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10.1146/annurev-biophys-062215-011140 http://scihub22266oqcxt.onion/10.1146/annurev-biophys-062215-011140 C5508521!5508521!28301767     free     free     free Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Annu+Rev+Biophys 2017 ; 46 (ä): 199-225 Nephropedia Template TP {{tp|p=28301767|t=2017. Progress in Human and Tetrahymena Telomerase Structure |pdf=|usr=}}{{28301767}} gab.com Text Progress in Human and Tetrahymena Telomerase Structure JO: Annu Rev Biophys http://www.kidney.de/pget.php?&tw=1&pmid=28301767 #FOAvip Telomerase is an RNA?protein complex that extends the 3? ends of linear chromosomes, using a unique telomerase reverse transcriptase (TERT) and template in the telomerase RNA (TR), thereby helping to maintain genome integrity. TR assembles with TERT and species-specific proteins, and telomerase function in vivo requires interaction with telomere-associated proteins. Over the past two decades, structures of domains of TR and TERT as well as other telomerase- and telomere-interacting proteins have provided insights into telomerase function. A recently reported 9-Å cryo?electron microscopy map of the Tetrahymena telomerase holoenzyme has provided a framework for understanding how TR, TERT, and other proteins from ciliate as well as vertebrate telomerase fit and function together as well as unexpected insight into telomerase interaction at telomeres. Here we review progress in understanding the structural basis of human and Tetrahymena telomerase activity, assembly, and interactions. Twit Text FOAVip Progress in Human and Tetrahymena Telomerase Structure ????Annu Rev Biophys http://www.kidney.de/pget.php?&tw=1&pmid=28301767 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28301767 #FOAvip English Wikipedia <ref>{{Cite pmid|28301767}}</ref> Progress in Human and Tetrahymena Telomerase Structure #MMPMID28301767 Chan H; Wang Y; Feigon J Annu Rev Biophys 2017[May]; 46 (ä): 199-225 PMID28301767show ga Telomerase is an RNA?protein complex that extends the 3? ends of linear chromosomes, using a unique telomerase reverse transcriptase (TERT) and template in the telomerase RNA (TR), thereby helping to maintain genome integrity. TR assembles with TERT and species-specific proteins, and telomerase function in vivo requires interaction with telomere-associated proteins. Over the past two decades, structures of domains of TR and TERT as well as other telomerase- and telomere-interacting proteins have provided insights into telomerase function. A recently reported 9-Å cryo?electron microscopy map of the Tetrahymena telomerase holoenzyme has provided a framework for understanding how TR, TERT, and other proteins from ciliate as well as vertebrate telomerase fit and function together as well as unexpected insight into telomerase interaction at telomeres. Here we review progress in understanding the structural basis of human and Tetrahymena telomerase activity, assembly, and interactions. äProgress in Human and Tetrahymena Telomerase Structure (epmc).pdf DeepDyve Pubget Overpricing