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10.1007/s12013-021-00977-y http://scihub22266oqcxt.onion/10.1007/s12013-021-00977-y 33792836!8014903!33792836     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 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 243.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 243.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Cell+Biochem+Biophys 2021 ; 79 (2): 175-187 Nephropedia Template TP {{tp|p=33792836|t=2021. Piece of the puzzle: Remdesivir disassembles the multimeric SARS-CoV-2 RNA-dependent RNA polymerase complex |pdf=|usr=}}{{33792836}} gab.com Text Piece of the puzzle: Remdesivir disassembles the multimeric SARS-CoV-2 RNA-dependent RNA polymerase complex JO: Cell Biochem Biophys http://www.kidney.de/pget.php?&tw=1&pmid=33792836 #FOAvip The recently emerged SARS-like coronavirus (SARS-CoV-2) has continued to spread rapidly among humans with alarming upsurges in global mortality rates. A major key to tackling this virus is to disrupt its RNA replication process as previously reported for Remdesivir (Rem-P(3)). In this study, we theorize, using computational simulations, novel mechanisms that may underlie the binding of Rem-P(3) to SARS-CoV-2 RdRp-NSPs complex; a multimeric assembly that drives viral RNA replication in human hosts. Findings revealed that while ATP-binding stabilized the replicative tripartite, Rem-P(3) disintegrated the RdRp-NSP complex, starting with the detachment of the NSP7-NSP8 heterodimer followed by minimal displacement of the second NSP8 subunit (NSP8(II)). More so, Rem-P(3) interacted with a relatively higher affinity (DeltaG(bind)) while inducing high perturbations across the RdRp-NSP domains. D452, T556, V557, S682, and D760 were identified for their crucial roles in stacking the cyano-adenosine and 3,4-dihydroxyoxolan rings of Rem-P(3) while its flexible P(3) tail extended towards the palm domain blocking D618 and K798; a residue-pair identified for essential roles in RNA replication. However, ATP folded away from D618 indicative of a more coordinated binding favorable for nucleotide polymerization. We believe findings from this study will significantly contribute to the structure-based design of novel disruptors of the SARS-CoV-2 RNA replicative machinery. Twit Text FOAVip Piece of the puzzle: Remdesivir disassembles the multimeric SARS-CoV-2 RNA-dependent RNA polymerase complex ????Cell Biochem Biophys http://www.kidney.de/pget.php?&tw=1&pmid=33792836 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33792836 #FOAvip English Wikipedia <ref>{{Cite pmid|33792836}}</ref> Piece of the puzzle: Remdesivir disassembles the multimeric SARS-CoV-2 RNA-dependent RNA polymerase complex #MMPMID33792836 Olotu FA; Omolabi KF; Soliman MES Cell Biochem Biophys 2021[Jun]; 79 (2): 175-187 PMID33792836show ga The recently emerged SARS-like coronavirus (SARS-CoV-2) has continued to spread rapidly among humans with alarming upsurges in global mortality rates. A major key to tackling this virus is to disrupt its RNA replication process as previously reported for Remdesivir (Rem-P(3)). In this study, we theorize, using computational simulations, novel mechanisms that may underlie the binding of Rem-P(3) to SARS-CoV-2 RdRp-NSPs complex; a multimeric assembly that drives viral RNA replication in human hosts. Findings revealed that while ATP-binding stabilized the replicative tripartite, Rem-P(3) disintegrated the RdRp-NSP complex, starting with the detachment of the NSP7-NSP8 heterodimer followed by minimal displacement of the second NSP8 subunit (NSP8(II)). More so, Rem-P(3) interacted with a relatively higher affinity (DeltaG(bind)) while inducing high perturbations across the RdRp-NSP domains. D452, T556, V557, S682, and D760 were identified for their crucial roles in stacking the cyano-adenosine and 3,4-dihydroxyoxolan rings of Rem-P(3) while its flexible P(3) tail extended towards the palm domain blocking D618 and K798; a residue-pair identified for essential roles in RNA replication. However, ATP folded away from D618 indicative of a more coordinated binding favorable for nucleotide polymerization. We believe findings from this study will significantly contribute to the structure-based design of novel disruptors of the SARS-CoV-2 RNA replicative machinery. |*COVID-19 Drug Treatment[MESH] |Adenosine Monophosphate/*analogs & derivatives/pharmacology[MESH] |Adenosine Triphosphate/metabolism[MESH] |Alanine/*analogs & derivatives/pharmacology[MESH] |Antiviral Agents/*pharmacology[MESH] |COVID-19/metabolism[MESH] |Coronavirus RNA-Dependent RNA Polymerase/*antagonists & inhibitors/chemistry/metabolism[MESH] |Humans[MESH] |Molecular Dynamics Simulation[MESH] |SARS-CoV-2/drug effects/*enzymology[MESH] |Thermodynamics[MESH]Piece of the puzzle: Remdesivir disassembles the multimeric SARS-CoV-2(epmc).pdf DeepDyve Pubget Overpricing