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10.3390/v12090909 http://scihub22266oqcxt.onion/10.3390/v12090909 32825063!7551769!32825063     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=32825063&cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215 Deprecated: Implicit conversion from float 225.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 225.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 225.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 225.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Viruses 2020 ; 12 (9): ä Nephropedia Template TP {{tp|p=32825063|t=2020. The Sialoside-Binding Pocket of SARS-CoV-2 Spike Glycoprotein Structurally Resembles MERS-CoV |pdf=|usr=}}{{32825063}} gab.com Text The Sialoside-Binding Pocket of SARS-CoV-2 Spike Glycoprotein Structurally Resembles MERS-CoV JO: Viruses http://www.kidney.de/pget.php?&tw=1&pmid=32825063 #FOAvip COVID-19 novel coronavirus (CoV) disease caused by severe acquired respiratory syndrome (SARS)-CoV-2 manifests severe lethal respiratory illness in humans and has recently developed into a worldwide pandemic. The lack of effective treatment strategy and vaccines against the SARS-CoV-2 poses a threat to human health. An extremely high infection rate and multi-organ secondary infection within a short period of time makes this virus more deadly and challenging for therapeutic interventions. Despite high sequence similarity and utilization of common host-cell receptor, human angiotensin-converting enzyme-2 (ACE2) for virus entry, SARS-CoV-2 is much more infectious than SARS-CoV. Structure-based sequence comparison of the N-terminal domain (NTD) of the spike protein of Middle East respiratory syndrome (MERS)-CoV, SARS-CoV, and SARS-CoV-2 illustrate three divergent loop regions in SARS-CoV-2, which is reminiscent of MERS-CoV sialoside binding pockets. Comparative binding analysis with host sialosides revealed conformational flexibility of SARS-CoV-2 divergent loop regions to accommodate diverse glycan-rich sialosides. These key differences with SARS-CoV and similarity with MERS-CoV suggest an evolutionary adaptation of SARS-CoV-2 spike glycoprotein reciprocal interaction with host surface sialosides to infect host cells with wide tissue tropism. Twit Text FOAVip The Sialoside-Binding Pocket of SARS-CoV-2 Spike Glycoprotein Structurally Resembles MERS-CoV ????Viruses http://www.kidney.de/pget.php?&tw=1&pmid=32825063 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32825063 #FOAvip English Wikipedia <ref>{{Cite pmid|32825063}}</ref> The Sialoside-Binding Pocket of SARS-CoV-2 Spike Glycoprotein Structurally Resembles MERS-CoV #MMPMID32825063 Awasthi M; Gulati S; Sarkar DP; Tiwari S; Kateriya S; Ranjan P; Verma SK Viruses 2020[Aug]; 12 (9): ä PMID32825063show ga COVID-19 novel coronavirus (CoV) disease caused by severe acquired respiratory syndrome (SARS)-CoV-2 manifests severe lethal respiratory illness in humans and has recently developed into a worldwide pandemic. The lack of effective treatment strategy and vaccines against the SARS-CoV-2 poses a threat to human health. An extremely high infection rate and multi-organ secondary infection within a short period of time makes this virus more deadly and challenging for therapeutic interventions. Despite high sequence similarity and utilization of common host-cell receptor, human angiotensin-converting enzyme-2 (ACE2) for virus entry, SARS-CoV-2 is much more infectious than SARS-CoV. Structure-based sequence comparison of the N-terminal domain (NTD) of the spike protein of Middle East respiratory syndrome (MERS)-CoV, SARS-CoV, and SARS-CoV-2 illustrate three divergent loop regions in SARS-CoV-2, which is reminiscent of MERS-CoV sialoside binding pockets. Comparative binding analysis with host sialosides revealed conformational flexibility of SARS-CoV-2 divergent loop regions to accommodate diverse glycan-rich sialosides. These key differences with SARS-CoV and similarity with MERS-CoV suggest an evolutionary adaptation of SARS-CoV-2 spike glycoprotein reciprocal interaction with host surface sialosides to infect host cells with wide tissue tropism. |Amino Sugars/metabolism[MESH] |Betacoronavirus/*chemistry/physiology[MESH] |Binding Sites[MESH] |Middle East Respiratory Syndrome Coronavirus/*chemistry[MESH] |Models, Molecular[MESH] |Molecular Docking Simulation[MESH] |Molecular Dynamics Simulation[MESH] |N-Acetylneuraminic Acid/metabolism[MESH] |Protein Binding[MESH] |Protein Domains[MESH] |Receptors, Coronavirus[MESH] |Receptors, Virus/chemistry/metabolism[MESH] |SARS-CoV-2[MESH] |Severe acute respiratory syndrome-related coronavirus/chemistry[MESH] |Sialic Acids/*metabolism[MESH] |Sialyl Lewis X Antigen/metabolism[MESH] |Spike Glycoprotein, Coronavirus/*chemistry/metabolism[MESH] |Viral Tropism[MESH]The Sialoside-Binding Pocket of SARS-CoV-2 Spike Glycoprotein Structur(epmc).pdf DeepDyve Pubget Overpricing