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Identification of the Tau phosphorylation pattern that drives its aggregation 1.0.0

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charles.hoyt@scai.fraunhofer.de at 2019-02-27 16:23:06.243256
Authors
Kristian Kolpeja
Contact
charles.hoyt@scai.fraunhofer.de
License
CC BY 4.0
Copyright
Copyright © 2018 Fraunhofer Institute SCAI, All rights reserved.
Number Nodes
13
Number Edges
22
Number Components
1
Network Density
0.141025641025641
Average Degree
1.69230769230769
Number Citations
1
Number BEL Errors
0

Content Statistics

Network Overlap

The node-based overlap between this network and other networks is calculated as the Szymkiewicz-Simpson coefficient of their respective nodes. Up to the top 10 are shown below.

Network Overlap
Tau Modifications v1.9.5 100%
Tau oligomers and tau toxicity in neurodegenerative disease v1.0.0 31%
Extracellular low-n oligomers of tau cause selective synaptotoxicity without affecting cell viability v1.0.0 31%
Caenorhabditis elegans models of tauopathy v1.0.0 31%
Inert and seed-competent tau monomers suggest structural origins of aggregation v1.0.0 25%
Pathological missorting of endogenous MAPT/Tau in neurons caused by failure of protein degradation systems v1.0.1 23%
Molecular chaperones and regulation of tau quality control: strategies for drug discovery in tauopathies v1.0.0 23%
Tau Protein Hyperphosphorylation and Aggregation in Alzheimer’s Disease and Other Tauopathies, and Possible Neuroprotective Strategies v1.0.0 23%
TAU and Interaction Partners v1.2.5 23%
PP2A and Alzheimer Disease v1.0.0 23%

Sample Edges

p(HGNC:MAPT) hasVariant p(HGNC:MAPT, pmod(Ph, Ser, 202)) View Subject | View Object

a(HBP:"Tau Protein Secondary Structure, Turn") decreases a(HBP:"Tau aggregates") View Subject | View Object

Our finding that the resulting Tau species with phosphorylation at Ser202/Th205, but with a disrupted turn-like structure, forms abundant fibers detectable by thioflavin fluorescence or electron microscopy (Figs. 2 and 4) suggests the initial turn-like structure induced by the phosphorylation of only Ser202 and Thr205 is protective against aggregation. PubMed:28784767

a(HBP:"Tau Protein Secondary Structure, Turn") decreases a(HBP:"Tau aggregates") View Subject | View Object

Indeed, Tau phosphorylation at the three positions, Ser202/Thr205/Ser208, while not at Ser262, is sufficient to induce aggregation without the addition of any exogenous aggregation inducer. PubMed:28784767

act(p(FPLX:CSNK1), ma(kin)) increases p(HGNC:MAPT, pmod(Ph, Ser, 208)) View Subject | View Object

Phosphorylation at Ser208 might be catalyzed by Casein kinase 1 (44), and its identification as a potential site for O-GlcNacylation (45) points to the important role of this residue. PubMed:28784767

p(HBP:"Tau epitope, AT8") equivalentTo p(HGNC:MAPT, pmod(Ph, Ser, 202), pmod(Ph, Thr, 205), pmod(Ph, Thr, 208)) View Subject | View Object

Sample Nodes

p(HGNC:MAPT)

In-Edges: 477 | Out-Edges: 480 | Classes: 11 | Children: 27 | Explore Neighborhood | Download JSON

p(HGNC:MAPK1)

In-Edges: 9 | Out-Edges: 9 | Explore Neighborhood | Download JSON

a(HBP:"Tau aggregates")

In-Edges: 224 | Out-Edges: 71 | Children: 3 | Explore Neighborhood | Download JSON

p(HGNC:MAPT, pmod(Ph, Ser, 202))

In-Edges: 45 | Out-Edges: 26 | Equivalencies: 2 | Classes: 2 | Explore Neighborhood | Download JSON

a(HBP:"Tau Protein Secondary Structure, Turn")

In-Edges: 3 | Out-Edges: 4 | Explore Neighborhood | Download JSON

About

BEL Commons is developed and maintained in an academic capacity by Charles Tapley Hoyt and Daniel Domingo-Fernández at the Fraunhofer SCAI Department of Bioinformatics with support from the IMI project, AETIONOMY. It is built on top of PyBEL, an open source project. Please feel free to contact us here to give us feedback or report any issues. Also, see our Publishing Notes and Data Protection information.

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.