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Appears in Networks 4

In-Edges 8

a(CHEBI:Anatabine) decreases p(HGNC:MAPT, pmod(Ph, Ser, 396), pmod(Ph, Ser, 404)) View Subject | View Object

In both the detergent soluble and insoluble fractions of the brain and spinal cord homogenates of Tg Tau P301S mice, we found that tau phosphorylation was significantly reduced (T-tests, P<0.05) by the anatabine treatment for all the AD phosphorylated epitopes tested (Figure 6) DOI:10.4172/2168-975X.1000126

a(CHEBI:tanespimycin) decreases p(HGNC:MAPT, pmod(Ph, Ser, 396), pmod(Ph, Ser, 404)) View Subject | View Object

However, this issue is more complicated, as other work has shown that chemical inhibition of Hsp90 by 17-AAG and other inhibitors reduces cellular levels of two phospho- tau species, pS202/T205 and pS396/S404, both of which are relevant to AD pathogenesis [119]. PubMed:21882945

path(MESH:"Alzheimer Disease") positiveCorrelation p(HGNC:MAPT, pmod(Ph, Ser, 396), pmod(Ph, Ser, 404)) View Subject | View Object

However, this issue is more complicated, as other work has shown that chemical inhibition of Hsp90 by 17-AAG and other inhibitors reduces cellular levels of two phospho- tau species, pS202/T205 and pS396/S404, both of which are relevant to AD pathogenesis [119]. PubMed:21882945

p(HGNC:GSK3B) increases p(HGNC:MAPT, pmod(Ph, Ser, 396), pmod(Ph, Ser, 404)) View Subject | View Object

More- over, the unbound tau protein was hyperphospho- rylated and especially at the AD-2 epitope, e.g., an epitope shown to contain serine 396 and serine 404. PubMed:12428809

path(MESH:"Alzheimer Disease") association p(HGNC:MAPT, pmod(Ph, Ser, 396), pmod(Ph, Ser, 404)) View Subject | View Object

More- over, the unbound tau protein was hyperphospho- rylated and especially at the AD-2 epitope, e.g., an epitope shown to contain serine 396 and serine 404. PubMed:12428809

act(p(HGNC:SYK)) increases p(HGNC:MAPT, pmod(Ph, Ser, 396), pmod(Ph, Ser, 404)) View Subject | View Object

Altogether, these data suggest that only certain pathogenic forms of tau (MC1, Y18) promote Syk activation, whereas Syk activation appears to directly in- duce tau phosphorylation at Y18 and to indirectly regulate tau phosphorylation at multiple epitopes (S396/404, S202) as well as tau misfolding (MC1, TOC1). PubMed:28877763

p(HGNC:SYK) increases p(HGNC:MAPT, pmod(Ph, Ser, 396), pmod(Ph, Ser, 404)) View Subject | View Object

Interestingly, Syk up- regulation in SH-SY5Y cells leads to a significant in- crease (1.7-fold) in phosphorylated tau at Y18 (Fig. 14c, p < 0.01) and at S396/404 (Fig. 14d, 3-fold, p < 0.0001) compared to control cells. PubMed:28877763

Out-Edges 2

p(HGNC:MAPT, pmod(Ph, Ser, 396), pmod(Ph, Ser, 404)) positiveCorrelation path(MESH:"Alzheimer Disease") View Subject | View Object

However, this issue is more complicated, as other work has shown that chemical inhibition of Hsp90 by 17-AAG and other inhibitors reduces cellular levels of two phospho- tau species, pS202/T205 and pS396/S404, both of which are relevant to AD pathogenesis [119]. PubMed:21882945

p(HGNC:MAPT, pmod(Ph, Ser, 396), pmod(Ph, Ser, 404)) association path(MESH:"Alzheimer Disease") View Subject | View Object

More- over, the unbound tau protein was hyperphospho- rylated and especially at the AD-2 epitope, e.g., an epitope shown to contain serine 396 and serine 404. PubMed:12428809

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If you find BEL Commons useful in your work, please consider citing: Hoyt, C. T., Domingo-Fernández, D., & Hofmann-Apitius, M. (2018). BEL Commons: an environment for exploration and analysis of networks encoded in Biological Expression Language. Database, 2018(3), 1–11.