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.

10.1016/j.molcel.2017.03.003 http://scihub22266oqcxt.onion/10.1016/j.molcel.2017.03.003 C5414311!5414311 !28392174     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=28392174 &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 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\28392174 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Mol+Cell 2017 ; 66 (2 ): 194-205.e5 Nephropedia Template TP {{tp|p=28392174 |t=2017. eIF5A Functions Globally in Translation Elongation and Termination |pdf=|usr=}}{{28392174 }} gab.com Text eIF5A Functions Globally in Translation Elongation and Termination JO: Mol Cell http://www.kidney.de/pget.php?&tw=1&pmid=28392174 #FOAvip The eukaryotic translation factor eIF5A, originally identified as an initiation factor, was later shown to promote translation elongation of iterated proline sequences. Using a combination of ribosome profiling and in vitro biochemistry, we report a much broader role for eIF5A in elongation and uncover a critical function for eIF5A in termination. Ribosome profiling of an eIF5A-depleted strain reveals a global elongation defect, with abundant ribosomes stalling at many sequences, not limited to proline stretches. Our data also show ribosome accumulation at stop codons and in the 3' UTR, suggesting a global defect in termination in the absence of eIF5A. Using an in vitro reconstituted translation system, we find that eIF5A strongly promotes the translation of the stalling sequences identified by profiling and increases the rate of peptidyl-tRNA hydrolysis more than 17-fold. We conclude that eIF5A functions broadly in elongation and termination, rationalizing its high cellular abundance and essential nature. Twit Text FOAVip eIF5A Functions Globally in Translation Elongation and Termination ????Mol Cell http://www.kidney.de/pget.php?&tw=1&pmid=28392174 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28392174 #FOAvip English Wikipedia <ref>{{Cite pmid|28392174 }}</ref> eIF5A Functions Globally in Translation Elongation and Termination #MMPMID28392174 Schuller AP ; Wu CC ; Dever TE ; Buskirk AR ; Green R Mol Cell 2017[Apr]; 66 (2 ): 194-205.e5 PMID28392174 show ga The eukaryotic translation factor eIF5A, originally identified as an initiation factor, was later shown to promote translation elongation of iterated proline sequences. Using a combination of ribosome profiling and in vitro biochemistry, we report a much broader role for eIF5A in elongation and uncover a critical function for eIF5A in termination. Ribosome profiling of an eIF5A-depleted strain reveals a global elongation defect, with abundant ribosomes stalling at many sequences, not limited to proline stretches. Our data also show ribosome accumulation at stop codons and in the 3' UTR, suggesting a global defect in termination in the absence of eIF5A. Using an in vitro reconstituted translation system, we find that eIF5A strongly promotes the translation of the stalling sequences identified by profiling and increases the rate of peptidyl-tRNA hydrolysis more than 17-fold. We conclude that eIF5A functions broadly in elongation and termination, rationalizing its high cellular abundance and essential nature. |*Peptide Chain Elongation, Translational [MESH] |*Peptide Chain Termination, Translational [MESH] |3' Untranslated Regions [MESH] |Amino Acid Motifs [MESH] |Codon, Terminator [MESH] |Eukaryotic Translation Initiation Factor 5A [MESH] |Gene Expression Profiling/methods [MESH] |Hydrolysis [MESH] |Kinetics [MESH] |Peptide Initiation Factors/genetics/*metabolism [MESH] |Peptide Termination Factors/genetics/metabolism [MESH] |Peptides/metabolism [MESH] |Peptidyl Transferases/genetics/metabolism [MESH] |RNA, Fungal/genetics/metabolism [MESH] |RNA, Transfer, Amino Acyl/genetics/metabolism [MESH] |RNA-Binding Proteins/genetics/*metabolism [MESH] |Ribosomes/genetics/*metabolism [MESH] |Saccharomyces cerevisiae Proteins/genetics/*metabolism [MESH]eIF5A Functions Globally in Translation Elongation and Termination (epmc).pdf DeepDyve Pubget Overpricing