-01
  3. 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.

  1. 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].

  2. APP processing is regulated by cytoplasmic phosphorylation

    ✓ Peer-reviewed alzhub usefulness score 40 out of 100. The Journal of cell biology 2003-10-01 Risk genes beyond APOE

    Amyloid-beta peptide (Abeta) aggregate in senile plaque is a key characteristic of Alzheimer's disease (AD).

  3. Notch and Presenilin: regulated intramembrane proteolysis links development and degeneration

    ✓ Peer-reviewed alzhub usefulness score 36 out of 100. Annual review of neuroscience 2003-04-18 Risk genes beyond APOE

    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.

All topic tags with their study counts