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10.1016/j.cell.2020.07.033 http://scihub22266oqcxt.onion/10.1016/j.cell.2020.07.033 C7386476!7386476!32783916     free     free     free 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 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       Cell 2020 ; 182 (6): 1560-1573.e13 Nephropedia Template TP {{tp|p=32783916|t=2020. Structural Basis for Helicase-Polymerase Coupling in the SARS-CoV-2 Replication-Transcription Complex |pdf=|usr=}}{{32783916}} gab.com Text Structural Basis for Helicase-Polymerase Coupling in the SARS-CoV-2 Replication-Transcription Complex JO: Cell http://www.kidney.de/pget.php?&tw=1&pmid=32783916 #FOAvip SARS-CoV-2 is the causative agent of the 2019?2020 pandemic. The SARS-CoV-2 genome is replicated and transcribed by the RNA-dependent RNA polymerase holoenzyme (subunits nsp7/nsp82/nsp12) along with a cast of accessory factors. One of these factors is the nsp13 helicase. Both the holo-RdRp and nsp13 are essential for viral replication and are targets for treating the disease COVID-19. Here we present cryoelectron microscopic structures of the SARS-CoV-2 holo-RdRp with an RNA template product in complex with two molecules of the nsp13 helicase. The Nidovirales order-specific N-terminal domains of each nsp13 interact with the N-terminal extension of each copy of nsp8. One nsp13 also contacts the nsp12 thumb. The structure places the nucleic acid-binding ATPase domains of the helicase directly in front of the replicating-transcribing holo-RdRp, constraining models for nsp13 function. We also observe ADP-Mg2+ bound in the nsp12 N-terminal nidovirus RdRp-associated nucleotidyltransferase domain, detailing a new pocket for anti-viral therapy development. Twit Text FOAVip Structural Basis for Helicase-Polymerase Coupling in the SARS-CoV-2 Replication-Transcription Complex ????Cell http://www.kidney.de/pget.php?&tw=1&pmid=32783916 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32783916 #FOAvip English Wikipedia <ref>{{Cite pmid|32783916}}</ref> Structural Basis for Helicase-Polymerase Coupling in the SARS-CoV-2 Replication-Transcription Complex #MMPMID32783916 Chen J; Malone B; Llewellyn E; Grasso M; Shelton PM; Olinares PDB; Maruthi K; Eng ET; Vatandaslar H; Chait BT; Kapoor TM; Darst SA; Campbell EA Cell 2020[Sep]; 182 (6): 1560-1573.e13 PMID32783916show ga SARS-CoV-2 is the causative agent of the 2019?2020 pandemic. The SARS-CoV-2 genome is replicated and transcribed by the RNA-dependent RNA polymerase holoenzyme (subunits nsp7/nsp82/nsp12) along with a cast of accessory factors. One of these factors is the nsp13 helicase. Both the holo-RdRp and nsp13 are essential for viral replication and are targets for treating the disease COVID-19. Here we present cryoelectron microscopic structures of the SARS-CoV-2 holo-RdRp with an RNA template product in complex with two molecules of the nsp13 helicase. The Nidovirales order-specific N-terminal domains of each nsp13 interact with the N-terminal extension of each copy of nsp8. One nsp13 also contacts the nsp12 thumb. The structure places the nucleic acid-binding ATPase domains of the helicase directly in front of the replicating-transcribing holo-RdRp, constraining models for nsp13 function. We also observe ADP-Mg2+ bound in the nsp12 N-terminal nidovirus RdRp-associated nucleotidyltransferase domain, detailing a new pocket for anti-viral therapy development. äStructural Basis for Helicase-Polymerase Coupling in the SARS-CoV-2 Re(epmc).pdf DeepDyve Pubget Overpricing