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10.3390/molecules27061882 http://scihub22266oqcxt.onion/10.3390/molecules27061882 35335246!8954242!35335246     free     free     free Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Molecules 2022 ; 27 (6): ä Nephropedia Template TP {{tp|p=35335246|t=2022. Rapid Degradation of SARS-CoV-2 Spike S Protein by A Specific Serine Protease |pdf=|usr=}}{{35335246}} gab.com Text Rapid Degradation of SARS-CoV-2 Spike S Protein by A Specific Serine Protease JO: Molecules http://www.kidney.de/pget.php?&tw=1&pmid=35335246 #FOAvip The S protein of SARS-CoV-2 is a crucial structural and functional component for virus entry. Due to the constant mutation of the virus, there are very limited ways to prevent and control COVID-19. This experiment used a macroscopic SDS-PAGE method and proved that the S protein of wild-type SARS-CoV-2 virus, especially the S1 subunit, is very sensitive to alkaline serine protease with acidic pI (ASPNJ), NJ represents Neanthes japonica (Izuka) from which ASP is purified). ASPNJ cleaves proteins when the carbonyl group of the peptide bond is contributed by arginine or lysine. ASPNJ can degrade the S protein very quickly and effectively in vitro with relative selectivity. It can be inferred that the S, S1 and RBD of SARS-CoV-2 variants can also be easily degraded by ASPNJ. This rapid and strong degradation of the S protein by ASPNJ may become a potential new treatment strategy. Twit Text FOAVip Rapid Degradation of SARS-CoV-2 Spike S Protein by A Specific Serine Protease ????Molecules http://www.kidney.de/pget.php?&tw=1&pmid=35335246 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=35335246 #FOAvip English Wikipedia <ref>{{Cite pmid|35335246}}</ref> Rapid Degradation of SARS-CoV-2 Spike S Protein by A Specific Serine Protease #MMPMID35335246 Liu J; Kan M; Zhang L; Yue Y; Wang S; Hong M; Hong X Molecules 2022[Mar]; 27 (6): ä PMID35335246show ga The S protein of SARS-CoV-2 is a crucial structural and functional component for virus entry. Due to the constant mutation of the virus, there are very limited ways to prevent and control COVID-19. This experiment used a macroscopic SDS-PAGE method and proved that the S protein of wild-type SARS-CoV-2 virus, especially the S1 subunit, is very sensitive to alkaline serine protease with acidic pI (ASPNJ), NJ represents Neanthes japonica (Izuka) from which ASP is purified). ASPNJ cleaves proteins when the carbonyl group of the peptide bond is contributed by arginine or lysine. ASPNJ can degrade the S protein very quickly and effectively in vitro with relative selectivity. It can be inferred that the S, S1 and RBD of SARS-CoV-2 variants can also be easily degraded by ASPNJ. This rapid and strong degradation of the S protein by ASPNJ may become a potential new treatment strategy. |*COVID-19[MESH] |*Serine Proteases/genetics[MESH] |Humans[MESH] |Membrane Glycoproteins/metabolism[MESH] |SARS-CoV-2[MESH]Rapid Degradation of SARS-CoV-2 Spike S Protein by A Specific Serine P(epmc).pdf DeepDyve Pubget Overpricing