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10.1021/acs.jpcb.1c02048 http://scihub22266oqcxt.onion/10.1021/acs.jpcb.1c02048 33979162!ä!33979162 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       J+Phys+Chem+B 2021 ; 125 (21): 5537-5548 Nephropedia Template TP {{tp|p=33979162|t=2021. Critical Interactions Between the SARS-CoV-2 Spike Glycoprotein and the Human ACE2 Receptor |pdf=|usr=}}{{33979162}} gab.com Text Critical Interactions Between the SARS-CoV-2 Spike Glycoprotein and the Human ACE2 Receptor JO: J Phys Chem B http://www.kidney.de/pget.php?&tw=1&pmid=33979162 #FOAvip Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infects human cells by binding its spike (S) glycoproteins to angiotensin-converting enzyme 2 (ACE2) receptors and causes the coronavirus disease 2019 (COVID-19). Therapeutic approaches to prevent SARS-CoV-2 infection are mostly focused on blocking S-ACE2 binding, but critical residues that stabilize this interaction are not well understood. By performing all-atom molecular dynamics (MD) simulations, we identified an extended network of salt bridges, hydrophobic and electrostatic interactions, and hydrogen bonds between the receptor-binding domain (RBD) of the S protein and ACE2. Mutagenesis of these residues on the RBD was not sufficient to destabilize binding but reduced the average work to unbind the S protein from ACE2. In particular, the hydrophobic end of RBD serves as the main anchor site and is the last to unbind from ACE2 under force. We propose that blocking the hydrophobic surface of RBD via neutralizing antibodies could prove to be an effective strategy to inhibit S-ACE2 interactions. Twit Text FOAVip Critical Interactions Between the SARS-CoV-2 Spike Glycoprotein and the Human ACE2 Receptor ????J Phys Chem B http://www.kidney.de/pget.php?&tw=1&pmid=33979162 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33979162 #FOAvip English Wikipedia <ref>{{Cite pmid|33979162}}</ref> Critical Interactions Between the SARS-CoV-2 Spike Glycoprotein and the Human ACE2 Receptor #MMPMID33979162 Taka E; Yilmaz SZ; Golcuk M; Kilinc C; Aktas U; Yildiz A; Gur M J Phys Chem B 2021[Jun]; 125 (21): 5537-5548 PMID33979162show ga Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infects human cells by binding its spike (S) glycoproteins to angiotensin-converting enzyme 2 (ACE2) receptors and causes the coronavirus disease 2019 (COVID-19). Therapeutic approaches to prevent SARS-CoV-2 infection are mostly focused on blocking S-ACE2 binding, but critical residues that stabilize this interaction are not well understood. By performing all-atom molecular dynamics (MD) simulations, we identified an extended network of salt bridges, hydrophobic and electrostatic interactions, and hydrogen bonds between the receptor-binding domain (RBD) of the S protein and ACE2. Mutagenesis of these residues on the RBD was not sufficient to destabilize binding but reduced the average work to unbind the S protein from ACE2. In particular, the hydrophobic end of RBD serves as the main anchor site and is the last to unbind from ACE2 under force. We propose that blocking the hydrophobic surface of RBD via neutralizing antibodies could prove to be an effective strategy to inhibit S-ACE2 interactions. |*Angiotensin-Converting Enzyme 2[MESH] |*COVID-19[MESH] |*SARS-CoV-2[MESH] |*Spike Glycoprotein, Coronavirus[MESH] |Humans[MESH] |Peptidyl-Dipeptidase A/genetics/metabolism[MESH]Critical Interactions Between the SARS-CoV-2 Spike Glycoprotein and th(epmc).pdf DeepDyve Pubget Overpricing