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10.1002/pro.4046 http://scihub22266oqcxt.onion/10.1002/pro.4046 33594727!7980517!33594727     free     free     free Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Protein+Sci 2021 ; 30 (4): 873-881 Nephropedia Template TP {{tp|p=33594727|t=2021. Nonstructural protein 7 and 8 complexes of SARS-CoV-2 |pdf=|usr=}}{{33594727}} gab.com Text Nonstructural protein 7 and 8 complexes of SARS-CoV-2 JO: Protein Sci http://www.kidney.de/pget.php?&tw=1&pmid=33594727 #FOAvip The pandemic outbreak of coronavirus disease 2019 (COVID-19) across the world has led to millions of infection cases and caused a global public health crisis. Current research suggests that SARS-CoV-2 is a highly contagious coronavirus that spreads rapidly through communities. To understand the mechanisms of viral replication, it is imperative to investigate coronavirus viral replicase, a huge protein complex comprising up to 16 viral nonstructural and associated host proteins, which is the most promising antiviral target for inhibiting viral genome replication and transcription. Recently, several components of the viral replicase complex in SARS-CoV-2 have been solved to provide a basis for the design of new antiviral therapeutics. Here, we report the crystal structure of the SARS-CoV-2 nsp7+8 tetramer, which comprises two copies of each protein representing nsp7's full-length and the C-terminus of nsp8 owing to N-terminus proteolysis during the process of crystallization. We also identified a long helical extension and highly flexible N-terminal domain of nsp8, which is preferred for interacting with single-stranded nucleic acids. Twit Text FOAVip Nonstructural protein 7 and 8 complexes of SARS-CoV-2 ????Protein Sci http://www.kidney.de/pget.php?&tw=1&pmid=33594727 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33594727 #FOAvip English Wikipedia <ref>{{Cite pmid|33594727}}</ref> Nonstructural protein 7 and 8 complexes of SARS-CoV-2 #MMPMID33594727 Zhang C; Li L; He J; Chen C; Su D Protein Sci 2021[Apr]; 30 (4): 873-881 PMID33594727show ga The pandemic outbreak of coronavirus disease 2019 (COVID-19) across the world has led to millions of infection cases and caused a global public health crisis. Current research suggests that SARS-CoV-2 is a highly contagious coronavirus that spreads rapidly through communities. To understand the mechanisms of viral replication, it is imperative to investigate coronavirus viral replicase, a huge protein complex comprising up to 16 viral nonstructural and associated host proteins, which is the most promising antiviral target for inhibiting viral genome replication and transcription. Recently, several components of the viral replicase complex in SARS-CoV-2 have been solved to provide a basis for the design of new antiviral therapeutics. Here, we report the crystal structure of the SARS-CoV-2 nsp7+8 tetramer, which comprises two copies of each protein representing nsp7's full-length and the C-terminus of nsp8 owing to N-terminus proteolysis during the process of crystallization. We also identified a long helical extension and highly flexible N-terminal domain of nsp8, which is preferred for interacting with single-stranded nucleic acids. |COVID-19/*virology[MESH] |Coronavirus RNA-Dependent RNA Polymerase/*chemistry[MESH] |Crystallography, X-Ray[MESH] |Humans[MESH] |Models, Molecular[MESH] |Protein Conformation[MESH] |Protein Domains[MESH] |Protein Multimerization[MESH] |SARS-CoV-2/*chemistry[MESH]Nonstructural protein 7 and 8 complexes of SARS-CoV-2 (epmc).pdf DeepDyve Pubget Overpricing