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p(MGI:Mapt, pmod(Ph))

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Entity

Name
Mapt
Namespace
mgi
Namespace Version
20181021
Namespace URL
https://raw.githubusercontent.com/pharmacome/terminology/f2f993e599694ab5ce989cc39d789a499f75db99/external/mgi-names.belns

Appears in Networks 7

Tau clearance mechanisms and their possible role in the pathogenesis of Alzheimer disease v1.0.0

TFEB enhances astroglial uptake of extracellular tau species and reduces tau spreading v1.0.0

Tau protein aggregation is associated with cellular senescence in the brain v1.0.0

TAU and Interaction Partners v1.2.5

TAU Interactions Section of NESTOR

Tau Effect on Mitochondria v1.0.3

Tau and mitochondria section of NESTOR

Tau Modifications v1.9.5

Tau Modifications Sections of NESTOR

mTOR-Related Brain Dysfunctions in Neuropsychiatric Disorders v1.0.0

In-Edges 12

p(MGI:Atg7) decreases p(MGI:Mapt, pmod(Ph)) View Subject | View Object

Mice in which the critical autophagy gene Atg7 is knocked out in forebrain neurons develop age-dependent neurodegeneration with accumulation of phosphorylated tau within intracellular inclusions (99). These inclusions specifically contained tau phosphorylated at AT8, AT100, and TG3 epitopes, but not PHF1. Significantly, if tau was also knocked out in these autophagy-deficient mice, neurodegeneration was reduced (99). PubMed:24027553

Appears in Networks:
Annotations
MeSH
Neurons
Text Location
Review

p(MGI:Mapt) hasVariant p(MGI:Mapt, pmod(Ph)) View Subject | View Object

Appears in Networks:

p(MGI:Tfeb) decreases p(MGI:Mapt, pmod(Ph)) View Subject | View Object

Western blot a reduction in phospho-tau species recognized by AT8 (trending), AT180, and CP13 antibodies in the TFEB-injected mice PubMed:30108137

Appears in Networks:
Annotations
Cell Ontology (CL)
astrocyte

p(MGI:Tfeb) decreases p(MGI:Mapt, pmod(Ph)) View Subject | View Object

In the insoluble fraction, phospho- and total tau species were all reduced in the TFEB mice, as demonstrated by Western blot PubMed:30108137

Appears in Networks:
Annotations
Cell Ontology (CL)
astrocyte

p(MGI:Tfeb) causesNoChange p(MGI:Mapt, pmod(Ph)) View Subject | View Object

Quantifying the area fluorescence of MC1 staining for both hippocampi from sections representing the entire volume of hippocampus showed that astroglial TFEB had no impact on MC1 staining on the ipsi- lateral side, but significantly reduced the area of MC1 staining on the contralateral side PubMed:30108137

Appears in Networks:
Annotations
Cell Ontology (CL)
astrocyte
MeSH
Hippocampus

act(p(MGI:Klc1)) negativeCorrelation p(MGI:Mapt, pmod(Ph)) View Subject | View Object

Thus, the lack of kinesin/JIP1 interaction occurs together with an aberrant Tau/JIP1 interaction in K3 brains.Taken together, our data reveal that hyperphosphorylated Tau competes with KLC for the interaction with JIP1. PubMed:19491104

Appears in Networks:

p(MGI:Mapk8ip1) association p(MGI:Mapt, pmod(Ph)) View Subject | View Object

Thus, the lack of kinesin/JIP1 interaction occurs together with an aberrant Tau/JIP1 interaction in K3 brains.Taken together, our data reveal that hyperphosphorylated Tau competes with KLC for the interaction with JIP1. PubMed:19491104

Appears in Networks:

act(p(MGI:Mapk8ip1)) negativeCorrelation p(MGI:Mapt, pmod(Ph)) View Subject | View Object

Thus, the lack of kinesin/JIP1 interaction occurs together with an aberrant Tau/JIP1 interaction in K3 brains.Taken together, our data reveal that hyperphosphorylated Tau competes with KLC for the interaction with JIP1. PubMed:19491104

Appears in Networks:

r(MGI:Dnm1l) positiveCorrelation p(MGI:Mapt, pmod(Ph)) View Subject | View Object

Mitochondrial dysfunction found to be reduced in TauXDrp1þ/+- mice relative to Tau mice. Phosphorylated Tau levels were significantly reduced in TauXDrp1þ/+- mice relative to Tau mice. These findings suggest that a partial reduction of Drp1 decreases the levels of phosphorylated Tau, reduces mitochondrial dysfunction, and maintains mitochondrial dynamics, enhances mitochondrial biogenesis and synaptic activity in Tau mice. PubMed:28173111

Appears in Networks:

a(HBP:"CM-414") decreases p(MGI:Mapt, pmod(Ph)) View Subject | View Object

Here we report the discovery of a new first-in-class small-molecule (CM-414) that acts as a dual inhibitor of PDE5 and HDACs. We have used this compound as a chemical probe to validate this systems therapeutics strategy, where an increase in the activation of cAMP/cGMP-responsive element-binding protein (CREB) induced by PDE5 inhibition, combined with moderate HDAC class I inhibition, leads to efficient histone acetylation. This molecule rescued the impaired long-term potentiation evident in hippocampal slices from APP/PS1 mice. Chronic treatment of Tg2576 mice with CM-414 diminished brain Aβ and tau phosphorylation (pTau) levels, increased the inactive form of GSK3β, reverted the decrease in dendritic spine density on hippocampal neurons, and reversed their cognitive deficits, at least in part by inducing the expression of genes related to synaptic transmission. PubMed:27550730

Appears in Networks:

path(MESH:Fasting) increases p(MGI:Mapt, pmod(Ph)) View Subject | View Object

We recently discovered that the human brain tau is also modified by O-GlcNAcylation in addition to phosphorylation and that O-GlcNAcylation modulates phosphorylation of tau inversely (Liu et al.,2004a). We found that fasting induced a time-dependent decrease in tau O-GlcNAcylation and concurrent hyperphosphorylation of tau at most of the phosphorylation sites studied. PubMed:16630055

Appears in Networks:

a(CHEBI:pimozide) decreases p(MGI:Mapt, pmod(Ph)) View Subject | View Object

For instance, the increase in autophagy flux induced by pimozide occurs along with a depression of phosphorylated tau in a transgenic mouse model of AD PubMed:30061532

Appears in Networks:
Annotations
MeSH
Frontal Lobe
MeSH
Alzheimer Disease

Out-Edges 6

p(MGI:Mapt, pmod(Ph)) increases path(HBP:Neurodegeneration) View Subject | View Object

Mice in which the critical autophagy gene Atg7 is knocked out in forebrain neurons develop age-dependent neurodegeneration with accumulation of phosphorylated tau within intracellular inclusions (99). These inclusions specifically contained tau phosphorylated at AT8, AT100, and TG3 epitopes, but not PHF1. Significantly, if tau was also knocked out in these autophagy-deficient mice, neurodegeneration was reduced (99). PubMed:24027553

Appears in Networks:
Annotations
MeSH
Neurons
Text Location
Review

p(MGI:Mapt, pmod(Ph)) causesNoChange p(MGI:Cdkn2a) View Subject | View Object

In 15-month-old mice with heavy Abeta deposition and phosphorylated tau, but lacking NFT pathology (Orr et al., 2014), Cdkn2a expression was not elevated (Figure 4e). These data indicate that Cdkn2a expression was neither a response to general protein accumulation, nor to pre-NFT tau pathology, but instead required the presence of NFTs PubMed:30126037

Appears in Networks:
Annotations
Confidence
High
MeSH
Cerebral Cortex
MeSH
Hippocampus
MeSH
Alzheimer Disease

p(MGI:Mapt, pmod(Ph)) association p(MGI:Mapk8ip1) View Subject | View Object

Thus, the lack of kinesin/JIP1 interaction occurs together with an aberrant Tau/JIP1 interaction in K3 brains.Taken together, our data reveal that hyperphosphorylated Tau competes with KLC for the interaction with JIP1. PubMed:19491104

Appears in Networks:

p(MGI:Mapt, pmod(Ph)) negativeCorrelation act(p(MGI:Mapk8ip1)) View Subject | View Object

Thus, the lack of kinesin/JIP1 interaction occurs together with an aberrant Tau/JIP1 interaction in K3 brains.Taken together, our data reveal that hyperphosphorylated Tau competes with KLC for the interaction with JIP1. PubMed:19491104

Appears in Networks:

p(MGI:Mapt, pmod(Ph)) negativeCorrelation act(p(MGI:Klc1)) View Subject | View Object

Thus, the lack of kinesin/JIP1 interaction occurs together with an aberrant Tau/JIP1 interaction in K3 brains.Taken together, our data reveal that hyperphosphorylated Tau competes with KLC for the interaction with JIP1. PubMed:19491104

Appears in Networks:

p(MGI:Mapt, pmod(Ph)) positiveCorrelation r(MGI:Dnm1l) View Subject | View Object

Mitochondrial dysfunction found to be reduced in TauXDrp1þ/+- mice relative to Tau mice. Phosphorylated Tau levels were significantly reduced in TauXDrp1þ/+- mice relative to Tau mice. These findings suggest that a partial reduction of Drp1 decreases the levels of phosphorylated Tau, reduces mitochondrial dysfunction, and maintains mitochondrial dynamics, enhances mitochondrial biogenesis and synaptic activity in Tau mice. PubMed:28173111

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.