Use my Search Websuite to scan PubMed, PMCentral, Journal Hosts and Journal Archives, FullText. Kick-your-searchterm to multiple Engines kick-your-query now !>

A dictionary by aggregated review articles of nephrology, medicine and the life sciences Your one-stop-run pathway from word to the immediate pdf of peer-reviewed on-topic knowledge.

10.3389/fphar.2021.685161 http://scihub22266oqcxt.onion/10.3389/fphar.2021.685161 34149429!8206564!34149429     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=34149429&cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\34149429.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Front+Pharmacol 2021 ; 12 (�): 685161 Nephropedia Template TP {{tp|p=34149429|t=2021. Discovery of New Potent anti-MERS CoV Fusion Inhibitors |pdf=|usr=}}{{34149429}} gab.com Text Discovery of New Potent anti-MERS CoV Fusion Inhibitors JO: Front Pharmacol http://www.kidney.de/pget.php?&tw=1&pmid=34149429 #FOAvip Middle East respiratory syndrome coronavirus (MERS-CoV), capable of zoonotic transmission, has been associated with emerging viral pneumonia in humans. In this study, a set of highly potent peptides were designed to prevent MERS-CoV fusion through competition with heptad repeat domain 2 (HR2) at its HR1 binding site. We designed eleven peptides with stronger estimated HR1 binding affinities than the wild-type peptide to prevent viral fusion with the cell membrane. Eight peptides showed strong inhibition of spike-mediated MERS-CoV cell-cell fusion with IC50 values in the nanomolar range (0.25-2.3 microM). Peptides #4-6 inhibited 95-98.3% of MERS-CoV plaque formation. Notably, peptide four showed strong inhibition of MERS-CoV plaques formation with EC50 = 0.302 microM. All peptides demonstrated safe profiles without cytotoxicity up to a concentration of 10 muM, and this cellular safety, combined with their anti-MERS-CoV antiviral activity, indicate all peptides can be regarded as potential promising antiviral agents. Twit Text FOAVip Discovery of New Potent anti-MERS CoV Fusion Inhibitors ????Front Pharmacol http://www.kidney.de/pget.php?&tw=1&pmid=34149429 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=34149429 #FOAvip English Wikipedia <ref>{{Cite pmid|34149429}}</ref> Discovery of New Potent anti-MERS CoV Fusion Inhibitors #MMPMID34149429 Kandeel M; Yamamoto M; Park BK; Al-Taher A; Watanabe A; Gohda J; Kawaguchi Y; Oh-Hashi K; Kwon HJ; Inoue JI Front Pharmacol 2021[]; 12 (�): 685161 PMID34149429show ga Middle East respiratory syndrome coronavirus (MERS-CoV), capable of zoonotic transmission, has been associated with emerging viral pneumonia in humans. In this study, a set of highly potent peptides were designed to prevent MERS-CoV fusion through competition with heptad repeat domain 2 (HR2) at its HR1 binding site. We designed eleven peptides with stronger estimated HR1 binding affinities than the wild-type peptide to prevent viral fusion with the cell membrane. Eight peptides showed strong inhibition of spike-mediated MERS-CoV cell-cell fusion with IC50 values in the nanomolar range (0.25-2.3 microM). Peptides #4-6 inhibited 95-98.3% of MERS-CoV plaque formation. Notably, peptide four showed strong inhibition of MERS-CoV plaques formation with EC50 = 0.302 microM. All peptides demonstrated safe profiles without cytotoxicity up to a concentration of 10 muM, and this cellular safety, combined with their anti-MERS-CoV antiviral activity, indicate all peptides can be regarded as potential promising antiviral agents. �Discovery of New Potent anti-MERS CoV Fusion Inhibitors (epmc).pdf DeepDyve Pubget Overpricing