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glycogen-synthase
4 studies tagged glycogen-synthase, dated 1998-04-01 to 2011-03-22. Bibliography: BibTeX (.bib) · RIS (.ris)
Newest in this topic
- Valproate reduces tau phosphorylation via cyclin-dependent kinase 5 and glycogen synthase kinase 3 signaling pathways 2011-03-22
- 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
- Presenilin 1 associates with glycogen synthase kinase-3beta and its substrate tau 1998-08-01
Studies
4 studies carry this tag.
Date range
1998 to 2011
Top journals
- Biochimica et biophysica acta 1
- Brain research bulletin 1
- Neuroscience 1
- Proceedings of the National Academy of Sciences of the United States of America 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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Valproate (VPA) is a widely used anticonvulsant and mood-stabilizing drug.
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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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Families bearing mutations in the presenilin 1 (PS1) gene develop Alzheimer's disease.
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One of the histopathological markers in Alzheimer's disease is the accumulation of hyperphosphorylated tau in neurons called neurofibrillary tangles (NFT) composing paired helical filaments (PHF).