+ |
ER stress | up-regulates
|
ERN1 |
0.7 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-253145 |
|
|
Homo sapiens |
|
pmid |
sentence |
18065414 |
Our findings suggest that MTHFR is up-regulated by ER stress and that this effect is mediated by IRE1 and c-Jun. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | COVID-19 Causal Network |
+ |
ER stress | up-regulates
|
QRICH1 |
0.7 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-269398 |
|
|
Homo sapiens |
|
pmid |
sentence |
33384352 |
QRICH1 promotes cell death under ER stress |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
ER stress | up-regulates
|
BBC3 |
0.7 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-196938 |
|
|
Homo sapiens |
|
pmid |
sentence |
22492984 |
Exposure to stress results in the induction of bh3-only proteins, which neutralise the pro-survival proteins |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Mitochondrial Control of Apoptosis |
+ |
ER stress | up-regulates
|
PRNP |
0.7 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-253609 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
21478263 |
ER stress specifically increases the synthesis of AltPrP from PrP cDNA. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
GPR37 | up-regulates
|
ER stress |
0.7 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-249701 |
|
|
Homo sapiens |
|
pmid |
sentence |
12666095 |
Parkin-associated endothelin receptor-like receptor (Pael-R). Overexpression of this protein causes it to become ubiquinated, insoluble, and unfolded, leading to endoplasmic reticulum stress and cell death. Furthermore, an insoluble form of Pael-R has been demonstrated to accumulate in the brains of patients with Parkin mutations, suggesting a possible toxic mechanism. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
ER stress | up-regulates
|
ATF4 |
0.7 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-253728 |
|
|
Homo sapiens |
|
pmid |
sentence |
23205607 |
Reporter gene analyses using the 5'-promoter region of FGF19 revealed that a functional AARE (amino-acid-response element) was localized in this region, and this site was responsible for inducing its transcription through ATF4 (activating transcription factor 4), which is activated in response to ER stress |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | COVID-19 Causal Network |
+ |
ER stress | up-regulates
|
BID |
0.7 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-196944 |
|
|
Homo sapiens |
|
pmid |
sentence |
22492984 |
Exposure to stress results in the induction of bh3-only proteins, which neutralise the pro-survival proteins |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | COVID-19 Causal Network, Mitochondrial Control of Apoptosis, SARS-COV APOPTOSIS |
+ |
SOD1 | up-regulates
|
ER stress |
0.7 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262788 |
|
|
Mus musculus |
|
pmid |
sentence |
18519638 |
SOD1mut-induced ER stress |we first examined whether SOD1mut induces ER stress in NSC34 motor neurons, as assessed by band-shift analyses of the ER transmembrane kinase receptors IRE1 and PERK. Adenovirus (Ad)-mediated expression of ALS-linked SOD1mut (SOD1G93A) was detectable within 48 h of infection (Supplemental Fig. S1A). SOD1mut (SOD1A4V, SOD1G85R, and SOD1G93A) but not wild-type SOD1 (SOD1wt) activated IRE1 and PERK |
|
Publications: |
1 |
Organism: |
Mus Musculus |
+ |
ER stress | up-regulates
|
BCL2L11 |
0.7 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-196941 |
|
|
Homo sapiens |
|
pmid |
sentence |
22492984 |
Exposure to stress results in the induction of bh3-only proteins, which neutralise the pro-survival proteins |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | COVID-19 Causal Network, Mitochondrial Control of Apoptosis, SARS-COV APOPTOSIS |
+ |
SNCA | up-regulates
|
ER stress |
0.7 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-249702 |
|
|
Homo sapiens |
|
pmid |
sentence |
12666095 |
Furthermore, mutant isoforms of alpha-synuclein more readily oligomerize, and it has been suggested that its tendency to aggregate into misfolded structures may confer toxic properties to the protein. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Parkinson |