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.

10.1128/Spectrum.00169-21 http://scihub22266oqcxt.onion/10.1128/Spectrum.00169-21 34132580!8552758!34132580     free     free     free Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Microbiol+Spectr 2021 ; 9 (1): e0016921 Nephropedia Template TP {{tp|p=34132580|t=2021. Structural Basis and Function of the N Terminus of SARS-CoV-2 Nonstructural Protein 1 |pdf=|usr=}}{{34132580}} gab.com Text Structural Basis and Function of the N Terminus of SARS-CoV-2 Nonstructural Protein 1 JO: Microbiol Spectr http://www.kidney.de/pget.php?&tw=1&pmid=34132580 #FOAvip Nonstructural protein 1 (Nsp1) of severe acute respiratory syndrome coronaviruses (SARS-CoVs) is an important pathogenic factor that inhibits host protein translation by means of its C terminus. However, its N-terminal function remains elusive. Here, we determined the crystal structure of the N terminus (amino acids [aa] 11 to 125) of SARS-CoV-2 Nsp1 at a 1.25-A resolution. Further functional assays showed that the N terminus of SARS-CoVs Nsp1 alone loses the ability to colocalize with ribosomes and inhibit protein translation. The C terminus of Nsp1 can colocalize with ribosomes, but its protein translation inhibition ability is significantly weakened. Interestingly, fusing the C terminus of Nsp1 with enhanced green fluorescent protein (EGFP) or other proteins in place of its N terminus restored the protein translation inhibitory ability to a level equivalent to that of full-length Nsp1. Thus, our results suggest that the N terminus of Nsp1 is able to stabilize the binding of the Nsp1 C terminus to ribosomes and act as a nonspecific barrier to block the mRNA channel, thus abrogating host mRNA translation. Twit Text FOAVip Structural Basis and Function of the N Terminus of SARS-CoV-2 Nonstructural Protein 1 ????Microbiol Spectr http://www.kidney.de/pget.php?&tw=1&pmid=34132580 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=34132580 #FOAvip English Wikipedia <ref>{{Cite pmid|34132580}}</ref> Structural Basis and Function of the N Terminus of SARS-CoV-2 Nonstructural Protein 1 #MMPMID34132580 Zhao K; Ke Z; Hu H; Liu Y; Li A; Hua R; Guo F; Xiao J; Zhang Y; Duan L; Yan XF; Gao YG; Liu B; Xia Y; Li Y Microbiol Spectr 2021[Sep]; 9 (1): e0016921 PMID34132580show ga Nonstructural protein 1 (Nsp1) of severe acute respiratory syndrome coronaviruses (SARS-CoVs) is an important pathogenic factor that inhibits host protein translation by means of its C terminus. However, its N-terminal function remains elusive. Here, we determined the crystal structure of the N terminus (amino acids [aa] 11 to 125) of SARS-CoV-2 Nsp1 at a 1.25-A resolution. Further functional assays showed that the N terminus of SARS-CoVs Nsp1 alone loses the ability to colocalize with ribosomes and inhibit protein translation. The C terminus of Nsp1 can colocalize with ribosomes, but its protein translation inhibition ability is significantly weakened. Interestingly, fusing the C terminus of Nsp1 with enhanced green fluorescent protein (EGFP) or other proteins in place of its N terminus restored the protein translation inhibitory ability to a level equivalent to that of full-length Nsp1. Thus, our results suggest that the N terminus of Nsp1 is able to stabilize the binding of the Nsp1 C terminus to ribosomes and act as a nonspecific barrier to block the mRNA channel, thus abrogating host mRNA translation. |COVID-19[MESH] |Crystallography, X-Ray[MESH] |HEK293 Cells[MESH] |Humans[MESH] |Protein Biosynthesis[MESH] |Protein Conformation[MESH] |Protein Domains[MESH] |RNA, Messenger[MESH] |SARS-CoV-2/*genetics[MESH] |Sequence Analysis, Protein[MESH]Structural Basis and Function of the N Terminus of SARS-CoV-2 Nonstruc(epmc).pdf DeepDyve Pubget Overpricing