Provenance

Upload
charles.hoyt@scai.fraunhofer.de at 2018-04-03 15:16:42
Authors
Causal Biological Networks Database
Contact
CausalBiologicalNetworks.RD@pmi.com
Description
The Hypoxic Stress network depicts the causal mechanisms that regulate hypoxic stress including activation of HIF1A and its targets, control of transcription, protein synthesis, and crosstalk with oxidative stress, ER stress, and osmotic stress response pathways.\u003c/p\u003e\n\u003ch2\u003eJamboree Review Focus\u003c/h2\u003e\n\u003cp\u003eExpand ER stress-relevant pathways. \nReviewed during Jamboree2014
License
Please cite: - www.causalbionet.com - https://bionet.sbvimprover.com as well as any relevant publications. The sbv IMPROVER project, the website and the Symposia are part of a collaborative project designed to enable scientists to learn about and contribute to the development of a new crowd sourcing method for verification of scientific data and results. The current challenges, website and biological network models were developed and are maintained as part of a collaboration among Selventa, OrangeBus and ADS. The project is led and funded by Philip Morris International. For more information on the focus of Philip Morris International’s research, please visit www.pmi.com.
Number Nodes
111
Number Edges
262
Number Components
28
Network Density
0.0214578
Average Degree
2.36036
Number Citations
144
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
BEL Framework Large Corpus Document v20170611 40%
Hypoxic Stress-2.0-Hs v2.0 29%
Hypoxic Stress-2.0-Mm v2.0 28%
Osmotic Stress-2.0-Rn v2.0 25%
Angiogenesis-2.0-Rn v2.0 22%
Autophagy-2.0-Rn v2.0 20%
Endoplasmic Reticulum Stress-2.0-Rn v2.0 19%
Oxidative Stress-2.0-Rn v2.0 18%
mTor-2.0-Rn v2.0 18%
Apoptosis-2.0-Rn v2.0 17%

Sample Edges

act(complex(SCOMP:"AMP Activated Protein Kinase Complex"), ma(kin)) directlyIncreases p(HGNC:CFTR, pmod(Ph, Ser, 768))

AMPK phosphorylates CFTR in vitro at two essential serines (Ser(737) and Ser(768)) in the R domain, PubMed:19095655

act(complex(SCOMP:"AMP Activated Protein Kinase Complex"), ma(kin)) directlyIncreases p(HGNC:CFTR, pmod(Ph, Ser, 768))

AMPK-dependent CFTR phosphorylation renders the channel resistant to activation by PKA and PKC without preventing phosphorylation by these kinases. We found that Ser768, a CFTR R domain residue considered to be an inhibitory PKA site, is the dominant site of AMPK phosphorylation in vitro. Ser-to-Ala mutation at this site enhanced baseline CFTR activity and rendered CFTR resistant to inhibition by AMPK PubMed:19419994

act(complex(SCOMP:"AMP Activated Protein Kinase Complex"), ma(kin)) directlyDecreases act(complex(SCOMP:"TORC1 Complex"), ma(kin))

The phosphorylation of raptor by AMPK is required for the inhibition of mTORC1 and cell-cycle arrest induced by energy stress. PubMed:18439900

Sample Nodes

p(RGD:Mtor)

In-Edges: 43 | Out-Edges: 18 | Explore Neighborhood | Download JSON

a(CHEBI:glutathione)

In-Edges: 132 | Out-Edges: 88 | Classes: 5 | Explore Neighborhood | Download JSON

a(CHEBI:"reactive oxygen species")

In-Edges: 1023 | Out-Edges: 827 | Classes: 1 | Children: 4 | Explore Neighborhood | Download JSON

p(RGD:Creb1)

In-Edges: 54 | Out-Edges: 15 | Explore Neighborhood | Download JSON

p(RGD:Il6)

In-Edges: 166 | Out-Edges: 99 | 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 the open source project, PyBEL. Please feel free to contact us here to give us feedback or report any issues.