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10.1016/j.isci.2020.101160 http://scihub22266oqcxt.onion/10.1016/j.isci.2020.101160 32405622!7219414!32405622     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 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       iScience 2020 ; 23 (6): 101160 Nephropedia Template TP {{tp|p=32405622|t=2020. The MERS-CoV Receptor DPP4 as a Candidate Binding Target of the SARS-CoV-2 Spike |pdf=|usr=}}{{32405622}} gab.com Text The MERS-CoV Receptor DPP4 as a Candidate Binding Target of the SARS-CoV-2 Spike JO: iScience http://www.kidney.de/pget.php?&tw=1&pmid=32405622 #FOAvip The ongoing outbreak of the novel coronavirus pneumonia COVID-19 has caused great number of cases and deaths, but our understanding about the pathogen SARS-CoV-2 remains largely unclear. The attachment of the virus with the cell-surface receptor and a cofactor is the first step for the infection. Here, bioinformatics approaches combining human-virus protein interaction prediction and protein docking based on crystal structures have revealed the high affinity between human dipeptidylpeptidase 4 (DPP4) and the spike (S) receptor-binding domain of SARS-CoV-2. Intriguingly, the crucial binding residues of DPP4 are identical to those that are bound to the MERS-CoV-S. Moreover, E484 insertion and adjacent substitutions should be most essential for this DPP4-binding ability acquirement of SARS-CoV-2-S compared with SARS-CoV-S. This potential utilization of DPP4 as a binding target for SARS-CoV-2 may offer novel insight into the viral pathogenesis and help the surveillance and therapeutics strategy for meeting the challenge of COVID-19. Twit Text FOAVip The MERS-CoV Receptor DPP4 as a Candidate Binding Target of the SARS-CoV-2 Spike ????iScience http://www.kidney.de/pget.php?&tw=1&pmid=32405622 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32405622 #FOAvip English Wikipedia <ref>{{Cite pmid|32405622}}</ref> The MERS-CoV Receptor DPP4 as a Candidate Binding Target of the SARS-CoV-2 Spike #MMPMID32405622 Li Y; Zhang Z; Yang L; Lian X; Xie Y; Li S; Xin S; Cao P; Lu J iScience 2020[Jun]; 23 (6): 101160 PMID32405622show ga The ongoing outbreak of the novel coronavirus pneumonia COVID-19 has caused great number of cases and deaths, but our understanding about the pathogen SARS-CoV-2 remains largely unclear. The attachment of the virus with the cell-surface receptor and a cofactor is the first step for the infection. Here, bioinformatics approaches combining human-virus protein interaction prediction and protein docking based on crystal structures have revealed the high affinity between human dipeptidylpeptidase 4 (DPP4) and the spike (S) receptor-binding domain of SARS-CoV-2. Intriguingly, the crucial binding residues of DPP4 are identical to those that are bound to the MERS-CoV-S. Moreover, E484 insertion and adjacent substitutions should be most essential for this DPP4-binding ability acquirement of SARS-CoV-2-S compared with SARS-CoV-S. This potential utilization of DPP4 as a binding target for SARS-CoV-2 may offer novel insight into the viral pathogenesis and help the surveillance and therapeutics strategy for meeting the challenge of COVID-19. äThe MERS-CoV Receptor DPP4 as a Candidate Binding Target of the SARS-C(epmc).pdf DeepDyve Pubget Overpricing