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Molecular Chaperone Functions in Protein Folding and Proteostasis 1.0.0

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charles.hoyt@scai.fraunhofer.de at 2019-03-15 15:44:01.698984
Authors
Esther Wollert
Contact
charles.hoyt@scai.fraunhofer.de
License
Private Ownership to Fraunhofer Institute SCAI
Copyright
Copyright © 2018 Fraunhofer Institute SCAI, All rights reserved.
Number Nodes
63
Number Edges
110
Number Components
2
Network Density
0.0281618023553507
Average Degree
1.74603174603175
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
A chaperome subnetwork safeguards proteostasis in aging and neurodegenerative disease. v1.0.0 34%
The Ubiquitin Proteasome System in Neurodegenerative Diseases: Sometimes the Chicken, Sometimes the Egg v1.0.0 33%
Model systems of protein-misfolding diseases reveal chaperone modifiers of proteotoxicity v1.0.0 30%
The Biology of Proteostasis in Aging and Disease v1.0.0 29%
Molecular chaperones and regulation of tau quality control: strategies for drug discovery in tauopathies v1.0.0 29%
Molecular chaperones and proteostasis regulation during redox imbalance v1.0.0 21%
In Vivo and In Vitro Characterization of Antalarmin, a Nonpeptide Corticotropin-Releasing Hormone (CRH) Receptor Antagonist: Suppression of Pituitary ACTH Release and Peripheral Inflammation v1.0.0 20%
Imbalances in the Hsp90 Chaperone Machinery: Implications for Tauopathies v1.0.0 19%
Autophagy and the ubiquitin-proteasome system: collaborators in neuroprotection v1.0.0 16%
Pathological missorting of endogenous MAPT/Tau in neurons caused by failure of protein degradation systems v1.0.1 15%

Sample Edges

complex(a(CHEBI:ATP), p(FPLX:HSP90)) hasComponent a(CHEBI:ATP) View Subject | View Object

complex(a(CHEBI:ATP), p(FPLX:HSP90)) hasComponent p(FPLX:HSP90) View Subject | View Object

a(CHEBI:ATP) regulates act(p(HGNCGENEFAMILY:Chaperonins)) View Subject | View Object

Chaperones that function broadly in de novo folding and refolding (i.e., the chaperonins, Hsp70s, and Hsp90s) are ATP regulated and recognize segments of exposed hydropho- bic amino acid residues, which are later buried in the interior of the natively folded protein. PubMed:23746257

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

Chaperones that function broadly in de novo folding and refolding (i.e., the chaperonins, Hsp70s, and Hsp90s) are ATP regulated and recognize segments of exposed hydropho- bic amino acid residues, which are later buried in the interior of the natively folded protein. PubMed:23746257

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

Chaperones that function broadly in de novo folding and refolding (i.e., the chaperonins, Hsp70s, and Hsp90s) are ATP regulated and recognize segments of exposed hydropho- bic amino acid residues, which are later buried in the interior of the natively folded protein. PubMed:23746257

Sample Nodes

bp(GO:"immune response")

In-Edges: 7 | Out-Edges: 5 | Explore Neighborhood | Download JSON

bp(GO:"inflammatory response")

In-Edges: 55 | Out-Edges: 24 | Explore Neighborhood | Download JSON

bp(GO:"response to oxidative stress")

In-Edges: 15 | Out-Edges: 12 | Explore Neighborhood | Download JSON

bp(GO:aging)

In-Edges: 27 | Out-Edges: 61 | Explore Neighborhood | Download JSON

bp(GO:"cell death")

In-Edges: 44 | Out-Edges: 5 | 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.