EC Number   |
Application |
Reference |
|---|
   3.4.17.23 | medicine |
compounds benzyl (6aS,9aS)-10-benzyl-4-[benzyl(methyl)amino]-8-(cyclopropanecarbonyl)-6a,7,8,9,9a,10-hexahydrocyclopenta[b]pyrimido[4,5-e][1,4]diazepine-6(5H)-carboxylate, benzyl (6aS,9aS)-4-[benzyl(methyl)amino]-8-(cyclopropanecarbonyl)-10-[(4-methylphenyl)methyl]-6a,7,8,9,9a,10-hexahydrocyclopenta[b]pyrimido[4,5-e][1,4]diazepine-6(5H)-carboxylate and benzyl (6aS,9aS)-4-[benzyl(methyl)amino]-10-[(4-chlorophenyl)methyl]-8-(cyclopropanecarbonyl)-6a,7,8,9,9a,10-hexahydrocyclopenta[b]pyrimido[4,5-e][1,4]diazepine-6(5H)-carboxylate inhibit the interactions between SARS-CoV-2 spike receptor-binding domain and ACE2 by modulating ACE2 without impairing its enzymatic activity necessary for normal physiological functions. The compounds suppress viral infection in cultured cells by inhibiting the entry of ancestral and variant SARS-CoV-2 |
763895 |
| 3.4.17.23 | medicine |
differential regulation of ACE2 activity during the progression of atherosclerosis suggest that this novel molecule of the reninangiotensin system may play a role in the pathogenesis of atherosclerosis |
693806 |
| 3.4.17.23 | medicine |
enhancing ACE2 action may serve to provide additional therapeutic benefits patients with cardiovascular and diabetic kidney disease. Increased ACE2 activity by the use of human recombinant ACE2 and/or a small molecule activator(xanthenone) of ACE2 may represent potential new therapies for lung, cardiovascular and kidney diseases by providing dual beneficial effects by antagonizing angiotensin II action while generating angiotensin-(1-7) |
694351 |
| 3.4.17.23 | medicine |
expression of ACE2 increases during aging in human lungs. ACE2 expression increases upon telomere shortening or dysfunction in cultured mammalian cells. This increase is controlled at the transcriptional level, and ACE2 promoter activity is DNA damage response-dependent. Both pharmacological global DNA damage response inhibition of ATM kinase activity and selective telomeric DNA damage response inhibition by the use of antisense oligonucleotides prevent ACE2 upregulation following telomere damage |
764575 |
| 3.4.17.23 | medicine |
expression of ACE2 increases during aging in lungs. ACE2 expression increases upon telomere shortening or dysfunction in mice. This increase is controlled at the transcriptional level, and ACE2 promoter activity is DNA damage response-dependent. Both pharmacological global DNA damage response inhibition of ATM kinase activity and selective telomeric DNA damage response inhibition by the use of antisense oligonucleotides prevent ACE2 upregulation following telomere damage |
764575 |
| 3.4.17.23 | medicine |
expression of both ACE2 and TMPRSS2 genes is necessary to support SARS-CoV-2 infection and replication in DF1 cells and a nonpermissive sub-lineage of MDCK cells. Titers of SARS-CoV-2 in these cell lines are comparable to those observed in control Vero cells. Permissive replication of SARS-CoV-2 is not found in pig or horse. Cells expressing genes from either bat species tested demonstrate temporal replication of SARS-CoV-2 that peaks early and is not sustained |
765871 |
| 3.4.17.23 | medicine |
identification of ACE2 as a receptor for SARS-CoV will contribute to the development of antivirals and vaccines |
668221 |
| 3.4.17.23 | medicine |
in lung tissues collected from mice that were sub-chronically exposed to air or 0.8 ppm ozone for three weeks, the ACE2 transcripts are significantly elevated in the parenchyma, but not in the extrapulmonary airways and alveolar macrophages. A significant proportion of additional known SARS-CoV-2 host susceptibility genes are upregulated in alveolar macrophages and parenchyma from ozone-exposed mice |
765794 |
| 3.4.17.23 | medicine |
inhibition of SARS-CoV-2 spike protein binding to ACE2 by a higher-affinity variant of the B38 monoclonal antibody, containing mutantion F27Q in the heavy chain (F27Q), which can bind to the rececptor-binding domain more tightly, and by Ty1 alpaca nanobody, i.e.a 38 amino acid peptide inhibitor taking components from Ty1. The peptide exhibits improved affinity for the rececptor-binding by up to 100fold, and like B38 mutant, it can outclass the binding affinity of ACE2 with the rececptor-binding domain |
765099 |
| 3.4.17.23 | medicine |
interaction of ACE2 and SARS-CoV-2 Omicron spike protein. The mutations in the Omicron variant at residues 493, 496, 498, and 501 restore ACE2 binding efficiency that would be lost as a result of other mutations such as K417N |
765834 |
