p(HGNC:CDK1)
This result confirms previous findings that T231 is an important Cdc2 phosphorylation site in tau, and is also consistent with Pin1 binding mitotically pTau (Fig. 1a) and being sequestered on to PHFs in AD brains, where Cdc2 is upregulated (Fig. 3). PubMed:10391244
In Alzheimer disease, 66 genes were identified that are also modulated by Protandim at the gene expression level. Of these 66 genes, the first 43 of them (65%) were regulated by Protandim in the opposing direction to that taken by the Alzheimer disease process. The beneficial effect of Protandim is further supported by the fact that of the 10 gene products currently targeted by drug therapies, eight of them are modulated by Protandim in the same direction that is proposed to be beneficial and caused by the drug. PubMed:22020111
In Alzheimer disease, 66 genes were identified that are also modulated by Protandim at the gene expression level. Of these 66 genes, the first 43 of them (65%) were regulated by Protandim in the opposing direction to that taken by the Alzheimer disease process. The beneficial effect of Protandim is further supported by the fact that of the 10 gene products currently targeted by drug therapies, eight of them are modulated by Protandim in the same direction that is proposed to be beneficial and caused by the drug. PubMed:22020111
This result confirms previous findings that T231 is an important Cdc2 phosphorylation site in tau, and is also consistent with Pin1 binding mitotically pTau (Fig. 1a) and being sequestered on to PHFs in AD brains, where Cdc2 is upregulated (Fig. 3). PubMed:10391244
This result confirms previous findings that T231 is an important Cdc2 phosphorylation site in tau, and is also consistent with Pin1 binding mitotically pTau (Fig. 1a) and being sequestered on to PHFs in AD brains, where Cdc2 is upregulated (Fig. 3). PubMed:10391244
Among the specific “proline-dependent” kinases that can phosphorylate protein tau at dif- ferent sites in vitro, special attention is dedicated to glycogen-synthase kinase-3β (GSK-3β) (Michel et al., 1998), mitogen-activated protein kinase (MAPK) (Drewes et al., 1992), stress-activated protein kinases (SAPKs) (Goedert et al., 1997) and cyclin-dependent kinases (CDKs) including cdc2 and cdk5 (Baumann et al., 1993; Patrick et al., 1999). PubMed:12428809
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