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10.1038/s41598-021-88696-5 http://scihub22266oqcxt.onion/10.1038/s41598-021-88696-5 33911163!8080587!33911163     free     free     free Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Sci+Rep 2021 ; 11 (1): 9166 Nephropedia Template TP {{tp|p=33911163|t=2021. Unraveling the stability landscape of mutations in the SARS-CoV-2 receptor-binding domain |pdf=|usr=}}{{33911163}} gab.com Text Unraveling the stability landscape of mutations in the SARS-CoV-2 receptor-binding domain JO: Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=33911163 #FOAvip The interaction between the receptor-binding domain (RBD) of the SARS-CoV-2 spike glycoprotein and the ACE2 enzyme is believed to be the entry point of the virus into various cells in the body, including the lungs, heart, liver, and kidneys. The current focus of several therapeutic design efforts explores attempts at affecting the binding potential between the two proteins to limit the activity of the virus and disease progression. In this work, we analyze the stability of the spike protein under all possible single-point mutations in the RBD and computationally explore mutations that can affect the binding with the ACE2 enzyme. We unravel the mutation landscape of the receptor region and assess the toxicity potential of single and multi-point mutations, generating insights for future vaccine efforts on mutations that might further stabilize the spike protein and increase its infectivity. We developed a tool, called SpikeMutator, to construct full atomic protein structures of the mutant spike proteins and shared a database of 3800 single-point mutant structures. We analyzed the recent 65,000 reported spike sequences across the globe and observed the emergence of stable multi-point mutant structures. Using the landscape, we searched through 7.5 million possible 2-point mutation combinations and report that the (R355D K424E) mutation produces one of the strongest spike proteins that therapeutic efforts should investigate for the sake of developing effective vaccines. Twit Text FOAVip Unraveling the stability landscape of mutations in the SARS-CoV-2 receptor-binding domain ????Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=33911163 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33911163 #FOAvip English Wikipedia <ref>{{Cite pmid|33911163}}</ref> Unraveling the stability landscape of mutations in the SARS-CoV-2 receptor-binding domain #MMPMID33911163 Smaoui MR; Yahyaoui H Sci Rep 2021[Apr]; 11 (1): 9166 PMID33911163show ga The interaction between the receptor-binding domain (RBD) of the SARS-CoV-2 spike glycoprotein and the ACE2 enzyme is believed to be the entry point of the virus into various cells in the body, including the lungs, heart, liver, and kidneys. The current focus of several therapeutic design efforts explores attempts at affecting the binding potential between the two proteins to limit the activity of the virus and disease progression. In this work, we analyze the stability of the spike protein under all possible single-point mutations in the RBD and computationally explore mutations that can affect the binding with the ACE2 enzyme. We unravel the mutation landscape of the receptor region and assess the toxicity potential of single and multi-point mutations, generating insights for future vaccine efforts on mutations that might further stabilize the spike protein and increase its infectivity. We developed a tool, called SpikeMutator, to construct full atomic protein structures of the mutant spike proteins and shared a database of 3800 single-point mutant structures. We analyzed the recent 65,000 reported spike sequences across the globe and observed the emergence of stable multi-point mutant structures. Using the landscape, we searched through 7.5 million possible 2-point mutation combinations and report that the (R355D K424E) mutation produces one of the strongest spike proteins that therapeutic efforts should investigate for the sake of developing effective vaccines. |*Mutation[MESH] |Angiotensin-Converting Enzyme 2/metabolism[MESH] |Binding Sites[MESH] |Computational Biology/methods[MESH] |Humans[MESH] |Models, Molecular[MESH] |Molecular Dynamics Simulation[MESH] |Protein Conformation[MESH] |Protein Stability[MESH] |SARS-CoV-2/genetics/isolation & purification[MESH]Unraveling the stability landscape of mutations in the SARS-CoV-2 rec(epmc).pdf DeepDyve Pubget Overpricing