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10.1002/bip.22832 http://scihub22266oqcxt.onion/10.1002/bip.22832 C5084732!5084732 !26971860     free     free     free Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\26971860 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Biopolymers 2016 ; 105 (8 ): 463-75 Nephropedia Template TP {{tp|p=26971860 |t=2016. Review: Translational GTPases |pdf=|usr=}}{{26971860 }} gab.com Text Review: Translational GTPases JO: Biopolymers http://www.kidney.de/pget.php?&tw=1&pmid=26971860 #FOAvip Translational GTPases (trGTPases) play key roles in facilitating protein synthesis on the ribosome. Despite the high degree of evolutionary conservation in the sequences of their GTP-binding domains, the rates of GTP hydrolysis and nucleotide exchange vary broadly between different trGTPases. EF-Tu, one of the best-characterized model G proteins, evolved an exceptionally rapid and tightly regulated GTPase activity, which ensures rapid and accurate incorporation of amino acids into the nascent chain. Other trGTPases instead use the energy of GTP hydrolysis to promote movement or to ensure the forward commitment of translation reactions. Recent data suggest the GTPase mechanism of EF-Tu and provide an insight in the catalysis of GTP hydrolysis by its unusual activator, the ribosome. Here we summarize these advances in understanding the functional cycle and the regulation of trGTPases, stimulated by the elucidation of their structures on the ribosome and the progress in dissecting the reaction mechanism of GTPases. © 2016 Wiley Periodicals, Inc. Biopolymers 105: 463-475, 2016. Twit Text FOAVip Review: Translational GTPases ????Biopolymers http://www.kidney.de/pget.php?&tw=1&pmid=26971860 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26971860 #FOAvip English Wikipedia <ref>{{Cite pmid|26971860 }}</ref> Review: Translational GTPases #MMPMID26971860 Maracci C ; Rodnina MV Biopolymers 2016[Aug]; 105 (8 ): 463-75 PMID26971860 show ga Translational GTPases (trGTPases) play key roles in facilitating protein synthesis on the ribosome. Despite the high degree of evolutionary conservation in the sequences of their GTP-binding domains, the rates of GTP hydrolysis and nucleotide exchange vary broadly between different trGTPases. EF-Tu, one of the best-characterized model G proteins, evolved an exceptionally rapid and tightly regulated GTPase activity, which ensures rapid and accurate incorporation of amino acids into the nascent chain. Other trGTPases instead use the energy of GTP hydrolysis to promote movement or to ensure the forward commitment of translation reactions. Recent data suggest the GTPase mechanism of EF-Tu and provide an insight in the catalysis of GTP hydrolysis by its unusual activator, the ribosome. Here we summarize these advances in understanding the functional cycle and the regulation of trGTPases, stimulated by the elucidation of their structures on the ribosome and the progress in dissecting the reaction mechanism of GTPases. © 2016 Wiley Periodicals, Inc. Biopolymers 105: 463-475, 2016. |*Guanosine Triphosphate/chemistry/metabolism [MESH] |*Peptide Elongation Factor Tu/chemistry/metabolism [MESH] |*Ribosomes/chemistry/metabolism [MESH] |Animals [MESH] |Catalysis [MESH] |Humans [MESH] |Hydrolysis [MESH]Review: Translational GTPases (epmc).pdf DeepDyve Pubget Overpricing