Use my Search Websuite to scan PubMed, PMCentral, Journal Hosts and Journal Archives, FullText. Kick-your-searchterm to multiple Engines kick-your-query now !>

A dictionary by aggregated review articles of nephrology, medicine and the life sciences Your one-stop-run pathway from word to the immediate pdf of peer-reviewed on-topic knowledge.

10.1016/j.cell.2020.05.034 http://scihub22266oqcxt.onion/10.1016/j.cell.2020.05.034 32526208!7242921!32526208     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=32526208&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 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\32526208.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Cell 2020 ; 182 (2): 417-428.e13 Nephropedia Template TP {{tp|p=32526208|t=2020. Structural Basis for RNA Replication by the SARS-CoV-2 Polymerase |pdf=|usr=}}{{32526208}} gab.com Text Structural Basis for RNA Replication by the SARS-CoV-2 Polymerase JO: Cell http://www.kidney.de/pget.php?&tw=1&pmid=32526208 #FOAvip Nucleotide analog inhibitors, including broad-spectrum remdesivir and favipiravir, have shown promise in in vitro assays and some clinical studies for COVID-19 treatment, this despite an incomplete mechanistic understanding of the viral RNA-dependent RNA polymerase nsp12 drug interactions. Here, we examine the molecular basis of SARS-CoV-2 RNA replication by determining the cryo-EM structures of the stalled pre- and post- translocated polymerase complexes. Compared with the apo complex, the structures show notable structural rearrangements happening to nsp12 and its co-factors nsp7 and nsp8 to accommodate the nucleic acid, whereas there are highly conserved residues in nsp12, positioning the template and primer for an in-line attack on the incoming nucleotide. Furthermore, we investigate the inhibition mechanism of the triphosphate metabolite of remdesivir through structural and kinetic analyses. A transition model from the nsp7-nsp8 hexadecameric primase complex to the nsp12-nsp7-nsp8 polymerase complex is also proposed to provide clues for the understanding of the coronavirus transcription and replication machinery. Twit Text FOAVip Structural Basis for RNA Replication by the SARS-CoV-2 Polymerase ????Cell http://www.kidney.de/pget.php?&tw=1&pmid=32526208 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32526208 #FOAvip English Wikipedia <ref>{{Cite pmid|32526208}}</ref> Structural Basis for RNA Replication by the SARS-CoV-2 Polymerase #MMPMID32526208 Wang Q; Wu J; Wang H; Gao Y; Liu Q; Mu A; Ji W; Yan L; Zhu Y; Zhu C; Fang X; Yang X; Huang Y; Gao H; Liu F; Ge J; Sun Q; Yang X; Xu W; Liu Z; Yang H; Lou Z; Jiang B; Guddat LW; Gong P; Rao Z Cell 2020[Jul]; 182 (2): 417-428.e13 PMID32526208show ga Nucleotide analog inhibitors, including broad-spectrum remdesivir and favipiravir, have shown promise in in vitro assays and some clinical studies for COVID-19 treatment, this despite an incomplete mechanistic understanding of the viral RNA-dependent RNA polymerase nsp12 drug interactions. Here, we examine the molecular basis of SARS-CoV-2 RNA replication by determining the cryo-EM structures of the stalled pre- and post- translocated polymerase complexes. Compared with the apo complex, the structures show notable structural rearrangements happening to nsp12 and its co-factors nsp7 and nsp8 to accommodate the nucleic acid, whereas there are highly conserved residues in nsp12, positioning the template and primer for an in-line attack on the incoming nucleotide. Furthermore, we investigate the inhibition mechanism of the triphosphate metabolite of remdesivir through structural and kinetic analyses. A transition model from the nsp7-nsp8 hexadecameric primase complex to the nsp12-nsp7-nsp8 polymerase complex is also proposed to provide clues for the understanding of the coronavirus transcription and replication machinery. |Adenosine Monophosphate/analogs & derivatives/chemistry/metabolism/pharmacology[MESH] |Alanine/analogs & derivatives/chemistry/metabolism/pharmacology[MESH] |Antiviral Agents/chemistry/metabolism/pharmacology[MESH] |Betacoronavirus/*chemistry/*enzymology[MESH] |Catalytic Domain[MESH] |Coronavirus RNA-Dependent RNA Polymerase[MESH] |Cryoelectron Microscopy[MESH] |Models, Chemical[MESH] |Models, Molecular[MESH] |RNA, Viral/metabolism[MESH] |RNA-Dependent RNA Polymerase/*chemistry[MESH] |SARS-CoV-2[MESH] |Transcription, Genetic[MESH] |Viral Nonstructural Proteins/*chemistry[MESH]Structural Basis for RNA Replication by the SARS-CoV-2 Polymerase (epmc).pdf DeepDyve Pubget Overpricing