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10.1080/07391102.2021.1886175 http://scihub22266oqcxt.onion/10.1080/07391102.2021.1886175 33583326!7885719!33583326     free     free     free 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       J+Biomol+Struct+Dyn 2022 ; 40 (14): 6545-6555 Nephropedia Template TP {{tp|p=33583326|t=2022. Structural genetics of circulating variants affecting the SARS-CoV-2 spike/human ACE2 complex |pdf=|usr=}}{{33583326}} gab.com Text Structural genetics of circulating variants affecting the SARS-CoV-2 spike/human ACE2 complex JO: J Biomol Struct Dyn http://www.kidney.de/pget.php?&tw=1&pmid=33583326 #FOAvip SARS-CoV-2 entry in human cells is mediated by the interaction between the viral Spike protein and the human ACE2 receptor. This mechanism evolved from the ancestor bat coronavirus and is currently one of the main targets for antiviral strategies. However, there currently exist several Spike protein variants in the SARS-CoV-2 population as the result of mutations, and it is unclear if these variants may exert a specific effect on the affinity with ACE2 which, in turn, is also characterized by multiple alleles in the human population. In the current study, the GBPM analysis, originally developed for highlighting host-guest interaction features, has been applied to define the key amino acids responsible for the Spike/ACE2 molecular recognition, using four different crystallographic structures. Then, we intersected these structural results with the current mutational status, based on more than 295,000 sequenced cases, in the SARS-CoV-2 population. We identified several Spike mutations interacting with ACE2 and mutated in at least 20 distinct patients: S477N, N439K, N501Y, Y453F, E484K, K417N, S477I and G476S. Among these, mutation N501Y in particular is one of the events characterizing SARS-CoV-2 lineage B.1.1.7, which has recently risen in frequency in Europe. We also identified five ACE2 rare variants that may affect interaction with Spike and susceptibility to infection: S19P, E37K, M82I, E329G and G352V.Communicated by Ramaswamy H. Sarma. Twit Text FOAVip Structural genetics of circulating variants affecting the SARS-CoV-2 spike/human ACE2 complex ????J Biomol Struct Dyn http://www.kidney.de/pget.php?&tw=1&pmid=33583326 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33583326 #FOAvip English Wikipedia <ref>{{Cite pmid|33583326}}</ref> Structural genetics of circulating variants affecting the SARS-CoV-2 spike/human ACE2 complex #MMPMID33583326 Ortuso F; Mercatelli D; Guzzi PH; Giorgi FM J Biomol Struct Dyn 2022[Sep]; 40 (14): 6545-6555 PMID33583326show ga SARS-CoV-2 entry in human cells is mediated by the interaction between the viral Spike protein and the human ACE2 receptor. This mechanism evolved from the ancestor bat coronavirus and is currently one of the main targets for antiviral strategies. However, there currently exist several Spike protein variants in the SARS-CoV-2 population as the result of mutations, and it is unclear if these variants may exert a specific effect on the affinity with ACE2 which, in turn, is also characterized by multiple alleles in the human population. In the current study, the GBPM analysis, originally developed for highlighting host-guest interaction features, has been applied to define the key amino acids responsible for the Spike/ACE2 molecular recognition, using four different crystallographic structures. Then, we intersected these structural results with the current mutational status, based on more than 295,000 sequenced cases, in the SARS-CoV-2 population. We identified several Spike mutations interacting with ACE2 and mutated in at least 20 distinct patients: S477N, N439K, N501Y, Y453F, E484K, K417N, S477I and G476S. Among these, mutation N501Y in particular is one of the events characterizing SARS-CoV-2 lineage B.1.1.7, which has recently risen in frequency in Europe. We also identified five ACE2 rare variants that may affect interaction with Spike and susceptibility to infection: S19P, E37K, M82I, E329G and G352V.Communicated by Ramaswamy H. Sarma. |*SARS-CoV-2/chemistry/genetics/metabolism[MESH] |Angiotensin-Converting Enzyme 2/*chemistry/*genetics/metabolism[MESH] |COVID-19/genetics/virology[MESH] |Humans[MESH] |Mutation[MESH] |Peptidyl-Dipeptidase A/chemistry[MESH] |Protein Binding[MESH]Structural genetics of circulating variants affecting the SARS-CoV-2 s(epmc).pdf DeepDyve Pubget Overpricing