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10.1101/2020.04.26.061705 http://scihub22266oqcxt.onion/10.1101/2020.04.26.061705 C7263512!7263512!32511383     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=32511383&cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215 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       bioRxiv ä ; ä (ä): ä Nephropedia Template TP {{tp|p=32511383|t=ä. Structural Basis of RNA Cap Modification by SARS-CoV-2 Coronavirus |pdf=|usr=}}{{32511383}} gab.com Text Structural Basis of RNA Cap Modification by SARS-CoV-2 Coronavirus JO: bioRxiv http://www.kidney.de/pget.php?&tw=1&pmid=32511383 #FOAvip The novel severe acute respiratory syndrome coronoavirus-2 (SARS-CoV-2), the causative agent of COVID-19 illness, has caused over 2 million infections worldwide in four months. In SARS coronaviruses, the non-structural protein 16 (nsp16) methylates the 5?-end of virally encoded mRNAs to mimic cellular mRNAs, thus protecting the virus from host innate immune restriction. We report here the high-resolution structure of a ternary complex of full-length nsp16 and nsp10 of SARS-CoV-2 in the presence of cognate RNA substrate and a methyl donor, S-adenosyl methionine. The nsp16/nsp10 heterodimer was captured in the act of 2?-O methylation of the ribose sugar of the first nucleotide of SARS-CoV-2 mRNA. We reveal large conformational changes associated with substrate binding as the enzyme transitions from a binary to a ternary state. This structure provides new mechanistic insights into the 2?-O methylation of the viral mRNA cap. We also discovered a distantly located ligand-binding site unique to SARS-CoV-2 that may serve as an alternative target site for antiviral development. Twit Text FOAVip Structural Basis of RNA Cap Modification by SARS-CoV-2 Coronavirus ????bioRxiv http://www.kidney.de/pget.php?&tw=1&pmid=32511383 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32511383 #FOAvip English Wikipedia <ref>{{Cite pmid|32511383}}</ref> Structural Basis of RNA Cap Modification by SARS-CoV-2 Coronavirus #MMPMID32511383 Viswanathan T; Arya S; Chan SH; Qi S; Dai N; Hromas RA; Park JG; Oladunni F; Martinez-Sobrido L; Gupta YK bioRxiv ä[]; ä (ä): ä PMID32511383show ga The novel severe acute respiratory syndrome coronoavirus-2 (SARS-CoV-2), the causative agent of COVID-19 illness, has caused over 2 million infections worldwide in four months. In SARS coronaviruses, the non-structural protein 16 (nsp16) methylates the 5?-end of virally encoded mRNAs to mimic cellular mRNAs, thus protecting the virus from host innate immune restriction. We report here the high-resolution structure of a ternary complex of full-length nsp16 and nsp10 of SARS-CoV-2 in the presence of cognate RNA substrate and a methyl donor, S-adenosyl methionine. The nsp16/nsp10 heterodimer was captured in the act of 2?-O methylation of the ribose sugar of the first nucleotide of SARS-CoV-2 mRNA. We reveal large conformational changes associated with substrate binding as the enzyme transitions from a binary to a ternary state. This structure provides new mechanistic insights into the 2?-O methylation of the viral mRNA cap. We also discovered a distantly located ligand-binding site unique to SARS-CoV-2 that may serve as an alternative target site for antiviral development. äStructural Basis of RNA Cap Modification by SARS-CoV-2 Coronavirus (epmc).pdf DeepDyve Pubget Overpricing