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Progress and Developments in Tau Aggregation Inhibitors for Alzheimer Disease 0.1.0

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charles.hoyt@scai.fraunhofer.de at 2019-02-27 16:22:58.886483
Authors
Charles Tapley Hoyt
Contact
charles.hoyt@scai.fraunhofer.de
Description
A small assortment of academic articles describing quantitatively described interactions between the MAPT (Tau) protein and small molecules
License
CC BY 4.0
Copyright
Copyright © 2018 Fraunhofer Institute SCAI, All rights reserved.
Number Nodes
23
Number Edges
23
Number Components
2
Network Density
0.0454545454545455
Average Degree
1.0
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
Promoting the clearance of neurotoxic proteins in neurodegenerative disorders of ageing v1.0.0 9%
Neuronal uptake and propagation of a rare phosphorylated high-molecular-weight tau derived from Alzheimer’s disease brain v1.0.1 6%
Abnormal Alzheimer-like phosphorylation of tau-protein by cyclin-dependent kinases cdk2 and cdk5 v1.0.0 5%
Interplay of pathogenic forms of human tau with different autophagic pathways v1.0.1 4%
Amyloid Precursor Protein Trafficking, Processing, and Function v1.0.0 4%
APP processing in Alzheimer's disease v1.0.1 4%
Proteolytic processing of Alzeimer's beta-amyloid precursor protein v1.0.1 4%
Functional aspects of meningeal lymphatics in ageing and Alzheimer’s disease v1.0.0 4%
Amyloid β oligomers (AβOs) in Alzheimer’s disease v1.0.0 4%
Nuclear receptors as therapeutic targets for Alzheimer's disease. v1.0.0 4%

Sample Edges

a(CHEBI:10642) decreases a(HBP:HBP00018) View Subject | View Object

Structures of Aβ-aggregation inhibitors evaluated in current or past clinical trials. PubMed:23484434

a(CHEBI:112284) decreases a(HBP:HBP00006) View Subject | View Object

Aminothienopyridazines (APTZs) Tau aggregation inhibitors (B/P: blood to plasma ratio). PubMed:23484434

a(CHEBI:1457) decreases a(HBP:HBP00018) View Subject | View Object

Structures of Aβ-aggregation inhibitors evaluated in current or past clinical trials. PubMed:23484434

a(CHEBI:18152) decreases a(HBP:HBP00006) View Subject | View Object

Pyrogallol generic substitution pattern commonly found in multiple polyphenolic Tau aggregation inhibitors such as 12 and 19. Note the structural overlap with the inactive pyrocatechol-substituted epicatechin PubMed:23484434

a(CHEBI:22580) decreases a(HBP:HBP00006) View Subject | View Object

Redox cycling of methylene blue and TAGI potencies. Upper panel (black): Reduced leuco form 2 and structural overlap with inactive phenothiazines 3, 4, and 5. Lower panel (blue): Structural overlap between oxidized form 1 and azure A (6), reduced anthraquinone, 8, and 9, showing the extended π-conjugated system (ND: not determined). PubMed:23484434

Sample Nodes

a(HBP:HBP00018)

In-Edges: 35 | Out-Edges: 8 | Explore Neighborhood | Download JSON

a(HBP:HBP00006)

In-Edges: 24 | Out-Edges: 8 | Explore Neighborhood | Download JSON

a(CHEBI:10642)

In-Edges: 0 | Out-Edges: 1 | Explore Neighborhood | Download JSON

a(CHEBI:112284)

In-Edges: 0 | Out-Edges: 1 | Explore Neighborhood | Download JSON

a(CHEBI:1457)

In-Edges: 0 | Out-Edges: 1 | 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.