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10.7554/eLife.22883 http://scihub22266oqcxt.onion/10.7554/eLife.22883 C5336357!5336357!28186489     free     free     free 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 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 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 Deprecated: Implicit conversion from float 267.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 267.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       eLife 2017 ; 6 (ä): ä Nephropedia Template TP {{tp|p=28186489|t=2017. Folding behavior of a T-shaped, ribosome-binding translation enhancer implicated in a wide-spread conformational switch |pdf=|usr=}}{{28186489}} gab.com Text Folding behavior of a T-shaped, ribosome-binding translation enhancer implicated in a wide-spread conformational switch JO: eLife http://www.kidney.de/pget.php?&tw=1&pmid=28186489 #FOAvip Turnip crinkle virus contains a T-shaped, ribosome-binding, translation enhancer (TSS) in its 3?UTR that serves as a hub for interactions throughout the region. The viral RNA-dependent RNA polymerase (RdRp) causes the TSS/surrounding region to undergo a conformational shift postulated to inhibit translation. Using optical tweezers (OT) and steered molecular dynamic simulations (SMD), we found that the unusual stability of pseudoknotted element H4a/?3 required five upstream adenylates, and H4a/?3 was necessary for cooperative association of two other hairpins (H5/H4b) in Mg2+. SMD recapitulated the TSS unfolding order in the absence of Mg2+, showed dependence of the resistance to pulling on the 3D orientation and gave structural insights into the measured contour lengths of the TSS structure elements. Adenylate mutations eliminated one-site RdRp binding to the 3?UTR, suggesting that RdRp binding to the adenylates disrupts H4a/?3, leading to loss of H5/H4b interaction and promoting a conformational switch interrupting translation and promoting replication.DOI:http://dx.doi.org/10.7554/eLife.22883.001 Twit Text FOAVip Folding behavior of a T-shaped, ribosome-binding translation enhancer implicated in a wide-spread conformational switch ????eLife http://www.kidney.de/pget.php?&tw=1&pmid=28186489 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28186489 #FOAvip English Wikipedia <ref>{{Cite pmid|28186489}}</ref> Folding behavior of a T-shaped, ribosome-binding translation enhancer implicated in a wide-spread conformational switch #MMPMID28186489 Le MT; Kasprzak WK; Kim T; Gao F; Young MY; Yuan X; Shapiro BA; Seog J; Simon AE eLife 2017[]; 6 (ä): ä PMID28186489show ga Turnip crinkle virus contains a T-shaped, ribosome-binding, translation enhancer (TSS) in its 3?UTR that serves as a hub for interactions throughout the region. The viral RNA-dependent RNA polymerase (RdRp) causes the TSS/surrounding region to undergo a conformational shift postulated to inhibit translation. Using optical tweezers (OT) and steered molecular dynamic simulations (SMD), we found that the unusual stability of pseudoknotted element H4a/?3 required five upstream adenylates, and H4a/?3 was necessary for cooperative association of two other hairpins (H5/H4b) in Mg2+. SMD recapitulated the TSS unfolding order in the absence of Mg2+, showed dependence of the resistance to pulling on the 3D orientation and gave structural insights into the measured contour lengths of the TSS structure elements. Adenylate mutations eliminated one-site RdRp binding to the 3?UTR, suggesting that RdRp binding to the adenylates disrupts H4a/?3, leading to loss of H5/H4b interaction and promoting a conformational switch interrupting translation and promoting replication.DOI:http://dx.doi.org/10.7554/eLife.22883.001 äFolding behavior of a T-shaped, ribosome-binding translation enhancer (epmc).pdf DeepDyve Pubget Overpricing