| + |
CSNK2A1 | up-regulates activity 
phosphorylation
|
ACE |
0.307 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264425 |
Ser1299 |
SHGPQFGsEVELRHS |
Sus scrofa |
Endothelial Cell |
| pmid |
sentence |
| 12386153 |
CK2 coprecipitated with ACE from endothelial cells, and CK2 phosphorylated both ACE and a peptide corresponding to the cytoplasmic tail. Mutation of serine(1270) within the CK2 consensus sequence almost abolished ACE phosphorylation.|These results indicate that the CK2-mediated phosphorylation of ACE regulates its retention in the plasma membrane and may determine plasma ACE levels. |
|
| Publications: |
1 |
Organism: |
Sus Scrofa |
| Pathways: | COVID-19 Causal Network |
| + |
lisinopril | down-regulates activity 
chemical inhibition
|
ACE |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261070 |
|
|
in vitro |
|
| pmid |
sentence |
| 12540854 |
The structure of tACE bound to the potent inhibitor lisinopril shows that the inhibitor binds in a highly ordered (overall B-factor of 15.26 A˚ 2) |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258611 |
|
|
in vitro |
|
| pmid |
sentence |
| 9187274 |
We analyzed the inhibition of angiotensin I and AcSDKP hydrolysis as well as that of three synthetic ACE substrates by wild-type ACE and the N and C domains by using a range of specific ACE inhibitors. We demonstrate that captopril, lisinopril, and fosinoprilat are potent inhibitors of AcSDKP hydrolysis by wild-type ACE, with K(i) values in the subnanomolar range. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
benazepril | down-regulates activity
chemical inhibition
|
ACE |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253343 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16407508 |
Angiotensin-converting-enzyme inhibitors provide renal protection in patients with mild-to-moderate renal insufficiency (serum creatinine level, 3.0 mg per deciliter or less). We assessed the efficacy and safety of benazepril in patients without diabetes who had advanced renal insufficiency. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Focal segmental glomerulosclerosis |
| + |
Angiotensin-1 | up-regulates activity
binding
|
ACE |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260231 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 32201502 |
Ang I is subsequently converted into the major RAS effector peptide Ang II or Ang (1–8), through activity of the zinc-dependent protease ACE, which hydrolyzes two amino acids from the carboxy terminus of Ang I |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | COVID-19 Causal Network, Fibrosis, SARS-CoV FIBROSIS |
| + |
fosinoprilat | down-regulates activity
chemical inhibition
|
ACE |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258613 |
|
|
in vitro |
|
| pmid |
sentence |
| 9187274 |
We analyzed the inhibition of angiotensin I and AcSDKP hydrolysis as well as that of three synthetic ACE substrates by wild-type ACE and the N and C domains by using a range of specific ACE inhibitors. We demonstrate that captopril, lisinopril, and fosinoprilat are potent inhibitors of AcSDKP hydrolysis by wild-type ACE, with K(i) values in the subnanomolar range. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
enalaprilat (anhydrous) | down-regulates activity
chemical inhibition
|
ACE |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258429 |
|
|
Rattus norvegicus |
|
| pmid |
sentence |
| 7527095 |
The effects of 14-day trandolapril or enalapril treatment of spontaneously hypertensive rats (SHRs) were studied on blood pressure and angiotensin-converting enzyme (ACE) activity measured ex vivo in various organs. Both ACE inhibitors caused dose-dependent decreases in blood pressure and ACE activity, trandolapril being 30- and 400- to 1,000-fold more active than enalapril on blood pressure and ACE activity, respectively. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
ACE | up-regulates quantity
cleavage
|
Angiotensin-2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260236 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 32201502 |
Ang I is subsequently converted into the major RAS effector peptide Ang II or Ang (1–8), through activity of the zinc-dependent protease ACE, which hydrolyzes two amino acids from the carboxy terminus of Ang I |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | COVID-19 Causal Network, Fibrosis, SARS-CoV FIBROSIS |
| + |
ramipril | down-regulates activity
chemical inhibition
|
ACE |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258400 |
|
|
in vitro |
|
| pmid |
sentence |
| 6097265 |
2-[N-[(S)-1-Ethoxycarbonyl-3-phenylpropyl]-L-alanyl] - (1S,3S,5S) -2-azabicyclo [3.3.0] octane-3-carboxylic acid (Hoe 498) is a new, very effective and long lasting, nonsulfhydryl angiotensin I converting enzyme inhibitor. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
ACE | up-regulates activity
cleavage
|
AGT |
0.775 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253326 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11076943 |
Angiotensin I-converting enzyme is a zinc metallopeptidase that plays an important role in blood pressure regulation by cleaving the inactive decapeptide angiotensin I to angiotensin II, a potent vasopressor octapeptide. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | COVID-19 Causal Network, Fibrosis, Focal segmental glomerulosclerosis, SARS-CoV FIBROSIS |
| + |
ACE | down-regulates quantity by destabilization
binding
|
bradykinin |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253341 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16219810 |
The angiotensin-converting enzyme (ACE) is a membrane-bound peptidyl dipeptidase known to act on a variety of peptide substrates in the extracellular space. Its most notable functions are the formation of angiotensin II and the degradation of bradykinin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Focal segmental glomerulosclerosis |
| + |
captopril | down-regulates activity
chemical inhibition
|
ACE |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258612 |
|
|
in vitro |
|
| pmid |
sentence |
| 9187274 |
We analyzed the inhibition of angiotensin I and AcSDKP hydrolysis as well as that of three synthetic ACE substrates by wild-type ACE and the N and C domains by using a range of specific ACE inhibitors. We demonstrate that captopril, lisinopril, and fosinoprilat are potent inhibitors of AcSDKP hydrolysis by wild-type ACE, with K(i) values in the subnanomolar range. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
enalapril | down-regulates activity
chemical inhibition
|
ACE |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258428 |
|
|
Rattus norvegicus |
|
| pmid |
sentence |
| 7527095 |
The effects of 14-day trandolapril or enalapril treatment of spontaneously hypertensive rats (SHRs) were studied on blood pressure and angiotensin-converting enzyme (ACE) activity measured ex vivo in various organs. Both ACE inhibitors caused dose-dependent decreases in blood pressure and ACE activity, trandolapril being 30- and 400- to 1,000-fold more active than enalapril on blood pressure and ACE activity, respectively. However, comparison of ACE inhibitory activities of the diacid forms of trandolapril and enalapril, i.e., trandolaprilat and enalaprilat, measured in vitro on various tissues, showed that trandolaprilat was only three- to fivefold more active than enalaprilat. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
trandolapril | down-regulates activity
chemical inhibition
|
ACE |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258427 |
|
|
Rattus norvegicus |
|
| pmid |
sentence |
| 7527095 |
The effects of 14-day trandolapril or enalapril treatment of spontaneously hypertensive rats (SHRs) were studied on blood pressure and angiotensin-converting enzyme (ACE) activity measured ex vivo in various organs. Both ACE inhibitors caused dose-dependent decreases in blood pressure and ACE activity, trandolapril being 30- and 400- to 1,000-fold more active than enalapril on blood pressure and ACE activity, respectively. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
3.0
ACE
- 
- 