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.

10.1038/s41467-020-17495-9 http://scihub22266oqcxt.onion/10.1038/s41467-020-17495-9 32709887!7381658!32709887     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 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 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       Nat+Commun 2020 ; 11 (1): 3717 Nephropedia Template TP {{tp|p=32709887|t=2020. Structural analysis of the SARS-CoV-2 methyltransferase complex involved in RNA cap creation bound to sinefungin |pdf=|usr=}}{{32709887}} gab.com Text Structural analysis of the SARS-CoV-2 methyltransferase complex involved in RNA cap creation bound to sinefungin JO: Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=32709887 #FOAvip Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is the cause of the COVID-19 pandemic. 2'-O-RNA methyltransferase (MTase) is one of the enzymes of this virus that is a potential target for antiviral therapy as it is crucial for RNA cap formation; an essential process for viral RNA stability. This MTase function is associated with the nsp16 protein, which requires a cofactor, nsp10, for its proper activity. Here we show the crystal structure of the nsp10-nsp16 complex bound to the pan-MTase inhibitor sinefungin in the active site. Our structural comparisons reveal low conservation of the MTase catalytic site between Zika and SARS-CoV-2 viruses, but high conservation of the MTase active site between SARS-CoV-2 and SARS-CoV viruses; these data suggest that the preparation of MTase inhibitors targeting several coronaviruses - but not flaviviruses - should be feasible. Together, our data add to important information for structure-based drug discovery. Twit Text FOAVip Structural analysis of the SARS-CoV-2 methyltransferase complex involved in RNA cap creation bound to sinefungin ????Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=32709887 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32709887 #FOAvip English Wikipedia <ref>{{Cite pmid|32709887}}</ref> Structural analysis of the SARS-CoV-2 methyltransferase complex involved in RNA cap creation bound to sinefungin #MMPMID32709887 Krafcikova P; Silhan J; Nencka R; Boura E Nat Commun 2020[Jul]; 11 (1): 3717 PMID32709887show ga Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is the cause of the COVID-19 pandemic. 2'-O-RNA methyltransferase (MTase) is one of the enzymes of this virus that is a potential target for antiviral therapy as it is crucial for RNA cap formation; an essential process for viral RNA stability. This MTase function is associated with the nsp16 protein, which requires a cofactor, nsp10, for its proper activity. Here we show the crystal structure of the nsp10-nsp16 complex bound to the pan-MTase inhibitor sinefungin in the active site. Our structural comparisons reveal low conservation of the MTase catalytic site between Zika and SARS-CoV-2 viruses, but high conservation of the MTase active site between SARS-CoV-2 and SARS-CoV viruses; these data suggest that the preparation of MTase inhibitors targeting several coronaviruses - but not flaviviruses - should be feasible. Together, our data add to important information for structure-based drug discovery. |Adenosine/analogs & derivatives/metabolism/pharmacology[MESH] |Betacoronavirus/*enzymology[MESH] |COVID-19[MESH] |Catalytic Domain[MESH] |Coronavirus Infections/virology[MESH] |Crystallography, X-Ray[MESH] |Enzyme Inhibitors/metabolism/pharmacology[MESH] |Humans[MESH] |Methyltransferases/*chemistry/metabolism[MESH] |Models, Chemical[MESH] |Models, Molecular[MESH] |Pandemics[MESH] |Pneumonia, Viral/virology[MESH] |RNA Caps[MESH] |RNA Stability[MESH] |RNA, Viral/metabolism[MESH] |SARS-CoV-2[MESH] |Viral Nonstructural Proteins/*chemistry/metabolism[MESH]Structural analysis of the SARS-CoV-2 methyltransferase complex involv(epmc).pdf DeepDyve Pubget Overpricing