Upload at 2018-04-03 15:16:42
Causal Biological Networks Database
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
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Number Nodes
Number Edges
Number Components
Network Density
Average Degree
Number Citations
Number BEL Errors

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


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


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


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


In-Edges: 166 | Out-Edges: 99 | Explore Neighborhood | Download JSON


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