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10.1016/j.celrep.2021.109650 http://scihub22266oqcxt.onion/10.1016/j.celrep.2021.109650 34433083!8367775!34433083     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       Cell+Rep 2021 ; 36 (9): 109650 Nephropedia Template TP {{tp|p=34433083|t=2021. The nucleotide addition cycle of the SARS-CoV-2 polymerase |pdf=|usr=}}{{34433083}} gab.com Text The nucleotide addition cycle of the SARS-CoV-2 polymerase JO: Cell Rep http://www.kidney.de/pget.php?&tw=1&pmid=34433083 #FOAvip Coronaviruses have evolved elaborate multisubunit machines to replicate and transcribe their genomes. Central to these machines are the RNA-dependent RNA polymerase subunit (nsp12) and its intimately associated cofactors (nsp7 and nsp8). We use a high-throughput magnetic-tweezers approach to develop a mechanochemical description of this core polymerase. The core polymerase exists in at least three catalytically distinct conformations, one being kinetically consistent with incorporation of incorrect nucleotides. We provide evidence that the RNA-dependent RNA polymerase (RdRp) uses a thermal ratchet instead of a power stroke to transition from the pre- to post-translocated state. Ultra-stable magnetic tweezers enable the direct observation of coronavirus polymerase deep and long-lived backtracking that is strongly stimulated by secondary structures in the template. The framework we present here elucidates one of the most important structure-dynamics-function relationships in human health today and will form the grounds for understanding the regulation of this complex. Twit Text FOAVip The nucleotide addition cycle of the SARS-CoV-2 polymerase ????Cell Rep http://www.kidney.de/pget.php?&tw=1&pmid=34433083 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=34433083 #FOAvip English Wikipedia <ref>{{Cite pmid|34433083}}</ref> The nucleotide addition cycle of the SARS-CoV-2 polymerase #MMPMID34433083 Bera SC; Seifert M; Kirchdoerfer RN; van Nies P; Wubulikasimu Y; Quack S; Papini FS; Arnold JJ; Canard B; Cameron CE; Depken M; Dulin D Cell Rep 2021[Aug]; 36 (9): 109650 PMID34433083show ga Coronaviruses have evolved elaborate multisubunit machines to replicate and transcribe their genomes. Central to these machines are the RNA-dependent RNA polymerase subunit (nsp12) and its intimately associated cofactors (nsp7 and nsp8). We use a high-throughput magnetic-tweezers approach to develop a mechanochemical description of this core polymerase. The core polymerase exists in at least three catalytically distinct conformations, one being kinetically consistent with incorporation of incorrect nucleotides. We provide evidence that the RNA-dependent RNA polymerase (RdRp) uses a thermal ratchet instead of a power stroke to transition from the pre- to post-translocated state. Ultra-stable magnetic tweezers enable the direct observation of coronavirus polymerase deep and long-lived backtracking that is strongly stimulated by secondary structures in the template. The framework we present here elucidates one of the most important structure-dynamics-function relationships in human health today and will form the grounds for understanding the regulation of this complex. |COVID-19/*virology[MESH] |Coronavirus RNA-Dependent RNA Polymerase/chemistry/*physiology[MESH] |High-Throughput Screening Assays[MESH] |Humans[MESH] |Models, Molecular[MESH] |Molecular Conformation[MESH] |Nucleotides/chemistry/*metabolism[MESH] |RNA, Viral/*biosynthesis/chemistry[MESH] |SARS-CoV-2/*physiology[MESH] |Single Molecule Imaging[MESH]The nucleotide addition cycle of the SARS-CoV-2 polymerase (epmc).pdf DeepDyve Pubget Overpricing