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10.1016/j.bpj.2021.06.003 http://scihub22266oqcxt.onion/10.1016/j.bpj.2021.06.003 34197802!8239202!34197802     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Biophys+J 2021 ; 120 (14): 2814-2827 Nephropedia Template TP {{tp|p=34197802|t=2021. Dynamics of the SARS-CoV-2 nucleoprotein N-terminal domain triggers RNA duplex destabilization |pdf=|usr=}}{{34197802}} gab.com Text Dynamics of the SARS-CoV-2 nucleoprotein N-terminal domain triggers RNA duplex destabilization JO: Biophys J http://www.kidney.de/pget.php?&tw=1&pmid=34197802 #FOAvip The nucleocapsid (N) protein of betacoronaviruses is responsible for nucleocapsid assembly and other essential regulatory functions. The N protein N-terminal domain (N-NTD) interacts and melts the double-stranded transcriptional regulatory sequences (dsTRSs), regulating the discontinuous subgenome transcription process. Here, we used molecular dynamics (MD) simulations to study the binding of the severe acute respiratory syndrome coronavirus 2 N-NTD to nonspecific (NS) and TRS dsRNAs. We probed dsRNAs' Watson-Crick basepairing over 25 replicas of 100 ns MD simulations, showing that only one N-NTD of dimeric N is enough to destabilize dsRNAs, triggering melting initiation. dsRNA destabilization driven by N-NTD was more efficient for dsTRSs than dsNS. N-NTD dynamics, especially a tweezer-like motion of beta2-beta3 and Delta2-beta5 loops, seems to play a key role in Watson-Crick basepairing destabilization. Based on experimental information available in the literature, we constructed kinetics models for N-NTD-mediated dsRNA melting. Our results support a 1:1 stoichiometry (N-NTD/dsRNA), matching MD simulations and raising different possibilities for N-NTD action: 1) two N-NTD arms of dimeric N would bind to two different RNA sites, either closely or spatially spaced in the viral genome, in a cooperative manner; and 2) monomeric N-NTD would be active, opening up the possibility of a regulatory dissociation event. Twit Text FOAVip Dynamics of the SARS-CoV-2 nucleoprotein N-terminal domain triggers RNA duplex destabilization ????Biophys J http://www.kidney.de/pget.php?&tw=1&pmid=34197802 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=34197802 #FOAvip English Wikipedia <ref>{{Cite pmid|34197802}}</ref> Dynamics of the SARS-CoV-2 nucleoprotein N-terminal domain triggers RNA duplex destabilization #MMPMID34197802 Caruso IP; Sanches K; Da Poian AT; Pinheiro AS; Almeida FCL Biophys J 2021[Jul]; 120 (14): 2814-2827 PMID34197802show ga The nucleocapsid (N) protein of betacoronaviruses is responsible for nucleocapsid assembly and other essential regulatory functions. The N protein N-terminal domain (N-NTD) interacts and melts the double-stranded transcriptional regulatory sequences (dsTRSs), regulating the discontinuous subgenome transcription process. Here, we used molecular dynamics (MD) simulations to study the binding of the severe acute respiratory syndrome coronavirus 2 N-NTD to nonspecific (NS) and TRS dsRNAs. We probed dsRNAs' Watson-Crick basepairing over 25 replicas of 100 ns MD simulations, showing that only one N-NTD of dimeric N is enough to destabilize dsRNAs, triggering melting initiation. dsRNA destabilization driven by N-NTD was more efficient for dsTRSs than dsNS. N-NTD dynamics, especially a tweezer-like motion of beta2-beta3 and Delta2-beta5 loops, seems to play a key role in Watson-Crick basepairing destabilization. Based on experimental information available in the literature, we constructed kinetics models for N-NTD-mediated dsRNA melting. Our results support a 1:1 stoichiometry (N-NTD/dsRNA), matching MD simulations and raising different possibilities for N-NTD action: 1) two N-NTD arms of dimeric N would bind to two different RNA sites, either closely or spatially spaced in the viral genome, in a cooperative manner; and 2) monomeric N-NTD would be active, opening up the possibility of a regulatory dissociation event. |*COVID-19[MESH] |*SARS-CoV-2[MESH] |Humans[MESH] |Nucleocapsid Proteins/genetics[MESH] |Nucleoproteins[MESH]Dynamics of the SARS-CoV-2 nucleoprotein N-terminal domain triggers RN(epmc).pdf DeepDyve Pubget Overpricing