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10.1093/bib/bbaa233 http://scihub22266oqcxt.onion/10.1093/bib/bbaa233 33006605!7665319!33006605     free     free     free 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 Deprecated: Implicit conversion from float 251.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 251.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Brief+Bioinform 2021 ; 22 (2): 1239-1253 Nephropedia Template TP {{tp|p=33006605|t=2021. Systemic effects of missense mutations on SARS-CoV-2 spike glycoprotein stability and receptor-binding affinity |pdf=|usr=}}{{33006605}} gab.com Text Systemic effects of missense mutations on SARS-CoV-2 spike glycoprotein stability and receptor-binding affinity JO: Brief Bioinform http://www.kidney.de/pget.php?&tw=1&pmid=33006605 #FOAvip The spike (S) glycoprotein of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is responsible for the binding to the permissive cells. The receptor-binding domain (RBD) of SARS-CoV-2 S protein directly interacts with the human angiotensin-converting enzyme 2 (ACE2) on the host cell membrane. In this study, we used computational saturation mutagenesis approaches, including structure-based energy calculations and sequence-based pathogenicity predictions, to quantify the systemic effects of missense mutations on SARS-CoV-2 S protein structure and function. A total of 18 354 mutations in S protein were analyzed, and we discovered that most of these mutations could destabilize the entire S protein and its RBD. Specifically, residues G431 and S514 in SARS-CoV-2 RBD are important for S protein stability. We analyzed 384 experimentally verified S missense variations and revealed that the dominant pandemic form, D614G, can stabilize the entire S protein. Moreover, many mutations in N-linked glycosylation sites can increase the stability of the S protein. In addition, we investigated 3705 mutations in SARS-CoV-2 RBD and 11 324 mutations in human ACE2 and found that SARS-CoV-2 neighbor residues G496 and F497 and ACE2 residues D355 and Y41 are critical for the RBD-ACE2 interaction. The findings comprehensively provide potential target sites in the development of drugs and vaccines against COVID-19. Twit Text FOAVip Systemic effects of missense mutations on SARS-CoV-2 spike glycoprotein stability and receptor-binding affinity ????Brief Bioinform http://www.kidney.de/pget.php?&tw=1&pmid=33006605 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33006605 #FOAvip English Wikipedia <ref>{{Cite pmid|33006605}}</ref> Systemic effects of missense mutations on SARS-CoV-2 spike glycoprotein stability and receptor-binding affinity #MMPMID33006605 Teng S; Sobitan A; Rhoades R; Liu D; Tang Q Brief Bioinform 2021[Mar]; 22 (2): 1239-1253 PMID33006605show ga The spike (S) glycoprotein of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is responsible for the binding to the permissive cells. The receptor-binding domain (RBD) of SARS-CoV-2 S protein directly interacts with the human angiotensin-converting enzyme 2 (ACE2) on the host cell membrane. In this study, we used computational saturation mutagenesis approaches, including structure-based energy calculations and sequence-based pathogenicity predictions, to quantify the systemic effects of missense mutations on SARS-CoV-2 S protein structure and function. A total of 18 354 mutations in S protein were analyzed, and we discovered that most of these mutations could destabilize the entire S protein and its RBD. Specifically, residues G431 and S514 in SARS-CoV-2 RBD are important for S protein stability. We analyzed 384 experimentally verified S missense variations and revealed that the dominant pandemic form, D614G, can stabilize the entire S protein. Moreover, many mutations in N-linked glycosylation sites can increase the stability of the S protein. In addition, we investigated 3705 mutations in SARS-CoV-2 RBD and 11 324 mutations in human ACE2 and found that SARS-CoV-2 neighbor residues G496 and F497 and ACE2 residues D355 and Y41 are critical for the RBD-ACE2 interaction. The findings comprehensively provide potential target sites in the development of drugs and vaccines against COVID-19. |*Mutation, Missense[MESH] |COVID-19/metabolism/virology[MESH] |Humans[MESH] |Protein Binding[MESH] |SARS-CoV-2/metabolism[MESH] |Spike Glycoprotein, Coronavirus/*genetics[MESH]Systemic effects of missense mutations on SARS-CoV-2 spike glycoprotei(epmc).pdf DeepDyve Pubget Overpricing