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10.1038/s41467-020-18319-6 http://scihub22266oqcxt.onion/10.1038/s41467-020-18319-6 32917884!7486399!32917884     free     free     free Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Nat+Commun 2020 ; 11 (1): 4541 Nephropedia Template TP {{tp|p=32917884|t=2020. Molecular interaction and inhibition of SARS-CoV-2 binding to the ACE2 receptor |pdf=|usr=}}{{32917884}} gab.com Text Molecular interaction and inhibition of SARS-CoV-2 binding to the ACE2 receptor JO: Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=32917884 #FOAvip Study of the interactions established between the viral glycoproteins and their host receptors is of critical importance for a better understanding of virus entry into cells. The novel coronavirus SARS-CoV-2 entry into host cells is mediated by its spike glycoprotein (S-glycoprotein), and the angiotensin-converting enzyme 2 (ACE2) has been identified as a cellular receptor. Here, we use atomic force microscopy to investigate the mechanisms by which the S-glycoprotein binds to the ACE2 receptor. We demonstrate, both on model surfaces and on living cells, that the receptor binding domain (RBD) serves as the binding interface within the S-glycoprotein with the ACE2 receptor and extract the kinetic and thermodynamic properties of this binding pocket. Altogether, these results provide a picture of the established interaction on living cells. Finally, we test several binding inhibitor peptides targeting the virus early attachment stages, offering new perspectives in the treatment of the SARS-CoV-2 infection. Twit Text FOAVip Molecular interaction and inhibition of SARS-CoV-2 binding to the ACE2 receptor ????Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=32917884 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32917884 #FOAvip English Wikipedia <ref>{{Cite pmid|32917884}}</ref> Molecular interaction and inhibition of SARS-CoV-2 binding to the ACE2 receptor #MMPMID32917884 Yang J; Petitjean SJL; Koehler M; Zhang Q; Dumitru AC; Chen W; Derclaye S; Vincent SP; Soumillion P; Alsteens D Nat Commun 2020[Sep]; 11 (1): 4541 PMID32917884show ga Study of the interactions established between the viral glycoproteins and their host receptors is of critical importance for a better understanding of virus entry into cells. The novel coronavirus SARS-CoV-2 entry into host cells is mediated by its spike glycoprotein (S-glycoprotein), and the angiotensin-converting enzyme 2 (ACE2) has been identified as a cellular receptor. Here, we use atomic force microscopy to investigate the mechanisms by which the S-glycoprotein binds to the ACE2 receptor. We demonstrate, both on model surfaces and on living cells, that the receptor binding domain (RBD) serves as the binding interface within the S-glycoprotein with the ACE2 receptor and extract the kinetic and thermodynamic properties of this binding pocket. Altogether, these results provide a picture of the established interaction on living cells. Finally, we test several binding inhibitor peptides targeting the virus early attachment stages, offering new perspectives in the treatment of the SARS-CoV-2 infection. |*Virus Attachment[MESH] |*Virus Internalization[MESH] |A549 Cells[MESH] |Angiotensin-Converting Enzyme 2[MESH] |Betacoronavirus/metabolism/*physiology[MESH] |Binding Sites[MESH] |COVID-19[MESH] |Coronavirus Infections/metabolism/*virology[MESH] |Humans[MESH] |Models, Molecular[MESH] |Pandemics[MESH] |Peptidyl-Dipeptidase A/chemistry/*metabolism[MESH] |Pneumonia, Viral/metabolism/*virology[MESH] |Protein Binding[MESH] |Protein Interaction Domains and Motifs[MESH] |Receptors, Virus/metabolism[MESH] |SARS-CoV-2[MESH]Molecular interaction and inhibition of SARS-CoV-2 binding to the ACE2(epmc).pdf DeepDyve Pubget Overpricing