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10.1016/j.celrep.2020.107774 http://scihub22266oqcxt.onion/10.1016/j.celrep.2020.107774 32531208!7260489!32531208     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=32531208&cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 265.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Cell+Rep 2020 ; 31 (11): 107774 Nephropedia Template TP {{tp|p=32531208|t=2020. Structural and Biochemical Characterization of the nsp12-nsp7-nsp8 Core Polymerase Complex from SARS-CoV-2 |pdf=|usr=}}{{32531208}} gab.com Text Structural and Biochemical Characterization of the nsp12-nsp7-nsp8 Core Polymerase Complex from SARS-CoV-2 JO: Cell Rep http://www.kidney.de/pget.php?&tw=1&pmid=32531208 #FOAvip The ongoing global pandemic of coronavirus disease 2019 (COVID-19) has caused a huge number of human deaths. Currently, there are no specific drugs or vaccines available for this virus (SARS-CoV-2). The viral polymerase is a promising antiviral target. Here, we describe the near-atomic-resolution structure of the SARS-CoV-2 polymerase complex consisting of the nsp12 catalytic subunit and nsp7-nsp8 cofactors. This structure highly resembles the counterpart of SARS-CoV with conserved motifs for all viral RNA-dependent RNA polymerases and suggests a mechanism of activation by cofactors. Biochemical studies reveal reduced activity of the core polymerase complex and lower thermostability of individual subunits of SARS-CoV-2 compared with SARS-CoV. These findings provide important insights into RNA synthesis by coronavirus polymerase and indicate adaptation of SARS-CoV-2 toward humans with a relatively lower body temperature than the natural bat hosts. Twit Text FOAVip Structural and Biochemical Characterization of the nsp12-nsp7-nsp8 Core Polymerase Complex from SARS-CoV-2 ????Cell Rep http://www.kidney.de/pget.php?&tw=1&pmid=32531208 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32531208 #FOAvip English Wikipedia <ref>{{Cite pmid|32531208}}</ref> Structural and Biochemical Characterization of the nsp12-nsp7-nsp8 Core Polymerase Complex from SARS-CoV-2 #MMPMID32531208 Peng Q; Peng R; Yuan B; Zhao J; Wang M; Wang X; Wang Q; Sun Y; Fan Z; Qi J; Gao GF; Shi Y Cell Rep 2020[Jun]; 31 (11): 107774 PMID32531208show ga The ongoing global pandemic of coronavirus disease 2019 (COVID-19) has caused a huge number of human deaths. Currently, there are no specific drugs or vaccines available for this virus (SARS-CoV-2). The viral polymerase is a promising antiviral target. Here, we describe the near-atomic-resolution structure of the SARS-CoV-2 polymerase complex consisting of the nsp12 catalytic subunit and nsp7-nsp8 cofactors. This structure highly resembles the counterpart of SARS-CoV with conserved motifs for all viral RNA-dependent RNA polymerases and suggests a mechanism of activation by cofactors. Biochemical studies reveal reduced activity of the core polymerase complex and lower thermostability of individual subunits of SARS-CoV-2 compared with SARS-CoV. These findings provide important insights into RNA synthesis by coronavirus polymerase and indicate adaptation of SARS-CoV-2 toward humans with a relatively lower body temperature than the natural bat hosts. |*Cryoelectron Microscopy[MESH] |Amino Acid Substitution[MESH] |Betacoronavirus/*enzymology[MESH] |Coronavirus RNA-Dependent RNA Polymerase[MESH] |Escherichia coli/genetics[MESH] |Evolution, Molecular[MESH] |Models, Molecular[MESH] |Multiprotein Complexes/chemistry[MESH] |RNA-Dependent RNA Polymerase/*chemistry/metabolism[MESH] |SARS-CoV-2[MESH] |Severe acute respiratory syndrome-related coronavirus/enzymology[MESH]Structural and Biochemical Characterization of the nsp12-nsp7-nsp8 Cor(epmc).pdf DeepDyve Pubget Overpricing