EC Number   |
Application |
Reference |
|---|
   3.4.17.23 | medicine |
angiotensin-converting enzyme 2 (ACE2) fused to the Fc portion of immunoglobulin neutralizes SARS-CoV-2 in vitro. Provision of soluble recombinant human ACE2 protein can be beneficial as a novel biologic therapeutic to combat or limit infection progression caused by coronaviruses that utilize ACE2 as a receptor. If given in its soluble form as an appropriate recombinant ACE2 protein, a new tool may be at hand to combat the spread of coronavirus in susceptible individuals by limiting coronavirus attachment to the cell membranes, cell entry, and replication |
753315 |
| 3.4.17.23 | medicine |
angiotensin-converting enzyme 2 is a target for gene therapy for hypertension disorders |
668528 |
| 3.4.17.23 | medicine |
antibodies and small molecular inhibitors that can block the interaction of the enzyme (ACE2) with the receptor binding domain can to combat the virus SARS-CoV-2 |
752692 |
| 3.4.17.23 | analysis |
application of CEBIT, i.e. Condensate-aided Enrichment of Biomolecular Interactions in Test tubes for high-throughput screening of drugs to inhibit the interaction between the receptor-binding domain of SARS-CoV-2 spike protein and its obligate receptor ACE2 |
764799 |
| 3.4.17.23 | medicine |
binding of SARS-CoV-2 spike protein, variant omicron B.1.1.529, to ACE2 is inhibited by caffeic acid hexoside (-6.4 kcal/mol, RMSD 2.382 A) and phloretin (-6.3 kcal/mol, RMSD 0.061 A) from Sargassum wightii, which interact with crucial residues Asn417, Ser496, Tyr501, and His505 of the spike protein. 5alpha-Cholestan-3beta-ol, 2-methylene- (-6.0 kcal/mol, RMSD 3.074 A) from Corallina officinalis shows inhibitory effect against the omicron receptor-binding domain mutated residues Leu452 and Ala484 |
765306 |
| 3.4.17.23 | medicine |
chronic treatment with the AT1R antagonist almesartan induces a fivefold increase in ACE2 mRNA in the aorta which leads to a significant increase in aortic angiotensin(1-7) protein expression. These effects are associated with significant decreases in aortic medial thickness and may represent an important protective mechanism in the prevention of cardiovascular events in hypertensive subjects |
667145 |
| 3.4.17.23 | medicine |
circulating extracellular vesicles that express ACE2 isolated from human plasma or cells neutralize SARS-CoV-2 infection by competing with cellular ACE2. Compared to vesicle-free recombinant human ACE2, ACE2 from extracellular vesicles shows a 135fold higher potency in blocking the binding of the viral spike protein receptor-binding domain, and a 60- to 80fold higher efficacy in preventing infections by both pseudotyped and authentic SARS-CoV-2. ACE2 from extracellular vesicles protects human ACE2 transgenic mice from SARS-CoV-2-induced lung injury and mortality. ACE2 from extracellular vesicles inhibits the infection of SARS-CoV-2 variants alpha, beta, and delta with equal or higher potency than for the wild-type strain |
765453 |
| 3.4.17.23 | medicine |
coexpression of intermediate filament protein vimentin with ACE2 increases SARS-CoV-2 entry in HEK-293 cells, and shRNA-mediated knockdown of vimentin significantly reduces SARS-CoV-2 infection of human endothelial cells. Incubation of A-549 cells expressing ACE2 with purified vimentin increases pseudotyped SARS-CoV-2 spike protein entry. The S-protein receptor-binding domain is sufficient for spike protein interaction with vimentin. Extracellular vimentin binds to SARS-CoV-2 spike protein and facilitates SARS-CoV-2 infection |
765690 |
| 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 | pharmacology |
conserved residues at the interface of the spike protein from three strains of coronaviruses NL63, SARS-CoV, and SARS-CoV are identified, which might act as a recognition site for ACE2 receptor. The conserved interaction sites can help in effective targeting of the ACE2 binding site by therapeutics in SARS-CoV as well as SARS-CoV-2 strain |
763676 |
