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10.1039/d1cc02305e http://scihub22266oqcxt.onion/10.1039/d1cc02305e 34019602!ä!34019602 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       Chem+Commun+(Camb) 2021 ; 57 (48): 5949-5952 Nephropedia Template TP {{tp|p=34019602|t=2021. ACE2 glycans preferentially interact with SARS-CoV-2 over SARS-CoV |pdf=|usr=}}{{34019602}} gab.com Text ACE2 glycans preferentially interact with SARS-CoV-2 over SARS-CoV JO: Chem Commun (Camb) http://www.kidney.de/pget.php?&tw=1&pmid=34019602 #FOAvip We report a distinct difference in the interactions of the glycans of the host-cell receptor, ACE2, with SARS-CoV-2 and SARS-CoV S-protein receptor-binding domains (RBDs). Our analysis demonstrates that the ACE2 glycan at N322 enhances interactions with the SARS-CoV-2 RBD while the ACE2 glycan at N90 may offer protection against infections of both coronaviruses depending on its composition. The interactions of the ACE2 glycan at N322 with SARS-CoV RBD are blocked by the presence of the RBD glycan at N357 of the SARS-CoV RBD. The absence of this glycosylation site on SARS-CoV-2 RBD may enhance its binding with ACE2. Twit Text FOAVip ACE2 glycans preferentially interact with SARS-CoV-2 over SARS-CoV ????Chem Commun (Camb) http://www.kidney.de/pget.php?&tw=1&pmid=34019602 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=34019602 #FOAvip English Wikipedia <ref>{{Cite pmid|34019602}}</ref> ACE2 glycans preferentially interact with SARS-CoV-2 over SARS-CoV #MMPMID34019602 Acharya A; Lynch DL; Pavlova A; Pang YT; Gumbart JC Chem Commun (Camb) 2021[Jun]; 57 (48): 5949-5952 PMID34019602show ga We report a distinct difference in the interactions of the glycans of the host-cell receptor, ACE2, with SARS-CoV-2 and SARS-CoV S-protein receptor-binding domains (RBDs). Our analysis demonstrates that the ACE2 glycan at N322 enhances interactions with the SARS-CoV-2 RBD while the ACE2 glycan at N90 may offer protection against infections of both coronaviruses depending on its composition. The interactions of the ACE2 glycan at N322 with SARS-CoV RBD are blocked by the presence of the RBD glycan at N357 of the SARS-CoV RBD. The absence of this glycosylation site on SARS-CoV-2 RBD may enhance its binding with ACE2. |Angiotensin-Converting Enzyme 2/chemistry/*metabolism[MESH] |Humans[MESH] |Molecular Dynamics Simulation[MESH] |Polysaccharides/*metabolism[MESH] |Protein Binding[MESH] |Protein Domains[MESH] |SARS-CoV-2/*chemistry[MESH] |Severe acute respiratory syndrome-related coronavirus/*chemistry[MESH]ACE2 glycans preferentially interact with SARS-CoV-2 over SARS-CoV (epmc).pdf DeepDyve Pubget Overpricing