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Tau Modifications v1.9.5

Tau Modifications Sections of NESTOR

In-Edges 6

act(p(MGI:Glp1r)) decreases p(MGI:Mapt, pmod(HBP:hyperphosphorylation)) View Subject | View Object

In this study, we demonstrated that GLP-1RA could inhibit oxidative stress and repair mitochondrial damage in addition to decreasing tau hyperphosphorylation in PC12 cells treated with AGEs. Importantly, we first observed AGEs in the circulatory system could induce tau hyperphosphorylation after we injected AGEs (1μg/kg bodyweight) into the mice tail vein. We found GLP-1RA could promote mitochondrial biogenesis and antioxidant system via regulating peroxisome proliferator-activated receptor γ coactivator 1α (PGC-1α) signaling pathway in vivo besides down-regulating the activity of glycogen synthase kinase 3β (GSK-3β) to reverse tau hyperphosphorylation directly. PubMed:25987199

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p(MGI:Ppp1ca) negativeCorrelation p(MGI:Mapt, pmod(HBP:hyperphosphorylation)) View Subject | View Object

We found strong Tau hyperphosphorylation in brain samples from R6/2 and 140CAG Tg knock-in, associated with a significant reduction in the levels of Tau phosphatases (PP1, PP2A and PP2B), with no apparent involvement of major Tau kinases. PubMed:25143394

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p(MGI:Ppp1cb) negativeCorrelation p(MGI:Mapt, pmod(HBP:hyperphosphorylation)) View Subject | View Object

We found strong Tau hyperphosphorylation in brain samples from R6/2 and 140CAG Tg knock-in, associated with a significant reduction in the levels of Tau phosphatases (PP1, PP2A and PP2B), with no apparent involvement of major Tau kinases. PubMed:25143394

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p(MGI:Ppp2ca) negativeCorrelation p(MGI:Mapt, pmod(HBP:hyperphosphorylation)) View Subject | View Object

We found strong Tau hyperphosphorylation in brain samples from R6/2 and 140CAG Tg knock-in, associated with a significant reduction in the levels of Tau phosphatases (PP1, PP2A and PP2B), with no apparent involvement of major Tau kinases. PubMed:25143394

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p(RGD:Ppp2ca) negativeCorrelation p(MGI:Mapt, pmod(HBP:hyperphosphorylation)) View Subject | View Object

PP2A expression decreased, whereas, PP1 and PP5 expression increased in lead-exposed rats. These results demonstrate that early postnatal exposure to lead decrease PP2A expression and induce tau hyperphosphorylation at several serine and threonine residues. PubMed:23134599

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Out-Edges 4

p(MGI:Mapt, pmod(HBP:hyperphosphorylation)) negativeCorrelation p(MGI:Ppp1ca) View Subject | View Object

We found strong Tau hyperphosphorylation in brain samples from R6/2 and 140CAG Tg knock-in, associated with a significant reduction in the levels of Tau phosphatases (PP1, PP2A and PP2B), with no apparent involvement of major Tau kinases. PubMed:25143394

Appears in Networks:

p(MGI:Mapt, pmod(HBP:hyperphosphorylation)) negativeCorrelation p(MGI:Ppp2ca) View Subject | View Object

We found strong Tau hyperphosphorylation in brain samples from R6/2 and 140CAG Tg knock-in, associated with a significant reduction in the levels of Tau phosphatases (PP1, PP2A and PP2B), with no apparent involvement of major Tau kinases. PubMed:25143394

Appears in Networks:

p(MGI:Mapt, pmod(HBP:hyperphosphorylation)) negativeCorrelation p(MGI:Ppp1cb) View Subject | View Object

We found strong Tau hyperphosphorylation in brain samples from R6/2 and 140CAG Tg knock-in, associated with a significant reduction in the levels of Tau phosphatases (PP1, PP2A and PP2B), with no apparent involvement of major Tau kinases. PubMed:25143394

Appears in Networks:

p(MGI:Mapt, pmod(HBP:hyperphosphorylation)) negativeCorrelation p(RGD:Ppp2ca) View Subject | View Object

PP2A expression decreased, whereas, PP1 and PP5 expression increased in lead-exposed rats. These results demonstrate that early postnatal exposure to lead decrease PP2A expression and induce tau hyperphosphorylation at several serine and threonine residues. PubMed:23134599

Appears in Networks:

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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.