| + |
E | up-regulates activity 
|
NLRP3 inflammasome |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261318 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 32133002 |
Viroporins are small, highly hydrophobic proteins derived from viruses, which interact with membranes to modify the host cell's permeability to ions or other small molecules. Several viroporins are observed to localize to the Golgi apparatus and other cytoplasmic structures during viral infection.Examples include 2B proteins from EMCV, poliovirus, enterovirus 71 (EV71), and human rhinoviruses (HRV), the envelope (E) protein of severe acute respiratory syndrome coronavirus (SARS-CoV), as well as influenza virus M2 protein. These viroporins activate the NLRP3 inflammasome by inducing different ionic fluxes.N protein from SARS-CoV, cause the flux of calcium from intracellular storages to the cytosol, which is indispensable for NLRP3 activation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | COVID-19 Causal Network |
| + |
E | up-regulates
|
Apoptosis |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260208 |
|
|
Homo sapiens |
JURKAT Cell |
| pmid |
sentence |
| 16048439 |
Overexpression of SARS-CoV E protein in T-cells promoted apoptosis |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | COVID-19 Causal Network, SARS-COV APOPTOSIS, SARS-CoV MAPK PERTURBATION, SARS-CoV ER STRESS |
| + |
E | up-regulates activity
|
p38 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260751 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 25122212 |
Interestingly, an increase in p38 MAPK activation was observed during infection with viruses containing E protein PBM, similarly to what was observed in the lungs of SARS-CoV-infected mice. These results indicated that the E protein PBM is involved in p38 MAPK activation in response to SARS-CoV infection. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Tissue: |
Lung |
| Pathways: | COVID-19 Causal Network, SARS-COV APOPTOSIS, SARS-CoV MAPK PERTURBATION |
| + |
E | up-regulates activity 
relocalization
|
SDCBP |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260752 |
|
|
Chlorocebus aethiops |
|
| pmid |
sentence |
| 25122212 |
Overall, these results support the hypothesis that the interaction of E protein PBM with syntenin facilitates the recruitment of syntenin in the cytosol and leads to p38 MAPK activation. |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| Pathways: | COVID-19 Causal Network, SARS-CoV MAPK PERTURBATION |
| + |
E | down-regulates activity 
|
ERN1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260347 |
|
|
Chlorocebus aethiops |
Vero Cell |
| pmid |
sentence |
| 22028656 |
SARS-CoV E protein down-regulated the signaling pathway inositol-requiring enzyme 1 (IRE-1) of the unfolded protein response, but not the PKR-like ER kinase (PERK) or activating transcription factor 6 (ATF-6) pathways, and reduced cell apoptosis. |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| Pathways: | COVID-19 Causal Network, SARS-CoV ER STRESS |
| + |
E | down-regulates activity
|
BCL2L1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260586 |
|
|
Homo sapiens |
JURKAT Cell |
| pmid |
sentence |
| 16048439 |
SARS-CoV E protein induces apoptosis by ‘sequestering’ Bcl-xL to the membranes of ER and Golgi, where the SARS-CoV E protein is located. As a consequence, the existing balance between pro-survival protein Bcl-xL and pro-apoptotic proteins, including Bax and BH3-domain-only proteins, is tipped by SARS CoV E protein, so that sequestered Bcl-xL could not fulfil its normal function in inhibition of apoptosis. | This result implied that SARS-CoV E protein might induce T-cell apoptosis via a pathway antagonistic to the mitochondrion-dependent mechanism of Bcl-xL. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | COVID-19 Causal Network, SARS-COV APOPTOSIS |
3.0
E
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