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10.2174/0929867328666210526111318 http://scihub22266oqcxt.onion/10.2174/0929867328666210526111318 34042026!ä!34042026 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Curr+Med+Chem 2022 ; 29 (4): 635-665 Nephropedia Template TP {{tp|p=34042026|t=2022. Interfering with Host Proteases in SARS-CoV-2 Entry as a Promising Therapeutic Strategy |pdf=|usr=}}{{34042026}} gab.com Text Interfering with Host Proteases in SARS-CoV-2 Entry as a Promising Therapeutic Strategy JO: Curr Med Chem http://www.kidney.de/pget.php?&tw=1&pmid=34042026 #FOAvip Due to its fast international spread and substantial mortality, the coronavirus disease COVID-19 evolved to a global threat. Since there is currently no causative drug against this viral infection available, science is striving for new drugs and other approaches to treat the new disease. Studies have shown that the cell entry of coronaviruses into host cells takes place through the binding of the viral spike (S) protein to cell receptors. Priming of the S protein occurs via hydrolysis by different host proteases. The inhibition of these proteases could impair the processing of the S protein, thereby affecting the interaction with the host-cell receptors and preventing virus cell entry. Hence, inhibition of these proteases could be a promising strategy for treatment against SARSCoV- 2. In this review, we discuss the current state of the art of developing inhibitors against the entry proteases furin, the transmembrane serine protease type-II (TMPRSS2), trypsin, and cathepsin L. Twit Text FOAVip Interfering with Host Proteases in SARS-CoV-2 Entry as a Promising Therapeutic Strategy ????Curr Med Chem http://www.kidney.de/pget.php?&tw=1&pmid=34042026 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=34042026 #FOAvip English Wikipedia <ref>{{Cite pmid|34042026}}</ref> Interfering with Host Proteases in SARS-CoV-2 Entry as a Promising Therapeutic Strategy #MMPMID34042026 Muller P; Maus H; Hammerschmidt SJ; Knaff PM; Mailander V; Schirmeister T; Kersten C Curr Med Chem 2022[]; 29 (4): 635-665 PMID34042026show ga Due to its fast international spread and substantial mortality, the coronavirus disease COVID-19 evolved to a global threat. Since there is currently no causative drug against this viral infection available, science is striving for new drugs and other approaches to treat the new disease. Studies have shown that the cell entry of coronaviruses into host cells takes place through the binding of the viral spike (S) protein to cell receptors. Priming of the S protein occurs via hydrolysis by different host proteases. The inhibition of these proteases could impair the processing of the S protein, thereby affecting the interaction with the host-cell receptors and preventing virus cell entry. Hence, inhibition of these proteases could be a promising strategy for treatment against SARSCoV- 2. In this review, we discuss the current state of the art of developing inhibitors against the entry proteases furin, the transmembrane serine protease type-II (TMPRSS2), trypsin, and cathepsin L. |*COVID-19 Drug Treatment[MESH] |*SARS-CoV-2[MESH] |Humans[MESH] |Serine Proteases[MESH] |Spike Glycoprotein, Coronavirus/metabolism[MESH]Interfering with Host Proteases in SARS-CoV-2 Entry as a Promising The(epmc).pdf DeepDyve Pubget Overpricing