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10.2174/1871526520666200804161650 http://scihub22266oqcxt.onion/10.2174/1871526520666200804161650 32753027!ä!32753027 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Infect+Disord+Drug+Targets 2021 ; 21 (4): 640-642 Nephropedia Template TP {{tp|p=32753027|t=2021. Role of key point Mutations in Receptor Binding Domain of SARS-CoV-2 Spike Glycoprotein |pdf=|usr=}}{{32753027}} gab.com Text Role of key point Mutations in Receptor Binding Domain of SARS-CoV-2 Spike Glycoprotein JO: Infect Disord Drug Targets http://www.kidney.de/pget.php?&tw=1&pmid=32753027 #FOAvip The recent outbreak of novel coronavirus (SARS-CoV-2 or 2019-nCoV) and its worldwide spread is posing one of the major threats to human health and the world economy. It has been suggested that SARS-CoV-2 is similar to SARS-CoV based on the comparison of the genome sequence. Despite the genomic similarity between SARS-CoV-2 and SARS-CoV, the spike glycoprotein and receptor binding domain in SARS-CoV-2 shows the considerable difference compared to SARS-CoV, due to the presence of several point mutations. The analysis of receptor binding domain (RBD) from recently published 3D structures of spike glycoprotein of SARS-CoV-2 (Yan, R., et al. (2020); Wrapp, D., et al. (2020); Walls, A. C., et al. (2020)) highlights the contribution of a few key point mutations in RBD of spike glycoprotein and molecular basis of its efficient binding with human angiotensin-converting enzyme 2 (ACE2). Twit Text FOAVip Role of key point Mutations in Receptor Binding Domain of SARS-CoV-2 Spike Glycoprotein ????Infect Disord Drug Targets http://www.kidney.de/pget.php?&tw=1&pmid=32753027 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32753027 #FOAvip English Wikipedia <ref>{{Cite pmid|32753027}}</ref> Role of key point Mutations in Receptor Binding Domain of SARS-CoV-2 Spike Glycoprotein #MMPMID32753027 Singh B Infect Disord Drug Targets 2021[]; 21 (4): 640-642 PMID32753027show ga The recent outbreak of novel coronavirus (SARS-CoV-2 or 2019-nCoV) and its worldwide spread is posing one of the major threats to human health and the world economy. It has been suggested that SARS-CoV-2 is similar to SARS-CoV based on the comparison of the genome sequence. Despite the genomic similarity between SARS-CoV-2 and SARS-CoV, the spike glycoprotein and receptor binding domain in SARS-CoV-2 shows the considerable difference compared to SARS-CoV, due to the presence of several point mutations. The analysis of receptor binding domain (RBD) from recently published 3D structures of spike glycoprotein of SARS-CoV-2 (Yan, R., et al. (2020); Wrapp, D., et al. (2020); Walls, A. C., et al. (2020)) highlights the contribution of a few key point mutations in RBD of spike glycoprotein and molecular basis of its efficient binding with human angiotensin-converting enzyme 2 (ACE2). |*Point Mutation[MESH] |*Spike Glycoprotein, Coronavirus/genetics[MESH] |Binding Sites[MESH] |Protein Binding[MESH] |Protein Domains[MESH] |Receptors, Virus[MESH]Role of key point Mutations in Receptor Binding Domain of SARS-CoV-2 S(epmc).pdf DeepDyve Pubget Overpricing