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10.1016/j.isci.2020.101903 http://scihub22266oqcxt.onion/10.1016/j.isci.2020.101903 33319167!7721355!33319167     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       iScience 2021 ; 24 (1): 101903 Nephropedia Template TP {{tp|p=33319167|t=2021. Structural characterization of nonstructural protein 1 from SARS-CoV-2 |pdf=|usr=}}{{33319167}} gab.com Text Structural characterization of nonstructural protein 1 from SARS-CoV-2 JO: iScience http://www.kidney.de/pget.php?&tw=1&pmid=33319167 #FOAvip Severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) is a single-stranded, enveloped RNA virus and the etiological agent of the current coronavirus disease 2019 pandemic. Efficient replication of the virus relies on the activity of nonstructural protein 1 (Nsp1), a major virulence factor shown to facilitate suppression of host gene expression through promotion of host mRNA degradation and interaction with the 40S ribosomal subunit. Here, we report the crystal structure of the globular domain of SARS-CoV-2 Nsp1, encompassing residues 13 to 127, at a resolution of 1.65 A. Our structure features a six-stranded, capped beta-barrel motif similar to Nsp1 from SARS-CoV and reveals how variations in amino acid sequence manifest as distinct structural features. Combining our high-resolution crystal structure with existing data on the C-terminus of Nsp1 from SARS-CoV-2, we propose a model of the full-length protein. Our results provide insight into the molecular structure of a major pathogenic determinant of SARS-CoV-2. Twit Text FOAVip Structural characterization of nonstructural protein 1 from SARS-CoV-2 ????iScience http://www.kidney.de/pget.php?&tw=1&pmid=33319167 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33319167 #FOAvip English Wikipedia <ref>{{Cite pmid|33319167}}</ref> Structural characterization of nonstructural protein 1 from SARS-CoV-2 #MMPMID33319167 Semper C; Watanabe N; Savchenko A iScience 2021[Jan]; 24 (1): 101903 PMID33319167show ga Severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) is a single-stranded, enveloped RNA virus and the etiological agent of the current coronavirus disease 2019 pandemic. Efficient replication of the virus relies on the activity of nonstructural protein 1 (Nsp1), a major virulence factor shown to facilitate suppression of host gene expression through promotion of host mRNA degradation and interaction with the 40S ribosomal subunit. Here, we report the crystal structure of the globular domain of SARS-CoV-2 Nsp1, encompassing residues 13 to 127, at a resolution of 1.65 A. Our structure features a six-stranded, capped beta-barrel motif similar to Nsp1 from SARS-CoV and reveals how variations in amino acid sequence manifest as distinct structural features. Combining our high-resolution crystal structure with existing data on the C-terminus of Nsp1 from SARS-CoV-2, we propose a model of the full-length protein. Our results provide insight into the molecular structure of a major pathogenic determinant of SARS-CoV-2. äStructural characterization of nonstructural protein 1 from SARS-CoV-2(epmc).pdf DeepDyve Pubget Overpricing