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10.1002/jmv.26597 http://scihub22266oqcxt.onion/10.1002/jmv.26597 33090512!7675365!33090512     free     free     free Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       J+Med+Virol 2021 ; 93 (4): 2132-2140 Nephropedia Template TP {{tp|p=33090512|t=2021. Effects of SARS-CoV-2 mutations on protein structures and intraviral protein-protein interactions |pdf=|usr=}}{{33090512}} gab.com Text Effects of SARS-CoV-2 mutations on protein structures and intraviral protein-protein interactions JO: J Med Virol http://www.kidney.de/pget.php?&tw=1&pmid=33090512 #FOAvip Since 2019, severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) causing coronavirus disease 2019 (COVID-19) has infected 10 millions of people across the globe, and massive mutations in virus genome have occurred during the rapid spread of this novel coronavirus. Variance in protein sequence might lead to a change in protein structure and interaction, then further affect the viral physiological characteristics, which could bring tremendous influence on the pandemic. In this study, we investigated 20 nonsynonymous mutations in the SARS-CoV-2 genome in which incidence rates were all >/= 1% as of September 1st, 2020, and then modeled and analyzed the mutant protein structures. The results showed that four types of mutations caused dramatic changes in protein structures (RMSD >/= 5.0 A), which were Q57H and G251V in open-reading frames 3a (ORF3a), S194L, and R203K/G204R in nucleocapsid (N). Next, we found that these mutations also affected the binding affinity of intraviral protein interactions. In addition, the hot spots within these docking mutant complexes were altered, among which the mutation Q57H was involved in both Orf3a-S and Orf3a-Orf8 protein interactions. Besides, these mutations were widely distributed all over the world, and their occurrences fluctuated as time went on. Notably, the incidences of R203K/G204R in N and Q57H in Orf3a were both over 50% in some countries. Overall, our findings suggest that SARS-CoV-2 mutations could change viral protein structure, binding affinity, and hot spots of the interface, thereby might have impacts on SARS-CoV-2 transmission, diagnosis, and treatment of COVID-19. Twit Text FOAVip Effects of SARS-CoV-2 mutations on protein structures and intraviral protein-protein interactions ????J Med Virol http://www.kidney.de/pget.php?&tw=1&pmid=33090512 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33090512 #FOAvip English Wikipedia <ref>{{Cite pmid|33090512}}</ref> Effects of SARS-CoV-2 mutations on protein structures and intraviral protein-protein interactions #MMPMID33090512 Wu S; Tian C; Liu P; Guo D; Zheng W; Huang X; Zhang Y; Liu L J Med Virol 2021[Apr]; 93 (4): 2132-2140 PMID33090512show ga Since 2019, severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) causing coronavirus disease 2019 (COVID-19) has infected 10 millions of people across the globe, and massive mutations in virus genome have occurred during the rapid spread of this novel coronavirus. Variance in protein sequence might lead to a change in protein structure and interaction, then further affect the viral physiological characteristics, which could bring tremendous influence on the pandemic. In this study, we investigated 20 nonsynonymous mutations in the SARS-CoV-2 genome in which incidence rates were all >/= 1% as of September 1st, 2020, and then modeled and analyzed the mutant protein structures. The results showed that four types of mutations caused dramatic changes in protein structures (RMSD >/= 5.0 A), which were Q57H and G251V in open-reading frames 3a (ORF3a), S194L, and R203K/G204R in nucleocapsid (N). Next, we found that these mutations also affected the binding affinity of intraviral protein interactions. In addition, the hot spots within these docking mutant complexes were altered, among which the mutation Q57H was involved in both Orf3a-S and Orf3a-Orf8 protein interactions. Besides, these mutations were widely distributed all over the world, and their occurrences fluctuated as time went on. Notably, the incidences of R203K/G204R in N and Q57H in Orf3a were both over 50% in some countries. Overall, our findings suggest that SARS-CoV-2 mutations could change viral protein structure, binding affinity, and hot spots of the interface, thereby might have impacts on SARS-CoV-2 transmission, diagnosis, and treatment of COVID-19. |*Genome, Viral[MESH] |COVID-19/*virology[MESH] |Humans[MESH] |Mutation[MESH] |Open Reading Frames[MESH] |Protein Binding[MESH] |Protein Structure, Tertiary[MESH] |SARS-CoV-2/*genetics[MESH]Effects of SARS-CoV-2 mutations on protein structures and intraviral (epmc).pdf DeepDyve Pubget Overpricing