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10.1021/acschembio.1c00691 http://scihub22266oqcxt.onion/10.1021/acschembio.1c00691 34928574!ä!34928574 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 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\34928574.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       ACS+Chem+Biol 2022 ; 17 (1): 103-117 Nephropedia Template TP {{tp|p=34928574|t=2022. Spike Protein and the Various Cell-Surface Carbohydrates: An Interaction Study |pdf=|usr=}}{{34928574}} gab.com Text Spike Protein and the Various Cell-Surface Carbohydrates: An Interaction Study JO: ACS Chem Biol http://www.kidney.de/pget.php?&tw=1&pmid=34928574 #FOAvip The SARS-CoV-2 virus has been known to gain entry into the host cell through the spike protein that binds to the host ACE2 cell surface protein. However, the role of the putative sugar-binding sites in the spike protein has remained unclear. We provide a comprehensive in silico outlook into the infection initiation wherein the virus first recognizes the sialosides on the cell via its S1A domain of the spike protein as it surfs over the cell surface. This facilitates the subsequent interaction with the cellular glycosaminoglycans through the S1B domain of the spike protein as it binds to the ACE2 receptor. The unique coadaptation to recognize both the host protein and the cell-surface carbohydrate receptors provides an additional coupling mechanism for efficient viral attachment and infection. Twit Text FOAVip Spike Protein and the Various Cell-Surface Carbohydrates: An Interaction Study ????ACS Chem Biol http://www.kidney.de/pget.php?&tw=1&pmid=34928574 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=34928574 #FOAvip English Wikipedia <ref>{{Cite pmid|34928574}}</ref> Spike Protein and the Various Cell-Surface Carbohydrates: An Interaction Study #MMPMID34928574 Jayaprakash NG; Surolia A ACS Chem Biol 2022[Jan]; 17 (1): 103-117 PMID34928574show ga The SARS-CoV-2 virus has been known to gain entry into the host cell through the spike protein that binds to the host ACE2 cell surface protein. However, the role of the putative sugar-binding sites in the spike protein has remained unclear. We provide a comprehensive in silico outlook into the infection initiation wherein the virus first recognizes the sialosides on the cell via its S1A domain of the spike protein as it surfs over the cell surface. This facilitates the subsequent interaction with the cellular glycosaminoglycans through the S1B domain of the spike protein as it binds to the ACE2 receptor. The unique coadaptation to recognize both the host protein and the cell-surface carbohydrate receptors provides an additional coupling mechanism for efficient viral attachment and infection. |Angiotensin-Converting Enzyme 2/chemistry[MESH] |Binding Sites[MESH] |Cell Membrane[MESH] |Gangliosides/chemistry[MESH] |Glycosaminoglycans/*chemistry[MESH] |Molecular Dynamics Simulation[MESH] |Protein Domains[MESH] |Protein Subunits[MESH]Spike Protein and the Various Cell-Surface Carbohydrates: An Interacti(epmc).pdf DeepDyve Pubget Overpricing