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A chaperome subnetwork safeguards proteostasis in aging and neurodegenerative disease. 1.0.0

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charles.hoyt@scai.fraunhofer.de at 2019-02-27 16:20:57.859383
Authors
Esther Wollert
Contact
charles.hoyt@scai.fraunhofer.de
License
CC BY 4.0
Copyright
Copyright © 2018 Fraunhofer Institute SCAI, All rights reserved.
Number Nodes
29
Number Edges
51
Number Components
1
Network Density
0.062807881773399
Average Degree
1.75862068965517
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
The Biology of Proteostasis in Aging and Disease v1.0.0 38%
Molecular Chaperone Functions in Protein Folding and Proteostasis v1.0.0 34%
Model systems of protein-misfolding diseases reveal chaperone modifiers of proteotoxicity v1.0.0 31%
Imbalances in the Hsp90 Chaperone Machinery: Implications for Tauopathies v1.0.0 28%
The Ubiquitin Proteasome System in Neurodegenerative Diseases: Sometimes the Chicken, Sometimes the Egg v1.0.0 24%
Molecular chaperones and regulation of tau quality control: strategies for drug discovery in tauopathies v1.0.0 17%
Estrogen receptor-α is localized to neurofibrillary tangles in Alzheimer's disease v1.0.0 17%
Protein aggregation can inhibit clathrin-mediated endocytosis by chaperone competition v1.0.0 15%
A Quantitative Chaperone Interaction Network Reveals the Architecture of Cellular Protein Homeostasis Pathways v1.0.0 14%
Promoting the clearance of neurotoxic proteins in neurodegenerative disorders of ageing v1.0.0 14%

Sample Edges

a(CHEBI:ATP) association act(p(FPLX:HSP90)) View Subject | View Object

The ATP-dependent chaperones are comprised of the 5 HSP90s, 17 HSP70s, 14 HSP60s, 6 ER-specific, and 8 MITO-specific Hsp100/AAA+ ATPases, respectively. PubMed:25437566

a(CHEBI:ATP) association act(p(FPLX:HSPA)) View Subject | View Object

The ATP-dependent chaperones are comprised of the 5 HSP90s, 17 HSP70s, 14 HSP60s, 6 ER-specific, and 8 MITO-specific Hsp100/AAA+ ATPases, respectively. PubMed:25437566

a(CHEBI:ATP) association act(p(HGNC:HSPD1)) View Subject | View Object

The ATP-dependent chaperones are comprised of the 5 HSP90s, 17 HSP70s, 14 HSP60s, 6 ER-specific, and 8 MITO-specific Hsp100/AAA+ ATPases, respectively. PubMed:25437566

bp(MESH:Aging) increases p(HGNC:TPR) View Subject | View Object

TPR proteins tend to be induced, whereas HSP40s are repressed (Figure 1B). PubMed:25437566

bp(MESH:Aging) increases p(HGNC:TPR) View Subject | View Object

Ranked by decreasing median aging correlation, the induction of sHSPs and TPR genes consistently ranked high and the HSP60s, HSP40s, and HSP70s were consistently repressed. PubMed:25437566

Sample Nodes

path(MESH:"Alzheimer Disease")

In-Edges: 536 | Out-Edges: 704 | Classes: 5 | Explore Neighborhood | Download JSON

path(MESH:"Huntington Disease")

In-Edges: 24 | Out-Edges: 40 | Explore Neighborhood | Download JSON

bp(MESH:Aging)

In-Edges: 10 | Out-Edges: 65 | Explore Neighborhood | Download JSON

a(CHEBI:"amyloid-beta polypeptide 42")

In-Edges: 66 | Out-Edges: 72 | Classes: 1 | Explore Neighborhood | Download JSON

a(CHEBI:ATP)

In-Edges: 20 | Out-Edges: 18 | 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.